data_7HDI
# 
_entry.id   7HDI 
# 
_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   7HDI         pdb_00007hdi 10.2210/pdb7hdi/pdb 
WWPDB D_1001407336 ?            ?                   
# 
_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                        7HDI 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                     18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                                         114.023   1   ? ? ? ? 
3 non-polymer syn '[(3S)-2-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-2-azaspiro[4.5]decan-3-yl]methanol' 286.372   1   ? ? ? ? 
4 water       nat water                                                                          18.015    423 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                                         TFA   
3 '[(3S)-2-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-2-azaspiro[4.5]decan-3-yl]methanol' A1A8G 
4 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 
A1A8G non-polymer         . '[(3S)-2-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-2-azaspiro[4.5]decan-3-yl]methanol' ? 'C16 H22 N4 O'   
286.372 
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 
CYS   'L-peptide linking' y CYSTEINE                                                                       ? 'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                      ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                        ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                      ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                          ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                     ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                        ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                         ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                     ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                  ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                        ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                         ? 'C3 H7 N O3'     
105.093 
TFA   non-polymer         . 'trifluoroacetic acid'                                                         ? 'C2 H F3 O2'     
114.023 
THR   'L-peptide linking' y THREONINE                                                                      ? 'C4 H9 N O3'     
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                       ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                         ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 A1A8G 1   202 201  A1A8G LA1 A . 
E 4 HOH   1   301 409  HOH   HOH A . 
E 4 HOH   2   302 196  HOH   HOH A . 
E 4 HOH   3   303 229  HOH   HOH A . 
E 4 HOH   4   304 292  HOH   HOH A . 
E 4 HOH   5   305 209  HOH   HOH A . 
E 4 HOH   6   306 1301 HOH   HOH A . 
E 4 HOH   7   307 136  HOH   HOH A . 
E 4 HOH   8   308 354  HOH   HOH A . 
E 4 HOH   9   309 109  HOH   HOH A . 
E 4 HOH   10  310 625  HOH   HOH A . 
E 4 HOH   11  311 26   HOH   HOH A . 
E 4 HOH   12  312 393  HOH   HOH A . 
E 4 HOH   13  313 1300 HOH   HOH A . 
E 4 HOH   14  314 132  HOH   HOH A . 
E 4 HOH   15  315 92   HOH   HOH A . 
E 4 HOH   16  316 461  HOH   HOH A . 
E 4 HOH   17  317 661  HOH   HOH A . 
E 4 HOH   18  318 1295 HOH   HOH A . 
E 4 HOH   19  319 1290 HOH   HOH A . 
E 4 HOH   20  320 1283 HOH   HOH A . 
E 4 HOH   21  321 164  HOH   HOH A . 
E 4 HOH   22  322 192  HOH   HOH A . 
E 4 HOH   23  323 195  HOH   HOH A . 
E 4 HOH   24  324 662  HOH   HOH A . 
E 4 HOH   25  325 124  HOH   HOH A . 
E 4 HOH   26  326 155  HOH   HOH A . 
E 4 HOH   27  327 630  HOH   HOH A . 
E 4 HOH   28  328 169  HOH   HOH A . 
E 4 HOH   29  329 159  HOH   HOH A . 
E 4 HOH   30  330 35   HOH   HOH A . 
E 4 HOH   31  331 76   HOH   HOH A . 
E 4 HOH   32  332 247  HOH   HOH A . 
E 4 HOH   33  333 93   HOH   HOH A . 
E 4 HOH   34  334 153  HOH   HOH A . 
E 4 HOH   35  335 85   HOH   HOH A . 
E 4 HOH   36  336 281  HOH   HOH A . 
E 4 HOH   37  337 102  HOH   HOH A . 
E 4 HOH   38  338 236  HOH   HOH A . 
E 4 HOH   39  339 964  HOH   HOH A . 
E 4 HOH   40  340 199  HOH   HOH A . 
E 4 HOH   41  341 17   HOH   HOH A . 
E 4 HOH   42  342 140  HOH   HOH A . 
E 4 HOH   43  343 218  HOH   HOH A . 
E 4 HOH   44  344 397  HOH   HOH A . 
E 4 HOH   45  345 225  HOH   HOH A . 
E 4 HOH   46  346 396  HOH   HOH A . 
E 4 HOH   47  347 57   HOH   HOH A . 
E 4 HOH   48  348 337  HOH   HOH A . 
E 4 HOH   49  349 165  HOH   HOH A . 
E 4 HOH   50  350 21   HOH   HOH A . 
E 4 HOH   51  351 56   HOH   HOH A . 
E 4 HOH   52  352 42   HOH   HOH A . 
E 4 HOH   53  353 212  HOH   HOH A . 
E 4 HOH   54  354 241  HOH   HOH A . 
E 4 HOH   55  355 4    HOH   HOH A . 
E 4 HOH   56  356 2    HOH   HOH A . 
E 4 HOH   57  357 33   HOH   HOH A . 
E 4 HOH   58  358 469  HOH   HOH A . 
E 4 HOH   59  359 46   HOH   HOH A . 
E 4 HOH   60  360 39   HOH   HOH A . 
E 4 HOH   61  361 74   HOH   HOH A . 
E 4 HOH   62  362 154  HOH   HOH A . 
E 4 HOH   63  363 381  HOH   HOH A . 
E 4 HOH   64  364 186  HOH   HOH A . 
E 4 HOH   65  365 18   HOH   HOH A . 
E 4 HOH   66  366 320  HOH   HOH A . 
E 4 HOH   67  367 3    HOH   HOH A . 
E 4 HOH   68  368 86   HOH   HOH A . 
E 4 HOH   69  369 138  HOH   HOH A . 
E 4 HOH   70  370 151  HOH   HOH A . 
E 4 HOH   71  371 366  HOH   HOH A . 
E 4 HOH   72  372 19   HOH   HOH A . 
E 4 HOH   73  373 66   HOH   HOH A . 
E 4 HOH   74  374 5    HOH   HOH A . 
E 4 HOH   75  375 1    HOH   HOH A . 
E 4 HOH   76  376 49   HOH   HOH A . 
E 4 HOH   77  377 83   HOH   HOH A . 
E 4 HOH   78  378 45   HOH   HOH A . 
E 4 HOH   79  379 36   HOH   HOH A . 
E 4 HOH   80  380 1134 HOH   HOH A . 
E 4 HOH   81  381 27   HOH   HOH A . 
E 4 HOH   82  382 1315 HOH   HOH A . 
E 4 HOH   83  383 939  HOH   HOH A . 
E 4 HOH   84  384 105  HOH   HOH A . 
E 4 HOH   85  385 134  HOH   HOH A . 
E 4 HOH   86  386 12   HOH   HOH A . 
E 4 HOH   87  387 6    HOH   HOH A . 
E 4 HOH   88  388 405  HOH   HOH A . 
E 4 HOH   89  389 162  HOH   HOH A . 
E 4 HOH   90  390 8    HOH   HOH A . 
E 4 HOH   91  391 303  HOH   HOH A . 
E 4 HOH   92  392 148  HOH   HOH A . 
E 4 HOH   93  393 1308 HOH   HOH A . 
E 4 HOH   94  394 278  HOH   HOH A . 
E 4 HOH   95  395 96   HOH   HOH A . 
E 4 HOH   96  396 67   HOH   HOH A . 
E 4 HOH   97  397 68   HOH   HOH A . 
E 4 HOH   98  398 140  HOH   HOH A . 
E 4 HOH   99  399 116  HOH   HOH A . 
E 4 HOH   100 400 1068 HOH   HOH A . 
E 4 HOH   101 401 944  HOH   HOH A . 
E 4 HOH   102 402 58   HOH   HOH A . 
E 4 HOH   103 403 34   HOH   HOH A . 
E 4 HOH   104 404 4    HOH   HOH A . 
E 4 HOH   105 405 24   HOH   HOH A . 
E 4 HOH   106 406 115  HOH   HOH A . 
E 4 HOH   107 407 139  HOH   HOH A . 
E 4 HOH   108 408 1275 HOH   HOH A . 
E 4 HOH   109 409 1279 HOH   HOH A . 
E 4 HOH   110 410 351  HOH   HOH A . 
E 4 HOH   111 411 78   HOH   HOH A . 
E 4 HOH   112 412 296  HOH   HOH A . 
E 4 HOH   113 413 1313 HOH   HOH A . 
E 4 HOH   114 414 576  HOH   HOH A . 
E 4 HOH   115 415 7    HOH   HOH A . 
E 4 HOH   116 416 2    HOH   HOH A . 
E 4 HOH   117 417 1094 HOH   HOH A . 
E 4 HOH   118 418 1289 HOH   HOH A . 
E 4 HOH   119 419 53   HOH   HOH A . 
E 4 HOH   120 420 25   HOH   HOH A . 
E 4 HOH   121 421 123  HOH   HOH A . 
E 4 HOH   122 422 156  HOH   HOH A . 
E 4 HOH   123 423 121  HOH   HOH A . 
E 4 HOH   124 424 95   HOH   HOH A . 
E 4 HOH   125 425 1296 HOH   HOH A . 
E 4 HOH   126 426 51   HOH   HOH A . 
E 4 HOH   127 427 125  HOH   HOH A . 
E 4 HOH   128 428 1222 HOH   HOH A . 
E 4 HOH   129 429 1310 HOH   HOH A . 
E 4 HOH   130 430 493  HOH   HOH A . 
E 4 HOH   131 431 122  HOH   HOH A . 
E 4 HOH   132 432 1309 HOH   HOH A . 
E 4 HOH   133 433 333  HOH   HOH A . 
E 4 HOH   134 434 16   HOH   HOH A . 
E 4 HOH   135 435 70   HOH   HOH A . 
E 4 HOH   136 436 582  HOH   HOH A . 
E 4 HOH   137 437 80   HOH   HOH A . 
E 4 HOH   138 438 1238 HOH   HOH A . 
E 4 HOH   139 439 73   HOH   HOH A . 
E 4 HOH   140 440 188  HOH   HOH A . 
E 4 HOH   141 441 71   HOH   HOH A . 
E 4 HOH   142 442 94   HOH   HOH A . 
E 4 HOH   143 443 40   HOH   HOH A . 
E 4 HOH   144 444 104  HOH   HOH A . 
E 4 HOH   145 445 1189 HOH   HOH A . 
E 4 HOH   146 446 79   HOH   HOH A . 
E 4 HOH   147 447 97   HOH   HOH A . 
E 4 HOH   148 448 5    HOH   HOH A . 
E 4 HOH   149 449 952  HOH   HOH A . 
E 4 HOH   150 450 330  HOH   HOH A . 
E 4 HOH   151 451 11   HOH   HOH A . 
E 4 HOH   152 452 6    HOH   HOH A . 
E 4 HOH   153 453 12   HOH   HOH A . 
E 4 HOH   154 454 107  HOH   HOH A . 
E 4 HOH   155 455 1286 HOH   HOH A . 
E 4 HOH   156 456 509  HOH   HOH A . 
E 4 HOH   157 457 163  HOH   HOH A . 
E 4 HOH   158 458 8    HOH   HOH A . 
E 4 HOH   159 459 726  HOH   HOH A . 
E 4 HOH   160 460 1119 HOH   HOH A . 
E 4 HOH   161 461 408  HOH   HOH A . 
E 4 HOH   162 462 756  HOH   HOH A . 
E 4 HOH   163 463 3    HOH   HOH A . 
E 4 HOH   164 464 801  HOH   HOH A . 
E 4 HOH   165 465 361  HOH   HOH A . 
E 4 HOH   166 466 711  HOH   HOH A . 
E 4 HOH   167 467 319  HOH   HOH A . 
E 4 HOH   168 468 370  HOH   HOH A . 
E 4 HOH   169 469 1276 HOH   HOH A . 
E 4 HOH   170 470 126  HOH   HOH A . 
E 4 HOH   171 471 63   HOH   HOH A . 
E 4 HOH   172 472 342  HOH   HOH A . 
E 4 HOH   173 473 280  HOH   HOH A . 
E 4 HOH   174 474 250  HOH   HOH A . 
E 4 HOH   175 475 521  HOH   HOH A . 
E 4 HOH   176 476 309  HOH   HOH A . 
E 4 HOH   177 477 556  HOH   HOH A . 
E 4 HOH   178 478 1307 HOH   HOH A . 
E 4 HOH   179 479 318  HOH   HOH A . 
E 4 HOH   180 480 7    HOH   HOH A . 
E 4 HOH   181 481 1306 HOH   HOH A . 
E 4 HOH   182 482 1287 HOH   HOH A . 
E 4 HOH   183 483 135  HOH   HOH A . 
E 4 HOH   184 484 224  HOH   HOH A . 
E 4 HOH   185 485 674  HOH   HOH A . 
E 4 HOH   186 486 695  HOH   HOH A . 
E 4 HOH   187 487 267  HOH   HOH A . 
E 4 HOH   188 488 919  HOH   HOH A . 
E 4 HOH   189 489 9    HOH   HOH A . 
E 4 HOH   190 490 941  HOH   HOH A . 
E 4 HOH   191 491 202  HOH   HOH A . 
E 4 HOH   192 492 1314 HOH   HOH A . 
E 4 HOH   193 493 331  HOH   HOH A . 
E 4 HOH   194 494 1299 HOH   HOH A . 
E 4 HOH   195 495 805  HOH   HOH A . 
E 4 HOH   196 496 315  HOH   HOH A . 
E 4 HOH   197 497 326  HOH   HOH A . 
E 4 HOH   198 498 981  HOH   HOH A . 
E 4 HOH   199 499 263  HOH   HOH A . 
E 4 HOH   200 500 208  HOH   HOH A . 
E 4 HOH   201 501 152  HOH   HOH A . 
E 4 HOH   202 502 363  HOH   HOH A . 
E 4 HOH   203 503 1071 HOH   HOH A . 
E 4 HOH   204 504 356  HOH   HOH A . 
E 4 HOH   205 505 1284 HOH   HOH A . 
E 4 HOH   206 506 13   HOH   HOH A . 
E 4 HOH   207 507 180  HOH   HOH A . 
E 4 HOH   208 508 371  HOH   HOH A . 
E 4 HOH   209 509 313  HOH   HOH A . 
E 4 HOH   210 510 429  HOH   HOH A . 
E 4 HOH   211 511 185  HOH   HOH A . 
E 4 HOH   212 512 70   HOH   HOH A . 
E 4 HOH   213 513 10   HOH   HOH A . 
E 4 HOH   214 514 772  HOH   HOH A . 
E 4 HOH   215 515 376  HOH   HOH A . 
E 4 HOH   216 516 1074 HOH   HOH A . 
E 4 HOH   217 517 1292 HOH   HOH A . 
E 4 HOH   218 518 346  HOH   HOH A . 
E 4 HOH   219 519 14   HOH   HOH A . 
E 4 HOH   220 520 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 240  HOH   HOH B . 
F 4 HOH   3   203 1249 HOH   HOH B . 
F 4 HOH   4   204 549  HOH   HOH B . 
F 4 HOH   5   205 232  HOH   HOH B . 
F 4 HOH   6   206 1278 HOH   HOH B . 
F 4 HOH   7   207 120  HOH   HOH B . 
F 4 HOH   8   208 364  HOH   HOH B . 
F 4 HOH   9   209 205  HOH   HOH B . 
F 4 HOH   10  210 50   HOH   HOH B . 
F 4 HOH   11  211 452  HOH   HOH B . 
F 4 HOH   12  212 276  HOH   HOH B . 
F 4 HOH   13  213 172  HOH   HOH B . 
F 4 HOH   14  214 654  HOH   HOH B . 
F 4 HOH   15  215 75   HOH   HOH B . 
F 4 HOH   16  216 900  HOH   HOH B . 
F 4 HOH   17  217 82   HOH   HOH B . 
F 4 HOH   18  218 332  HOH   HOH B . 
F 4 HOH   19  219 743  HOH   HOH B . 
F 4 HOH   20  220 264  HOH   HOH B . 
F 4 HOH   21  221 444  HOH   HOH B . 
F 4 HOH   22  222 15   HOH   HOH B . 
F 4 HOH   23  223 398  HOH   HOH B . 
F 4 HOH   24  224 166  HOH   HOH B . 
F 4 HOH   25  225 758  HOH   HOH B . 
F 4 HOH   26  226 127  HOH   HOH B . 
F 4 HOH   27  227 133  HOH   HOH B . 
F 4 HOH   28  228 723  HOH   HOH B . 
F 4 HOH   29  229 353  HOH   HOH B . 
F 4 HOH   30  230 110  HOH   HOH B . 
F 4 HOH   31  231 54   HOH   HOH B . 
F 4 HOH   32  232 128  HOH   HOH B . 
F 4 HOH   33  233 252  HOH   HOH B . 
F 4 HOH   34  234 81   HOH   HOH B . 
F 4 HOH   35  235 47   HOH   HOH B . 
F 4 HOH   36  236 131  HOH   HOH B . 
F 4 HOH   37  237 72   HOH   HOH B . 
F 4 HOH   38  238 325  HOH   HOH B . 
F 4 HOH   39  239 282  HOH   HOH B . 
F 4 HOH   40  240 181  HOH   HOH B . 
F 4 HOH   41  241 69   HOH   HOH B . 
F 4 HOH   42  242 14   HOH   HOH B . 
F 4 HOH   43  243 358  HOH   HOH B . 
F 4 HOH   44  244 62   HOH   HOH B . 
F 4 HOH   45  245 391  HOH   HOH B . 
F 4 HOH   46  246 272  HOH   HOH B . 
F 4 HOH   47  247 531  HOH   HOH B . 
F 4 HOH   48  248 1    HOH   HOH B . 
F 4 HOH   49  249 343  HOH   HOH B . 
F 4 HOH   50  250 52   HOH   HOH B . 
F 4 HOH   51  251 242  HOH   HOH B . 
F 4 HOH   52  252 9    HOH   HOH B . 
F 4 HOH   53  253 1312 HOH   HOH B . 
F 4 HOH   54  254 129  HOH   HOH B . 
F 4 HOH   55  255 60   HOH   HOH B . 
F 4 HOH   56  256 31   HOH   HOH B . 
F 4 HOH   57  257 30   HOH   HOH B . 
F 4 HOH   58  258 1140 HOH   HOH B . 
F 4 HOH   59  259 41   HOH   HOH B . 
F 4 HOH   60  260 150  HOH   HOH B . 
F 4 HOH   61  261 300  HOH   HOH B . 
F 4 HOH   62  262 10   HOH   HOH B . 
F 4 HOH   63  263 59   HOH   HOH B . 
F 4 HOH   64  264 103  HOH   HOH B . 
F 4 HOH   65  265 221  HOH   HOH B . 
F 4 HOH   66  266 20   HOH   HOH B . 
F 4 HOH   67  267 302  HOH   HOH B . 
F 4 HOH   68  268 271  HOH   HOH B . 
F 4 HOH   69  269 243  HOH   HOH B . 
F 4 HOH   70  270 144  HOH   HOH B . 
F 4 HOH   71  271 143  HOH   HOH B . 
F 4 HOH   72  272 61   HOH   HOH B . 
F 4 HOH   73  273 84   HOH   HOH B . 
F 4 HOH   74  274 207  HOH   HOH B . 
F 4 HOH   75  275 11   HOH   HOH B . 
F 4 HOH   76  276 77   HOH   HOH B . 
F 4 HOH   77  277 114  HOH   HOH B . 
F 4 HOH   78  278 175  HOH   HOH B . 
F 4 HOH   79  279 22   HOH   HOH B . 
F 4 HOH   80  280 347  HOH   HOH B . 
F 4 HOH   81  281 1066 HOH   HOH B . 
F 4 HOH   82  282 220  HOH   HOH B . 
F 4 HOH   83  283 117  HOH   HOH B . 
F 4 HOH   84  284 147  HOH   HOH B . 
F 4 HOH   85  285 231  HOH   HOH B . 
F 4 HOH   86  286 197  HOH   HOH B . 
F 4 HOH   87  287 1285 HOH   HOH B . 
F 4 HOH   88  288 43   HOH   HOH B . 
F 4 HOH   89  289 287  HOH   HOH B . 
F 4 HOH   90  290 416  HOH   HOH B . 
F 4 HOH   91  291 89   HOH   HOH B . 
F 4 HOH   92  292 99   HOH   HOH B . 
F 4 HOH   93  293 13   HOH   HOH B . 
F 4 HOH   94  294 235  HOH   HOH B . 
F 4 HOH   95  295 106  HOH   HOH B . 
F 4 HOH   96  296 1277 HOH   HOH B . 
F 4 HOH   97  297 1106 HOH   HOH B . 
F 4 HOH   98  298 316  HOH   HOH B . 
F 4 HOH   99  299 215  HOH   HOH B . 
F 4 HOH   100 300 32   HOH   HOH B . 
F 4 HOH   101 301 299  HOH   HOH B . 
F 4 HOH   102 302 137  HOH   HOH B . 
F 4 HOH   103 303 88   HOH   HOH B . 
F 4 HOH   104 304 170  HOH   HOH B . 
F 4 HOH   105 305 112  HOH   HOH B . 
F 4 HOH   106 306 216  HOH   HOH B . 
F 4 HOH   107 307 160  HOH   HOH B . 
F 4 HOH   108 308 37   HOH   HOH B . 
F 4 HOH   109 309 38   HOH   HOH B . 
F 4 HOH   110 310 142  HOH   HOH B . 
F 4 HOH   111 311 311  HOH   HOH B . 
F 4 HOH   112 312 161  HOH   HOH B . 
F 4 HOH   113 313 23   HOH   HOH B . 
F 4 HOH   114 314 341  HOH   HOH B . 
F 4 HOH   115 315 91   HOH   HOH B . 
F 4 HOH   116 316 1305 HOH   HOH B . 
F 4 HOH   117 317 1291 HOH   HOH B . 
F 4 HOH   118 318 1274 HOH   HOH B . 
F 4 HOH   119 319 44   HOH   HOH B . 
F 4 HOH   120 320 101  HOH   HOH B . 
F 4 HOH   121 321 297  HOH   HOH B . 
F 4 HOH   122 322 717  HOH   HOH B . 
F 4 HOH   123 323 177  HOH   HOH B . 
F 4 HOH   124 324 118  HOH   HOH B . 
F 4 HOH   125 325 48   HOH   HOH B . 
F 4 HOH   126 326 28   HOH   HOH B . 
F 4 HOH   127 327 635  HOH   HOH B . 
F 4 HOH   128 328 704  HOH   HOH B . 
F 4 HOH   129 329 1294 HOH   HOH B . 
F 4 HOH   130 330 445  HOH   HOH B . 
F 4 HOH   131 331 100  HOH   HOH B . 
F 4 HOH   132 332 334  HOH   HOH B . 
F 4 HOH   133 333 387  HOH   HOH B . 
F 4 HOH   134 334 29   HOH   HOH B . 
F 4 HOH   135 335 1126 HOH   HOH B . 
F 4 HOH   136 336 98   HOH   HOH B . 
F 4 HOH   137 337 141  HOH   HOH B . 
F 4 HOH   138 338 234  HOH   HOH B . 
F 4 HOH   139 339 55   HOH   HOH B . 
F 4 HOH   140 340 339  HOH   HOH B . 
F 4 HOH   141 341 1293 HOH   HOH B . 
F 4 HOH   142 342 65   HOH   HOH B . 
F 4 HOH   143 343 182  HOH   HOH B . 
F 4 HOH   144 344 362  HOH   HOH B . 
F 4 HOH   145 345 87   HOH   HOH B . 
F 4 HOH   146 346 619  HOH   HOH B . 
F 4 HOH   147 347 178  HOH   HOH B . 
F 4 HOH   148 348 1304 HOH   HOH B . 
F 4 HOH   149 349 90   HOH   HOH B . 
F 4 HOH   150 350 960  HOH   HOH B . 
F 4 HOH   151 351 191  HOH   HOH B . 
F 4 HOH   152 352 1280 HOH   HOH B . 
F 4 HOH   153 353 203  HOH   HOH B . 
F 4 HOH   154 354 1046 HOH   HOH B . 
F 4 HOH   155 355 623  HOH   HOH B . 
F 4 HOH   156 356 463  HOH   HOH B . 
F 4 HOH   157 357 335  HOH   HOH B . 
F 4 HOH   158 358 541  HOH   HOH B . 
F 4 HOH   159 359 304  HOH   HOH B . 
F 4 HOH   160 360 479  HOH   HOH B . 
F 4 HOH   161 361 290  HOH   HOH B . 
F 4 HOH   162 362 1077 HOH   HOH B . 
F 4 HOH   163 363 718  HOH   HOH B . 
F 4 HOH   164 364 389  HOH   HOH B . 
F 4 HOH   165 365 1072 HOH   HOH B . 
F 4 HOH   166 366 283  HOH   HOH B . 
F 4 HOH   167 367 291  HOH   HOH B . 
F 4 HOH   168 368 615  HOH   HOH B . 
F 4 HOH   169 369 340  HOH   HOH B . 
F 4 HOH   170 370 1316 HOH   HOH B . 
F 4 HOH   171 371 667  HOH   HOH B . 
F 4 HOH   172 372 898  HOH   HOH B . 
F 4 HOH   173 373 373  HOH   HOH B . 
F 4 HOH   174 374 431  HOH   HOH B . 
F 4 HOH   175 375 418  HOH   HOH B . 
F 4 HOH   176 376 190  HOH   HOH B . 
F 4 HOH   177 377 1303 HOH   HOH B . 
F 4 HOH   178 378 1173 HOH   HOH B . 
F 4 HOH   179 379 183  HOH   HOH B . 
F 4 HOH   180 380 1000 HOH   HOH B . 
F 4 HOH   181 381 310  HOH   HOH B . 
F 4 HOH   182 382 149  HOH   HOH B . 
F 4 HOH   183 383 1163 HOH   HOH B . 
F 4 HOH   184 384 491  HOH   HOH B . 
F 4 HOH   185 385 176  HOH   HOH B . 
F 4 HOH   186 386 1311 HOH   HOH B . 
F 4 HOH   187 387 424  HOH   HOH B . 
F 4 HOH   188 388 470  HOH   HOH B . 
F 4 HOH   189 389 350  HOH   HOH B . 
F 4 HOH   190 390 1298 HOH   HOH B . 
F 4 HOH   191 391 248  HOH   HOH B . 
F 4 HOH   192 392 184  HOH   HOH B . 
F 4 HOH   193 393 265  HOH   HOH B . 
F 4 HOH   194 394 360  HOH   HOH B . 
F 4 HOH   195 395 410  HOH   HOH B . 
F 4 HOH   196 396 355  HOH   HOH B . 
F 4 HOH   197 397 274  HOH   HOH B . 
F 4 HOH   198 398 566  HOH   HOH B . 
F 4 HOH   199 399 314  HOH   HOH B . 
F 4 HOH   200 400 157  HOH   HOH B . 
F 4 HOH   201 401 321  HOH   HOH B . 
F 4 HOH   202 402 792  HOH   HOH B . 
F 4 HOH   203 403 558  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           7HDI 
_cell.length_a           88.813 
_cell.length_b           88.813 
_cell.length_c           39.414 
_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                         7HDI 
_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          7HDI 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.55 
_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   2023-05-20 
_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                     7HDI 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.410 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   155969 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.052 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.000 
_reflns.B_iso_Wilson_estimate        12.530 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.057 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1003283 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.020 1.040  ? 41528 7541 ? 2.024 ? ? ? 5.500 ? 0.600  ? ? ? ? ? ? 97.800 2.237 0.932 0.415 
1 2 5.590 44.410 ? 7090  1035 ? 0.024 ? ? ? 6.900 ? 51.500 ? ? ? ? ? ? 99.800 0.026 0.010 0.999 
# 
_refine.entry_id                                 7HDI 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             39.7200 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7300 
_refine.ls_number_reflns_obs                     155791 
_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                          0.1502 
_refine.ls_R_factor_R_work                       0.1494 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1660 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  7518 
_refine.ls_number_reflns_R_work                  148273 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.9744 
_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                            0.1200 
_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                                94.600 
_refine.B_iso_min                                8.800 
_refine.pdbx_overall_phase_error                 17.7000 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0200 
_refine_hist.d_res_low                        39.7200 
_refine_hist.pdbx_number_atoms_ligand         50 
_refine_hist.number_atoms_solvent             423 
_refine_hist.number_atoms_total               3015 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           20.51 
_refine_hist.pdbx_B_iso_mean_solvent          32.66 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0200 1.0300  30 94.0000  4693 . 0.3877 0.3594 . 189 0.0000 4882 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4907 . 0.3308 0.3165 . 285 0.0000 5192 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4886 . 0.2914 0.3078 . 282 0.0000 5168 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4896 . 0.2629 0.2945 . 281 0.0000 5177 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4934 . 0.2558 0.2675 . 235 0.0000 5169 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4934 . 0.2398 0.2828 . 230 0.0000 5164 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4921 . 0.2227 0.2419 . 265 0.0000 5186 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 4935 . 0.2102 0.2447 . 226 0.0000 5161 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4941 . 0.1960 0.2081 . 234 0.0000 5175 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4939 . 0.1756 0.2105 . 260 0.0000 5199 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4929 . 0.1610 0.1851 . 249 0.0000 5178 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4897 . 0.1463 0.1812 . 270 0.0000 5167 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5009 . 0.1404 0.1620 . 215 0.0000 5224 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4904 . 0.1379 0.1561 . 241 0.0000 5145 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4926 . 0.1377 0.1593 . 259 0.0000 5185 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4938 . 0.1374 0.1716 . 268 0.0000 5206 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4961 . 0.1387 0.1590 . 247 0.0000 5208 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4921 . 0.1396 0.1570 . 250 0.0000 5171 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4964 . 0.1381 0.1682 . 243 0.0000 5207 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4974 . 0.1287 0.1532 . 246 0.0000 5220 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4948 . 0.1177 0.1325 . 240 0.0000 5188 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 4951 . 0.1202 0.1389 . 259 0.0000 5210 . 'X-RAY DIFFRACTION' 
1.5900 1.6600  30 100.0000 4939 . 0.1247 0.1320 . 270 0.0000 5209 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5025 . 0.1344 0.1543 . 196 0.0000 5221 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4958 . 0.1354 0.1485 . 294 0.0000 5252 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4951 . 0.1360 0.1434 . 244 0.0000 5195 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4949 . 0.1384 0.1408 . 288 0.0000 5237 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 4992 . 0.1376 0.1468 . 252 0.0000 5244 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5011 . 0.1523 0.1741 . 249 0.0000 5260 . 'X-RAY DIFFRACTION' 
3.1700 39.7200 30 99.0000  5140 . 0.1514 0.1756 . 251 0.0000 5391 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDI 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003727' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDI 
_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 4 ? 
# 
_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 7HDI A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDI 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 7HDI SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDI MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDI SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDI 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 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HDI 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B HOH 247 ? ? O B HOH 286 ? ? 2.04 
2 1 O   A HOH 329 ? ? O A HOH 476 ? ? 2.10 
3 1 O   A HOH 329 ? ? O A HOH 479 ? ? 2.15 
4 1 OD2 A ASP 162 ? B O A HOH 301 ? ? 2.17 
5 1 O   A HOH 370 ? ? O A HOH 433 ? ? 2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? A 54.55  -127.77 
2 1 HIS A 86  ? B 57.97  -136.37 
3 1 PHE A 168 ? B 111.50 -123.49 
4 1 HIS B 86  ? ? 57.23  -127.39 
# 
_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 518 ? 5.98 . 
2 1 O B A HOH 519 ? 6.81 . 
3 1 O ? A HOH 520 ? 7.66 . 
4 1 O ? B HOH 403 ? 6.26 . 
# 
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 
A1A8G N2   N Y N 1   
A1A8G C3   C N N 2   
A1A8G C6   C N N 3   
A1A8G C9   C N N 4   
A1A8G C12  C Y N 5   
A1A8G C14  C Y N 6   
A1A8G C1   C N N 7   
A1A8G C10  C N N 8   
A1A8G C11  C Y N 9   
A1A8G C13  C Y N 10  
A1A8G C15  C Y N 11  
A1A8G C16  C Y N 12  
A1A8G C2   C N S 13  
A1A8G C4   C N N 14  
A1A8G C5   C N N 15  
A1A8G C7   C N N 16  
A1A8G C8   C N N 17  
A1A8G N1   N N N 18  
A1A8G N3   N Y N 19  
A1A8G N4   N Y N 20  
A1A8G O1   O N N 21  
A1A8G H6   H N N 22  
A1A8G H5   H N N 23  
A1A8G H9   H N N 24  
A1A8G H10  H N N 25  
A1A8G H15  H N N 26  
A1A8G H16  H N N 27  
A1A8G H19  H N N 28  
A1A8G H3   H N N 29  
A1A8G H4   H N N 30  
A1A8G H18  H N N 31  
A1A8G H17  H N N 32  
A1A8G H20  H N N 33  
A1A8G H21  H N N 34  
A1A8G H1   H N N 35  
A1A8G H8   H N N 36  
A1A8G H7   H N N 37  
A1A8G H11  H N N 38  
A1A8G H12  H N N 39  
A1A8G H14  H N N 40  
A1A8G H13  H N N 41  
A1A8G H22  H N N 42  
A1A8G H2   H N N 43  
ALA   N    N N N 44  
ALA   CA   C N S 45  
ALA   C    C N N 46  
ALA   O    O N N 47  
ALA   CB   C N N 48  
ALA   OXT  O N N 49  
ALA   H    H N N 50  
ALA   H2   H N N 51  
ALA   HA   H N N 52  
ALA   HB1  H N N 53  
ALA   HB2  H N N 54  
ALA   HB3  H N N 55  
ALA   HXT  H N N 56  
ARG   N    N N N 57  
ARG   CA   C N S 58  
ARG   C    C N N 59  
ARG   O    O N N 60  
ARG   CB   C N N 61  
ARG   CG   C N N 62  
ARG   CD   C N N 63  
ARG   NE   N N N 64  
ARG   CZ   C N N 65  
ARG   NH1  N N N 66  
ARG   NH2  N N N 67  
ARG   OXT  O N N 68  
ARG   H    H N N 69  
ARG   H2   H N N 70  
ARG   HA   H N N 71  
ARG   HB2  H N N 72  
ARG   HB3  H N N 73  
ARG   HG2  H N N 74  
ARG   HG3  H N N 75  
ARG   HD2  H N N 76  
ARG   HD3  H N N 77  
ARG   HE   H N N 78  
ARG   HH11 H N N 79  
ARG   HH12 H N N 80  
ARG   HH21 H N N 81  
ARG   HH22 H N N 82  
ARG   HXT  H N N 83  
ASN   N    N N N 84  
ASN   CA   C N S 85  
ASN   C    C N N 86  
ASN   O    O N N 87  
ASN   CB   C N N 88  
ASN   CG   C N N 89  
ASN   OD1  O N N 90  
ASN   ND2  N N N 91  
ASN   OXT  O N N 92  
ASN   H    H N N 93  
ASN   H2   H N N 94  
ASN   HA   H N N 95  
ASN   HB2  H N N 96  
ASN   HB3  H N N 97  
ASN   HD21 H N N 98  
ASN   HD22 H N N 99  
ASN   HXT  H N N 100 
ASP   N    N N N 101 
ASP   CA   C N S 102 
ASP   C    C N N 103 
ASP   O    O N N 104 
ASP   CB   C N N 105 
ASP   CG   C N N 106 
ASP   OD1  O N N 107 
ASP   OD2  O N N 108 
ASP   OXT  O N N 109 
ASP   H    H N N 110 
ASP   H2   H N N 111 
ASP   HA   H N N 112 
ASP   HB2  H N N 113 
ASP   HB3  H N N 114 
ASP   HD2  H N N 115 
ASP   HXT  H N N 116 
CYS   N    N N N 117 
CYS   CA   C N R 118 
CYS   C    C N N 119 
CYS   O    O N N 120 
CYS   CB   C N N 121 
CYS   SG   S N N 122 
CYS   OXT  O N N 123 
CYS   H    H N N 124 
CYS   H2   H N N 125 
CYS   HA   H N N 126 
CYS   HB2  H N N 127 
CYS   HB3  H N N 128 
CYS   HG   H N N 129 
CYS   HXT  H N N 130 
GLN   N    N N N 131 
GLN   CA   C N S 132 
GLN   C    C N N 133 
GLN   O    O N N 134 
GLN   CB   C N N 135 
GLN   CG   C N N 136 
GLN   CD   C N N 137 
GLN   OE1  O N N 138 
GLN   NE2  N N N 139 
GLN   OXT  O N N 140 
GLN   H    H N N 141 
GLN   H2   H N N 142 
GLN   HA   H N N 143 
GLN   HB2  H N N 144 
GLN   HB3  H N N 145 
GLN   HG2  H N N 146 
GLN   HG3  H N N 147 
GLN   HE21 H N N 148 
GLN   HE22 H N N 149 
GLN   HXT  H N N 150 
GLU   N    N N N 151 
GLU   CA   C N S 152 
GLU   C    C N N 153 
GLU   O    O N N 154 
GLU   CB   C N N 155 
GLU   CG   C N N 156 
GLU   CD   C N N 157 
GLU   OE1  O N N 158 
GLU   OE2  O N N 159 
GLU   OXT  O N N 160 
GLU   H    H N N 161 
GLU   H2   H N N 162 
GLU   HA   H N N 163 
GLU   HB2  H N N 164 
GLU   HB3  H N N 165 
GLU   HG2  H N N 166 
GLU   HG3  H N N 167 
GLU   HE2  H N N 168 
GLU   HXT  H N N 169 
GLY   N    N N N 170 
GLY   CA   C N N 171 
GLY   C    C N N 172 
GLY   O    O N N 173 
GLY   OXT  O N N 174 
GLY   H    H N N 175 
GLY   H2   H N N 176 
GLY   HA2  H N N 177 
GLY   HA3  H N N 178 
GLY   HXT  H N N 179 
HIS   N    N N N 180 
HIS   CA   C N S 181 
HIS   C    C N N 182 
HIS   O    O N N 183 
HIS   CB   C N N 184 
HIS   CG   C Y N 185 
HIS   ND1  N Y N 186 
HIS   CD2  C Y N 187 
HIS   CE1  C Y N 188 
HIS   NE2  N Y N 189 
HIS   OXT  O N N 190 
HIS   H    H N N 191 
HIS   H2   H N N 192 
HIS   HA   H N N 193 
HIS   HB2  H N N 194 
HIS   HB3  H N N 195 
HIS   HD1  H N N 196 
HIS   HD2  H N N 197 
HIS   HE1  H N N 198 
HIS   HE2  H N N 199 
HIS   HXT  H N N 200 
HOH   O    O N N 201 
HOH   H1   H N N 202 
HOH   H2   H N N 203 
ILE   N    N N N 204 
ILE   CA   C N S 205 
ILE   C    C N N 206 
ILE   O    O N N 207 
ILE   CB   C N S 208 
ILE   CG1  C N N 209 
ILE   CG2  C N N 210 
ILE   CD1  C N N 211 
ILE   OXT  O N N 212 
ILE   H    H N N 213 
ILE   H2   H N N 214 
ILE   HA   H N N 215 
ILE   HB   H N N 216 
ILE   HG12 H N N 217 
ILE   HG13 H N N 218 
ILE   HG21 H N N 219 
ILE   HG22 H N N 220 
ILE   HG23 H N N 221 
ILE   HD11 H N N 222 
ILE   HD12 H N N 223 
ILE   HD13 H N N 224 
ILE   HXT  H N N 225 
LEU   N    N N N 226 
LEU   CA   C N S 227 
LEU   C    C N N 228 
LEU   O    O N N 229 
LEU   CB   C N N 230 
LEU   CG   C N N 231 
LEU   CD1  C N N 232 
LEU   CD2  C N N 233 
LEU   OXT  O N N 234 
LEU   H    H N N 235 
LEU   H2   H N N 236 
LEU   HA   H N N 237 
LEU   HB2  H N N 238 
LEU   HB3  H N N 239 
LEU   HG   H N N 240 
LEU   HD11 H N N 241 
LEU   HD12 H N N 242 
LEU   HD13 H N N 243 
LEU   HD21 H N N 244 
LEU   HD22 H N N 245 
LEU   HD23 H N N 246 
LEU   HXT  H N N 247 
LYS   N    N N N 248 
LYS   CA   C N S 249 
LYS   C    C N N 250 
LYS   O    O N N 251 
LYS   CB   C N N 252 
LYS   CG   C N N 253 
LYS   CD   C N N 254 
LYS   CE   C N N 255 
LYS   NZ   N N N 256 
LYS   OXT  O N N 257 
LYS   H    H N N 258 
LYS   H2   H N N 259 
LYS   HA   H N N 260 
LYS   HB2  H N N 261 
LYS   HB3  H N N 262 
LYS   HG2  H N N 263 
LYS   HG3  H N N 264 
LYS   HD2  H N N 265 
LYS   HD3  H N N 266 
LYS   HE2  H N N 267 
LYS   HE3  H N N 268 
LYS   HZ1  H N N 269 
LYS   HZ2  H N N 270 
LYS   HZ3  H N N 271 
LYS   HXT  H N N 272 
MET   N    N N N 273 
MET   CA   C N S 274 
MET   C    C N N 275 
MET   O    O N N 276 
MET   CB   C N N 277 
MET   CG   C N N 278 
MET   SD   S N N 279 
MET   CE   C N N 280 
MET   OXT  O N N 281 
MET   H    H N N 282 
MET   H2   H N N 283 
MET   HA   H N N 284 
MET   HB2  H N N 285 
MET   HB3  H N N 286 
MET   HG2  H N N 287 
MET   HG3  H N N 288 
MET   HE1  H N N 289 
MET   HE2  H N N 290 
MET   HE3  H N N 291 
MET   HXT  H N N 292 
PHE   N    N N N 293 
PHE   CA   C N S 294 
PHE   C    C N N 295 
PHE   O    O N N 296 
PHE   CB   C N N 297 
PHE   CG   C Y N 298 
PHE   CD1  C Y N 299 
PHE   CD2  C Y N 300 
PHE   CE1  C Y N 301 
PHE   CE2  C Y N 302 
PHE   CZ   C Y N 303 
PHE   OXT  O N N 304 
PHE   H    H N N 305 
PHE   H2   H N N 306 
PHE   HA   H N N 307 
PHE   HB2  H N N 308 
PHE   HB3  H N N 309 
PHE   HD1  H N N 310 
PHE   HD2  H N N 311 
PHE   HE1  H N N 312 
PHE   HE2  H N N 313 
PHE   HZ   H N N 314 
PHE   HXT  H N N 315 
PRO   N    N N N 316 
PRO   CA   C N S 317 
PRO   C    C N N 318 
PRO   O    O N N 319 
PRO   CB   C N N 320 
PRO   CG   C N N 321 
PRO   CD   C N N 322 
PRO   OXT  O N N 323 
PRO   H    H N N 324 
PRO   HA   H N N 325 
PRO   HB2  H N N 326 
PRO   HB3  H N N 327 
PRO   HG2  H N N 328 
PRO   HG3  H N N 329 
PRO   HD2  H N N 330 
PRO   HD3  H N N 331 
PRO   HXT  H N N 332 
SER   N    N N N 333 
SER   CA   C N S 334 
SER   C    C N N 335 
SER   O    O N N 336 
SER   CB   C N N 337 
SER   OG   O N N 338 
SER   OXT  O N N 339 
SER   H    H N N 340 
SER   H2   H N N 341 
SER   HA   H N N 342 
SER   HB2  H N N 343 
SER   HB3  H N N 344 
SER   HG   H N N 345 
SER   HXT  H N N 346 
TFA   C1   C N N 347 
TFA   C2   C N N 348 
TFA   O    O N N 349 
TFA   F1   F N N 350 
TFA   F2   F N N 351 
TFA   F3   F N N 352 
TFA   OXT  O N N 353 
TFA   HXT  H N N 354 
THR   N    N N N 355 
THR   CA   C N S 356 
THR   C    C N N 357 
THR   O    O N N 358 
THR   CB   C N R 359 
THR   OG1  O N N 360 
THR   CG2  C N N 361 
THR   OXT  O N N 362 
THR   H    H N N 363 
THR   H2   H N N 364 
THR   HA   H N N 365 
THR   HB   H N N 366 
THR   HG1  H N N 367 
THR   HG21 H N N 368 
THR   HG22 H N N 369 
THR   HG23 H N N 370 
THR   HXT  H N N 371 
TYR   N    N N N 372 
TYR   CA   C N S 373 
TYR   C    C N N 374 
TYR   O    O N N 375 
TYR   CB   C N N 376 
TYR   CG   C Y N 377 
TYR   CD1  C Y N 378 
TYR   CD2  C Y N 379 
TYR   CE1  C Y N 380 
TYR   CE2  C Y N 381 
TYR   CZ   C Y N 382 
TYR   OH   O N N 383 
TYR   OXT  O N N 384 
TYR   H    H N N 385 
TYR   H2   H N N 386 
TYR   HA   H N N 387 
TYR   HB2  H N N 388 
TYR   HB3  H N N 389 
TYR   HD1  H N N 390 
TYR   HD2  H N N 391 
TYR   HE1  H N N 392 
TYR   HE2  H N N 393 
TYR   HH   H N N 394 
TYR   HXT  H N N 395 
VAL   N    N N N 396 
VAL   CA   C N S 397 
VAL   C    C N N 398 
VAL   O    O N N 399 
VAL   CB   C N N 400 
VAL   CG1  C N N 401 
VAL   CG2  C N N 402 
VAL   OXT  O N N 403 
VAL   H    H N N 404 
VAL   H2   H N N 405 
VAL   HA   H N N 406 
VAL   HB   H N N 407 
VAL   HG11 H N N 408 
VAL   HG12 H N N 409 
VAL   HG13 H N N 410 
VAL   HG21 H N N 411 
VAL   HG22 H N N 412 
VAL   HG23 H N N 413 
VAL   HXT  H N N 414 
# 
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 
A1A8G C6  C7   sing N N 1   
A1A8G C6  C5   sing N N 2   
A1A8G C7  C8   sing N N 3   
A1A8G C5  C4   sing N N 4   
A1A8G C3  C4   sing N N 5   
A1A8G C3  C2   sing N N 6   
A1A8G C8  C9   sing N N 7   
A1A8G C4  C9   sing N N 8   
A1A8G C4  C10  sing N N 9   
A1A8G O1  C1   sing N N 10  
A1A8G C1  C2   sing N N 11  
A1A8G C10 N1   sing N N 12  
A1A8G C2  N1   sing N N 13  
A1A8G N1  C11  sing N N 14  
A1A8G C11 C14  doub Y N 15  
A1A8G C11 N2   sing Y N 16  
A1A8G C15 C14  sing Y N 17  
A1A8G C15 C16  doub Y N 18  
A1A8G C14 C13  sing Y N 19  
A1A8G N2  C12  doub Y N 20  
A1A8G C16 N4   sing Y N 21  
A1A8G C13 N4   sing Y N 22  
A1A8G C13 N3   doub Y N 23  
A1A8G C12 N3   sing Y N 24  
A1A8G C3  H6   sing N N 25  
A1A8G C3  H5   sing N N 26  
A1A8G C6  H9   sing N N 27  
A1A8G C6  H10  sing N N 28  
A1A8G C9  H15  sing N N 29  
A1A8G C9  H16  sing N N 30  
A1A8G C12 H19  sing N N 31  
A1A8G C1  H3   sing N N 32  
A1A8G C1  H4   sing N N 33  
A1A8G C10 H18  sing N N 34  
A1A8G C10 H17  sing N N 35  
A1A8G C15 H20  sing N N 36  
A1A8G C16 H21  sing N N 37  
A1A8G C2  H1   sing N N 38  
A1A8G C5  H8   sing N N 39  
A1A8G C5  H7   sing N N 40  
A1A8G C7  H11  sing N N 41  
A1A8G C7  H12  sing N N 42  
A1A8G C8  H14  sing N N 43  
A1A8G C8  H13  sing N N 44  
A1A8G N4  H22  sing N N 45  
A1A8G O1  H2   sing N N 46  
ALA   N   CA   sing N N 47  
ALA   N   H    sing N N 48  
ALA   N   H2   sing N N 49  
ALA   CA  C    sing N N 50  
ALA   CA  CB   sing N N 51  
ALA   CA  HA   sing N N 52  
ALA   C   O    doub N N 53  
ALA   C   OXT  sing N N 54  
ALA   CB  HB1  sing N N 55  
ALA   CB  HB2  sing N N 56  
ALA   CB  HB3  sing N N 57  
ALA   OXT HXT  sing N N 58  
ARG   N   CA   sing N N 59  
ARG   N   H    sing N N 60  
ARG   N   H2   sing N N 61  
ARG   CA  C    sing N N 62  
ARG   CA  CB   sing N N 63  
ARG   CA  HA   sing N N 64  
ARG   C   O    doub N N 65  
ARG   C   OXT  sing N N 66  
ARG   CB  CG   sing N N 67  
ARG   CB  HB2  sing N N 68  
ARG   CB  HB3  sing N N 69  
ARG   CG  CD   sing N N 70  
ARG   CG  HG2  sing N N 71  
ARG   CG  HG3  sing N N 72  
ARG   CD  NE   sing N N 73  
ARG   CD  HD2  sing N N 74  
ARG   CD  HD3  sing N N 75  
ARG   NE  CZ   sing N N 76  
ARG   NE  HE   sing N N 77  
ARG   CZ  NH1  sing N N 78  
ARG   CZ  NH2  doub N N 79  
ARG   NH1 HH11 sing N N 80  
ARG   NH1 HH12 sing N N 81  
ARG   NH2 HH21 sing N N 82  
ARG   NH2 HH22 sing N N 83  
ARG   OXT HXT  sing N N 84  
ASN   N   CA   sing N N 85  
ASN   N   H    sing N N 86  
ASN   N   H2   sing N N 87  
ASN   CA  C    sing N N 88  
ASN   CA  CB   sing N N 89  
ASN   CA  HA   sing N N 90  
ASN   C   O    doub N N 91  
ASN   C   OXT  sing N N 92  
ASN   CB  CG   sing N N 93  
ASN   CB  HB2  sing N N 94  
ASN   CB  HB3  sing N N 95  
ASN   CG  OD1  doub N N 96  
ASN   CG  ND2  sing N N 97  
ASN   ND2 HD21 sing N N 98  
ASN   ND2 HD22 sing N N 99  
ASN   OXT HXT  sing N N 100 
ASP   N   CA   sing N N 101 
ASP   N   H    sing N N 102 
ASP   N   H2   sing N N 103 
ASP   CA  C    sing N N 104 
ASP   CA  CB   sing N N 105 
ASP   CA  HA   sing N N 106 
ASP   C   O    doub N N 107 
ASP   C   OXT  sing N N 108 
ASP   CB  CG   sing N N 109 
ASP   CB  HB2  sing N N 110 
ASP   CB  HB3  sing N N 111 
ASP   CG  OD1  doub N N 112 
ASP   CG  OD2  sing N N 113 
ASP   OD2 HD2  sing N N 114 
ASP   OXT HXT  sing N N 115 
CYS   N   CA   sing N N 116 
CYS   N   H    sing N N 117 
CYS   N   H2   sing N N 118 
CYS   CA  C    sing N N 119 
CYS   CA  CB   sing N N 120 
CYS   CA  HA   sing N N 121 
CYS   C   O    doub N N 122 
CYS   C   OXT  sing N N 123 
CYS   CB  SG   sing N N 124 
CYS   CB  HB2  sing N N 125 
CYS   CB  HB3  sing N N 126 
CYS   SG  HG   sing N N 127 
CYS   OXT HXT  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
HIS   N   CA   sing N N 175 
HIS   N   H    sing N N 176 
HIS   N   H2   sing N N 177 
HIS   CA  C    sing N N 178 
HIS   CA  CB   sing N N 179 
HIS   CA  HA   sing N N 180 
HIS   C   O    doub N N 181 
HIS   C   OXT  sing N N 182 
HIS   CB  CG   sing N N 183 
HIS   CB  HB2  sing N N 184 
HIS   CB  HB3  sing N N 185 
HIS   CG  ND1  sing Y N 186 
HIS   CG  CD2  doub Y N 187 
HIS   ND1 CE1  doub Y N 188 
HIS   ND1 HD1  sing N N 189 
HIS   CD2 NE2  sing Y N 190 
HIS   CD2 HD2  sing N N 191 
HIS   CE1 NE2  sing Y N 192 
HIS   CE1 HE1  sing N N 193 
HIS   NE2 HE2  sing N N 194 
HIS   OXT HXT  sing N N 195 
HOH   O   H1   sing N N 196 
HOH   O   H2   sing N N 197 
ILE   N   CA   sing N N 198 
ILE   N   H    sing N N 199 
ILE   N   H2   sing N N 200 
ILE   CA  C    sing N N 201 
ILE   CA  CB   sing N N 202 
ILE   CA  HA   sing N N 203 
ILE   C   O    doub N N 204 
ILE   C   OXT  sing N N 205 
ILE   CB  CG1  sing N N 206 
ILE   CB  CG2  sing N N 207 
ILE   CB  HB   sing N N 208 
ILE   CG1 CD1  sing N N 209 
ILE   CG1 HG12 sing N N 210 
ILE   CG1 HG13 sing N N 211 
ILE   CG2 HG21 sing N N 212 
ILE   CG2 HG22 sing N N 213 
ILE   CG2 HG23 sing N N 214 
ILE   CD1 HD11 sing N N 215 
ILE   CD1 HD12 sing N N 216 
ILE   CD1 HD13 sing N N 217 
ILE   OXT HXT  sing N N 218 
LEU   N   CA   sing N N 219 
LEU   N   H    sing N N 220 
LEU   N   H2   sing N N 221 
LEU   CA  C    sing N N 222 
LEU   CA  CB   sing N N 223 
LEU   CA  HA   sing N N 224 
LEU   C   O    doub N N 225 
LEU   C   OXT  sing N N 226 
LEU   CB  CG   sing N N 227 
LEU   CB  HB2  sing N N 228 
LEU   CB  HB3  sing N N 229 
LEU   CG  CD1  sing N N 230 
LEU   CG  CD2  sing N N 231 
LEU   CG  HG   sing N N 232 
LEU   CD1 HD11 sing N N 233 
LEU   CD1 HD12 sing N N 234 
LEU   CD1 HD13 sing N N 235 
LEU   CD2 HD21 sing N N 236 
LEU   CD2 HD22 sing N N 237 
LEU   CD2 HD23 sing N N 238 
LEU   OXT HXT  sing N N 239 
LYS   N   CA   sing N N 240 
LYS   N   H    sing N N 241 
LYS   N   H2   sing N N 242 
LYS   CA  C    sing N N 243 
LYS   CA  CB   sing N N 244 
LYS   CA  HA   sing N N 245 
LYS   C   O    doub N N 246 
LYS   C   OXT  sing N N 247 
LYS   CB  CG   sing N N 248 
LYS   CB  HB2  sing N N 249 
LYS   CB  HB3  sing N N 250 
LYS   CG  CD   sing N N 251 
LYS   CG  HG2  sing N N 252 
LYS   CG  HG3  sing N N 253 
LYS   CD  CE   sing N N 254 
LYS   CD  HD2  sing N N 255 
LYS   CD  HD3  sing N N 256 
LYS   CE  NZ   sing N N 257 
LYS   CE  HE2  sing N N 258 
LYS   CE  HE3  sing N N 259 
LYS   NZ  HZ1  sing N N 260 
LYS   NZ  HZ2  sing N N 261 
LYS   NZ  HZ3  sing N N 262 
LYS   OXT HXT  sing N N 263 
MET   N   CA   sing N N 264 
MET   N   H    sing N N 265 
MET   N   H2   sing N N 266 
MET   CA  C    sing N N 267 
MET   CA  CB   sing N N 268 
MET   CA  HA   sing N N 269 
MET   C   O    doub N N 270 
MET   C   OXT  sing N N 271 
MET   CB  CG   sing N N 272 
MET   CB  HB2  sing N N 273 
MET   CB  HB3  sing N N 274 
MET   CG  SD   sing N N 275 
MET   CG  HG2  sing N N 276 
MET   CG  HG3  sing N N 277 
MET   SD  CE   sing N N 278 
MET   CE  HE1  sing N N 279 
MET   CE  HE2  sing N N 280 
MET   CE  HE3  sing N N 281 
MET   OXT HXT  sing N N 282 
PHE   N   CA   sing N N 283 
PHE   N   H    sing N N 284 
PHE   N   H2   sing N N 285 
PHE   CA  C    sing N N 286 
PHE   CA  CB   sing N N 287 
PHE   CA  HA   sing N N 288 
PHE   C   O    doub N N 289 
PHE   C   OXT  sing N N 290 
PHE   CB  CG   sing N N 291 
PHE   CB  HB2  sing N N 292 
PHE   CB  HB3  sing N N 293 
PHE   CG  CD1  doub Y N 294 
PHE   CG  CD2  sing Y N 295 
PHE   CD1 CE1  sing Y N 296 
PHE   CD1 HD1  sing N N 297 
PHE   CD2 CE2  doub Y N 298 
PHE   CD2 HD2  sing N N 299 
PHE   CE1 CZ   doub Y N 300 
PHE   CE1 HE1  sing N N 301 
PHE   CE2 CZ   sing Y N 302 
PHE   CE2 HE2  sing N N 303 
PHE   CZ  HZ   sing N N 304 
PHE   OXT HXT  sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
TFA   C1  C2   sing N N 336 
TFA   C1  O    doub N N 337 
TFA   C1  OXT  sing N N 338 
TFA   C2  F1   sing N N 339 
TFA   C2  F2   sing N N 340 
TFA   C2  F3   sing N N 341 
TFA   OXT HXT  sing N N 342 
THR   N   CA   sing N N 343 
THR   N   H    sing N N 344 
THR   N   H2   sing N N 345 
THR   CA  C    sing N N 346 
THR   CA  CB   sing N N 347 
THR   CA  HA   sing N N 348 
THR   C   O    doub N N 349 
THR   C   OXT  sing N N 350 
THR   CB  OG1  sing N N 351 
THR   CB  CG2  sing N N 352 
THR   CB  HB   sing N N 353 
THR   OG1 HG1  sing N N 354 
THR   CG2 HG21 sing N N 355 
THR   CG2 HG22 sing N N 356 
THR   CG2 HG23 sing N N 357 
THR   OXT HXT  sing N N 358 
TYR   N   CA   sing N N 359 
TYR   N   H    sing N N 360 
TYR   N   H2   sing N N 361 
TYR   CA  C    sing N N 362 
TYR   CA  CB   sing N N 363 
TYR   CA  HA   sing N N 364 
TYR   C   O    doub N N 365 
TYR   C   OXT  sing N N 366 
TYR   CB  CG   sing N N 367 
TYR   CB  HB2  sing N N 368 
TYR   CB  HB3  sing N N 369 
TYR   CG  CD1  doub Y N 370 
TYR   CG  CD2  sing Y N 371 
TYR   CD1 CE1  sing Y N 372 
TYR   CD1 HD1  sing N N 373 
TYR   CD2 CE2  doub Y N 374 
TYR   CD2 HD2  sing N N 375 
TYR   CE1 CZ   doub Y N 376 
TYR   CE1 HE1  sing N N 377 
TYR   CE2 CZ   sing Y N 378 
TYR   CE2 HE2  sing N N 379 
TYR   CZ  OH   sing N N 380 
TYR   OH  HH   sing N N 381 
TYR   OXT HXT  sing N N 382 
VAL   N   CA   sing N N 383 
VAL   N   H    sing N N 384 
VAL   N   H2   sing N N 385 
VAL   CA  C    sing N N 386 
VAL   CA  CB   sing N N 387 
VAL   CA  HA   sing N N 388 
VAL   C   O    doub N N 389 
VAL   C   OXT  sing N N 390 
VAL   CB  CG1  sing N N 391 
VAL   CB  CG2  sing N N 392 
VAL   CB  HB   sing N N 393 
VAL   CG1 HG11 sing N N 394 
VAL   CG1 HG12 sing N N 395 
VAL   CG1 HG13 sing N N 396 
VAL   CG2 HG21 sing N N 397 
VAL   CG2 HG22 sing N N 398 
VAL   CG2 HG23 sing N N 399 
VAL   OXT HXT  sing N N 400 
# 
_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                    7HDI 
_atom_sites.fract_transf_matrix[1][1]   0.011260 
_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]   0.011260 
_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]   0.025372 
_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 
F 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.612 -16.227 22.156  0.42 59.95 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.603 -15.450 22.366  0.58 59.72 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.643 -15.150 22.310  0.42 59.50 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.566 -14.450 22.590  0.58 59.09 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.301 -13.804 22.029  0.42 57.44 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.124 -13.053 22.331  0.58 56.43 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.418 -13.544 22.479  0.42 57.98 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.179 -12.692 22.855  0.58 57.01 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 17.992 -15.177 23.710  0.42 60.73 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 17.972 -14.570 24.006  0.58 60.58 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 16.962 -14.062 23.844  0.42 61.10 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.876 -13.537 24.209  0.58 61.06 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.351 -16.532 23.973  0.42 61.12 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.436 -15.977 24.243  0.58 61.09 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.938 -15.269 21.659  0.42 71.42 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.846 -14.602 21.962  0.58 70.92 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.676 -15.034 24.382  0.42 72.89 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.668 -14.404 24.660  0.58 72.72 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.450 -14.203 24.656  0.42 73.34 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.406 -13.734 25.033  0.58 73.29 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.421 -13.209 23.887  0.42 73.34 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.277 -12.656 24.259  0.58 73.29 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.372 -14.084 23.075  0.42 73.34 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.260 -13.581 23.460  0.58 73.29 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.888 -16.501 24.825  0.42 73.36 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.991 -16.005 25.105  0.58 73.33 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.722 -16.726 23.261  0.42 73.36 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.805 -16.197 23.539  0.58 73.33 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.044 -17.210 23.997  0.42 73.36 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.175 -16.605 24.232  0.58 73.33 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.608 -12.953 21.274  0.42 54.43 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.413 -12.272 21.519  0.58 52.61 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.061 -11.598 20.992  0.42 51.01 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 18.836 -10.927 21.146  0.58 48.38 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.909 -10.624 21.227  0.42 47.90 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.698 -9.943  21.404  0.58 44.71 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.798 -11.017 21.595  0.42 48.18 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.631 -10.309 21.909  0.58 44.72 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.648 -11.476 19.578  0.42 50.41 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.324 -10.877 19.691  0.58 47.65 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.679 -11.913 18.500  0.42 49.75 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.295 -11.399 18.712  0.58 46.83 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.517 -11.506 18.486  0.42 49.52 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.144 -10.962 18.711  0.58 46.44 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.155 -12.752 17.585  0.42 49.56 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.704 -12.348 17.878  0.58 46.57 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.854 -13.148 20.907  0.42 65.33 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.663 -12.510 21.170  0.58 63.15 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.766 -11.376 21.616  0.42 61.23 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.581 -10.675 21.706  0.58 58.07 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.885 -10.549 19.413  0.42 60.51 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.527 -9.957  19.455  0.58 57.20 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.438 -12.034 19.516  0.42 60.51 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.123 -11.421 19.605  0.58 57.20 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.648 -13.030 16.949  0.42 59.49 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.159 -12.679 17.302  0.58 55.91 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.973 -13.018 17.630  0.42 59.49 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.516 -12.632 17.913  0.58 55.91 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.182 -9.339  21.007  0.42 44.22 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 17.929 -8.678  21.048  0.58 40.82 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.264 -8.265  21.364  0.42 40.38 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.016 -7.590  21.374  0.58 37.03 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.418 -7.777  20.192  0.42 35.99 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.149 -7.152  20.196  0.58 32.33 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.771 -6.732  20.306  0.42 36.03 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.440 -6.146  20.303  0.58 32.04 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.035 -7.093  21.976  0.42 40.95 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 17.788 -6.394  21.940  0.58 38.07 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.058 -6.645  21.103  0.42 41.25 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.684 -5.862  20.982  0.58 38.77 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.907 -9.063  20.639  0.42 53.08 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.623 -8.429  20.606  0.58 49.00 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.661 -8.597  22.047  0.42 48.47 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.421 -7.896  22.072  0.58 44.45 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.418 -6.361  22.141  0.42 49.15 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.156 -5.705  22.197  0.58 45.70 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.436 -7.380  22.812  0.42 49.15 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.294 -6.684  22.717  0.58 45.70 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.471 -6.002  21.452  0.42 49.52 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.099 -5.207  21.308  0.58 46.54 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.413 -8.495  19.071  0.42 31.29 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.183 -7.876  19.080  0.58 27.59 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.523 -8.145  17.969  0.42 26.84 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.254 -7.603  17.992  0.58 23.98 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.091 -8.535  18.318  0.42 25.60 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 13.840 -7.958  18.436  0.58 24.19 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.835 -9.654  18.773  0.42 26.22 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.626 -8.963  19.118  0.58 25.44 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 15.963 -8.857  16.692  0.42 24.01 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.629 -8.426  16.761  0.58 21.56 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.232 -8.310  16.097  0.42 21.89 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 16.939 -8.023  16.134  0.58 19.83 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.220 -7.133  15.368  0.42 21.00 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.021 -6.891  15.341  0.58 19.29 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.433 -8.979  16.259  0.42 21.37 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.079 -8.787  16.323  0.58 19.98 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.385 -6.628  14.816  0.42 20.80 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.222 -6.519  14.757  0.58 19.35 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.601 -8.479  15.708  0.42 21.22 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.280 -8.422  15.740  0.58 20.30 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.575 -7.304  14.987  0.42 20.87 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.350 -7.287  14.958  0.58 19.67 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 16.916 -9.176  18.923  0.42 37.56 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 16.724 -8.527  18.933  0.58 33.12 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.556 -7.189  17.818  0.42 32.22 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.277 -6.664  17.769  0.58 28.80 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.108 -9.796  16.892  0.42 28.82 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.693 -9.359  17.018  0.58 25.88 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.261 -8.768  16.029  0.42 28.82 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 14.932 -8.317  16.094  0.58 25.88 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.420 -6.674  15.250  0.42 25.21 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.260 -6.368  15.204  0.58 23.17 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.455 -9.774  16.746  0.42 25.66 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.035 -9.552  16.854  0.58 23.99 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.365 -5.836  14.330  0.42 24.98 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.265 -5.753  14.228  0.58 23.23 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.402 -8.938  15.826  0.42 25.48 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.039 -8.941  15.880  0.58 24.37 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.359 -6.968  14.618  0.42 25.06 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.155 -7.040  14.567  0.58 23.62 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.154 -7.615  18.091  0.42 24.06 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 12.869 -7.127  18.056  0.58 23.38 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.779 -7.762  18.552  0.42 23.16 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.501 -7.287  18.531  0.58 23.56 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.801 -7.495  17.417  0.42 21.70 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.510 -7.144  17.383  0.58 21.33 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.022 -6.610  16.586  0.42 22.01 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.669 -6.284  16.513  0.58 20.75 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.497 -6.784  19.704  0.42 24.17 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.179 -6.257  19.626  0.58 26.67 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.109 -6.703  19.985  0.42 24.84 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.719 -6.900  20.801  0.58 28.44 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.297 -6.886  17.658  0.42 28.89 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 12.978 -6.461  17.522  0.58 28.07 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.641 -8.665  18.877  0.42 27.81 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.390 -8.171  18.913  0.58 28.29 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 11.966 -7.089  20.498  0.42 29.03 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 11.985 -5.761  19.841  0.58 32.02 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.822 -5.903  19.452  0.42 29.03 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 10.493 -5.653  19.303  0.58 32.02 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 9.981  -6.163  20.617  0.42 29.82 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 10.537 -6.330  21.392  0.58 34.14 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.715  -8.265  17.389  0.42 20.18 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.482  -7.990  17.388  0.58 19.98 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.622  -7.986  16.480  0.42 19.04 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.409  -7.867  16.426  0.58 19.10 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.814  -8.450  15.055  0.42 17.66 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.696  -8.430  15.056  0.58 17.56 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.121  -7.956  14.161  0.42 18.31 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 7.939  -8.147  14.121  0.58 18.06 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.594  -8.952  17.891  0.42 24.23 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.391  -8.645  17.940  0.58 23.99 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.818  -8.400  16.831  0.42 22.86 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.625  -8.316  16.771  0.58 22.94 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.476  -7.027  16.459  0.42 22.86 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.194  -6.928  16.316  0.58 22.94 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.735  -9.379  14.810  0.42 16.39 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.754  -9.221  14.901  0.58 16.80 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 9.989  -9.886  13.471  0.42 15.16 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.083 -9.777  13.599  0.58 15.82 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.141  -11.118 13.185  0.42 14.51 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.256  -11.023 13.317  0.58 15.66 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.866  -11.938 14.068  0.42 15.22 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 9.002  -11.844 14.207  0.58 17.19 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.463 -10.272 13.302  0.42 14.95 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.579 -10.102 13.498  0.58 16.06 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.409 -9.102  13.173  0.42 14.80 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.433 -8.875  13.251  0.58 15.79 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.748 -8.343  14.278  0.42 15.06 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 12.689 -7.982  14.275  0.58 16.86 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 12.953 -8.757  11.944  0.42 14.62 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 12.938 -8.594  11.989  0.58 15.03 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.603 -7.268  14.168  0.42 15.46 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.437 -6.849  14.061  0.58 16.92 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.809 -7.686  11.822  0.42 14.92 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 13.696 -7.461  11.763  0.58 15.36 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.128 -6.945  12.936  0.42 15.65 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 13.939 -6.594  12.802  0.58 15.75 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 14.979 -5.879  12.816  0.42 16.65 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 14.680 -5.460  12.584  0.58 15.89 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.233 -9.734  15.414  0.42 19.69 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.286 -9.461  15.536  0.58 20.18 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.775  -9.201  12.815  0.42 18.21 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 9.874  -9.123  12.920  0.58 19.00 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.741 -10.794 14.070  0.42 17.95 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 11.868 -10.519 14.326  0.58 19.28 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.543 -10.803 12.496  0.42 17.95 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.707 -10.718 12.758  0.58 19.28 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.383 -8.560  15.109  0.42 18.09 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.342 -8.158  15.125  0.58 20.25 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.735 -9.259  11.188  0.42 17.56 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.767 -9.183  11.285  0.58 18.05 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.815 -6.763  14.919  0.42 18.57 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 13.606 -6.266  14.762  0.58 20.32 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.167 -7.465  10.993  0.42 17.92 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.036 -7.286  10.915  0.58 18.45 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 15.084 -5.517  13.565  0.42 20.00 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 14.765 -5.029  13.300  0.58 19.09 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.739  -11.245 11.928  0.42 14.62 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 8.829  -11.147 12.067  0.58 15.45 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.201  -12.493 11.417  0.42 14.54 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.188  -12.350 11.563  0.58 15.16 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.362  -13.415 11.062  0.42 13.53 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.270  -13.315 11.093  0.58 14.69 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.386 -12.966 10.542  0.42 12.77 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.153 -12.935 10.320  0.58 13.92 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.383  -12.207 10.162  0.42 16.04 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.285  -11.985 10.387  0.58 15.97 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.658  -13.394 9.537   0.42 18.09 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 6.692  -13.150 9.593   0.58 17.80 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.603  -13.912 10.493  0.42 18.85 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.683  -13.895 10.433  0.58 18.71 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 6.049  -12.998 8.204   0.42 19.48 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 6.072  -12.641 8.301   0.58 19.05 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 8.781  -10.617 11.339  0.42 17.57 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 8.912  -10.526 11.472  0.58 18.56 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.639  -12.913 12.088  0.42 17.47 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.658  -12.765 12.260  0.58 18.21 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.712  -11.543 10.381  0.42 19.27 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 6.542  -11.459 10.725  0.58 19.18 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.983  -11.847 9.488   0.42 19.27 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.801  -11.443 9.766   0.58 19.18 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.298  -14.106 9.373   0.42 21.72 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 7.401  -13.766 9.354   0.58 21.38 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.134  -14.649 10.074  0.42 22.64 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 5.318  -14.628 9.912   0.58 22.46 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 6.033  -14.215 11.308  0.42 22.64 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 6.123  -14.238 11.226  0.58 22.46 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.982  -13.195 10.695  0.42 22.64 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 4.973  -13.286 10.690  0.58 22.46 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.595  -13.766 7.826   0.42 23.40 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 5.732  -13.402 7.802   0.58 22.87 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.417  -12.277 8.350   0.42 23.40 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 5.347  -12.036 8.517   0.58 22.87 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.756  -12.704 7.609   0.42 23.40 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 6.749  -12.182 7.783   0.58 22.87 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.203  -14.708 11.345  0.42 14.12 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.189  -14.561 11.547  0.58 15.74 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.248 -15.696 11.100  0.42 14.27 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.148 -15.583 11.152  0.58 15.28 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.956  -16.377 9.768   0.42 14.32 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 9.776  -16.100 9.769   0.58 14.83 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 8.966  -17.105 9.645   0.42 15.47 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.642  -16.543 9.557   0.58 14.98 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.303 -16.703 12.249  0.42 14.59 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.124 -16.713 12.176  0.58 15.81 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.330 -17.819 12.088  0.42 14.52 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.168 -17.794 11.981  0.58 15.54 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.441 -18.644 13.372  0.42 14.48 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.177 -18.707 13.196  0.58 16.08 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.411 -19.822 13.227  0.42 14.75 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.197 -19.835 13.077  0.58 16.84 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.811 -19.390 12.931  0.42 14.39 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.595 -19.319 12.937  0.58 16.65 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.482  -15.045 11.681  0.42 16.96 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.579  -14.836 12.082  0.58 18.90 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 11.104 -15.246 11.036  0.42 17.14 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 11.042 -15.198 11.114  0.58 18.36 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.517 -16.222 13.066  0.42 17.52 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.262 -16.328 13.054  0.58 18.99 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.430  -17.116 12.338  0.42 17.52 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.256  -17.136 12.137  0.58 18.99 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 11.056 -18.406 11.367  0.42 17.44 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 10.957 -18.319 11.195  0.58 18.67 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.199 -17.430 11.896  0.42 17.44 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 12.048 -17.386 11.891  0.58 18.67 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.761 -18.075 14.091  0.42 17.39 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.394 -18.185 13.984  0.58 19.31 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.565 -19.000 13.598  0.42 17.39 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.298 -19.107 13.294  0.58 19.31 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.422 -20.328 14.054  0.42 17.72 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 12.158 -20.384 13.874  0.58 20.23 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 12.112 -20.387 12.497  0.42 17.72 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 11.994 -20.366 12.293  0.58 20.23 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.315 -20.101 12.742  0.42 17.29 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 14.136 -19.977 12.675  0.58 20.00 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.821 -18.838 12.234  0.42 17.29 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 13.625 -18.666 12.335  0.58 20.00 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 14.158 -18.973 13.636  0.42 17.29 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 13.885 -19.007 13.719  0.58 20.00 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.809 -16.138 8.767   0.42 14.06 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.714 -16.036 8.822   0.58 14.84 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.593 -16.731 7.450   0.42 14.40 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.495 -16.584 7.489   0.58 14.93 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.181 -18.134 7.341   0.42 14.99 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.079 -17.978 7.333   0.58 14.83 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.527 -19.039 6.810   0.42 15.59 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.458 -18.835 6.699   0.58 14.98 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.177 -15.847 6.343   0.42 14.60 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.092 -15.672 6.411   0.58 15.65 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.477 -14.518 6.044   0.42 15.27 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.505 -14.265 6.297   0.58 16.71 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.228 -13.763 4.958   0.42 15.66 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 11.091 -13.535 5.091   0.58 17.09 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 9.020  -14.732 5.646   0.42 15.57 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 8.983  -14.326 6.221   0.58 17.44 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.512 -15.644 8.827   0.42 16.88 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.489 -15.682 8.927   0.58 17.82 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.639  -16.799 7.298   0.42 17.30 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.541  -16.659 7.328   0.58 17.94 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 12.093 -15.636 6.579   0.42 17.54 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 12.040 -15.576 6.594   0.58 18.80 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 11.172 -16.361 5.519   0.42 17.54 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 10.975 -16.106 5.552   0.58 18.80 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.487 -13.974 6.844   0.42 18.34 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.744 -13.765 7.091   0.58 20.07 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.787 -12.914 4.799   0.42 18.81 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.707 -12.648 5.041   0.58 20.52 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.140 -13.612 5.253   0.42 18.81 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 12.056 -13.472 5.198   0.58 20.52 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.228 -14.293 4.144   0.42 18.81 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 10.883 -14.035 4.285   0.58 20.52 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.775  -14.078 4.972   0.42 18.70 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.647  -13.454 5.967   0.58 20.95 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 8.918  -15.628 5.290   0.42 18.70 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.726  -14.989 5.562   0.58 20.95 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.460  -14.626 6.431   0.42 18.70 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.634  -14.574 7.093   0.58 20.95 ?  12  LEU   A HD23 1 
ATOM   319  N N    A THR   A 1 13  ? 12.405 -18.327 7.827   0.42 14.99 ?  13  THR   A N    1 
ATOM   320  N N    B THR   A 1 13  ? 12.266 -18.210 7.888   0.58 14.75 ?  13  THR   A N    1 
ATOM   321  C CA   A THR   A 1 13  ? 13.090 -19.613 7.756   0.42 15.25 ?  13  THR   A CA   1 
ATOM   322  C CA   B THR   A 1 13  ? 12.961 -19.486 7.811   0.58 15.23 ?  13  THR   A CA   1 
ATOM   323  C C    A THR   A 1 13  ? 13.857 -19.812 9.055   0.42 15.05 ?  13  THR   A C    1 
ATOM   324  C C    B THR   A 1 13  ? 13.695 -19.701 9.125   0.58 15.36 ?  13  THR   A C    1 
ATOM   325  O O    A THR   A 1 13  ? 13.744 -19.024 10.000  0.42 15.00 ?  13  THR   A O    1 
ATOM   326  O O    B THR   A 1 13  ? 13.572 -18.920 10.074  0.58 15.71 ?  13  THR   A O    1 
ATOM   327  C CB   A THR   A 1 13  ? 14.042 -19.687 6.554   0.42 16.16 ?  13  THR   A CB   1 
ATOM   328  C CB   B THR   A 1 13  ? 13.975 -19.514 6.659   0.58 15.90 ?  13  THR   A CB   1 
ATOM   329  O OG1  A THR   A 1 13  ? 15.180 -18.849 6.792   0.42 15.89 ?  13  THR   A OG1  1 
ATOM   330  O OG1  B THR   A 1 13  ? 14.976 -18.519 6.897   0.58 15.47 ?  13  THR   A OG1  1 
ATOM   331  C CG2  A THR   A 1 13  ? 13.363 -19.246 5.272   0.42 16.85 ?  13  THR   A CG2  1 
ATOM   332  C CG2  B THR   A 1 13  ? 13.316 -19.284 5.305   0.58 16.89 ?  13  THR   A CG2  1 
ATOM   333  H H    A THR   A 1 13  ? 12.868 -17.712 8.217   0.42 18.01 ?  13  THR   A H    1 
ATOM   334  H H    B THR   A 1 13  ? 12.709 -17.612 8.320   0.58 17.72 ?  13  THR   A H    1 
ATOM   335  H HA   A THR   A 1 13  ? 12.435 -20.323 7.676   0.42 18.32 ?  13  THR   A HA   1 
ATOM   336  H HA   B THR   A 1 13  ? 12.325 -20.203 7.683   0.58 18.29 ?  13  THR   A HA   1 
ATOM   337  H HB   A THR   A 1 13  ? 14.335 -20.606 6.447   0.42 19.41 ?  13  THR   A HB   1 
ATOM   338  H HB   B THR   A 1 13  ? 14.410 -20.378 6.635   0.58 19.10 ?  13  THR   A HB   1 
ATOM   339  H HG1  A THR   A 1 13  ? 15.721 -18.903 6.147   0.42 19.09 ?  13  THR   A HG1  1 
ATOM   340  H HG1  B THR   A 1 13  ? 15.542 -18.510 6.272   0.58 18.58 ?  13  THR   A HG1  1 
ATOM   341  H HG21 A THR   A 1 13  ? 13.963 -19.386 4.521   0.42 20.24 ?  13  THR   A HG21 1 
ATOM   342  H HG21 B THR   A 1 13  ? 13.979 -19.366 4.597   0.58 20.29 ?  13  THR   A HG21 1 
ATOM   343  H HG22 A THR   A 1 13  ? 12.557 -19.762 5.133   0.42 20.24 ?  13  THR   A HG22 1 
ATOM   344  H HG22 B THR   A 1 13  ? 12.624 -19.947 5.164   0.58 20.29 ?  13  THR   A HG22 1 
ATOM   345  H HG23 A THR   A 1 13  ? 13.137 -18.306 5.323   0.42 20.24 ?  13  THR   A HG23 1 
ATOM   346  H HG23 B THR   A 1 13  ? 12.926 -18.401 5.270   0.58 20.29 ?  13  THR   A HG23 1 
ATOM   347  N N    A ASP   A 1 14  ? 14.681 -20.861 9.086   0.42 15.08 ?  14  ASP   A N    1 
ATOM   348  N N    B ASP   A 1 14  ? 14.499 -20.761 9.159   0.58 15.72 ?  14  ASP   A N    1 
ATOM   349  C CA   A ASP   A 1 14  ? 15.472 -21.137 10.276  0.42 15.86 ?  14  ASP   A CA   1 
ATOM   350  C CA   B ASP   A 1 14  ? 15.338 -21.026 10.315  0.58 16.30 ?  14  ASP   A CA   1 
ATOM   351  C C    A ASP   A 1 14  ? 16.339 -19.947 10.674  0.42 14.91 ?  14  ASP   A C    1 
ATOM   352  C C    B ASP   A 1 14  ? 16.153 -19.798 10.706  0.58 15.42 ?  14  ASP   A C    1 
ATOM   353  O O    A ASP   A 1 14  ? 16.684 -19.802 11.853  0.42 14.53 ?  14  ASP   A O    1 
ATOM   354  O O    B ASP   A 1 14  ? 16.289 -19.486 11.895  0.58 15.89 ?  14  ASP   A O    1 
ATOM   355  C CB   A ASP   A 1 14  ? 16.353 -22.360 10.039  0.42 18.61 ?  14  ASP   A CB   1 
ATOM   356  C CB   B ASP   A 1 14  ? 16.277 -22.185 9.992   0.58 19.05 ?  14  ASP   A CB   1 
ATOM   357  C CG   A ASP   A 1 14  ? 17.280 -22.620 11.193  0.42 21.28 ?  14  ASP   A CG   1 
ATOM   358  C CG   B ASP   A 1 14  ? 17.199 -22.506 11.139  0.58 22.84 ?  14  ASP   A CG   1 
ATOM   359  O OD1  A ASP   A 1 14  ? 16.825 -23.252 12.176  0.42 22.17 ?  14  ASP   A OD1  1 
ATOM   360  O OD1  B ASP   A 1 14  ? 16.690 -22.702 12.265  0.58 24.06 ?  14  ASP   A OD1  1 
ATOM   361  O OD2  A ASP   A 1 14  ? 18.441 -22.164 11.125  0.42 22.72 -1 14  ASP   A OD2  1 
ATOM   362  O OD2  B ASP   A 1 14  ? 18.423 -22.565 10.918  0.58 25.16 -1 14  ASP   A OD2  1 
ATOM   363  H H    A ASP   A 1 14  ? 14.805 -21.415 8.439   0.42 18.11 ?  14  ASP   A H    1 
ATOM   364  H H    B ASP   A 1 14  ? 14.579 -21.328 8.525   0.58 18.88 ?  14  ASP   A H    1 
ATOM   365  H HA   A ASP   A 1 14  ? 14.887 -21.341 11.019  0.42 19.05 ?  14  ASP   A HA   1 
ATOM   366  H HA   B ASP   A 1 14  ? 14.782 -21.286 11.068  0.58 19.58 ?  14  ASP   A HA   1 
ATOM   367  H HB2  A ASP   A 1 14  ? 15.790 -23.150 9.942   0.42 22.35 ?  14  ASP   A HB2  1 
ATOM   368  H HB2  B ASP   A 1 14  ? 15.743 -22.980 9.792   0.58 22.88 ?  14  ASP   A HB2  1 
ATOM   369  H HB3  A ASP   A 1 14  ? 16.878 -22.233 9.232   0.42 22.35 ?  14  ASP   A HB3  1 
ATOM   370  H HB3  B ASP   A 1 14  ? 16.812 -21.955 9.214   0.58 22.88 ?  14  ASP   A HB3  1 
ATOM   371  N N    . ASN   A 1 15  ? 16.701 -19.085 9.720   1.00 14.72 ?  15  ASN   A N    1 
ATOM   372  C CA   . ASN   A 1 15  ? 17.681 -18.035 9.976   1.00 14.78 ?  15  ASN   A CA   1 
ATOM   373  C C    . ASN   A 1 15  ? 17.314 -16.653 9.454   1.00 14.80 ?  15  ASN   A C    1 
ATOM   374  O O    . ASN   A 1 15  ? 18.088 -15.720 9.684   1.00 16.49 ?  15  ASN   A O    1 
ATOM   375  C CB   . ASN   A 1 15  ? 19.057 -18.433 9.411   1.00 14.92 ?  15  ASN   A CB   1 
ATOM   376  C CG   . ASN   A 1 15  ? 19.064 -18.530 7.900   1.00 15.31 ?  15  ASN   A CG   1 
ATOM   377  O OD1  . ASN   A 1 15  ? 18.368 -19.366 7.320   1.00 16.28 ?  15  ASN   A OD1  1 
ATOM   378  N ND2  . ASN   A 1 15  ? 19.857 -17.680 7.250   1.00 15.04 ?  15  ASN   A ND2  1 
ATOM   379  H H    A ASN   A 1 15  ? 16.388 -19.088 8.928   0.42 17.68 ?  15  ASN   A H    1 
ATOM   380  H H    B ASN   A 1 15  ? 16.526 -19.204 8.893   0.58 17.68 ?  15  ASN   A H    1 
ATOM   381  H HA   . ASN   A 1 15  ? 17.796 -17.953 10.936  1.00 17.75 ?  15  ASN   A HA   1 
ATOM   382  H HB2  . ASN   A 1 15  ? 19.714 -17.760 9.676   1.00 17.92 ?  15  ASN   A HB2  1 
ATOM   383  H HB3  . ASN   A 1 15  ? 19.317 -19.297 9.771   1.00 17.92 ?  15  ASN   A HB3  1 
ATOM   384  H HD21 . ASN   A 1 15  ? 19.889 -17.691 6.390   1.00 18.07 ?  15  ASN   A HD21 1 
ATOM   385  H HD22 . ASN   A 1 15  ? 20.326 -17.100 7.685   1.00 18.07 ?  15  ASN   A HD22 1 
ATOM   386  N N    A VAL   A 1 16  ? 16.182 -16.487 8.768   0.42 14.40 ?  16  VAL   A N    1 
ATOM   387  N N    B VAL   A 1 16  ? 16.181 -16.489 8.768   0.58 14.56 ?  16  VAL   A N    1 
ATOM   388  C CA   A VAL   A 1 16  ? 15.802 -15.208 8.175   0.42 14.35 ?  16  VAL   A CA   1 
ATOM   389  C CA   B VAL   A 1 16  ? 15.790 -15.215 8.171   0.58 14.78 ?  16  VAL   A CA   1 
ATOM   390  C C    A VAL   A 1 16  ? 14.524 -14.704 8.832   0.42 14.11 ?  16  VAL   A C    1 
ATOM   391  C C    B VAL   A 1 16  ? 14.523 -14.710 8.848   0.58 14.34 ?  16  VAL   A C    1 
ATOM   392  O O    A VAL   A 1 16  ? 13.524 -15.431 8.914   0.42 14.05 ?  16  VAL   A O    1 
ATOM   393  O O    B VAL   A 1 16  ? 13.526 -15.440 8.956   0.58 14.26 ?  16  VAL   A O    1 
ATOM   394  C CB   A VAL   A 1 16  ? 15.646 -15.299 6.646   0.42 14.63 ?  16  VAL   A CB   1 
ATOM   395  C CB   B VAL   A 1 16  ? 15.598 -15.329 6.648   0.58 15.45 ?  16  VAL   A CB   1 
ATOM   396  C CG1  A VAL   A 1 16  ? 15.231 -13.946 6.074   0.42 15.04 ?  16  VAL   A CG1  1 
ATOM   397  C CG1  B VAL   A 1 16  ? 15.147 -13.991 6.058   0.58 16.04 ?  16  VAL   A CG1  1 
ATOM   398  C CG2  A VAL   A 1 16  ? 16.943 -15.773 6.004   0.42 14.81 ?  16  VAL   A CG2  1 
ATOM   399  C CG2  B VAL   A 1 16  ? 16.880 -15.812 5.975   0.58 15.83 ?  16  VAL   A CG2  1 
ATOM   400  H H    A VAL   A 1 16  ? 15.615 -17.121 8.629   0.42 17.30 ?  16  VAL   A H    1 
ATOM   401  H H    B VAL   A 1 16  ? 15.620 -17.128 8.627   0.58 17.48 ?  16  VAL   A H    1 
ATOM   402  H HA   A VAL   A 1 16  ? 16.503 -14.566 8.357   0.42 17.23 ?  16  VAL   A HA   1 
ATOM   403  H HA   B VAL   A 1 16  ? 16.497 -14.572 8.333   0.58 17.75 ?  16  VAL   A HA   1 
ATOM   404  H HB   A VAL   A 1 16  ? 14.955 -15.946 6.436   0.42 17.57 ?  16  VAL   A HB   1 
ATOM   405  H HB   B VAL   A 1 16  ? 14.909 -15.987 6.472   0.58 18.56 ?  16  VAL   A HB   1 
ATOM   406  H HG11 A VAL   A 1 16  ? 15.337 -13.968 5.112   0.42 18.07 ?  16  VAL   A HG11 1 
ATOM   407  H HG11 B VAL   A 1 16  ? 15.214 -14.038 5.092   0.58 19.26 ?  16  VAL   A HG11 1 
ATOM   408  H HG12 A VAL   A 1 16  ? 14.303 -13.779 6.302   0.42 18.07 ?  16  VAL   A HG12 1 
ATOM   409  H HG12 B VAL   A 1 16  ? 14.227 -13.827 6.318   0.58 19.26 ?  16  VAL   A HG12 1 
ATOM   410  H HG13 A VAL   A 1 16  ? 15.797 -13.257 6.455   0.42 18.07 ?  16  VAL   A HG13 1 
ATOM   411  H HG13 B VAL   A 1 16  ? 15.721 -13.287 6.397   0.58 19.26 ?  16  VAL   A HG13 1 
ATOM   412  H HG21 A VAL   A 1 16  ? 16.840 -15.764 5.041   0.42 17.79 ?  16  VAL   A HG21 1 
ATOM   413  H HG21 B VAL   A 1 16  ? 16.741 -15.838 5.016   0.58 19.01 ?  16  VAL   A HG21 1 
ATOM   414  H HG22 A VAL   A 1 16  ? 17.663 -15.180 6.267   0.42 17.79 ?  16  VAL   A HG22 1 
ATOM   415  H HG22 B VAL   A 1 16  ? 17.603 -15.202 6.189   0.58 19.01 ?  16  VAL   A HG22 1 
ATOM   416  H HG23 A VAL   A 1 16  ? 17.135 -16.677 6.307   0.42 17.79 ?  16  VAL   A HG23 1 
ATOM   417  H HG23 B VAL   A 1 16  ? 17.096 -16.704 6.299   0.58 19.01 ?  16  VAL   A HG23 1 
ATOM   418  N N    . TYR   A 1 17  ? 14.567 -13.449 9.280   1.00 13.74 ?  17  TYR   A N    1 
ATOM   419  C CA   . TYR   A 1 17  ? 13.463 -12.771 9.949   1.00 13.32 ?  17  TYR   A CA   1 
ATOM   420  C C    . TYR   A 1 17  ? 13.201 -11.451 9.223   1.00 14.41 ?  17  TYR   A C    1 
ATOM   421  O O    . TYR   A 1 17  ? 14.106 -10.897 8.597   1.00 14.59 ?  17  TYR   A O    1 
ATOM   422  C CB   . TYR   A 1 17  ? 13.866 -12.479 11.396  1.00 13.86 ?  17  TYR   A CB   1 
ATOM   423  C CG   . TYR   A 1 17  ? 14.072 -13.733 12.218  1.00 15.50 ?  17  TYR   A CG   1 
ATOM   424  C CD1  . TYR   A 1 17  ? 15.260 -14.462 12.152  1.00 16.53 ?  17  TYR   A CD1  1 
ATOM   425  C CD2  . TYR   A 1 17  ? 13.069 -14.203 13.055  1.00 15.79 ?  17  TYR   A CD2  1 
ATOM   426  C CE1  . TYR   A 1 17  ? 15.437 -15.635 12.896  1.00 17.18 ?  17  TYR   A CE1  1 
ATOM   427  C CE2  . TYR   A 1 17  ? 13.233 -15.380 13.801  1.00 16.74 ?  17  TYR   A CE2  1 
ATOM   428  C CZ   . TYR   A 1 17  ? 14.419 -16.080 13.720  1.00 17.35 ?  17  TYR   A CZ   1 
ATOM   429  O OH   . TYR   A 1 17  ? 14.575 -17.228 14.463  1.00 18.40 ?  17  TYR   A OH   1 
ATOM   430  H H    A TYR   A 1 17  ? 15.267 -12.949 9.202   0.42 16.50 ?  17  TYR   A H    1 
ATOM   431  H H    B TYR   A 1 17  ? 15.261 -12.943 9.182   0.58 16.50 ?  17  TYR   A H    1 
ATOM   432  H HA   . TYR   A 1 17  ? 12.667 -13.324 9.930   1.00 16.00 ?  17  TYR   A HA   1 
ATOM   433  H HB2  . TYR   A 1 17  ? 14.695 -11.985 11.395  1.00 16.65 ?  17  TYR   A HB2  1 
ATOM   434  H HB3  . TYR   A 1 17  ? 13.167 -11.965 11.813  1.00 16.65 ?  17  TYR   A HB3  1 
ATOM   435  H HD1  . TYR   A 1 17  ? 15.946 -14.164 11.595  1.00 19.85 ?  17  TYR   A HD1  1 
ATOM   436  H HD2  . TYR   A 1 17  ? 12.263 -13.744 13.110  1.00 18.96 ?  17  TYR   A HD2  1 
ATOM   437  H HE1  . TYR   A 1 17  ? 16.245 -16.102 12.849  1.00 20.63 ?  17  TYR   A HE1  1 
ATOM   438  H HE2  . TYR   A 1 17  ? 12.553 -15.673 14.361  1.00 20.11 ?  17  TYR   A HE2  1 
ATOM   439  H HH   . TYR   A 1 17  ? 13.826 -17.479 14.747  1.00 22.09 ?  17  TYR   A HH   1 
ATOM   440  N N    A ILE   A 1 18  ? 11.964 -10.941 9.298   0.42 14.22 ?  18  ILE   A N    1 
ATOM   441  N N    B ILE   A 1 18  ? 11.975 -10.931 9.328   0.58 14.06 ?  18  ILE   A N    1 
ATOM   442  C CA   A ILE   A 1 18  ? 11.576 -9.763  8.515   0.42 14.17 ?  18  ILE   A CA   1 
ATOM   443  C CA   B ILE   A 1 18  ? 11.601 -9.739  8.570   0.58 13.91 ?  18  ILE   A CA   1 
ATOM   444  C C    A ILE   A 1 18  ? 10.582 -8.898  9.289   0.42 14.65 ?  18  ILE   A C    1 
ATOM   445  C C    B ILE   A 1 18  ? 10.630 -8.875  9.367   0.58 14.01 ?  18  ILE   A C    1 
ATOM   446  O O    A ILE   A 1 18  ? 9.725  -9.404  10.017  0.42 14.59 ?  18  ILE   A O    1 
ATOM   447  O O    B ILE   A 1 18  ? 9.814  -9.372  10.149  0.58 14.13 ?  18  ILE   A O    1 
ATOM   448  C CB   A ILE   A 1 18  ? 11.049 -10.182 7.119   0.42 14.21 ?  18  ILE   A CB   1 
ATOM   449  C CB   B ILE   A 1 18  ? 11.037 -10.137 7.187   0.58 14.37 ?  18  ILE   A CB   1 
ATOM   450  C CG1  A ILE   A 1 18  ? 10.936 -8.978  6.184   0.42 15.08 ?  18  ILE   A CG1  1 
ATOM   451  C CG1  B ILE   A 1 18  ? 11.005 -8.942  6.237   0.58 15.59 ?  18  ILE   A CG1  1 
ATOM   452  C CG2  A ILE   A 1 18  ? 9.723  -10.938 7.233   0.42 14.44 ?  18  ILE   A CG2  1 
ATOM   453  C CG2  B ILE   A 1 18  ? 9.664  -10.777 7.332   0.58 15.41 ?  18  ILE   A CG2  1 
ATOM   454  C CD1  A ILE   A 1 18  ? 10.700 -9.364  4.743   0.42 16.56 ?  18  ILE   A CD1  1 
ATOM   455  C CD1  B ILE   A 1 18  ? 10.768 -9.344  4.806   0.58 17.12 ?  18  ILE   A CD1  1 
ATOM   456  H H    A ILE   A 1 18  ? 11.333 -11.265 9.785   0.42 17.08 ?  18  ILE   A H    1 
ATOM   457  H H    B ILE   A 1 18  ? 11.348 -11.257 9.820   0.58 16.89 ?  18  ILE   A H    1 
ATOM   458  H HA   A ILE   A 1 18  ? 12.366 -9.226  8.368   0.42 17.02 ?  18  ILE   A HA   1 
ATOM   459  H HA   B ILE   A 1 18  ? 12.406 -9.220  8.413   0.58 16.71 ?  18  ILE   A HA   1 
ATOM   460  H HB   A ILE   A 1 18  ? 11.694 -10.790 6.734   0.42 17.07 ?  18  ILE   A HB   1 
ATOM   461  H HB   B ILE   A 1 18  ? 11.629 -10.799 6.803   0.58 17.26 ?  18  ILE   A HB   1 
ATOM   462  H HG12 A ILE   A 1 18  ? 10.197 -8.422  6.467   0.42 18.11 ?  18  ILE   A HG12 1 
ATOM   463  H HG12 B ILE   A 1 18  ? 10.292 -8.343  6.502   0.58 18.72 ?  18  ILE   A HG12 1 
ATOM   464  H HG13 A ILE   A 1 18  ? 11.765 -8.474  6.221   0.42 18.11 ?  18  ILE   A HG13 1 
ATOM   465  H HG13 B ILE   A 1 18  ? 11.859 -8.482  6.278   0.58 18.72 ?  18  ILE   A HG13 1 
ATOM   466  H HG21 A ILE   A 1 18  ? 9.501  -11.318 6.366   0.42 17.35 ?  18  ILE   A HG21 1 
ATOM   467  H HG21 B ILE   A 1 18  ? 9.420  -11.190 6.488   0.58 18.51 ?  18  ILE   A HG21 1 
ATOM   468  H HG22 A ILE   A 1 18  ? 9.819  -11.647 7.887   0.42 17.35 ?  18  ILE   A HG22 1 
ATOM   469  H HG22 B ILE   A 1 18  ? 9.703  -11.448 8.030   0.58 18.51 ?  18  ILE   A HG22 1 
ATOM   470  H HG23 A ILE   A 1 18  ? 9.027  -10.323 7.510   0.42 17.35 ?  18  ILE   A HG23 1 
ATOM   471  H HG23 B ILE   A 1 18  ? 9.018  -10.093 7.565   0.58 18.51 ?  18  ILE   A HG23 1 
ATOM   472  H HD11 A ILE   A 1 18  ? 10.716 -8.563  4.195   0.42 19.89 ?  18  ILE   A HD11 1 
ATOM   473  H HD11 B ILE   A 1 18  ? 10.827 -8.557  4.242   0.58 20.56 ?  18  ILE   A HD11 1 
ATOM   474  H HD12 A ILE   A 1 18  ? 11.398 -9.974  4.459   0.42 19.89 ?  18  ILE   A HD12 1 
ATOM   475  H HD12 B ILE   A 1 18  ? 11.439 -9.991  4.544   0.58 20.56 ?  18  ILE   A HD12 1 
ATOM   476  H HD13 A ILE   A 1 18  ? 9.834  -9.796  4.670   0.42 19.89 ?  18  ILE   A HD13 1 
ATOM   477  H HD13 B ILE   A 1 18  ? 9.882  -9.736  4.732   0.58 20.56 ?  18  ILE   A HD13 1 
ATOM   478  N N    A LYS   A 1 19  ? 10.683 -7.576  9.098   0.42 14.89 ?  19  LYS   A N    1 
ATOM   479  N N    B LYS   A 1 19  ? 10.709 -7.565  9.136   0.58 14.14 ?  19  LYS   A N    1 
ATOM   480  C CA   A LYS   A 1 19  ? 9.906  -6.614  9.875   0.42 15.24 ?  19  LYS   A CA   1 
ATOM   481  C CA   B LYS   A 1 19  ? 9.834  -6.596  9.780   0.58 14.93 ?  19  LYS   A CA   1 
ATOM   482  C C    A LYS   A 1 19  ? 9.757  -5.316  9.093   0.42 14.80 ?  19  LYS   A C    1 
ATOM   483  C C    B LYS   A 1 19  ? 9.635  -5.416  8.838   0.58 14.91 ?  19  LYS   A C    1 
ATOM   484  O O    A LYS   A 1 19  ? 10.683 -4.907  8.391   0.42 14.80 ?  19  LYS   A O    1 
ATOM   485  O O    B LYS   A 1 19  ? 10.539 -5.052  8.083   0.58 14.75 ?  19  LYS   A O    1 
ATOM   486  C CB   A LYS   A 1 19  ? 10.613 -6.330  11.207  0.42 15.52 ?  19  LYS   A CB   1 
ATOM   487  C CB   B LYS   A 1 19  ? 10.485 -6.104  11.077  0.58 14.98 ?  19  LYS   A CB   1 
ATOM   488  C CG   A LYS   A 1 19  ? 9.944  -5.311  12.121  0.42 16.38 ?  19  LYS   A CG   1 
ATOM   489  C CG   B LYS   A 1 19  ? 9.627  -5.209  11.956  0.58 16.48 ?  19  LYS   A CG   1 
ATOM   490  C CD   A LYS   A 1 19  ? 10.822 -5.066  13.345  0.42 16.85 ?  19  LYS   A CD   1 
ATOM   491  C CD   B LYS   A 1 19  ? 10.418 -4.833  13.202  0.58 17.48 ?  19  LYS   A CD   1 
ATOM   492  C CE   A LYS   A 1 19  ? 10.184 -4.121  14.344  0.42 17.23 ?  19  LYS   A CE   1 
ATOM   493  C CE   B LYS   A 1 19  ? 9.652  -3.930  14.150  0.58 18.32 ?  19  LYS   A CE   1 
ATOM   494  N NZ   A LYS   A 1 19  ? 11.050 -3.952  15.544  0.42 17.25 ?  19  LYS   A NZ   1 
ATOM   495  N NZ   B LYS   A 1 19  ? 10.511 -3.546  15.309  0.58 18.39 ?  19  LYS   A NZ   1 
ATOM   496  H H    A LYS   A 1 19  ? 11.200 -7.208  8.506   0.42 17.89 ?  19  LYS   A H    1 
ATOM   497  H H    B LYS   A 1 19  ? 11.284 -7.212  8.595   0.58 16.98 ?  19  LYS   A H    1 
ATOM   498  H HA   A LYS   A 1 19  ? 9.024  -6.960  10.049  0.42 18.31 ?  19  LYS   A HA   1 
ATOM   499  H HA   B LYS   A 1 19  ? 8.981  -7.018  9.981   0.58 17.93 ?  19  LYS   A HA   1 
ATOM   500  H HB2  A LYS   A 1 19  ? 10.664 -7.164  11.698  0.42 18.64 ?  19  LYS   A HB2  1 
ATOM   501  H HB2  B LYS   A 1 19  ? 10.733 -6.878  11.607  0.58 18.00 ?  19  LYS   A HB2  1 
ATOM   502  H HB3  A LYS   A 1 19  ? 11.506 -6.008  11.019  0.42 18.64 ?  19  LYS   A HB3  1 
ATOM   503  H HB3  B LYS   A 1 19  ? 11.280 -5.605  10.842  0.58 18.00 ?  19  LYS   A HB3  1 
ATOM   504  H HG2  A LYS   A 1 19  ? 9.831  -4.469  11.653  0.42 19.68 ?  19  LYS   A HG2  1 
ATOM   505  H HG2  B LYS   A 1 19  ? 9.397  -4.398  11.474  0.58 19.80 ?  19  LYS   A HG2  1 
ATOM   506  H HG3  A LYS   A 1 19  ? 9.086  -5.653  12.419  0.42 19.68 ?  19  LYS   A HG3  1 
ATOM   507  H HG3  B LYS   A 1 19  ? 8.823  -5.684  12.227  0.58 19.80 ?  19  LYS   A HG3  1 
ATOM   508  H HD2  A LYS   A 1 19  ? 10.982 -5.912  13.793  0.42 20.24 ?  19  LYS   A HD2  1 
ATOM   509  H HD2  B LYS   A 1 19  ? 10.649 -5.645  13.681  0.58 20.99 ?  19  LYS   A HD2  1 
ATOM   510  H HD3  A LYS   A 1 19  ? 11.663 -4.678  13.058  0.42 20.24 ?  19  LYS   A HD3  1 
ATOM   511  H HD3  B LYS   A 1 19  ? 11.225 -4.369  12.930  0.58 20.99 ?  19  LYS   A HD3  1 
ATOM   512  H HE2  A LYS   A 1 19  ? 10.060 -3.251  13.931  0.42 20.70 ?  19  LYS   A HE2  1 
ATOM   513  H HE2  B LYS   A 1 19  ? 9.385  -3.123  13.684  0.58 22.00 ?  19  LYS   A HE2  1 
ATOM   514  H HE3  A LYS   A 1 19  ? 9.330  -4.482  14.631  0.42 20.70 ?  19  LYS   A HE3  1 
ATOM   515  H HE3  B LYS   A 1 19  ? 8.874  -4.401  14.487  0.58 22.00 ?  19  LYS   A HE3  1 
ATOM   516  H HZ1  A LYS   A 1 19  ? 10.668 -3.388  16.116  0.42 20.72 ?  19  LYS   A HZ1  1 
ATOM   517  H HZ1  B LYS   A 1 19  ? 10.059 -3.018  15.863  0.58 22.09 ?  19  LYS   A HZ1  1 
ATOM   518  H HZ2  A LYS   A 1 19  ? 11.167 -4.737  15.945  0.42 20.72 ?  19  LYS   A HZ2  1 
ATOM   519  H HZ2  B LYS   A 1 19  ? 10.771 -4.275  15.751  0.58 22.09 ?  19  LYS   A HZ2  1 
ATOM   520  H HZ3  A LYS   A 1 19  ? 11.842 -3.629  15.303  0.42 20.72 ?  19  LYS   A HZ3  1 
ATOM   521  H HZ3  B LYS   A 1 19  ? 11.235 -3.113  15.021  0.58 22.09 ?  19  LYS   A HZ3  1 
ATOM   522  N N    A ASN   A 1 20  ? 8.593  -4.673  9.221   0.42 14.58 ?  20  ASN   A N    1 
ATOM   523  N N    B ASN   A 1 20  ? 8.439  -4.830  8.870   0.58 15.16 ?  20  ASN   A N    1 
ATOM   524  C CA   A ASN   A 1 20  ? 8.385  -3.336  8.667   0.42 14.45 ?  20  ASN   A CA   1 
ATOM   525  C CA   B ASN   A 1 20  ? 8.188  -3.565  8.177   0.58 15.43 ?  20  ASN   A CA   1 
ATOM   526  C C    A ASN   A 1 20  ? 8.992  -2.332  9.634   0.42 14.57 ?  20  ASN   A C    1 
ATOM   527  C C    B ASN   A 1 20  ? 8.739  -2.457  9.062   0.58 15.55 ?  20  ASN   A C    1 
ATOM   528  O O    A ASN   A 1 20  ? 8.463  -2.116  10.728  0.42 14.41 ?  20  ASN   A O    1 
ATOM   529  O O    B ASN   A 1 20  ? 8.101  -2.046  10.035  0.58 17.21 ?  20  ASN   A O    1 
ATOM   530  C CB   A ASN   A 1 20  ? 6.895  -3.072  8.458   0.42 14.71 ?  20  ASN   A CB   1 
ATOM   531  C CB   B ASN   A 1 20  ? 6.693  -3.383  7.924   0.58 16.26 ?  20  ASN   A CB   1 
ATOM   532  C CG   A ASN   A 1 20  ? 6.587  -1.619  8.096   0.42 15.68 ?  20  ASN   A CG   1 
ATOM   533  C CG   B ASN   A 1 20  ? 6.342  -2.009  7.342   0.58 17.16 ?  20  ASN   A CG   1 
ATOM   534  O OD1  A ASN   A 1 20  ? 5.638  -1.037  8.621   0.42 18.38 ?  20  ASN   A OD1  1 
ATOM   535  O OD1  B ASN   A 1 20  ? 5.273  -1.447  7.638   0.58 18.04 ?  20  ASN   A OD1  1 
ATOM   536  N ND2  A ASN   A 1 20  ? 7.379  -1.034  7.199   0.42 15.34 ?  20  ASN   A ND2  1 
ATOM   537  N ND2  B ASN   A 1 20  ? 7.222  -1.479  6.496   0.58 17.43 ?  20  ASN   A ND2  1 
ATOM   538  H H    A ASN   A 1 20  ? 7.906  -4.989  9.629   0.42 17.51 ?  20  ASN   A H    1 
ATOM   539  H H    B ASN   A 1 20  ? 7.752  -5.165  9.273   0.58 18.21 ?  20  ASN   A H    1 
ATOM   540  H HA   A ASN   A 1 20  ? 8.836  -3.256  7.819   0.42 17.35 ?  20  ASN   A HA   1 
ATOM   541  H HA   B ASN   A 1 20  ? 8.654  -3.569  7.324   0.58 18.53 ?  20  ASN   A HA   1 
ATOM   542  H HB2  A ASN   A 1 20  ? 6.573  -3.634  7.738   0.42 17.66 ?  20  ASN   A HB2  1 
ATOM   543  H HB2  B ASN   A 1 20  ? 6.394  -4.047  7.289   0.58 19.53 ?  20  ASN   A HB2  1 
ATOM   544  H HB3  A ASN   A 1 20  ? 6.415  -3.276  9.278   0.42 17.66 ?  20  ASN   A HB3  1 
ATOM   545  H HB3  B ASN   A 1 20  ? 6.214  -3.498  8.761   0.58 19.53 ?  20  ASN   A HB3  1 
ATOM   546  H HD21 A ASN   A 1 20  ? 7.238  -0.218  6.963   0.42 18.42 ?  20  ASN   A HD21 1 
ATOM   547  H HD21 B ASN   A 1 20  ? 7.071  -0.711  6.150   0.58 20.93 ?  20  ASN   A HD21 1 
ATOM   548  H HD22 A ASN   A 1 20  ? 8.036  -1.470  6.857   0.42 18.42 ?  20  ASN   A HD22 1 
ATOM   549  H HD22 B ASN   A 1 20  ? 7.947  -1.905  6.298   0.58 20.93 ?  20  ASN   A HD22 1 
ATOM   550  N N    A ALA   A 1 21  ? 10.111 -1.729  9.248   0.42 14.14 ?  21  ALA   A N    1 
ATOM   551  N N    B ALA   A 1 21  ? 9.937  -1.975  8.739   0.58 15.50 ?  21  ALA   A N    1 
ATOM   552  C CA   A ALA   A 1 21  ? 10.794 -0.819  10.151  0.42 14.32 ?  21  ALA   A CA   1 
ATOM   553  C CA   B ALA   A 1 21  ? 10.585 -0.985  9.588   0.58 15.89 ?  21  ALA   A CA   1 
ATOM   554  C C    A ALA   A 1 21  ? 11.760 0.051   9.366   0.42 14.15 ?  21  ALA   A C    1 
ATOM   555  C C    B ALA   A 1 21  ? 11.659 -0.246  8.806   0.58 14.73 ?  21  ALA   A C    1 
ATOM   556  O O    A ALA   A 1 21  ? 12.233 -0.330  8.292   0.42 14.93 ?  21  ALA   A O    1 
ATOM   557  O O    B ALA   A 1 21  ? 12.161 -0.733  7.790   0.58 14.51 ?  21  ALA   A O    1 
ATOM   558  C CB   A ALA   A 1 21  ? 11.556 -1.588  11.235  0.42 15.30 ?  21  ALA   A CB   1 
ATOM   559  C CB   B ALA   A 1 21  ? 11.195 -1.636  10.832  0.58 17.47 ?  21  ALA   A CB   1 
ATOM   560  H H    A ALA   A 1 21  ? 10.489 -1.824  8.481   0.42 16.99 ?  21  ALA   A H    1 
ATOM   561  H H    B ALA   A 1 21  ? 10.384 -2.213  8.044   0.58 18.61 ?  21  ALA   A H    1 
ATOM   562  H HA   A ALA   A 1 21  ? 10.147 -0.237  10.583  0.42 17.21 ?  21  ALA   A HA   1 
ATOM   563  H HA   B ALA   A 1 21  ? 9.913  -0.351  9.880   0.58 19.08 ?  21  ALA   A HA   1 
ATOM   564  H HB1  A ALA   A 1 21  ? 11.940 -0.952  11.855  0.42 18.37 ?  21  ALA   A HB1  1 
ATOM   565  H HB1  B ALA   A 1 21  ? 11.612 -0.947  11.371  0.58 20.98 ?  21  ALA   A HB1  1 
ATOM   566  H HB2  A ALA   A 1 21  ? 10.931 -2.168  11.700  0.42 18.37 ?  21  ALA   A HB2  1 
ATOM   567  H HB2  B ALA   A 1 21  ? 10.493 -2.075  11.343  0.58 20.98 ?  21  ALA   A HB2  1 
ATOM   568  H HB3  A ALA   A 1 21  ? 12.251 -2.116  10.817  0.42 18.37 ?  21  ALA   A HB3  1 
ATOM   569  H HB3  B ALA   A 1 21  ? 11.857 -2.289  10.557  0.58 20.98 ?  21  ALA   A HB3  1 
ATOM   570  N N    A ASP   A 1 22  ? 12.025 1.230   9.922   0.42 14.82 ?  22  ASP   A N    1 
ATOM   571  N N    B ASP   A 1 22  ? 12.000 0.941   9.309   0.58 14.24 ?  22  ASP   A N    1 
ATOM   572  C CA   A ASP   A 1 22  ? 13.092 2.101   9.455   0.42 15.35 ?  22  ASP   A CA   1 
ATOM   573  C CA   B ASP   A 1 22  ? 13.130 1.717   8.809   0.58 13.93 ?  22  ASP   A CA   1 
ATOM   574  C C    A ASP   A 1 22  ? 14.410 1.586   10.017  0.42 14.25 ?  22  ASP   A C    1 
ATOM   575  C C    B ASP   A 1 22  ? 14.405 1.202   9.473   0.58 13.04 ?  22  ASP   A C    1 
ATOM   576  O O    A ASP   A 1 22  ? 14.607 1.585   11.236  0.42 14.41 ?  22  ASP   A O    1 
ATOM   577  O O    B ASP   A 1 22  ? 14.513 1.212   10.703  0.58 13.78 ?  22  ASP   A O    1 
ATOM   578  C CB   A ASP   A 1 22  ? 12.827 3.515   9.963   0.42 16.89 ?  22  ASP   A CB   1 
ATOM   579  C CB   B ASP   A 1 22  ? 12.913 3.190   9.154   0.58 15.75 ?  22  ASP   A CB   1 
ATOM   580  C CG   A ASP   A 1 22  ? 13.809 4.532   9.414   0.42 17.94 ?  22  ASP   A CG   1 
ATOM   581  C CG   B ASP   A 1 22  ? 13.990 4.105   8.587   0.58 16.88 ?  22  ASP   A CG   1 
ATOM   582  O OD1  A ASP   A 1 22  ? 14.822 4.128   8.811   0.42 18.01 ?  22  ASP   A OD1  1 
ATOM   583  O OD1  B ASP   A 1 22  ? 15.113 3.643   8.271   0.58 15.67 ?  22  ASP   A OD1  1 
ATOM   584  O OD2  A ASP   A 1 22  ? 13.552 5.744   9.578   0.42 18.74 -1 22  ASP   A OD2  1 
ATOM   585  O OD2  B ASP   A 1 22  ? 13.702 5.311   8.459   0.58 19.61 -1 22  ASP   A OD2  1 
ATOM   586  H H    A ASP   A 1 22  ? 11.581 1.556   10.581  0.42 17.80 ?  22  ASP   A H    1 
ATOM   587  H H    B ASP   A 1 22  ? 11.575 1.318   9.959   0.58 17.10 ?  22  ASP   A H    1 
ATOM   588  H HA   A ASP   A 1 22  ? 13.134 2.106   8.487   0.42 18.44 ?  22  ASP   A HA   1 
ATOM   589  H HA   B ASP   A 1 22  ? 13.196 1.615   7.846   0.58 16.73 ?  22  ASP   A HA   1 
ATOM   590  H HB2  A ASP   A 1 22  ? 11.938 3.787   9.691   0.42 20.29 ?  22  ASP   A HB2  1 
ATOM   591  H HB2  B ASP   A 1 22  ? 12.060 3.476   8.793   0.58 18.92 ?  22  ASP   A HB2  1 
ATOM   592  H HB3  A ASP   A 1 22  ? 12.886 3.514   10.936  0.42 20.29 ?  22  ASP   A HB3  1 
ATOM   593  H HB3  B ASP   A 1 22  ? 12.914 3.287   10.119  0.58 18.92 ?  22  ASP   A HB3  1 
ATOM   594  N N    A ILE   A 1 23  ? 15.307 1.145   9.132   0.42 13.87 ?  23  ILE   A N    1 
ATOM   595  N N    B ILE   A 1 23  ? 15.361 0.732   8.662   0.58 12.77 ?  23  ILE   A N    1 
ATOM   596  C CA   A ILE   A 1 23  ? 16.561 0.535   9.570   0.42 13.41 ?  23  ILE   A CA   1 
ATOM   597  C CA   B ILE   A 1 23  ? 16.601 0.166   9.198   0.58 12.60 ?  23  ILE   A CA   1 
ATOM   598  C C    A ILE   A 1 23  ? 17.358 1.484   10.458  0.42 13.46 ?  23  ILE   A C    1 
ATOM   599  C C    B ILE   A 1 23  ? 17.315 1.152   10.112  0.58 12.92 ?  23  ILE   A C    1 
ATOM   600  O O    A ILE   A 1 23  ? 18.071 1.042   11.369  0.42 13.91 ?  23  ILE   A O    1 
ATOM   601  O O    B ILE   A 1 23  ? 17.991 0.744   11.067  0.58 13.29 ?  23  ILE   A O    1 
ATOM   602  C CB   A ILE   A 1 23  ? 17.365 0.034   8.350   0.42 12.90 ?  23  ILE   A CB   1 
ATOM   603  C CB   B ILE   A 1 23  ? 17.520 -0.367  8.073   0.58 12.97 ?  23  ILE   A CB   1 
ATOM   604  C CG1  A ILE   A 1 23  ? 18.549 -0.827  8.804   0.42 13.08 ?  23  ILE   A CG1  1 
ATOM   605  C CG1  B ILE   A 1 23  ? 18.568 -1.319  8.658   0.58 13.44 ?  23  ILE   A CG1  1 
ATOM   606  C CG2  A ILE   A 1 23  ? 17.800 1.202   7.460   0.42 13.68 ?  23  ILE   A CG2  1 
ATOM   607  C CG2  B ILE   A 1 23  ? 18.198 0.776   7.316   0.58 13.11 ?  23  ILE   A CG2  1 
ATOM   608  C CD1  A ILE   A 1 23  ? 19.215 -1.588  7.678   0.42 13.78 ?  23  ILE   A CD1  1 
ATOM   609  C CD1  B ILE   A 1 23  ? 19.452 -1.983  7.614   0.58 13.74 ?  23  ILE   A CD1  1 
ATOM   610  H H    A ILE   A 1 23  ? 15.212 1.185   8.283   0.42 16.66 ?  23  ILE   A H    1 
ATOM   611  H H    B ILE   A 1 23  ? 15.310 0.711   7.812   0.58 15.34 ?  23  ILE   A H    1 
ATOM   612  H HA   A ILE   A 1 23  ? 16.354 -0.243  10.108  0.42 16.11 ?  23  ILE   A HA   1 
ATOM   613  H HA   B ILE   A 1 23  ? 16.359 -0.602  9.738   0.58 15.14 ?  23  ILE   A HA   1 
ATOM   614  H HB   A ILE   A 1 23  ? 16.780 -0.530  7.825   0.42 15.49 ?  23  ILE   A HB   1 
ATOM   615  H HB   B ILE   A 1 23  ? 16.980 -0.869  7.442   0.58 15.58 ?  23  ILE   A HB   1 
ATOM   616  H HG12 A ILE   A 1 23  ? 19.218 -0.255  9.210   0.42 15.71 ?  23  ILE   A HG12 1 
ATOM   617  H HG12 B ILE   A 1 23  ? 19.144 -0.826  9.261   0.58 16.14 ?  23  ILE   A HG12 1 
ATOM   618  H HG13 A ILE   A 1 23  ? 18.232 -1.476  9.452   0.42 15.71 ?  23  ILE   A HG13 1 
ATOM   619  H HG13 B ILE   A 1 23  ? 18.112 -2.027  9.147   0.58 16.14 ?  23  ILE   A HG13 1 
ATOM   620  H HG21 A ILE   A 1 23  ? 18.205 0.851   6.651   0.42 16.43 ?  23  ILE   A HG21 1 
ATOM   621  H HG21 B ILE   A 1 23  ? 18.590 0.424   6.498   0.58 15.75 ?  23  ILE   A HG21 1 
ATOM   622  H HG22 A ILE   A 1 23  ? 17.015 1.729   7.230   0.42 16.43 ?  23  ILE   A HG22 1 
ATOM   623  H HG22 B ILE   A 1 23  ? 17.536 1.447   7.103   0.58 15.75 ?  23  ILE   A HG22 1 
ATOM   624  H HG23 A ILE   A 1 23  ? 18.436 1.751   7.940   0.42 16.43 ?  23  ILE   A HG23 1 
ATOM   625  H HG23 B ILE   A 1 23  ? 18.894 1.157   7.875   0.58 15.75 ?  23  ILE   A HG23 1 
ATOM   626  H HD11 A ILE   A 1 23  ? 19.916 -2.147  8.047   0.42 16.55 ?  23  ILE   A HD11 1 
ATOM   627  H HD11 B ILE   A 1 23  ? 20.010 -2.645  8.050   0.58 16.50 ?  23  ILE   A HD11 1 
ATOM   628  H HD12 A ILE   A 1 23  ? 18.550 -2.139  7.235   0.42 16.55 ?  23  ILE   A HD12 1 
ATOM   629  H HD12 B ILE   A 1 23  ? 18.887 -2.408  6.952   0.58 16.50 ?  23  ILE   A HD12 1 
ATOM   630  H HD13 A ILE   A 1 23  ? 19.592 -0.954  7.049   0.42 16.55 ?  23  ILE   A HD13 1 
ATOM   631  H HD13 B ILE   A 1 23  ? 20.003 -1.305  7.196   0.58 16.50 ?  23  ILE   A HD13 1 
ATOM   632  N N    A VAL   A 1 24  ? 17.252 2.792   10.217  0.42 13.86 ?  24  VAL   A N    1 
ATOM   633  N N    B VAL   A 1 24  ? 17.190 2.454   9.842   0.58 13.31 ?  24  VAL   A N    1 
ATOM   634  C CA   A VAL   A 1 24  ? 17.916 3.768   11.079  0.42 14.81 ?  24  VAL   A CA   1 
ATOM   635  C CA   B VAL   A 1 24  ? 17.844 3.451   10.684  0.58 14.65 ?  24  VAL   A CA   1 
ATOM   636  C C    A VAL   A 1 24  ? 17.391 3.663   12.504  0.42 15.68 ?  24  VAL   A C    1 
ATOM   637  C C    B VAL   A 1 24  ? 17.237 3.455   12.082  0.58 15.71 ?  24  VAL   A C    1 
ATOM   638  O O    A VAL   A 1 24  ? 18.162 3.586   13.469  0.42 16.05 ?  24  VAL   A O    1 
ATOM   639  O O    B VAL   A 1 24  ? 17.954 3.494   13.088  0.58 16.78 ?  24  VAL   A O    1 
ATOM   640  C CB   A VAL   A 1 24  ? 17.730 5.190   10.518  0.42 14.43 ?  24  VAL   A CB   1 
ATOM   641  C CB   B VAL   A 1 24  ? 17.778 4.840   10.026  0.58 15.80 ?  24  VAL   A CB   1 
ATOM   642  C CG1  A VAL   A 1 24  ? 18.174 6.233   11.539  0.42 14.11 ?  24  VAL   A CG1  1 
ATOM   643  C CG1  B VAL   A 1 24  ? 18.475 5.865   10.901  0.58 17.33 ?  24  VAL   A CG1  1 
ATOM   644  C CG2  A VAL   A 1 24  ? 18.481 5.352   9.206   0.42 14.69 ?  24  VAL   A CG2  1 
ATOM   645  C CG2  B VAL   A 1 24  ? 18.393 4.788   8.638   0.58 16.31 ?  24  VAL   A CG2  1 
ATOM   646  H H    A VAL   A 1 24  ? 16.802 3.137   9.572   0.42 16.64 ?  24  VAL   A H    1 
ATOM   647  H H    B VAL   A 1 24  ? 16.729 2.780   9.189   0.58 15.98 ?  24  VAL   A H    1 
ATOM   648  H HA   A VAL   A 1 24  ? 18.867 3.583   11.098  0.42 17.79 ?  24  VAL   A HA   1 
ATOM   649  H HA   B VAL   A 1 24  ? 18.776 3.215   10.772  0.58 17.60 ?  24  VAL   A HA   1 
ATOM   650  H HB   A VAL   A 1 24  ? 16.788 5.338   10.336  0.42 17.33 ?  24  VAL   A HB   1 
ATOM   651  H HB   B VAL   A 1 24  ? 16.847 5.106   9.933   0.58 18.98 ?  24  VAL   A HB   1 
ATOM   652  H HG11 A VAL   A 1 24  ? 18.323 7.076   11.082  0.42 16.95 ?  24  VAL   A HG11 1 
ATOM   653  H HG11 B VAL   A 1 24  ? 18.610 6.676   10.389  0.58 20.81 ?  24  VAL   A HG11 1 
ATOM   654  H HG12 A VAL   A 1 24  ? 17.480 6.339   12.208  0.42 16.95 ?  24  VAL   A HG12 1 
ATOM   655  H HG12 B VAL   A 1 24  ? 17.919 6.051   11.675  0.58 20.81 ?  24  VAL   A HG12 1 
ATOM   656  H HG13 A VAL   A 1 24  ? 18.998 5.934   11.955  0.42 16.95 ?  24  VAL   A HG13 1 
ATOM   657  H HG13 B VAL   A 1 24  ? 19.330 5.505   11.185  0.58 20.81 ?  24  VAL   A HG13 1 
ATOM   658  H HG21 A VAL   A 1 24  ? 18.257 6.211   8.814   0.42 17.65 ?  24  VAL   A HG21 1 
ATOM   659  H HG21 B VAL   A 1 24  ? 18.453 5.686   8.285   0.58 19.59 ?  24  VAL   A HG21 1 
ATOM   660  H HG22 A VAL   A 1 24  ? 19.436 5.310   9.381   0.42 17.65 ?  24  VAL   A HG22 1 
ATOM   661  H HG22 B VAL   A 1 24  ? 19.277 4.394   8.704   0.58 19.59 ?  24  VAL   A HG22 1 
ATOM   662  H HG23 A VAL   A 1 24  ? 18.224 4.637   8.602   0.42 17.65 ?  24  VAL   A HG23 1 
ATOM   663  H HG23 B VAL   A 1 24  ? 17.831 4.241   8.064   0.58 19.59 ?  24  VAL   A HG23 1 
ATOM   664  N N    A GLU   A 1 25  ? 16.065 3.684   12.657  0.42 15.99 ?  25  GLU   A N    1 
ATOM   665  N N    B GLU   A 1 25  ? 15.904 3.423   12.167  0.58 16.22 ?  25  GLU   A N    1 
ATOM   666  C CA   A GLU   A 1 25  ? 15.473 3.616   13.988  0.42 17.40 ?  25  GLU   A CA   1 
ATOM   667  C CA   B GLU   A 1 25  ? 15.252 3.378   13.474  0.58 16.53 ?  25  GLU   A CA   1 
ATOM   668  C C    A GLU   A 1 25  ? 15.685 2.247   14.623  0.42 16.08 ?  25  GLU   A C    1 
ATOM   669  C C    B GLU   A 1 25  ? 15.521 2.056   14.181  0.58 15.99 ?  25  GLU   A C    1 
ATOM   670  O O    A GLU   A 1 25  ? 15.888 2.148   15.840  0.42 16.45 ?  25  GLU   A O    1 
ATOM   671  O O    B GLU   A 1 25  ? 15.726 2.029   15.401  0.58 16.93 ?  25  GLU   A O    1 
ATOM   672  C CB   A GLU   A 1 25  ? 13.988 3.983   13.924  0.42 19.69 ?  25  GLU   A CB   1 
ATOM   673  C CB   B GLU   A 1 25  ? 13.750 3.627   13.326  0.58 18.35 ?  25  GLU   A CB   1 
ATOM   674  C CG   A GLU   A 1 25  ? 13.735 5.445   13.570  0.42 22.00 ?  25  GLU   A CG   1 
ATOM   675  C CG   B GLU   A 1 25  ? 13.414 5.032   12.846  0.58 22.32 ?  25  GLU   A CG   1 
ATOM   676  C CD   A GLU   A 1 25  ? 14.526 6.410   14.441  0.42 23.95 ?  25  GLU   A CD   1 
ATOM   677  C CD   B GLU   A 1 25  ? 14.040 6.104   13.708  0.58 25.93 ?  25  GLU   A CD   1 
ATOM   678  O OE1  A GLU   A 1 25  ? 14.558 6.217   15.676  0.42 24.63 ?  25  GLU   A OE1  1 
ATOM   679  O OE1  B GLU   A 1 25  ? 14.070 5.928   14.945  0.58 27.54 ?  25  GLU   A OE1  1 
ATOM   680  O OE2  A GLU   A 1 25  ? 15.131 7.349   13.886  0.42 24.71 -1 25  GLU   A OE2  1 
ATOM   681  O OE2  B GLU   A 1 25  ? 14.508 7.115   13.149  0.58 27.21 -1 25  GLU   A OE2  1 
ATOM   682  H H    A GLU   A 1 25  ? 15.497 3.751   12.014  0.42 19.21 ?  25  GLU   A H    1 
ATOM   683  H H    B GLU   A 1 25  ? 15.365 3.434   11.495  0.58 19.48 ?  25  GLU   A H    1 
ATOM   684  H HA   A GLU   A 1 25  ? 15.918 4.261   14.557  0.42 20.90 ?  25  GLU   A HA   1 
ATOM   685  H HA   B GLU   A 1 25  ? 15.618 4.078   14.029  0.58 19.85 ?  25  GLU   A HA   1 
ATOM   686  H HB2  A GLU   A 1 25  ? 13.555 3.437   13.246  0.42 23.64 ?  25  GLU   A HB2  1 
ATOM   687  H HB2  B GLU   A 1 25  ? 13.385 3.001   12.681  0.58 22.04 ?  25  GLU   A HB2  1 
ATOM   688  H HB3  A GLU   A 1 25  ? 13.582 3.814   14.788  0.42 23.64 ?  25  GLU   A HB3  1 
ATOM   689  H HB3  B GLU   A 1 25  ? 13.321 3.498   14.188  0.58 22.04 ?  25  GLU   A HB3  1 
ATOM   690  H HG2  A GLU   A 1 25  ? 13.997 5.595   12.649  0.42 26.42 ?  25  GLU   A HG2  1 
ATOM   691  H HG2  B GLU   A 1 25  ? 13.734 5.141   11.937  0.58 26.80 ?  25  GLU   A HG2  1 
ATOM   692  H HG3  A GLU   A 1 25  ? 12.791 5.638   13.686  0.42 26.42 ?  25  GLU   A HG3  1 
ATOM   693  H HG3  B GLU   A 1 25  ? 12.458 5.165   12.885  0.58 26.80 ?  25  GLU   A HG3  1 
ATOM   694  N N    A GLU   A 1 26  ? 15.655 1.179   13.821  0.42 15.39 ?  26  GLU   A N    1 
ATOM   695  N N    B GLU   A 1 26  ? 15.521 0.951   13.434  0.58 15.97 ?  26  GLU   A N    1 
ATOM   696  C CA   A GLU   A 1 26  ? 15.964 -0.147  14.350  0.42 15.69 ?  26  GLU   A CA   1 
ATOM   697  C CA   B GLU   A 1 26  ? 15.857 -0.336  14.032  0.58 16.26 ?  26  GLU   A CA   1 
ATOM   698  C C    A GLU   A 1 26  ? 17.380 -0.189  14.908  0.42 15.33 ?  26  GLU   A C    1 
ATOM   699  C C    B GLU   A 1 26  ? 17.268 -0.318  14.606  0.58 15.32 ?  26  GLU   A C    1 
ATOM   700  O O    A GLU   A 1 26  ? 17.604 -0.646  16.035  0.42 15.40 ?  26  GLU   A O    1 
ATOM   701  O O    B GLU   A 1 26  ? 17.510 -0.846  15.697  0.58 15.97 ?  26  GLU   A O    1 
ATOM   702  C CB   A GLU   A 1 26  ? 15.803 -1.212  13.261  0.42 16.54 ?  26  GLU   A CB   1 
ATOM   703  C CB   B GLU   A 1 26  ? 15.718 -1.453  12.995  0.58 17.84 ?  26  GLU   A CB   1 
ATOM   704  C CG   A GLU   A 1 26  ? 14.403 -1.761  13.081  0.42 19.30 ?  26  GLU   A CG   1 
ATOM   705  C CG   B GLU   A 1 26  ? 14.290 -1.833  12.691  0.58 19.47 ?  26  GLU   A CG   1 
ATOM   706  C CD   A GLU   A 1 26  ? 13.936 -2.615  14.252  0.42 20.63 ?  26  GLU   A CD   1 
ATOM   707  C CD   B GLU   A 1 26  ? 13.599 -2.420  13.901  0.58 20.14 ?  26  GLU   A CD   1 
ATOM   708  O OE1  A GLU   A 1 26  ? 14.294 -3.816  14.331  0.42 21.14 ?  26  GLU   A OE1  1 
ATOM   709  O OE1  B GLU   A 1 26  ? 14.145 -3.377  14.491  0.58 20.84 ?  26  GLU   A OE1  1 
ATOM   710  O OE2  A GLU   A 1 26  ? 13.201 -2.075  15.096  0.42 21.31 -1 26  GLU   A OE2  1 
ATOM   711  O OE2  B GLU   A 1 26  ? 12.529 -1.907  14.276  0.58 19.01 -1 26  GLU   A OE2  1 
ATOM   712  H H    A GLU   A 1 26  ? 15.472 1.201   12.983  0.42 18.49 ?  26  GLU   A H    1 
ATOM   713  H H    B GLU   A 1 26  ? 15.328 0.920   12.598  0.58 19.18 ?  26  GLU   A H    1 
ATOM   714  H HA   A GLU   A 1 26  ? 15.354 -0.351  15.070  0.42 18.85 ?  26  GLU   A HA   1 
ATOM   715  H HA   B GLU   A 1 26  ? 15.245 -0.522  14.759  0.58 19.53 ?  26  GLU   A HA   1 
ATOM   716  H HB2  A GLU   A 1 26  ? 16.076 -0.824  12.412  0.42 19.86 ?  26  GLU   A HB2  1 
ATOM   717  H HB2  B GLU   A 1 26  ? 16.131 -1.162  12.165  0.58 21.43 ?  26  GLU   A HB2  1 
ATOM   718  H HB3  A GLU   A 1 26  ? 16.384 -1.957  13.475  0.42 19.86 ?  26  GLU   A HB3  1 
ATOM   719  H HB3  B GLU   A 1 26  ? 16.174 -2.246  13.324  0.58 21.43 ?  26  GLU   A HB3  1 
ATOM   720  H HG2  A GLU   A 1 26  ? 13.795 -1.012  12.983  0.42 23.18 ?  26  GLU   A HG2  1 
ATOM   721  H HG2  B GLU   A 1 26  ? 13.800 -1.042  12.416  0.58 23.38 ?  26  GLU   A HG2  1 
ATOM   722  H HG3  A GLU   A 1 26  ? 14.384 -2.312  12.285  0.42 23.18 ?  26  GLU   A HG3  1 
ATOM   723  H HG3  B GLU   A 1 26  ? 14.277 -2.497  11.984  0.58 23.38 ?  26  GLU   A HG3  1 
ATOM   724  N N    A ALA   A 1 27  ? 18.354 0.285   14.126  0.42 14.56 ?  27  ALA   A N    1 
ATOM   725  N N    B ALA   A 1 27  ? 18.215 0.287   13.885  0.58 13.74 ?  27  ALA   A N    1 
ATOM   726  C CA   A ALA   A 1 27  ? 19.745 0.227   14.566  0.42 15.38 ?  27  ALA   A CA   1 
ATOM   727  C CA   B ALA   A 1 27  ? 19.591 0.342   14.371  0.58 14.03 ?  27  ALA   A CA   1 
ATOM   728  C C    A ALA   A 1 27  ? 19.948 1.015   15.853  0.42 16.73 ?  27  ALA   A C    1 
ATOM   729  C C    B ALA   A 1 27  ? 19.701 1.206   15.621  0.58 14.65 ?  27  ALA   A C    1 
ATOM   730  O O    A ALA   A 1 27  ? 20.611 0.539   16.782  0.42 16.99 ?  27  ALA   A O    1 
ATOM   731  O O    B ALA   A 1 27  ? 20.357 0.818   16.594  0.58 14.71 ?  27  ALA   A O    1 
ATOM   732  C CB   A ALA   A 1 27  ? 20.674 0.735   13.459  0.42 14.96 ?  27  ALA   A CB   1 
ATOM   733  C CB   B ALA   A 1 27  ? 20.521 0.858   13.273  0.58 14.36 ?  27  ALA   A CB   1 
ATOM   734  H H    A ALA   A 1 27  ? 18.238 0.646   13.351  0.42 17.49 ?  27  ALA   A H    1 
ATOM   735  H H    B ALA   A 1 27  ? 18.084 0.669   13.124  0.58 16.50 ?  27  ALA   A H    1 
ATOM   736  H HA   A ALA   A 1 27  ? 19.979 -0.695  14.742  0.42 18.47 ?  27  ALA   A HA   1 
ATOM   737  H HA   B ALA   A 1 27  ? 19.873 -0.553  14.603  0.58 16.85 ?  27  ALA   A HA   1 
ATOM   738  H HB1  A ALA   A 1 27  ? 21.593 0.688   13.768  0.42 17.97 ?  27  ALA   A HB1  1 
ATOM   739  H HB1  B ALA   A 1 27  ? 21.427 0.887   13.617  0.58 17.25 ?  27  ALA   A HB1  1 
ATOM   740  H HB2  A ALA   A 1 27  ? 20.564 0.176   12.671  0.42 17.97 ?  27  ALA   A HB2  1 
ATOM   741  H HB2  B ALA   A 1 27  ? 20.475 0.257   12.512  0.58 17.25 ?  27  ALA   A HB2  1 
ATOM   742  H HB3  A ALA   A 1 27  ? 20.444 1.653   13.245  0.42 17.97 ?  27  ALA   A HB3  1 
ATOM   743  H HB3  B ALA   A 1 27  ? 20.238 1.748   13.009  0.58 17.25 ?  27  ALA   A HB3  1 
ATOM   744  N N    A LYS   A 1 28  ? 19.367 2.215   15.938  0.42 18.54 ?  28  LYS   A N    1 
ATOM   745  N N    B LYS   A 1 28  ? 19.056 2.377   15.623  0.58 16.46 ?  28  LYS   A N    1 
ATOM   746  C CA   A LYS   A 1 28  ? 19.533 3.023   17.142  0.42 20.89 ?  28  LYS   A CA   1 
ATOM   747  C CA   B LYS   A 1 28  ? 19.125 3.249   16.791  0.58 19.13 ?  28  LYS   A CA   1 
ATOM   748  C C    A LYS   A 1 28  ? 18.963 2.324   18.369  0.42 22.26 ?  28  LYS   A C    1 
ATOM   749  C C    B LYS   A 1 28  ? 18.580 2.562   18.037  0.58 19.74 ?  28  LYS   A C    1 
ATOM   750  O O    A LYS   A 1 28  ? 19.502 2.471   19.472  0.42 23.11 ?  28  LYS   A O    1 
ATOM   751  O O    B LYS   A 1 28  ? 19.107 2.752   19.139  0.58 20.87 ?  28  LYS   A O    1 
ATOM   752  C CB   A LYS   A 1 28  ? 18.902 4.405   16.949  0.42 22.24 ?  28  LYS   A CB   1 
ATOM   753  C CB   B LYS   A 1 28  ? 18.371 4.554   16.529  0.58 21.75 ?  28  LYS   A CB   1 
ATOM   754  C CG   A LYS   A 1 28  ? 19.728 5.332   16.068  0.42 23.77 ?  28  LYS   A CG   1 
ATOM   755  C CG   B LYS   A 1 28  ? 19.118 5.530   15.644  0.58 24.08 ?  28  LYS   A CG   1 
ATOM   756  C CD   A LYS   A 1 28  ? 19.244 6.771   16.134  0.42 25.53 ?  28  LYS   A CD   1 
ATOM   757  C CD   B LYS   A 1 28  ? 18.485 6.913   15.676  0.58 27.24 ?  28  LYS   A CD   1 
ATOM   758  C CE   A LYS   A 1 28  ? 17.939 6.957   15.387  0.42 26.46 ?  28  LYS   A CE   1 
ATOM   759  C CE   B LYS   A 1 28  ? 17.509 7.114   14.531  0.58 29.59 ?  28  LYS   A CE   1 
ATOM   760  N NZ   A LYS   A 1 28  ? 17.577 8.399   15.293  0.42 27.23 ?  28  LYS   A NZ   1 
ATOM   761  N NZ   B LYS   A 1 28  ? 16.875 8.464   14.584  0.58 30.71 ?  28  LYS   A NZ   1 
ATOM   762  H H    A LYS   A 1 28  ? 18.882 2.573   15.327  0.42 22.27 ?  28  LYS   A H    1 
ATOM   763  H H    B LYS   A 1 28  ? 18.584 2.685   14.970  0.58 19.77 ?  28  LYS   A H    1 
ATOM   764  H HA   A LYS   A 1 28  ? 20.479 3.154   17.299  0.42 25.09 ?  28  LYS   A HA   1 
ATOM   765  H HA   B LYS   A 1 28  ? 20.047 3.477   16.963  0.58 22.97 ?  28  LYS   A HA   1 
ATOM   766  H HB2  A LYS   A 1 28  ? 18.034 4.302   16.532  0.42 26.71 ?  28  LYS   A HB2  1 
ATOM   767  H HB2  B LYS   A 1 28  ? 17.528 4.353   16.091  0.58 26.11 ?  28  LYS   A HB2  1 
ATOM   768  H HB3  A LYS   A 1 28  ? 18.807 4.832   17.813  0.42 26.71 ?  28  LYS   A HB3  1 
ATOM   769  H HB3  B LYS   A 1 28  ? 18.203 4.997   17.375  0.58 26.11 ?  28  LYS   A HB3  1 
ATOM   770  H HG2  A LYS   A 1 28  ? 20.652 5.312   16.361  0.42 28.54 ?  28  LYS   A HG2  1 
ATOM   771  H HG2  B LYS   A 1 28  ? 20.032 5.608   15.954  0.58 28.91 ?  28  LYS   A HG2  1 
ATOM   772  H HG3  A LYS   A 1 28  ? 19.664 5.036   15.146  0.42 28.54 ?  28  LYS   A HG3  1 
ATOM   773  H HG3  B LYS   A 1 28  ? 19.098 5.211   14.728  0.58 28.91 ?  28  LYS   A HG3  1 
ATOM   774  H HD2  A LYS   A 1 28  ? 19.101 7.019   17.061  0.42 30.66 ?  28  LYS   A HD2  1 
ATOM   775  H HD2  B LYS   A 1 28  ? 17.999 7.027   16.509  0.58 32.71 ?  28  LYS   A HD2  1 
ATOM   776  H HD3  A LYS   A 1 28  ? 19.909 7.352   15.731  0.42 30.66 ?  28  LYS   A HD3  1 
ATOM   777  H HD3  B LYS   A 1 28  ? 19.181 7.584   15.602  0.58 32.71 ?  28  LYS   A HD3  1 
ATOM   778  H HE2  A LYS   A 1 28  ? 18.031 6.606   14.487  0.42 31.77 ?  28  LYS   A HE2  1 
ATOM   779  H HE2  B LYS   A 1 28  ? 17.987 7.035   13.689  0.58 35.53 ?  28  LYS   A HE2  1 
ATOM   780  H HE3  A LYS   A 1 28  ? 17.229 6.494   15.859  0.42 31.77 ?  28  LYS   A HE3  1 
ATOM   781  H HE3  B LYS   A 1 28  ? 16.809 6.445   14.583  0.58 35.53 ?  28  LYS   A HE3  1 
ATOM   782  H HZ1  A LYS   A 1 28  ? 16.809 8.492   14.852  0.42 32.69 ?  28  LYS   A HZ1  1 
ATOM   783  H HZ1  B LYS   A 1 28  ? 16.310 8.562   13.905  0.58 36.87 ?  28  LYS   A HZ1  1 
ATOM   784  H HZ2  A LYS   A 1 28  ? 17.486 8.743   16.109  0.42 32.69 ?  28  LYS   A HZ2  1 
ATOM   785  H HZ2  B LYS   A 1 28  ? 16.430 8.561   15.348  0.58 36.87 ?  28  LYS   A HZ2  1 
ATOM   786  H HZ3  A LYS   A 1 28  ? 18.214 8.845   14.861  0.42 32.69 ?  28  LYS   A HZ3  1 
ATOM   787  H HZ3  B LYS   A 1 28  ? 17.501 9.096   14.532  0.58 36.87 ?  28  LYS   A HZ3  1 
ATOM   788  N N    A LYS   A 1 29  ? 17.894 1.546   18.198  0.42 22.93 ?  29  LYS   A N    1 
ATOM   789  N N    B LYS   A 1 29  ? 17.522 1.765   17.885  0.58 19.81 ?  29  LYS   A N    1 
ATOM   790  C CA   A LYS   A 1 29  ? 17.293 0.842   19.326  0.42 24.24 ?  29  LYS   A CA   1 
ATOM   791  C CA   B LYS   A 1 29  ? 16.892 1.131   19.037  0.58 20.52 ?  29  LYS   A CA   1 
ATOM   792  C C    A LYS   A 1 29  ? 18.116 -0.382  19.716  0.42 23.13 ?  29  LYS   A C    1 
ATOM   793  C C    B LYS   A 1 29  ? 17.671 -0.094  19.497  0.58 19.53 ?  29  LYS   A C    1 
ATOM   794  O O    A LYS   A 1 29  ? 18.464 -0.563  20.888  0.42 23.93 ?  29  LYS   A O    1 
ATOM   795  O O    B LYS   A 1 29  ? 17.873 -0.293  20.700  0.58 20.90 ?  29  LYS   A O    1 
ATOM   796  C CB   A LYS   A 1 29  ? 15.865 0.429   18.965  0.42 26.68 ?  29  LYS   A CB   1 
ATOM   797  C CB   B LYS   A 1 29  ? 15.463 0.725   18.681  0.58 23.31 ?  29  LYS   A CB   1 
ATOM   798  C CG   A LYS   A 1 29  ? 15.125 -0.307  20.072  0.42 29.37 ?  29  LYS   A CG   1 
ATOM   799  C CG   B LYS   A 1 29  ? 14.730 -0.008  19.793  0.58 26.87 ?  29  LYS   A CG   1 
ATOM   800  C CD   A LYS   A 1 29  ? 14.784 0.624   21.222  0.42 31.90 ?  29  LYS   A CD   1 
ATOM   801  C CD   B LYS   A 1 29  ? 14.470 0.911   20.972  0.58 30.26 ?  29  LYS   A CD   1 
ATOM   802  C CE   A LYS   A 1 29  ? 13.902 -0.069  22.250  0.42 33.58 ?  29  LYS   A CE   1 
ATOM   803  C CE   B LYS   A 1 29  ? 13.630 0.227   22.037  0.58 32.54 ?  29  LYS   A CE   1 
ATOM   804  N NZ   A LYS   A 1 29  ? 13.432 0.873   23.303  0.42 34.58 ?  29  LYS   A NZ   1 
ATOM   805  N NZ   B LYS   A 1 29  ? 13.375 1.130   23.189  0.58 34.04 ?  29  LYS   A NZ   1 
ATOM   806  H H    A LYS   A 1 29  ? 17.505 1.408   17.442  0.42 27.53 ?  29  LYS   A H    1 
ATOM   807  H H    B LYS   A 1 29  ? 17.150 1.581   17.128  0.58 23.78 ?  29  LYS   A H    1 
ATOM   808  H HA   A LYS   A 1 29  ? 17.250 1.442   20.087  0.42 29.11 ?  29  LYS   A HA   1 
ATOM   809  H HA   B LYS   A 1 29  ? 16.854 1.766   19.770  0.58 24.64 ?  29  LYS   A HA   1 
ATOM   810  H HB2  A LYS   A 1 29  ? 15.352 1.226   18.751  0.42 32.03 ?  29  LYS   A HB2  1 
ATOM   811  H HB2  B LYS   A 1 29  ? 14.952 1.523   18.474  0.58 27.99 ?  29  LYS   A HB2  1 
ATOM   812  H HB3  A LYS   A 1 29  ? 15.895 -0.155  18.192  0.42 32.03 ?  29  LYS   A HB3  1 
ATOM   813  H HB3  B LYS   A 1 29  ? 15.486 0.141   17.909  0.58 27.99 ?  29  LYS   A HB3  1 
ATOM   814  H HG2  A LYS   A 1 29  ? 14.298 -0.664  19.716  0.42 35.26 ?  29  LYS   A HG2  1 
ATOM   815  H HG2  B LYS   A 1 29  ? 13.876 -0.319  19.458  0.58 32.27 ?  29  LYS   A HG2  1 
ATOM   816  H HG3  A LYS   A 1 29  ? 15.678 -1.027  20.414  0.42 35.26 ?  29  LYS   A HG3  1 
ATOM   817  H HG3  B LYS   A 1 29  ? 15.260 -0.763  20.100  0.58 32.27 ?  29  LYS   A HG3  1 
ATOM   818  H HD2  A LYS   A 1 29  ? 15.601 0.906   21.662  0.42 38.30 ?  29  LYS   A HD2  1 
ATOM   819  H HD2  B LYS   A 1 29  ? 15.316 1.168   21.372  0.58 36.33 ?  29  LYS   A HD2  1 
ATOM   820  H HD3  A LYS   A 1 29  ? 14.305 1.395   20.879  0.42 38.30 ?  29  LYS   A HD3  1 
ATOM   821  H HD3  B LYS   A 1 29  ? 13.992 1.697   20.665  0.58 36.33 ?  29  LYS   A HD3  1 
ATOM   822  H HE2  A LYS   A 1 29  ? 13.123 -0.438  21.803  0.42 40.31 ?  29  LYS   A HE2  1 
ATOM   823  H HE2  B LYS   A 1 29  ? 12.777 -0.030  21.654  0.58 39.07 ?  29  LYS   A HE2  1 
ATOM   824  H HE3  A LYS   A 1 29  ? 14.408 -0.776  22.679  0.42 40.31 ?  29  LYS   A HE3  1 
ATOM   825  H HE3  B LYS   A 1 29  ? 14.102 -0.557  22.362  0.58 39.07 ?  29  LYS   A HE3  1 
ATOM   826  H HZ1  A LYS   A 1 29  ? 12.919 0.442   23.889  0.42 41.52 ?  29  LYS   A HZ1  1 
ATOM   827  H HZ1  B LYS   A 1 29  ? 12.882 0.712   23.801  0.58 40.86 ?  29  LYS   A HZ1  1 
ATOM   828  H HZ2  A LYS   A 1 29  ? 14.130 1.223   23.731  0.42 41.52 ?  29  LYS   A HZ2  1 
ATOM   829  H HZ2  B LYS   A 1 29  ? 14.146 1.378   23.558  0.58 40.86 ?  29  LYS   A HZ2  1 
ATOM   830  H HZ3  A LYS   A 1 29  ? 12.959 1.531   22.934  0.42 41.52 ?  29  LYS   A HZ3  1 
ATOM   831  H HZ3  B LYS   A 1 29  ? 12.940 1.857   22.915  0.58 40.86 ?  29  LYS   A HZ3  1 
ATOM   832  N N    A VAL   A 1 30  ? 18.439 -1.232  18.741  0.42 22.06 ?  30  VAL   A N    1 
ATOM   833  N N    B VAL   A 1 30  ? 18.084 -0.939  18.552  0.58 18.79 ?  30  VAL   A N    1 
ATOM   834  C CA   A VAL   A 1 30  ? 19.081 -2.509  19.035  0.42 20.79 ?  30  VAL   A CA   1 
ATOM   835  C CA   B VAL   A 1 30  ? 18.719 -2.205  18.904  0.58 18.18 ?  30  VAL   A CA   1 
ATOM   836  C C    A VAL   A 1 30  ? 20.586 -2.353  19.238  0.42 19.32 ?  30  VAL   A C    1 
ATOM   837  C C    B VAL   A 1 30  ? 20.215 -2.040  19.160  0.58 17.36 ?  30  VAL   A C    1 
ATOM   838  O O    A VAL   A 1 30  ? 21.187 -3.087  20.031  0.42 19.97 ?  30  VAL   A O    1 
ATOM   839  O O    B VAL   A 1 30  ? 20.781 -2.736  20.011  0.58 17.88 ?  30  VAL   A O    1 
ATOM   840  C CB   A VAL   A 1 30  ? 18.769 -3.513  17.912  0.42 21.28 ?  30  VAL   A CB   1 
ATOM   841  C CB   B VAL   A 1 30  ? 18.436 -3.244  17.803  0.58 18.96 ?  30  VAL   A CB   1 
ATOM   842  C CG1  A VAL   A 1 30  ? 19.512 -4.824  18.138  0.42 21.46 ?  30  VAL   A CG1  1 
ATOM   843  C CG1  B VAL   A 1 30  ? 19.178 -4.544  18.079  0.58 19.62 ?  30  VAL   A CG1  1 
ATOM   844  C CG2  A VAL   A 1 30  ? 17.271 -3.751  17.813  0.42 21.97 ?  30  VAL   A CG2  1 
ATOM   845  C CG2  B VAL   A 1 30  ? 16.935 -3.491  17.682  0.58 19.67 ?  30  VAL   A CG2  1 
ATOM   846  H H    A VAL   A 1 30  ? 18.293 -1.091  17.907  0.42 26.49 ?  30  VAL   A H    1 
ATOM   847  H H    B VAL   A 1 30  ? 17.988 -0.810  17.703  0.58 22.57 ?  30  VAL   A H    1 
ATOM   848  H HA   A VAL   A 1 30  ? 18.701 -2.860  19.856  0.42 24.97 ?  30  VAL   A HA   1 
ATOM   849  H HA   B VAL   A 1 30  ? 18.313 -2.531  19.718  0.58 21.84 ?  30  VAL   A HA   1 
ATOM   850  H HB   A VAL   A 1 30  ? 19.071 -3.144  17.067  0.42 25.55 ?  30  VAL   A HB   1 
ATOM   851  H HB   B VAL   A 1 30  ? 18.749 -2.900  16.952  0.58 22.77 ?  30  VAL   A HB   1 
ATOM   852  H HG11 A VAL   A 1 30  ? 19.140 -5.500  17.549  0.42 25.77 ?  30  VAL   A HG11 1 
ATOM   853  H HG11 B VAL   A 1 30  ? 18.722 -5.273  17.626  0.58 23.56 ?  30  VAL   A HG11 1 
ATOM   854  H HG12 A VAL   A 1 30  ? 20.452 -4.698  17.942  0.42 25.77 ?  30  VAL   A HG12 1 
ATOM   855  H HG12 B VAL   A 1 30  ? 20.086 -4.469  17.754  0.58 23.56 ?  30  VAL   A HG12 1 
ATOM   856  H HG13 A VAL   A 1 30  ? 19.397 -5.096  19.062  0.42 25.77 ?  30  VAL   A HG13 1 
ATOM   857  H HG13 B VAL   A 1 30  ? 19.180 -4.706  19.036  0.58 23.56 ?  30  VAL   A HG13 1 
ATOM   858  H HG21 A VAL   A 1 30  ? 17.103 -4.426  17.137  0.42 26.38 ?  30  VAL   A HG21 1 
ATOM   859  H HG21 B VAL   A 1 30  ? 16.779 -4.179  17.016  0.58 23.62 ?  30  VAL   A HG21 1 
ATOM   860  H HG22 A VAL   A 1 30  ? 16.944 -4.055  18.674  0.42 26.38 ?  30  VAL   A HG22 1 
ATOM   861  H HG22 B VAL   A 1 30  ? 16.593 -3.782  18.543  0.58 23.62 ?  30  VAL   A HG22 1 
ATOM   862  H HG23 A VAL   A 1 30  ? 16.836 -2.920  17.567  0.42 26.38 ?  30  VAL   A HG23 1 
ATOM   863  H HG23 B VAL   A 1 30  ? 16.498 -2.668  17.415  0.58 23.62 ?  30  VAL   A HG23 1 
ATOM   864  N N    A LYS   A 1 31  ? 21.216 -1.418  18.536  0.42 17.94 ?  31  LYS   A N    1 
ATOM   865  N N    B LYS   A 1 31  ? 20.871 -1.126  18.453  0.58 17.28 ?  31  LYS   A N    1 
ATOM   866  C CA   A LYS   A 1 31  ? 22.669 -1.310  18.483  0.42 18.62 ?  31  LYS   A CA   1 
ATOM   867  C CA   B LYS   A 1 31  ? 22.326 -1.018  18.444  0.58 17.91 ?  31  LYS   A CA   1 
ATOM   868  C C    A LYS   A 1 31  ? 23.298 -2.666  18.151  0.42 16.17 ?  31  LYS   A C    1 
ATOM   869  C C    B LYS   A 1 31  ? 22.957 -2.392  18.197  0.58 16.48 ?  31  LYS   A C    1 
ATOM   870  O O    A LYS   A 1 31  ? 24.088 -3.202  18.936  0.42 16.34 ?  31  LYS   A O    1 
ATOM   871  O O    B LYS   A 1 31  ? 23.700 -2.903  19.040  0.58 17.68 ?  31  LYS   A O    1 
ATOM   872  C CB   A LYS   A 1 31  ? 23.246 -0.744  19.773  0.42 22.93 ?  31  LYS   A CB   1 
ATOM   873  C CB   B LYS   A 1 31  ? 22.861 -0.387  19.722  0.58 21.82 ?  31  LYS   A CB   1 
ATOM   874  C CG   A LYS   A 1 31  ? 22.560 0.517   20.269  0.42 27.14 ?  31  LYS   A CG   1 
ATOM   875  C CG   B LYS   A 1 31  ? 22.171 0.917   20.096  0.58 26.96 ?  31  LYS   A CG   1 
ATOM   876  C CD   A LYS   A 1 31  ? 23.568 1.548   20.757  0.42 30.47 ?  31  LYS   A CD   1 
ATOM   877  C CD   B LYS   A 1 31  ? 23.157 1.939   20.637  0.58 30.91 ?  31  LYS   A CD   1 
ATOM   878  C CE   A LYS   A 1 31  ? 22.911 2.585   21.657  0.42 32.77 ?  31  LYS   A CE   1 
ATOM   879  C CE   B LYS   A 1 31  ? 22.452 3.003   21.463  0.58 34.03 ?  31  LYS   A CE   1 
ATOM   880  N NZ   A LYS   A 1 31  ? 21.729 3.230   21.022  0.42 33.80 ?  31  LYS   A NZ   1 
ATOM   881  N NZ   B LYS   A 1 31  ? 21.217 3.510   20.804  0.58 35.50 ?  31  LYS   A NZ   1 
ATOM   882  H H    A LYS   A 1 31  ? 20.808 -0.819  18.072  0.42 21.54 ?  31  LYS   A H    1 
ATOM   883  H H    B LYS   A 1 31  ? 20.480 -0.527  17.967  0.58 20.75 ?  31  LYS   A H    1 
ATOM   884  H HA   A LYS   A 1 31  ? 22.899 -0.701  17.771  0.42 22.37 ?  31  LYS   A HA   1 
ATOM   885  H HA   B LYS   A 1 31  ? 22.578 -0.438  17.712  0.58 21.51 ?  31  LYS   A HA   1 
ATOM   886  H HB2  A LYS   A 1 31  ? 23.172 -1.417  20.464  0.42 27.53 ?  31  LYS   A HB2  1 
ATOM   887  H HB2  B LYS   A 1 31  ? 22.741 -1.006  20.456  0.58 26.20 ?  31  LYS   A HB2  1 
ATOM   888  H HB3  A LYS   A 1 31  ? 24.183 -0.531  19.625  0.42 27.53 ?  31  LYS   A HB3  1 
ATOM   889  H HB3  B LYS   A 1 31  ? 23.806 -0.196  19.602  0.58 26.20 ?  31  LYS   A HB3  1 
ATOM   890  H HG2  A LYS   A 1 31  ? 22.050 0.911   19.545  0.42 32.58 ?  31  LYS   A HG2  1 
ATOM   891  H HG2  B LYS   A 1 31  ? 21.746 1.293   19.308  0.58 32.37 ?  31  LYS   A HG2  1 
ATOM   892  H HG3  A LYS   A 1 31  ? 21.974 0.293   21.010  0.42 32.58 ?  31  LYS   A HG3  1 
ATOM   893  H HG3  B LYS   A 1 31  ? 21.508 0.743   20.783  0.58 32.37 ?  31  LYS   A HG3  1 
ATOM   894  H HD2  A LYS   A 1 31  ? 24.265 1.103   21.264  0.42 36.58 ?  31  LYS   A HD2  1 
ATOM   895  H HD2  B LYS   A 1 31  ? 23.806 1.491   21.203  0.58 37.11 ?  31  LYS   A HD2  1 
ATOM   896  H HD3  A LYS   A 1 31  ? 23.952 2.008   19.992  0.42 36.58 ?  31  LYS   A HD3  1 
ATOM   897  H HD3  B LYS   A 1 31  ? 23.606 2.377   19.895  0.58 37.11 ?  31  LYS   A HD3  1 
ATOM   898  H HE2  A LYS   A 1 31  ? 22.615 2.152   22.472  0.42 39.35 ?  31  LYS   A HE2  1 
ATOM   899  H HE2  B LYS   A 1 31  ? 22.207 2.624   22.320  0.58 40.85 ?  31  LYS   A HE2  1 
ATOM   900  H HE3  A LYS   A 1 31  ? 23.556 3.279   21.864  0.42 39.35 ?  31  LYS   A HE3  1 
ATOM   901  H HE3  B LYS   A 1 31  ? 23.054 3.751   21.592  0.58 40.85 ?  31  LYS   A HE3  1 
ATOM   902  H HZ1  A LYS   A 1 31  ? 21.390 3.848   21.567  0.42 40.58 ?  31  LYS   A HZ1  1 
ATOM   903  H HZ1  B LYS   A 1 31  ? 20.880 4.187   21.273  0.58 42.61 ?  31  LYS   A HZ1  1 
ATOM   904  H HZ2  A LYS   A 1 31  ? 21.967 3.620   20.258  0.42 40.58 ?  31  LYS   A HZ2  1 
ATOM   905  H HZ2  B LYS   A 1 31  ? 21.406 3.793   19.982  0.58 42.61 ?  31  LYS   A HZ2  1 
ATOM   906  H HZ3  A LYS   A 1 31  ? 21.102 2.621   20.853  0.42 40.58 ?  31  LYS   A HZ3  1 
ATOM   907  H HZ3  B LYS   A 1 31  ? 20.609 2.862   20.754  0.58 42.61 ?  31  LYS   A HZ3  1 
ATOM   908  N N    A PRO   A 1 32  ? 22.980 -3.235  16.992  0.42 14.55 ?  32  PRO   A N    1 
ATOM   909  N N    B PRO   A 1 32  ? 22.686 -3.000  17.046  0.58 14.82 ?  32  PRO   A N    1 
ATOM   910  C CA   A PRO   A 1 32  ? 23.460 -4.582  16.669  0.42 14.89 ?  32  PRO   A CA   1 
ATOM   911  C CA   B PRO   A 1 32  ? 23.177 -4.353  16.780  0.58 15.13 ?  32  PRO   A CA   1 
ATOM   912  C C    A PRO   A 1 32  ? 24.959 -4.599  16.425  0.42 14.55 ?  32  PRO   A C    1 
ATOM   913  C C    B PRO   A 1 32  ? 24.685 -4.365  16.603  0.58 14.83 ?  32  PRO   A C    1 
ATOM   914  O O    A PRO   A 1 32  ? 25.595 -3.576  16.167  0.42 13.70 ?  32  PRO   A O    1 
ATOM   915  O O    B PRO   A 1 32  ? 25.339 -3.333  16.442  0.58 15.43 ?  32  PRO   A O    1 
ATOM   916  C CB   A PRO   A 1 32  ? 22.715 -4.913  15.374  0.42 15.27 ?  32  PRO   A CB   1 
ATOM   917  C CB   B PRO   A 1 32  ? 22.479 -4.703  15.464  0.58 15.64 ?  32  PRO   A CB   1 
ATOM   918  C CG   A PRO   A 1 32  ? 22.534 -3.585  14.724  0.42 14.78 ?  32  PRO   A CG   1 
ATOM   919  C CG   B PRO   A 1 32  ? 22.340 -3.383  14.774  0.58 15.48 ?  32  PRO   A CG   1 
ATOM   920  C CD   A PRO   A 1 32  ? 22.253 -2.633  15.862  0.42 14.19 ?  32  PRO   A CD   1 
ATOM   921  C CD   B PRO   A 1 32  ? 21.991 -2.431  15.878  0.58 14.96 ?  32  PRO   A CD   1 
ATOM   922  H HA   A PRO   A 1 32  ? 23.216 -5.214  17.369  0.42 17.89 ?  32  PRO   A HA   1 
ATOM   923  H HA   B PRO   A 1 32  ? 22.909 -4.968  17.481  0.58 18.17 ?  32  PRO   A HA   1 
ATOM   924  H HB2  A PRO   A 1 32  ? 23.260 -5.500  14.825  0.42 18.34 ?  32  PRO   A HB2  1 
ATOM   925  H HB2  B PRO   A 1 32  ? 23.029 -5.312  14.951  0.58 18.78 ?  32  PRO   A HB2  1 
ATOM   926  H HB3  A PRO   A 1 32  ? 21.860 -5.325  15.578  0.42 18.34 ?  32  PRO   A HB3  1 
ATOM   927  H HB3  B PRO   A 1 32  ? 21.605 -5.093  15.646  0.58 18.78 ?  32  PRO   A HB3  1 
ATOM   928  H HG2  A PRO   A 1 32  ? 23.346 -3.338  14.256  0.42 17.76 ?  32  PRO   A HG2  1 
ATOM   929  H HG2  B PRO   A 1 32  ? 23.182 -3.143  14.360  0.58 18.60 ?  32  PRO   A HG2  1 
ATOM   930  H HG3  A PRO   A 1 32  ? 21.782 -3.625  14.110  0.42 17.76 ?  32  PRO   A HG3  1 
ATOM   931  H HG3  B PRO   A 1 32  ? 21.629 -3.433  14.115  0.58 18.60 ?  32  PRO   A HG3  1 
ATOM   932  H HD2  A PRO   A 1 32  ? 22.609 -1.755  15.655  0.42 17.05 ?  32  PRO   A HD2  1 
ATOM   933  H HD2  B PRO   A 1 32  ? 22.327 -1.545  15.672  0.58 17.96 ?  32  PRO   A HD2  1 
ATOM   934  H HD3  A PRO   A 1 32  ? 21.300 -2.599  16.041  0.42 17.05 ?  32  PRO   A HD3  1 
ATOM   935  H HD3  B PRO   A 1 32  ? 21.028 -2.421  16.019  0.58 17.96 ?  32  PRO   A HD3  1 
ATOM   936  N N    A THR   A 1 33  ? 25.516 -5.809  16.471  0.42 14.51 ?  33  THR   A N    1 
ATOM   937  N N    B THR   A 1 33  ? 25.234 -5.577  16.609  0.58 14.35 ?  33  THR   A N    1 
ATOM   938  C CA   A THR   A 1 33  ? 26.925 -5.976  16.139  0.42 14.67 ?  33  THR   A CA   1 
ATOM   939  C CA   B THR   A 1 33  ? 26.654 -5.740  16.327  0.58 14.45 ?  33  THR   A CA   1 
ATOM   940  C C    A THR   A 1 33  ? 27.213 -5.514  14.712  0.42 13.66 ?  33  THR   A C    1 
ATOM   941  C C    B THR   A 1 33  ? 26.986 -5.302  14.909  0.58 13.37 ?  33  THR   A C    1 
ATOM   942  O O    A THR   A 1 33  ? 28.268 -4.922  14.449  0.42 13.68 ?  33  THR   A O    1 
ATOM   943  O O    B THR   A 1 33  ? 27.998 -4.626  14.684  0.58 13.30 ?  33  THR   A O    1 
ATOM   944  C CB   A THR   A 1 33  ? 27.332 -7.439  16.334  0.42 16.32 ?  33  THR   A CB   1 
ATOM   945  C CB   B THR   A 1 33  ? 27.055 -7.195  16.542  0.58 16.56 ?  33  THR   A CB   1 
ATOM   946  O OG1  A THR   A 1 33  ? 27.078 -7.834  17.688  0.42 17.72 ?  33  THR   A OG1  1 
ATOM   947  O OG1  B THR   A 1 33  ? 26.688 -7.590  17.868  0.58 18.41 ?  33  THR   A OG1  1 
ATOM   948  C CG2  A THR   A 1 33  ? 28.807 -7.641  16.035  0.42 16.59 ?  33  THR   A CG2  1 
ATOM   949  C CG2  B THR   A 1 33  ? 28.553 -7.368  16.348  0.58 17.83 ?  33  THR   A CG2  1 
ATOM   950  H H    A THR   A 1 33  ? 25.103 -6.532  16.684  0.42 17.43 ?  33  THR   A H    1 
ATOM   951  H H    B THR   A 1 33  ? 24.812 -6.303  16.770  0.58 17.23 ?  33  THR   A H    1 
ATOM   952  H HA   A THR   A 1 33  ? 27.456 -5.434  16.744  0.42 17.63 ?  33  THR   A HA   1 
ATOM   953  H HA   B THR   A 1 33  ? 27.165 -5.183  16.934  0.58 17.36 ?  33  THR   A HA   1 
ATOM   954  H HB   A THR   A 1 33  ? 26.811 -7.999  15.736  0.42 19.60 ?  33  THR   A HB   1 
ATOM   955  H HB   B THR   A 1 33  ? 26.594 -7.754  15.893  0.58 19.89 ?  33  THR   A HB   1 
ATOM   956  H HG1  A THR   A 1 33  ? 27.511 -7.345  18.219  0.42 21.28 ?  33  THR   A HG1  1 
ATOM   957  H HG1  B THR   A 1 33  ? 27.091 -7.107  18.426  0.58 22.11 ?  33  THR   A HG1  1 
ATOM   958  H HG21 A THR   A 1 33  ? 29.077 -8.532  16.309  0.42 19.93 ?  33  THR   A HG21 1 
ATOM   959  H HG21 B THR   A 1 33  ? 28.821 -8.252  16.638  0.58 21.41 ?  33  THR   A HG21 1 
ATOM   960  H HG22 A THR   A 1 33  ? 28.972 -7.538  15.087  0.42 19.93 ?  33  THR   A HG22 1 
ATOM   961  H HG22 B THR   A 1 33  ? 28.786 -7.261  15.410  0.58 21.41 ?  33  THR   A HG22 1 
ATOM   962  H HG23 A THR   A 1 33  ? 29.334 -6.989  16.524  0.42 19.93 ?  33  THR   A HG23 1 
ATOM   963  H HG23 B THR   A 1 33  ? 29.033 -6.705  16.868  0.58 21.41 ?  33  THR   A HG23 1 
ATOM   964  N N    A VAL   A 1 34  ? 26.285 -5.761  13.781  0.42 12.63 ?  34  VAL   A N    1 
ATOM   965  N N    B VAL   A 1 34  ? 26.146 -5.673  13.940  0.58 13.12 ?  34  VAL   A N    1 
ATOM   966  C CA   A VAL   A 1 34  ? 26.480 -5.436  12.369  0.42 12.11 ?  34  VAL   A CA   1 
ATOM   967  C CA   B VAL   A 1 34  ? 26.368 -5.358  12.535  0.58 12.28 ?  34  VAL   A CA   1 
ATOM   968  C C    A VAL   A 1 34  ? 25.175 -4.908  11.781  0.42 11.50 ?  34  VAL   A C    1 
ATOM   969  C C    B VAL   A 1 34  ? 25.083 -4.807  11.944  0.58 12.03 ?  34  VAL   A C    1 
ATOM   970  O O    A VAL   A 1 34  ? 24.176 -5.636  11.737  0.42 10.72 ?  34  VAL   A O    1 
ATOM   971  O O    B VAL   A 1 34  ? 24.016 -5.421  12.078  0.58 12.59 ?  34  VAL   A O    1 
ATOM   972  C CB   A VAL   A 1 34  ? 26.949 -6.656  11.551  0.42 12.09 ?  34  VAL   A CB   1 
ATOM   973  C CB   B VAL   A 1 34  ? 26.834 -6.580  11.717  0.58 13.24 ?  34  VAL   A CB   1 
ATOM   974  C CG1  A VAL   A 1 34  ? 27.121 -6.278  10.088  0.42 12.32 ?  34  VAL   A CG1  1 
ATOM   975  C CG1  B VAL   A 1 34  ? 27.089 -6.180  10.258  0.58 13.63 ?  34  VAL   A CG1  1 
ATOM   976  C CG2  A VAL   A 1 34  ? 28.240 -7.240  12.117  0.42 13.39 ?  34  VAL   A CG2  1 
ATOM   977  C CG2  B VAL   A 1 34  ? 28.076 -7.202  12.334  0.58 14.69 ?  34  VAL   A CG2  1 
ATOM   978  H H    A VAL   A 1 34  ? 25.523 -6.130  13.950  0.42 15.17 ?  34  VAL   A H    1 
ATOM   979  H H    B VAL   A 1 34  ? 25.416 -6.116  14.077  0.58 15.76 ?  34  VAL   A H    1 
ATOM   980  H HA   A VAL   A 1 34  ? 27.155 -4.745  12.295  0.42 14.55 ?  34  VAL   A HA   1 
ATOM   981  H HA   B VAL   A 1 34  ? 27.045 -4.671  12.460  0.58 14.76 ?  34  VAL   A HA   1 
ATOM   982  H HB   A VAL   A 1 34  ? 26.270 -7.344  11.606  0.42 14.52 ?  34  VAL   A HB   1 
ATOM   983  H HB   B VAL   A 1 34  ? 26.135 -7.250  11.721  0.58 15.91 ?  34  VAL   A HB   1 
ATOM   984  H HG11 A VAL   A 1 34  ? 27.635 -6.971  9.646   0.42 14.80 ?  34  VAL   A HG11 1 
ATOM   985  H HG11 B VAL   A 1 34  ? 27.572 -6.897  9.812   0.58 16.38 ?  34  VAL   A HG11 1 
ATOM   986  H HG12 A VAL   A 1 34  ? 26.249 -6.198  9.678   0.42 14.80 ?  34  VAL   A HG12 1 
ATOM   987  H HG12 B VAL   A 1 34  ? 26.243 -6.028  9.812   0.58 16.38 ?  34  VAL   A HG12 1 
ATOM   988  H HG13 A VAL   A 1 34  ? 27.596 -5.433  10.036  0.42 14.80 ?  34  VAL   A HG13 1 
ATOM   989  H HG13 B VAL   A 1 34  ? 27.625 -5.368  10.239  0.58 16.38 ?  34  VAL   A HG13 1 
ATOM   990  H HG21 A VAL   A 1 34  ? 28.546 -7.956  11.533  0.42 16.09 ?  34  VAL   A HG21 1 
ATOM   991  H HG21 B VAL   A 1 34  ? 28.373 -7.940  11.777  0.58 17.65 ?  34  VAL   A HG21 1 
ATOM   992  H HG22 A VAL   A 1 34  ? 28.914 -6.545  12.164  0.42 16.09 ?  34  VAL   A HG22 1 
ATOM   993  H HG22 B VAL   A 1 34  ? 28.774 -6.530  12.390  0.58 17.65 ?  34  VAL   A HG22 1 
ATOM   994  H HG23 A VAL   A 1 34  ? 28.069 -7.595  13.005  0.42 16.09 ?  34  VAL   A HG23 1 
ATOM   995  H HG23 B VAL   A 1 34  ? 27.860 -7.527  13.223  0.58 17.65 ?  34  VAL   A HG23 1 
ATOM   996  N N    . VAL   A 1 35  ? 25.192 -3.655  11.289  1.00 11.46 ?  35  VAL   A N    1 
ATOM   997  C CA   . VAL   A 1 35  ? 24.159 -3.140  10.397  1.00 11.31 ?  35  VAL   A CA   1 
ATOM   998  C C    . VAL   A 1 35  ? 24.728 -3.147  8.983   1.00 11.05 ?  35  VAL   A C    1 
ATOM   999  O O    . VAL   A 1 35  ? 25.874 -2.740  8.762   1.00 11.73 ?  35  VAL   A O    1 
ATOM   1000 C CB   . VAL   A 1 35  ? 23.629 -1.741  10.793  1.00 12.20 ?  35  VAL   A CB   1 
ATOM   1001 C CG1  . VAL   A 1 35  ? 24.702 -0.652  10.674  1.00 12.76 ?  35  VAL   A CG1  1 
ATOM   1002 C CG2  . VAL   A 1 35  ? 22.404 -1.392  9.949   1.00 12.65 ?  35  VAL   A CG2  1 
ATOM   1003 H H    A VAL   A 1 35  ? 25.808 -3.079  11.454  0.42 13.76 ?  35  VAL   A H    1 
ATOM   1004 H H    B VAL   A 1 35  ? 25.874 -3.135  11.345  0.58 13.76 ?  35  VAL   A H    1 
ATOM   1005 H HA   . VAL   A 1 35  ? 23.402 -3.751  10.411  1.00 13.59 ?  35  VAL   A HA   1 
ATOM   1006 H HB   . VAL   A 1 35  ? 23.336 -1.774  11.715  1.00 14.66 ?  35  VAL   A HB   1 
ATOM   1007 H HG11 . VAL   A 1 35  ? 24.349 0.177   11.033  1.00 15.33 ?  35  VAL   A HG11 1 
ATOM   1008 H HG12 . VAL   A 1 35  ? 25.482 -0.927  11.176  1.00 15.33 ?  35  VAL   A HG12 1 
ATOM   1009 H HG13 . VAL   A 1 35  ? 24.933 -0.534  9.738   1.00 15.33 ?  35  VAL   A HG13 1 
ATOM   1010 H HG21 . VAL   A 1 35  ? 22.037 -0.553  10.254  1.00 15.20 ?  35  VAL   A HG21 1 
ATOM   1011 H HG22 . VAL   A 1 35  ? 22.671 -1.321  9.016   1.00 15.20 ?  35  VAL   A HG22 1 
ATOM   1012 H HG23 . VAL   A 1 35  ? 21.742 -2.100  10.043  1.00 15.20 ?  35  VAL   A HG23 1 
ATOM   1013 N N    . VAL   A 1 36  ? 23.931 -3.614  8.024   1.00 10.29 ?  36  VAL   A N    1 
ATOM   1014 C CA   . VAL   A 1 36  ? 24.326 -3.633  6.620   1.00 10.21 ?  36  VAL   A CA   1 
ATOM   1015 C C    . VAL   A 1 36  ? 23.866 -2.346  5.941   1.00 10.68 ?  36  VAL   A C    1 
ATOM   1016 O O    . VAL   A 1 36  ? 22.705 -1.944  6.072   1.00 10.82 ?  36  VAL   A O    1 
ATOM   1017 C CB   . VAL   A 1 36  ? 23.738 -4.858  5.904   1.00 10.67 ?  36  VAL   A CB   1 
ATOM   1018 C CG1  . VAL   A 1 36  ? 24.013 -4.786  4.415   1.00 11.36 ?  36  VAL   A CG1  1 
ATOM   1019 C CG2  . VAL   A 1 36  ? 24.285 -6.136  6.502   1.00 11.30 ?  36  VAL   A CG2  1 
ATOM   1020 H H    . VAL   A 1 36  ? 23.140 -3.933  8.165   1.00 12.36 ?  36  VAL   A H    1 
ATOM   1021 H HA   . VAL   A 1 36  ? 25.296 -3.688  6.565   1.00 12.27 ?  36  VAL   A HA   1 
ATOM   1022 H HB   . VAL   A 1 36  ? 22.777 -4.858  6.031   1.00 12.82 ?  36  VAL   A HB   1 
ATOM   1023 H HG11 . VAL   A 1 36  ? 23.886 -5.668  4.031   1.00 13.65 ?  36  VAL   A HG11 1 
ATOM   1024 H HG12 . VAL   A 1 36  ? 23.392 -4.160  4.007   1.00 13.65 ?  36  VAL   A HG12 1 
ATOM   1025 H HG13 . VAL   A 1 36  ? 24.924 -4.492  4.275   1.00 13.65 ?  36  VAL   A HG13 1 
ATOM   1026 H HG21 . VAL   A 1 36  ? 23.910 -6.892  6.019   1.00 13.58 ?  36  VAL   A HG21 1 
ATOM   1027 H HG22 . VAL   A 1 36  ? 25.251 -6.137  6.411   1.00 13.58 ?  36  VAL   A HG22 1 
ATOM   1028 H HG23 . VAL   A 1 36  ? 24.037 -6.183  7.435   1.00 13.58 ?  36  VAL   A HG23 1 
ATOM   1029 N N    . ASN   A 1 37  ? 24.786 -1.712  5.203   1.00 9.85  ?  37  ASN   A N    1 
ATOM   1030 C CA   . ASN   A 1 37  ? 24.463 -0.605  4.323   1.00 9.91  ?  37  ASN   A CA   1 
ATOM   1031 C C    . ASN   A 1 37  ? 24.345 -1.097  2.891   1.00 9.89  ?  37  ASN   A C    1 
ATOM   1032 O O    . ASN   A 1 37  ? 25.154 -1.915  2.427   1.00 10.48 ?  37  ASN   A O    1 
ATOM   1033 C CB   . ASN   A 1 37  ? 25.537 0.473   4.411   1.00 10.58 ?  37  ASN   A CB   1 
ATOM   1034 C CG   . ASN   A 1 37  ? 25.219 1.665   3.548   1.00 10.37 ?  37  ASN   A CG   1 
ATOM   1035 O OD1  . ASN   A 1 37  ? 24.044 1.989   3.330   1.00 11.04 ?  37  ASN   A OD1  1 
ATOM   1036 N ND2  . ASN   A 1 37  ? 26.261 2.342   3.060   1.00 10.81 ?  37  ASN   A ND2  1 
ATOM   1037 H H    . ASN   A 1 37  ? 25.626 -1.922  5.203   1.00 11.84 ?  37  ASN   A H    1 
ATOM   1038 H HA   . ASN   A 1 37  ? 23.624 -0.216  4.589   1.00 11.90 ?  37  ASN   A HA   1 
ATOM   1039 H HB2  . ASN   A 1 37  ? 25.612 0.777   5.331   1.00 12.71 ?  37  ASN   A HB2  1 
ATOM   1040 H HB3  . ASN   A 1 37  ? 26.390 0.106   4.117   1.00 12.71 ?  37  ASN   A HB3  1 
ATOM   1041 H HD21 . ASN   A 1 37  ? 26.134 3.030   2.562   1.00 12.99 ?  37  ASN   A HD21 1 
ATOM   1042 H HD22 . ASN   A 1 37  ? 27.060 2.086   3.232   1.00 12.99 ?  37  ASN   A HD22 1 
ATOM   1043 N N    A ALA   A 1 38  ? 23.343 -0.553  2.200   0.42 10.48 ?  38  ALA   A N    1 
ATOM   1044 N N    B ALA   A 1 38  ? 23.342 -0.597  2.176   0.58 10.82 ?  38  ALA   A N    1 
ATOM   1045 C CA   A ALA   A 1 38  ? 23.178 -0.650  0.752   0.42 10.43 ?  38  ALA   A CA   1 
ATOM   1046 C CA   B ALA   A 1 38  ? 23.194 -0.886  0.750   0.58 10.93 ?  38  ALA   A CA   1 
ATOM   1047 C C    A ALA   A 1 38  ? 24.110 0.372   0.098   0.42 9.92  ?  38  ALA   A C    1 
ATOM   1048 C C    B ALA   A 1 38  ? 24.003 0.156   -0.020  0.58 10.99 ?  38  ALA   A C    1 
ATOM   1049 O O    A ALA   A 1 38  ? 23.714 1.472   -0.298  0.42 9.14  ?  38  ALA   A O    1 
ATOM   1050 O O    B ALA   A 1 38  ? 23.495 1.206   -0.424  0.58 11.60 ?  38  ALA   A O    1 
ATOM   1051 C CB   A ALA   A 1 38  ? 21.722 -0.390  0.382   0.42 10.68 ?  38  ALA   A CB   1 
ATOM   1052 C CB   B ALA   A 1 38  ? 21.725 -0.893  0.347   0.58 11.70 ?  38  ALA   A CB   1 
ATOM   1053 H H    A ALA   A 1 38  ? 22.722 -0.095  2.576   0.42 12.59 ?  38  ALA   A H    1 
ATOM   1054 H H    B ALA   A 1 38  ? 22.739 -0.077  2.497   0.58 13.00 ?  38  ALA   A H    1 
ATOM   1055 H HA   A ALA   A 1 38  ? 23.425 -1.532  0.452   0.42 12.54 ?  38  ALA   A HA   1 
ATOM   1056 H HA   B ALA   A 1 38  ? 23.567 -1.761  0.562   0.58 13.13 ?  38  ALA   A HA   1 
ATOM   1057 H HB1  A ALA   A 1 38  ? 21.624 -0.455  -0.580  0.42 12.83 ?  38  ALA   A HB1  1 
ATOM   1058 H HB1  B ALA   A 1 38  ? 21.663 -1.052  -0.609  0.58 14.06 ?  38  ALA   A HB1  1 
ATOM   1059 H HB2  A ALA   A 1 38  ? 21.161 -1.049  0.820   0.42 12.83 ?  38  ALA   A HB2  1 
ATOM   1060 H HB2  B ALA   A 1 38  ? 21.268 -1.604  0.827   0.58 14.06 ?  38  ALA   A HB2  1 
ATOM   1061 H HB3  A ALA   A 1 38  ? 21.472 0.503   0.678   0.42 12.83 ?  38  ALA   A HB3  1 
ATOM   1062 H HB3  B ALA   A 1 38  ? 21.330 -0.037  0.565   0.58 14.06 ?  38  ALA   A HB3  1 
ATOM   1063 N N    A ALA   A 1 39  ? 25.379 -0.008  -0.007  0.42 10.30 ?  39  ALA   A N    1 
ATOM   1064 N N    B ALA   A 1 39  ? 25.282 -0.144  -0.227  0.58 11.25 ?  39  ALA   A N    1 
ATOM   1065 C CA   A ALA   A 1 39  ? 26.444 0.872   -0.465  0.42 10.80 ?  39  ALA   A CA   1 
ATOM   1066 C CA   B ALA   A 1 39  ? 26.247 0.833   -0.708  0.58 10.27 ?  39  ALA   A CA   1 
ATOM   1067 C C    A ALA   A 1 39  ? 26.621 0.792   -1.978  0.42 10.41 ?  39  ALA   A C    1 
ATOM   1068 C C    B ALA   A 1 39  ? 26.397 0.788   -2.227  0.58 9.96  ?  39  ALA   A C    1 
ATOM   1069 O O    A ALA   A 1 39  ? 26.155 -0.143  -2.635  0.42 10.13 ?  39  ALA   A O    1 
ATOM   1070 O O    B ALA   A 1 39  ? 25.928 -0.129  -2.905  0.58 11.19 ?  39  ALA   A O    1 
ATOM   1071 C CB   A ALA   A 1 39  ? 27.757 0.477   0.212   0.42 11.78 ?  39  ALA   A CB   1 
ATOM   1072 C CB   B ALA   A 1 39  ? 27.601 0.599   -0.035  0.58 11.34 ?  39  ALA   A CB   1 
ATOM   1073 H H    A ALA   A 1 39  ? 25.656 -0.798  0.190   0.42 12.38 ?  39  ALA   A H    1 
ATOM   1074 H H    B ALA   A 1 39  ? 25.621 -0.929  -0.088  0.58 13.52 ?  39  ALA   A H    1 
ATOM   1075 H HA   A ALA   A 1 39  ? 26.237 1.789   -0.219  0.42 12.97 ?  39  ALA   A HA   1 
ATOM   1076 H HA   B ALA   A 1 39  ? 25.940 1.718   -0.457  0.58 12.34 ?  39  ALA   A HA   1 
ATOM   1077 H HB1  A ALA   A 1 39  ? 28.463 1.068   -0.099  0.42 14.15 ?  39  ALA   A HB1  1 
ATOM   1078 H HB1  B ALA   A 1 39  ? 28.234 1.262   -0.359  0.58 13.62 ?  39  ALA   A HB1  1 
ATOM   1079 H HB2  A ALA   A 1 39  ? 27.657 0.562   1.174   0.42 14.15 ?  39  ALA   A HB2  1 
ATOM   1080 H HB2  B ALA   A 1 39  ? 27.503 0.691   0.930   0.58 13.62 ?  39  ALA   A HB2  1 
ATOM   1081 H HB3  A ALA   A 1 39  ? 27.969 -0.440  -0.019  0.42 14.15 ?  39  ALA   A HB3  1 
ATOM   1082 H HB3  B ALA   A 1 39  ? 27.917 -0.291  -0.248  0.58 13.62 ?  39  ALA   A HB3  1 
ATOM   1083 N N    A ASN   A 1 40  ? 27.325 1.786   -2.523  0.42 11.23 ?  40  ASN   A N    1 
ATOM   1084 N N    B ASN   A 1 40  ? 27.053 1.815   -2.761  0.58 10.16 ?  40  ASN   A N    1 
ATOM   1085 C CA   A ASN   A 1 40  ? 27.893 1.713   -3.865  0.42 10.78 ?  40  ASN   A CA   1 
ATOM   1086 C CA   B ASN   A 1 40  ? 27.612 1.780   -4.103  0.58 10.25 ?  40  ASN   A CA   1 
ATOM   1087 C C    A ASN   A 1 40  ? 29.414 1.610   -3.771  0.42 10.77 ?  40  ASN   A C    1 
ATOM   1088 C C    B ASN   A 1 40  ? 29.126 1.622   -4.004  0.58 9.44  ?  40  ASN   A C    1 
ATOM   1089 O O    A ASN   A 1 40  ? 29.999 1.739   -2.691  0.42 11.13 ?  40  ASN   A O    1 
ATOM   1090 O O    B ASN   A 1 40  ? 29.709 1.700   -2.920  0.58 9.72  ?  40  ASN   A O    1 
ATOM   1091 C CB   A ASN   A 1 40  ? 27.435 2.882   -4.756  0.42 11.99 ?  40  ASN   A CB   1 
ATOM   1092 C CB   B ASN   A 1 40  ? 27.207 3.022   -4.910  0.58 11.13 ?  40  ASN   A CB   1 
ATOM   1093 C CG   A ASN   A 1 40  ? 27.734 4.239   -4.157  0.42 13.15 ?  40  ASN   A CG   1 
ATOM   1094 C CG   B ASN   A 1 40  ? 27.635 4.316   -4.258  0.58 11.74 ?  40  ASN   A CG   1 
ATOM   1095 O OD1  A ASN   A 1 40  ? 28.865 4.522   -3.762  0.42 13.24 ?  40  ASN   A OD1  1 
ATOM   1096 O OD1  B ASN   A 1 40  ? 28.822 4.537   -4.028  0.58 11.96 ?  40  ASN   A OD1  1 
ATOM   1097 N ND2  A ASN   A 1 40  ? 26.711 5.093   -4.092  0.42 14.10 ?  40  ASN   A ND2  1 
ATOM   1098 N ND2  B ASN   A 1 40  ? 26.667 5.185   -3.966  0.58 13.40 ?  40  ASN   A ND2  1 
ATOM   1099 H H    A ASN   A 1 40  ? 27.493 2.531   -2.123  0.42 13.49 ?  40  ASN   A H    1 
ATOM   1100 H H    B ASN   A 1 40  ? 27.184 2.555   -2.347  0.58 12.21 ?  40  ASN   A H    1 
ATOM   1101 H HA   A ASN   A 1 40  ? 27.573 0.904   -4.285  0.42 12.95 ?  40  ASN   A HA   1 
ATOM   1102 H HA   B ASN   A 1 40  ? 27.255 0.994   -4.560  0.58 12.31 ?  40  ASN   A HA   1 
ATOM   1103 H HB2  A ASN   A 1 40  ? 27.891 2.819   -5.620  0.42 14.41 ?  40  ASN   A HB2  1 
ATOM   1104 H HB2  B ASN   A 1 40  ? 27.620 2.969   -5.780  0.58 13.37 ?  40  ASN   A HB2  1 
ATOM   1105 H HB3  A ASN   A 1 40  ? 26.477 2.824   -4.897  0.42 14.41 ?  40  ASN   A HB3  1 
ATOM   1106 H HB3  B ASN   A 1 40  ? 26.240 3.035   -4.997  0.58 13.37 ?  40  ASN   A HB3  1 
ATOM   1107 H HD21 A ASN   A 1 40  ? 26.829 5.886   -3.774  0.42 16.93 ?  40  ASN   A HD21 1 
ATOM   1108 H HD21 B ASN   A 1 40  ? 26.867 5.939   -3.600  0.58 16.10 ?  40  ASN   A HD21 1 
ATOM   1109 H HD22 A ASN   A 1 40  ? 25.932 4.855   -4.365  0.42 16.93 ?  40  ASN   A HD22 1 
ATOM   1110 H HD22 B ASN   A 1 40  ? 25.853 4.997   -4.150  0.58 16.10 ?  40  ASN   A HD22 1 
ATOM   1111 N N    A VAL   A 1 41  ? 30.051 1.343   -4.918  0.42 10.76 ?  41  VAL   A N    1 
ATOM   1112 N N    B VAL   A 1 41  ? 29.758 1.355   -5.150  0.58 9.98  ?  41  VAL   A N    1 
ATOM   1113 C CA   A VAL   A 1 41  ? 31.481 1.029   -4.924  0.42 10.47 ?  41  VAL   A CA   1 
ATOM   1114 C CA   B VAL   A 1 41  ? 31.183 1.034   -5.158  0.58 10.81 ?  41  VAL   A CA   1 
ATOM   1115 C C    A VAL   A 1 41  ? 32.314 2.187   -4.404  0.42 10.32 ?  41  VAL   A C    1 
ATOM   1116 C C    B VAL   A 1 41  ? 32.065 2.170   -4.656  0.58 10.66 ?  41  VAL   A C    1 
ATOM   1117 O O    A VAL   A 1 41  ? 33.394 1.977   -3.837  0.42 10.59 ?  41  VAL   A O    1 
ATOM   1118 O O    B VAL   A 1 41  ? 33.224 1.927   -4.297  0.58 10.40 ?  41  VAL   A O    1 
ATOM   1119 C CB   A VAL   A 1 41  ? 31.975 0.537   -6.307  0.42 10.46 ?  41  VAL   A CB   1 
ATOM   1120 C CB   B VAL   A 1 41  ? 31.668 0.563   -6.551  0.58 12.25 ?  41  VAL   A CB   1 
ATOM   1121 C CG1  A VAL   A 1 41  ? 31.297 -0.768  -6.700  0.42 10.54 ?  41  VAL   A CG1  1 
ATOM   1122 C CG1  B VAL   A 1 41  ? 30.942 -0.700  -6.990  0.58 13.38 ?  41  VAL   A CG1  1 
ATOM   1123 C CG2  A VAL   A 1 41  ? 31.789 1.601   -7.389  0.42 11.32 ?  41  VAL   A CG2  1 
ATOM   1124 C CG2  B VAL   A 1 41  ? 31.535 1.674   -7.591  0.58 13.80 ?  41  VAL   A CG2  1 
ATOM   1125 H H    A VAL   A 1 41  ? 29.684 1.337   -5.691  0.42 12.93 ?  41  VAL   A H    1 
ATOM   1126 H H    B VAL   A 1 41  ? 29.381 1.338   -5.921  0.58 11.99 ?  41  VAL   A H    1 
ATOM   1127 H HA   A VAL   A 1 41  ? 31.630 0.306   -4.307  0.42 12.58 ?  41  VAL   A HA   1 
ATOM   1128 H HA   B VAL   A 1 41  ? 31.318 0.284   -4.551  0.58 12.99 ?  41  VAL   A HA   1 
ATOM   1129 H HB   A VAL   A 1 41  ? 32.930 0.356   -6.248  0.42 12.57 ?  41  VAL   A HB   1 
ATOM   1130 H HB   B VAL   A 1 41  ? 32.612 0.341   -6.481  0.58 14.72 ?  41  VAL   A HB   1 
ATOM   1131 H HG11 A VAL   A 1 41  ? 31.669 -1.085  -7.539  0.42 12.67 ?  41  VAL   A HG11 1 
ATOM   1132 H HG11 B VAL   A 1 41  ? 31.257 -0.957  -7.870  0.58 16.07 ?  41  VAL   A HG11 1 
ATOM   1133 H HG12 A VAL   A 1 41  ? 31.450 -1.427  -6.003  0.42 12.67 ?  41  VAL   A HG12 1 
ATOM   1134 H HG12 B VAL   A 1 41  ? 31.123 -1.411  -6.354  0.58 16.07 ?  41  VAL   A HG12 1 
ATOM   1135 H HG13 A VAL   A 1 41  ? 30.345 -0.611  -6.800  0.42 12.67 ?  41  VAL   A HG13 1 
ATOM   1136 H HG13 B VAL   A 1 41  ? 29.988 -0.523  -7.021  0.58 16.07 ?  41  VAL   A HG13 1 
ATOM   1137 H HG21 A VAL   A 1 41  ? 32.058 1.229   -8.247  0.42 13.60 ?  41  VAL   A HG21 1 
ATOM   1138 H HG21 B VAL   A 1 41  ? 31.766 1.313   -8.460  0.58 16.57 ?  41  VAL   A HG21 1 
ATOM   1139 H HG22 A VAL   A 1 41  ? 30.853 1.853   -7.422  0.42 13.60 ?  41  VAL   A HG22 1 
ATOM   1140 H HG22 B VAL   A 1 41  ? 30.620 1.989   -7.592  0.58 16.57 ?  41  VAL   A HG22 1 
ATOM   1141 H HG23 A VAL   A 1 41  ? 32.335 2.370   -7.176  0.42 13.60 ?  41  VAL   A HG23 1 
ATOM   1142 H HG23 B VAL   A 1 41  ? 32.138 2.395   -7.358  0.58 16.57 ?  41  VAL   A HG23 1 
ATOM   1143 N N    A TYR   A 1 42  ? 31.837 3.416   -4.579  0.42 10.44 ?  42  TYR   A N    1 
ATOM   1144 N N    B TYR   A 1 42  ? 31.565 3.411   -4.648  0.58 11.41 ?  42  TYR   A N    1 
ATOM   1145 C CA   A TYR   A 1 42  ? 32.547 4.602   -4.127  0.42 10.72 ?  42  TYR   A CA   1 
ATOM   1146 C CA   B TYR   A 1 42  ? 32.338 4.583   -4.240  0.58 11.44 ?  42  TYR   A CA   1 
ATOM   1147 C C    A TYR   A 1 42  ? 32.203 4.964   -2.693  0.42 10.79 ?  42  TYR   A C    1 
ATOM   1148 C C    B TYR   A 1 42  ? 32.113 4.977   -2.787  0.58 11.09 ?  42  TYR   A C    1 
ATOM   1149 O O    A TYR   A 1 42  ? 32.770 5.919   -2.153  0.42 11.29 ?  42  TYR   A O    1 
ATOM   1150 O O    B TYR   A 1 42  ? 32.671 5.979   -2.333  0.58 11.15 ?  42  TYR   A O    1 
ATOM   1151 C CB   A TYR   A 1 42  ? 32.241 5.786   -5.058  0.42 11.18 ?  42  TYR   A CB   1 
ATOM   1152 C CB   B TYR   A 1 42  ? 31.989 5.783   -5.128  0.58 12.13 ?  42  TYR   A CB   1 
ATOM   1153 C CG   A TYR   A 1 42  ? 32.445 5.450   -6.520  0.42 11.45 ?  42  TYR   A CG   1 
ATOM   1154 C CG   B TYR   A 1 42  ? 32.111 5.495   -6.603  0.58 12.81 ?  42  TYR   A CG   1 
ATOM   1155 C CD1  A TYR   A 1 42  ? 33.719 5.270   -7.034  0.42 11.78 ?  42  TYR   A CD1  1 
ATOM   1156 C CD1  B TYR   A 1 42  ? 33.350 5.269   -7.184  0.58 13.03 ?  42  TYR   A CD1  1 
ATOM   1157 C CD2  A TYR   A 1 42  ? 31.364 5.301   -7.384  0.42 11.88 ?  42  TYR   A CD2  1 
ATOM   1158 C CD2  B TYR   A 1 42  ? 30.987 5.448   -7.416  0.58 14.16 ?  42  TYR   A CD2  1 
ATOM   1159 C CE1  A TYR   A 1 42  ? 33.914 4.948   -8.363  0.42 12.11 ?  42  TYR   A CE1  1 
ATOM   1160 C CE1  B TYR   A 1 42  ? 33.468 4.987   -8.530  0.58 12.85 ?  42  TYR   A CE1  1 
ATOM   1161 C CE2  A TYR   A 1 42  ? 31.551 4.984   -8.719  0.42 12.12 ?  42  TYR   A CE2  1 
ATOM   1162 C CE2  B TYR   A 1 42  ? 31.094 5.184   -8.766  0.58 14.56 ?  42  TYR   A CE2  1 
ATOM   1163 C CZ   A TYR   A 1 42  ? 32.829 4.809   -9.203  0.42 11.79 ?  42  TYR   A CZ   1 
ATOM   1164 C CZ   B TYR   A 1 42  ? 32.341 4.952   -9.319  0.58 13.75 ?  42  TYR   A CZ   1 
ATOM   1165 O OH   A TYR   A 1 42  ? 33.020 4.490   -10.529 0.42 12.57 ?  42  TYR   A OH   1 
ATOM   1166 O OH   B TYR   A 1 42  ? 32.469 4.688   -10.663 0.58 14.69 ?  42  TYR   A OH   1 
ATOM   1167 H H    A TYR   A 1 42  ? 31.086 3.592   -4.949  0.42 12.55 ?  42  TYR   A H    1 
ATOM   1168 H H    B TYR   A 1 42  ? 30.760 3.600   -4.891  0.58 13.71 ?  42  TYR   A H    1 
ATOM   1169 H HA   A TYR   A 1 42  ? 33.503 4.438   -4.165  0.42 12.88 ?  42  TYR   A HA   1 
ATOM   1170 H HA   B TYR   A 1 42  ? 33.280 4.388   -4.357  0.58 13.74 ?  42  TYR   A HA   1 
ATOM   1171 H HB2  A TYR   A 1 42  ? 31.317 6.052   -4.940  0.42 13.43 ?  42  TYR   A HB2  1 
ATOM   1172 H HB2  B TYR   A 1 42  ? 31.073 6.047   -4.948  0.58 14.57 ?  42  TYR   A HB2  1 
ATOM   1173 H HB3  A TYR   A 1 42  ? 32.831 6.524   -4.839  0.42 13.43 ?  42  TYR   A HB3  1 
ATOM   1174 H HB3  B TYR   A 1 42  ? 32.591 6.512   -4.914  0.58 14.57 ?  42  TYR   A HB3  1 
ATOM   1175 H HD1  A TYR   A 1 42  ? 34.456 5.357   -6.472  0.42 14.15 ?  42  TYR   A HD1  1 
ATOM   1176 H HD1  B TYR   A 1 42  ? 34.118 5.283   -6.653  0.58 15.65 ?  42  TYR   A HD1  1 
ATOM   1177 H HD2  A TYR   A 1 42  ? 30.499 5.417   -7.061  0.42 14.28 ?  42  TYR   A HD2  1 
ATOM   1178 H HD2  B TYR   A 1 42  ? 30.147 5.602   -7.041  0.58 17.00 ?  42  TYR   A HD2  1 
ATOM   1179 H HE1  A TYR   A 1 42  ? 34.778 4.830   -8.692  0.42 14.55 ?  42  TYR   A HE1  1 
ATOM   1180 H HE1  B TYR   A 1 42  ? 34.306 4.835   -8.906  0.58 15.44 ?  42  TYR   A HE1  1 
ATOM   1181 H HE2  A TYR   A 1 42  ? 30.817 4.888   -9.289  0.42 14.56 ?  42  TYR   A HE2  1 
ATOM   1182 H HE2  B TYR   A 1 42  ? 30.327 5.156   -9.294  0.58 17.49 ?  42  TYR   A HE2  1 
ATOM   1183 H HH   A TYR   A 1 42  ? 33.826 4.294   -10.664 0.42 15.10 ?  42  TYR   A HH   1 
ATOM   1184 H HH   B TYR   A 1 42  ? 31.713 4.693   -11.030 0.58 17.65 ?  42  TYR   A HH   1 
ATOM   1185 N N    . LEU   A 1 43  ? 31.291 4.225   -2.064  1.00 10.77 ?  43  LEU   A N    1 
ATOM   1186 C CA   . LEU   A 1 43  ? 30.832 4.574   -0.723  1.00 10.55 ?  43  LEU   A CA   1 
ATOM   1187 C C    . LEU   A 1 43  ? 30.356 6.025   -0.644  1.00 10.52 ?  43  LEU   A C    1 
ATOM   1188 O O    . LEU   A 1 43  ? 30.602 6.731   0.335   1.00 11.96 ?  43  LEU   A O    1 
ATOM   1189 C CB   . LEU   A 1 43  ? 31.859 4.256   0.367   1.00 11.13 ?  43  LEU   A CB   1 
ATOM   1190 C CG   . LEU   A 1 43  ? 32.356 2.808   0.448   1.00 11.51 ?  43  LEU   A CG   1 
ATOM   1191 C CD1  . LEU   A 1 43  ? 33.388 2.693   1.550   1.00 12.02 ?  43  LEU   A CD1  1 
ATOM   1192 C CD2  . LEU   A 1 43  ? 31.212 1.820   0.658   1.00 12.10 ?  43  LEU   A CD2  1 
ATOM   1193 H H    A LEU   A 1 43  ? 30.926 3.512   -2.385  0.42 12.95 ?  43  LEU   A H    1 
ATOM   1194 H H    B LEU   A 1 43  ? 30.960 3.478   -2.341  0.58 12.95 ?  43  LEU   A H    1 
ATOM   1195 H HA   . LEU   A 1 43  ? 30.051 4.023   -0.530  1.00 12.68 ?  43  LEU   A HA   1 
ATOM   1196 H HB2  . LEU   A 1 43  ? 32.625 4.821   0.234   1.00 13.38 ?  43  LEU   A HB2  1 
ATOM   1197 H HB3  . LEU   A 1 43  ? 31.450 4.459   1.229   1.00 13.38 ?  43  LEU   A HB3  1 
ATOM   1198 H HG   . LEU   A 1 43  ? 32.793 2.584   -0.394  1.00 13.83 ?  43  LEU   A HG   1 
ATOM   1199 H HD11 . LEU   A 1 43  ? 33.706 1.774   1.589   1.00 14.44 ?  43  LEU   A HD11 1 
ATOM   1200 H HD12 . LEU   A 1 43  ? 34.129 3.287   1.353   1.00 14.44 ?  43  LEU   A HD12 1 
ATOM   1201 H HD13 . LEU   A 1 43  ? 32.979 2.937   2.391   1.00 14.44 ?  43  LEU   A HD13 1 
ATOM   1202 H HD21 . LEU   A 1 43  ? 31.593 0.934   0.792   1.00 14.54 ?  43  LEU   A HD21 1 
ATOM   1203 H HD22 . LEU   A 1 43  ? 30.708 2.089   1.431   1.00 14.54 ?  43  LEU   A HD22 1 
ATOM   1204 H HD23 . LEU   A 1 43  ? 30.654 1.820   -0.134  1.00 14.54 ?  43  LEU   A HD23 1 
ATOM   1205 N N    A LYS   A 1 44  ? 29.647 6.468   -1.681  0.42 10.90 ?  44  LYS   A N    1 
ATOM   1206 N N    B LYS   A 1 44  ? 29.645 6.460   -1.685  0.58 10.62 ?  44  LYS   A N    1 
ATOM   1207 C CA   A LYS   A 1 44  ? 29.020 7.791   -1.680  0.42 11.70 ?  44  LYS   A CA   1 
ATOM   1208 C CA   B LYS   A 1 44  ? 29.005 7.776   -1.706  0.58 11.44 ?  44  LYS   A CA   1 
ATOM   1209 C C    A LYS   A 1 44  ? 27.584 7.615   -1.206  0.42 11.01 ?  44  LYS   A C    1 
ATOM   1210 C C    B LYS   A 1 44  ? 27.577 7.589   -1.215  0.58 11.11 ?  44  LYS   A C    1 
ATOM   1211 O O    A LYS   A 1 44  ? 26.725 7.128   -1.947  0.42 11.93 ?  44  LYS   A O    1 
ATOM   1212 O O    B LYS   A 1 44  ? 26.725 7.051   -1.929  0.58 12.18 ?  44  LYS   A O    1 
ATOM   1213 C CB   A LYS   A 1 44  ? 29.091 8.424   -3.064  0.42 13.83 ?  44  LYS   A CB   1 
ATOM   1214 C CB   B LYS   A 1 44  ? 29.044 8.370   -3.108  0.58 13.65 ?  44  LYS   A CB   1 
ATOM   1215 C CG   A LYS   A 1 44  ? 30.492 8.806   -3.502  0.42 17.07 ?  44  LYS   A CG   1 
ATOM   1216 C CG   B LYS   A 1 44  ? 30.399 8.897   -3.527  0.58 17.80 ?  44  LYS   A CG   1 
ATOM   1217 C CD   A LYS   A 1 44  ? 31.178 9.698   -2.483  0.42 21.11 ?  44  LYS   A CD   1 
ATOM   1218 C CD   B LYS   A 1 44  ? 30.958 9.873   -2.509  0.58 22.53 ?  44  LYS   A CD   1 
ATOM   1219 C CE   A LYS   A 1 44  ? 32.524 10.177  -2.985  0.42 23.47 ?  44  LYS   A CE   1 
ATOM   1220 C CE   B LYS   A 1 44  ? 32.126 10.654  -3.082  0.58 25.18 ?  44  LYS   A CE   1 
ATOM   1221 N NZ   A LYS   A 1 44  ? 33.295 10.852  -1.909  0.42 24.77 ?  44  LYS   A NZ   1 
ATOM   1222 N NZ   B LYS   A 1 44  ? 33.109 11.018  -2.029  0.58 27.10 ?  44  LYS   A NZ   1 
ATOM   1223 H H    A LYS   A 1 44  ? 29.519 6.019   -2.403  0.42 13.10 ?  44  LYS   A H    1 
ATOM   1224 H H    B LYS   A 1 44  ? 29.521 6.003   -2.402  0.58 12.76 ?  44  LYS   A H    1 
ATOM   1225 H HA   A LYS   A 1 44  ? 29.472 8.363   -1.040  0.42 14.06 ?  44  LYS   A HA   1 
ATOM   1226 H HA   B LYS   A 1 44  ? 29.459 8.369   -1.085  0.58 13.74 ?  44  LYS   A HA   1 
ATOM   1227 H HB2  A LYS   A 1 44  ? 28.737 7.796   -3.712  0.42 16.61 ?  44  LYS   A HB2  1 
ATOM   1228 H HB2  B LYS   A 1 44  ? 28.781 7.684   -3.742  0.58 16.40 ?  44  LYS   A HB2  1 
ATOM   1229 H HB3  A LYS   A 1 44  ? 28.551 9.232   -3.061  0.42 16.61 ?  44  LYS   A HB3  1 
ATOM   1230 H HB3  B LYS   A 1 44  ? 28.413 9.108   -3.148  0.58 16.40 ?  44  LYS   A HB3  1 
ATOM   1231 H HG2  A LYS   A 1 44  ? 31.022 8.002   -3.609  0.42 20.50 ?  44  LYS   A HG2  1 
ATOM   1232 H HG2  B LYS   A 1 44  ? 31.018 8.155   -3.613  0.58 21.38 ?  44  LYS   A HG2  1 
ATOM   1233 H HG3  A LYS   A 1 44  ? 30.441 9.289   -4.344  0.42 20.50 ?  44  LYS   A HG3  1 
ATOM   1234 H HG3  B LYS   A 1 44  ? 30.313 9.361   -4.376  0.58 21.38 ?  44  LYS   A HG3  1 
ATOM   1235 H HD2  A LYS   A 1 44  ? 30.616 10.472  -2.307  0.42 25.35 ?  44  LYS   A HD2  1 
ATOM   1236 H HD2  B LYS   A 1 44  ? 30.264 10.498  -2.247  0.58 27.06 ?  44  LYS   A HD2  1 
ATOM   1237 H HD3  A LYS   A 1 44  ? 31.327 9.199   -1.666  0.42 25.35 ?  44  LYS   A HD3  1 
ATOM   1238 H HD3  B LYS   A 1 44  ? 31.277 9.380   -1.735  0.58 27.06 ?  44  LYS   A HD3  1 
ATOM   1239 H HE2  A LYS   A 1 44  ? 33.037 9.417   -3.296  0.42 28.19 ?  44  LYS   A HE2  1 
ATOM   1240 H HE2  B LYS   A 1 44  ? 32.579 10.110  -3.746  0.58 30.23 ?  44  LYS   A HE2  1 
ATOM   1241 H HE3  A LYS   A 1 44  ? 32.388 10.811  -3.708  0.42 28.19 ?  44  LYS   A HE3  1 
ATOM   1242 H HE3  B LYS   A 1 44  ? 31.796 11.471  -3.486  0.58 30.23 ?  44  LYS   A HE3  1 
ATOM   1243 H HZ1  A LYS   A 1 44  ? 34.079 11.128  -2.224  0.42 29.74 ?  44  LYS   A HZ1  1 
ATOM   1244 H HZ1  B LYS   A 1 44  ? 33.785 11.471  -2.388  0.58 32.54 ?  44  LYS   A HZ1  1 
ATOM   1245 H HZ2  A LYS   A 1 44  ? 32.841 11.560  -1.609  0.42 29.74 ?  44  LYS   A HZ2  1 
ATOM   1246 H HZ2  B LYS   A 1 44  ? 32.718 11.523  -1.410  0.58 32.54 ?  44  LYS   A HZ2  1 
ATOM   1247 H HZ3  A LYS   A 1 44  ? 33.432 10.292  -1.234  0.42 29.74 ?  44  LYS   A HZ3  1 
ATOM   1248 H HZ3  B LYS   A 1 44  ? 33.427 10.281  -1.643  0.58 32.54 ?  44  LYS   A HZ3  1 
ATOM   1249 N N    A HIS   A 1 45  ? 27.326 7.994   0.043   0.42 10.22 ?  45  HIS   A N    1 
ATOM   1250 N N    B HIS   A 1 45  ? 27.320 8.000   0.025   0.58 10.85 ?  45  HIS   A N    1 
ATOM   1251 C CA   A HIS   A 1 45  ? 26.078 7.635   0.720   0.42 10.26 ?  45  HIS   A CA   1 
ATOM   1252 C CA   B HIS   A 1 45  ? 26.063 7.688   0.709   0.58 11.45 ?  45  HIS   A CA   1 
ATOM   1253 C C    A HIS   A 1 45  ? 25.063 8.773   0.597   0.42 10.60 ?  45  HIS   A C    1 
ATOM   1254 C C    B HIS   A 1 45  ? 25.076 8.822   0.461   0.58 11.79 ?  45  HIS   A C    1 
ATOM   1255 O O    A HIS   A 1 45  ? 24.697 9.447   1.563   0.42 10.89 ?  45  HIS   A O    1 
ATOM   1256 O O    B HIS   A 1 45  ? 24.959 9.758   1.254   0.58 13.17 ?  45  HIS   A O    1 
ATOM   1257 C CB   A HIS   A 1 45  ? 26.362 7.281   2.172   0.42 9.71  ?  45  HIS   A CB   1 
ATOM   1258 C CB   B HIS   A 1 45  ? 26.319 7.507   2.195   0.58 11.13 ?  45  HIS   A CB   1 
ATOM   1259 C CG   A HIS   A 1 45  ? 27.485 6.310   2.350   0.42 9.37  ?  45  HIS   A CG   1 
ATOM   1260 C CG   B HIS   A 1 45  ? 27.428 6.557   2.500   0.58 10.25 ?  45  HIS   A CG   1 
ATOM   1261 N ND1  A HIS   A 1 45  ? 27.474 5.046   1.797   0.42 8.80  ?  45  HIS   A ND1  1 
ATOM   1262 N ND1  B HIS   A 1 45  ? 27.431 5.258   2.042   0.58 10.86 ?  45  HIS   A ND1  1 
ATOM   1263 C CD2  A HIS   A 1 45  ? 28.650 6.418   3.031   0.42 10.10 ?  45  HIS   A CD2  1 
ATOM   1264 C CD2  B HIS   A 1 45  ? 28.571 6.716   3.207   0.58 9.86  ?  45  HIS   A CD2  1 
ATOM   1265 C CE1  A HIS   A 1 45  ? 28.588 4.419   2.133   0.42 10.13 ?  45  HIS   A CE1  1 
ATOM   1266 C CE1  B HIS   A 1 45  ? 28.528 4.655   2.464   0.58 9.45  ?  45  HIS   A CE1  1 
ATOM   1267 N NE2  A HIS   A 1 45  ? 29.321 5.231   2.875   0.42 10.88 ?  45  HIS   A NE2  1 
ATOM   1268 N NE2  B HIS   A 1 45  ? 29.243 5.519   3.166   0.58 9.29  ?  45  HIS   A NE2  1 
ATOM   1269 H H    A HIS   A 1 45  ? 27.865 8.462   0.527   0.42 12.29 ?  45  HIS   A H    1 
ATOM   1270 H H    B HIS   A 1 45  ? 27.865 8.461   0.503   0.58 13.04 ?  45  HIS   A H    1 
ATOM   1271 H HA   A HIS   A 1 45  ? 25.701 6.853   0.292   0.42 12.33 ?  45  HIS   A HA   1 
ATOM   1272 H HA   B HIS   A 1 45  ? 25.690 6.861   0.353   0.58 13.75 ?  45  HIS   A HA   1 
ATOM   1273 H HB2  A HIS   A 1 45  ? 26.584 8.087   2.657   0.42 11.67 ?  45  HIS   A HB2  1 
ATOM   1274 H HB2  B HIS   A 1 45  ? 26.546 8.363   2.580   0.58 13.38 ?  45  HIS   A HB2  1 
ATOM   1275 H HB3  A HIS   A 1 45  ? 25.560 6.878   2.554   0.42 11.67 ?  45  HIS   A HB3  1 
ATOM   1276 H HB3  B HIS   A 1 45  ? 25.508 7.162   2.611   0.58 13.38 ?  45  HIS   A HB3  1 
ATOM   1277 H HD2  A HIS   A 1 45  ? 28.943 7.162   3.506   0.42 12.13 ?  45  HIS   A HD2  1 
ATOM   1278 H HD2  B HIS   A 1 45  ? 28.854 7.491   3.631   0.58 11.85 ?  45  HIS   A HD2  1 
ATOM   1279 H HE1  A HIS   A 1 45  ? 28.820 3.550   1.892   0.42 12.17 ?  45  HIS   A HE1  1 
ATOM   1280 H HE1  B HIS   A 1 45  ? 28.762 3.769   2.294   0.58 11.36 ?  45  HIS   A HE1  1 
ATOM   1281 H HE2  A HIS   A 1 45  ? 30.091 5.045   3.214   0.42 13.07 ?  45  HIS   A HE2  1 
ATOM   1282 H HE2  B HIS   A 1 45  ? 30.000 5.353   3.540   0.58 11.17 ?  45  HIS   A HE2  1 
ATOM   1283 N N    A GLY   A 1 46  ? 24.583 8.956   -0.629  0.42 11.48 ?  46  GLY   A N    1 
ATOM   1284 N N    B GLY   A 1 46  ? 24.337 8.731   -0.639  0.58 11.66 ?  46  GLY   A N    1 
ATOM   1285 C CA   A GLY   A 1 46  ? 23.776 10.121  -0.957  0.42 12.26 ?  46  GLY   A CA   1 
ATOM   1286 C CA   B GLY   A 1 46  ? 23.494 9.847   -1.036  0.58 12.38 ?  46  GLY   A CA   1 
ATOM   1287 C C    A GLY   A 1 46  ? 22.276 9.959   -0.788  0.42 12.20 ?  46  GLY   A C    1 
ATOM   1288 C C    B GLY   A 1 46  ? 22.041 9.731   -0.617  0.58 12.42 ?  46  GLY   A C    1 
ATOM   1289 O O    A GLY   A 1 46  ? 21.576 10.940  -0.525  0.42 12.93 ?  46  GLY   A O    1 
ATOM   1290 O O    B GLY   A 1 46  ? 21.458 10.680  -0.083  0.58 13.90 ?  46  GLY   A O    1 
ATOM   1291 H H    A GLY   A 1 46  ? 24.715 8.419   -1.284  0.42 13.79 ?  46  GLY   A H    1 
ATOM   1292 H H    B GLY   A 1 46  ? 24.310 8.046   -1.162  0.58 14.01 ?  46  GLY   A H    1 
ATOM   1293 H HA2  A GLY   A 1 46  ? 24.066 10.863  -0.398  0.42 14.72 ?  46  GLY   A HA2  1 
ATOM   1294 H HA2  B GLY   A 1 46  ? 23.854 10.662  -0.648  0.58 14.88 ?  46  GLY   A HA2  1 
ATOM   1295 H HA3  A GLY   A 1 46  ? 23.948 10.361  -1.879  0.42 14.72 ?  46  GLY   A HA3  1 
ATOM   1296 H HA3  B GLY   A 1 46  ? 23.526 9.932   -1.996  0.58 14.88 ?  46  GLY   A HA3  1 
ATOM   1297 N N    A GLY   A 1 47  ? 21.763 8.743   -0.946  0.42 12.42 ?  47  GLY   A N    1 
ATOM   1298 N N    B GLY   A 1 47  ? 21.442 8.568   -0.856  0.58 13.00 ?  47  GLY   A N    1 
ATOM   1299 C CA   A GLY   A 1 47  ? 20.329 8.525   -0.932  0.42 12.01 ?  47  GLY   A CA   1 
ATOM   1300 C CA   B GLY   A 1 47  ? 20.019 8.390   -0.660  0.58 12.36 ?  47  GLY   A CA   1 
ATOM   1301 C C    A GLY   A 1 47  ? 20.013 7.094   -0.550  0.42 11.65 ?  47  GLY   A C    1 
ATOM   1302 C C    B GLY   A 1 47  ? 19.704 6.973   -0.236  0.58 11.18 ?  47  GLY   A C    1 
ATOM   1303 O O    A GLY   A 1 47  ? 20.904 6.286   -0.283  0.42 11.51 ?  47  GLY   A O    1 
ATOM   1304 O O    B GLY   A 1 47  ? 20.596 6.144   -0.051  0.58 11.51 ?  47  GLY   A O    1 
ATOM   1305 H H    A GLY   A 1 47  ? 22.227 8.032   -1.054  0.42 14.92 ?  47  GLY   A H    1 
ATOM   1306 H H    B GLY   A 1 47  ? 21.856 7.860   -1.121  0.58 15.62 ?  47  GLY   A H    1 
ATOM   1307 H HA2  A GLY   A 1 47  ? 19.905 9.124   -0.295  0.42 14.43 ?  47  GLY   A HA2  1 
ATOM   1308 H HA2  B GLY   A 1 47  ? 19.702 8.998   0.021   0.58 14.85 ?  47  GLY   A HA2  1 
ATOM   1309 H HA3  A GLY   A 1 47  ? 19.966 8.702   -1.815  0.42 14.43 ?  47  GLY   A HA3  1 
ATOM   1310 H HA3  B GLY   A 1 47  ? 19.556 8.577   -1.491  0.58 14.85 ?  47  GLY   A HA3  1 
ATOM   1311 N N    A GLY   A 1 48  ? 18.720 6.781   -0.539  0.42 11.06 ?  48  GLY   A N    1 
ATOM   1312 N N    B GLY   A 1 48  ? 18.411 6.698   -0.090  0.58 11.00 ?  48  GLY   A N    1 
ATOM   1313 C CA   A GLY   A 1 48  ? 18.316 5.440   -0.161  0.42 10.67 ?  48  GLY   A CA   1 
ATOM   1314 C CA   B GLY   A 1 48  ? 17.983 5.393   0.367   0.58 10.82 ?  48  GLY   A CA   1 
ATOM   1315 C C    A GLY   A 1 48  ? 18.721 5.114   1.265   0.42 10.74 ?  48  GLY   A C    1 
ATOM   1316 C C    B GLY   A 1 48  ? 18.590 5.040   1.711   0.58 10.49 ?  48  GLY   A C    1 
ATOM   1317 O O    A GLY   A 1 48  ? 18.873 5.997   2.115   0.42 11.01 ?  48  GLY   A O    1 
ATOM   1318 O O    B GLY   A 1 48  ? 18.791 5.889   2.589   0.58 11.41 ?  48  GLY   A O    1 
ATOM   1319 H H    A GLY   A 1 48  ? 18.080 7.311   -0.742  0.42 13.29 ?  48  GLY   A H    1 
ATOM   1320 H H    B GLY   A 1 48  ? 17.771 7.249   -0.243  0.58 13.21 ?  48  GLY   A H    1 
ATOM   1321 H HA2  A GLY   A 1 48  ? 17.356 5.356   -0.233  0.42 12.82 ?  48  GLY   A HA2  1 
ATOM   1322 H HA2  B GLY   A 1 48  ? 17.015 5.375   0.448   0.58 13.01 ?  48  GLY   A HA2  1 
ATOM   1323 H HA3  A GLY   A 1 48  ? 18.733 4.792   -0.751  0.42 12.82 ?  48  GLY   A HA3  1 
ATOM   1324 H HA3  B GLY   A 1 48  ? 18.251 4.716   -0.276  0.58 13.01 ?  48  GLY   A HA3  1 
ATOM   1325 N N    A VAL   A 1 49  ? 18.904 3.816   1.534   0.42 11.14 ?  49  VAL   A N    1 
ATOM   1326 N N    B VAL   A 1 49  ? 18.872 3.746   1.878   0.58 10.74 ?  49  VAL   A N    1 
ATOM   1327 C CA   A VAL   A 1 49  ? 19.358 3.397   2.860   0.42 11.31 ?  49  VAL   A CA   1 
ATOM   1328 C CA   B VAL   A 1 49  ? 19.492 3.252   3.105   0.58 10.92 ?  49  VAL   A CA   1 
ATOM   1329 C C    A VAL   A 1 49  ? 20.690 4.051   3.204   0.42 10.00 ?  49  VAL   A C    1 
ATOM   1330 C C    B VAL   A 1 49  ? 20.755 4.044   3.432   0.58 10.26 ?  49  VAL   A C    1 
ATOM   1331 O O    A VAL   A 1 49  ? 20.920 4.447   4.349   0.42 9.83  ?  49  VAL   A O    1 
ATOM   1332 O O    B VAL   A 1 49  ? 20.958 4.476   4.571   0.58 10.97 ?  49  VAL   A O    1 
ATOM   1333 C CB   A VAL   A 1 49  ? 19.447 1.860   2.950   0.42 12.52 ?  49  VAL   A CB   1 
ATOM   1334 C CB   B VAL   A 1 49  ? 19.795 1.748   2.969   0.58 10.85 ?  49  VAL   A CB   1 
ATOM   1335 C CG1  A VAL   A 1 49  ? 20.214 1.434   4.205   0.42 13.18 ?  49  VAL   A CG1  1 
ATOM   1336 C CG1  B VAL   A 1 49  ? 20.633 1.263   4.137   0.58 10.77 ?  49  VAL   A CG1  1 
ATOM   1337 C CG2  A VAL   A 1 49  ? 18.057 1.234   2.949   0.42 13.66 ?  49  VAL   A CG2  1 
ATOM   1338 C CG2  B VAL   A 1 49  ? 18.502 0.927   2.853   0.58 11.92 ?  49  VAL   A CG2  1 
ATOM   1339 H H    A VAL   A 1 49  ? 18.772 3.173   0.980   0.42 13.38 ?  49  VAL   A H    1 
ATOM   1340 H H    B VAL   A 1 49  ? 18.706 3.138   1.296   0.58 12.90 ?  49  VAL   A H    1 
ATOM   1341 H HA   A VAL   A 1 49  ? 18.708 3.685   3.518   0.42 13.59 ?  49  VAL   A HA   1 
ATOM   1342 H HA   B VAL   A 1 49  ? 18.870 3.360   3.841   0.58 13.12 ?  49  VAL   A HA   1 
ATOM   1343 H HB   A VAL   A 1 49  ? 19.928 1.521   2.180   0.42 15.04 ?  49  VAL   A HB   1 
ATOM   1344 H HB   B VAL   A 1 49  ? 20.306 1.600   2.157   0.58 13.04 ?  49  VAL   A HB   1 
ATOM   1345 H HG11 A VAL   A 1 49  ? 20.019 0.501   4.393   0.42 15.84 ?  49  VAL   A HG11 1 
ATOM   1346 H HG11 B VAL   A 1 49  ? 20.568 0.297   4.190   0.58 12.94 ?  49  VAL   A HG11 1 
ATOM   1347 H HG12 A VAL   A 1 49  ? 21.165 1.546   4.054   0.42 15.84 ?  49  VAL   A HG12 1 
ATOM   1348 H HG12 B VAL   A 1 49  ? 21.555 1.524   3.993   0.58 12.94 ?  49  VAL   A HG12 1 
ATOM   1349 H HG13 A VAL   A 1 49  ? 19.928 1.984   4.953   0.42 15.84 ?  49  VAL   A HG13 1 
ATOM   1350 H HG13 B VAL   A 1 49  ? 20.294 1.662   4.952   0.58 12.94 ?  49  VAL   A HG13 1 
ATOM   1351 H HG21 A VAL   A 1 49  ? 18.146 0.269   2.996   0.42 16.41 ?  49  VAL   A HG21 1 
ATOM   1352 H HG21 B VAL   A 1 49  ? 18.727 -0.009  2.734   0.58 14.33 ?  49  VAL   A HG21 1 
ATOM   1353 H HG22 A VAL   A 1 49  ? 17.567 1.558   3.721   0.42 16.41 ?  49  VAL   A HG22 1 
ATOM   1354 H HG22 B VAL   A 1 49  ? 17.981 1.040   3.665   0.58 14.33 ?  49  VAL   A HG22 1 
ATOM   1355 H HG23 A VAL   A 1 49  ? 17.601 1.487   2.134   0.42 16.41 ?  49  VAL   A HG23 1 
ATOM   1356 H HG23 B VAL   A 1 49  ? 17.992 1.243   2.089   0.58 14.33 ?  49  VAL   A HG23 1 
ATOM   1357 N N    A ALA   A 1 50  ? 21.606 4.115   2.237   0.42 9.99  ?  50  ALA   A N    1 
ATOM   1358 N N    B ALA   A 1 50  ? 21.644 4.196   2.449   0.58 9.98  ?  50  ALA   A N    1 
ATOM   1359 C CA   A ALA   A 1 50  ? 22.933 4.663   2.506   0.42 9.94  ?  50  ALA   A CA   1 
ATOM   1360 C CA   B ALA   A 1 50  ? 22.963 4.758   2.726   0.58 9.31  ?  50  ALA   A CA   1 
ATOM   1361 C C    A ALA   A 1 50  ? 22.850 6.115   2.956   0.42 10.22 ?  50  ALA   A C    1 
ATOM   1362 C C    B ALA   A 1 50  ? 22.864 6.219   3.137   0.58 9.08  ?  50  ALA   A C    1 
ATOM   1363 O O    A ALA   A 1 50  ? 23.505 6.516   3.923   0.42 10.52 ?  50  ALA   A O    1 
ATOM   1364 O O    B ALA   A 1 50  ? 23.462 6.639   4.134   0.58 9.65  ?  50  ALA   A O    1 
ATOM   1365 C CB   A ALA   A 1 50  ? 23.804 4.532   1.259   0.42 10.38 ?  50  ALA   A CB   1 
ATOM   1366 C CB   B ALA   A 1 50  ? 23.855 4.616   1.497   0.58 10.09 ?  50  ALA   A CB   1 
ATOM   1367 H H    A ALA   A 1 50  ? 21.488 3.843   1.434   0.42 12.00 ?  50  ALA   A H    1 
ATOM   1368 H H    B ALA   A 1 50  ? 21.505 3.991   1.626   0.58 11.99 ?  50  ALA   A H    1 
ATOM   1369 H HA   A ALA   A 1 50  ? 23.349 4.160   3.224   0.42 11.94 ?  50  ALA   A HA   1 
ATOM   1370 H HA   B ALA   A 1 50  ? 23.367 4.272   3.460   0.58 11.19 ?  50  ALA   A HA   1 
ATOM   1371 H HB1  A ALA   A 1 50  ? 24.679 4.904   1.448   0.42 12.47 ?  50  ALA   A HB1  1 
ATOM   1372 H HB1  B ALA   A 1 50  ? 24.724 4.995   1.697   0.58 12.13 ?  50  ALA   A HB1  1 
ATOM   1373 H HB2  A ALA   A 1 50  ? 23.884 3.594   1.029   0.42 12.47 ?  50  ALA   A HB2  1 
ATOM   1374 H HB2  B ALA   A 1 50  ? 23.942 3.676   1.281   0.58 12.13 ?  50  ALA   A HB2  1 
ATOM   1375 H HB3  A ALA   A 1 50  ? 23.385 5.018   0.533   0.42 12.47 ?  50  ALA   A HB3  1 
ATOM   1376 H HB3  B ALA   A 1 50  ? 23.447 5.092   0.757   0.58 12.13 ?  50  ALA   A HB3  1 
ATOM   1377 N N    A GLY   A 1 51  ? 22.041 6.922   2.271   0.42 10.89 ?  51  GLY   A N    1 
ATOM   1378 N N    B GLY   A 1 51  ? 22.097 7.007   2.385   0.58 10.05 ?  51  GLY   A N    1 
ATOM   1379 C CA   A GLY   A 1 51  ? 21.887 8.306   2.689   0.42 11.59 ?  51  GLY   A CA   1 
ATOM   1380 C CA   B GLY   A 1 51  ? 21.945 8.409   2.733   0.58 10.08 ?  51  GLY   A CA   1 
ATOM   1381 C C    A GLY   A 1 51  ? 21.258 8.423   4.064   0.42 11.76 ?  51  GLY   A C    1 
ATOM   1382 C C    B GLY   A 1 51  ? 21.312 8.587   4.098   0.58 9.50  ?  51  GLY   A C    1 
ATOM   1383 O O    A GLY   A 1 51  ? 21.634 9.286   4.861   0.42 12.39 ?  51  GLY   A O    1 
ATOM   1384 O O    B GLY   A 1 51  ? 21.687 9.487   4.856   0.58 10.09 ?  51  GLY   A O    1 
ATOM   1385 H H    A GLY   A 1 51  ? 21.591 6.701   1.574   0.42 13.08 ?  51  GLY   A H    1 
ATOM   1386 H H    B GLY   A 1 51  ? 21.665 6.759   1.683   0.58 12.07 ?  51  GLY   A H    1 
ATOM   1387 H HA2  A GLY   A 1 51  ? 22.754 8.740   2.714   0.42 13.93 ?  51  GLY   A HA2  1 
ATOM   1388 H HA2  B GLY   A 1 51  ? 22.809 8.842   2.735   0.58 12.11 ?  51  GLY   A HA2  1 
ATOM   1389 H HA3  A GLY   A 1 51  ? 21.326 8.779   2.051   0.42 13.93 ?  51  GLY   A HA3  1 
ATOM   1390 H HA3  B GLY   A 1 51  ? 21.381 8.849   2.069   0.58 12.11 ?  51  GLY   A HA3  1 
ATOM   1391 N N    A ALA   A 1 52  ? 20.297 7.544   4.364   0.42 11.73 ?  52  ALA   A N    1 
ATOM   1392 N N    B ALA   A 1 52  ? 20.343 7.723   4.433   0.58 9.86  ?  52  ALA   A N    1 
ATOM   1393 C CA   A ALA   A 1 52  ? 19.636 7.570   5.665   0.42 11.36 ?  52  ALA   A CA   1 
ATOM   1394 C CA   B ALA   A 1 52  ? 19.663 7.829   5.721   0.58 10.70 ?  52  ALA   A CA   1 
ATOM   1395 C C    A ALA   A 1 52  ? 20.598 7.191   6.785   0.42 11.59 ?  52  ALA   A C    1 
ATOM   1396 C C    B ALA   A 1 52  ? 20.559 7.377   6.872   0.58 10.18 ?  52  ALA   A C    1 
ATOM   1397 O O    A ALA   A 1 52  ? 20.665 7.869   7.816   0.42 12.01 ?  52  ALA   A O    1 
ATOM   1398 O O    B ALA   A 1 52  ? 20.602 8.027   7.924   0.58 10.93 ?  52  ALA   A O    1 
ATOM   1399 C CB   A ALA   A 1 52  ? 18.422 6.639   5.652   0.42 11.72 ?  52  ALA   A CB   1 
ATOM   1400 C CB   B ALA   A 1 52  ? 18.344 7.056   5.698   0.58 11.56 ?  52  ALA   A CB   1 
ATOM   1401 H H    A ALA   A 1 52  ? 20.015 6.930   3.837   0.42 14.10 ?  52  ALA   A H    1 
ATOM   1402 H H    B ALA   A 1 52  ? 20.064 7.076   3.929   0.58 11.85 ?  52  ALA   A H    1 
ATOM   1403 H HA   A ALA   A 1 52  ? 19.320 8.469   5.843   0.42 13.64 ?  52  ALA   A HA   1 
ATOM   1404 H HA   B ALA   A 1 52  ? 19.443 8.761   5.868   0.58 12.86 ?  52  ALA   A HA   1 
ATOM   1405 H HB1  A ALA   A 1 52  ? 17.992 6.669   6.524   0.42 14.08 ?  52  ALA   A HB1  1 
ATOM   1406 H HB1  B ALA   A 1 52  ? 17.909 7.150   6.562   0.58 13.89 ?  52  ALA   A HB1  1 
ATOM   1407 H HB2  A ALA   A 1 52  ? 17.803 6.940   4.970   0.42 14.08 ?  52  ALA   A HB2  1 
ATOM   1408 H HB2  B ALA   A 1 52  ? 17.774 7.417   5.001   0.58 13.89 ?  52  ALA   A HB2  1 
ATOM   1409 H HB3  A ALA   A 1 52  ? 18.717 5.737   5.461   0.42 14.08 ?  52  ALA   A HB3  1 
ATOM   1410 H HB3  B ALA   A 1 52  ? 18.527 6.119   5.522   0.58 13.89 ?  52  ALA   A HB3  1 
ATOM   1411 N N    A LEU   A 1 53  ? 21.360 6.108   6.606   0.42 11.24 ?  53  LEU   A N    1 
ATOM   1412 N N    B LEU   A 1 53  ? 21.292 6.270   6.697   0.58 10.19 ?  53  LEU   A N    1 
ATOM   1413 C CA   A LEU   A 1 53  ? 22.300 5.711   7.649   0.42 11.69 ?  53  LEU   A CA   1 
ATOM   1414 C CA   B LEU   A 1 53  ? 22.249 5.862   7.724   0.58 9.97  ?  53  LEU   A CA   1 
ATOM   1415 C C    A LEU   A 1 53  ? 23.364 6.778   7.851   0.42 11.16 ?  53  LEU   A C    1 
ATOM   1416 C C    B LEU   A 1 53  ? 23.283 6.953   7.939   0.58 9.05  ?  53  LEU   A C    1 
ATOM   1417 O O    A LEU   A 1 53  ? 23.729 7.097   8.987   0.42 11.43 ?  53  LEU   A O    1 
ATOM   1418 O O    B LEU   A 1 53  ? 23.558 7.354   9.073   0.58 9.85  ?  53  LEU   A O    1 
ATOM   1419 C CB   A LEU   A 1 53  ? 22.943 4.364   7.311   0.42 12.04 ?  53  LEU   A CB   1 
ATOM   1420 C CB   B LEU   A 1 53  ? 22.954 4.554   7.338   0.58 10.41 ?  53  LEU   A CB   1 
ATOM   1421 C CG   A LEU   A 1 53  ? 21.994 3.163   7.294   0.42 12.14 ?  53  LEU   A CG   1 
ATOM   1422 C CG   B LEU   A 1 53  ? 22.218 3.207   7.444   0.58 10.85 ?  53  LEU   A CG   1 
ATOM   1423 C CD1  A LEU   A 1 53  ? 22.718 1.953   6.752   0.42 12.66 ?  53  LEU   A CD1  1 
ATOM   1424 C CD1  B LEU   A 1 53  ? 23.032 2.099   6.786   0.58 10.90 ?  53  LEU   A CD1  1 
ATOM   1425 C CD2  A LEU   A 1 53  ? 21.437 2.883   8.687   0.42 12.12 ?  53  LEU   A CD2  1 
ATOM   1426 C CD2  B LEU   A 1 53  ? 21.907 2.845   8.887   0.58 11.35 ?  53  LEU   A CD2  1 
ATOM   1427 H H    A LEU   A 1 53  ? 21.352 5.600   5.910   0.42 13.50 ?  53  LEU   A H    1 
ATOM   1428 H H    B LEU   A 1 53  ? 21.254 5.755   6.012   0.58 12.24 ?  53  LEU   A H    1 
ATOM   1429 H HA   A LEU   A 1 53  ? 21.822 5.606   8.484   0.42 14.05 ?  53  LEU   A HA   1 
ATOM   1430 H HA   B LEU   A 1 53  ? 21.784 5.720   8.559   0.58 11.98 ?  53  LEU   A HA   1 
ATOM   1431 H HB2  A LEU   A 1 53  ? 23.348 4.423   6.430   0.42 14.46 ?  53  LEU   A HB2  1 
ATOM   1432 H HB2  B LEU   A 1 53  ? 23.236 4.638   6.411   0.58 12.50 ?  53  LEU   A HB2  1 
ATOM   1433 H HB3  A LEU   A 1 53  ? 23.634 4.173   7.968   0.42 14.46 ?  53  LEU   A HB3  1 
ATOM   1434 H HB3  B LEU   A 1 53  ? 23.747 4.475   7.892   0.58 12.50 ?  53  LEU   A HB3  1 
ATOM   1435 H HG   A LEU   A 1 53  ? 21.248 3.360   6.703   0.42 14.58 ?  53  LEU   A HG   1 
ATOM   1436 H HG   B LEU   A 1 53  ? 21.380 3.277   6.965   0.58 13.04 ?  53  LEU   A HG   1 
ATOM   1437 H HD11 A LEU   A 1 53  ? 22.109 1.200   6.749   0.42 15.21 ?  53  LEU   A HD11 1 
ATOM   1438 H HD11 B LEU   A 1 53  ? 22.542 1.262   6.872   0.58 13.09 ?  53  LEU   A HD11 1 
ATOM   1439 H HD12 A LEU   A 1 53  ? 23.017 2.145   5.850   0.42 15.21 ?  53  LEU   A HD12 1 
ATOM   1440 H HD12 B LEU   A 1 53  ? 23.160 2.311   5.851   0.58 13.09 ?  53  LEU   A HD12 1 
ATOM   1441 H HD13 A LEU   A 1 53  ? 23.479 1.765   7.322   0.42 15.21 ?  53  LEU   A HD13 1 
ATOM   1442 H HD13 B LEU   A 1 53  ? 23.887 2.026   7.235   0.58 13.09 ?  53  LEU   A HD13 1 
ATOM   1443 H HD21 A LEU   A 1 53  ? 20.917 2.067   8.661   0.42 14.56 ?  53  LEU   A HD21 1 
ATOM   1444 H HD21 B LEU   A 1 53  ? 21.430 2.002   8.904   0.58 13.64 ?  53  LEU   A HD21 1 
ATOM   1445 H HD22 A LEU   A 1 53  ? 22.177 2.787   9.308   0.42 14.56 ?  53  LEU   A HD22 1 
ATOM   1446 H HD22 B LEU   A 1 53  ? 22.737 2.769   9.381   0.58 13.64 ?  53  LEU   A HD22 1 
ATOM   1447 H HD23 A LEU   A 1 53  ? 20.874 3.625   8.960   0.42 14.56 ?  53  LEU   A HD23 1 
ATOM   1448 H HD23 B LEU   A 1 53  ? 21.355 3.545   9.274   0.58 13.64 ?  53  LEU   A HD23 1 
ATOM   1449 N N    A ASN   A 1 54  ? 23.862 7.358   6.760   0.42 10.75 ?  54  ASN   A N    1 
ATOM   1450 N N    B ASN   A 1 54  ? 23.856 7.457   6.850   0.58 9.37  ?  54  ASN   A N    1 
ATOM   1451 C CA   A ASN   A 1 54  ? 24.909 8.361   6.894   0.42 10.74 ?  54  ASN   A CA   1 
ATOM   1452 C CA   B ASN   A 1 54  ? 24.902 8.455   6.996   0.58 10.10 ?  54  ASN   A CA   1 
ATOM   1453 C C    A ASN   A 1 54  ? 24.391 9.627   7.578   0.42 11.18 ?  54  ASN   A C    1 
ATOM   1454 C C    B ASN   A 1 54  ? 24.380 9.681   7.737   0.58 9.86  ?  54  ASN   A C    1 
ATOM   1455 O O    A ASN   A 1 54  ? 25.109 10.248  8.371   0.42 10.97 ?  54  ASN   A O    1 
ATOM   1456 O O    B ASN   A 1 54  ? 25.034 10.193  8.654   0.58 10.33 ?  54  ASN   A O    1 
ATOM   1457 C CB   A ASN   A 1 54  ? 25.508 8.682   5.529   0.42 10.91 ?  54  ASN   A CB   1 
ATOM   1458 C CB   B ASN   A 1 54  ? 25.459 8.853   5.637   0.58 10.01 ?  54  ASN   A CB   1 
ATOM   1459 C CG   A ASN   A 1 54  ? 26.569 9.751   5.613   0.42 11.73 ?  54  ASN   A CG   1 
ATOM   1460 C CG   B ASN   A 1 54  ? 26.475 9.953   5.765   0.58 9.93  ?  54  ASN   A CG   1 
ATOM   1461 O OD1  A ASN   A 1 54  ? 27.571 9.593   6.313   0.42 12.52 ?  54  ASN   A OD1  1 
ATOM   1462 O OD1  B ASN   A 1 54  ? 27.476 9.804   6.481   0.58 9.74  ?  54  ASN   A OD1  1 
ATOM   1463 N ND2  A ASN   A 1 54  ? 26.355 10.850  4.914   0.42 11.99 ?  54  ASN   A ND2  1 
ATOM   1464 N ND2  B ASN   A 1 54  ? 26.216 11.076  5.117   0.58 10.46 ?  54  ASN   A ND2  1 
ATOM   1465 H H    A ASN   A 1 54  ? 23.616 7.182   5.952   0.42 12.91 ?  54  ASN   A H    1 
ATOM   1466 H H    B ASN   A 1 54  ? 23.655 7.249   6.039   0.58 11.26 ?  54  ASN   A H    1 
ATOM   1467 H HA   A ASN   A 1 54  ? 25.612 7.990   7.447   0.42 12.90 ?  54  ASN   A HA   1 
ATOM   1468 H HA   B ASN   A 1 54  ? 25.620 8.082   7.517   0.58 12.14 ?  54  ASN   A HA   1 
ATOM   1469 H HB2  A ASN   A 1 54  ? 25.909 7.876   5.165   0.42 13.11 ?  54  ASN   A HB2  1 
ATOM   1470 H HB2  B ASN   A 1 54  ? 25.889 8.082   5.234   0.58 12.03 ?  54  ASN   A HB2  1 
ATOM   1471 H HB3  A ASN   A 1 54  ? 24.804 8.997   4.942   0.42 13.11 ?  54  ASN   A HB3  1 
ATOM   1472 H HB3  B ASN   A 1 54  ? 24.736 9.167   5.071   0.58 12.03 ?  54  ASN   A HB3  1 
ATOM   1473 H HD21 A ASN   A 1 54  ? 26.932 11.486  4.933   0.42 14.41 ?  54  ASN   A HD21 1 
ATOM   1474 H HD21 B ASN   A 1 54  ? 26.763 11.736  5.166   0.58 12.57 ?  54  ASN   A HD21 1 
ATOM   1475 H HD22 A ASN   A 1 54  ? 25.641 10.926  4.443   0.42 14.41 ?  54  ASN   A HD22 1 
ATOM   1476 H HD22 B ASN   A 1 54  ? 25.504 11.142  4.637   0.58 12.57 ?  54  ASN   A HD22 1 
ATOM   1477 N N    A LYS   A 1 55  ? 23.155 10.041  7.271   0.42 11.73 ?  55  LYS   A N    1 
ATOM   1478 N N    B LYS   A 1 55  ? 23.200 10.177  7.345   0.58 9.61  ?  55  LYS   A N    1 
ATOM   1479 C CA   A LYS   A 1 55  ? 22.564 11.208  7.928   0.42 12.50 ?  55  LYS   A CA   1 
ATOM   1480 C CA   B LYS   A 1 55  ? 22.626 11.337  8.021   0.58 11.18 ?  55  LYS   A CA   1 
ATOM   1481 C C    A LYS   A 1 55  ? 22.513 11.018  9.440   0.42 12.00 ?  55  LYS   A C    1 
ATOM   1482 C C    B LYS   A 1 55  ? 22.465 11.066  9.512   0.58 11.40 ?  55  LYS   A C    1 
ATOM   1483 O O    A LYS   A 1 55  ? 22.855 11.928  10.206  0.42 12.39 ?  55  LYS   A O    1 
ATOM   1484 O O    B LYS   A 1 55  ? 22.697 11.957  10.342  0.58 11.43 ?  55  LYS   A O    1 
ATOM   1485 C CB   A LYS   A 1 55  ? 21.159 11.443  7.367   0.42 12.45 ?  55  LYS   A CB   1 
ATOM   1486 C CB   B LYS   A 1 55  ? 21.294 11.704  7.362   0.58 11.78 ?  55  LYS   A CB   1 
ATOM   1487 C CG   A LYS   A 1 55  ? 20.374 12.577  8.014   0.42 13.41 ?  55  LYS   A CG   1 
ATOM   1488 C CG   B LYS   A 1 55  ? 20.601 12.942  7.925   0.58 14.33 ?  55  LYS   A CG   1 
ATOM   1489 C CD   A LYS   A 1 55  ? 19.052 12.789  7.285   0.42 15.29 ?  55  LYS   A CD   1 
ATOM   1490 C CD   B LYS   A 1 55  ? 19.252 13.154  7.237   0.58 16.50 ?  55  LYS   A CD   1 
ATOM   1491 C CE   A LYS   A 1 55  ? 18.318 14.024  7.777   0.42 17.50 ?  55  LYS   A CE   1 
ATOM   1492 C CE   B LYS   A 1 55  ? 18.359 14.146  7.976   0.58 19.24 ?  55  LYS   A CE   1 
ATOM   1493 N NZ   A LYS   A 1 55  ? 16.980 14.169  7.144   0.42 18.72 ?  55  LYS   A NZ   1 
ATOM   1494 N NZ   B LYS   A 1 55  ? 16.987 14.223  7.387   0.58 20.67 ?  55  LYS   A NZ   1 
ATOM   1495 H H    A LYS   A 1 55  ? 22.644 9.662   6.693   0.42 14.09 ?  55  LYS   A H    1 
ATOM   1496 H H    B LYS   A 1 55  ? 22.708 9.853   6.710   0.58 11.54 ?  55  LYS   A H    1 
ATOM   1497 H HA   A LYS   A 1 55  ? 23.101 11.987  7.735   0.42 15.02 ?  55  LYS   A HA   1 
ATOM   1498 H HA   B LYS   A 1 55  ? 23.230 12.086  7.914   0.58 13.43 ?  55  LYS   A HA   1 
ATOM   1499 H HB2  A LYS   A 1 55  ? 21.233 11.640  6.421   0.42 14.96 ?  55  LYS   A HB2  1 
ATOM   1500 H HB2  B LYS   A 1 55  ? 21.454 11.869  6.418   0.58 14.16 ?  55  LYS   A HB2  1 
ATOM   1501 H HB3  A LYS   A 1 55  ? 20.639 10.626  7.484   0.42 14.96 ?  55  LYS   A HB3  1 
ATOM   1502 H HB3  B LYS   A 1 55  ? 20.684 10.961  7.463   0.58 14.16 ?  55  LYS   A HB3  1 
ATOM   1503 H HG2  A LYS   A 1 55  ? 20.180 12.354  8.939   0.42 16.11 ?  55  LYS   A HG2  1 
ATOM   1504 H HG2  B LYS   A 1 55  ? 20.450 12.822  8.875   0.58 17.21 ?  55  LYS   A HG2  1 
ATOM   1505 H HG3  A LYS   A 1 55  ? 20.889 13.396  7.962   0.42 16.11 ?  55  LYS   A HG3  1 
ATOM   1506 H HG3  B LYS   A 1 55  ? 21.159 13.722  7.766   0.58 17.21 ?  55  LYS   A HG3  1 
ATOM   1507 H HD2  A LYS   A 1 55  ? 19.229 12.894  6.336   0.42 18.36 ?  55  LYS   A HD2  1 
ATOM   1508 H HD2  B LYS   A 1 55  ? 19.411 13.494  6.342   0.58 19.82 ?  55  LYS   A HD2  1 
ATOM   1509 H HD3  A LYS   A 1 55  ? 18.483 12.016  7.433   0.42 18.36 ?  55  LYS   A HD3  1 
ATOM   1510 H HD3  B LYS   A 1 55  ? 18.791 12.302  7.191   0.58 19.82 ?  55  LYS   A HD3  1 
ATOM   1511 H HE2  A LYS   A 1 55  ? 18.199 13.960  8.737   0.42 21.01 ?  55  LYS   A HE2  1 
ATOM   1512 H HE2  B LYS   A 1 55  ? 18.277 13.866  8.901   0.58 23.10 ?  55  LYS   A HE2  1 
ATOM   1513 H HE3  A LYS   A 1 55  ? 18.847 14.811  7.560   0.42 21.01 ?  55  LYS   A HE3  1 
ATOM   1514 H HE3  B LYS   A 1 55  ? 18.761 15.027  7.929   0.58 23.10 ?  55  LYS   A HE3  1 
ATOM   1515 H HZ1  A LYS   A 1 55  ? 16.395 14.468  7.744   0.42 22.48 ?  55  LYS   A HZ1  1 
ATOM   1516 H HZ1  B LYS   A 1 55  ? 16.456 14.707  7.913   0.58 24.82 ?  55  LYS   A HZ1  1 
ATOM   1517 H HZ2  A LYS   A 1 55  ? 17.023 14.750  6.470   0.42 22.48 ?  55  LYS   A HZ2  1 
ATOM   1518 H HZ2  B LYS   A 1 55  ? 17.020 14.606  6.583   0.58 24.82 ?  55  LYS   A HZ2  1 
ATOM   1519 H HZ3  A LYS   A 1 55  ? 16.702 13.383  6.835   0.42 22.48 ?  55  LYS   A HZ3  1 
ATOM   1520 H HZ3  B LYS   A 1 55  ? 16.642 13.406  7.303   0.58 24.82 ?  55  LYS   A HZ3  1 
ATOM   1521 N N    . ALA   A 1 56  ? 22.089 9.835   9.879   1.00 12.11 ?  56  ALA   A N    1 
ATOM   1522 C CA   . ALA   A 1 56  ? 21.947 9.524   11.294  1.00 12.67 ?  56  ALA   A CA   1 
ATOM   1523 C C    . ALA   A 1 56  ? 23.281 9.545   12.030  1.00 11.96 ?  56  ALA   A C    1 
ATOM   1524 O O    . ALA   A 1 56  ? 23.293 9.731   13.248  1.00 13.39 ?  56  ALA   A O    1 
ATOM   1525 C CB   . ALA   A 1 56  ? 21.233 8.180   11.469  1.00 13.58 ?  56  ALA   A CB   1 
ATOM   1526 H H    A ALA   A 1 56  ? 21.877 9.184   9.363   0.42 14.54 ?  56  ALA   A H    1 
ATOM   1527 H H    B ALA   A 1 56  ? 21.913 9.189   9.344   0.58 14.54 ?  56  ALA   A H    1 
ATOM   1528 H HA   . ALA   A 1 56  ? 21.397 10.199  11.707  1.00 15.23 ?  56  ALA   A HA   1 
ATOM   1529 H HB1  . ALA   A 1 56  ? 21.157 7.983   12.420  1.00 16.31 ?  56  ALA   A HB1  1 
ATOM   1530 H HB2  . ALA   A 1 56  ? 20.348 8.245   11.078  1.00 16.31 ?  56  ALA   A HB2  1 
ATOM   1531 H HB3  . ALA   A 1 56  ? 21.742 7.485   11.029  1.00 16.31 ?  56  ALA   A HB3  1 
ATOM   1532 N N    . THR   A 1 57  ? 24.399 9.356   11.327  1.00 11.62 ?  57  THR   A N    1 
ATOM   1533 C CA   . THR   A 1 57  ? 25.729 9.483   11.923  1.00 11.77 ?  57  THR   A CA   1 
ATOM   1534 C C    . THR   A 1 57  ? 26.287 10.898  11.845  1.00 11.91 ?  57  THR   A C    1 
ATOM   1535 O O    . THR   A 1 57  ? 27.476 11.101  12.138  1.00 12.56 ?  57  THR   A O    1 
ATOM   1536 C CB   . THR   A 1 57  ? 26.741 8.528   11.263  1.00 11.33 ?  57  THR   A CB   1 
ATOM   1537 O OG1  . THR   A 1 57  ? 27.148 9.029   9.974   1.00 10.99 ?  57  THR   A OG1  1 
ATOM   1538 C CG2  . THR   A 1 57  ? 26.223 7.106   11.162  1.00 11.44 ?  57  THR   A CG2  1 
ATOM   1539 H H    . THR   A 1 57  ? 24.415 9.123   10.491  1.00 13.96 ?  57  THR   A H    1 
ATOM   1540 H HA   . THR   A 1 57  ? 25.674 9.233   12.859  1.00 14.14 ?  57  THR   A HA   1 
ATOM   1541 H HB   . THR   A 1 57  ? 27.540 8.494   11.830  1.00 13.61 ?  57  THR   A HB   1 
ATOM   1542 H HG1  . THR   A 1 57  ? 26.479 9.094   9.473   1.00 13.21 ?  57  THR   A HG1  1 
ATOM   1543 H HG21 . THR   A 1 57  ? 26.900 6.527   10.770  1.00 13.74 ?  57  THR   A HG21 1 
ATOM   1544 H HG22 . THR   A 1 57  ? 26.002 6.769   12.046  1.00 13.74 ?  57  THR   A HG22 1 
ATOM   1545 H HG23 . THR   A 1 57  ? 25.432 7.080   10.609  1.00 13.74 ?  57  THR   A HG23 1 
ATOM   1546 N N    A ASN   A 1 58  ? 25.479 11.872  11.428  0.42 12.59 ?  58  ASN   A N    1 
ATOM   1547 N N    B ASN   A 1 58  ? 25.478 11.873  11.430  0.58 12.58 ?  58  ASN   A N    1 
ATOM   1548 C CA   A ASN   A 1 58  ? 25.950 13.249  11.326  0.42 13.57 ?  58  ASN   A CA   1 
ATOM   1549 C CA   B ASN   A 1 58  ? 25.934 13.255  11.337  0.58 13.70 ?  58  ASN   A CA   1 
ATOM   1550 C C    A ASN   A 1 58  ? 27.141 13.342  10.369  0.42 12.19 ?  58  ASN   A C    1 
ATOM   1551 C C    B ASN   A 1 58  ? 27.078 13.402  10.327  0.58 12.31 ?  58  ASN   A C    1 
ATOM   1552 O O    A ASN   A 1 58  ? 28.090 14.097  10.592  0.42 12.68 ?  58  ASN   A O    1 
ATOM   1553 O O    B ASN   A 1 58  ? 27.924 14.291  10.455  0.58 12.94 ?  58  ASN   A O    1 
ATOM   1554 C CB   A ASN   A 1 58  ? 26.283 13.799  12.718  0.42 15.90 ?  58  ASN   A CB   1 
ATOM   1555 C CB   B ASN   A 1 58  ? 26.311 13.787  12.729  0.58 16.42 ?  58  ASN   A CB   1 
ATOM   1556 C CG   A ASN   A 1 58  ? 26.702 15.256  12.705  0.42 19.38 ?  58  ASN   A CG   1 
ATOM   1557 C CG   B ASN   A 1 58  ? 26.608 15.268  12.744  0.58 21.03 ?  58  ASN   A CG   1 
ATOM   1558 O OD1  A ASN   A 1 58  ? 26.105 16.083  12.023  0.42 20.78 ?  58  ASN   A OD1  1 
ATOM   1559 O OD1  B ASN   A 1 58  ? 25.957 16.054  12.059  0.58 22.46 ?  58  ASN   A OD1  1 
ATOM   1560 N ND2  A ASN   A 1 58  ? 27.735 15.577  13.472  0.42 20.60 ?  58  ASN   A ND2  1 
ATOM   1561 N ND2  B ASN   A 1 58  ? 27.595 15.661  13.548  0.58 23.05 ?  58  ASN   A ND2  1 
ATOM   1562 H H    A ASN   A 1 58  ? 24.658 11.754  11.187  0.42 15.12 ?  58  ASN   A H    1 
ATOM   1563 H H    B ASN   A 1 58  ? 24.660 11.753  11.189  0.58 15.11 ?  58  ASN   A H    1 
ATOM   1564 H HA   A ASN   A 1 58  ? 25.233 13.787  10.959  0.42 16.30 ?  58  ASN   A HA   1 
ATOM   1565 H HA   B ASN   A 1 58  ? 25.198 13.789  11.012  0.58 16.45 ?  58  ASN   A HA   1 
ATOM   1566 H HB2  A ASN   A 1 58  ? 25.492 13.710  13.284  0.42 19.10 ?  58  ASN   A HB2  1 
ATOM   1567 H HB2  B ASN   A 1 58  ? 25.567 13.626  13.337  0.58 19.73 ?  58  ASN   A HB2  1 
ATOM   1568 H HB3  A ASN   A 1 58  ? 27.011 13.288  13.096  0.42 19.10 ?  58  ASN   A HB3  1 
ATOM   1569 H HB3  B ASN   A 1 58  ? 27.098 13.325  13.047  0.58 19.73 ?  58  ASN   A HB3  1 
ATOM   1570 H HD21 A ASN   A 1 58  ? 27.998 16.396  13.508  0.42 24.73 ?  58  ASN   A HD21 1 
ATOM   1571 H HD21 B ASN   A 1 58  ? 27.808 16.494  13.595  0.58 27.68 ?  58  ASN   A HD21 1 
ATOM   1572 H HD22 A ASN   A 1 58  ? 28.125 14.973  13.932  0.42 24.73 ?  58  ASN   A HD22 1 
ATOM   1573 H HD22 B ASN   A 1 58  ? 28.024 15.082  14.016  0.58 27.68 ?  58  ASN   A HD22 1 
ATOM   1574 N N    . ASN   A 1 59  ? 27.096 12.553  9.293   1.00 11.39 ?  59  ASN   A N    1 
ATOM   1575 C CA   . ASN   A 1 59  ? 28.093 12.517  8.213   1.00 10.85 ?  59  ASN   A CA   1 
ATOM   1576 C C    . ASN   A 1 59  ? 29.402 11.844  8.627   1.00 10.61 ?  59  ASN   A C    1 
ATOM   1577 O O    . ASN   A 1 59  ? 30.322 11.785  7.805   1.00 10.94 ?  59  ASN   A O    1 
ATOM   1578 C CB   . ASN   A 1 59  ? 28.392 13.900  7.597   1.00 11.62 ?  59  ASN   A CB   1 
ATOM   1579 C CG   . ASN   A 1 59  ? 28.766 13.815  6.129   1.00 11.45 ?  59  ASN   A CG   1 
ATOM   1580 O OD1  . ASN   A 1 59  ? 28.063 13.199  5.327   1.00 12.19 ?  59  ASN   A OD1  1 
ATOM   1581 N ND2  . ASN   A 1 59  ? 29.852 14.480  5.752   1.00 12.46 ?  59  ASN   A ND2  1 
ATOM   1582 H H    A ASN   A 1 59  ? 26.456 11.992  9.154   0.42 13.69 ?  59  ASN   A H    1 
ATOM   1583 H H    B ASN   A 1 59  ? 26.492 11.948  9.183   0.58 13.69 ?  59  ASN   A H    1 
ATOM   1584 H HA   . ASN   A 1 59  ? 27.725 11.984  7.499   1.00 13.03 ?  59  ASN   A HA   1 
ATOM   1585 H HB2  . ASN   A 1 59  ? 27.610 14.467  7.667   1.00 13.97 ?  59  ASN   A HB2  1 
ATOM   1586 H HB3  . ASN   A 1 59  ? 29.142 14.309  8.059   1.00 13.97 ?  59  ASN   A HB3  1 
ATOM   1587 H HD21 . ASN   A 1 59  ? 30.099 14.472  4.923   1.00 14.97 ?  59  ASN   A HD21 1 
ATOM   1588 H HD22 . ASN   A 1 59  ? 30.319 14.915  6.328   1.00 14.97 ?  59  ASN   A HD22 1 
ATOM   1589 N N    . ALA   A 1 60  ? 29.512 11.294  9.836   1.00 11.20 ?  60  ALA   A N    1 
ATOM   1590 C CA   . ALA   A 1 60  ? 30.747 10.604  10.201  1.00 11.32 ?  60  ALA   A CA   1 
ATOM   1591 C C    . ALA   A 1 60  ? 30.975 9.363   9.345   1.00 11.36 ?  60  ALA   A C    1 
ATOM   1592 O O    . ALA   A 1 60  ? 32.124 9.036   9.034   1.00 11.55 ?  60  ALA   A O    1 
ATOM   1593 C CB   . ALA   A 1 60  ? 30.729 10.242  11.682  1.00 12.23 ?  60  ALA   A CB   1 
ATOM   1594 H H    . ALA   A 1 60  ? 28.906 11.314  10.451  1.00 13.46 ?  60  ALA   A H    1 
ATOM   1595 H HA   . ALA   A 1 60  ? 31.493 11.215  10.058  1.00 13.60 ?  60  ALA   A HA   1 
ATOM   1596 H HB1  . ALA   A 1 60  ? 31.557 9.793   11.905  1.00 14.69 ?  60  ALA   A HB1  1 
ATOM   1597 H HB2  . ALA   A 1 60  ? 30.646 11.060  12.208  1.00 14.69 ?  60  ALA   A HB2  1 
ATOM   1598 H HB3  . ALA   A 1 60  ? 29.974 9.664   11.855  1.00 14.69 ?  60  ALA   A HB3  1 
ATOM   1599 N N    . MET   A 1 61  ? 29.906 8.672   8.942   1.00 10.62 ?  61  MET   A N    1 
ATOM   1600 C CA   . MET   A 1 61  ? 30.054 7.526   8.049   1.00 10.60 ?  61  MET   A CA   1 
ATOM   1601 C C    . MET   A 1 61  ? 30.702 7.944   6.729   1.00 10.82 ?  61  MET   A C    1 
ATOM   1602 O O    . MET   A 1 61  ? 31.598 7.258   6.219   1.00 11.31 ?  61  MET   A O    1 
ATOM   1603 C CB   . MET   A 1 61  ? 28.689 6.871   7.821   1.00 10.99 ?  61  MET   A CB   1 
ATOM   1604 C CG   . MET   A 1 61  ? 28.698 5.700   6.845   1.00 11.17 ?  61  MET   A CG   1 
ATOM   1605 S SD   . MET   A 1 61  ? 27.080 4.954   6.630   1.00 12.15 ?  61  MET   A SD   1 
ATOM   1606 C CE   . MET   A 1 61  ? 26.957 4.054   8.178   1.00 13.58 ?  61  MET   A CE   1 
ATOM   1607 H H    . MET   A 1 61  ? 29.094 8.853   9.164   1.00 12.76 ?  61  MET   A H    1 
ATOM   1608 H HA   . MET   A 1 61  ? 30.625 6.871   8.482   1.00 12.74 ?  61  MET   A HA   1 
ATOM   1609 H HB2  . MET   A 1 61  ? 28.357 6.546   8.670   1.00 13.21 ?  61  MET   A HB2  1 
ATOM   1610 H HB3  . MET   A 1 61  ? 28.081 7.541   7.468   1.00 13.21 ?  61  MET   A HB3  1 
ATOM   1611 H HG2  . MET   A 1 61  ? 28.994 6.003   5.973   1.00 13.42 ?  61  MET   A HG2  1 
ATOM   1612 H HG3  . MET   A 1 61  ? 29.297 5.011   7.176   1.00 13.42 ?  61  MET   A HG3  1 
ATOM   1613 H HE1  . MET   A 1 61  ? 26.116 3.570   8.197   1.00 16.31 ?  61  MET   A HE1  1 
ATOM   1614 H HE2  . MET   A 1 61  ? 27.698 3.438   8.248   1.00 16.31 ?  61  MET   A HE2  1 
ATOM   1615 H HE3  . MET   A 1 61  ? 26.985 4.690   8.915   1.00 16.31 ?  61  MET   A HE3  1 
ATOM   1616 N N    . GLN   A 1 62  ? 30.264 9.072   6.158   1.00 11.10 ?  62  GLN   A N    1 
ATOM   1617 C CA   . GLN   A 1 62  ? 30.845 9.534   4.902   1.00 10.66 ?  62  GLN   A CA   1 
ATOM   1618 C C    . GLN   A 1 62  ? 32.313 9.909   5.067   1.00 10.42 ?  62  GLN   A C    1 
ATOM   1619 O O    . GLN   A 1 62  ? 33.134 9.581   4.209   1.00 11.24 ?  62  GLN   A O    1 
ATOM   1620 C CB   . GLN   A 1 62  ? 30.059 10.720  4.349   1.00 10.79 ?  62  GLN   A CB   1 
ATOM   1621 C CG   . GLN   A 1 62  ? 30.473 11.086  2.931   1.00 11.40 ?  62  GLN   A CG   1 
ATOM   1622 C CD   . GLN   A 1 62  ? 30.142 9.957   1.975   1.00 11.33 ?  62  GLN   A CD   1 
ATOM   1623 O OE1  . GLN   A 1 62  ? 28.962 9.653   1.757   1.00 11.91 ?  62  GLN   A OE1  1 
ATOM   1624 N NE2  . GLN   A 1 62  ? 31.168 9.285   1.450   1.00 11.87 ?  62  GLN   A NE2  1 
ATOM   1625 H H    . GLN   A 1 62  ? 29.640 9.571   6.476   1.00 13.34 ?  62  GLN   A H    1 
ATOM   1626 H HA   . GLN   A 1 62  ? 30.799 8.813   4.259   1.00 12.81 ?  62  GLN   A HA   1 
ATOM   1627 H HB2  . GLN   A 1 62  ? 29.118 10.502  4.341   1.00 12.97 ?  62  GLN   A HB2  1 
ATOM   1628 H HB3  . GLN   A 1 62  ? 30.218 11.497  4.913   1.00 12.97 ?  62  GLN   A HB3  1 
ATOM   1629 H HG2  . GLN   A 1 62  ? 29.986 11.871  2.648   1.00 13.70 ?  62  GLN   A HG2  1 
ATOM   1630 H HG3  . GLN   A 1 62  ? 31.428 11.246  2.903   1.00 13.70 ?  62  GLN   A HG3  1 
ATOM   1631 H HE21 . GLN   A 1 62  ? 31.980 9.515   1.641   1.00 14.25 ?  62  GLN   A HE21 1 
ATOM   1632 H HE22 . GLN   A 1 62  ? 31.030 8.632   0.910   1.00 14.25 ?  62  GLN   A HE22 1 
ATOM   1633 N N    . VAL   A 1 63  ? 32.662 10.594  6.158   1.00 11.23 ?  63  VAL   A N    1 
ATOM   1634 C CA   . VAL   A 1 63  ? 34.057 10.975  6.396   1.00 12.04 ?  63  VAL   A CA   1 
ATOM   1635 C C    . VAL   A 1 63  ? 34.942 9.733   6.474   1.00 11.48 ?  63  VAL   A C    1 
ATOM   1636 O O    . VAL   A 1 63  ? 36.004 9.652   5.841   1.00 12.38 ?  63  VAL   A O    1 
ATOM   1637 C CB   . VAL   A 1 63  ? 34.140 11.842  7.665   1.00 13.75 ?  63  VAL   A CB   1 
ATOM   1638 C CG1  . VAL   A 1 63  ? 35.580 12.038  8.089   1.00 15.84 ?  63  VAL   A CG1  1 
ATOM   1639 C CG2  . VAL   A 1 63  ? 33.460 13.200  7.425   1.00 14.25 ?  63  VAL   A CG2  1 
ATOM   1640 H H    . VAL   A 1 63  ? 32.110 10.854  6.772   1.00 13.49 ?  63  VAL   A H    1 
ATOM   1641 H HA   . VAL   A 1 63  ? 34.360 11.516  5.653   1.00 14.47 ?  63  VAL   A HA   1 
ATOM   1642 H HB   . VAL   A 1 63  ? 33.673 11.400  8.391   1.00 16.52 ?  63  VAL   A HB   1 
ATOM   1643 H HG11 . VAL   A 1 63  ? 35.628 12.779  8.714   1.00 19.03 ?  63  VAL   A HG11 1 
ATOM   1644 H HG12 . VAL   A 1 63  ? 35.900 11.228  8.514   1.00 19.03 ?  63  VAL   A HG12 1 
ATOM   1645 H HG13 . VAL   A 1 63  ? 36.115 12.237  7.304   1.00 19.03 ?  63  VAL   A HG13 1 
ATOM   1646 H HG21 . VAL   A 1 63  ? 33.530 13.741  8.233   1.00 17.11 ?  63  VAL   A HG21 1 
ATOM   1647 H HG22 . VAL   A 1 63  ? 33.912 13.657  6.693   1.00 17.11 ?  63  VAL   A HG22 1 
ATOM   1648 H HG23 . VAL   A 1 63  ? 32.530 13.060  7.203   1.00 17.11 ?  63  VAL   A HG23 1 
ATOM   1649 N N    A GLU   A 1 64  ? 34.512 8.739   7.254   0.42 11.39 ?  64  GLU   A N    1 
ATOM   1650 N N    B GLU   A 1 64  ? 34.502 8.736   7.244   0.58 11.41 ?  64  GLU   A N    1 
ATOM   1651 C CA   A GLU   A 1 64  ? 35.271 7.497   7.345   0.42 11.76 ?  64  GLU   A CA   1 
ATOM   1652 C CA   B GLU   A 1 64  ? 35.251 7.491   7.359   0.58 11.86 ?  64  GLU   A CA   1 
ATOM   1653 C C    A GLU   A 1 64  ? 35.364 6.817   5.985   0.42 11.13 ?  64  GLU   A C    1 
ATOM   1654 C C    B GLU   A 1 64  ? 35.350 6.787   6.010   0.58 11.51 ?  64  GLU   A C    1 
ATOM   1655 O O    A GLU   A 1 64  ? 36.424 6.301   5.603   0.42 11.13 ?  64  GLU   A O    1 
ATOM   1656 O O    B GLU   A 1 64  ? 36.396 6.217   5.663   0.58 12.16 ?  64  GLU   A O    1 
ATOM   1657 C CB   A GLU   A 1 64  ? 34.602 6.569   8.359   0.42 12.29 ?  64  GLU   A CB   1 
ATOM   1658 C CB   B GLU   A 1 64  ? 34.541 6.601   8.378   0.58 12.29 ?  64  GLU   A CB   1 
ATOM   1659 C CG   A GLU   A 1 64  ? 35.266 5.211   8.450   0.42 12.96 ?  64  GLU   A CG   1 
ATOM   1660 C CG   B GLU   A 1 64  ? 35.200 5.256   8.592   0.58 12.90 ?  64  GLU   A CG   1 
ATOM   1661 C CD   A GLU   A 1 64  ? 34.413 4.203   9.164   0.42 12.81 ?  64  GLU   A CD   1 
ATOM   1662 C CD   B GLU   A 1 64  ? 34.297 4.262   9.300   0.58 13.60 ?  64  GLU   A CD   1 
ATOM   1663 O OE1  A GLU   A 1 64  ? 33.174 4.334   9.089   0.42 13.36 ?  64  GLU   A OE1  1 
ATOM   1664 O OE1  B GLU   A 1 64  ? 33.065 4.343   9.108   0.58 14.40 ?  64  GLU   A OE1  1 
ATOM   1665 O OE2  A GLU   A 1 64  ? 34.989 3.284   9.792   0.42 12.10 -1 64  GLU   A OE2  1 
ATOM   1666 O OE2  B GLU   A 1 64  ? 34.824 3.393   10.034  0.58 13.95 -1 64  GLU   A OE2  1 
ATOM   1667 H H    A GLU   A 1 64  ? 33.791 8.760   7.729   0.42 13.68 ?  64  GLU   A H    1 
ATOM   1668 H H    B GLU   A 1 64  ? 33.775 8.761   7.708   0.58 13.71 ?  64  GLU   A H    1 
ATOM   1669 H HA   A GLU   A 1 64  ? 36.167 7.691   7.659   0.42 14.13 ?  64  GLU   A HA   1 
ATOM   1670 H HA   B GLU   A 1 64  ? 36.147 7.685   7.681   0.58 14.24 ?  64  GLU   A HA   1 
ATOM   1671 H HB2  A GLU   A 1 64  ? 34.642 6.979   9.243   0.42 14.76 ?  64  GLU   A HB2  1 
ATOM   1672 H HB2  B GLU   A 1 64  ? 34.524 7.065   9.234   0.58 14.76 ?  64  GLU   A HB2  1 
ATOM   1673 H HB3  A GLU   A 1 64  ? 33.673 6.440   8.105   0.42 14.76 ?  64  GLU   A HB3  1 
ATOM   1674 H HB3  B GLU   A 1 64  ? 33.634 6.452   8.071   0.58 14.76 ?  64  GLU   A HB3  1 
ATOM   1675 H HG2  A GLU   A 1 64  ? 35.452 4.870   7.559   0.42 15.57 ?  64  GLU   A HG2  1 
ATOM   1676 H HG2  B GLU   A 1 64  ? 35.434 4.875   7.730   0.58 15.50 ?  64  GLU   A HG2  1 
ATOM   1677 H HG3  A GLU   A 1 64  ? 36.088 5.295   8.948   0.42 15.57 ?  64  GLU   A HG3  1 
ATOM   1678 H HG3  B GLU   A 1 64  ? 35.998 5.384   9.125   0.58 15.50 ?  64  GLU   A HG3  1 
ATOM   1679 N N    . SER   A 1 65  ? 34.253 6.803   5.244   1.00 10.91 ?  65  SER   A N    1 
ATOM   1680 C CA   . SER   A 1 65  ? 34.217 6.138   3.946   1.00 11.24 ?  65  SER   A CA   1 
ATOM   1681 C C    . SER   A 1 65  ? 35.156 6.798   2.943   1.00 11.19 ?  65  SER   A C    1 
ATOM   1682 O O    . SER   A 1 65  ? 35.807 6.105   2.151   1.00 12.27 ?  65  SER   A O    1 
ATOM   1683 C CB   . SER   A 1 65  ? 32.788 6.154   3.395   1.00 11.50 ?  65  SER   A CB   1 
ATOM   1684 O OG   . SER   A 1 65  ? 31.922 5.344   4.184   1.00 11.46 ?  65  SER   A OG   1 
ATOM   1685 H H    A SER   A 1 65  ? 33.510 7.177   5.472   0.42 13.11 ?  65  SER   A H    1 
ATOM   1686 H H    B SER   A 1 65  ? 33.513 7.187   5.464   0.58 13.11 ?  65  SER   A H    1 
ATOM   1687 H HA   . SER   A 1 65  ? 34.492 5.214   4.057   1.00 13.50 ?  65  SER   A HA   1 
ATOM   1688 H HB2  . SER   A 1 65  ? 32.462 7.063   3.399   1.00 13.81 ?  65  SER   A HB2  1 
ATOM   1689 H HB3  . SER   A 1 65  ? 32.803 5.806   2.491   1.00 13.81 ?  65  SER   A HB3  1 
ATOM   1690 H HG   . SER   A 1 65  ? 31.900 5.633   4.977   1.00 13.77 ?  65  SER   A HG   1 
ATOM   1691 N N    . ASP   A 1 66  ? 35.236 8.132   2.950   1.00 11.47 ?  66  ASP   A N    1 
ATOM   1692 C CA   . ASP   A 1 66  ? 36.119 8.814   2.015   1.00 12.49 ?  66  ASP   A CA   1 
ATOM   1693 C C    . ASP   A 1 66  ? 37.577 8.461   2.294   1.00 12.15 ?  66  ASP   A C    1 
ATOM   1694 O O    . ASP   A 1 66  ? 38.373 8.301   1.362   1.00 12.62 ?  66  ASP   A O    1 
ATOM   1695 C CB   . ASP   A 1 66  ? 35.893 10.322  2.081   1.00 14.46 ?  66  ASP   A CB   1 
ATOM   1696 C CG   . ASP   A 1 66  ? 34.569 10.772  1.430   1.00 16.88 ?  66  ASP   A CG   1 
ATOM   1697 O OD1  . ASP   A 1 66  ? 33.886 9.980   0.749   1.00 17.07 ?  66  ASP   A OD1  1 
ATOM   1698 O OD2  . ASP   A 1 66  ? 34.256 11.971  1.567   1.00 20.20 -1 66  ASP   A OD2  1 
ATOM   1699 H H    . ASP   A 1 66  ? 34.782 8.653   3.469   1.00 13.78 ?  66  ASP   A H    1 
ATOM   1700 H HA   . ASP   A 1 66  ? 35.910 8.516   1.115   1.00 15.01 ?  66  ASP   A HA   1 
ATOM   1701 H HB2  . ASP   A 1 66  ? 35.872 10.598  3.005   1.00 17.36 ?  66  ASP   A HB2  1 
ATOM   1702 H HB3  . ASP   A 1 66  ? 36.621 10.765  1.614   1.00 17.36 ?  66  ASP   A HB3  1 
ATOM   1703 N N    A ASP   A 1 67  ? 37.958 8.352   3.567   0.42 12.15 ?  67  ASP   A N    1 
ATOM   1704 N N    B ASP   A 1 67  ? 37.934 8.309   3.575   0.58 11.86 ?  67  ASP   A N    1 
ATOM   1705 C CA   A ASP   A 1 67  ? 39.308 7.881   3.867   0.42 12.96 ?  67  ASP   A CA   1 
ATOM   1706 C CA   B ASP   A 1 67  ? 39.287 7.883   3.933   0.58 12.48 ?  67  ASP   A CA   1 
ATOM   1707 C C    A ASP   A 1 67  ? 39.509 6.454   3.370   0.42 12.76 ?  67  ASP   A C    1 
ATOM   1708 C C    B ASP   A 1 67  ? 39.549 6.431   3.530   0.58 12.93 ?  67  ASP   A C    1 
ATOM   1709 O O    A ASP   A 1 67  ? 40.531 6.148   2.741   0.42 12.35 ?  67  ASP   A O    1 
ATOM   1710 O O    B ASP   A 1 67  ? 40.666 6.093   3.117   0.58 13.58 ?  67  ASP   A O    1 
ATOM   1711 C CB   A ASP   A 1 67  ? 39.594 7.989   5.364   0.42 13.69 ?  67  ASP   A CB   1 
ATOM   1712 C CB   B ASP   A 1 67  ? 39.531 8.122   5.428   0.58 12.66 ?  67  ASP   A CB   1 
ATOM   1713 C CG   A ASP   A 1 67  ? 40.906 7.338   5.757   0.42 14.04 ?  67  ASP   A CG   1 
ATOM   1714 C CG   B ASP   A 1 67  ? 40.801 7.468   5.925   0.58 12.79 ?  67  ASP   A CG   1 
ATOM   1715 O OD1  A ASP   A 1 67  ? 41.978 7.852   5.342   0.42 14.84 ?  67  ASP   A OD1  1 
ATOM   1716 O OD1  B ASP   A 1 67  ? 40.761 6.243   6.192   0.58 14.34 ?  67  ASP   A OD1  1 
ATOM   1717 O OD2  A ASP   A 1 67  ? 40.854 6.317   6.484   0.42 14.14 -1 67  ASP   A OD2  1 
ATOM   1718 O OD2  B ASP   A 1 67  ? 41.833 8.179   6.023   0.58 12.76 -1 67  ASP   A OD2  1 
ATOM   1719 H H    A ASP   A 1 67  ? 37.475 8.549   4.251   0.42 14.59 ?  67  ASP   A H    1 
ATOM   1720 H H    B ASP   A 1 67  ? 37.412 8.444   4.247   0.58 14.25 ?  67  ASP   A H    1 
ATOM   1721 H HA   A ASP   A 1 67  ? 39.942 8.452   3.399   0.42 15.56 ?  67  ASP   A HA   1 
ATOM   1722 H HA   B ASP   A 1 67  ? 39.918 8.438   3.450   0.58 15.00 ?  67  ASP   A HA   1 
ATOM   1723 H HB2  A ASP   A 1 67  ? 39.640 8.926   5.607   0.42 16.45 ?  67  ASP   A HB2  1 
ATOM   1724 H HB2  B ASP   A 1 67  ? 39.609 9.079   5.589   0.58 15.21 ?  67  ASP   A HB2  1 
ATOM   1725 H HB3  A ASP   A 1 67  ? 38.890 7.546   5.851   0.42 16.45 ?  67  ASP   A HB3  1 
ATOM   1726 H HB3  B ASP   A 1 67  ? 38.792 7.761   5.938   0.58 15.21 ?  67  ASP   A HB3  1 
ATOM   1727 N N    . TYR   A 1 68  ? 38.526 5.575   3.607   1.00 13.07 ?  68  TYR   A N    1 
ATOM   1728 C CA   . TYR   A 1 68  ? 38.649 4.195   3.142   1.00 12.85 ?  68  TYR   A CA   1 
ATOM   1729 C C    . TYR   A 1 68  ? 38.910 4.143   1.636   1.00 12.81 ?  68  TYR   A C    1 
ATOM   1730 O O    . TYR   A 1 68  ? 39.797 3.411   1.173   1.00 13.45 ?  68  TYR   A O    1 
ATOM   1731 C CB   . TYR   A 1 68  ? 37.391 3.382   3.507   1.00 12.96 ?  68  TYR   A CB   1 
ATOM   1732 C CG   . TYR   A 1 68  ? 37.410 1.998   2.861   1.00 13.86 ?  68  TYR   A CG   1 
ATOM   1733 C CD1  . TYR   A 1 68  ? 36.965 1.822   1.555   1.00 14.29 ?  68  TYR   A CD1  1 
ATOM   1734 C CD2  . TYR   A 1 68  ? 37.935 0.900   3.522   1.00 15.53 ?  68  TYR   A CD2  1 
ATOM   1735 C CE1  . TYR   A 1 68  ? 37.034 0.616   0.923   1.00 15.54 ?  68  TYR   A CE1  1 
ATOM   1736 C CE2  . TYR   A 1 68  ? 37.990 -0.352  2.894   1.00 15.50 ?  68  TYR   A CE2  1 
ATOM   1737 C CZ   . TYR   A 1 68  ? 37.547 -0.469  1.593   1.00 15.48 ?  68  TYR   A CZ   1 
ATOM   1738 O OH   . TYR   A 1 68  ? 37.632 -1.684  0.949   1.00 17.24 ?  68  TYR   A OH   1 
ATOM   1739 H H    A TYR   A 1 68  ? 37.791 5.762   4.019   0.42 15.70 ?  68  TYR   A H    1 
ATOM   1740 H H    B TYR   A 1 68  ? 37.740 5.785   3.899   0.58 15.70 ?  68  TYR   A H    1 
ATOM   1741 H HA   . TYR   A 1 68  ? 39.401 3.791   3.586   1.00 15.43 ?  68  TYR   A HA   1 
ATOM   1742 H HB2  . TYR   A 1 68  ? 37.354 3.268   4.471   1.00 15.57 ?  68  TYR   A HB2  1 
ATOM   1743 H HB3  . TYR   A 1 68  ? 36.599 3.854   3.198   1.00 15.57 ?  68  TYR   A HB3  1 
ATOM   1744 H HD1  . TYR   A 1 68  ? 36.631 2.559   1.092   1.00 17.17 ?  68  TYR   A HD1  1 
ATOM   1745 H HD2  . TYR   A 1 68  ? 38.257 0.992   4.389   1.00 18.66 ?  68  TYR   A HD2  1 
ATOM   1746 H HE1  . TYR   A 1 68  ? 36.727 0.528   0.050   1.00 18.67 ?  68  TYR   A HE1  1 
ATOM   1747 H HE2  . TYR   A 1 68  ? 38.356 -1.088  3.329   1.00 18.62 ?  68  TYR   A HE2  1 
ATOM   1748 H HH   . TYR   A 1 68  ? 37.956 -2.261  1.464   1.00 20.70 ?  68  TYR   A HH   1 
ATOM   1749 N N    A ILE   A 1 69  ? 38.162 4.932   0.852   0.42 12.34 ?  69  ILE   A N    1 
ATOM   1750 N N    B ILE   A 1 69  ? 38.128 4.895   0.859   0.58 12.11 ?  69  ILE   A N    1 
ATOM   1751 C CA   A ILE   A 1 69  ? 38.243 4.849   -0.608  0.42 12.80 ?  69  ILE   A CA   1 
ATOM   1752 C CA   B ILE   A 1 69  ? 38.339 4.942   -0.584  0.58 12.64 ?  69  ILE   A CA   1 
ATOM   1753 C C    A ILE   A 1 69  ? 39.552 5.442   -1.118  0.42 12.97 ?  69  ILE   A C    1 
ATOM   1754 C C    B ILE   A 1 69  ? 39.721 5.506   -0.904  0.58 12.10 ?  69  ILE   A C    1 
ATOM   1755 O O    A ILE   A 1 69  ? 40.179 4.898   -2.038  0.42 13.28 ?  69  ILE   A O    1 
ATOM   1756 O O    B ILE   A 1 69  ? 40.399 5.045   -1.833  0.58 12.75 ?  69  ILE   A O    1 
ATOM   1757 C CB   A ILE   A 1 69  ? 37.022 5.528   -1.258  0.42 12.79 ?  69  ILE   A CB   1 
ATOM   1758 C CB   B ILE   A 1 69  ? 37.217 5.752   -1.261  0.58 12.48 ?  69  ILE   A CB   1 
ATOM   1759 C CG1  A ILE   A 1 69  ? 35.747 4.726   -0.995  0.42 12.53 ?  69  ILE   A CG1  1 
ATOM   1760 C CG1  B ILE   A 1 69  ? 35.845 5.087   -1.051  0.58 12.24 ?  69  ILE   A CG1  1 
ATOM   1761 C CG2  A ILE   A 1 69  ? 37.242 5.720   -2.759  0.42 14.35 ?  69  ILE   A CG2  1 
ATOM   1762 C CG2  B ILE   A 1 69  ? 37.535 5.974   -2.741  0.58 13.46 ?  69  ILE   A CG2  1 
ATOM   1763 C CD1  A ILE   A 1 69  ? 35.624 3.487   -1.848  0.42 12.90 ?  69  ILE   A CD1  1 
ATOM   1764 C CD1  B ILE   A 1 69  ? 35.664 3.773   -1.771  0.58 12.69 ?  69  ILE   A CD1  1 
ATOM   1765 H H    A ILE   A 1 69  ? 37.609 5.526   1.135   0.42 14.83 ?  69  ILE   A H    1 
ATOM   1766 H H    B ILE   A 1 69  ? 37.467 5.373   1.142   0.58 14.54 ?  69  ILE   A H    1 
ATOM   1767 H HA   A ILE   A 1 69  ? 38.235 3.919   -0.874  0.42 15.37 ?  69  ILE   A HA   1 
ATOM   1768 H HA   B ILE   A 1 69  ? 38.303 4.037   -0.925  0.58 15.19 ?  69  ILE   A HA   1 
ATOM   1769 H HB   A ILE   A 1 69  ? 36.912 6.405   -0.863  0.42 15.36 ?  69  ILE   A HB   1 
ATOM   1770 H HB   B ILE   A 1 69  ? 37.188 6.621   -0.835  0.58 14.99 ?  69  ILE   A HB   1 
ATOM   1771 H HG12 A ILE   A 1 69  ? 35.746 4.449   -0.065  0.42 15.05 ?  69  ILE   A HG12 1 
ATOM   1772 H HG12 B ILE   A 1 69  ? 35.721 4.924   -0.100  0.58 14.70 ?  69  ILE   A HG12 1 
ATOM   1773 H HG13 A ILE   A 1 69  ? 34.979 5.290   -1.172  0.42 15.05 ?  69  ILE   A HG13 1 
ATOM   1774 H HG13 B ILE   A 1 69  ? 35.158 5.695   -1.366  0.58 14.70 ?  69  ILE   A HG13 1 
ATOM   1775 H HG21 A ILE   A 1 69  ? 36.382 5.858   -3.190  0.42 17.24 ?  69  ILE   A HG21 1 
ATOM   1776 H HG21 B ILE   A 1 69  ? 36.728 6.274   -3.192  0.58 16.17 ?  69  ILE   A HG21 1 
ATOM   1777 H HG22 A ILE   A 1 69  ? 37.804 6.500   -2.902  0.42 17.24 ?  69  ILE   A HG22 1 
ATOM   1778 H HG22 B ILE   A 1 69  ? 38.226 6.648   -2.822  0.58 16.17 ?  69  ILE   A HG22 1 
ATOM   1779 H HG23 A ILE   A 1 69  ? 37.668 4.931   -3.123  0.42 17.24 ?  69  ILE   A HG23 1 
ATOM   1780 H HG23 B ILE   A 1 69  ? 37.835 5.138   -3.130  0.58 16.17 ?  69  ILE   A HG23 1 
ATOM   1781 H HD11 A ILE   A 1 69  ? 34.923 2.927   -1.482  0.42 15.50 ?  69  ILE   A HD11 1 
ATOM   1782 H HD11 B ILE   A 1 69  ? 34.772 3.434   -1.585  0.58 15.25 ?  69  ILE   A HD11 1 
ATOM   1783 H HD12 A ILE   A 1 69  ? 35.397 3.749   -2.754  0.42 15.50 ?  69  ILE   A HD12 1 
ATOM   1784 H HD12 B ILE   A 1 69  ? 35.767 3.915   -2.724  0.58 15.25 ?  69  ILE   A HD12 1 
ATOM   1785 H HD13 A ILE   A 1 69  ? 36.467 3.009   -1.841  0.42 15.50 ?  69  ILE   A HD13 1 
ATOM   1786 H HD13 B ILE   A 1 69  ? 36.327 3.141   -1.455  0.58 15.25 ?  69  ILE   A HD13 1 
ATOM   1787 N N    A ALA   A 1 70  ? 39.971 6.575   -0.554  0.42 12.95 ?  70  ALA   A N    1 
ATOM   1788 N N    B ALA   A 1 70  ? 40.164 6.510   -0.144  0.58 12.32 ?  70  ALA   A N    1 
ATOM   1789 C CA   A ALA   A 1 70  ? 41.243 7.171   -0.947  0.42 13.00 ?  70  ALA   A CA   1 
ATOM   1790 C CA   B ALA   A 1 70  ? 41.481 7.088   -0.400  0.58 12.25 ?  70  ALA   A CA   1 
ATOM   1791 C C    A ALA   A 1 70  ? 42.392 6.178   -0.807  0.42 12.87 ?  70  ALA   A C    1 
ATOM   1792 C C    B ALA   A 1 70  ? 42.598 6.076   -0.168  0.58 12.15 ?  70  ALA   A C    1 
ATOM   1793 O O    A ALA   A 1 70  ? 43.345 6.213   -1.592  0.42 13.53 ?  70  ALA   A O    1 
ATOM   1794 O O    B ALA   A 1 70  ? 43.619 6.113   -0.863  0.58 13.72 ?  70  ALA   A O    1 
ATOM   1795 C CB   A ALA   A 1 70  ? 41.505 8.424   -0.108  0.42 13.25 ?  70  ALA   A CB   1 
ATOM   1796 C CB   B ALA   A 1 70  ? 41.684 8.351   0.443   0.58 13.15 ?  70  ALA   A CB   1 
ATOM   1797 H H    A ALA   A 1 70  ? 39.539 7.014   0.047   0.42 15.56 ?  70  ALA   A H    1 
ATOM   1798 H H    B ALA   A 1 70  ? 39.733 6.875   0.506   0.58 14.81 ?  70  ALA   A H    1 
ATOM   1799 H HA   A ALA   A 1 70  ? 41.194 7.449   -1.877  0.42 15.61 ?  70  ALA   A HA   1 
ATOM   1800 H HA   B ALA   A 1 70  ? 41.531 7.352   -1.325  0.58 14.71 ?  70  ALA   A HA   1 
ATOM   1801 H HB1  A ALA   A 1 70  ? 42.356 8.810   -0.373  0.42 15.91 ?  70  ALA   A HB1  1 
ATOM   1802 H HB1  B ALA   A 1 70  ? 42.577 8.704   0.283   0.58 15.80 ?  70  ALA   A HB1  1 
ATOM   1803 H HB2  A ALA   A 1 70  ? 40.792 9.064   -0.259  0.42 15.91 ?  70  ALA   A HB2  1 
ATOM   1804 H HB2  B ALA   A 1 70  ? 41.022 9.014   0.181   0.58 15.80 ?  70  ALA   A HB2  1 
ATOM   1805 H HB3  A ALA   A 1 70  ? 41.534 8.174   0.829   0.42 15.91 ?  70  ALA   A HB3  1 
ATOM   1806 H HB3  B ALA   A 1 70  ? 41.581 8.135   1.381   0.58 15.80 ?  70  ALA   A HB3  1 
ATOM   1807 N N    A THR   A 1 71  ? 42.313 5.275   0.168   0.42 12.66 ?  71  THR   A N    1 
ATOM   1808 N N    B THR   A 1 71  ? 42.432 5.182   0.805   0.58 12.10 ?  71  THR   A N    1 
ATOM   1809 C CA   A THR   A 1 71  ? 43.371 4.294   0.389   0.42 13.29 ?  71  THR   A CA   1 
ATOM   1810 C CA   B THR   A 1 71  ? 43.446 4.178   1.119   0.58 13.57 ?  71  THR   A CA   1 
ATOM   1811 C C    A THR   A 1 71  ? 43.220 3.056   -0.490  0.42 12.75 ?  71  THR   A C    1 
ATOM   1812 C C    B THR   A 1 71  ? 43.351 2.961   0.205   0.58 13.69 ?  71  THR   A C    1 
ATOM   1813 O O    A THR   A 1 71  ? 44.216 2.556   -1.028  0.42 13.28 ?  71  THR   A O    1 
ATOM   1814 O O    B THR   A 1 71  ? 44.379 2.389   -0.179  0.58 14.41 ?  71  THR   A O    1 
ATOM   1815 C CB   A THR   A 1 71  ? 43.376 3.872   1.860   0.42 15.38 ?  71  THR   A CB   1 
ATOM   1816 C CB   B THR   A 1 71  ? 43.266 3.727   2.573   0.58 15.72 ?  71  THR   A CB   1 
ATOM   1817 O OG1  A THR   A 1 71  ? 43.677 5.005   2.680   0.42 15.78 ?  71  THR   A OG1  1 
ATOM   1818 O OG1  B THR   A 1 71  ? 43.392 4.852   3.449   0.58 17.07 ?  71  THR   A OG1  1 
ATOM   1819 C CG2  A THR   A 1 71  ? 44.410 2.786   2.110   0.42 16.07 ?  71  THR   A CG2  1 
ATOM   1820 C CG2  B THR   A 1 71  ? 44.289 2.671   2.959   0.58 16.67 ?  71  THR   A CG2  1 
ATOM   1821 H H    A THR   A 1 71  ? 41.646 5.203   0.710   0.42 15.21 ?  71  THR   A H    1 
ATOM   1822 H H    B THR   A 1 71  ? 41.739 5.138   1.307   0.58 14.54 ?  71  THR   A H    1 
ATOM   1823 H HA   A THR   A 1 71  ? 44.225 4.703   0.187   0.42 15.96 ?  71  THR   A HA   1 
ATOM   1824 H HA   B THR   A 1 71  ? 44.332 4.566   1.030   0.58 16.30 ?  71  THR   A HA   1 
ATOM   1825 H HB   A THR   A 1 71  ? 42.502 3.522   2.095   0.42 18.48 ?  71  THR   A HB   1 
ATOM   1826 H HB   B THR   A 1 71  ? 42.387 3.335   2.681   0.58 18.89 ?  71  THR   A HB   1 
ATOM   1827 H HG1  A THR   A 1 71  ? 43.668 4.785   3.490   0.42 18.95 ?  71  THR   A HG1  1 
ATOM   1828 H HG1  B THR   A 1 71  ? 43.357 4.598   4.254   0.58 20.50 ?  71  THR   A HG1  1 
ATOM   1829 H HG21 A THR   A 1 71  ? 44.594 2.721   3.061   0.42 19.30 ?  71  THR   A HG21 1 
ATOM   1830 H HG21 B THR   A 1 71  ? 44.302 2.558   3.925   0.58 20.02 ?  71  THR   A HG21 1 
ATOM   1831 H HG22 A THR   A 1 71  ? 44.082 1.931   1.795   0.42 19.30 ?  71  THR   A HG22 1 
ATOM   1832 H HG22 B THR   A 1 71  ? 44.070 1.822   2.549   0.58 20.02 ?  71  THR   A HG22 1 
ATOM   1833 H HG23 A THR   A 1 71  ? 45.236 3.001   1.647   0.42 19.30 ?  71  THR   A HG23 1 
ATOM   1834 H HG23 B THR   A 1 71  ? 45.175 2.944   2.669   0.58 20.02 ?  71  THR   A HG23 1 
ATOM   1835 N N    A ASN   A 1 72  ? 41.988 2.548   -0.643  0.42 12.92 ?  72  ASN   A N    1 
ATOM   1836 N N    B ASN   A 1 72  ? 42.130 2.533   -0.133  0.58 13.74 ?  72  ASN   A N    1 
ATOM   1837 C CA   A ASN   A 1 72  ? 41.748 1.221   -1.201  0.42 13.25 ?  72  ASN   A CA   1 
ATOM   1838 C CA   B ASN   A 1 72  ? 41.904 1.219   -0.721  0.58 14.71 ?  72  ASN   A CA   1 
ATOM   1839 C C    A ASN   A 1 72  ? 41.089 1.220   -2.573  0.42 13.65 ?  72  ASN   A C    1 
ATOM   1840 C C    B ASN   A 1 72  ? 41.321 1.229   -2.124  0.58 14.47 ?  72  ASN   A C    1 
ATOM   1841 O O    A ASN   A 1 72  ? 41.061 0.168   -3.224  0.42 13.86 ?  72  ASN   A O    1 
ATOM   1842 O O    B ASN   A 1 72  ? 41.313 0.175   -2.774  0.58 15.61 ?  72  ASN   A O    1 
ATOM   1843 C CB   A ASN   A 1 72  ? 40.873 0.405   -0.237  0.42 14.08 ?  72  ASN   A CB   1 
ATOM   1844 C CB   B ASN   A 1 72  ? 40.966 0.404   0.178   0.58 15.98 ?  72  ASN   A CB   1 
ATOM   1845 C CG   A ASN   A 1 72  ? 41.499 0.267   1.134   0.42 15.01 ?  72  ASN   A CG   1 
ATOM   1846 C CG   B ASN   A 1 72  ? 41.535 0.201   1.559   0.58 17.60 ?  72  ASN   A CG   1 
ATOM   1847 O OD1  A ASN   A 1 72  ? 41.024 0.851   2.107   0.42 16.40 ?  72  ASN   A OD1  1 
ATOM   1848 O OD1  B ASN   A 1 72  ? 41.082 0.796   2.533   0.58 19.16 ?  72  ASN   A OD1  1 
ATOM   1849 N ND2  A ASN   A 1 72  ? 42.576 -0.493  1.215   0.42 14.84 ?  72  ASN   A ND2  1 
ATOM   1850 N ND2  B ASN   A 1 72  ? 42.545 -0.629  1.648   0.58 18.68 ?  72  ASN   A ND2  1 
ATOM   1851 H H    A ASN   A 1 72  ? 41.266 2.965   -0.423  0.42 15.53 ?  72  ASN   A H    1 
ATOM   1852 H H    B ASN   A 1 72  ? 41.415 2.997   -0.022  0.58 16.51 ?  72  ASN   A H    1 
ATOM   1853 H HA   A ASN   A 1 72  ? 42.594 0.765   -1.287  0.42 15.92 ?  72  ASN   A HA   1 
ATOM   1854 H HA   B ASN   A 1 72  ? 42.754 0.755   -0.762  0.58 17.67 ?  72  ASN   A HA   1 
ATOM   1855 H HB2  A ASN   A 1 72  ? 40.014 0.844   -0.135  0.42 16.91 ?  72  ASN   A HB2  1 
ATOM   1856 H HB2  B ASN   A 1 72  ? 40.120 0.870   0.251   0.58 19.19 ?  72  ASN   A HB2  1 
ATOM   1857 H HB3  A ASN   A 1 72  ? 40.750 -0.486  -0.599  0.42 16.91 ?  72  ASN   A HB3  1 
ATOM   1858 H HB3  B ASN   A 1 72  ? 40.833 -0.468  -0.228  0.58 19.19 ?  72  ASN   A HB3  1 
ATOM   1859 H HD21 A ASN   A 1 72  ? 42.971 -0.604  1.972   0.42 17.82 ?  72  ASN   A HD21 1 
ATOM   1860 H HD21 B ASN   A 1 72  ? 42.907 -0.767  2.411   0.58 22.43 ?  72  ASN   A HD21 1 
ATOM   1861 H HD22 A ASN   A 1 72  ? 42.879 -0.886  0.513   0.42 17.82 ?  72  ASN   A HD22 1 
ATOM   1862 H HD22 B ASN   A 1 72  ? 42.840 -1.027  0.945   0.58 22.43 ?  72  ASN   A HD22 1 
ATOM   1863 N N    A GLY   A 1 73  ? 40.544 2.344   -3.023  0.42 13.20 ?  73  GLY   A N    1 
ATOM   1864 N N    B GLY   A 1 73  ? 40.812 2.359   -2.601  0.58 13.65 ?  73  GLY   A N    1 
ATOM   1865 C CA   A GLY   A 1 73  ? 39.813 2.381   -4.265  0.42 12.87 ?  73  GLY   A CA   1 
ATOM   1866 C CA   B GLY   A 1 73  ? 40.081 2.384   -3.844  0.58 13.69 ?  73  GLY   A CA   1 
ATOM   1867 C C    A GLY   A 1 73  ? 38.427 1.788   -4.127  0.42 12.35 ?  73  GLY   A C    1 
ATOM   1868 C C    B GLY   A 1 73  ? 38.680 1.809   -3.687  0.58 13.33 ?  73  GLY   A C    1 
ATOM   1869 O O    A GLY   A 1 73  ? 38.039 1.284   -3.067  0.42 12.27 ?  73  GLY   A O    1 
ATOM   1870 O O    B GLY   A 1 73  ? 38.262 1.407   -2.595  0.58 13.14 ?  73  GLY   A O    1 
ATOM   1871 H H    A GLY   A 1 73  ? 40.583 3.107   -2.620  0.42 15.86 ?  73  GLY   A H    1 
ATOM   1872 H H    B GLY   A 1 73  ? 40.884 3.136   -2.218  0.58 16.39 ?  73  GLY   A H    1 
ATOM   1873 H HA2  A GLY   A 1 73  ? 39.715 3.303   -4.556  0.42 15.46 ?  73  GLY   A HA2  1 
ATOM   1874 H HA2  B GLY   A 1 73  ? 40.016 3.306   -4.162  0.58 16.44 ?  73  GLY   A HA2  1 
ATOM   1875 H HA3  A GLY   A 1 73  ? 40.294 1.891   -4.946  0.42 15.46 ?  73  GLY   A HA3  1 
ATOM   1876 H HA3  B GLY   A 1 73  ? 40.558 1.868   -4.509  0.58 16.44 ?  73  GLY   A HA3  1 
ATOM   1877 N N    A PRO   A 1 74  ? 37.652 1.841   -5.208  0.42 12.44 ?  74  PRO   A N    1 
ATOM   1878 N N    B PRO   A 1 74  ? 37.933 1.757   -4.785  0.58 12.70 ?  74  PRO   A N    1 
ATOM   1879 C CA   A PRO   A 1 74  ? 36.254 1.402   -5.139  0.42 13.03 ?  74  PRO   A CA   1 
ATOM   1880 C CA   B PRO   A 1 74  ? 36.517 1.370   -4.706  0.58 12.93 ?  74  PRO   A CA   1 
ATOM   1881 C C    A PRO   A 1 74  ? 36.131 -0.076  -4.802  0.42 12.39 ?  74  PRO   A C    1 
ATOM   1882 C C    B PRO   A 1 74  ? 36.314 -0.118  -4.442  0.58 12.43 ?  74  PRO   A C    1 
ATOM   1883 O O    A PRO   A 1 74  ? 36.971 -0.902  -5.180  0.42 12.02 ?  74  PRO   A O    1 
ATOM   1884 O O    B PRO   A 1 74  ? 37.197 -0.960  -4.646  0.58 12.37 ?  74  PRO   A O    1 
ATOM   1885 C CB   A PRO   A 1 74  ? 35.722 1.693   -6.550  0.42 14.06 ?  74  PRO   A CB   1 
ATOM   1886 C CB   B PRO   A 1 74  ? 35.974 1.728   -6.094  0.58 14.50 ?  74  PRO   A CB   1 
ATOM   1887 C CG   A PRO   A 1 74  ? 36.638 2.746   -7.100  0.42 15.23 ?  74  PRO   A CG   1 
ATOM   1888 C CG   B PRO   A 1 74  ? 37.028 2.557   -6.752  0.58 16.94 ?  74  PRO   A CG   1 
ATOM   1889 C CD   A PRO   A 1 74  ? 37.986 2.407   -6.523  0.42 13.78 ?  74  PRO   A CD   1 
ATOM   1890 C CD   B PRO   A 1 74  ? 38.322 2.176   -6.142  0.58 14.29 ?  74  PRO   A CD   1 
ATOM   1891 H HA   A PRO   A 1 74  ? 35.754 1.925   -4.488  0.42 15.66 ?  74  PRO   A HA   1 
ATOM   1892 H HA   B PRO   A 1 74  ? 36.056 1.907   -4.025  0.58 15.53 ?  74  PRO   A HA   1 
ATOM   1893 H HB2  A PRO   A 1 74  ? 35.758 0.887   -7.089  0.42 16.89 ?  74  PRO   A HB2  1 
ATOM   1894 H HB2  B PRO   A 1 74  ? 35.819 0.908   -6.589  0.58 17.42 ?  74  PRO   A HB2  1 
ATOM   1895 H HB3  A PRO   A 1 74  ? 34.810 2.029   -6.499  0.42 16.89 ?  74  PRO   A HB3  1 
ATOM   1896 H HB3  B PRO   A 1 74  ? 35.146 2.228   -5.999  0.58 17.42 ?  74  PRO   A HB3  1 
ATOM   1897 H HG2  A PRO   A 1 74  ? 36.666 2.694   -8.066  0.42 18.29 ?  74  PRO   A HG2  1 
ATOM   1898 H HG2  B PRO   A 1 74  ? 37.031 2.372   -7.703  0.58 20.34 ?  74  PRO   A HG2  1 
ATOM   1899 H HG3  A PRO   A 1 74  ? 36.355 3.622   -6.804  0.42 18.29 ?  74  PRO   A HG3  1 
ATOM   1900 H HG3  B PRO   A 1 74  ? 36.840 3.496   -6.592  0.58 20.34 ?  74  PRO   A HG3  1 
ATOM   1901 H HD2  A PRO   A 1 74  ? 38.438 1.739   -7.063  0.42 16.56 ?  74  PRO   A HD2  1 
ATOM   1902 H HD2  B PRO   A 1 74  ? 38.718 1.433   -6.623  0.58 17.16 ?  74  PRO   A HD2  1 
ATOM   1903 H HD3  A PRO   A 1 74  ? 38.523 3.207   -6.422  0.42 16.56 ?  74  PRO   A HD3  1 
ATOM   1904 H HD3  B PRO   A 1 74  ? 38.916 2.944   -6.121  0.58 17.16 ?  74  PRO   A HD3  1 
ATOM   1905 N N    A LEU   A 1 75  ? 35.064 -0.404  -4.075  0.42 12.35 ?  75  LEU   A N    1 
ATOM   1906 N N    B LEU   A 1 75  ? 35.092 -0.435  -4.018  0.58 12.38 ?  75  LEU   A N    1 
ATOM   1907 C CA   A LEU   A 1 75  ? 34.689 -1.795  -3.920  0.42 11.93 ?  75  LEU   A CA   1 
ATOM   1908 C CA   B LEU   A 1 75  ? 34.668 -1.815  -3.889  0.58 12.20 ?  75  LEU   A CA   1 
ATOM   1909 C C    A LEU   A 1 75  ? 34.382 -2.390  -5.290  0.42 11.62 ?  75  LEU   A C    1 
ATOM   1910 C C    B LEU   A 1 75  ? 34.260 -2.378  -5.245  0.58 12.22 ?  75  LEU   A C    1 
ATOM   1911 O O    A LEU   A 1 75  ? 34.342 -1.696  -6.308  0.42 12.12 ?  75  LEU   A O    1 
ATOM   1912 O O    B LEU   A 1 75  ? 33.989 -1.647  -6.199  0.58 13.19 ?  75  LEU   A O    1 
ATOM   1913 C CB   A LEU   A 1 75  ? 33.465 -1.931  -3.009  0.42 12.26 ?  75  LEU   A CB   1 
ATOM   1914 C CB   B LEU   A 1 75  ? 33.469 -1.926  -2.950  0.58 12.58 ?  75  LEU   A CB   1 
ATOM   1915 C CG   A LEU   A 1 75  ? 33.612 -1.406  -1.580  0.42 13.35 ?  75  LEU   A CG   1 
ATOM   1916 C CG   B LEU   A 1 75  ? 33.667 -1.561  -1.484  0.58 13.98 ?  75  LEU   A CG   1 
ATOM   1917 C CD1  A LEU   A 1 75  ? 32.278 -1.437  -0.833  0.42 13.10 ?  75  LEU   A CD1  1 
ATOM   1918 C CD1  B LEU   A 1 75  ? 32.407 -1.896  -0.717  0.58 14.28 ?  75  LEU   A CD1  1 
ATOM   1919 C CD2  A LEU   A 1 75  ? 34.663 -2.163  -0.808  0.42 14.81 ?  75  LEU   A CD2  1 
ATOM   1920 C CD2  B LEU   A 1 75  ? 34.842 -2.270  -0.880  0.58 17.75 ?  75  LEU   A CD2  1 
ATOM   1921 H H    A LEU   A 1 75  ? 34.544 0.154   -3.669  0.42 14.84 ?  75  LEU   A H    1 
ATOM   1922 H H    B LEU   A 1 75  ? 34.485 0.141   -3.805  0.58 14.88 ?  75  LEU   A H    1 
ATOM   1923 H HA   A LEU   A 1 75  ? 35.421 -2.287  -3.527  0.42 14.33 ?  75  LEU   A HA   1 
ATOM   1924 H HA   B LEU   A 1 75  ? 35.397 -2.349  -3.536  0.58 14.66 ?  75  LEU   A HA   1 
ATOM   1925 H HB2  A LEU   A 1 75  ? 32.723 -1.460  -3.417  0.42 14.73 ?  75  LEU   A HB2  1 
ATOM   1926 H HB2  B LEU   A 1 75  ? 32.765 -1.358  -3.295  0.58 15.11 ?  75  LEU   A HB2  1 
ATOM   1927 H HB3  A LEU   A 1 75  ? 33.241 -2.878  -2.944  0.42 14.73 ?  75  LEU   A HB3  1 
ATOM   1928 H HB3  B LEU   A 1 75  ? 33.163 -2.852  -2.970  0.58 15.11 ?  75  LEU   A HB3  1 
ATOM   1929 H HG   A LEU   A 1 75  ? 33.893 -0.481  -1.624  0.42 16.04 ?  75  LEU   A HG   1 
ATOM   1930 H HG   B LEU   A 1 75  ? 33.822 -0.604  -1.417  0.58 16.79 ?  75  LEU   A HG   1 
ATOM   1931 H HD11 A LEU   A 1 75  ? 32.413 -1.126  0.077   0.42 15.73 ?  75  LEU   A HD11 1 
ATOM   1932 H HD11 B LEU   A 1 75  ? 32.527 -1.651  0.212   0.58 17.15 ?  75  LEU   A HD11 1 
ATOM   1933 H HD12 A LEU   A 1 75  ? 31.643 -0.859  -1.287  0.42 15.73 ?  75  LEU   A HD12 1 
ATOM   1934 H HD12 B LEU   A 1 75  ? 31.664 -1.398  -1.098  0.58 17.15 ?  75  LEU   A HD12 1 
ATOM   1935 H HD13 A LEU   A 1 75  ? 31.939 -2.349  -0.820  0.42 15.73 ?  75  LEU   A HD13 1 
ATOM   1936 H HD13 B LEU   A 1 75  ? 32.236 -2.848  -0.792  0.58 17.15 ?  75  LEU   A HD13 1 
ATOM   1937 H HD21 A LEU   A 1 75  ? 34.691 -1.830  0.102   0.42 17.79 ?  75  LEU   A HD21 1 
ATOM   1938 H HD21 B LEU   A 1 75  ? 34.866 -2.077  0.070   0.58 21.31 ?  75  LEU   A HD21 1 
ATOM   1939 H HD22 A LEU   A 1 75  ? 34.442 -3.108  -0.809  0.42 17.79 ?  75  LEU   A HD22 1 
ATOM   1940 H HD22 B LEU   A 1 75  ? 34.741 -3.222  -1.024  0.58 21.31 ?  75  LEU   A HD22 1 
ATOM   1941 H HD23 A LEU   A 1 75  ? 35.527 -2.028  -1.234  0.42 17.79 ?  75  LEU   A HD23 1 
ATOM   1942 H HD23 B LEU   A 1 75  ? 35.655 -1.953  -1.302  0.58 21.31 ?  75  LEU   A HD23 1 
ATOM   1943 N N    . LYS   A 1 76  ? 34.186 -3.705  -5.303  1.00 12.72 ?  76  LYS   A N    1 
ATOM   1944 C CA   . LYS   A 1 76  ? 33.619 -4.406  -6.446  1.00 13.05 ?  76  LYS   A CA   1 
ATOM   1945 C C    . LYS   A 1 76  ? 32.101 -4.494  -6.288  1.00 12.31 ?  76  LYS   A C    1 
ATOM   1946 O O    . LYS   A 1 76  ? 31.586 -4.586  -5.174  1.00 12.48 ?  76  LYS   A O    1 
ATOM   1947 C CB   . LYS   A 1 76  ? 34.150 -5.848  -6.481  1.00 14.30 ?  76  LYS   A CB   1 
ATOM   1948 C CG   . LYS   A 1 76  ? 35.658 -5.962  -6.653  1.00 15.77 ?  76  LYS   A CG   1 
ATOM   1949 C CD   . LYS   A 1 76  ? 36.158 -7.381  -6.460  1.00 17.61 ?  76  LYS   A CD   1 
ATOM   1950 C CE   . LYS   A 1 76  ? 37.651 -7.443  -6.699  1.00 19.74 ?  76  LYS   A CE   1 
ATOM   1951 N NZ   . LYS   A 1 76  ? 38.215 -8.787  -6.492  1.00 21.00 ?  76  LYS   A NZ   1 
ATOM   1952 H H    A LYS   A 1 76  ? 34.380 -4.225  -4.646  0.42 15.28 ?  76  LYS   A H    1 
ATOM   1953 H H    B LYS   A 1 76  ? 34.457 -4.231  -4.679  0.58 15.28 ?  76  LYS   A H    1 
ATOM   1954 H HA   . LYS   A 1 76  ? 33.840 -3.955  -7.278  1.00 15.68 ?  76  LYS   A HA   1 
ATOM   1955 H HB2  . LYS   A 1 76  ? 33.918 -6.283  -5.650  1.00 17.18 ?  76  LYS   A HB2  1 
ATOM   1956 H HB3  . LYS   A 1 76  ? 33.739 -6.312  -7.225  1.00 17.18 ?  76  LYS   A HB3  1 
ATOM   1957 H HG2  . LYS   A 1 76  ? 35.903 -5.674  -7.547  1.00 18.94 ?  76  LYS   A HG2  1 
ATOM   1958 H HG3  . LYS   A 1 76  ? 36.098 -5.398  -5.993  1.00 18.94 ?  76  LYS   A HG3  1 
ATOM   1959 H HD2  . LYS   A 1 76  ? 35.976 -7.671  -5.552  1.00 21.15 ?  76  LYS   A HD2  1 
ATOM   1960 H HD3  . LYS   A 1 76  ? 35.717 -7.969  -7.098  1.00 21.15 ?  76  LYS   A HD3  1 
ATOM   1961 H HE2  . LYS   A 1 76  ? 37.832 -7.178  -7.615  1.00 23.71 ?  76  LYS   A HE2  1 
ATOM   1962 H HE3  . LYS   A 1 76  ? 38.091 -6.837  -6.085  1.00 23.71 ?  76  LYS   A HE3  1 
ATOM   1963 H HZ1  . LYS   A 1 76  ? 39.092 -8.781  -6.645  1.00 25.22 ?  76  LYS   A HZ1  1 
ATOM   1964 H HZ2  . LYS   A 1 76  ? 38.069 -9.059  -5.657  1.00 25.22 ?  76  LYS   A HZ2  1 
ATOM   1965 H HZ3  . LYS   A 1 76  ? 37.833 -9.371  -7.053  1.00 25.22 ?  76  LYS   A HZ3  1 
ATOM   1966 N N    A VAL   A 1 77  ? 31.389 -4.518  -7.415  0.42 12.79 ?  77  VAL   A N    1 
ATOM   1967 N N    B VAL   A 1 77  ? 31.385 -4.463  -7.412  0.58 12.83 ?  77  VAL   A N    1 
ATOM   1968 C CA   A VAL   A 1 77  ? 29.969 -4.857  -7.363  0.42 12.76 ?  77  VAL   A CA   1 
ATOM   1969 C CA   B VAL   A 1 77  ? 29.983 -4.860  -7.359  0.58 12.94 ?  77  VAL   A CA   1 
ATOM   1970 C C    A VAL   A 1 77  ? 29.845 -6.315  -6.938  0.42 12.07 ?  77  VAL   A C    1 
ATOM   1971 C C    B VAL   A 1 77  ? 29.930 -6.300  -6.869  0.58 11.84 ?  77  VAL   A C    1 
ATOM   1972 O O    A VAL   A 1 77  ? 30.422 -7.210  -7.568  0.42 12.68 ?  77  VAL   A O    1 
ATOM   1973 O O    B VAL   A 1 77  ? 30.654 -7.168  -7.373  0.58 12.04 ?  77  VAL   A O    1 
ATOM   1974 C CB   A VAL   A 1 77  ? 29.276 -4.600  -8.708  0.42 13.42 ?  77  VAL   A CB   1 
ATOM   1975 C CB   B VAL   A 1 77  ? 29.311 -4.699  -8.730  0.58 14.10 ?  77  VAL   A CB   1 
ATOM   1976 C CG1  A VAL   A 1 77  ? 27.822 -5.059  -8.646  0.42 14.29 ?  77  VAL   A CG1  1 
ATOM   1977 C CG1  B VAL   A 1 77  ? 27.831 -5.061  -8.640  0.58 15.18 ?  77  VAL   A CG1  1 
ATOM   1978 C CG2  A VAL   A 1 77  ? 29.355 -3.126  -9.072  0.42 14.10 ?  77  VAL   A CG2  1 
ATOM   1979 C CG2  B VAL   A 1 77  ? 29.485 -3.279  -9.245  0.58 15.41 ?  77  VAL   A CG2  1 
ATOM   1980 H H    A VAL   A 1 77  ? 31.697 -4.357  -8.201  0.42 15.36 ?  77  VAL   A H    1 
ATOM   1981 H H    B VAL   A 1 77  ? 31.680 -4.233  -8.186  0.58 15.41 ?  77  VAL   A H    1 
ATOM   1982 H HA   A VAL   A 1 77  ? 29.539 -4.315  -6.691  0.42 15.33 ?  77  VAL   A HA   1 
ATOM   1983 H HA   B VAL   A 1 77  ? 29.519 -4.306  -6.718  0.58 15.54 ?  77  VAL   A HA   1 
ATOM   1984 H HB   A VAL   A 1 77  ? 29.721 -5.109  -9.404  0.42 16.13 ?  77  VAL   A HB   1 
ATOM   1985 H HB   B VAL   A 1 77  ? 29.733 -5.302  -9.362  0.58 16.94 ?  77  VAL   A HB   1 
ATOM   1986 H HG11 A VAL   A 1 77  ? 27.344 -4.686  -9.401  0.42 17.17 ?  77  VAL   A HG11 1 
ATOM   1987 H HG11 B VAL   A 1 77  ? 27.405 -4.846  -9.483  0.58 18.23 ?  77  VAL   A HG11 1 
ATOM   1988 H HG12 A VAL   A 1 77  ? 27.793 -6.028  -8.681  0.42 17.17 ?  77  VAL   A HG12 1 
ATOM   1989 H HG12 B VAL   A 1 77  ? 27.746 -6.009  -8.457  0.58 18.23 ?  77  VAL   A HG12 1 
ATOM   1990 H HG13 A VAL   A 1 77  ? 27.430 -4.744  -7.817  0.42 17.17 ?  77  VAL   A HG13 1 
ATOM   1991 H HG13 B VAL   A 1 77  ? 27.425 -4.547  -7.924  0.58 18.23 ?  77  VAL   A HG13 1 
ATOM   1992 H HG21 A VAL   A 1 77  ? 28.892 -2.981  -9.909  0.42 16.94 ?  77  VAL   A HG21 1 
ATOM   1993 H HG21 B VAL   A 1 77  ? 28.948 -3.165  -10.040 0.58 18.51 ?  77  VAL   A HG21 1 
ATOM   1994 H HG22 A VAL   A 1 77  ? 28.940 -2.606  -8.366  0.42 16.94 ?  77  VAL   A HG22 1 
ATOM   1995 H HG22 B VAL   A 1 77  ? 29.197 -2.658  -8.556  0.58 18.51 ?  77  VAL   A HG22 1 
ATOM   1996 H HG23 A VAL   A 1 77  ? 30.290 -2.876  -9.160  0.42 16.94 ?  77  VAL   A HG23 1 
ATOM   1997 H HG23 B VAL   A 1 77  ? 30.422 -3.128  -9.450  0.58 18.51 ?  77  VAL   A HG23 1 
ATOM   1998 N N    . GLY   A 1 78  ? 29.090 -6.560  -5.864  1.00 11.68 ?  78  GLY   A N    1 
ATOM   1999 C CA   . GLY   A 1 78  ? 29.045 -7.847  -5.198  1.00 12.34 ?  78  GLY   A CA   1 
ATOM   2000 C C    . GLY   A 1 78  ? 29.951 -7.934  -3.986  1.00 11.54 ?  78  GLY   A C    1 
ATOM   2001 O O    . GLY   A 1 78  ? 29.886 -8.933  -3.253  1.00 12.39 ?  78  GLY   A O    1 
ATOM   2002 H H    A GLY   A 1 78  ? 28.581 -5.971  -5.495  0.42 14.03 ?  78  GLY   A H    1 
ATOM   2003 H H    B GLY   A 1 78  ? 28.521 -5.992  -5.553  0.58 14.03 ?  78  GLY   A H    1 
ATOM   2004 H HA2  . GLY   A 1 78  ? 28.137 -8.033  -4.917  1.00 14.82 ?  78  GLY   A HA2  1 
ATOM   2005 H HA3  . GLY   A 1 78  ? 29.314 -8.542  -5.825  1.00 14.82 ?  78  GLY   A HA3  1 
ATOM   2006 N N    . GLY   A 1 79  ? 30.803 -6.926  -3.758  1.00 11.71 ?  79  GLY   A N    1 
ATOM   2007 C CA   . GLY   A 1 79  ? 31.751 -6.937  -2.668  1.00 12.22 ?  79  GLY   A CA   1 
ATOM   2008 C C    . GLY   A 1 79  ? 31.278 -6.137  -1.463  1.00 11.07 ?  79  GLY   A C    1 
ATOM   2009 O O    . GLY   A 1 79  ? 30.151 -5.648  -1.395  1.00 12.08 ?  79  GLY   A O    1 
ATOM   2010 H H    . GLY   A 1 79  ? 30.846 -6.215  -4.244  1.00 14.06 ?  79  GLY   A H    1 
ATOM   2011 H HA2  . GLY   A 1 79  ? 31.908 -7.857  -2.393  1.00 14.68 ?  79  GLY   A HA2  1 
ATOM   2012 H HA3  . GLY   A 1 79  ? 32.592 -6.565  -2.973  1.00 14.68 ?  79  GLY   A HA3  1 
ATOM   2013 N N    . SER   A 1 80  ? 32.168 -6.039  -0.478  1.00 12.08 ?  80  SER   A N    1 
ATOM   2014 C CA   . SER   A 1 80  ? 31.839 -5.409  0.792   1.00 11.24 ?  80  SER   A CA   1 
ATOM   2015 C C    . SER   A 1 80  ? 33.103 -4.953  1.508   1.00 11.44 ?  80  SER   A C    1 
ATOM   2016 O O    . SER   A 1 80  ? 34.216 -5.393  1.205   1.00 13.04 ?  80  SER   A O    1 
ATOM   2017 C CB   . SER   A 1 80  ? 31.070 -6.367  1.711   1.00 12.17 ?  80  SER   A CB   1 
ATOM   2018 O OG   . SER   A 1 80  ? 31.903 -7.423  2.176   1.00 14.49 ?  80  SER   A OG   1 
ATOM   2019 H H    . SER   A 1 80  ? 32.980 -6.331  -0.525  1.00 14.52 ?  80  SER   A H    1 
ATOM   2020 H HA   . SER   A 1 80  ? 31.284 -4.639  0.611   1.00 13.50 ?  80  SER   A HA   1 
ATOM   2021 H HB2  . SER   A 1 80  ? 30.741 -5.870  2.475   1.00 14.63 ?  80  SER   A HB2  1 
ATOM   2022 H HB3  . SER   A 1 80  ? 30.323 -6.746  1.218   1.00 14.63 ?  80  SER   A HB3  1 
ATOM   2023 H HG   . SER   A 1 80  ? 32.187 -7.868  1.519   1.00 17.40 ?  80  SER   A HG   1 
ATOM   2024 N N    . CYS   A 1 81  ? 32.904 -4.095  2.507   1.00 11.25 ?  81  CYS   A N    1 
ATOM   2025 C CA   . CYS   A 1 81  ? 33.934 -3.811  3.495   1.00 11.39 ?  81  CYS   A CA   1 
ATOM   2026 C C    . CYS   A 1 81  ? 33.273 -3.583  4.850   1.00 10.90 ?  81  CYS   A C    1 
ATOM   2027 O O    . CYS   A 1 81  ? 32.106 -3.183  4.931   1.00 12.36 ?  81  CYS   A O    1 
ATOM   2028 C CB   . CYS   A 1 81  ? 34.803 -2.610  3.106   1.00 11.93 ?  81  CYS   A CB   1 
ATOM   2029 S SG   . CYS   A 1 81  ? 33.905 -1.045  3.106   1.00 12.16 ?  81  CYS   A SG   1 
ATOM   2030 H H    . CYS   A 1 81  ? 32.171 -3.660  2.632   1.00 13.52 ?  81  CYS   A H    1 
ATOM   2031 H HA   . CYS   A 1 81  ? 34.518 -4.580  3.566   1.00 13.69 ?  81  CYS   A HA   1 
ATOM   2032 H HB2  . CYS   A 1 81  ? 35.536 -2.537  3.739   1.00 14.33 ?  81  CYS   A HB2  1 
ATOM   2033 H HB3  . CYS   A 1 81  ? 35.156 -2.753  2.212   1.00 14.33 ?  81  CYS   A HB3  1 
ATOM   2034 H HG   . CYS   A 1 81  ? 34.662 -0.162  2.797   1.00 14.61 ?  81  CYS   A HG   1 
ATOM   2035 N N    . VAL   A 1 82  ? 34.037 -3.833  5.915   1.00 11.13 ?  82  VAL   A N    1 
ATOM   2036 C CA   . VAL   A 1 82  ? 33.591 -3.590  7.280   1.00 12.00 ?  82  VAL   A CA   1 
ATOM   2037 C C    . VAL   A 1 82  ? 34.185 -2.279  7.761   1.00 11.99 ?  82  VAL   A C    1 
ATOM   2038 O O    . VAL   A 1 82  ? 35.412 -2.117  7.770   1.00 12.45 ?  82  VAL   A O    1 
ATOM   2039 C CB   . VAL   A 1 82  ? 33.996 -4.734  8.222   1.00 13.55 ?  82  VAL   A CB   1 
ATOM   2040 C CG1  . VAL   A 1 82  ? 33.534 -4.440  9.635   1.00 14.86 ?  82  VAL   A CG1  1 
ATOM   2041 C CG2  . VAL   A 1 82  ? 33.443 -6.059  7.742   1.00 14.51 ?  82  VAL   A CG2  1 
ATOM   2042 H H    . VAL   A 1 82  ? 34.837 -4.166  5.863   1.00 13.37 ?  82  VAL   A H    1 
ATOM   2043 H HA   . VAL   A 1 82  ? 32.626 -3.508  7.285   1.00 14.41 ?  82  VAL   A HA   1 
ATOM   2044 H HB   . VAL   A 1 82  ? 34.962 -4.802  8.231   1.00 16.28 ?  82  VAL   A HB   1 
ATOM   2045 H HG11 . VAL   A 1 82  ? 33.609 -5.248  10.166  1.00 17.85 ?  82  VAL   A HG11 1 
ATOM   2046 H HG12 . VAL   A 1 82  ? 34.090 -3.742  10.017  1.00 17.85 ?  82  VAL   A HG12 1 
ATOM   2047 H HG13 . VAL   A 1 82  ? 32.607 -4.149  9.612   1.00 17.85 ?  82  VAL   A HG13 1 
ATOM   2048 H HG21 . VAL   A 1 82  ? 33.679 -6.748  8.379   1.00 17.43 ?  82  VAL   A HG21 1 
ATOM   2049 H HG22 . VAL   A 1 82  ? 32.475 -5.988  7.674   1.00 17.43 ?  82  VAL   A HG22 1 
ATOM   2050 H HG23 . VAL   A 1 82  ? 33.818 -6.264  6.872   1.00 17.43 ?  82  VAL   A HG23 1 
ATOM   2051 N N    . LEU   A 1 83  ? 33.328 -1.353  8.180   1.00 11.53 ?  83  LEU   A N    1 
ATOM   2052 C CA   . LEU   A 1 83  ? 33.751 -0.092  8.771   1.00 11.33 ?  83  LEU   A CA   1 
ATOM   2053 C C    . LEU   A 1 83  ? 33.011 0.092   10.093  1.00 11.76 ?  83  LEU   A C    1 
ATOM   2054 O O    . LEU   A 1 83  ? 32.283 -0.796  10.545  1.00 12.26 ?  83  LEU   A O    1 
ATOM   2055 C CB   . LEU   A 1 83  ? 33.505 1.065   7.793   1.00 12.13 ?  83  LEU   A CB   1 
ATOM   2056 C CG   . LEU   A 1 83  ? 34.404 1.077   6.553   1.00 12.72 ?  83  LEU   A CG   1 
ATOM   2057 C CD1  . LEU   A 1 83  ? 33.974 2.142   5.565   1.00 13.50 ?  83  LEU   A CD1  1 
ATOM   2058 C CD2  . LEU   A 1 83  ? 35.887 1.278   6.930   1.00 13.28 ?  83  LEU   A CD2  1 
ATOM   2059 H H    . LEU   A 1 83  ? 32.478 -1.433  8.132   1.00 13.85 ?  83  LEU   A H    1 
ATOM   2060 H HA   . LEU   A 1 83  ? 34.708 -0.118  8.956   1.00 13.61 ?  83  LEU   A HA   1 
ATOM   2061 H HB2  . LEU   A 1 83  ? 32.582 1.017   7.484   1.00 14.58 ?  83  LEU   A HB2  1 
ATOM   2062 H HB3  . LEU   A 1 83  ? 33.633 1.906   8.260   1.00 14.58 ?  83  LEU   A HB3  1 
ATOM   2063 H HG   . LEU   A 1 83  ? 34.324 0.221   6.112   1.00 15.28 ?  83  LEU   A HG   1 
ATOM   2064 H HD11 . LEU   A 1 83  ? 34.564 2.113   4.794   1.00 16.22 ?  83  LEU   A HD11 1 
ATOM   2065 H HD12 . LEU   A 1 83  ? 33.060 1.970   5.289   1.00 16.22 ?  83  LEU   A HD12 1 
ATOM   2066 H HD13 . LEU   A 1 83  ? 34.031 3.013   5.990   1.00 16.22 ?  83  LEU   A HD13 1 
ATOM   2067 H HD21 . LEU   A 1 83  ? 36.403 1.420   6.118   1.00 15.95 ?  83  LEU   A HD21 1 
ATOM   2068 H HD22 . LEU   A 1 83  ? 35.969 2.054   7.508   1.00 15.95 ?  83  LEU   A HD22 1 
ATOM   2069 H HD23 . LEU   A 1 83  ? 36.210 0.489   7.390   1.00 15.95 ?  83  LEU   A HD23 1 
ATOM   2070 N N    . SER   A 1 84  ? 33.208 1.241   10.730  1.00 12.66 ?  84  SER   A N    1 
ATOM   2071 C CA   . SER   A 1 84  ? 32.541 1.488   11.998  1.00 12.47 ?  84  SER   A CA   1 
ATOM   2072 C C    . SER   A 1 84  ? 31.028 1.602   11.819  1.00 12.68 ?  84  SER   A C    1 
ATOM   2073 O O    . SER   A 1 84  ? 30.533 2.061   10.788  1.00 12.42 ?  84  SER   A O    1 
ATOM   2074 C CB   . SER   A 1 84  ? 33.035 2.806   12.585  1.00 13.39 ?  84  SER   A CB   1 
ATOM   2075 O OG   . SER   A 1 84  ? 32.393 3.086   13.806  1.00 14.74 ?  84  SER   A OG   1 
ATOM   2076 H H    . SER   A 1 84  ? 33.716 1.883   10.460  1.00 15.21 ?  84  SER   A H    1 
ATOM   2077 H HA   . SER   A 1 84  ? 32.736 0.767   12.622  1.00 14.98 ?  84  SER   A HA   1 
ATOM   2078 H HB2  . SER   A 1 84  ? 33.991 2.746   12.727  1.00 16.08 ?  84  SER   A HB2  1 
ATOM   2079 H HB3  . SER   A 1 84  ? 32.834 3.518   11.961  1.00 16.08 ?  84  SER   A HB3  1 
ATOM   2080 H HG   . SER   A 1 84  ? 32.687 3.811   14.122  1.00 17.71 ?  84  SER   A HG   1 
ATOM   2081 N N    A GLY   A 1 85  ? 30.294 1.163   12.841  0.42 13.18 ?  85  GLY   A N    1 
ATOM   2082 N N    B GLY   A 1 85  ? 30.291 1.241   12.871  0.58 13.27 ?  85  GLY   A N    1 
ATOM   2083 C CA   A GLY   A 1 85  ? 28.871 1.404   12.926  0.42 13.52 ?  85  GLY   A CA   1 
ATOM   2084 C CA   B GLY   A 1 85  ? 28.866 1.494   12.923  0.58 13.91 ?  85  GLY   A CA   1 
ATOM   2085 C C    A GLY   A 1 85  ? 28.518 2.719   13.578  0.42 13.31 ?  85  GLY   A C    1 
ATOM   2086 C C    B GLY   A 1 85  ? 28.482 2.810   13.563  0.58 13.46 ?  85  GLY   A C    1 
ATOM   2087 O O    A GLY   A 1 85  ? 27.333 3.038   13.725  0.42 13.39 ?  85  GLY   A O    1 
ATOM   2088 O O    B GLY   A 1 85  ? 27.293 3.145   13.604  0.58 14.25 ?  85  GLY   A O    1 
ATOM   2089 H H    A GLY   A 1 85  ? 30.609 0.715   13.508  0.42 15.83 ?  85  GLY   A H    1 
ATOM   2090 H H    B GLY   A 1 85  ? 30.599 0.843   13.571  0.58 15.94 ?  85  GLY   A H    1 
ATOM   2091 H HA2  A GLY   A 1 85  ? 28.495 1.390   12.031  0.42 16.24 ?  85  GLY   A HA2  1 
ATOM   2092 H HA2  B GLY   A 1 85  ? 28.511 1.503   12.021  0.58 16.71 ?  85  GLY   A HA2  1 
ATOM   2093 H HA3  A GLY   A 1 85  ? 28.456 0.698   13.440  0.42 16.24 ?  85  GLY   A HA3  1 
ATOM   2094 H HA3  B GLY   A 1 85  ? 28.431 0.781   13.410  0.58 16.71 ?  85  GLY   A HA3  1 
ATOM   2095 N N    A HIS   A 1 86  ? 29.525 3.483   14.003  0.42 13.21 ?  86  HIS   A N    1 
ATOM   2096 N N    B HIS   A 1 86  ? 29.448 3.564   14.074  0.58 13.29 ?  86  HIS   A N    1 
ATOM   2097 C CA   A HIS   A 1 86  ? 29.350 4.825   14.568  0.42 13.34 ?  86  HIS   A CA   1 
ATOM   2098 C CA   B HIS   A 1 86  ? 29.207 4.905   14.633  0.58 13.55 ?  86  HIS   A CA   1 
ATOM   2099 C C    A HIS   A 1 86  ? 28.360 4.735   15.728  0.42 13.42 ?  86  HIS   A C    1 
ATOM   2100 C C    B HIS   A 1 86  ? 28.182 4.783   15.760  0.58 14.84 ?  86  HIS   A C    1 
ATOM   2101 O O    A HIS   A 1 86  ? 28.566 3.917   16.634  0.42 13.94 ?  86  HIS   A O    1 
ATOM   2102 O O    B HIS   A 1 86  ? 28.282 3.863   16.587  0.58 16.01 ?  86  HIS   A O    1 
ATOM   2103 C CB   A HIS   A 1 86  ? 29.012 5.805   13.453  0.42 14.32 ?  86  HIS   A CB   1 
ATOM   2104 C CB   B HIS   A 1 86  ? 28.865 5.869   13.522  0.58 13.46 ?  86  HIS   A CB   1 
ATOM   2105 C CG   A HIS   A 1 86  ? 30.072 5.872   12.402  0.42 14.94 ?  86  HIS   A CG   1 
ATOM   2106 C CG   B HIS   A 1 86  ? 29.953 5.975   12.510  0.58 13.15 ?  86  HIS   A CG   1 
ATOM   2107 N ND1  A HIS   A 1 86  ? 31.176 6.689   12.516  0.42 15.89 ?  86  HIS   A ND1  1 
ATOM   2108 N ND1  B HIS   A 1 86  ? 31.035 6.811   12.678  0.58 14.29 ?  86  HIS   A ND1  1 
ATOM   2109 C CD2  A HIS   A 1 86  ? 30.228 5.183   11.248  0.42 14.99 ?  86  HIS   A CD2  1 
ATOM   2110 C CD2  B HIS   A 1 86  ? 30.174 5.291   11.362  0.58 12.50 ?  86  HIS   A CD2  1 
ATOM   2111 C CE1  A HIS   A 1 86  ? 31.956 6.516   11.465  0.42 15.89 ?  86  HIS   A CE1  1 
ATOM   2112 C CE1  B HIS   A 1 86  ? 31.865 6.654   11.663  0.58 13.91 ?  86  HIS   A CE1  1 
ATOM   2113 N NE2  A HIS   A 1 86  ? 31.406 5.605   10.682  0.42 15.40 ?  86  HIS   A NE2  1 
ATOM   2114 N NE2  B HIS   A 1 86  ? 31.369 5.737   10.853  0.58 12.98 ?  86  HIS   A NE2  1 
ATOM   2115 H H    A HIS   A 1 86  ? 30.345 3.233   13.983  0.42 15.87 ?  86  HIS   A H    1 
ATOM   2116 H H    B HIS   A 1 86  ? 30.268 3.327   14.117  0.58 15.97 ?  86  HIS   A H    1 
ATOM   2117 H HA   A HIS   A 1 86  ? 30.196 5.107   14.940  0.42 16.02 ?  86  HIS   A HA   1 
ATOM   2118 H HA   B HIS   A 1 86  ? 30.030 5.221   15.028  0.58 16.28 ?  86  HIS   A HA   1 
ATOM   2119 H HB2  A HIS   A 1 86  ? 28.182 5.531   13.028  0.42 17.20 ?  86  HIS   A HB2  1 
ATOM   2120 H HB2  B HIS   A 1 86  ? 28.057 5.567   13.078  0.58 16.17 ?  86  HIS   A HB2  1 
ATOM   2121 H HB3  A HIS   A 1 86  ? 28.907 6.694   13.832  0.42 17.20 ?  86  HIS   A HB3  1 
ATOM   2122 H HB3  B HIS   A 1 86  ? 28.721 6.753   13.904  0.58 16.17 ?  86  HIS   A HB3  1 
ATOM   2123 H HD2  A HIS   A 1 86  ? 29.646 4.544   10.902  0.42 18.01 ?  86  HIS   A HD2  1 
ATOM   2124 H HD2  B HIS   A 1 86  ? 29.620 4.640   10.988  0.58 15.02 ?  86  HIS   A HD2  1 
ATOM   2125 H HE1  A HIS   A 1 86  ? 32.752 6.963   11.305  0.42 19.09 ?  86  HIS   A HE1  1 
ATOM   2126 H HE1  B HIS   A 1 86  ? 32.656 7.119   11.535  0.58 16.71 ?  86  HIS   A HE1  1 
ATOM   2127 H HE2  A HIS   A 1 86  ? 31.729 5.331   9.935   0.42 18.50 ?  86  HIS   A HE2  1 
ATOM   2128 H HE2  B HIS   A 1 86  ? 31.724 5.477   10.114  0.58 15.59 ?  86  HIS   A HE2  1 
ATOM   2129 N N    A ASN   A 1 87  ? 27.311 5.547   15.752  0.42 14.43 ?  87  ASN   A N    1 
ATOM   2130 N N    B ASN   A 1 87  ? 27.209 5.684   15.819  0.58 15.72 ?  87  ASN   A N    1 
ATOM   2131 C CA   A ASN   A 1 87  ? 26.320 5.522   16.816  0.42 15.09 ?  87  ASN   A CA   1 
ATOM   2132 C CA   B ASN   A 1 87  ? 26.209 5.694   16.873  0.58 16.69 ?  87  ASN   A CA   1 
ATOM   2133 C C    A ASN   A 1 87  ? 25.211 4.508   16.572  0.42 15.73 ?  87  ASN   A C    1 
ATOM   2134 C C    B ASN   A 1 87  ? 25.070 4.726   16.614  0.58 17.17 ?  87  ASN   A C    1 
ATOM   2135 O O    A ASN   A 1 87  ? 24.302 4.405   17.398  0.42 17.40 ?  87  ASN   A O    1 
ATOM   2136 O O    B ASN   A 1 87  ? 24.101 4.730   17.379  0.58 18.93 ?  87  ASN   A O    1 
ATOM   2137 C CB   A ASN   A 1 87  ? 25.716 6.922   17.000  0.42 16.21 ?  87  ASN   A CB   1 
ATOM   2138 C CB   B ASN   A 1 87  ? 25.614 7.096   17.003  0.58 17.70 ?  87  ASN   A CB   1 
ATOM   2139 C CG   A ASN   A 1 87  ? 25.262 7.542   15.691  0.42 16.73 ?  87  ASN   A CG   1 
ATOM   2140 C CG   B ASN   A 1 87  ? 25.086 7.631   15.682  0.58 18.43 ?  87  ASN   A CG   1 
ATOM   2141 O OD1  A ASN   A 1 87  ? 25.962 7.473   14.681  0.42 17.29 ?  87  ASN   A OD1  1 
ATOM   2142 O OD1  B ASN   A 1 87  ? 25.703 7.455   14.634  0.58 18.92 ?  87  ASN   A OD1  1 
ATOM   2143 N ND2  A ASN   A 1 87  ? 24.085 8.154   15.704  0.42 17.68 ?  87  ASN   A ND2  1 
ATOM   2144 N ND2  B ASN   A 1 87  ? 23.938 8.286   15.729  0.58 19.70 ?  87  ASN   A ND2  1 
ATOM   2145 H H    A ASN   A 1 87  ? 27.146 6.129   15.150  0.42 17.33 ?  87  ASN   A H    1 
ATOM   2146 H H    B ASN   A 1 87  ? 27.096 6.303   15.237  0.58 18.88 ?  87  ASN   A H    1 
ATOM   2147 H HA   A ASN   A 1 87  ? 26.747 5.273   17.651  0.42 18.13 ?  87  ASN   A HA   1 
ATOM   2148 H HA   B ASN   A 1 87  ? 26.633 5.458   17.716  0.58 20.04 ?  87  ASN   A HA   1 
ATOM   2149 H HB2  A ASN   A 1 87  ? 24.945 6.861   17.589  0.42 19.47 ?  87  ASN   A HB2  1 
ATOM   2150 H HB2  B ASN   A 1 87  ? 24.874 7.061   17.633  0.58 21.26 ?  87  ASN   A HB2  1 
ATOM   2151 H HB3  A ASN   A 1 87  ? 26.386 7.502   17.392  0.42 19.47 ?  87  ASN   A HB3  1 
ATOM   2152 H HB3  B ASN   A 1 87  ? 26.299 7.695   17.326  0.58 21.26 ?  87  ASN   A HB3  1 
ATOM   2153 H HD21 A ASN   A 1 87  ? 23.784 8.522   14.988  0.42 21.24 ?  87  ASN   A HD21 1 
ATOM   2154 H HD21 B ASN   A 1 87  ? 23.599 8.606   15.007  0.58 23.66 ?  87  ASN   A HD21 1 
ATOM   2155 H HD22 A ASN   A 1 87  ? 23.626 8.188   16.431  0.42 21.24 ?  87  ASN   A HD22 1 
ATOM   2156 H HD22 B ASN   A 1 87  ? 23.535 8.389   16.480  0.58 23.66 ?  87  ASN   A HD22 1 
ATOM   2157 N N    A LEU   A 1 88  ? 25.282 3.733   15.492  0.42 14.84 ?  88  LEU   A N    1 
ATOM   2158 N N    B LEU   A 1 88  ? 25.148 3.923   15.555  0.58 15.64 ?  88  LEU   A N    1 
ATOM   2159 C CA   A LEU   A 1 88  ? 24.188 2.860   15.081  0.42 14.18 ?  88  LEU   A CA   1 
ATOM   2160 C CA   B LEU   A 1 88  ? 24.039 3.071   15.147  0.58 15.61 ?  88  LEU   A CA   1 
ATOM   2161 C C    A LEU   A 1 88  ? 24.423 1.385   15.377  0.42 13.78 ?  88  LEU   A C    1 
ATOM   2162 C C    B LEU   A 1 88  ? 24.254 1.593   15.432  0.58 15.33 ?  88  LEU   A C    1 
ATOM   2163 O O    A LEU   A 1 88  ? 23.455 0.639   15.543  0.42 15.43 ?  88  LEU   A O    1 
ATOM   2164 O O    B LEU   A 1 88  ? 23.279 0.860   15.605  0.58 16.41 ?  88  LEU   A O    1 
ATOM   2165 C CB   A LEU   A 1 88  ? 23.945 3.004   13.575  0.42 13.91 ?  88  LEU   A CB   1 
ATOM   2166 C CB   B LEU   A 1 88  ? 23.781 3.248   13.649  0.58 16.00 ?  88  LEU   A CB   1 
ATOM   2167 C CG   A LEU   A 1 88  ? 23.709 4.414   13.036  0.42 14.88 ?  88  LEU   A CG   1 
ATOM   2168 C CG   B LEU   A 1 88  ? 23.475 4.684   13.219  0.58 17.08 ?  88  LEU   A CG   1 
ATOM   2169 C CD1  A LEU   A 1 88  ? 23.657 4.368   11.522  0.42 14.79 ?  88  LEU   A CD1  1 
ATOM   2170 C CD1  B LEU   A 1 88  ? 23.298 4.768   11.713  0.58 17.30 ?  88  LEU   A CD1  1 
ATOM   2171 C CD2  A LEU   A 1 88  ? 22.433 5.013   13.614  0.42 16.95 ?  88  LEU   A CD2  1 
ATOM   2172 C CD2  B LEU   A 1 88  ? 22.236 5.203   13.935  0.58 17.79 ?  88  LEU   A CD2  1 
ATOM   2173 H H    A LEU   A 1 88  ? 25.978 3.677   14.989  0.42 17.83 ?  88  LEU   A H    1 
ATOM   2174 H H    B LEU   A 1 88  ? 25.842 3.859   15.041  0.58 18.78 ?  88  LEU   A H    1 
ATOM   2175 H HA   A LEU   A 1 88  ? 23.377 3.133   15.539  0.42 17.03 ?  88  LEU   A HA   1 
ATOM   2176 H HA   B LEU   A 1 88  ? 23.243 3.356   15.620  0.58 18.75 ?  88  LEU   A HA   1 
ATOM   2177 H HB2  A LEU   A 1 88  ? 24.717 2.649   13.113  0.42 16.71 ?  88  LEU   A HB2  1 
ATOM   2178 H HB2  B LEU   A 1 88  ? 24.566 2.957   13.164  0.58 19.22 ?  88  LEU   A HB2  1 
ATOM   2179 H HB3  A LEU   A 1 88  ? 23.163 2.479   13.348  0.42 16.71 ?  88  LEU   A HB3  1 
ATOM   2180 H HB3  B LEU   A 1 88  ? 23.020 2.701   13.403  0.58 19.22 ?  88  LEU   A HB3  1 
ATOM   2181 H HG   A LEU   A 1 88  ? 24.451 4.982   13.297  0.42 17.87 ?  88  LEU   A HG   1 
ATOM   2182 H HG   B LEU   A 1 88  ? 24.222 5.254   13.463  0.58 20.51 ?  88  LEU   A HG   1 
ATOM   2183 H HD11 A LEU   A 1 88  ? 23.511 5.265   11.185  0.42 17.77 ?  88  LEU   A HD11 1 
ATOM   2184 H HD11 B LEU   A 1 88  ? 23.137 5.692   11.465  0.58 20.78 ?  88  LEU   A HD11 1 
ATOM   2185 H HD12 A LEU   A 1 88  ? 24.499 4.022   11.189  0.42 17.77 ?  88  LEU   A HD12 1 
ATOM   2186 H HD12 B LEU   A 1 88  ? 24.105 4.445   11.283  0.58 20.78 ?  88  LEU   A HD12 1 
ATOM   2187 H HD13 A LEU   A 1 88  ? 22.929 3.788   11.250  0.42 17.77 ?  88  LEU   A HD13 1 
ATOM   2188 H HD13 B LEU   A 1 88  ? 22.542 4.219   11.454  0.58 20.78 ?  88  LEU   A HD13 1 
ATOM   2189 H HD21 A LEU   A 1 88  ? 22.293 5.892   13.226  0.42 20.36 ?  88  LEU   A HD21 1 
ATOM   2190 H HD21 B LEU   A 1 88  ? 21.963 6.036   13.522  0.58 21.36 ?  88  LEU   A HD21 1 
ATOM   2191 H HD22 A LEU   A 1 88  ? 21.685 4.434   13.399  0.42 20.36 ?  88  LEU   A HD22 1 
ATOM   2192 H HD22 B LEU   A 1 88  ? 21.531 4.544   13.853  0.58 21.36 ?  88  LEU   A HD22 1 
ATOM   2193 H HD23 A LEU   A 1 88  ? 22.526 5.089   14.577  0.42 20.36 ?  88  LEU   A HD23 1 
ATOM   2194 H HD23 B LEU   A 1 88  ? 22.451 5.348   14.868  0.58 21.36 ?  88  LEU   A HD23 1 
ATOM   2195 N N    A ALA   A 1 89  ? 25.678 0.952   15.435  0.42 13.83 ?  89  ALA   A N    1 
ATOM   2196 N N    B ALA   A 1 89  ? 25.503 1.149   15.496  0.58 14.93 ?  89  ALA   A N    1 
ATOM   2197 C CA   A ALA   A 1 89  ? 26.024 -0.459  15.539  0.42 13.38 ?  89  ALA   A CA   1 
ATOM   2198 C CA   B ALA   A 1 89  ? 25.848 -0.262  15.585  0.58 14.64 ?  89  ALA   A CA   1 
ATOM   2199 C C    A ALA   A 1 89  ? 27.503 -0.532  15.880  0.42 13.62 ?  89  ALA   A C    1 
ATOM   2200 C C    B ALA   A 1 89  ? 27.336 -0.331  15.879  0.58 14.93 ?  89  ALA   A C    1 
ATOM   2201 O O    A ALA   A 1 89  ? 28.215 0.473   15.829  0.42 14.64 ?  89  ALA   A O    1 
ATOM   2202 O O    B ALA   A 1 89  ? 28.055 0.656   15.710  0.58 15.97 ?  89  ALA   A O    1 
ATOM   2203 C CB   A ALA   A 1 89  ? 25.758 -1.182  14.219  0.42 12.69 ?  89  ALA   A CB   1 
ATOM   2204 C CB   B ALA   A 1 89  ? 25.567 -0.974  14.264  0.58 14.38 ?  89  ALA   A CB   1 
ATOM   2205 H H    A ALA   A 1 89  ? 26.362 1.473   15.410  0.42 16.62 ?  89  ALA   A H    1 
ATOM   2206 H H    B ALA   A 1 89  ? 26.182 1.668   15.491  0.58 17.93 ?  89  ALA   A H    1 
ATOM   2207 H HA   A ALA   A 1 89  ? 25.503 -0.877  16.244  0.42 16.07 ?  89  ALA   A HA   1 
ATOM   2208 H HA   B ALA   A 1 89  ? 25.340 -0.689  16.299  0.58 17.58 ?  89  ALA   A HA   1 
ATOM   2209 H HB1  A ALA   A 1 89  ? 26.018 -2.111  14.311  0.42 15.25 ?  89  ALA   A HB1  1 
ATOM   2210 H HB1  B ALA   A 1 89  ? 25.808 -1.907  14.353  0.58 17.27 ?  89  ALA   A HB1  1 
ATOM   2211 H HB2  A ALA   A 1 89  ? 24.813 -1.121  14.006  0.42 15.25 ?  89  ALA   A HB2  1 
ATOM   2212 H HB2  B ALA   A 1 89  ? 24.623 -0.893  14.053  0.58 17.27 ?  89  ALA   A HB2  1 
ATOM   2213 H HB3  A ALA   A 1 89  ? 26.282 -0.760  13.519  0.42 15.25 ?  89  ALA   A HB3  1 
ATOM   2214 H HB3  B ALA   A 1 89  ? 26.098 -0.558  13.566  0.58 17.27 ?  89  ALA   A HB3  1 
ATOM   2215 N N    A LYS   A 1 90  ? 27.969 -1.732  16.223  0.42 14.60 ?  90  LYS   A N    1 
ATOM   2216 N N    B LYS   A 1 90  ? 27.802 -1.500  16.310  0.58 14.29 ?  90  LYS   A N    1 
ATOM   2217 C CA   A LYS   A 1 90  ? 29.408 -1.898  16.396  0.42 16.76 ?  90  LYS   A CA   1 
ATOM   2218 C CA   B LYS   A 1 90  ? 29.243 -1.652  16.485  0.58 14.38 ?  90  LYS   A CA   1 
ATOM   2219 C C    A LYS   A 1 90  ? 30.129 -1.760  15.062  0.42 16.28 ?  90  LYS   A C    1 
ATOM   2220 C C    B LYS   A 1 90  ? 29.962 -1.483  15.150  0.58 12.84 ?  90  LYS   A C    1 
ATOM   2221 O O    A LYS   A 1 90  ? 31.122 -1.029  14.952  0.42 17.53 ?  90  LYS   A O    1 
ATOM   2222 O O    B LYS   A 1 90  ? 30.891 -0.670  15.025  0.58 13.22 ?  90  LYS   A O    1 
ATOM   2223 C CB   A LYS   A 1 90  ? 29.731 -3.240  17.049  0.42 19.36 ?  90  LYS   A CB   1 
ATOM   2224 C CB   B LYS   A 1 90  ? 29.567 -3.004  17.117  0.58 16.14 ?  90  LYS   A CB   1 
ATOM   2225 C CG   A LYS   A 1 90  ? 31.209 -3.397  17.379  0.42 22.75 ?  90  LYS   A CG   1 
ATOM   2226 C CG   B LYS   A 1 90  ? 31.024 -3.152  17.514  0.58 20.38 ?  90  LYS   A CG   1 
ATOM   2227 C CD   A LYS   A 1 90  ? 31.450 -4.602  18.272  0.42 25.73 ?  90  LYS   A CD   1 
ATOM   2228 C CD   B LYS   A 1 90  ? 31.271 -4.470  18.231  0.58 24.24 ?  90  LYS   A CD   1 
ATOM   2229 C CE   A LYS   A 1 90  ? 32.875 -4.633  18.808  0.42 28.08 ?  90  LYS   A CE   1 
ATOM   2230 C CE   B LYS   A 1 90  ? 32.624 -4.477  18.927  0.58 27.34 ?  90  LYS   A CE   1 
ATOM   2231 N NZ   A LYS   A 1 90  ? 33.872 -4.999  17.767  0.42 29.73 ?  90  LYS   A NZ   1 
ATOM   2232 N NZ   B LYS   A 1 90  ? 33.755 -4.364  17.967  0.58 28.85 ?  90  LYS   A NZ   1 
ATOM   2233 H H    A LYS   A 1 90  ? 27.489 -2.430  16.368  0.42 17.54 ?  90  LYS   A H    1 
ATOM   2234 H H    B LYS   A 1 90  ? 27.322 -2.188  16.507  0.58 17.17 ?  90  LYS   A H    1 
ATOM   2235 H HA   A LYS   A 1 90  ? 29.731 -1.194  16.978  0.42 20.13 ?  90  LYS   A HA   1 
ATOM   2236 H HA   B LYS   A 1 90  ? 29.558 -0.958  17.084  0.58 17.27 ?  90  LYS   A HA   1 
ATOM   2237 H HB2  A LYS   A 1 90  ? 29.225 -3.314  17.872  0.42 23.24 ?  90  LYS   A HB2  1 
ATOM   2238 H HB2  B LYS   A 1 90  ? 29.022 -3.113  17.915  0.58 19.39 ?  90  LYS   A HB2  1 
ATOM   2239 H HB3  A LYS   A 1 90  ? 29.479 -3.951  16.439  0.42 23.24 ?  90  LYS   A HB3  1 
ATOM   2240 H HB3  B LYS   A 1 90  ? 29.354 -3.703  16.479  0.58 19.39 ?  90  LYS   A HB3  1 
ATOM   2241 H HG2  A LYS   A 1 90  ? 31.710 -3.517  16.557  0.42 27.32 ?  90  LYS   A HG2  1 
ATOM   2242 H HG2  B LYS   A 1 90  ? 31.578 -3.130  16.719  0.58 24.47 ?  90  LYS   A HG2  1 
ATOM   2243 H HG3  A LYS   A 1 90  ? 31.517 -2.603  17.846  0.42 27.32 ?  90  LYS   A HG3  1 
ATOM   2244 H HG3  B LYS   A 1 90  ? 31.268 -2.430  18.114  0.58 24.47 ?  90  LYS   A HG3  1 
ATOM   2245 H HD2  A LYS   A 1 90  ? 30.841 -4.567  19.026  0.42 30.89 ?  90  LYS   A HD2  1 
ATOM   2246 H HD2  B LYS   A 1 90  ? 30.583 -4.607  18.903  0.58 29.11 ?  90  LYS   A HD2  1 
ATOM   2247 H HD3  A LYS   A 1 90  ? 31.301 -5.412  17.759  0.42 30.89 ?  90  LYS   A HD3  1 
ATOM   2248 H HD3  B LYS   A 1 90  ? 31.257 -5.196  17.586  0.58 29.11 ?  90  LYS   A HD3  1 
ATOM   2249 H HE2  A LYS   A 1 90  ? 33.104 -3.754  19.149  0.42 33.71 ?  90  LYS   A HE2  1 
ATOM   2250 H HE2  B LYS   A 1 90  ? 32.673 -3.723  19.537  0.58 32.83 ?  90  LYS   A HE2  1 
ATOM   2251 H HE3  A LYS   A 1 90  ? 32.930 -5.289  19.521  0.42 33.71 ?  90  LYS   A HE3  1 
ATOM   2252 H HE3  B LYS   A 1 90  ? 32.728 -5.308  19.418  0.58 32.83 ?  90  LYS   A HE3  1 
ATOM   2253 H HZ1  A LYS   A 1 90  ? 34.687 -5.033  18.125  0.42 35.69 ?  90  LYS   A HZ1  1 
ATOM   2254 H HZ1  B LYS   A 1 90  ? 34.530 -4.362  18.407  0.58 34.64 ?  90  LYS   A HZ1  1 
ATOM   2255 H HZ2  A LYS   A 1 90  ? 33.674 -5.795  17.422  0.42 35.69 ?  90  LYS   A HZ2  1 
ATOM   2256 H HZ2  B LYS   A 1 90  ? 33.746 -5.056  17.405  0.58 34.64 ?  90  LYS   A HZ2  1 
ATOM   2257 H HZ3  A LYS   A 1 90  ? 33.869 -4.392  17.116  0.42 35.69 ?  90  LYS   A HZ3  1 
ATOM   2258 H HZ3  B LYS   A 1 90  ? 33.685 -3.612  17.500  0.58 34.64 ?  90  LYS   A HZ3  1 
ATOM   2259 N N    A HIS   A 1 91  ? 29.630 -2.440  14.032  0.42 15.15 ?  91  HIS   A N    1 
ATOM   2260 N N    B HIS   A 1 91  ? 29.504 -2.208  14.131  0.58 11.51 ?  91  HIS   A N    1 
ATOM   2261 C CA   A HIS   A 1 91  ? 30.208 -2.398  12.701  0.42 14.37 ?  91  HIS   A CA   1 
ATOM   2262 C CA   B HIS   A 1 91  ? 30.103 -2.219  12.808  0.58 11.29 ?  91  HIS   A CA   1 
ATOM   2263 C C    A HIS   A 1 91  ? 29.119 -2.136  11.678  0.42 12.27 ?  91  HIS   A C    1 
ATOM   2264 C C    B HIS   A 1 91  ? 29.041 -1.949  11.757  0.58 10.71 ?  91  HIS   A C    1 
ATOM   2265 O O    A HIS   A 1 91  ? 27.974 -2.567  11.839  0.42 12.08 ?  91  HIS   A O    1 
ATOM   2266 O O    B HIS   A 1 91  ? 27.855 -2.227  11.952  0.58 11.51 ?  91  HIS   A O    1 
ATOM   2267 C CB   A HIS   A 1 91  ? 30.862 -3.730  12.328  0.42 16.66 ?  91  HIS   A CB   1 
ATOM   2268 C CB   B HIS   A 1 91  ? 30.692 -3.588  12.475  0.58 13.64 ?  91  HIS   A CB   1 
ATOM   2269 C CG   A HIS   A 1 91  ? 31.845 -4.225  13.338  0.42 19.57 ?  91  HIS   A CG   1 
ATOM   2270 C CG   B HIS   A 1 91  ? 31.658 -4.091  13.492  0.58 17.35 ?  91  HIS   A CG   1 
ATOM   2271 N ND1  A HIS   A 1 91  ? 33.112 -3.699  13.461  0.42 21.32 ?  91  HIS   A ND1  1 
ATOM   2272 N ND1  B HIS   A 1 91  ? 32.931 -3.582  13.616  0.58 19.99 ?  91  HIS   A ND1  1 
ATOM   2273 C CD2  A HIS   A 1 91  ? 31.752 -5.204  14.268  0.42 20.77 ?  91  HIS   A CD2  1 
ATOM   2274 C CD2  B HIS   A 1 91  ? 31.543 -5.057  14.433  0.58 19.19 ?  91  HIS   A CD2  1 
ATOM   2275 C CE1  A HIS   A 1 91  ? 33.757 -4.331  14.425  0.42 21.73 ?  91  HIS   A CE1  1 
ATOM   2276 C CE1  B HIS   A 1 91  ? 33.565 -4.219  14.585  0.58 20.98 ?  91  HIS   A CE1  1 
ATOM   2277 N NE2  A HIS   A 1 91  ? 32.954 -5.249  14.932  0.42 21.60 ?  91  HIS   A NE2  1 
ATOM   2278 N NE2  B HIS   A 1 91  ? 32.743 -5.118  15.099  0.58 20.78 ?  91  HIS   A NE2  1 
ATOM   2279 H H    A HIS   A 1 91  ? 28.929 -2.946  14.082  0.42 18.19 ?  91  HIS   A H    1 
ATOM   2280 H H    B HIS   A 1 91  ? 28.806 -2.720  14.191  0.58 13.83 ?  91  HIS   A H    1 
ATOM   2281 H HA   A HIS   A 1 91  ? 30.864 -1.692  12.638  0.42 17.26 ?  91  HIS   A HA   1 
ATOM   2282 H HA   B HIS   A 1 91  ? 30.789 -1.541  12.747  0.58 13.57 ?  91  HIS   A HA   1 
ATOM   2283 H HB2  A HIS   A 1 91  ? 30.169 -4.402  12.230  0.42 20.01 ?  91  HIS   A HB2  1 
ATOM   2284 H HB2  B HIS   A 1 91  ? 29.964 -4.229  12.410  0.58 16.38 ?  91  HIS   A HB2  1 
ATOM   2285 H HB3  A HIS   A 1 91  ? 31.330 -3.619  11.484  0.42 20.01 ?  91  HIS   A HB3  1 
ATOM   2286 H HB3  B HIS   A 1 91  ? 31.150 -3.525  11.624  0.58 16.38 ?  91  HIS   A HB3  1 
ATOM   2287 H HD1  A HIS   A 1 91  ? 33.432 -3.057  12.982  0.42 25.60 ?  91  HIS   A HD1  1 
ATOM   2288 H HD1  B HIS   A 1 91  ? 33.265 -2.951  13.127  0.58 24.01 ?  91  HIS   A HD1  1 
ATOM   2289 H HD2  A HIS   A 1 91  ? 31.009 -5.741  14.428  0.42 24.94 ?  91  HIS   A HD2  1 
ATOM   2290 H HD2  B HIS   A 1 91  ? 30.797 -5.583  14.592  0.58 23.04 ?  91  HIS   A HD2  1 
ATOM   2291 H HE1  A HIS   A 1 91  ? 34.626 -4.155  14.702  0.42 26.09 ?  91  HIS   A HE1  1 
ATOM   2292 H HE1  B HIS   A 1 91  ? 34.439 -4.055  14.856  0.58 25.19 ?  91  HIS   A HE1  1 
ATOM   2293 N N    . CYS   A 1 92  ? 29.491 -1.441  10.612  1.00 11.41 ?  92  CYS   A N    1 
ATOM   2294 C CA   . CYS   A 1 92  ? 28.672 -1.362  9.413   1.00 10.93 ?  92  CYS   A CA   1 
ATOM   2295 C C    . CYS   A 1 92  ? 29.328 -2.178  8.308   1.00 10.88 ?  92  CYS   A C    1 
ATOM   2296 O O    . CYS   A 1 92  ? 30.490 -1.938  7.960   1.00 11.59 ?  92  CYS   A O    1 
ATOM   2297 C CB   . CYS   A 1 92  ? 28.451 0.082   8.949   1.00 11.93 ?  92  CYS   A CB   1 
ATOM   2298 S SG   . CYS   A 1 92  ? 27.466 0.184   7.419   1.00 11.39 ?  92  CYS   A SG   1 
ATOM   2299 H H    A CYS   A 1 92  ? 30.227 -1.001  10.555  0.42 13.71 ?  92  CYS   A H    1 
ATOM   2300 H H    B CYS   A 1 92  ? 30.291 -1.146  10.496  0.58 13.71 ?  92  CYS   A H    1 
ATOM   2301 H HA   . CYS   A 1 92  ? 27.803 -1.749  9.591   1.00 13.14 ?  92  CYS   A HA   1 
ATOM   2302 H HB2  . CYS   A 1 92  ? 27.976 0.570   9.642   1.00 14.34 ?  92  CYS   A HB2  1 
ATOM   2303 H HB3  . CYS   A 1 92  ? 29.308 0.499   8.778   1.00 14.34 ?  92  CYS   A HB3  1 
ATOM   2304 H HG   . CYS   A 1 92  ? 27.318 1.336   7.123   1.00 13.68 ?  92  CYS   A HG   1 
ATOM   2305 N N    . LEU   A 1 93  ? 28.602 -3.168  7.798   1.00 10.70 ?  93  LEU   A N    1 
ATOM   2306 C CA   . LEU   A 1 93  ? 29.022 -3.929  6.630   1.00 10.41 ?  93  LEU   A CA   1 
ATOM   2307 C C    . LEU   A 1 93  ? 28.439 -3.250  5.392   1.00 10.42 ?  93  LEU   A C    1 
ATOM   2308 O O    . LEU   A 1 93  ? 27.226 -3.307  5.156   1.00 10.46 ?  93  LEU   A O    1 
ATOM   2309 C CB   . LEU   A 1 93  ? 28.555 -5.378  6.759   1.00 10.56 ?  93  LEU   A CB   1 
ATOM   2310 C CG   . LEU   A 1 93  ? 28.948 -6.271  5.583   1.00 11.49 ?  93  LEU   A CG   1 
ATOM   2311 C CD1  . LEU   A 1 93  ? 30.458 -6.534  5.543   1.00 12.64 ?  93  LEU   A CD1  1 
ATOM   2312 C CD2  . LEU   A 1 93  ? 28.167 -7.592  5.628   1.00 12.57 ?  93  LEU   A CD2  1 
ATOM   2313 H H    . LEU   A 1 93  ? 27.845 -3.420  8.129   1.00 12.85 ?  93  LEU   A H    1 
ATOM   2314 H HA   . LEU   A 1 93  ? 29.986 -3.912  6.569   1.00 12.51 ?  93  LEU   A HA   1 
ATOM   2315 H HB2  . LEU   A 1 93  ? 28.951 -5.757  7.567   1.00 12.69 ?  93  LEU   A HB2  1 
ATOM   2316 H HB3  . LEU   A 1 93  ? 27.592 -5.393  6.836   1.00 12.69 ?  93  LEU   A HB3  1 
ATOM   2317 H HG   . LEU   A 1 93  ? 28.713 -5.820  4.768   1.00 13.80 ?  93  LEU   A HG   1 
ATOM   2318 H HD11 . LEU   A 1 93  ? 30.656 -7.128  4.804   1.00 15.19 ?  93  LEU   A HD11 1 
ATOM   2319 H HD12 . LEU   A 1 93  ? 30.926 -5.691  5.425   1.00 15.19 ?  93  LEU   A HD12 1 
ATOM   2320 H HD13 . LEU   A 1 93  ? 30.736 -6.946  6.380   1.00 15.19 ?  93  LEU   A HD13 1 
ATOM   2321 H HD21 . LEU   A 1 93  ? 28.433 -8.143  4.878   1.00 15.10 ?  93  LEU   A HD21 1 
ATOM   2322 H HD22 . LEU   A 1 93  ? 28.364 -8.054  6.463   1.00 15.10 ?  93  LEU   A HD22 1 
ATOM   2323 H HD23 . LEU   A 1 93  ? 27.216 -7.401  5.580   1.00 15.10 ?  93  LEU   A HD23 1 
ATOM   2324 N N    . HIS   A 1 94  ? 29.295 -2.553  4.634   1.00 10.09 ?  94  HIS   A N    1 
ATOM   2325 C CA   . HIS   A 1 94  ? 28.877 -1.896  3.398   1.00 10.52 ?  94  HIS   A CA   1 
ATOM   2326 C C    . HIS   A 1 94  ? 28.911 -2.932  2.287   1.00 10.34 ?  94  HIS   A C    1 
ATOM   2327 O O    . HIS   A 1 94  ? 29.981 -3.453  1.970   1.00 11.52 ?  94  HIS   A O    1 
ATOM   2328 C CB   . HIS   A 1 94  ? 29.833 -0.738  3.079   1.00 10.21 ?  94  HIS   A CB   1 
ATOM   2329 C CG   . HIS   A 1 94  ? 29.813 0.355   4.101   1.00 10.27 ?  94  HIS   A CG   1 
ATOM   2330 N ND1  . HIS   A 1 94  ? 28.936 1.418   4.035   1.00 10.31 ?  94  HIS   A ND1  1 
ATOM   2331 C CD2  . HIS   A 1 94  ? 30.542 0.530   5.226   1.00 11.17 ?  94  HIS   A CD2  1 
ATOM   2332 C CE1  . HIS   A 1 94  ? 29.138 2.199   5.078   1.00 10.59 ?  94  HIS   A CE1  1 
ATOM   2333 N NE2  . HIS   A 1 94  ? 30.101 1.683   5.819   1.00 10.98 ?  94  HIS   A NE2  1 
ATOM   2334 H H    . HIS   A 1 94  ? 30.128 -2.445  4.817   1.00 12.13 ?  94  HIS   A H    1 
ATOM   2335 H HA   . HIS   A 1 94  ? 27.973 -1.547  3.487   1.00 12.64 ?  94  HIS   A HA   1 
ATOM   2336 H HB2  . HIS   A 1 94  ? 30.731 -1.078  3.028   1.00 12.27 ?  94  HIS   A HB2  1 
ATOM   2337 H HB3  . HIS   A 1 94  ? 29.573 -0.345  2.227   1.00 12.27 ?  94  HIS   A HB3  1 
ATOM   2338 H HD2  . HIS   A 1 94  ? 31.213 -0.020  5.544   1.00 13.42 ?  94  HIS   A HD2  1 
ATOM   2339 H HE1  . HIS   A 1 94  ? 28.665 2.989   5.251   1.00 12.72 ?  94  HIS   A HE1  1 
ATOM   2340 H HE2  . HIS   A 1 94  ? 30.404 2.038   6.538   1.00 13.19 ?  94  HIS   A HE2  1 
ATOM   2341 N N    A VAL   A 1 95  ? 27.753 -3.246  1.707   0.42 9.90  ?  95  VAL   A N    1 
ATOM   2342 N N    B VAL   A 1 95  ? 27.746 -3.247  1.723   0.58 9.91  ?  95  VAL   A N    1 
ATOM   2343 C CA   A VAL   A 1 95  ? 27.634 -4.308  0.713   0.42 9.73  ?  95  VAL   A CA   1 
ATOM   2344 C CA   B VAL   A 1 95  ? 27.613 -4.260  0.683   0.58 10.07 ?  95  VAL   A CA   1 
ATOM   2345 C C    A VAL   A 1 95  ? 27.079 -3.715  -0.571  0.42 9.30  ?  95  VAL   A C    1 
ATOM   2346 C C    B VAL   A 1 95  ? 27.104 -3.592  -0.583  0.58 10.48 ?  95  VAL   A C    1 
ATOM   2347 O O    A VAL   A 1 95  ? 26.020 -3.077  -0.552  0.42 8.87  ?  95  VAL   A O    1 
ATOM   2348 O O    B VAL   A 1 95  ? 26.190 -2.761  -0.526  0.58 11.27 ?  95  VAL   A O    1 
ATOM   2349 C CB   A VAL   A 1 95  ? 26.723 -5.449  1.204   0.42 9.79  ?  95  VAL   A CB   1 
ATOM   2350 C CB   B VAL   A 1 95  ? 26.661 -5.402  1.108   0.58 10.57 ?  95  VAL   A CB   1 
ATOM   2351 C CG1  A VAL   A 1 95  ? 26.671 -6.555  0.159   0.42 10.81 ?  95  VAL   A CG1  1 
ATOM   2352 C CG1  B VAL   A 1 95  ? 26.517 -6.405  -0.032  0.58 11.62 ?  95  VAL   A CG1  1 
ATOM   2353 C CG2  A VAL   A 1 95  ? 27.203 -5.979  2.537   0.42 10.10 ?  95  VAL   A CG2  1 
ATOM   2354 C CG2  B VAL   A 1 95  ? 27.160 -6.083  2.373   0.58 11.07 ?  95  VAL   A CG2  1 
ATOM   2355 H H    A VAL   A 1 95  ? 27.004 -2.852  1.878   0.42 11.89 ?  95  VAL   A H    1 
ATOM   2356 H H    B VAL   A 1 95  ? 26.995 -2.879  1.935   0.58 11.91 ?  95  VAL   A H    1 
ATOM   2357 H HA   A VAL   A 1 95  ? 28.510 -4.675  0.525   0.42 11.69 ?  95  VAL   A HA   1 
ATOM   2358 H HA   B VAL   A 1 95  ? 28.479 -4.647  0.497   0.58 12.10 ?  95  VAL   A HA   1 
ATOM   2359 H HB   A VAL   A 1 95  ? 25.825 -5.109  1.321   0.42 11.77 ?  95  VAL   A HB   1 
ATOM   2360 H HB   B VAL   A 1 95  ? 25.785 -5.037  1.295   0.58 12.70 ?  95  VAL   A HB   1 
ATOM   2361 H HG11 A VAL   A 1 95  ? 26.261 -7.341  0.552   0.42 12.99 ?  95  VAL   A HG11 1 
ATOM   2362 H HG11 B VAL   A 1 95  ? 26.137 -7.228  0.315   0.58 13.96 ?  95  VAL   A HG11 1 
ATOM   2363 H HG12 A VAL   A 1 95  ? 26.144 -6.255  -0.599  0.42 12.99 ?  95  VAL   A HG12 1 
ATOM   2364 H HG12 B VAL   A 1 95  ? 25.935 -6.034  -0.712  0.58 13.96 ?  95  VAL   A HG12 1 
ATOM   2365 H HG13 A VAL   A 1 95  ? 27.574 -6.764  -0.129  0.42 12.99 ?  95  VAL   A HG13 1 
ATOM   2366 H HG13 B VAL   A 1 95  ? 27.396 -6.585  -0.408  0.58 13.96 ?  95  VAL   A HG13 1 
ATOM   2367 H HG21 A VAL   A 1 95  ? 26.670 -6.753  2.777   0.42 12.13 ?  95  VAL   A HG21 1 
ATOM   2368 H HG21 B VAL   A 1 95  ? 26.570 -6.824  2.588   0.58 13.30 ?  95  VAL   A HG21 1 
ATOM   2369 H HG22 A VAL   A 1 95  ? 28.136 -6.232  2.458   0.42 12.13 ?  95  VAL   A HG22 1 
ATOM   2370 H HG22 B VAL   A 1 95  ? 28.060 -6.414  2.221   0.58 13.30 ?  95  VAL   A HG22 1 
ATOM   2371 H HG23 A VAL   A 1 95  ? 27.102 -5.286  3.204   0.42 12.13 ?  95  VAL   A HG23 1 
ATOM   2372 H HG23 B VAL   A 1 95  ? 27.161 -5.440  3.097   0.58 13.30 ?  95  VAL   A HG23 1 
ATOM   2373 N N    A VAL   A 1 96  ? 27.758 -3.974  -1.687  0.42 9.81  ?  96  VAL   A N    1 
ATOM   2374 N N    B VAL   A 1 96  ? 27.689 -3.959  -1.723  0.58 10.94 ?  96  VAL   A N    1 
ATOM   2375 C CA   A VAL   A 1 96  ? 27.385 -3.418  -2.983  0.42 10.16 ?  96  VAL   A CA   1 
ATOM   2376 C CA   B VAL   A 1 96  ? 27.292 -3.431  -3.024  0.58 11.13 ?  96  VAL   A CA   1 
ATOM   2377 C C    A VAL   A 1 96  ? 26.548 -4.449  -3.737  0.42 10.80 ?  96  VAL   A C    1 
ATOM   2378 C C    B VAL   A 1 96  ? 26.555 -4.519  -3.798  0.58 11.39 ?  96  VAL   A C    1 
ATOM   2379 O O    A VAL   A 1 96  ? 27.080 -5.395  -4.323  0.42 11.51 ?  96  VAL   A O    1 
ATOM   2380 O O    B VAL   A 1 96  ? 27.173 -5.466  -4.299  0.58 12.65 ?  96  VAL   A O    1 
ATOM   2381 C CB   A VAL   A 1 96  ? 28.609 -2.985  -3.793  0.42 10.43 ?  96  VAL   A CB   1 
ATOM   2382 C CB   B VAL   A 1 96  ? 28.491 -2.911  -3.827  0.58 11.32 ?  96  VAL   A CB   1 
ATOM   2383 C CG1  A VAL   A 1 96  ? 28.162 -2.270  -5.053  0.42 11.11 ?  96  VAL   A CG1  1 
ATOM   2384 C CG1  B VAL   A 1 96  ? 28.008 -2.359  -5.156  0.58 11.46 ?  96  VAL   A CG1  1 
ATOM   2385 C CG2  A VAL   A 1 96  ? 29.510 -2.087  -2.964  0.42 10.43 ?  96  VAL   A CG2  1 
ATOM   2386 C CG2  B VAL   A 1 96  ? 29.263 -1.851  -3.044  0.58 11.60 ?  96  VAL   A CG2  1 
ATOM   2387 H H    A VAL   A 1 96  ? 28.456 -4.484  -1.720  0.42 11.79 ?  96  VAL   A H    1 
ATOM   2388 H H    B VAL   A 1 96  ? 28.346 -4.518  -1.764  0.58 13.14 ?  96  VAL   A H    1 
ATOM   2389 H HA   A VAL   A 1 96  ? 26.837 -2.635  -2.841  0.42 12.21 ?  96  VAL   A HA   1 
ATOM   2390 H HA   B VAL   A 1 96  ? 26.683 -2.692  -2.889  0.58 13.37 ?  96  VAL   A HA   1 
ATOM   2391 H HB   A VAL   A 1 96  ? 29.119 -3.767  -4.058  0.42 12.53 ?  96  VAL   A HB   1 
ATOM   2392 H HB   B VAL   A 1 96  ? 29.095 -3.644  -4.011  0.58 13.61 ?  96  VAL   A HB   1 
ATOM   2393 H HG11 A VAL   A 1 96  ? 28.942 -1.892  -5.494  0.42 13.35 ?  96  VAL   A HG11 1 
ATOM   2394 H HG11 B VAL   A 1 96  ? 28.727 -1.840  -5.561  0.58 13.77 ?  96  VAL   A HG11 1 
ATOM   2395 H HG12 A VAL   A 1 96  ? 27.724 -2.899  -5.642  0.42 13.35 ?  96  VAL   A HG12 1 
ATOM   2396 H HG12 B VAL   A 1 96  ? 27.765 -3.090  -5.740  0.58 13.77 ?  96  VAL   A HG12 1 
ATOM   2397 H HG13 A VAL   A 1 96  ? 27.549 -1.556  -4.810  0.42 13.35 ?  96  VAL   A HG13 1 
ATOM   2398 H HG13 B VAL   A 1 96  ? 27.242 -1.782  -5.003  0.58 13.77 ?  96  VAL   A HG13 1 
ATOM   2399 H HG21 A VAL   A 1 96  ? 30.216 -1.741  -3.530  0.42 12.54 ?  96  VAL   A HG21 1 
ATOM   2400 H HG21 B VAL   A 1 96  ? 29.984 -1.513  -3.597  0.58 13.94 ?  96  VAL   A HG21 1 
ATOM   2401 H HG22 A VAL   A 1 96  ? 28.980 -1.356  -2.609  0.42 12.54 ?  96  VAL   A HG22 1 
ATOM   2402 H HG22 B VAL   A 1 96  ? 28.658 -1.129  -2.810  0.58 13.94 ?  96  VAL   A HG22 1 
ATOM   2403 H HG23 A VAL   A 1 96  ? 29.888 -2.607  -2.240  0.42 12.54 ?  96  VAL   A HG23 1 
ATOM   2404 H HG23 B VAL   A 1 96  ? 29.623 -2.255  -2.239  0.58 13.94 ?  96  VAL   A HG23 1 
ATOM   2405 N N    A GLY   A 1 97  ? 25.230 -4.256  -3.744  0.42 10.75 ?  97  GLY   A N    1 
ATOM   2406 N N    B GLY   A 1 97  ? 25.234 -4.381  -3.910  0.58 10.97 ?  97  GLY   A N    1 
ATOM   2407 C CA   A GLY   A 1 97  ? 24.370 -4.988  -4.640  0.42 11.23 ?  97  GLY   A CA   1 
ATOM   2408 C CA   B GLY   A 1 97  ? 24.475 -5.170  -4.847  0.58 11.43 ?  97  GLY   A CA   1 
ATOM   2409 C C    A GLY   A 1 97  ? 24.340 -4.326  -6.004  0.42 11.10 ?  97  GLY   A C    1 
ATOM   2410 C C    B GLY   A 1 97  ? 24.576 -4.608  -6.253  0.58 11.37 ?  97  GLY   A C    1 
ATOM   2411 O O    A GLY   A 1 97  ? 24.595 -3.123  -6.131  0.42 11.07 ?  97  GLY   A O    1 
ATOM   2412 O O    B GLY   A 1 97  ? 24.971 -3.455  -6.455  0.58 12.46 ?  97  GLY   A O    1 
ATOM   2413 H H    A GLY   A 1 97  ? 24.814 -3.694  -3.240  0.42 12.92 ?  97  GLY   A H    1 
ATOM   2414 H H    B GLY   A 1 97  ? 24.759 -3.837  -3.436  0.58 13.18 ?  97  GLY   A H    1 
ATOM   2415 H HA2  A GLY   A 1 97  ? 24.701 -5.891  -4.737  0.42 13.49 ?  97  GLY   A HA2  1 
ATOM   2416 H HA2  B GLY   A 1 97  ? 24.812 -6.078  -4.842  0.58 13.73 ?  97  GLY   A HA2  1 
ATOM   2417 H HA3  A GLY   A 1 97  ? 23.468 -5.018  -4.282  0.42 13.49 ?  97  GLY   A HA3  1 
ATOM   2418 H HA3  B GLY   A 1 97  ? 23.542 -5.181  -4.582  0.58 13.73 ?  97  GLY   A HA3  1 
ATOM   2419 N N    A PRO   A 1 98  ? 24.028 -5.090  -7.052  0.42 11.08 ?  98  PRO   A N    1 
ATOM   2420 N N    B PRO   A 1 98  ? 24.225 -5.412  -7.254  0.58 11.87 ?  98  PRO   A N    1 
ATOM   2421 C CA   A PRO   A 1 98  ? 23.942 -4.492  -8.388  0.42 11.73 ?  98  PRO   A CA   1 
ATOM   2422 C CA   B PRO   A 1 98  ? 24.230 -4.912  -8.632  0.58 13.14 ?  98  PRO   A CA   1 
ATOM   2423 C C    A PRO   A 1 98  ? 22.829 -3.458  -8.462  0.42 11.88 ?  98  PRO   A C    1 
ATOM   2424 C C    B PRO   A 1 98  ? 23.157 -3.858  -8.846  0.58 13.60 ?  98  PRO   A C    1 
ATOM   2425 O O    A PRO   A 1 98  ? 21.744 -3.641  -7.903  0.42 11.99 ?  98  PRO   A O    1 
ATOM   2426 O O    B PRO   A 1 98  ? 22.051 -3.938  -8.304  0.58 14.45 ?  98  PRO   A O    1 
ATOM   2427 C CB   A PRO   A 1 98  ? 23.651 -5.691  -9.297  0.42 11.91 ?  98  PRO   A CB   1 
ATOM   2428 C CB   B PRO   A 1 98  ? 23.953 -6.170  -9.467  0.58 13.73 ?  98  PRO   A CB   1 
ATOM   2429 C CG   A PRO   A 1 98  ? 23.021 -6.709  -8.401  0.42 11.68 ?  98  PRO   A CG   1 
ATOM   2430 C CG   B PRO   A 1 98  ? 23.244 -7.095  -8.531  0.58 13.79 ?  98  PRO   A CG   1 
ATOM   2431 C CD   A PRO   A 1 98  ? 23.704 -6.529  -7.068  0.42 11.27 ?  98  PRO   A CD   1 
ATOM   2432 C CD   B PRO   A 1 98  ? 23.867 -6.839  -7.184  0.58 12.97 ?  98  PRO   A CD   1 
ATOM   2433 H HA   A PRO   A 1 98  ? 24.785 -4.092  -8.635  0.42 14.10 ?  98  PRO   A HA   1 
ATOM   2434 H HA   B PRO   A 1 98  ? 25.100 -4.548  -8.858  0.58 15.79 ?  98  PRO   A HA   1 
ATOM   2435 H HB2  A PRO   A 1 98  ? 23.037 -5.433  -10.002 0.42 14.31 ?  98  PRO   A HB2  1 
ATOM   2436 H HB2  B PRO   A 1 98  ? 23.389 -5.939  -10.218 0.58 16.50 ?  98  PRO   A HB2  1 
ATOM   2437 H HB3  A PRO   A 1 98  ? 24.479 -6.033  -9.670  0.42 14.31 ?  98  PRO   A HB3  1 
ATOM   2438 H HB3  B PRO   A 1 98  ? 24.792 -6.552  -9.763  0.58 16.50 ?  98  PRO   A HB3  1 
ATOM   2439 H HG2  A PRO   A 1 98  ? 22.069 -6.536  -8.326  0.42 14.03 ?  98  PRO   A HG2  1 
ATOM   2440 H HG2  B PRO   A 1 98  ? 22.296 -6.885  -8.513  0.58 16.56 ?  98  PRO   A HG2  1 
ATOM   2441 H HG3  A PRO   A 1 98  ? 23.179 -7.601  -8.752  0.42 14.03 ?  98  PRO   A HG3  1 
ATOM   2442 H HG3  B PRO   A 1 98  ? 23.388 -8.014  -8.806  0.58 16.56 ?  98  PRO   A HG3  1 
ATOM   2443 H HD2  A PRO   A 1 98  ? 23.099 -6.760  -6.341  0.42 13.54 ?  98  PRO   A HD2  1 
ATOM   2444 H HD2  B PRO   A 1 98  ? 23.226 -6.995  -6.469  0.58 15.58 ?  98  PRO   A HD2  1 
ATOM   2445 H HD3  A PRO   A 1 98  ? 24.519 -7.057  -7.027  0.42 13.54 ?  98  PRO   A HD3  1 
ATOM   2446 H HD3  B PRO   A 1 98  ? 24.666 -7.383  -7.063  0.58 15.58 ?  98  PRO   A HD3  1 
ATOM   2447 N N    A ASN   A 1 99  ? 23.118 -2.355  -9.149  0.42 13.20 ?  99  ASN   A N    1 
ATOM   2448 N N    B ASN   A 1 99  ? 23.505 -2.855  -9.643  0.58 14.67 ?  99  ASN   A N    1 
ATOM   2449 C CA   A ASN   A 1 99  ? 22.146 -1.293  -9.392  0.42 14.29 ?  99  ASN   A CA   1 
ATOM   2450 C CA   B ASN   A 1 99  ? 22.587 -1.803  -10.070 0.58 16.60 ?  99  ASN   A CA   1 
ATOM   2451 C C    A ASN   A 1 99  ? 21.597 -1.485  -10.801 0.42 15.07 ?  99  ASN   A C    1 
ATOM   2452 C C    B ASN   A 1 99  ? 22.073 -2.200  -11.450 0.58 17.39 ?  99  ASN   A C    1 
ATOM   2453 O O    A ASN   A 1 99  ? 22.275 -1.188  -11.789 0.42 16.32 ?  99  ASN   A O    1 
ATOM   2454 O O    B ASN   A 1 99  ? 22.735 -1.964  -12.465 0.58 16.44 ?  99  ASN   A O    1 
ATOM   2455 C CB   A ASN   A 1 99  ? 22.796 0.079   -9.240  0.42 14.84 ?  99  ASN   A CB   1 
ATOM   2456 C CB   B ASN   A 1 99  ? 23.319 -0.467  -10.124 0.58 18.54 ?  99  ASN   A CB   1 
ATOM   2457 C CG   A ASN   A 1 99  ? 21.774 1.214   -9.180  0.42 15.65 ?  99  ASN   A CG   1 
ATOM   2458 C CG   B ASN   A 1 99  ? 22.407 0.689   -10.482 0.58 20.55 ?  99  ASN   A CG   1 
ATOM   2459 O OD1  A ASN   A 1 99  ? 20.752 1.192   -9.868  0.42 15.93 ?  99  ASN   A OD1  1 
ATOM   2460 O OD1  B ASN   A 1 99  ? 21.273 0.494   -10.920 0.58 20.35 ?  99  ASN   A OD1  1 
ATOM   2461 N ND2  A ASN   A 1 99  ? 22.054 2.211   -8.352  0.42 16.33 ?  99  ASN   A ND2  1 
ATOM   2462 N ND2  B ASN   A 1 99  ? 22.903 1.906   -10.295 0.58 22.62 ?  99  ASN   A ND2  1 
ATOM   2463 H H    A ASN   A 1 99  ? 23.895 -2.192  -9.474  0.42 15.86 ?  99  ASN   A H    1 
ATOM   2464 H H    B ASN   A 1 99  ? 24.298 -2.760  -9.958  0.58 17.62 ?  99  ASN   A H    1 
ATOM   2465 H HA   A ASN   A 1 99  ? 21.414 -1.369  -8.760  0.42 17.16 ?  99  ASN   A HA   1 
ATOM   2466 H HA   B ASN   A 1 99  ? 21.838 -1.737  -9.452  0.58 19.93 ?  99  ASN   A HA   1 
ATOM   2467 H HB2  A ASN   A 1 99  ? 23.316 0.093   -8.426  0.42 17.83 ?  99  ASN   A HB2  1 
ATOM   2468 H HB2  B ASN   A 1 99  ? 23.705 -0.285  -9.254  0.58 22.26 ?  99  ASN   A HB2  1 
ATOM   2469 H HB3  A ASN   A 1 99  ? 23.375 0.233   -10.007 0.42 17.83 ?  99  ASN   A HB3  1 
ATOM   2470 H HB3  B ASN   A 1 99  ? 24.021 -0.522  -10.789 0.58 22.26 ?  99  ASN   A HB3  1 
ATOM   2471 H HD21 A ASN   A 1 99  ? 21.514 2.873   -8.281  0.42 19.61 ?  99  ASN   A HD21 1 
ATOM   2472 H HD21 B ASN   A 1 99  ? 22.429 2.599   -10.482 0.58 27.16 ?  99  ASN   A HD21 1 
ATOM   2473 H HD22 A ASN   A 1 99  ? 22.778 2.192   -7.887  0.42 19.61 ?  99  ASN   A HD22 1 
ATOM   2474 H HD22 B ASN   A 1 99  ? 23.705 2.003   -9.999  0.58 27.16 ?  99  ASN   A HD22 1 
ATOM   2475 N N    A VAL   A 1 100 ? 20.362 -1.989  -10.887 0.42 15.91 ?  100 VAL   A N    1 
ATOM   2476 N N    B VAL   A 1 100 ? 20.890 -2.816  -11.485 0.58 20.84 ?  100 VAL   A N    1 
ATOM   2477 C CA   A VAL   A 1 100 ? 19.729 -2.230  -12.181 0.42 18.46 ?  100 VAL   A CA   1 
ATOM   2478 C CA   B VAL   A 1 100 ? 20.329 -3.270  -12.754 0.58 24.68 ?  100 VAL   A CA   1 
ATOM   2479 C C    A VAL   A 1 100 ? 19.637 -0.940  -12.983 0.42 19.69 ?  100 VAL   A C    1 
ATOM   2480 C C    B VAL   A 1 100 ? 20.040 -2.097  -13.682 0.58 26.08 ?  100 VAL   A C    1 
ATOM   2481 O O    A VAL   A 1 100 ? 19.744 -0.955  -14.215 0.42 20.90 ?  100 VAL   A O    1 
ATOM   2482 O O    B VAL   A 1 100 ? 20.037 -2.253  -14.909 0.58 25.80 ?  100 VAL   A O    1 
ATOM   2483 C CB   A VAL   A 1 100 ? 18.350 -2.903  -11.984 0.42 19.43 ?  100 VAL   A CB   1 
ATOM   2484 C CB   B VAL   A 1 100 ? 19.087 -4.143  -12.497 0.58 27.02 ?  100 VAL   A CB   1 
ATOM   2485 C CG1  A VAL   A 1 100 ? 17.643 -3.112  -13.318 0.42 20.05 ?  100 VAL   A CG1  1 
ATOM   2486 C CG1  B VAL   A 1 100 ? 18.245 -4.274  -13.756 0.58 27.75 ?  100 VAL   A CG1  1 
ATOM   2487 C CG2  A VAL   A 1 100 ? 18.510 -4.233  -11.258 0.42 19.70 ?  100 VAL   A CG2  1 
ATOM   2488 C CG2  B VAL   A 1 100 ? 19.514 -5.509  -11.998 0.58 28.01 ?  100 VAL   A CG2  1 
ATOM   2489 H H    A VAL   A 1 100 ? 19.866 -2.196  -10.213 0.42 19.11 ?  100 VAL   A H    1 
ATOM   2490 H H    B VAL   A 1 100 ? 20.403 -2.983  -10.795 0.58 25.02 ?  100 VAL   A H    1 
ATOM   2491 H HA   A VAL   A 1 100 ? 20.275 -2.848  -12.689 0.42 22.17 ?  100 VAL   A HA   1 
ATOM   2492 H HA   B VAL   A 1 100 ? 20.989 -3.831  -13.190 0.58 29.63 ?  100 VAL   A HA   1 
ATOM   2493 H HB   A VAL   A 1 100 ? 17.789 -2.333  -11.437 0.42 23.33 ?  100 VAL   A HB   1 
ATOM   2494 H HB   B VAL   A 1 100 ? 18.542 -3.725  -11.813 0.58 32.44 ?  100 VAL   A HB   1 
ATOM   2495 H HG11 A VAL   A 1 100 ? 16.876 -3.694  -13.184 0.42 24.07 ?  100 VAL   A HG11 1 
ATOM   2496 H HG11 B VAL   A 1 100 ? 17.600 -4.986  -13.624 0.58 33.32 ?  100 VAL   A HG11 1 
ATOM   2497 H HG12 A VAL   A 1 100 ? 17.347 -2.254  -13.659 0.42 24.07 ?  100 VAL   A HG12 1 
ATOM   2498 H HG12 B VAL   A 1 100 ? 17.779 -3.438  -13.919 0.58 33.32 ?  100 VAL   A HG12 1 
ATOM   2499 H HG13 A VAL   A 1 100 ? 18.260 -3.523  -13.943 0.42 24.07 ?  100 VAL   A HG13 1 
ATOM   2500 H HG13 B VAL   A 1 100 ? 18.823 -4.486  -14.504 0.58 33.32 ?  100 VAL   A HG13 1 
ATOM   2501 H HG21 A VAL   A 1 100 ? 17.646 -4.675  -11.209 0.42 23.66 ?  100 VAL   A HG21 1 
ATOM   2502 H HG21 B VAL   A 1 100 ? 18.723 -6.054  -11.864 0.58 33.62 ?  100 VAL   A HG21 1 
ATOM   2503 H HG22 A VAL   A 1 100 ? 19.136 -4.788  -11.749 0.42 23.66 ?  100 VAL   A HG22 1 
ATOM   2504 H HG22 B VAL   A 1 100 ? 20.091 -5.922  -12.661 0.58 33.62 ?  100 VAL   A HG22 1 
ATOM   2505 H HG23 A VAL   A 1 100 ? 18.846 -4.066  -10.364 0.42 23.66 ?  100 VAL   A HG23 1 
ATOM   2506 H HG23 B VAL   A 1 100 ? 19.992 -5.406  -11.161 0.58 33.62 ?  100 VAL   A HG23 1 
ATOM   2507 N N    A ASN   A 1 101 ? 19.443 0.192   -12.308 0.42 20.43 ?  101 ASN   A N    1 
ATOM   2508 N N    B ASN   A 1 101 ? 19.785 -0.913  -13.126 0.58 26.93 ?  101 ASN   A N    1 
ATOM   2509 C CA   A ASN   A 1 101 ? 19.367 1.476   -12.995 0.42 21.96 ?  101 ASN   A CA   1 
ATOM   2510 C CA   B ASN   A 1 101 ? 19.631 0.269   -13.966 0.58 28.20 ?  101 ASN   A CA   1 
ATOM   2511 C C    A ASN   A 1 101 ? 20.713 1.931   -13.548 0.42 23.19 ?  101 ASN   A C    1 
ATOM   2512 C C    B ASN   A 1 101 ? 20.955 0.748   -14.551 0.58 29.12 ?  101 ASN   A C    1 
ATOM   2513 O O    A ASN   A 1 101 ? 20.765 2.966   -14.225 0.42 23.90 ?  101 ASN   A O    1 
ATOM   2514 O O    B ASN   A 1 101 ? 20.941 1.582   -15.463 0.58 29.63 ?  101 ASN   A O    1 
ATOM   2515 C CB   A ASN   A 1 101 ? 18.773 2.531   -12.060 0.42 22.12 ?  101 ASN   A CB   1 
ATOM   2516 C CB   B ASN   A 1 101 ? 18.941 1.387   -13.182 0.58 28.95 ?  101 ASN   A CB   1 
ATOM   2517 C CG   A ASN   A 1 101 ? 17.407 2.132   -11.530 0.42 22.50 ?  101 ASN   A CG   1 
ATOM   2518 C CG   B ASN   A 1 101 ? 17.546 0.999   -12.717 0.58 29.38 ?  101 ASN   A CG   1 
ATOM   2519 O OD1  A ASN   A 1 101 ? 16.562 1.624   -12.273 0.42 22.45 ?  101 ASN   A OD1  1 
ATOM   2520 O OD1  B ASN   A 1 101 ? 16.853 0.215   -13.367 0.58 29.72 ?  101 ASN   A OD1  1 
ATOM   2521 N ND2  A ASN   A 1 101 ? 17.186 2.354   -10.239 0.42 22.96 ?  101 ASN   A ND2  1 
ATOM   2522 N ND2  B ASN   A 1 101 ? 17.129 1.549   -11.589 0.58 29.52 ?  101 ASN   A ND2  1 
ATOM   2523 H H    A ASN   A 1 101 ? 19.345 0.238   -11.456 0.42 24.53 ?  101 ASN   A H    1 
ATOM   2524 H H    B ASN   A 1 101 ? 19.680 -0.774  -12.285 0.58 32.34 ?  101 ASN   A H    1 
ATOM   2525 H HA   A ASN   A 1 101 ? 18.762 1.384   -13.746 0.42 26.37 ?  101 ASN   A HA   1 
ATOM   2526 H HA   B ASN   A 1 101 ? 19.060 0.043   -14.713 0.58 33.86 ?  101 ASN   A HA   1 
ATOM   2527 H HB2  A ASN   A 1 101 ? 19.367 2.657   -11.305 0.42 26.56 ?  101 ASN   A HB2  1 
ATOM   2528 H HB2  B ASN   A 1 101 ? 19.468 1.603   -12.399 0.58 34.75 ?  101 ASN   A HB2  1 
ATOM   2529 H HB3  A ASN   A 1 101 ? 18.672 3.363   -12.548 0.42 26.56 ?  101 ASN   A HB3  1 
ATOM   2530 H HB3  B ASN   A 1 101 ? 18.856 2.164   -13.755 0.58 34.75 ?  101 ASN   A HB3  1 
ATOM   2531 H HD21 A ASN   A 1 101 ? 16.430 2.140   -9.889  0.42 27.56 ?  101 ASN   A HD21 1 
ATOM   2532 H HD21 B ASN   A 1 101 ? 16.346 1.362   -11.288 0.58 35.44 ?  101 ASN   A HD21 1 
ATOM   2533 H HD22 A ASN   A 1 101 ? 17.798 2.713   -9.752  0.42 27.56 ?  101 ASN   A HD22 1 
ATOM   2534 H HD22 B ASN   A 1 101 ? 17.635 2.098   -11.168 0.58 35.44 ?  101 ASN   A HD22 1 
ATOM   2535 N N    A LYS   A 1 102 ? 21.791 1.192   -13.281 0.42 24.39 ?  102 LYS   A N    1 
ATOM   2536 N N    B LYS   A 1 102 ? 22.085 0.245   -14.052 0.58 29.64 ?  102 LYS   A N    1 
ATOM   2537 C CA   A LYS   A 1 102 ? 23.074 1.397   -13.939 0.42 25.34 ?  102 LYS   A CA   1 
ATOM   2538 C CA   B LYS   A 1 102 ? 23.398 0.465   -14.649 0.58 29.43 ?  102 LYS   A CA   1 
ATOM   2539 C C    A LYS   A 1 102 ? 23.389 0.305   -14.950 0.42 25.38 ?  102 LYS   A C    1 
ATOM   2540 C C    B LYS   A 1 102 ? 23.800 -0.654  -15.603 0.58 26.20 ?  102 LYS   A C    1 
ATOM   2541 O O    A LYS   A 1 102 ? 24.466 0.335   -15.556 0.42 26.24 ?  102 LYS   A O    1 
ATOM   2542 O O    B LYS   A 1 102 ? 24.934 -0.655  -16.092 0.58 26.72 ?  102 LYS   A O    1 
ATOM   2543 C CB   A LYS   A 1 102 ? 24.205 1.461   -12.906 0.42 26.39 ?  102 LYS   A CB   1 
ATOM   2544 C CB   B LYS   A 1 102 ? 24.473 0.555   -13.557 0.58 32.86 ?  102 LYS   A CB   1 
ATOM   2545 C CG   A LYS   A 1 102 ? 24.061 2.564   -11.877 0.42 26.96 ?  102 LYS   A CG   1 
ATOM   2546 C CG   B LYS   A 1 102 ? 24.753 1.940   -13.002 0.58 35.84 ?  102 LYS   A CG   1 
ATOM   2547 C CD   A LYS   A 1 102 ? 25.198 2.503   -10.869 0.42 27.82 ?  102 LYS   A CD   1 
ATOM   2548 C CD   B LYS   A 1 102 ? 26.106 1.948   -12.292 0.58 38.41 ?  102 LYS   A CD   1 
ATOM   2549 C CE   A LYS   A 1 102 ? 25.095 3.606   -9.833  0.42 28.58 ?  102 LYS   A CE   1 
ATOM   2550 C CE   B LYS   A 1 102 ? 26.262 3.131   -11.353 0.58 40.48 ?  102 LYS   A CE   1 
ATOM   2551 N NZ   A LYS   A 1 102 ? 26.133 3.455   -8.772  0.42 28.98 ?  102 LYS   A NZ   1 
ATOM   2552 N NZ   B LYS   A 1 102 ? 26.312 2.691   -9.928  0.58 41.55 ?  102 LYS   A NZ   1 
ATOM   2553 H H    A LYS   A 1 102 ? 21.803 0.549   -12.709 0.42 29.29 ?  102 LYS   A H    1 
ATOM   2554 H H    B LYS   A 1 102 ? 22.114 -0.244  -13.345 0.58 35.58 ?  102 LYS   A H    1 
ATOM   2555 H HA   A LYS   A 1 102 ? 23.056 2.238   -14.414 0.42 30.43 ?  102 LYS   A HA   1 
ATOM   2556 H HA   B LYS   A 1 102 ? 23.394 1.304   -15.133 0.58 35.33 ?  102 LYS   A HA   1 
ATOM   2557 H HB2  A LYS   A 1 102 ? 24.239 0.616   -12.430 0.42 31.69 ?  102 LYS   A HB2  1 
ATOM   2558 H HB2  B LYS   A 1 102 ? 24.200 -0.003  -12.815 0.58 39.45 ?  102 LYS   A HB2  1 
ATOM   2559 H HB3  A LYS   A 1 102 ? 25.043 1.603   -13.375 0.42 31.69 ?  102 LYS   A HB3  1 
ATOM   2560 H HB3  B LYS   A 1 102 ? 25.309 0.221   -13.917 0.58 39.45 ?  102 LYS   A HB3  1 
ATOM   2561 H HG2  A LYS   A 1 102 ? 24.089 3.426   -12.321 0.42 32.37 ?  102 LYS   A HG2  1 
ATOM   2562 H HG2  B LYS   A 1 102 ? 24.788 2.579   -13.728 0.58 43.03 ?  102 LYS   A HG2  1 
ATOM   2563 H HG3  A LYS   A 1 102 ? 23.222 2.455   -11.402 0.42 32.37 ?  102 LYS   A HG3  1 
ATOM   2564 H HG3  B LYS   A 1 102 ? 24.066 2.189   -12.367 0.58 43.03 ?  102 LYS   A HG3  1 
ATOM   2565 H HD2  A LYS   A 1 102 ? 25.169 1.649   -10.408 0.42 33.40 ?  102 LYS   A HD2  1 
ATOM   2566 H HD2  B LYS   A 1 102 ? 26.198 1.135   -11.770 0.58 46.11 ?  102 LYS   A HD2  1 
ATOM   2567 H HD3  A LYS   A 1 102 ? 26.043 2.601   -11.336 0.42 33.40 ?  102 LYS   A HD3  1 
ATOM   2568 H HD3  B LYS   A 1 102 ? 26.812 1.997   -12.957 0.58 46.11 ?  102 LYS   A HD3  1 
ATOM   2569 H HE2  A LYS   A 1 102 ? 25.225 4.464   -10.267 0.42 34.31 ?  102 LYS   A HE2  1 
ATOM   2570 H HE2  B LYS   A 1 102 ? 27.089 3.597   -11.557 0.58 48.60 ?  102 LYS   A HE2  1 
ATOM   2571 H HE3  A LYS   A 1 102 ? 24.222 3.570   -9.413  0.42 34.31 ?  102 LYS   A HE3  1 
ATOM   2572 H HE3  B LYS   A 1 102 ? 25.506 3.728   -11.460 0.58 48.60 ?  102 LYS   A HE3  1 
ATOM   2573 H HZ1  A LYS   A 1 102 ? 26.056 4.111   -8.177  0.42 34.79 ?  102 LYS   A HZ1  1 
ATOM   2574 H HZ1  B LYS   A 1 102 ? 26.345 3.400   -9.391  0.58 49.87 ?  102 LYS   A HZ1  1 
ATOM   2575 H HZ2  A LYS   A 1 102 ? 26.032 2.674   -8.358  0.42 34.79 ?  102 LYS   A HZ2  1 
ATOM   2576 H HZ2  B LYS   A 1 102 ? 25.588 2.213   -9.732  0.58 49.87 ?  102 LYS   A HZ2  1 
ATOM   2577 H HZ3  A LYS   A 1 102 ? 26.945 3.488   -9.136  0.42 34.79 ?  102 LYS   A HZ3  1 
ATOM   2578 H HZ3  B LYS   A 1 102 ? 27.035 2.190   -9.790  0.58 49.87 ?  102 LYS   A HZ3  1 
ATOM   2579 N N    A GLY   A 1 103 ? 22.489 -0.658  -15.142 0.42 25.74 ?  103 GLY   A N    1 
ATOM   2580 N N    B GLY   A 1 103 ? 22.922 -1.618  -15.858 0.58 23.12 ?  103 GLY   A N    1 
ATOM   2581 C CA   A GLY   A 1 103 ? 22.734 -1.757  -16.053 0.42 25.96 ?  103 GLY   A CA   1 
ATOM   2582 C CA   B GLY   A 1 103 ? 23.287 -2.760  -16.674 0.58 22.12 ?  103 GLY   A CA   1 
ATOM   2583 C C    A GLY   A 1 103 ? 23.616 -2.851  -15.499 0.42 26.15 ?  103 GLY   A C    1 
ATOM   2584 C C    B GLY   A 1 103 ? 24.081 -3.829  -15.952 0.58 20.97 ?  103 GLY   A C    1 
ATOM   2585 O O    A GLY   A 1 103 ? 24.224 -3.592  -16.277 0.42 26.98 ?  103 GLY   A O    1 
ATOM   2586 O O    B GLY   A 1 103 ? 24.619 -4.733  -16.604 0.58 21.83 ?  103 GLY   A O    1 
ATOM   2587 H H    A GLY   A 1 103 ? 21.726 -0.698  -14.750 0.42 30.91 ?  103 GLY   A H    1 
ATOM   2588 H H    B GLY   A 1 103 ? 22.113 -1.627  -15.565 0.58 27.77 ?  103 GLY   A H    1 
ATOM   2589 H HA2  A GLY   A 1 103 ? 21.881 -2.140  -16.331 0.42 31.17 ?  103 GLY   A HA2  1 
ATOM   2590 H HA2  B GLY   A 1 103 ? 22.479 -3.170  -17.007 0.58 26.56 ?  103 GLY   A HA2  1 
ATOM   2591 H HA3  A GLY   A 1 103 ? 23.177 -1.415  -16.842 0.42 31.17 ?  103 GLY   A HA3  1 
ATOM   2592 H HA3  B GLY   A 1 103 ? 23.801 -2.440  -17.436 0.58 26.56 ?  103 GLY   A HA3  1 
ATOM   2593 N N    A GLU   A 1 104 ? 23.718 -2.970  -14.179 0.42 25.20 ?  104 GLU   A N    1 
ATOM   2594 N N    B GLU   A 1 104 ? 24.161 -3.767  -14.629 0.58 19.37 ?  104 GLU   A N    1 
ATOM   2595 C CA   A GLU   A 1 104 ? 24.594 -3.962  -13.571 0.42 24.38 ?  104 GLU   A CA   1 
ATOM   2596 C CA   B GLU   A 1 104 ? 24.983 -4.703  -13.874 0.58 18.28 ?  104 GLU   A CA   1 
ATOM   2597 C C    A GLU   A 1 104 ? 23.905 -5.321  -13.469 0.42 24.91 ?  104 GLU   A C    1 
ATOM   2598 C C    B GLU   A 1 104 ? 24.255 -6.031  -13.692 0.58 18.88 ?  104 GLU   A C    1 
ATOM   2599 O O    A GLU   A 1 104 ? 22.687 -5.417  -13.298 0.42 25.30 ?  104 GLU   A O    1 
ATOM   2600 O O    B GLU   A 1 104 ? 23.025 -6.084  -13.594 0.58 20.08 ?  104 GLU   A O    1 
ATOM   2601 C CB   A GLU   A 1 104 ? 25.073 -3.471  -12.203 0.42 23.07 ?  104 GLU   A CB   1 
ATOM   2602 C CB   B GLU   A 1 104 ? 25.398 -4.084  -12.536 0.58 17.94 ?  104 GLU   A CB   1 
ATOM   2603 C CG   A GLU   A 1 104 ? 25.961 -2.226  -12.333 0.42 22.47 ?  104 GLU   A CG   1 
ATOM   2604 C CG   B GLU   A 1 104 ? 26.244 -2.822  -12.740 0.58 18.72 ?  104 GLU   A CG   1 
ATOM   2605 C CD   A GLU   A 1 104 ? 26.295 -1.527  -11.021 0.42 21.56 ?  104 GLU   A CD   1 
ATOM   2606 C CD   B GLU   A 1 104 ? 26.642 -2.102  -11.465 0.58 18.99 ?  104 GLU   A CD   1 
ATOM   2607 O OE1  A GLU   A 1 104 ? 25.736 -1.888  -9.967  0.42 20.20 ?  104 GLU   A OE1  1 
ATOM   2608 O OE1  B GLU   A 1 104 ? 26.097 -2.410  -10.392 0.58 19.18 ?  104 GLU   A OE1  1 
ATOM   2609 O OE2  A GLU   A 1 104 ? 27.117 -0.583  -11.061 0.42 21.70 -1 104 GLU   A OE2  1 
ATOM   2610 O OE2  B GLU   A 1 104 ? 27.499 -1.192  -11.553 0.58 19.69 -1 104 GLU   A OE2  1 
ATOM   2611 H H    A GLU   A 1 104 ? 23.299 -2.478  -13.615 0.42 30.26 ?  104 GLU   A H    1 
ATOM   2612 H H    B GLU   A 1 104 ? 23.744 -3.191  -14.145 0.58 23.26 ?  104 GLU   A H    1 
ATOM   2613 H HA   A GLU   A 1 104 ? 25.370 -4.073  -14.138 0.42 29.27 ?  104 GLU   A HA   1 
ATOM   2614 H HA   B GLU   A 1 104 ? 25.793 -4.878  -14.382 0.58 21.96 ?  104 GLU   A HA   1 
ATOM   2615 H HB2  A GLU   A 1 104 ? 24.302 -3.248  -11.660 0.42 27.70 ?  104 GLU   A HB2  1 
ATOM   2616 H HB2  B GLU   A 1 104 ? 24.606 -3.844  -12.037 0.58 21.55 ?  104 GLU   A HB2  1 
ATOM   2617 H HB3  A GLU   A 1 104 ? 25.588 -4.177  -11.781 0.42 27.70 ?  104 GLU   A HB3  1 
ATOM   2618 H HB3  B GLU   A 1 104 ? 25.929 -4.728  -12.042 0.58 21.55 ?  104 GLU   A HB3  1 
ATOM   2619 H HG2  A GLU   A 1 104 ? 26.792 -2.491  -12.753 0.42 26.98 ?  104 GLU   A HG2  1 
ATOM   2620 H HG2  B GLU   A 1 104 ? 27.053 -3.063  -13.215 0.58 22.48 ?  104 GLU   A HG2  1 
ATOM   2621 H HG3  A GLU   A 1 104 ? 25.499 -1.581  -12.887 0.42 26.98 ?  104 GLU   A HG3  1 
ATOM   2622 H HG3  B GLU   A 1 104 ? 25.732 -2.187  -13.263 0.58 22.48 ?  104 GLU   A HG3  1 
ATOM   2623 N N    A ASP   A 1 105 ? 24.712 -6.375  -13.579 0.42 25.19 ?  105 ASP   A N    1 
ATOM   2624 N N    B ASP   A 1 105 ? 25.038 -7.112  -13.668 0.58 18.72 ?  105 ASP   A N    1 
ATOM   2625 C CA   A ASP   A 1 105 ? 24.207 -7.741  -13.677 0.42 25.73 ?  105 ASP   A CA   1 
ATOM   2626 C CA   B ASP   A 1 105 ? 24.501 -8.469  -13.737 0.58 19.71 ?  105 ASP   A CA   1 
ATOM   2627 C C    A ASP   A 1 105 ? 23.514 -8.146  -12.378 0.42 24.43 ?  105 ASP   A C    1 
ATOM   2628 C C    B ASP   A 1 105 ? 23.752 -8.825  -12.456 0.58 17.62 ?  105 ASP   A C    1 
ATOM   2629 O O    A ASP   A 1 105 ? 24.122 -8.108  -11.303 0.42 24.66 ?  105 ASP   A O    1 
ATOM   2630 O O    B ASP   A 1 105 ? 24.311 -8.769  -11.357 0.58 15.61 ?  105 ASP   A O    1 
ATOM   2631 C CB   A ASP   A 1 105 ? 25.379 -8.676  -13.972 0.42 27.39 ?  105 ASP   A CB   1 
ATOM   2632 C CB   B ASP   A 1 105 ? 25.652 -9.445  -13.969 0.58 22.62 ?  105 ASP   A CB   1 
ATOM   2633 C CG   A ASP   A 1 105 ? 24.935 -10.088 -14.276 0.42 28.88 ?  105 ASP   A CG   1 
ATOM   2634 C CG   B ASP   A 1 105 ? 25.204 -10.891 -14.028 0.58 25.37 ?  105 ASP   A CG   1 
ATOM   2635 O OD1  A ASP   A 1 105 ? 23.712 -10.324 -14.354 0.42 29.42 ?  105 ASP   A OD1  1 
ATOM   2636 O OD1  B ASP   A 1 105 ? 23.985 -11.152 -14.072 0.58 25.31 ?  105 ASP   A OD1  1 
ATOM   2637 O OD2  A ASP   A 1 105 ? 25.814 -10.960 -14.444 0.42 29.74 -1 105 ASP   A OD2  1 
ATOM   2638 O OD2  B ASP   A 1 105 ? 26.090 -11.773 -14.031 0.58 27.53 -1 105 ASP   A OD2  1 
ATOM   2639 H H    A ASP   A 1 105 ? 25.569 -6.327  -13.598 0.42 30.24 ?  105 ASP   A H    1 
ATOM   2640 H H    B ASP   A 1 105 ? 25.897 -7.082  -13.621 0.58 22.48 ?  105 ASP   A H    1 
ATOM   2641 H HA   A ASP   A 1 105 ? 23.570 -7.813  -14.406 0.42 30.89 ?  105 ASP   A HA   1 
ATOM   2642 H HA   B ASP   A 1 105 ? 23.884 -8.535  -14.484 0.58 23.66 ?  105 ASP   A HA   1 
ATOM   2643 H HB2  A ASP   A 1 105 ? 25.862 -8.351  -14.751 0.42 32.89 ?  105 ASP   A HB2  1 
ATOM   2644 H HB2  B ASP   A 1 105 ? 26.084 -9.234  -14.812 0.58 27.16 ?  105 ASP   A HB2  1 
ATOM   2645 H HB3  A ASP   A 1 105 ? 25.974 -8.698  -13.204 0.42 32.89 ?  105 ASP   A HB3  1 
ATOM   2646 H HB3  B ASP   A 1 105 ? 26.284 -9.369  -13.242 0.58 27.16 ?  105 ASP   A HB3  1 
ATOM   2647 N N    A ILE   A 1 106 ? 22.240 -8.540  -12.478 0.42 22.78 ?  106 ILE   A N    1 
ATOM   2648 N N    B ILE   A 1 106 ? 22.490 -9.230  -12.612 0.58 19.25 ?  106 ILE   A N    1 
ATOM   2649 C CA   A ILE   A 1 106 ? 21.484 -8.959  -11.302 0.42 21.66 ?  106 ILE   A CA   1 
ATOM   2650 C CA   B ILE   A 1 106 ? 21.665 -9.597  -11.467 0.58 20.51 ?  106 ILE   A CA   1 
ATOM   2651 C C    A ILE   A 1 106 ? 22.023 -10.255 -10.715 0.42 21.80 ?  106 ILE   A C    1 
ATOM   2652 C C    B ILE   A 1 106 ? 22.272 -10.762 -10.702 0.58 19.98 ?  106 ILE   A C    1 
ATOM   2653 O O    A ILE   A 1 106 ? 21.794 -10.538 -9.533  0.42 20.89 ?  106 ILE   A O    1 
ATOM   2654 O O    B ILE   A 1 106 ? 22.047 -10.901 -9.493  0.58 19.28 ?  106 ILE   A O    1 
ATOM   2655 C CB   A ILE   A 1 106 ? 19.979 -9.081  -11.626 0.42 21.64 ?  106 ILE   A CB   1 
ATOM   2656 C CB   B ILE   A 1 106 ? 20.235 -9.914  -11.943 0.58 22.53 ?  106 ILE   A CB   1 
ATOM   2657 C CG1  A ILE   A 1 106 ? 19.149 -9.106  -10.341 0.42 21.98 ?  106 ILE   A CG1  1 
ATOM   2658 C CG1  B ILE   A 1 106 ? 19.268 -9.953  -10.760 0.58 23.58 ?  106 ILE   A CG1  1 
ATOM   2659 C CG2  A ILE   A 1 106 ? 19.698 -10.351 -12.410 0.42 21.60 ?  106 ILE   A CG2  1 
ATOM   2660 C CG2  B ILE   A 1 106 ? 20.208 -11.248 -12.672 0.58 23.22 ?  106 ILE   A CG2  1 
ATOM   2661 C CD1  A ILE   A 1 106 ? 19.307 -7.869  -9.484  0.42 22.09 ?  106 ILE   A CD1  1 
ATOM   2662 C CD1  B ILE   A 1 106 ? 19.142 -8.638  -10.047 0.58 24.91 ?  106 ILE   A CD1  1 
ATOM   2663 H H    A ILE   A 1 106 ? 21.797 -8.564  -13.211 0.42 27.35 ?  106 ILE   A H    1 
ATOM   2664 H H    B ILE   A 1 106 ? 22.096 -9.302  -13.370 0.58 23.12 ?  106 ILE   A H    1 
ATOM   2665 H HA   A ILE   A 1 106 ? 21.589 -8.276  -10.626 0.42 26.01 ?  106 ILE   A HA   1 
ATOM   2666 H HA   B ILE   A 1 106 ? 21.628 -8.848  -10.862 0.58 24.63 ?  106 ILE   A HA   1 
ATOM   2667 H HB   A ILE   A 1 106 ? 19.706 -8.315  -12.159 0.42 25.99 ?  106 ILE   A HB   1 
ATOM   2668 H HB   B ILE   A 1 106 ? 19.952 -9.222  -12.560 0.58 27.06 ?  106 ILE   A HB   1 
ATOM   2669 H HG12 A ILE   A 1 106 ? 18.209 -9.179  -10.574 0.42 26.39 ?  106 ILE   A HG12 1 
ATOM   2670 H HG12 B ILE   A 1 106 ? 18.389 -10.202 -11.088 0.58 28.31 ?  106 ILE   A HG12 1 
ATOM   2671 H HG13 A ILE   A 1 106 ? 19.414 -9.869  -9.807  0.42 26.39 ?  106 ILE   A HG13 1 
ATOM   2672 H HG13 B ILE   A 1 106 ? 19.580 -10.613 -10.123 0.58 28.31 ?  106 ILE   A HG13 1 
ATOM   2673 H HG21 A ILE   A 1 106 ? 18.824 -10.277 -12.817 0.42 25.93 ?  106 ILE   A HG21 1 
ATOM   2674 H HG21 B ILE   A 1 106 ? 19.359 -11.341 -13.128 0.58 27.88 ?  106 ILE   A HG21 1 
ATOM   2675 H HG22 A ILE   A 1 106 ? 20.380 -10.451 -13.088 0.42 25.93 ?  106 ILE   A HG22 1 
ATOM   2676 H HG22 B ILE   A 1 106 ? 20.935 -11.275 -13.314 0.58 27.88 ?  106 ILE   A HG22 1 
ATOM   2677 H HG23 A ILE   A 1 106 ? 19.719 -11.105 -11.800 0.42 25.93 ?  106 ILE   A HG23 1 
ATOM   2678 H HG23 B ILE   A 1 106 ? 20.312 -11.967 -12.027 0.58 27.88 ?  106 ILE   A HG23 1 
ATOM   2679 H HD11 A ILE   A 1 106 ? 18.555 -7.807  -8.876  0.42 26.53 ?  106 ILE   A HD11 1 
ATOM   2680 H HD11 B ILE   A 1 106 ? 18.334 -8.650  -9.516  0.58 29.91 ?  106 ILE   A HD11 1 
ATOM   2681 H HD12 A ILE   A 1 106 ? 20.133 -7.936  -8.979  0.42 26.53 ?  106 ILE   A HD12 1 
ATOM   2682 H HD12 B ILE   A 1 106 ? 19.915 -8.513  -9.479  0.58 29.91 ?  106 ILE   A HD12 1 
ATOM   2683 H HD13 A ILE   A 1 106 ? 19.331 -7.087  -10.059 0.42 26.53 ?  106 ILE   A HD13 1 
ATOM   2684 H HD13 B ILE   A 1 106 ? 19.094 -7.930  -10.708 0.58 29.91 ?  106 ILE   A HD13 1 
ATOM   2685 N N    A GLN   A 1 107 ? 22.743 -11.050 -11.511 0.42 23.32 ?  107 GLN   A N    1 
ATOM   2686 N N    B GLN   A 1 107 ? 23.047 -11.616 -11.384 0.58 20.90 ?  107 GLN   A N    1 
ATOM   2687 C CA   A GLN   A 1 107 ? 23.320 -12.291 -11.008 0.42 24.80 ?  107 GLN   A CA   1 
ATOM   2688 C CA   B GLN   A 1 107 ? 23.694 -12.732 -10.702 0.58 22.98 ?  107 GLN   A CA   1 
ATOM   2689 C C    A GLN   A 1 107 ? 24.315 -12.044 -9.881  0.42 22.75 ?  107 GLN   A C    1 
ATOM   2690 C C    B GLN   A 1 107 ? 24.602 -12.249 -9.581  0.58 19.85 ?  107 GLN   A C    1 
ATOM   2691 O O    A GLN   A 1 107 ? 24.548 -12.946 -9.069  0.42 24.48 ?  107 GLN   A O    1 
ATOM   2692 O O    B GLN   A 1 107 ? 24.833 -12.984 -8.611  0.58 19.78 ?  107 GLN   A O    1 
ATOM   2693 C CB   A GLN   A 1 107 ? 23.995 -13.049 -12.155 0.42 28.83 ?  107 GLN   A CB   1 
ATOM   2694 C CB   B GLN   A 1 107 ? 24.486 -13.581 -11.708 0.58 28.03 ?  107 GLN   A CB   1 
ATOM   2695 C CG   A GLN   A 1 107 ? 23.090 -13.291 -13.357 0.42 33.29 ?  107 GLN   A CG   1 
ATOM   2696 C CG   B GLN   A 1 107 ? 23.658 -14.085 -12.884 0.58 33.57 ?  107 GLN   A CG   1 
ATOM   2697 C CD   A GLN   A 1 107 ? 21.832 -14.059 -12.999 0.42 36.87 ?  107 GLN   A CD   1 
ATOM   2698 C CD   B GLN   A 1 107 ? 22.518 -14.983 -12.450 0.58 38.06 ?  107 GLN   A CD   1 
ATOM   2699 O OE1  A GLN   A 1 107 ? 21.890 -15.099 -12.342 0.42 37.92 ?  107 GLN   A OE1  1 
ATOM   2700 O OE1  B GLN   A 1 107 ? 22.680 -15.835 -11.575 0.58 39.23 ?  107 GLN   A OE1  1 
ATOM   2701 N NE2  A GLN   A 1 107 ? 20.684 -13.545 -13.424 0.42 37.76 ?  107 GLN   A NE2  1 
ATOM   2702 N NE2  B GLN   A 1 107 ? 21.352 -14.793 -13.059 0.58 39.06 ?  107 GLN   A NE2  1 
ATOM   2703 H H    A GLN   A 1 107 ? 22.916 -10.886 -12.335 0.42 28.00 ?  107 GLN   A H    1 
ATOM   2704 H H    B GLN   A 1 107 ? 23.223 -11.563 -12.228 0.58 25.10 ?  107 GLN   A H    1 
ATOM   2705 H HA   A GLN   A 1 107 ? 22.610 -12.850 -10.661 0.42 29.77 ?  107 GLN   A HA   1 
ATOM   2706 H HA   B GLN   A 1 107 ? 23.015 -13.304 -10.318 0.58 27.59 ?  107 GLN   A HA   1 
ATOM   2707 H HB2  A GLN   A 1 107 ? 24.761 -12.539 -12.462 0.42 34.62 ?  107 GLN   A HB2  1 
ATOM   2708 H HB2  B GLN   A 1 107 ? 25.212 -13.052 -12.071 0.58 33.65 ?  107 GLN   A HB2  1 
ATOM   2709 H HB3  A GLN   A 1 107 ? 24.287 -13.915 -11.831 0.42 34.62 ?  107 GLN   A HB3  1 
ATOM   2710 H HB3  B GLN   A 1 107 ? 24.845 -14.362 -11.254 0.58 33.65 ?  107 GLN   A HB3  1 
ATOM   2711 H HG2  A GLN   A 1 107 ? 22.822 -12.438 -13.733 0.42 39.96 ?  107 GLN   A HG2  1 
ATOM   2712 H HG2  B GLN   A 1 107 ? 23.279 -13.328 -13.357 0.58 40.30 ?  107 GLN   A HG2  1 
ATOM   2713 H HG3  A GLN   A 1 107 ? 23.578 -13.804 -14.022 0.42 39.96 ?  107 GLN   A HG3  1 
ATOM   2714 H HG3  B GLN   A 1 107 ? 24.230 -14.594 -13.482 0.58 40.30 ?  107 GLN   A HG3  1 
ATOM   2715 H HE21 A GLN   A 1 107 ? 20.682 -12.815 -13.879 0.42 45.33 ?  107 GLN   A HE21 1 
ATOM   2716 H HE21 B GLN   A 1 107 ? 21.277 -14.186 -13.664 0.58 46.89 ?  107 GLN   A HE21 1 
ATOM   2717 H HE22 A GLN   A 1 107 ? 19.944 -13.944 -13.246 0.42 45.33 ?  107 GLN   A HE22 1 
ATOM   2718 H HE22 B GLN   A 1 107 ? 20.673 -15.276 -12.848 0.58 46.89 ?  107 GLN   A HE22 1 
ATOM   2719 N N    A LEU   A 1 108 ? 24.894 -10.842 -9.805  0.42 19.26 ?  108 LEU   A N    1 
ATOM   2720 N N    B LEU   A 1 108 ? 25.100 -11.017 -9.681  0.58 16.98 ?  108 LEU   A N    1 
ATOM   2721 C CA   A LEU   A 1 108 ? 25.838 -10.509 -8.743  0.42 16.72 ?  108 LEU   A CA   1 
ATOM   2722 C CA   B LEU   A 1 108 ? 25.934 -10.460 -8.631  0.58 15.63 ?  108 LEU   A CA   1 
ATOM   2723 C C    A LEU   A 1 108 ? 25.158 -10.308 -7.393  0.42 14.89 ?  108 LEU   A C    1 
ATOM   2724 C C    B LEU   A 1 108 ? 25.163 -10.230 -7.340  0.58 13.97 ?  108 LEU   A C    1 
ATOM   2725 O O    A LEU   A 1 108 ? 25.854 -10.165 -6.383  0.42 15.45 ?  108 LEU   A O    1 
ATOM   2726 O O    B LEU   A 1 108 ? 25.796 -9.996  -6.304  0.58 14.22 ?  108 LEU   A O    1 
ATOM   2727 C CB   A LEU   A 1 108 ? 26.636 -9.258  -9.125  0.42 16.58 ?  108 LEU   A CB   1 
ATOM   2728 C CB   B LEU   A 1 108 ? 26.588 -9.160  -9.108  0.58 16.08 ?  108 LEU   A CB   1 
ATOM   2729 C CG   A LEU   A 1 108 ? 27.559 -9.435  -10.333 0.42 17.27 ?  108 LEU   A CG   1 
ATOM   2730 C CG   B LEU   A 1 108 ? 27.668 -9.370  -10.171 0.58 18.09 ?  108 LEU   A CG   1 
ATOM   2731 C CD1  A LEU   A 1 108 ? 28.072 -8.092  -10.830 0.42 17.97 ?  108 LEU   A CD1  1 
ATOM   2732 C CD1  B LEU   A 1 108 ? 28.064 -8.057  -10.822 0.58 19.23 ?  108 LEU   A CD1  1 
ATOM   2733 C CD2  A LEU   A 1 108 ? 28.725 -10.350 -9.985  0.42 17.83 ?  108 LEU   A CD2  1 
ATOM   2734 C CD2  B LEU   A 1 108 ? 28.886 -10.042 -9.554  0.58 19.03 ?  108 LEU   A CD2  1 
ATOM   2735 H H    A LEU   A 1 108 ? 24.751 -10.206 -10.363 0.42 23.12 ?  108 LEU   A H    1 
ATOM   2736 H H    B LEU   A 1 108 ? 24.958 -10.495 -10.342 0.58 20.40 ?  108 LEU   A H    1 
ATOM   2737 H HA   A LEU   A 1 108 ? 26.461 -11.241 -8.645  0.42 20.09 ?  108 LEU   A HA   1 
ATOM   2738 H HA   B LEU   A 1 108 ? 26.639 -11.096 -8.435  0.58 18.78 ?  108 LEU   A HA   1 
ATOM   2739 H HB2  A LEU   A 1 108 ? 26.014 -8.545  -9.336  0.42 19.91 ?  108 LEU   A HB2  1 
ATOM   2740 H HB2  B LEU   A 1 108 ? 25.903 -8.591  -9.491  0.58 19.31 ?  108 LEU   A HB2  1 
ATOM   2741 H HB3  A LEU   A 1 108 ? 27.187 -9.001  -8.372  0.42 19.91 ?  108 LEU   A HB3  1 
ATOM   2742 H HB3  B LEU   A 1 108 ? 26.997 -8.724  -8.350  0.58 19.31 ?  108 LEU   A HB3  1 
ATOM   2743 H HG   A LEU   A 1 108 ? 27.061 -9.847  -11.056 0.42 20.74 ?  108 LEU   A HG   1 
ATOM   2744 H HG   B LEU   A 1 108 ? 27.323 -9.955  -10.865 0.58 21.72 ?  108 LEU   A HG   1 
ATOM   2745 H HD11 A LEU   A 1 108 ? 28.629 -8.234  -11.613 0.42 21.59 ?  108 LEU   A HD11 1 
ATOM   2746 H HD11 B LEU   A 1 108 ? 28.732 -8.231  -11.505 0.58 23.09 ?  108 LEU   A HD11 1 
ATOM   2747 H HD12 A LEU   A 1 108 ? 27.316 -7.529  -11.062 0.42 21.59 ?  108 LEU   A HD12 1 
ATOM   2748 H HD12 B LEU   A 1 108 ? 27.279 -7.652  -11.222 0.58 23.09 ?  108 LEU   A HD12 1 
ATOM   2749 H HD13 A LEU   A 1 108 ? 28.593 -7.672  -10.127 0.42 21.59 ?  108 LEU   A HD13 1 
ATOM   2750 H HD13 B LEU   A 1 108 ? 28.432 -7.467  -10.144 0.58 23.09 ?  108 LEU   A HD13 1 
ATOM   2751 H HD21 A LEU   A 1 108 ? 29.352 -10.357 -10.724 0.42 21.41 ?  108 LEU   A HD21 1 
ATOM   2752 H HD21 B LEU   A 1 108 ? 29.620 -10.007 -10.186 0.58 22.85 ?  108 LEU   A HD21 1 
ATOM   2753 H HD22 A LEU   A 1 108 ? 29.160 -10.012 -9.185  0.42 21.41 ?  108 LEU   A HD22 1 
ATOM   2754 H HD22 B LEU   A 1 108 ? 29.126 -9.571  -8.740  0.58 22.85 ?  108 LEU   A HD22 1 
ATOM   2755 H HD23 A LEU   A 1 108 ? 28.388 -11.243 -9.825  0.42 21.41 ?  108 LEU   A HD23 1 
ATOM   2756 H HD23 B LEU   A 1 108 ? 28.669 -10.965 -9.349  0.58 22.85 ?  108 LEU   A HD23 1 
ATOM   2757 N N    . LEU   A 1 109 ? 23.824 -10.307 -7.358  1.00 13.71 ?  109 LEU   A N    1 
ATOM   2758 C CA   . LEU   A 1 109 ? 23.097 -10.173 -6.102  1.00 12.83 ?  109 LEU   A CA   1 
ATOM   2759 C C    . LEU   A 1 109 ? 23.417 -11.328 -5.154  1.00 12.67 ?  109 LEU   A C    1 
ATOM   2760 O O    . LEU   A 1 109 ? 23.527 -11.134 -3.939  1.00 13.02 ?  109 LEU   A O    1 
ATOM   2761 C CB   . LEU   A 1 109 ? 21.596 -10.094 -6.389  1.00 13.62 ?  109 LEU   A CB   1 
ATOM   2762 C CG   . LEU   A 1 109 ? 20.676 -9.800  -5.202  1.00 14.87 ?  109 LEU   A CG   1 
ATOM   2763 C CD1  . LEU   A 1 109 ? 21.101 -8.527  -4.489  1.00 15.21 ?  109 LEU   A CD1  1 
ATOM   2764 C CD2  . LEU   A 1 109 ? 19.219 -9.696  -5.652  1.00 16.49 ?  109 LEU   A CD2  1 
ATOM   2765 H H    A LEU   A 1 109 ? 23.315 -10.389 -8.048  0.42 16.47 ?  109 LEU   A H    1 
ATOM   2766 H H    B LEU   A 1 109 ? 23.334 -10.432 -8.056  0.58 16.47 ?  109 LEU   A H    1 
ATOM   2767 H HA   . LEU   A 1 109 ? 23.367 -9.344  -5.674  1.00 15.41 ?  109 LEU   A HA   1 
ATOM   2768 H HB2  . LEU   A 1 109 ? 21.449 -9.393  -7.042  1.00 16.36 ?  109 LEU   A HB2  1 
ATOM   2769 H HB3  . LEU   A 1 109 ? 21.315 -10.943 -6.760  1.00 16.36 ?  109 LEU   A HB3  1 
ATOM   2770 H HG   . LEU   A 1 109 ? 20.741 -10.527 -4.563  1.00 17.86 ?  109 LEU   A HG   1 
ATOM   2771 H HD11 . LEU   A 1 109 ? 20.412 -8.269  -3.859  1.00 18.27 ?  109 LEU   A HD11 1 
ATOM   2772 H HD12 . LEU   A 1 109 ? 21.935 -8.686  -4.022  1.00 18.27 ?  109 LEU   A HD12 1 
ATOM   2773 H HD13 . LEU   A 1 109 ? 21.222 -7.822  -5.150  1.00 18.27 ?  109 LEU   A HD13 1 
ATOM   2774 H HD21 . LEU   A 1 109 ? 18.682 -9.345  -4.922  1.00 19.81 ?  109 LEU   A HD21 1 
ATOM   2775 H HD22 . LEU   A 1 109 ? 19.161 -9.106  -6.417  1.00 19.81 ?  109 LEU   A HD22 1 
ATOM   2776 H HD23 . LEU   A 1 109 ? 18.899 -10.583 -5.895  1.00 19.81 ?  109 LEU   A HD23 1 
ATOM   2777 N N    . LYS   A 1 110 ? 23.575 -12.540 -5.684  1.00 12.90 ?  110 LYS   A N    1 
ATOM   2778 C CA   . LYS   A 1 110 ? 23.939 -13.655 -4.815  1.00 12.70 ?  110 LYS   A CA   1 
ATOM   2779 C C    . LYS   A 1 110 ? 25.312 -13.425 -4.192  1.00 12.06 ?  110 LYS   A C    1 
ATOM   2780 O O    . LYS   A 1 110 ? 25.502 -13.635 -2.992  1.00 12.32 ?  110 LYS   A O    1 
ATOM   2781 C CB   . LYS   A 1 110 ? 23.895 -14.974 -5.583  1.00 14.19 ?  110 LYS   A CB   1 
ATOM   2782 C CG   . LYS   A 1 110 ? 24.036 -16.189 -4.675  1.00 14.14 ?  110 LYS   A CG   1 
ATOM   2783 C CD   . LYS   A 1 110 ? 23.804 -17.498 -5.407  1.00 14.53 ?  110 LYS   A CD   1 
ATOM   2784 C CE   . LYS   A 1 110 ? 23.895 -18.696 -4.461  1.00 15.67 ?  110 LYS   A CE   1 
ATOM   2785 N NZ   . LYS   A 1 110 ? 22.722 -18.805 -3.554  1.00 15.91 ?  110 LYS   A NZ   1 
ATOM   2786 H H    . LYS   A 1 110 ? 23.482 -12.733 -6.511  1.00 15.50 ?  110 LYS   A H    1 
ATOM   2787 H HA   . LYS   A 1 110 ? 23.291 -13.709 -4.092  1.00 15.25 ?  110 LYS   A HA   1 
ATOM   2788 H HB2  . LYS   A 1 110 ? 23.047 -15.041 -6.043  1.00 17.04 ?  110 LYS   A HB2  1 
ATOM   2789 H HB3  . LYS   A 1 110 ? 24.625 -14.989 -6.219  1.00 17.04 ?  110 LYS   A HB3  1 
ATOM   2790 H HG2  . LYS   A 1 110 ? 24.934 -16.200 -4.306  1.00 16.98 ?  110 LYS   A HG2  1 
ATOM   2791 H HG3  . LYS   A 1 110 ? 23.386 -16.119 -3.959  1.00 16.98 ?  110 LYS   A HG3  1 
ATOM   2792 H HD2  . LYS   A 1 110 ? 22.919 -17.490 -5.799  1.00 17.45 ?  110 LYS   A HD2  1 
ATOM   2793 H HD3  . LYS   A 1 110 ? 24.478 -17.600 -6.096  1.00 17.45 ?  110 LYS   A HD3  1 
ATOM   2794 H HE2  . LYS   A 1 110 ? 23.952 -19.511 -4.983  1.00 18.82 ?  110 LYS   A HE2  1 
ATOM   2795 H HE3  . LYS   A 1 110 ? 24.693 -18.605 -3.907  1.00 18.82 ?  110 LYS   A HE3  1 
ATOM   2796 H HZ1  . LYS   A 1 110 ? 22.808 -19.509 -3.020  1.00 19.10 ?  110 LYS   A HZ1  1 
ATOM   2797 H HZ2  . LYS   A 1 110 ? 22.652 -18.069 -3.055  1.00 19.10 ?  110 LYS   A HZ2  1 
ATOM   2798 H HZ3  . LYS   A 1 110 ? 21.976 -18.895 -4.035  1.00 19.10 ?  110 LYS   A HZ3  1 
ATOM   2799 N N    . SER   A 1 111 ? 26.281 -12.986 -4.999  1.00 12.41 ?  111 SER   A N    1 
ATOM   2800 C CA   . SER   A 1 111 ? 27.605 -12.667 -4.464  1.00 12.37 ?  111 SER   A CA   1 
ATOM   2801 C C    . SER   A 1 111 ? 27.522 -11.620 -3.357  1.00 12.01 ?  111 SER   A C    1 
ATOM   2802 O O    . SER   A 1 111 ? 28.200 -11.728 -2.330  1.00 12.43 ?  111 SER   A O    1 
ATOM   2803 C CB   . SER   A 1 111 ? 28.509 -12.176 -5.593  1.00 13.40 ?  111 SER   A CB   1 
ATOM   2804 O OG   . SER   A 1 111 ? 28.562 -13.145 -6.625  1.00 15.36 ?  111 SER   A OG   1 
ATOM   2805 H H    . SER   A 1 111 ? 26.198 -12.878 -5.844  1.00 14.91 ?  111 SER   A H    1 
ATOM   2806 H HA   . SER   A 1 111 ? 28.000 -13.477 -4.092  1.00 14.86 ?  111 SER   A HA   1 
ATOM   2807 H HB2  . SER   A 1 111 ? 28.144 -11.352 -5.951  1.00 16.10 ?  111 SER   A HB2  1 
ATOM   2808 H HB3  . SER   A 1 111 ? 29.399 -12.029 -5.246  1.00 16.10 ?  111 SER   A HB3  1 
ATOM   2809 H HG   . SER   A 1 111 ? 29.062 -12.872 -7.249  1.00 18.45 ?  111 SER   A HG   1 
ATOM   2810 N N    . ALA   A 1 112 ? 26.674 -10.608 -3.544  1.00 11.86 ?  112 ALA   A N    1 
ATOM   2811 C CA   . ALA   A 1 112 ? 26.507 -9.571  -2.528  1.00 11.77 ?  112 ALA   A CA   1 
ATOM   2812 C C    . ALA   A 1 112 ? 26.013 -10.174 -1.212  1.00 11.26 ?  112 ALA   A C    1 
ATOM   2813 O O    . ALA   A 1 112 ? 26.554 -9.891  -0.137  1.00 11.87 ?  112 ALA   A O    1 
ATOM   2814 C CB   . ALA   A 1 112 ? 25.533 -8.504  -3.033  1.00 12.35 ?  112 ALA   A CB   1 
ATOM   2815 H H    . ALA   A 1 112 ? 26.187 -10.500 -4.245  1.00 14.24 ?  112 ALA   A H    1 
ATOM   2816 H HA   . ALA   A 1 112 ? 27.363 -9.148  -2.364  1.00 14.14 ?  112 ALA   A HA   1 
ATOM   2817 H HB1  . ALA   A 1 112 ? 25.462 -7.801  -2.362  1.00 14.84 ?  112 ALA   A HB1  1 
ATOM   2818 H HB2  . ALA   A 1 112 ? 25.869 -8.135  -3.861  1.00 14.84 ?  112 ALA   A HB2  1 
ATOM   2819 H HB3  . ALA   A 1 112 ? 24.663 -8.909  -3.176  1.00 14.84 ?  112 ALA   A HB3  1 
ATOM   2820 N N    . TYR   A 1 113 ? 24.977 -11.015 -1.273  1.00 11.38 ?  113 TYR   A N    1 
ATOM   2821 C CA   . TYR   A 1 113 ? 24.458 -11.624 -0.051  1.00 11.12 ?  113 TYR   A CA   1 
ATOM   2822 C C    . TYR   A 1 113 ? 25.458 -12.576 0.602   1.00 11.00 ?  113 TYR   A C    1 
ATOM   2823 O O    . TYR   A 1 113 ? 25.408 -12.770 1.822   1.00 11.61 ?  113 TYR   A O    1 
ATOM   2824 C CB   . TYR   A 1 113 ? 23.132 -12.340 -0.324  1.00 11.57 ?  113 TYR   A CB   1 
ATOM   2825 C CG   . TYR   A 1 113 ? 21.927 -11.421 -0.308  1.00 11.84 ?  113 TYR   A CG   1 
ATOM   2826 C CD1  . TYR   A 1 113 ? 21.537 -10.771 0.859   1.00 11.76 ?  113 TYR   A CD1  1 
ATOM   2827 C CD2  . TYR   A 1 113 ? 21.148 -11.241 -1.442  1.00 12.71 ?  113 TYR   A CD2  1 
ATOM   2828 C CE1  . TYR   A 1 113 ? 20.420 -9.966  0.891   1.00 12.63 ?  113 TYR   A CE1  1 
ATOM   2829 C CE2  . TYR   A 1 113 ? 20.020 -10.428 -1.421  1.00 12.96 ?  113 TYR   A CE2  1 
ATOM   2830 C CZ   . TYR   A 1 113 ? 19.661 -9.794  -0.248  1.00 12.85 ?  113 TYR   A CZ   1 
ATOM   2831 O OH   . TYR   A 1 113 ? 18.542 -8.995  -0.193  1.00 14.00 ?  113 TYR   A OH   1 
ATOM   2832 H H    . TYR   A 1 113 ? 24.575 -11.249 -1.996  1.00 13.68 ?  113 TYR   A H    1 
ATOM   2833 H HA   . TYR   A 1 113 ? 24.283 -10.923 0.587   1.00 13.36 ?  113 TYR   A HA   1 
ATOM   2834 H HB2  . TYR   A 1 113 ? 23.167 -12.754 -1.200  1.00 13.90 ?  113 TYR   A HB2  1 
ATOM   2835 H HB3  . TYR   A 1 113 ? 22.994 -13.022 0.353   1.00 13.90 ?  113 TYR   A HB3  1 
ATOM   2836 H HD1  . TYR   A 1 113 ? 22.044 -10.903 1.634   1.00 14.13 ?  113 TYR   A HD1  1 
ATOM   2837 H HD2  . TYR   A 1 113 ? 21.380 -11.676 -2.226  1.00 15.26 ?  113 TYR   A HD2  1 
ATOM   2838 H HE1  . TYR   A 1 113 ? 20.187 -9.549  1.686   1.00 15.18 ?  113 TYR   A HE1  1 
ATOM   2839 H HE2  . TYR   A 1 113 ? 19.504 -10.311 -2.184  1.00 15.57 ?  113 TYR   A HE2  1 
ATOM   2840 H HH   . TYR   A 1 113 ? 18.105 -9.074  -0.913  1.00 16.82 ?  113 TYR   A HH   1 
ATOM   2841 N N    . GLU   A 1 114 ? 26.362 -13.189 -0.177  1.00 11.03 ?  114 GLU   A N    1 
ATOM   2842 C CA   . GLU   A 1 114 ? 27.350 -14.089 0.421   1.00 11.67 ?  114 GLU   A CA   1 
ATOM   2843 C C    . GLU   A 1 114 ? 28.193 -13.375 1.472   1.00 11.25 ?  114 GLU   A C    1 
ATOM   2844 O O    . GLU   A 1 114 ? 28.665 -14.007 2.429   1.00 11.73 ?  114 GLU   A O    1 
ATOM   2845 C CB   . GLU   A 1 114 ? 28.223 -14.730 -0.666  1.00 11.98 ?  114 GLU   A CB   1 
ATOM   2846 C CG   . GLU   A 1 114 ? 27.470 -15.767 -1.476  1.00 12.60 ?  114 GLU   A CG   1 
ATOM   2847 C CD   . GLU   A 1 114 ? 28.206 -16.304 -2.704  1.00 12.87 ?  114 GLU   A CD   1 
ATOM   2848 O OE1  . GLU   A 1 114 ? 29.160 -15.672 -3.207  1.00 13.30 ?  114 GLU   A OE1  1 
ATOM   2849 O OE2  . GLU   A 1 114 ? 27.787 -17.376 -3.200  1.00 14.15 -1 114 GLU   A OE2  1 
ATOM   2850 H H    . GLU   A 1 114 ? 26.422 -13.094 -1.039  1.00 13.25 ?  114 GLU   A H    1 
ATOM   2851 H HA   . GLU   A 1 114 ? 26.873 -14.803 0.860   1.00 14.02 ?  114 GLU   A HA   1 
ATOM   2852 H HB2  . GLU   A 1 114 ? 28.535 -14.040 -1.277  1.00 14.39 ?  114 GLU   A HB2  1 
ATOM   2853 H HB3  . GLU   A 1 114 ? 28.978 -15.168 -0.248  1.00 14.39 ?  114 GLU   A HB3  1 
ATOM   2854 H HG2  . GLU   A 1 114 ? 27.280 -16.525 -0.908  1.00 15.14 ?  114 GLU   A HG2  1 
ATOM   2855 H HG3  . GLU   A 1 114 ? 26.635 -15.375 -1.783  1.00 15.14 ?  114 GLU   A HG3  1 
ATOM   2856 N N    . ASN   A 1 115 ? 28.387 -12.060 1.335   1.00 11.39 ?  115 ASN   A N    1 
ATOM   2857 C CA   . ASN   A 1 115 ? 29.150 -11.336 2.347   1.00 11.75 ?  115 ASN   A CA   1 
ATOM   2858 C C    . ASN   A 1 115 ? 28.513 -11.458 3.729   1.00 11.48 ?  115 ASN   A C    1 
ATOM   2859 O O    . ASN   A 1 115 ? 29.214 -11.378 4.746   1.00 11.86 ?  115 ASN   A O    1 
ATOM   2860 C CB   . ASN   A 1 115 ? 29.266 -9.862  1.965   1.00 12.06 ?  115 ASN   A CB   1 
ATOM   2861 C CG   . ASN   A 1 115 ? 30.073 -9.654  0.707   1.00 12.41 ?  115 ASN   A CG   1 
ATOM   2862 O OD1  . ASN   A 1 115 ? 31.289 -9.793  0.724   1.00 15.83 ?  115 ASN   A OD1  1 
ATOM   2863 N ND2  . ASN   A 1 115 ? 29.408 -9.337  -0.388  1.00 12.09 ?  115 ASN   A ND2  1 
ATOM   2864 H H    . ASN   A 1 115 ? 28.088 -11.571 0.695   1.00 13.68 ?  115 ASN   A H    1 
ATOM   2865 H HA   . ASN   A 1 115 ? 30.044 -11.710 2.398   1.00 14.12 ?  115 ASN   A HA   1 
ATOM   2866 H HB2  . ASN   A 1 115 ? 28.379 -9.503  1.828   1.00 14.49 ?  115 ASN   A HB2  1 
ATOM   2867 H HB3  . ASN   A 1 115 ? 29.712 -9.386  2.685   1.00 14.49 ?  115 ASN   A HB3  1 
ATOM   2868 H HD21 . ASN   A 1 115 ? 29.825 -9.212  -1.132  1.00 14.52 ?  115 ASN   A HD21 1 
ATOM   2869 H HD22 . ASN   A 1 115 ? 28.547 -9.269  -0.369  1.00 14.52 ?  115 ASN   A HD22 1 
ATOM   2870 N N    . PHE   A 1 116 ? 27.184 -11.615 3.800   1.00 11.63 ?  116 PHE   A N    1 
ATOM   2871 C CA   . PHE   A 1 116 ? 26.524 -11.701 5.102   1.00 11.38 ?  116 PHE   A CA   1 
ATOM   2872 C C    . PHE   A 1 116 ? 26.989 -12.931 5.886   1.00 12.12 ?  116 PHE   A C    1 
ATOM   2873 O O    . PHE   A 1 116 ? 26.918 -12.944 7.114   1.00 12.42 ?  116 PHE   A O    1 
ATOM   2874 C CB   . PHE   A 1 116 ? 24.997 -11.833 4.956   1.00 11.42 ?  116 PHE   A CB   1 
ATOM   2875 C CG   . PHE   A 1 116 ? 24.243 -10.596 4.458   1.00 11.22 ?  116 PHE   A CG   1 
ATOM   2876 C CD1  . PHE   A 1 116 ? 24.819 -9.591  3.684   1.00 11.78 ?  116 PHE   A CD1  1 
ATOM   2877 C CD2  . PHE   A 1 116 ? 22.896 -10.473 4.783   1.00 11.89 ?  116 PHE   A CD2  1 
ATOM   2878 C CE1  . PHE   A 1 116 ? 24.048 -8.524  3.235   1.00 12.01 ?  116 PHE   A CE1  1 
ATOM   2879 C CE2  . PHE   A 1 116 ? 22.132 -9.414  4.340   1.00 12.17 ?  116 PHE   A CE2  1 
ATOM   2880 C CZ   . PHE   A 1 116 ? 22.705 -8.437  3.568   1.00 11.64 ?  116 PHE   A CZ   1 
ATOM   2881 H H    . PHE   A 1 116 ? 26.656 -11.658 3.124   1.00 13.97 ?  116 PHE   A H    1 
ATOM   2882 H HA   . PHE   A 1 116 ? 26.717 -10.909 5.627   1.00 13.67 ?  116 PHE   A HA   1 
ATOM   2883 H HB2  . PHE   A 1 116 ? 24.814 -12.558 4.336   1.00 13.72 ?  116 PHE   A HB2  1 
ATOM   2884 H HB3  . PHE   A 1 116 ? 24.630 -12.069 5.829   1.00 13.72 ?  116 PHE   A HB3  1 
ATOM   2885 H HD1  . PHE   A 1 116 ? 25.714 -9.664  3.448   1.00 14.15 ?  116 PHE   A HD1  1 
ATOM   2886 H HD2  . PHE   A 1 116 ? 22.491 -11.146 5.294   1.00 14.28 ?  116 PHE   A HD2  1 
ATOM   2887 H HE1  . PHE   A 1 116 ? 24.445 -7.859  2.721   1.00 14.43 ?  116 PHE   A HE1  1 
ATOM   2888 H HE2  . PHE   A 1 116 ? 21.231 -9.355  4.573   1.00 14.62 ?  116 PHE   A HE2  1 
ATOM   2889 H HZ   . PHE   A 1 116 ? 22.205 -7.705  3.283   1.00 13.98 ?  116 PHE   A HZ   1 
ATOM   2890 N N    . ASN   A 1 117 ? 27.434 -13.982 5.191   1.00 11.95 ?  117 ASN   A N    1 
ATOM   2891 C CA   . ASN   A 1 117 ? 27.801 -15.221 5.871   1.00 12.31 ?  117 ASN   A CA   1 
ATOM   2892 C C    . ASN   A 1 117 ? 29.058 -15.095 6.713   1.00 12.85 ?  117 ASN   A C    1 
ATOM   2893 O O    . ASN   A 1 117 ? 29.342 -16.006 7.497   1.00 13.52 ?  117 ASN   A O    1 
ATOM   2894 C CB   . ASN   A 1 117 ? 27.933 -16.344 4.850   1.00 12.39 ?  117 ASN   A CB   1 
ATOM   2895 C CG   . ASN   A 1 117 ? 26.593 -16.742 4.301   1.00 12.68 ?  117 ASN   A CG   1 
ATOM   2896 O OD1  . ASN   A 1 117 ? 25.612 -16.770 5.035   1.00 13.75 ?  117 ASN   A OD1  1 
ATOM   2897 N ND2  . ASN   A 1 117 ? 26.527 -17.004 3.010   1.00 12.39 ?  117 ASN   A ND2  1 
ATOM   2898 H H    . ASN   A 1 117 ? 27.522 -13.999 4.331   1.00 14.35 ?  117 ASN   A H    1 
ATOM   2899 H HA   . ASN   A 1 117 ? 27.075 -15.456 6.467   1.00 14.79 ?  117 ASN   A HA   1 
ATOM   2900 H HB2  . ASN   A 1 117 ? 28.489 -16.040 4.113   1.00 14.88 ?  117 ASN   A HB2  1 
ATOM   2901 H HB3  . ASN   A 1 117 ? 28.329 -17.113 5.277   1.00 14.88 ?  117 ASN   A HB3  1 
ATOM   2902 H HD21 . ASN   A 1 117 ? 25.785 -17.229 2.657   1.00 14.88 ?  117 ASN   A HD21 1 
ATOM   2903 H HD22 . ASN   A 1 117 ? 27.244 -16.958 2.531   1.00 14.88 ?  117 ASN   A HD22 1 
ATOM   2904 N N    . GLN   A 1 118 ? 29.790 -13.986 6.598   1.00 12.86 ?  118 GLN   A N    1 
ATOM   2905 C CA   . GLN   A 1 118 ? 30.960 -13.754 7.435   1.00 13.39 ?  118 GLN   A CA   1 
ATOM   2906 C C    . GLN   A 1 118 ? 30.605 -13.175 8.800   1.00 13.30 ?  118 GLN   A C    1 
ATOM   2907 O O    . GLN   A 1 118 ? 31.515 -12.888 9.585   1.00 14.38 ?  118 GLN   A O    1 
ATOM   2908 C CB   . GLN   A 1 118 ? 31.965 -12.854 6.712   1.00 13.47 ?  118 GLN   A CB   1 
ATOM   2909 C CG   . GLN   A 1 118 ? 32.434 -13.444 5.393   1.00 13.62 ?  118 GLN   A CG   1 
ATOM   2910 C CD   . GLN   A 1 118 ? 33.284 -14.690 5.574   1.00 14.22 ?  118 GLN   A CD   1 
ATOM   2911 O OE1  . GLN   A 1 118 ? 34.122 -14.760 6.477   1.00 14.79 ?  118 GLN   A OE1  1 
ATOM   2912 N NE2  . GLN   A 1 118 ? 33.052 -15.697 4.722   1.00 13.95 ?  118 GLN   A NE2  1 
ATOM   2913 H H    . GLN   A 1 118 ? 29.616 -13.338 6.046   1.00 15.45 ?  118 GLN   A H    1 
ATOM   2914 H HA   . GLN   A 1 118 ? 31.385 -14.613 7.587   1.00 16.08 ?  118 GLN   A HA   1 
ATOM   2915 H HB2  . GLN   A 1 118 ? 31.549 -11.999 6.535   1.00 16.19 ?  118 GLN   A HB2  1 
ATOM   2916 H HB3  . GLN   A 1 118 ? 32.741 -12.737 7.285   1.00 16.19 ?  118 GLN   A HB3  1 
ATOM   2917 H HG2  . GLN   A 1 118 ? 31.662 -13.681 4.854   1.00 16.37 ?  118 GLN   A HG2  1 
ATOM   2918 H HG3  . GLN   A 1 118 ? 32.972 -12.785 4.925   1.00 16.37 ?  118 GLN   A HG3  1 
ATOM   2919 H HE21 . GLN   A 1 118 ? 32.449 -15.613 4.106   1.00 16.76 ?  118 GLN   A HE21 1 
ATOM   2920 H HE22 . GLN   A 1 118 ? 33.500 -16.427 4.777   1.00 16.76 ?  118 GLN   A HE22 1 
ATOM   2921 N N    . HIS   A 1 119 ? 29.313 -13.005 9.101   1.00 12.77 ?  119 HIS   A N    1 
ATOM   2922 C CA   . HIS   A 1 119 ? 28.851 -12.395 10.346  1.00 13.27 ?  119 HIS   A CA   1 
ATOM   2923 C C    . HIS   A 1 119 ? 27.712 -13.221 10.916  1.00 13.48 ?  119 HIS   A C    1 
ATOM   2924 O O    . HIS   A 1 119 ? 26.781 -13.577 10.191  1.00 13.73 ?  119 HIS   A O    1 
ATOM   2925 C CB   . HIS   A 1 119 ? 28.394 -10.966 10.076  1.00 13.63 ?  119 HIS   A CB   1 
ATOM   2926 C CG   . HIS   A 1 119 ? 29.475 -10.158 9.461   1.00 15.04 ?  119 HIS   A CG   1 
ATOM   2927 N ND1  . HIS   A 1 119 ? 30.442 -9.535  10.216  1.00 17.61 ?  119 HIS   A ND1  1 
ATOM   2928 C CD2  . HIS   A 1 119 ? 29.824 -9.986  8.167   1.00 16.10 ?  119 HIS   A CD2  1 
ATOM   2929 C CE1  . HIS   A 1 119 ? 31.312 -8.958  9.407   1.00 18.06 ?  119 HIS   A CE1  1 
ATOM   2930 N NE2  . HIS   A 1 119 ? 30.966 -9.226  8.159   1.00 17.71 ?  119 HIS   A NE2  1 
ATOM   2931 H H    . HIS   A 1 119 ? 28.661 -13.264 8.590   1.00 15.34 ?  119 HIS   A H    1 
ATOM   2932 H HA   . HIS   A 1 119 ? 29.569 -12.375 10.986  1.00 15.94 ?  119 HIS   A HA   1 
ATOM   2933 H HB2  . HIS   A 1 119 ? 27.633 -10.978 9.465   1.00 16.37 ?  119 HIS   A HB2  1 
ATOM   2934 H HB3  . HIS   A 1 119 ? 28.136 -10.548 10.913  1.00 16.37 ?  119 HIS   A HB3  1 
ATOM   2935 H HD2  . HIS   A 1 119 ? 29.373 -10.311 7.419   1.00 19.34 ?  119 HIS   A HD2  1 
ATOM   2936 H HE1  . HIS   A 1 119 ? 32.039 -8.442  9.669   1.00 21.69 ?  119 HIS   A HE1  1 
ATOM   2937 H HE2  . HIS   A 1 119 ? 31.377 -8.942  7.456   1.00 21.27 ?  119 HIS   A HE2  1 
ATOM   2938 N N    A GLU   A 1 120 ? 27.802 -13.567 12.202  0.42 14.66 ?  120 GLU   A N    1 
ATOM   2939 N N    B GLU   A 1 120 ? 27.777 -13.465 12.229  0.58 13.87 ?  120 GLU   A N    1 
ATOM   2940 C CA   A GLU   A 1 120 ? 26.839 -14.516 12.758  0.42 16.83 ?  120 GLU   A CA   1 
ATOM   2941 C CA   B GLU   A 1 120 ? 26.836 -14.376 12.878  0.58 15.49 ?  120 GLU   A CA   1 
ATOM   2942 C C    A GLU   A 1 120 ? 25.419 -13.957 12.788  0.42 15.24 ?  120 GLU   A C    1 
ATOM   2943 C C    B GLU   A 1 120 ? 25.422 -13.813 12.939  0.58 14.68 ?  120 GLU   A C    1 
ATOM   2944 O O    A GLU   A 1 120 ? 24.455 -14.718 12.625  0.42 14.81 ?  120 GLU   A O    1 
ATOM   2945 O O    B GLU   A 1 120 ? 24.449 -14.581 12.864  0.58 15.00 ?  120 GLU   A O    1 
ATOM   2946 C CB   A GLU   A 1 120 ? 27.274 -14.967 14.153  0.42 21.10 ?  120 GLU   A CB   1 
ATOM   2947 C CB   B GLU   A 1 120 ? 27.325 -14.726 14.283  0.58 19.03 ?  120 GLU   A CB   1 
ATOM   2948 C CG   A GLU   A 1 120 ? 28.473 -15.903 14.146  0.42 26.30 ?  120 GLU   A CG   1 
ATOM   2949 C CG   B GLU   A 1 120 ? 28.524 -15.655 14.289  0.58 25.40 ?  120 GLU   A CG   1 
ATOM   2950 C CD   A GLU   A 1 120 ? 28.663 -16.628 15.463  0.42 30.77 ?  120 GLU   A CD   1 
ATOM   2951 C CD   B GLU   A 1 120 ? 28.649 -16.437 15.576  0.58 30.80 ?  120 GLU   A CD   1 
ATOM   2952 O OE1  A GLU   A 1 120 ? 28.346 -16.040 16.520  0.42 31.85 ?  120 GLU   A OE1  1 
ATOM   2953 O OE1  B GLU   A 1 120 ? 28.232 -15.913 16.632  0.58 32.01 ?  120 GLU   A OE1  1 
ATOM   2954 O OE2  A GLU   A 1 120 ? 29.123 -17.790 15.440  0.42 32.28 -1 120 GLU   A OE2  1 
ATOM   2955 O OE2  B GLU   A 1 120 ? 29.157 -17.578 15.530  0.58 32.94 -1 120 GLU   A OE2  1 
ATOM   2956 H H    A GLU   A 1 120 ? 28.397 -13.279 12.755  0.42 17.61 ?  120 GLU   A H    1 
ATOM   2957 H H    B GLU   A 1 120 ? 28.360 -13.120 12.761  0.58 16.66 ?  120 GLU   A H    1 
ATOM   2958 H HA   A GLU   A 1 120 ? 26.832 -15.305 12.194  0.42 20.21 ?  120 GLU   A HA   1 
ATOM   2959 H HA   B GLU   A 1 120 ? 26.793 -15.192 12.372  0.58 18.60 ?  120 GLU   A HA   1 
ATOM   2960 H HB2  A GLU   A 1 120 ? 27.511 -14.187 14.677  0.42 25.34 ?  120 GLU   A HB2  1 
ATOM   2961 H HB2  B GLU   A 1 120 ? 27.582 -13.913 14.747  0.58 22.85 ?  120 GLU   A HB2  1 
ATOM   2962 H HB3  A GLU   A 1 120 ? 26.536 -15.436 14.575  0.42 25.34 ?  120 GLU   A HB3  1 
ATOM   2963 H HB3  B GLU   A 1 120 ? 26.608 -15.166 14.769  0.58 22.85 ?  120 GLU   A HB3  1 
ATOM   2964 H HG2  A GLU   A 1 120 ? 28.352 -16.569 13.453  0.42 31.58 ?  120 GLU   A HG2  1 
ATOM   2965 H HG2  B GLU   A 1 120 ? 28.446 -16.281 13.552  0.58 30.50 ?  120 GLU   A HG2  1 
ATOM   2966 H HG3  A GLU   A 1 120 ? 29.276 -15.386 13.976  0.42 31.58 ?  120 GLU   A HG3  1 
ATOM   2967 H HG3  B GLU   A 1 120 ? 29.335 -15.133 14.199  0.58 30.50 ?  120 GLU   A HG3  1 
ATOM   2968 N N    A VAL   A 1 121 ? 25.273 -12.649 13.005  0.42 14.50 ?  121 VAL   A N    1 
ATOM   2969 N N    B VAL   A 1 121 ? 25.283 -12.498 13.126  0.58 14.01 ?  121 VAL   A N    1 
ATOM   2970 C CA   A VAL   A 1 121 ? 23.980 -11.974 13.091  0.42 14.55 ?  121 VAL   A CA   1 
ATOM   2971 C CA   B VAL   A 1 121 ? 23.975 -11.852 13.243  0.58 14.06 ?  121 VAL   A CA   1 
ATOM   2972 C C    A VAL   A 1 121 ? 24.121 -10.605 12.431  0.42 13.61 ?  121 VAL   A C    1 
ATOM   2973 C C    B VAL   A 1 121 ? 24.055 -10.489 12.575  0.58 12.81 ?  121 VAL   A C    1 
ATOM   2974 O O    A VAL   A 1 121 ? 25.151 -9.941  12.585  0.42 14.12 ?  121 VAL   A O    1 
ATOM   2975 O O    B VAL   A 1 121 ? 24.979 -9.720  12.858  0.58 11.83 ?  121 VAL   A O    1 
ATOM   2976 C CB   A VAL   A 1 121 ? 23.527 -11.798 14.562  0.42 16.95 ?  121 VAL   A CB   1 
ATOM   2977 C CB   B VAL   A 1 121 ? 23.529 -11.670 14.712  0.58 17.05 ?  121 VAL   A CB   1 
ATOM   2978 C CG1  A VAL   A 1 121 ? 22.136 -11.174 14.638  0.42 17.31 ?  121 VAL   A CG1  1 
ATOM   2979 C CG1  B VAL   A 1 121 ? 22.144 -11.039 14.774  0.58 17.45 ?  121 VAL   A CG1  1 
ATOM   2980 C CG2  A VAL   A 1 121 ? 23.553 -13.115 15.325  0.42 18.65 ?  121 VAL   A CG2  1 
ATOM   2981 C CG2  B VAL   A 1 121 ? 23.527 -12.986 15.467  0.58 18.79 ?  121 VAL   A CG2  1 
ATOM   2982 H H    A VAL   A 1 121 ? 25.934 -12.118 13.109  0.42 17.42 ?  121 VAL   A H    1 
ATOM   2983 H H    B VAL   A 1 121 ? 25.947 -11.938 13.194  0.58 16.83 ?  121 VAL   A H    1 
ATOM   2984 H HA   A VAL   A 1 121 ? 23.309 -12.499 12.622  0.42 17.48 ?  121 VAL   A HA   1 
ATOM   2985 H HA   B VAL   A 1 121 ? 23.314 -12.382 12.784  0.58 16.89 ?  121 VAL   A HA   1 
ATOM   2986 H HB   A VAL   A 1 121 ? 24.144 -11.196 15.003  0.42 20.36 ?  121 VAL   A HB   1 
ATOM   2987 H HB   B VAL   A 1 121 ? 24.147 -11.071 15.160  0.58 20.48 ?  121 VAL   A HB   1 
ATOM   2988 H HG11 A VAL   A 1 121 ? 21.837 -11.178 15.563  0.42 20.79 ?  121 VAL   A HG11 1 
ATOM   2989 H HG11 B VAL   A 1 121 ? 21.807 -11.105 15.682  0.58 20.96 ?  121 VAL   A HG11 1 
ATOM   2990 H HG12 A VAL   A 1 121 ? 22.178 -10.262 14.312  0.42 20.79 ?  121 VAL   A HG12 1 
ATOM   2991 H HG12 B VAL   A 1 121 ? 22.204 -10.107 14.513  0.58 20.96 ?  121 VAL   A HG12 1 
ATOM   2992 H HG13 A VAL   A 1 121 ? 21.524 -11.694 14.094  0.42 20.79 ?  121 VAL   A HG13 1 
ATOM   2993 H HG13 B VAL   A 1 121 ? 21.552 -11.516 14.169  0.58 20.96 ?  121 VAL   A HG13 1 
ATOM   2994 H HG21 A VAL   A 1 121 ? 23.200 -12.967 16.221  0.42 22.40 ?  121 VAL   A HG21 1 
ATOM   2995 H HG21 B VAL   A 1 121 ? 23.191 -12.834 16.368  0.58 22.56 ?  121 VAL   A HG21 1 
ATOM   2996 H HG22 A VAL   A 1 121 ? 23.000 -13.762 14.861  0.42 22.40 ?  121 VAL   A HG22 1 
ATOM   2997 H HG22 B VAL   A 1 121 ? 22.949 -13.615 15.006  0.58 22.56 ?  121 VAL   A HG22 1 
ATOM   2998 H HG23 A VAL   A 1 121 ? 24.464 -13.434 15.381  0.42 22.40 ?  121 VAL   A HG23 1 
ATOM   2999 H HG23 B VAL   A 1 121 ? 24.429 -13.333 15.507  0.58 22.56 ?  121 VAL   A HG23 1 
ATOM   3000 N N    . LEU   A 1 122 ? 23.079 -10.171 11.719  1.00 12.54 ?  122 LEU   A N    1 
ATOM   3001 C CA   . LEU   A 1 122 ? 23.073 -8.881  11.030  1.00 12.39 ?  122 LEU   A CA   1 
ATOM   3002 C C    . LEU   A 1 122 ? 21.667 -8.295  10.990  1.00 12.20 ?  122 LEU   A C    1 
ATOM   3003 O O    . LEU   A 1 122 ? 20.684 -9.024  10.835  1.00 13.20 ?  122 LEU   A O    1 
ATOM   3004 C CB   . LEU   A 1 122 ? 23.515 -8.990  9.567   1.00 13.78 ?  122 LEU   A CB   1 
ATOM   3005 C CG   . LEU   A 1 122 ? 24.727 -9.837  9.213   1.00 13.92 ?  122 LEU   A CG   1 
ATOM   3006 C CD1  . LEU   A 1 122 ? 24.339 -11.288 9.001   1.00 14.84 ?  122 LEU   A CD1  1 
ATOM   3007 C CD2  . LEU   A 1 122 ? 25.400 -9.282  7.968   1.00 13.50 ?  122 LEU   A CD2  1 
ATOM   3008 H H    A LEU   A 1 122 ? 22.343 -10.615 11.618  0.42 15.07 ?  122 LEU   A H    1 
ATOM   3009 H H    B LEU   A 1 122 ? 22.413 -10.686 11.519  0.58 15.07 ?  122 LEU   A H    1 
ATOM   3010 H HA   . LEU   A 1 122 ? 23.660 -8.260  11.487  1.00 14.89 ?  122 LEU   A HA   1 
ATOM   3011 H HB2  . LEU   A 1 122 ? 22.781 -9.355  9.056   1.00 16.55 ?  122 LEU   A HB2  1 
ATOM   3012 H HB3  . LEU   A 1 122 ? 23.712 -8.098  9.246   1.00 16.55 ?  122 LEU   A HB3  1 
ATOM   3013 H HG   . LEU   A 1 122 ? 25.380 -9.804  9.930   1.00 16.72 ?  122 LEU   A HG   1 
ATOM   3014 H HD11 . LEU   A 1 122 ? 25.119 -11.806 8.742   1.00 17.82 ?  122 LEU   A HD11 1 
ATOM   3015 H HD12 . LEU   A 1 122 ? 23.976 -11.644 9.832   1.00 17.82 ?  122 LEU   A HD12 1 
ATOM   3016 H HD13 . LEU   A 1 122 ? 23.664 -11.344 8.304   1.00 17.82 ?  122 LEU   A HD13 1 
ATOM   3017 H HD21 . LEU   A 1 122 ? 26.151 -9.852  7.716   1.00 16.22 ?  122 LEU   A HD21 1 
ATOM   3018 H HD22 . LEU   A 1 122 ? 24.759 -9.254  7.239   1.00 16.22 ?  122 LEU   A HD22 1 
ATOM   3019 H HD23 . LEU   A 1 122 ? 25.727 -8.384  8.150   1.00 16.22 ?  122 LEU   A HD23 1 
ATOM   3020 N N    . LEU   A 1 123 ? 21.596 -6.963  11.087  1.00 11.94 ?  123 LEU   A N    1 
ATOM   3021 C CA   . LEU   A 1 123 ? 20.426 -6.172  10.700  1.00 11.91 ?  123 LEU   A CA   1 
ATOM   3022 C C    . LEU   A 1 123 ? 20.692 -5.651  9.294   1.00 11.61 ?  123 LEU   A C    1 
ATOM   3023 O O    . LEU   A 1 123 ? 21.748 -5.053  9.056   1.00 12.18 ?  123 LEU   A O    1 
ATOM   3024 C CB   . LEU   A 1 123 ? 20.284 -4.994  11.665  1.00 12.63 ?  123 LEU   A CB   1 
ATOM   3025 C CG   . LEU   A 1 123 ? 19.246 -3.932  11.309  1.00 13.37 ?  123 LEU   A CG   1 
ATOM   3026 C CD1  . LEU   A 1 123 ? 17.828 -4.513  11.326  1.00 14.14 ?  123 LEU   A CD1  1 
ATOM   3027 C CD2  . LEU   A 1 123 ? 19.372 -2.755  12.261  1.00 13.98 ?  123 LEU   A CD2  1 
ATOM   3028 H H    . LEU   A 1 123 ? 22.239 -6.476  11.391  1.00 14.34 ?  123 LEU   A H    1 
ATOM   3029 H HA   . LEU   A 1 123 ? 19.620 -6.716  10.717  1.00 14.31 ?  123 LEU   A HA   1 
ATOM   3030 H HB2  . LEU   A 1 123 ? 20.032 -5.343  12.541  1.00 15.17 ?  123 LEU   A HB2  1 
ATOM   3031 H HB3  . LEU   A 1 123 ? 21.134 -4.546  11.732  1.00 15.17 ?  123 LEU   A HB3  1 
ATOM   3032 H HG   . LEU   A 1 123 ? 19.418 -3.602  10.413  1.00 16.06 ?  123 LEU   A HG   1 
ATOM   3033 H HD11 . LEU   A 1 123 ? 17.189 -3.802  11.168  1.00 16.98 ?  123 LEU   A HD11 1 
ATOM   3034 H HD12 . LEU   A 1 123 ? 17.754 -5.186  10.632  1.00 16.98 ?  123 LEU   A HD12 1 
ATOM   3035 H HD13 . LEU   A 1 123 ? 17.663 -4.917  12.195  1.00 16.98 ?  123 LEU   A HD13 1 
ATOM   3036 H HD21 . LEU   A 1 123 ? 18.712 -2.087  12.032  1.00 16.79 ?  123 LEU   A HD21 1 
ATOM   3037 H HD22 . LEU   A 1 123 ? 19.227 -3.070  13.169  1.00 16.79 ?  123 LEU   A HD22 1 
ATOM   3038 H HD23 . LEU   A 1 123 ? 20.265 -2.383  12.182  1.00 16.79 ?  123 LEU   A HD23 1 
ATOM   3039 N N    A ALA   A 1 124 ? 19.748 -5.842  8.375   0.42 11.13 ?  124 ALA   A N    1 
ATOM   3040 N N    B ALA   A 1 124 ? 19.758 -5.882  8.372   0.58 11.68 ?  124 ALA   A N    1 
ATOM   3041 C CA   A ALA   A 1 124 ? 20.039 -5.538  6.982   0.42 10.31 ?  124 ALA   A CA   1 
ATOM   3042 C CA   B ALA   A 1 124 ? 20.051 -5.650  6.967   0.58 11.34 ?  124 ALA   A CA   1 
ATOM   3043 C C    A ALA   A 1 124 ? 18.793 -5.054  6.259   0.42 11.34 ?  124 ALA   A C    1 
ATOM   3044 C C    B ALA   A 1 124 ? 18.834 -5.194  6.182   0.58 10.64 ?  124 ALA   A C    1 
ATOM   3045 O O    A ALA   A 1 124 ? 17.665 -5.320  6.695   0.42 11.74 ?  124 ALA   A O    1 
ATOM   3046 O O    B ALA   A 1 124 ? 17.700 -5.578  6.500   0.58 11.30 ?  124 ALA   A O    1 
ATOM   3047 C CB   A ALA   A 1 124 ? 20.587 -6.764  6.250   0.42 9.96  ?  124 ALA   A CB   1 
ATOM   3048 C CB   B ALA   A 1 124 ? 20.639 -6.905  6.312   0.58 12.48 ?  124 ALA   A CB   1 
ATOM   3049 H H    A ALA   A 1 124 ? 18.949 -6.131  8.536   0.42 13.37 ?  124 ALA   A H    1 
ATOM   3050 H H    B ALA   A 1 124 ? 18.955 -6.159  8.535   0.58 14.03 ?  124 ALA   A H    1 
ATOM   3051 H HA   A ALA   A 1 124 ? 20.712 -4.841  6.959   0.42 12.38 ?  124 ALA   A HA   1 
ATOM   3052 H HA   B ALA   A 1 124 ? 20.716 -4.955  6.915   0.58 13.63 ?  124 ALA   A HA   1 
ATOM   3053 H HB1  A ALA   A 1 124 ? 20.768 -6.519  5.331   0.42 11.97 ?  124 ALA   A HB1  1 
ATOM   3054 H HB1  B ALA   A 1 124 ? 20.823 -6.723  5.379   0.58 14.99 ?  124 ALA   A HB1  1 
ATOM   3055 H HB2  A ALA   A 1 124 ? 21.402 -7.052  6.687   0.42 11.97 ?  124 ALA   A HB2  1 
ATOM   3056 H HB2  B ALA   A 1 124 ? 21.465 -7.139  6.771   0.58 14.99 ?  124 ALA   A HB2  1 
ATOM   3057 H HB3  A ALA   A 1 124 ? 19.923 -7.469  6.283   0.42 11.97 ?  124 ALA   A HB3  1 
ATOM   3058 H HB3  B ALA   A 1 124 ? 20.004 -7.634  6.391   0.58 14.99 ?  124 ALA   A HB3  1 
ATOM   3059 N N    A PRO   A 1 125 ? 18.969 -4.348  5.145   0.42 12.04 ?  125 PRO   A N    1 
ATOM   3060 N N    B PRO   A 1 125 ? 19.048 -4.421  5.123   0.58 9.79  ?  125 PRO   A N    1 
ATOM   3061 C CA   A PRO   A 1 125 ? 17.899 -4.157  4.167   0.42 12.65 ?  125 PRO   A CA   1 
ATOM   3062 C CA   B PRO   A 1 125 ? 17.987 -4.093  4.177   0.58 10.25 ?  125 PRO   A CA   1 
ATOM   3063 C C    A PRO   A 1 125 ? 17.984 -5.205  3.057   0.42 12.44 ?  125 PRO   A C    1 
ATOM   3064 C C    B PRO   A 1 125 ? 17.961 -5.149  3.076   0.58 10.73 ?  125 PRO   A C    1 
ATOM   3065 O O    A PRO   A 1 125 ? 18.932 -5.991  2.976   0.42 12.74 ?  125 PRO   A O    1 
ATOM   3066 O O    B PRO   A 1 125 ? 18.891 -5.949  2.927   0.58 11.42 ?  125 PRO   A O    1 
ATOM   3067 C CB   A PRO   A 1 125 ? 18.235 -2.770  3.602   0.42 13.15 ?  125 PRO   A CB   1 
ATOM   3068 C CB   B PRO   A 1 125 ? 18.504 -2.770  3.591   0.58 10.34 ?  125 PRO   A CB   1 
ATOM   3069 C CG   A PRO   A 1 125 ? 19.745 -2.771  3.577   0.42 12.91 ?  125 PRO   A CG   1 
ATOM   3070 C CG   B PRO   A 1 125 ? 19.993 -3.034  3.448   0.58 9.60  ?  125 PRO   A CG   1 
ATOM   3071 C CD   A PRO   A 1 125 ? 20.163 -3.541  4.815   0.42 12.42 ?  125 PRO   A CD   1 
ATOM   3072 C CD   B PRO   A 1 125 ? 20.353 -3.917  4.644   0.58 9.25  ?  125 PRO   A CD   1 
ATOM   3073 H HA   A PRO   A 1 125 ? 17.026 -4.166  4.576   0.42 15.20 ?  125 PRO   A HA   1 
ATOM   3074 H HA   B PRO   A 1 125 ? 17.119 -3.975  4.604   0.58 12.31 ?  125 PRO   A HA   1 
ATOM   3075 H HB2  A PRO   A 1 125 ? 17.873 -2.670  2.708   0.42 15.79 ?  125 PRO   A HB2  1 
ATOM   3076 H HB2  B PRO   A 1 125 ? 18.092 -2.599  2.726   0.58 12.43 ?  125 PRO   A HB2  1 
ATOM   3077 H HB3  A PRO   A 1 125 ? 17.898 -2.079  4.196   0.42 15.79 ?  125 PRO   A HB3  1 
ATOM   3078 H HB3  B PRO   A 1 125 ? 18.333 -2.035  4.205   0.58 12.43 ?  125 PRO   A HB3  1 
ATOM   3079 H HG2  A PRO   A 1 125 ? 20.064 -3.218  2.776   0.42 15.50 ?  125 PRO   A HG2  1 
ATOM   3080 H HG2  B PRO   A 1 125 ? 20.169 -3.494  2.612   0.58 11.54 ?  125 PRO   A HG2  1 
ATOM   3081 H HG3  A PRO   A 1 125 ? 20.080 -1.858  3.611   0.42 15.50 ?  125 PRO   A HG3  1 
ATOM   3082 H HG3  B PRO   A 1 125 ? 20.482 -2.192  3.482   0.58 11.54 ?  125 PRO   A HG3  1 
ATOM   3083 H HD2  A PRO   A 1 125 ? 20.925 -4.108  4.622   0.42 14.93 ?  125 PRO   A HD2  1 
ATOM   3084 H HD2  B PRO   A 1 125 ? 20.920 -4.653  4.358   0.58 11.12 ?  125 PRO   A HD2  1 
ATOM   3085 H HD3  A PRO   A 1 125 ? 20.361 -2.925  5.543   0.42 14.93 ?  125 PRO   A HD3  1 
ATOM   3086 H HD3  B PRO   A 1 125 ? 20.785 -3.386  5.332   0.58 11.12 ?  125 PRO   A HD3  1 
ATOM   3087 N N    A LEU   A 1 126 ? 16.973 -5.191  2.186   0.42 12.54 ?  126 LEU   A N    1 
ATOM   3088 N N    B LEU   A 1 126 ? 16.906 -5.107  2.267   0.58 12.27 ?  126 LEU   A N    1 
ATOM   3089 C CA   A LEU   A 1 126 ? 16.974 -6.026  0.990   0.42 12.72 ?  126 LEU   A CA   1 
ATOM   3090 C CA   B LEU   A 1 126 ? 16.943 -5.845  1.014   0.58 13.11 ?  126 LEU   A CA   1 
ATOM   3091 C C    A LEU   A 1 126 ? 17.890 -5.417  -0.065  0.42 12.61 ?  126 LEU   A C    1 
ATOM   3092 C C    B LEU   A 1 126 ? 17.909 -5.161  0.054   0.58 13.32 ?  126 LEU   A C    1 
ATOM   3093 O O    A LEU   A 1 126 ? 17.612 -4.336  -0.599  0.42 12.76 ?  126 LEU   A O    1 
ATOM   3094 O O    B LEU   A 1 126 ? 17.852 -3.944  -0.142  0.58 14.95 ?  126 LEU   A O    1 
ATOM   3095 C CB   A LEU   A 1 126 ? 15.556 -6.189  0.454   0.42 13.56 ?  126 LEU   A CB   1 
ATOM   3096 C CB   B LEU   A 1 126 ? 15.554 -5.926  0.392   0.58 15.18 ?  126 LEU   A CB   1 
ATOM   3097 C CG   A LEU   A 1 126 ? 14.668 -7.100  1.297   0.42 13.78 ?  126 LEU   A CG   1 
ATOM   3098 C CG   B LEU   A 1 126 ? 14.605 -6.979  0.960   0.58 16.59 ?  126 LEU   A CG   1 
ATOM   3099 C CD1  A LEU   A 1 126 ? 13.231 -6.981  0.842   0.42 14.66 ?  126 LEU   A CD1  1 
ATOM   3100 C CD1  B LEU   A 1 126 ? 13.246 -6.821  0.315   0.58 16.87 ?  126 LEU   A CD1  1 
ATOM   3101 C CD2  A LEU   A 1 126 ? 15.138 -8.545  1.203   0.42 12.81 ?  126 LEU   A CD2  1 
ATOM   3102 C CD2  B LEU   A 1 126 ? 15.132 -8.398  0.737   0.58 17.27 ?  126 LEU   A CD2  1 
ATOM   3103 H H    A LEU   A 1 126 ? 16.268 -4.705  2.266   0.42 15.06 ?  126 LEU   A H    1 
ATOM   3104 H H    B LEU   A 1 126 ? 16.185 -4.643  2.402   0.58 14.74 ?  126 LEU   A H    1 
ATOM   3105 H HA   A LEU   A 1 126 ? 17.320 -6.902  1.210   0.42 15.29 ?  126 LEU   A HA   1 
ATOM   3106 H HA   B LEU   A 1 126 ? 17.262 -6.740  1.189   0.58 15.75 ?  126 LEU   A HA   1 
ATOM   3107 H HB2  A LEU   A 1 126 ? 15.130 -5.317  0.422   0.42 16.29 ?  126 LEU   A HB2  1 
ATOM   3108 H HB2  B LEU   A 1 126 ? 15.119 -5.067  0.503   0.58 18.23 ?  126 LEU   A HB2  1 
ATOM   3109 H HB3  A LEU   A 1 126 ? 15.595 -6.565  -0.440  0.42 16.29 ?  126 LEU   A HB3  1 
ATOM   3110 H HB3  B LEU   A 1 126 ? 15.656 -6.116  -0.551  0.58 18.23 ?  126 LEU   A HB3  1 
ATOM   3111 H HG   A LEU   A 1 126 ? 14.715 -6.829  2.228   0.42 16.55 ?  126 LEU   A HG   1 
ATOM   3112 H HG   B LEU   A 1 126 ? 14.506 -6.844  1.917   0.58 19.93 ?  126 LEU   A HG   1 
ATOM   3113 H HD11 A LEU   A 1 126 ? 12.678 -7.567  1.382   0.42 17.61 ?  126 LEU   A HD11 1 
ATOM   3114 H HD11 B LEU   A 1 126 ? 12.644 -7.493  0.673   0.58 20.27 ?  126 LEU   A HD11 1 
ATOM   3115 H HD12 A LEU   A 1 126 ? 12.944 -6.061  0.952   0.42 17.61 ?  126 LEU   A HD12 1 
ATOM   3116 H HD12 B LEU   A 1 126 ? 12.907 -5.934  0.512   0.58 20.27 ?  126 LEU   A HD12 1 
ATOM   3117 H HD13 A LEU   A 1 126 ? 13.175 -7.238  -0.091  0.42 17.61 ?  126 LEU   A HD13 1 
ATOM   3118 H HD13 B LEU   A 1 126 ? 13.338 -6.936  -0.644  0.58 20.27 ?  126 LEU   A HD13 1 
ATOM   3119 H HD21 A LEU   A 1 126 ? 14.475 -9.123  1.608   0.42 15.39 ?  126 LEU   A HD21 1 
ATOM   3120 H HD21 B LEU   A 1 126 ? 14.443 -9.038  0.975   0.58 20.74 ?  126 LEU   A HD21 1 
ATOM   3121 H HD22 A LEU   A 1 126 ? 15.253 -8.777  0.267   0.42 15.39 ?  126 LEU   A HD22 1 
ATOM   3122 H HD22 B LEU   A 1 126 ? 15.371 -8.504  -0.199  0.58 20.74 ?  126 LEU   A HD22 1 
ATOM   3123 H HD23 A LEU   A 1 126 ? 15.985 -8.634  1.669   0.42 15.39 ?  126 LEU   A HD23 1 
ATOM   3124 H HD23 B LEU   A 1 126 ? 15.918 -8.539  1.292   0.58 20.74 ?  126 LEU   A HD23 1 
ATOM   3125 N N    A LEU   A 1 127 ? 18.967 -6.130  -0.388  0.42 12.77 ?  127 LEU   A N    1 
ATOM   3126 N N    B LEU   A 1 127 ? 18.812 -5.937  -0.536  0.58 12.84 ?  127 LEU   A N    1 
ATOM   3127 C CA   A LEU   A 1 127 ? 19.944 -5.640  -1.348  0.42 12.63 ?  127 LEU   A CA   1 
ATOM   3128 C CA   B LEU   A 1 127 ? 19.829 -5.381  -1.415  0.58 13.65 ?  127 LEU   A CA   1 
ATOM   3129 C C    A LEU   A 1 127 ? 19.309 -5.451  -2.717  0.42 11.71 ?  127 LEU   A C    1 
ATOM   3130 C C    B LEU   A 1 127 ? 19.313 -5.252  -2.843  0.58 14.77 ?  127 LEU   A C    1 
ATOM   3131 O O    A LEU   A 1 127 ? 18.454 -6.235  -3.145  0.42 11.60 ?  127 LEU   A O    1 
ATOM   3132 O O    B LEU   A 1 127 ? 18.475 -6.033  -3.308  0.58 15.49 ?  127 LEU   A O    1 
ATOM   3133 C CB   A LEU   A 1 127 ? 21.109 -6.622  -1.457  0.42 13.51 ?  127 LEU   A CB   1 
ATOM   3134 C CB   B LEU   A 1 127 ? 21.102 -6.231  -1.401  0.58 13.57 ?  127 LEU   A CB   1 
ATOM   3135 C CG   A LEU   A 1 127 ? 21.910 -6.863  -0.179  0.42 13.86 ?  127 LEU   A CG   1 
ATOM   3136 C CG   B LEU   A 1 127 ? 21.884 -6.303  -0.081  0.58 14.28 ?  127 LEU   A CG   1 
ATOM   3137 C CD1  A LEU   A 1 127 ? 22.994 -7.882  -0.450  0.42 13.63 ?  127 LEU   A CD1  1 
ATOM   3138 C CD1  B LEU   A 1 127 ? 23.060 -7.271  -0.191  0.58 15.39 ?  127 LEU   A CD1  1 
ATOM   3139 C CD2  A LEU   A 1 127 ? 22.508 -5.574  0.342   0.42 14.95 ?  127 LEU   A CD2  1 
ATOM   3140 C CD2  B LEU   A 1 127 ? 22.356 -4.922  0.360   0.58 15.52 ?  127 LEU   A CD2  1 
ATOM   3141 H H    A LEU   A 1 127 ? 19.146 -6.911  -0.072  0.42 15.34 ?  127 LEU   A H    1 
ATOM   3142 H H    B LEU   A 1 127 ? 18.854 -6.795  -0.435  0.58 15.43 ?  127 LEU   A H    1 
ATOM   3143 H HA   A LEU   A 1 127 ? 20.288 -4.789  -1.054  0.42 15.17 ?  127 LEU   A HA   1 
ATOM   3144 H HA   B LEU   A 1 127 ? 20.057 -4.496  -1.097  0.58 16.40 ?  127 LEU   A HA   1 
ATOM   3145 H HB2  A LEU   A 1 127 ? 20.762 -7.484  -1.744  0.42 16.23 ?  127 LEU   A HB2  1 
ATOM   3146 H HB2  B LEU   A 1 127 ? 20.862 -7.138  -1.641  0.58 16.31 ?  127 LEU   A HB2  1 
ATOM   3147 H HB3  A LEU   A 1 127 ? 21.731 -6.292  -2.125  0.42 16.23 ?  127 LEU   A HB3  1 
ATOM   3148 H HB3  B LEU   A 1 127 ? 21.704 -5.870  -2.070  0.58 16.31 ?  127 LEU   A HB3  1 
ATOM   3149 H HG   A LEU   A 1 127 ? 21.322 -7.229  0.502   0.42 16.65 ?  127 LEU   A HG   1 
ATOM   3150 H HG   B LEU   A 1 127 ? 21.293 -6.643  0.609   0.58 17.15 ?  127 LEU   A HG   1 
ATOM   3151 H HD11 A LEU   A 1 127 ? 23.462 -8.075  0.378   0.42 16.38 ?  127 LEU   A HD11 1 
ATOM   3152 H HD11 B LEU   A 1 127 ? 23.533 -7.289  0.657   0.58 18.49 ?  127 LEU   A HD11 1 
ATOM   3153 H HD12 A LEU   A 1 127 ? 22.588 -8.694  -0.796  0.42 16.38 ?  127 LEU   A HD12 1 
ATOM   3154 H HD12 B LEU   A 1 127 ? 22.724 -8.155  -0.402  0.58 18.49 ?  127 LEU   A HD12 1 
ATOM   3155 H HD13 A LEU   A 1 127 ? 23.611 -7.518  -1.103  0.42 16.38 ?  127 LEU   A HD13 1 
ATOM   3156 H HD13 B LEU   A 1 127 ? 23.656 -6.965  -0.893  0.58 18.49 ?  127 LEU   A HD13 1 
ATOM   3157 H HD21 A LEU   A 1 127 ? 23.111 -5.779  1.072   0.42 17.96 ?  127 LEU   A HD21 1 
ATOM   3158 H HD21 B LEU   A 1 127 ? 22.935 -5.018  1.131   0.58 18.65 ?  127 LEU   A HD21 1 
ATOM   3159 H HD22 A LEU   A 1 127 ? 22.994 -5.142  -0.379  0.42 17.96 ?  127 LEU   A HD22 1 
ATOM   3160 H HD22 B LEU   A 1 127 ? 22.843 -4.508  -0.371  0.58 18.65 ?  127 LEU   A HD22 1 
ATOM   3161 H HD23 A LEU   A 1 127 ? 21.793 -5.000  0.651   0.42 17.96 ?  127 LEU   A HD23 1 
ATOM   3162 H HD23 B LEU   A 1 127 ? 21.583 -4.383  0.589   0.58 18.65 ?  127 LEU   A HD23 1 
ATOM   3163 N N    A SER   A 1 128 ? 19.752 -4.404  -3.408  0.42 12.01 ?  128 SER   A N    1 
ATOM   3164 N N    B SER   A 1 128 ? 19.823 -4.233  -3.528  0.58 15.84 ?  128 SER   A N    1 
ATOM   3165 C CA   A SER   A 1 128 ? 19.351 -4.029  -4.757  0.42 11.91 ?  128 SER   A CA   1 
ATOM   3166 C CA   B SER   A 1 128 ? 19.608 -3.943  -4.941  0.58 16.99 ?  128 SER   A CA   1 
ATOM   3167 C C    A SER   A 1 128 ? 17.904 -3.568  -4.855  0.42 11.43 ?  128 SER   A C    1 
ATOM   3168 C C    B SER   A 1 128 ? 18.228 -3.392  -5.261  0.58 19.12 ?  128 SER   A C    1 
ATOM   3169 O O    A SER   A 1 128 ? 17.452 -3.241  -5.960  0.42 12.06 ?  128 SER   A O    1 
ATOM   3170 O O    B SER   A 1 128 ? 17.871 -3.300  -6.442  0.58 19.62 ?  128 SER   A O    1 
ATOM   3171 C CB   A SER   A 1 128 ? 19.662 -5.105  -5.807  0.42 12.47 ?  128 SER   A CB   1 
ATOM   3172 C CB   B SER   A 1 128 ? 19.948 -5.119  -5.860  0.58 15.63 ?  128 SER   A CB   1 
ATOM   3173 O OG   A SER   A 1 128 ? 21.060 -5.345  -5.876  0.42 13.05 ?  128 SER   A OG   1 
ATOM   3174 O OG   B SER   A 1 128 ? 21.351 -5.298  -5.915  0.58 14.85 ?  128 SER   A OG   1 
ATOM   3175 H H    A SER   A 1 128 ? 20.333 -3.860  -3.087  0.42 14.42 ?  128 SER   A H    1 
ATOM   3176 H H    B SER   A 1 128 ? 20.334 -3.655  -3.158  0.58 19.03 ?  128 SER   A H    1 
ATOM   3177 H HA   A SER   A 1 128 ? 19.877 -3.266  -5.000  0.42 14.31 ?  128 SER   A HA   1 
ATOM   3178 H HA   B SER   A 1 128 ? 20.225 -3.241  -5.167  0.58 20.41 ?  128 SER   A HA   1 
ATOM   3179 H HB2  A SER   A 1 128 ? 19.206 -5.929  -5.572  0.42 14.98 ?  128 SER   A HB2  1 
ATOM   3180 H HB2  B SER   A 1 128 ? 19.523 -5.921  -5.520  0.58 18.78 ?  128 SER   A HB2  1 
ATOM   3181 H HB3  A SER   A 1 128 ? 19.361 -4.795  -6.677  0.42 14.98 ?  128 SER   A HB3  1 
ATOM   3182 H HB3  B SER   A 1 128 ? 19.622 -4.920  -6.754  0.58 18.78 ?  128 SER   A HB3  1 
ATOM   3183 H HG   A SER   A 1 128 ? 21.463 -4.635  -6.058  0.42 15.68 ?  128 SER   A HG   1 
ATOM   3184 H HG   B SER   A 1 128 ? 21.709 -4.584  -6.171  0.58 17.84 ?  128 SER   A HG   1 
ATOM   3185 N N    A ALA   A 1 129 ? 17.166 -3.517  -3.746  0.42 11.32 ?  129 ALA   A N    1 
ATOM   3186 N N    B ALA   A 1 129 ? 17.449 -3.003  -4.260  0.58 21.58 ?  129 ALA   A N    1 
ATOM   3187 C CA   A ALA   A 1 129 ? 15.801 -3.020  -3.770  0.42 11.84 ?  129 ALA   A CA   1 
ATOM   3188 C CA   B ALA   A 1 129 ? 16.209 -2.295  -4.526  0.58 23.86 ?  129 ALA   A CA   1 
ATOM   3189 C C    A ALA   A 1 129 ? 15.792 -1.492  -3.718  0.42 11.70 ?  129 ALA   A C    1 
ATOM   3190 C C    B ALA   A 1 129 ? 16.492 -0.796  -4.600  0.58 25.03 ?  129 ALA   A C    1 
ATOM   3191 O O    A ALA   A 1 129 ? 16.834 -0.832  -3.744  0.42 12.40 ?  129 ALA   A O    1 
ATOM   3192 O O    B ALA   A 1 129 ? 17.645 -0.357  -4.607  0.58 26.02 ?  129 ALA   A O    1 
ATOM   3193 C CB   A ALA   A 1 129 ? 14.995 -3.621  -2.617  0.42 12.14 ?  129 ALA   A CB   1 
ATOM   3194 C CB   B ALA   A 1 129 ? 15.156 -2.641  -3.481  0.58 24.62 ?  129 ALA   A CB   1 
ATOM   3195 H H    A ALA   A 1 129 ? 17.435 -3.766  -2.962  0.42 13.61 ?  129 ALA   A H    1 
ATOM   3196 H H    B ALA   A 1 129 ? 17.608 -3.139  -3.422  0.58 25.91 ?  129 ALA   A H    1 
ATOM   3197 H HA   A ALA   A 1 129 ? 15.378 -3.290  -4.594  0.42 14.23 ?  129 ALA   A HA   1 
ATOM   3198 H HA   B ALA   A 1 129 ? 15.869 -2.573  -5.390  0.58 28.65 ?  129 ALA   A HA   1 
ATOM   3199 H HB1  A ALA   A 1 129 ? 14.082 -3.290  -2.657  0.42 14.59 ?  129 ALA   A HB1  1 
ATOM   3200 H HB1  B ALA   A 1 129 ? 14.335 -2.174  -3.700  0.58 29.56 ?  129 ALA   A HB1  1 
ATOM   3201 H HB2  A ALA   A 1 129 ? 14.998 -4.588  -2.694  0.42 14.59 ?  129 ALA   A HB2  1 
ATOM   3202 H HB2  B ALA   A 1 129 ? 15.011 -3.598  -3.500  0.58 29.56 ?  129 ALA   A HB2  1 
ATOM   3203 H HB3  A ALA   A 1 129 ? 15.400 -3.359  -1.772  0.42 14.59 ?  129 ALA   A HB3  1 
ATOM   3204 H HB3  B ALA   A 1 129 ? 15.477 -2.365  -2.613  0.58 29.56 ?  129 ALA   A HB3  1 
ATOM   3205 N N    A GLY   A 1 130 ? 14.597 -0.922  -3.638  0.42 12.36 ?  130 GLY   A N    1 
ATOM   3206 N N    B GLY   A 1 130 ? 15.433 0.008   -4.652  0.58 25.01 ?  130 GLY   A N    1 
ATOM   3207 C CA   A GLY   A 1 130 ? 14.486 0.526   -3.571  0.42 12.81 ?  130 GLY   A CA   1 
ATOM   3208 C CA   B GLY   A 1 130 ? 15.619 1.439   -4.808  0.58 25.57 ?  130 GLY   A CA   1 
ATOM   3209 C C    A GLY   A 1 130 ? 15.083 1.176   -4.804  0.42 12.96 ?  130 GLY   A C    1 
ATOM   3210 C C    B GLY   A 1 130 ? 16.228 1.761   -6.158  0.58 25.63 ?  130 GLY   A C    1 
ATOM   3211 O O    A GLY   A 1 130 ? 14.847 0.745   -5.940  0.42 13.01 ?  130 GLY   A O    1 
ATOM   3212 O O    B GLY   A 1 130 ? 15.845 1.204   -7.191  0.58 25.20 ?  130 GLY   A O    1 
ATOM   3213 H H    A GLY   A 1 130 ? 13.850 -1.346  -3.631  0.42 14.84 ?  130 GLY   A H    1 
ATOM   3214 H H    B GLY   A 1 130 ? 14.615 -0.246  -4.600  0.58 30.03 ?  130 GLY   A H    1 
ATOM   3215 H HA2  A GLY   A 1 130 ? 13.551 0.774   -3.494  0.42 15.39 ?  130 GLY   A HA2  1 
ATOM   3216 H HA2  B GLY   A 1 130 ? 14.763 1.892   -4.733  0.58 30.70 ?  130 GLY   A HA2  1 
ATOM   3217 H HA3  A GLY   A 1 130 ? 14.959 0.852   -2.791  0.42 15.39 ?  130 GLY   A HA3  1 
ATOM   3218 H HA3  B GLY   A 1 130 ? 16.209 1.772   -4.115  0.58 30.70 ?  130 GLY   A HA3  1 
ATOM   3219 N N    A ILE   A 1 131 ? 15.887 2.221   -4.580  0.42 14.05 ?  131 ILE   A N    1 
ATOM   3220 N N    B ILE   A 1 131 ? 17.208 2.668   -6.151  0.58 26.63 ?  131 ILE   A N    1 
ATOM   3221 C CA   A ILE   A 1 131 ? 16.458 2.995   -5.678  0.42 14.28 ?  131 ILE   A CA   1 
ATOM   3222 C CA   B ILE   A 1 131 ? 17.802 3.136   -7.397  0.58 27.99 ?  131 ILE   A CA   1 
ATOM   3223 C C    A ILE   A 1 131 ? 17.492 2.225   -6.483  0.42 13.99 ?  131 ILE   A C    1 
ATOM   3224 C C    B ILE   A 1 131 ? 18.497 2.024   -8.169  0.58 27.42 ?  131 ILE   A C    1 
ATOM   3225 O O    A ILE   A 1 131 ? 17.917 2.715   -7.536  0.42 13.63 ?  131 ILE   A O    1 
ATOM   3226 O O    B ILE   A 1 131 ? 18.776 2.188   -9.361  0.58 27.98 ?  131 ILE   A O    1 
ATOM   3227 C CB   A ILE   A 1 131 ? 17.050 4.345   -5.220  0.42 15.52 ?  131 ILE   A CB   1 
ATOM   3228 C CB   B ILE   A 1 131 ? 18.749 4.328   -7.142  0.58 29.84 ?  131 ILE   A CB   1 
ATOM   3229 C CG1  A ILE   A 1 131 ? 18.343 4.145   -4.420  0.42 17.04 ?  131 ILE   A CG1  1 
ATOM   3230 C CG1  B ILE   A 1 131 ? 19.944 3.892   -6.291  0.58 30.94 ?  131 ILE   A CG1  1 
ATOM   3231 C CG2  A ILE   A 1 131 ? 16.030 5.119   -4.407  0.42 16.26 ?  131 ILE   A CG2  1 
ATOM   3232 C CG2  B ILE   A 1 131 ? 17.992 5.463   -6.470  0.58 30.13 ?  131 ILE   A CG2  1 
ATOM   3233 C CD1  A ILE   A 1 131 ? 18.999 5.452   -4.003  0.42 18.33 ?  131 ILE   A CD1  1 
ATOM   3234 C CD1  B ILE   A 1 131 ? 21.025 4.940   -6.172  0.58 31.85 ?  131 ILE   A CD1  1 
ATOM   3235 H H    A ILE   A 1 131 ? 16.103 2.500   -3.800  0.42 16.88 ?  131 ILE   A H    1 
ATOM   3236 H H    B ILE   A 1 131 ? 17.536 3.025   -5.445  0.58 31.97 ?  131 ILE   A H    1 
ATOM   3237 H HA   A ILE   A 1 131 ? 15.740 3.195   -6.294  0.42 17.15 ?  131 ILE   A HA   1 
ATOM   3238 H HA   B ILE   A 1 131 ? 17.091 3.458   -7.964  0.58 33.60 ?  131 ILE   A HA   1 
ATOM   3239 H HB   A ILE   A 1 131 ? 17.260 4.857   -6.015  0.42 18.64 ?  131 ILE   A HB   1 
ATOM   3240 H HB   B ILE   A 1 131 ? 19.078 4.645   -7.997  0.58 35.83 ?  131 ILE   A HB   1 
ATOM   3241 H HG12 A ILE   A 1 131 ? 18.139 3.640   -3.617  0.42 20.46 ?  131 ILE   A HG12 1 
ATOM   3242 H HG12 B ILE   A 1 131 ? 19.631 3.686   -5.397  0.58 37.15 ?  131 ILE   A HG12 1 
ATOM   3243 H HG13 A ILE   A 1 131 ? 18.984 3.657   -4.961  0.42 20.46 ?  131 ILE   A HG13 1 
ATOM   3244 H HG13 B ILE   A 1 131 ? 20.347 3.105   -6.687  0.58 37.15 ?  131 ILE   A HG13 1 
ATOM   3245 H HG21 A ILE   A 1 131 ? 16.340 6.030   -4.299  0.42 19.53 ?  131 ILE   A HG21 1 
ATOM   3246 H HG21 B ILE   A 1 131 ? 18.561 6.248   -6.438  0.58 36.17 ?  131 ILE   A HG21 1 
ATOM   3247 H HG22 A ILE   A 1 131 ? 15.181 5.111   -4.876  0.42 19.53 ?  131 ILE   A HG22 1 
ATOM   3248 H HG22 B ILE   A 1 131 ? 17.192 5.657   -6.985  0.58 36.17 ?  131 ILE   A HG22 1 
ATOM   3249 H HG23 A ILE   A 1 131 ? 15.931 4.694   -3.540  0.42 19.53 ?  131 ILE   A HG23 1 
ATOM   3250 H HG23 B ILE   A 1 131 ? 17.748 5.194   -5.571  0.58 36.17 ?  131 ILE   A HG23 1 
ATOM   3251 H HD11 A ILE   A 1 131 ? 19.873 5.261   -3.631  0.42 22.02 ?  131 ILE   A HD11 1 
ATOM   3252 H HD11 B ILE   A 1 131 ? 21.776 4.562   -5.690  0.58 38.24 ?  131 ILE   A HD11 1 
ATOM   3253 H HD12 A ILE   A 1 131 ? 19.088 6.022   -4.784  0.42 22.02 ?  131 ILE   A HD12 1 
ATOM   3254 H HD12 B ILE   A 1 131 ? 21.303 5.208   -7.061  0.58 38.24 ?  131 ILE   A HD12 1 
ATOM   3255 H HD13 A ILE   A 1 131 ? 18.443 5.887   -3.338  0.42 22.02 ?  131 ILE   A HD13 1 
ATOM   3256 H HD13 B ILE   A 1 131 ? 20.671 5.704   -5.693  0.58 38.24 ?  131 ILE   A HD13 1 
ATOM   3257 N N    A PHE   A 1 132 ? 17.911 1.038   -6.023  0.42 13.26 ?  132 PHE   A N    1 
ATOM   3258 N N    B PHE   A 1 132 ? 18.789 0.890   -7.529  0.58 26.25 ?  132 PHE   A N    1 
ATOM   3259 C CA   A PHE   A 1 132 ? 18.794 0.199   -6.826  0.42 13.77 ?  132 PHE   A CA   1 
ATOM   3260 C CA   B PHE   A 1 132 ? 19.443 -0.196  -8.247  0.58 25.72 ?  132 PHE   A CA   1 
ATOM   3261 C C    A PHE   A 1 132 ? 18.056 -0.549  -7.935  0.42 14.00 ?  132 PHE   A C    1 
ATOM   3262 C C    B PHE   A 1 132 ? 18.474 -1.035  -9.068  0.58 24.89 ?  132 PHE   A C    1 
ATOM   3263 O O    A PHE   A 1 132 ? 18.710 -1.150  -8.793  0.42 13.70 ?  132 PHE   A O    1 
ATOM   3264 O O    B PHE   A 1 132 ? 18.920 -1.813  -9.916  0.58 23.94 ?  132 PHE   A O    1 
ATOM   3265 C CB   A PHE   A 1 132 ? 19.581 -0.784  -5.947  0.42 12.81 ?  132 PHE   A CB   1 
ATOM   3266 C CB   B PHE   A 1 132 ? 20.275 -1.056  -7.293  0.58 26.58 ?  132 PHE   A CB   1 
ATOM   3267 C CG   A PHE   A 1 132 ? 20.802 -0.186  -5.277  0.42 12.75 ?  132 PHE   A CG   1 
ATOM   3268 C CG   B PHE   A 1 132 ? 21.574 -0.415  -6.881  0.58 27.91 ?  132 PHE   A CG   1 
ATOM   3269 C CD1  A PHE   A 1 132 ? 20.681 0.850   -4.368  0.42 12.92 ?  132 PHE   A CD1  1 
ATOM   3270 C CD1  B PHE   A 1 132 ? 21.899 0.872   -7.295  0.58 28.81 ?  132 PHE   A CD1  1 
ATOM   3271 C CD2  A PHE   A 1 132 ? 22.065 -0.696  -5.536  0.42 13.80 ?  132 PHE   A CD2  1 
ATOM   3272 C CD2  B PHE   A 1 132 ? 22.472 -1.101  -6.089  0.58 28.12 ?  132 PHE   A CD2  1 
ATOM   3273 C CE1  A PHE   A 1 132 ? 21.807 1.381   -3.748  0.42 13.01 ?  132 PHE   A CE1  1 
ATOM   3274 C CE1  B PHE   A 1 132 ? 23.087 1.456   -6.920  0.58 29.23 ?  132 PHE   A CE1  1 
ATOM   3275 C CE2  A PHE   A 1 132 ? 23.188 -0.175  -4.913  0.42 13.65 ?  132 PHE   A CE2  1 
ATOM   3276 C CE2  B PHE   A 1 132 ? 23.663 -0.521  -5.710  0.58 28.79 ?  132 PHE   A CE2  1 
ATOM   3277 C CZ   A PHE   A 1 132 ? 23.057 0.865   -4.020  0.42 12.85 ?  132 PHE   A CZ   1 
ATOM   3278 C CZ   B PHE   A 1 132 ? 23.972 0.758   -6.126  0.58 29.06 ?  132 PHE   A CZ   1 
ATOM   3279 H H    A PHE   A 1 132 ? 17.709 0.701   -5.249  0.42 15.93 ?  132 PHE   A H    1 
ATOM   3280 H H    B PHE   A 1 132 ? 18.617 0.727   -6.699  0.58 31.51 ?  132 PHE   A H    1 
ATOM   3281 H HA   A PHE   A 1 132 ? 19.442 0.772   -7.253  0.42 16.55 ?  132 PHE   A HA   1 
ATOM   3282 H HA   B PHE   A 1 132 ? 20.051 0.192   -8.890  0.58 30.88 ?  132 PHE   A HA   1 
ATOM   3283 H HB2  A PHE   A 1 132 ? 18.997 -1.115  -5.247  0.42 15.39 ?  132 PHE   A HB2  1 
ATOM   3284 H HB2  B PHE   A 1 132 ? 19.762 -1.218  -6.488  0.58 31.92 ?  132 PHE   A HB2  1 
ATOM   3285 H HB3  A PHE   A 1 132 ? 19.884 -1.524  -6.498  0.42 15.39 ?  132 PHE   A HB3  1 
ATOM   3286 H HB3  B PHE   A 1 132 ? 20.482 -1.899  -7.726  0.58 31.92 ?  132 PHE   A HB3  1 
ATOM   3287 H HD1  A PHE   A 1 132 ? 19.840 1.203   -4.176  0.42 15.52 ?  132 PHE   A HD1  1 
ATOM   3288 H HD1  B PHE   A 1 132 ? 21.305 1.350   -7.833  0.58 34.59 ?  132 PHE   A HD1  1 
ATOM   3289 H HD2  A PHE   A 1 132 ? 22.159 -1.398  -6.136  0.42 16.58 ?  132 PHE   A HD2  1 
ATOM   3290 H HD2  B PHE   A 1 132 ? 22.267 -1.963  -5.807  0.58 33.76 ?  132 PHE   A HD2  1 
ATOM   3291 H HE1  A PHE   A 1 132 ? 21.713 2.083   -3.141  0.42 15.63 ?  132 PHE   A HE1  1 
ATOM   3292 H HE1  B PHE   A 1 132 ? 23.291 2.319   -7.204  0.58 35.09 ?  132 PHE   A HE1  1 
ATOM   3293 H HE2  A PHE   A 1 132 ? 24.026 -0.521  -5.104  0.42 16.40 ?  132 PHE   A HE2  1 
ATOM   3294 H HE2  B PHE   A 1 132 ? 24.257 -0.992  -5.175  0.58 34.56 ?  132 PHE   A HE2  1 
ATOM   3295 H HZ   A PHE   A 1 132 ? 23.808 1.222   -3.605  0.42 15.43 ?  132 PHE   A HZ   1 
ATOM   3296 H HZ   B PHE   A 1 132 ? 24.774 1.148   -5.871  0.58 34.88 ?  132 PHE   A HZ   1 
ATOM   3297 N N    A GLY   A 1 133 ? 16.722 -0.542  -7.934  0.42 14.24 ?  133 GLY   A N    1 
ATOM   3298 N N    B GLY   A 1 133 ? 17.172 -0.889  -8.846  0.58 24.98 ?  133 GLY   A N    1 
ATOM   3299 C CA   A GLY   A 1 133 ? 15.943 -0.898  -9.105  0.42 14.53 ?  133 GLY   A CA   1 
ATOM   3300 C CA   B GLY   A 1 133 ? 16.187 -1.346  -9.802  0.58 25.35 ?  133 GLY   A CA   1 
ATOM   3301 C C    A GLY   A 1 133 ? 15.610 -2.361  -9.304  0.42 15.21 ?  133 GLY   A C    1 
ATOM   3302 C C    B GLY   A 1 133 ? 15.905 -2.832  -9.826  0.58 25.60 ?  133 GLY   A C    1 
ATOM   3303 O O    A GLY   A 1 133 ? 14.987 -2.692  -10.321 0.42 15.75 ?  133 GLY   A O    1 
ATOM   3304 O O    B GLY   A 1 133 ? 15.271 -3.304  -10.776 0.58 26.61 ?  133 GLY   A O    1 
ATOM   3305 H H    A GLY   A 1 133 ? 16.240 -0.330  -7.253  0.42 17.11 ?  133 GLY   A H    1 
ATOM   3306 H H    B GLY   A 1 133 ? 16.842 -0.520  -8.147  0.58 29.99 ?  133 GLY   A H    1 
ATOM   3307 H HA2  A GLY   A 1 133 ? 15.102 -0.412  -9.076  0.42 17.45 ?  133 GLY   A HA2  1 
ATOM   3308 H HA2  B GLY   A 1 133 ? 15.351 -0.901  -9.610  0.58 30.43 ?  133 GLY   A HA2  1 
ATOM   3309 H HA3  A GLY   A 1 133 ? 16.421 -0.611  -9.896  0.42 17.45 ?  133 GLY   A HA3  1 
ATOM   3310 H HA3  B GLY   A 1 133 ? 16.474 -1.072  -10.689 0.58 30.43 ?  133 GLY   A HA3  1 
ATOM   3311 N N    A ALA   A 1 134 ? 15.978 -3.246  -8.382  0.42 15.92 ?  134 ALA   A N    1 
ATOM   3312 N N    B ALA   A 1 134 ? 16.337 -3.587  -8.822  0.58 24.80 ?  134 ALA   A N    1 
ATOM   3313 C CA   A ALA   A 1 134 ? 15.661 -4.655  -8.560  0.42 16.66 ?  134 ALA   A CA   1 
ATOM   3314 C CA   B ALA   A 1 134 ? 16.004 -5.002  -8.757  0.58 24.66 ?  134 ALA   A CA   1 
ATOM   3315 C C    A ALA   A 1 134 ? 14.314 -5.001  -7.931  0.42 16.82 ?  134 ALA   A C    1 
ATOM   3316 C C    B ALA   A 1 134 ? 14.664 -5.190  -8.055  0.58 24.40 ?  134 ALA   A C    1 
ATOM   3317 O O    A ALA   A 1 134 ? 13.721 -4.218  -7.186  0.42 17.71 ?  134 ALA   A O    1 
ATOM   3318 O O    B ALA   A 1 134 ? 14.300 -4.429  -7.154  0.58 24.86 ?  134 ALA   A O    1 
ATOM   3319 C CB   A ALA   A 1 134 ? 16.755 -5.545  -7.980  0.42 17.50 ?  134 ALA   A CB   1 
ATOM   3320 C CB   B ALA   A 1 134 ? 17.086 -5.785  -8.014  0.58 25.20 ?  134 ALA   A CB   1 
ATOM   3321 H H    A ALA   A 1 134 ? 16.393 -3.056  -7.650  0.42 19.13 ?  134 ALA   A H    1 
ATOM   3322 H H    B ALA   A 1 134 ? 16.820 -3.300  -8.170  0.58 29.78 ?  134 ALA   A H    1 
ATOM   3323 H HA   A ALA   A 1 134 ? 15.594 -4.838  -9.505  0.42 20.01 ?  134 ALA   A HA   1 
ATOM   3324 H HA   B ALA   A 1 134 ? 15.938 -5.359  -9.658  0.58 29.61 ?  134 ALA   A HA   1 
ATOM   3325 H HB1  A ALA   A 1 134 ? 16.522 -6.471  -8.143  0.42 21.01 ?  134 ALA   A HB1  1 
ATOM   3326 H HB1  B ALA   A 1 134 ? 16.850 -6.726  -8.018  0.58 30.25 ?  134 ALA   A HB1  1 
ATOM   3327 H HB2  A ALA   A 1 134 ? 17.590 -5.327  -8.420  0.42 21.01 ?  134 ALA   A HB2  1 
ATOM   3328 H HB2  B ALA   A 1 134 ? 17.937 -5.656  -8.463  0.58 30.25 ?  134 ALA   A HB2  1 
ATOM   3329 H HB3  A ALA   A 1 134 ? 16.826 -5.380  -7.029  0.42 21.01 ?  134 ALA   A HB3  1 
ATOM   3330 H HB3  B ALA   A 1 134 ? 17.141 -5.460  -7.103  0.58 30.25 ?  134 ALA   A HB3  1 
ATOM   3331 N N    A ASP   A 1 135 ? 13.836 -6.202  -8.250  0.42 16.65 ?  135 ASP   A N    1 
ATOM   3332 N N    B ASP   A 1 135 ? 13.930 -6.210  -8.480  0.58 24.10 ?  135 ASP   A N    1 
ATOM   3333 C CA   A ASP   A 1 135 ? 12.581 -6.713  -7.709  0.42 16.88 ?  135 ASP   A CA   1 
ATOM   3334 C CA   B ASP   A 1 135 ? 12.628 -6.491  -7.885  0.58 24.54 ?  135 ASP   A CA   1 
ATOM   3335 C C    A ASP   A 1 135 ? 12.789 -7.142  -6.262  0.42 15.38 ?  135 ASP   A C    1 
ATOM   3336 C C    B ASP   A 1 135 ? 12.823 -6.998  -6.462  0.58 22.81 ?  135 ASP   A C    1 
ATOM   3337 O O    A ASP   A 1 135 ? 13.597 -8.043  -6.006  0.42 14.32 ?  135 ASP   A O    1 
ATOM   3338 O O    B ASP   A 1 135 ? 13.479 -8.031  -6.266  0.58 22.42 ?  135 ASP   A O    1 
ATOM   3339 C CB   A ASP   A 1 135 ? 12.131 -7.917  -8.530  0.42 18.58 ?  135 ASP   A CB   1 
ATOM   3340 C CB   B ASP   A 1 135 ? 11.885 -7.533  -8.711  0.58 27.08 ?  135 ASP   A CB   1 
ATOM   3341 C CG   A ASP   A 1 135 ? 10.850 -8.545  -8.013  0.42 20.64 ?  135 ASP   A CG   1 
ATOM   3342 C CG   B ASP   A 1 135 ? 10.449 -7.740  -8.254  0.58 29.51 ?  135 ASP   A CG   1 
ATOM   3343 O OD1  A ASP   A 1 135 ? 10.217 -7.978  -7.100  0.42 21.05 ?  135 ASP   A OD1  1 
ATOM   3344 O OD1  B ASP   A 1 135 ? 10.019 -7.070  -7.292  0.58 30.88 ?  135 ASP   A OD1  1 
ATOM   3345 O OD2  A ASP   A 1 135 ? 10.492 -9.628  -8.520  0.42 23.06 -1 135 ASP   A OD2  1 
ATOM   3346 O OD2  B ASP   A 1 135 ? 9.753  -8.587  -8.856  0.58 30.22 -1 135 ASP   A OD2  1 
ATOM   3347 H H    A ASP   A 1 135 ? 14.225 -6.755  -8.776  0.42 20.00 ?  135 ASP   A H    1 
ATOM   3348 H H    B ASP   A 1 135 ? 14.158 -6.752  -9.105  0.58 28.94 ?  135 ASP   A H    1 
ATOM   3349 H HA   A ASP   A 1 135 ? 11.896 -6.035  -7.754  0.42 20.27 ?  135 ASP   A HA   1 
ATOM   3350 H HA   B ASP   A 1 135 ? 12.110 -5.675  -7.877  0.58 29.47 ?  135 ASP   A HA   1 
ATOM   3351 H HB2  A ASP   A 1 135 ? 11.997 -7.640  -9.448  0.42 22.31 ?  135 ASP   A HB2  1 
ATOM   3352 H HB2  B ASP   A 1 135 ? 11.895 -7.254  -9.638  0.58 32.51 ?  135 ASP   A HB2  1 
ATOM   3353 H HB3  A ASP   A 1 135 ? 12.800 -8.612  -8.482  0.42 22.31 ?  135 ASP   A HB3  1 
ATOM   3354 H HB3  B ASP   A 1 135 ? 12.322 -8.385  -8.607  0.58 32.51 ?  135 ASP   A HB3  1 
ATOM   3355 N N    A PRO   A 1 136 ? 12.086 -6.543  -5.295  0.42 16.03 ?  136 PRO   A N    1 
ATOM   3356 N N    B PRO   A 1 136 ? 12.290 -6.313  -5.449  0.58 22.55 ?  136 PRO   A N    1 
ATOM   3357 C CA   A PRO   A 1 136 ? 12.301 -6.935  -3.889  0.42 15.69 ?  136 PRO   A CA   1 
ATOM   3358 C CA   B PRO   A 1 136 ? 12.513 -6.764  -4.063  0.58 22.17 ?  136 PRO   A CA   1 
ATOM   3359 C C    A PRO   A 1 136 ? 11.951 -8.380  -3.584  0.42 14.66 ?  136 PRO   A C    1 
ATOM   3360 C C    B PRO   A 1 136 ? 12.015 -8.174  -3.782  0.58 22.07 ?  136 PRO   A C    1 
ATOM   3361 O O    A PRO   A 1 136 ? 12.588 -8.980  -2.710  0.42 13.89 ?  136 PRO   A O    1 
ATOM   3362 O O    B PRO   A 1 136 ? 12.579 -8.854  -2.915  0.58 21.78 ?  136 PRO   A O    1 
ATOM   3363 C CB   A PRO   A 1 136 ? 11.417 -5.955  -3.104  0.42 16.67 ?  136 PRO   A CB   1 
ATOM   3364 C CB   B PRO   A 1 136 ? 11.792 -5.700  -3.220  0.58 22.34 ?  136 PRO   A CB   1 
ATOM   3365 C CG   A PRO   A 1 136 ? 10.417 -5.455  -4.100  0.42 17.07 ?  136 PRO   A CG   1 
ATOM   3366 C CG   B PRO   A 1 136 ? 10.939 -4.925  -4.192  0.58 22.79 ?  136 PRO   A CG   1 
ATOM   3367 C CD   A PRO   A 1 136 ? 11.118 -5.443  -5.419  0.42 16.46 ?  136 PRO   A CD   1 
ATOM   3368 C CD   B PRO   A 1 136 ? 11.594 -5.020  -5.513  0.58 22.95 ?  136 PRO   A CD   1 
ATOM   3369 H HA   A PRO   A 1 136 ? 13.226 -6.792  -3.638  0.42 18.85 ?  136 PRO   A HA   1 
ATOM   3370 H HA   B PRO   A 1 136 ? 13.458 -6.730  -3.854  0.58 26.62 ?  136 PRO   A HA   1 
ATOM   3371 H HB2  A PRO   A 1 136 ? 10.973 -6.423  -2.374  0.42 20.02 ?  136 PRO   A HB2  1 
ATOM   3372 H HB2  B PRO   A 1 136 ? 11.238 -6.128  -2.549  0.58 26.82 ?  136 PRO   A HB2  1 
ATOM   3373 H HB3  A PRO   A 1 136 ? 11.962 -5.231  -2.763  0.42 20.02 ?  136 PRO   A HB3  1 
ATOM   3374 H HB3  B PRO   A 1 136 ? 12.446 -5.117  -2.802  0.58 26.82 ?  136 PRO   A HB3  1 
ATOM   3375 H HG2  A PRO   A 1 136 ? 9.656  -6.055  -4.125  0.42 20.50 ?  136 PRO   A HG2  1 
ATOM   3376 H HG2  B PRO   A 1 136 ? 10.054 -5.317  -4.233  0.58 27.37 ?  136 PRO   A HG2  1 
ATOM   3377 H HG3  A PRO   A 1 136 ? 10.141 -4.560  -3.859  0.42 20.50 ?  136 PRO   A HG3  1 
ATOM   3378 H HG3  B PRO   A 1 136 ? 10.890 -3.998  -3.917  0.58 27.37 ?  136 PRO   A HG3  1 
ATOM   3379 H HD2  A PRO   A 1 136 ? 10.492 -5.629  -6.136  0.42 19.76 ?  136 PRO   A HD2  1 
ATOM   3380 H HD2  B PRO   A 1 136 ? 10.931 -5.026  -6.221  0.58 27.55 ?  136 PRO   A HD2  1 
ATOM   3381 H HD3  A PRO   A 1 136 ? 11.587 -4.609  -5.556  0.42 19.76 ?  136 PRO   A HD3  1 
ATOM   3382 H HD3  B PRO   A 1 136 ? 12.241 -4.308  -5.636  0.58 27.55 ?  136 PRO   A HD3  1 
ATOM   3383 N N    A ILE   A 1 137 ? 10.948 -8.953  -4.255  0.42 14.60 ?  137 ILE   A N    1 
ATOM   3384 N N    B ILE   A 1 137 ? 10.974 -8.631  -4.478  0.58 22.48 ?  137 ILE   A N    1 
ATOM   3385 C CA   A ILE   A 1 137 ? 10.611 -10.359 -4.037  0.42 14.61 ?  137 ILE   A CA   1 
ATOM   3386 C CA   B ILE   A 1 137 ? 10.545 -10.024 -4.365  0.58 23.20 ?  137 ILE   A CA   1 
ATOM   3387 C C    A ILE   A 1 137 ? 11.785 -11.252 -4.424  0.42 13.77 ?  137 ILE   A C    1 
ATOM   3388 C C    B ILE   A 1 137 ? 11.701 -10.960 -4.698  0.58 21.92 ?  137 ILE   A C    1 
ATOM   3389 O O    A ILE   A 1 137 ? 12.138 -12.189 -3.697  0.42 12.55 ?  137 ILE   A O    1 
ATOM   3390 O O    B ILE   A 1 137 ? 11.960 -11.944 -3.992  0.58 22.15 ?  137 ILE   A O    1 
ATOM   3391 C CB   A ILE   A 1 137 ? 9.319  -10.724 -4.795  0.42 16.14 ?  137 ILE   A CB   1 
ATOM   3392 C CB   B ILE   A 1 137 ? 9.328  -10.273 -5.276  0.58 25.14 ?  137 ILE   A CB   1 
ATOM   3393 C CG1  A ILE   A 1 137 ? 8.154  -9.852  -4.312  0.42 17.93 ?  137 ILE   A CG1  1 
ATOM   3394 C CG1  B ILE   A 1 137 ? 8.127  -9.449  -4.797  0.58 26.80 ?  137 ILE   A CG1  1 
ATOM   3395 C CG2  A ILE   A 1 137 ? 8.983  -12.201 -4.609  0.42 15.96 ?  137 ILE   A CG2  1 
ATOM   3396 C CG2  B ILE   A 1 137 ? 8.987  -11.750 -5.321  0.58 25.43 ?  137 ILE   A CG2  1 
ATOM   3397 C CD1  A ILE   A 1 137 ? 6.878  -10.011 -5.119  0.42 18.94 ?  137 ILE   A CD1  1 
ATOM   3398 C CD1  B ILE   A 1 137 ? 7.762  -8.284  -5.701  0.58 28.16 ?  137 ILE   A CD1  1 
ATOM   3399 H H    A ILE   A 1 137 ? 10.459 -8.563  -4.834  0.42 17.53 ?  137 ILE   A H    1 
ATOM   3400 H H    B ILE   A 1 137 ? 10.504 -8.157  -5.013  0.58 26.99 ?  137 ILE   A H    1 
ATOM   3401 H HA   A ILE   A 1 137 ? 10.443 -10.505 -3.092  0.42 17.55 ?  137 ILE   A HA   1 
ATOM   3402 H HA   B ILE   A 1 137 ? 10.273 -10.203 -3.453  0.58 27.85 ?  137 ILE   A HA   1 
ATOM   3403 H HB   A ILE   A 1 137 ? 9.453  -10.560 -5.736  0.42 19.38 ?  137 ILE   A HB   1 
ATOM   3404 H HB   B ILE   A 1 137 ? 9.558  -9.986  -6.175  0.58 30.19 ?  137 ILE   A HB   1 
ATOM   3405 H HG12 A ILE   A 1 137 ? 7.954  -10.078 -3.389  0.42 21.53 ?  137 ILE   A HG12 1 
ATOM   3406 H HG12 B ILE   A 1 137 ? 7.353  -10.028 -4.734  0.58 32.18 ?  137 ILE   A HG12 1 
ATOM   3407 H HG13 A ILE   A 1 137 ? 8.420  -8.919  -4.366  0.42 21.53 ?  137 ILE   A HG13 1 
ATOM   3408 H HG13 B ILE   A 1 137 ? 8.333  -9.083  -3.923  0.58 32.18 ?  137 ILE   A HG13 1 
ATOM   3409 H HG21 A ILE   A 1 137 ? 8.197  -12.423 -5.139  0.42 19.17 ?  137 ILE   A HG21 1 
ATOM   3410 H HG21 B ILE   A 1 137 ? 8.125  -11.860 -5.752  0.58 30.53 ?  137 ILE   A HG21 1 
ATOM   3411 H HG22 A ILE   A 1 137 ? 9.725  -12.745 -4.902  0.42 19.17 ?  137 ILE   A HG22 1 
ATOM   3412 H HG22 B ILE   A 1 137 ? 9.669  -12.214 -5.829  0.58 30.53 ?  137 ILE   A HG22 1 
ATOM   3413 H HG23 A ILE   A 1 137 ? 8.797  -12.369 -3.671  0.42 19.17 ?  137 ILE   A HG23 1 
ATOM   3414 H HG23 B ILE   A 1 137 ? 8.952  -12.092 -4.416  0.58 30.53 ?  137 ILE   A HG23 1 
ATOM   3415 H HD11 A ILE   A 1 137 ? 6.157  -9.605  -4.622  0.42 22.75 ?  137 ILE   A HD11 1 
ATOM   3416 H HD11 B ILE   A 1 137 ? 6.865  -7.983  -5.480  0.58 33.81 ?  137 ILE   A HD11 1 
ATOM   3417 H HD12 A ILE   A 1 137 ? 6.989  -9.571  -5.975  0.42 22.75 ?  137 ILE   A HD12 1 
ATOM   3418 H HD12 B ILE   A 1 137 ? 8.394  -7.563  -5.563  0.58 33.81 ?  137 ILE   A HD12 1 
ATOM   3419 H HD13 A ILE   A 1 137 ? 6.690  -10.953 -5.250  0.42 22.75 ?  137 ILE   A HD13 1 
ATOM   3420 H HD13 B ILE   A 1 137 ? 7.787  -8.579  -6.623  0.58 33.81 ?  137 ILE   A HD13 1 
ATOM   3421 N N    A HIS   A 1 138 ? 12.421 -10.968 -5.561  0.42 14.67 ?  138 HIS   A N    1 
ATOM   3422 N N    B HIS   A 1 138 ? 12.416 -10.663 -5.782  0.58 20.79 ?  138 HIS   A N    1 
ATOM   3423 C CA   A HIS   A 1 138 ? 13.603 -11.730 -5.954  0.42 15.04 ?  138 HIS   A CA   1 
ATOM   3424 C CA   B HIS   A 1 138 ? 13.562 -11.480 -6.160  0.58 19.82 ?  138 HIS   A CA   1 
ATOM   3425 C C    A HIS   A 1 138 ? 14.743 -11.536 -4.957  0.42 14.18 ?  138 HIS   A C    1 
ATOM   3426 C C    B HIS   A 1 138 ? 14.679 -11.378 -5.130  0.58 18.25 ?  138 HIS   A C    1 
ATOM   3427 O O    A HIS   A 1 138 ? 15.449 -12.493 -4.613  0.42 14.21 ?  138 HIS   A O    1 
ATOM   3428 O O    B HIS   A 1 138 ? 15.303 -12.388 -4.781  0.58 18.77 ?  138 HIS   A O    1 
ATOM   3429 C CB   A HIS   A 1 138 ? 14.040 -11.318 -7.359  0.42 16.04 ?  138 HIS   A CB   1 
ATOM   3430 C CB   B HIS   A 1 138 ? 14.056 -11.056 -7.541  0.58 20.25 ?  138 HIS   A CB   1 
ATOM   3431 C CG   A HIS   A 1 138 ? 15.298 -11.985 -7.821  0.42 17.10 ?  138 HIS   A CG   1 
ATOM   3432 C CG   B HIS   A 1 138 ? 15.323 -11.730 -7.961  0.58 20.73 ?  138 HIS   A CG   1 
ATOM   3433 N ND1  A HIS   A 1 138 ? 15.380 -13.341 -8.055  0.42 18.38 ?  138 HIS   A ND1  1 
ATOM   3434 N ND1  B HIS   A 1 138 ? 15.395 -13.079 -8.230  0.58 21.71 ?  138 HIS   A ND1  1 
ATOM   3435 C CD2  A HIS   A 1 138 ? 16.527 -11.484 -8.086  0.42 17.44 ?  138 HIS   A CD2  1 
ATOM   3436 C CD2  B HIS   A 1 138 ? 16.570 -11.240 -8.156  0.58 21.04 ?  138 HIS   A CD2  1 
ATOM   3437 C CE1  A HIS   A 1 138 ? 16.603 -13.645 -8.451  0.42 18.86 ?  138 HIS   A CE1  1 
ATOM   3438 C CE1  B HIS   A 1 138 ? 16.631 -13.391 -8.577  0.58 21.82 ?  138 HIS   A CE1  1 
ATOM   3439 N NE2  A HIS   A 1 138 ? 17.321 -12.536 -8.474  0.42 17.85 ?  138 HIS   A NE2  1 
ATOM   3440 N NE2  B HIS   A 1 138 ? 17.365 -12.294 -8.536  0.58 21.20 ?  138 HIS   A NE2  1 
ATOM   3441 H H    A HIS   A 1 138 ? 12.195 -10.351 -6.109  0.42 17.62 ?  138 HIS   A H    1 
ATOM   3442 H H    B HIS   A 1 138 ? 12.260 -10.004 -6.304  0.58 24.96 ?  138 HIS   A H    1 
ATOM   3443 H HA   A HIS   A 1 138 ? 13.380 -12.676 -5.979  0.42 18.06 ?  138 HIS   A HA   1 
ATOM   3444 H HA   B HIS   A 1 138 ? 13.290 -12.407 -6.207  0.58 23.80 ?  138 HIS   A HA   1 
ATOM   3445 H HB2  A HIS   A 1 138 ? 13.338 -11.546 -7.986  0.42 19.26 ?  138 HIS   A HB2  1 
ATOM   3446 H HB2  B HIS   A 1 138 ? 13.372 -11.275 -8.191  0.58 24.32 ?  138 HIS   A HB2  1 
ATOM   3447 H HB3  A HIS   A 1 138 ? 14.194 -10.361 -7.369  0.42 19.26 ?  138 HIS   A HB3  1 
ATOM   3448 H HB3  B HIS   A 1 138 ? 14.214 -10.100 -7.535  0.58 24.32 ?  138 HIS   A HB3  1 
ATOM   3449 H HD1  A HIS   A 1 138 ? 14.733 -13.902 -7.964  0.42 22.08 ?  138 HIS   A HD1  1 
ATOM   3450 H HD2  A HIS   A 1 138 ? 16.786 -10.594 -8.020  0.42 20.94 ?  138 HIS   A HD2  1 
ATOM   3451 H HD2  B HIS   A 1 138 ? 16.836 -10.357 -8.052  0.58 25.27 ?  138 HIS   A HD2  1 
ATOM   3452 H HE1  A HIS   A 1 138 ? 16.906 -14.496 -8.674  0.42 22.65 ?  138 HIS   A HE1  1 
ATOM   3453 H HE1  B HIS   A 1 138 ? 16.932 -14.242 -8.804  0.58 26.20 ?  138 HIS   A HE1  1 
ATOM   3454 H HE2  B HIS   A 1 138 ? 18.200 -12.247 -8.723  0.58 25.46 ?  138 HIS   A HE2  1 
ATOM   3455 N N    A SER   A 1 139 ? 14.941 -10.305 -4.485  0.42 14.01 ?  139 SER   A N    1 
ATOM   3456 N N    B SER   A 1 139 ? 14.939 -10.173 -4.622  0.58 16.95 ?  139 SER   A N    1 
ATOM   3457 C CA   A SER   A 1 139 ? 15.997 -10.045 -3.513  0.42 13.82 ?  139 SER   A CA   1 
ATOM   3458 C CA   B SER   A 1 139 ? 16.018 -10.002 -3.659  0.58 16.43 ?  139 SER   A CA   1 
ATOM   3459 C C    A SER   A 1 139 ? 15.794 -10.870 -2.246  0.42 13.15 ?  139 SER   A C    1 
ATOM   3460 C C    B SER   A 1 139 ? 15.779 -10.816 -2.392  0.58 16.15 ?  139 SER   A C    1 
ATOM   3461 O O    A SER   A 1 139 ? 16.733 -11.509 -1.752  0.42 12.20 ?  139 SER   A O    1 
ATOM   3462 O O    B SER   A 1 139 ? 16.738 -11.310 -1.785  0.58 16.03 ?  139 SER   A O    1 
ATOM   3463 C CB   A SER   A 1 139 ? 16.049 -8.551  -3.190  0.42 13.94 ?  139 SER   A CB   1 
ATOM   3464 C CB   B SER   A 1 139 ? 16.191 -8.522  -3.327  0.58 16.06 ?  139 SER   A CB   1 
ATOM   3465 O OG   A SER   A 1 139 ? 17.083 -8.276  -2.263  0.42 13.90 ?  139 SER   A OG   1 
ATOM   3466 O OG   B SER   A 1 139 ? 17.322 -8.349  -2.502  0.58 16.18 ?  139 SER   A OG   1 
ATOM   3467 H H    A SER   A 1 139 ? 14.483 -9.620  -4.708  0.42 16.83 ?  139 SER   A H    1 
ATOM   3468 H H    B SER   A 1 139 ? 14.510 -9.455  -4.806  0.58 20.36 ?  139 SER   A H    1 
ATOM   3469 H HA   A SER   A 1 139 ? 16.852 -10.297 -3.898  0.42 16.60 ?  139 SER   A HA   1 
ATOM   3470 H HA   B SER   A 1 139 ? 16.848 -10.312 -4.051  0.58 19.74 ?  139 SER   A HA   1 
ATOM   3471 H HB2  A SER   A 1 139 ? 16.215 -8.056  -4.004  0.42 16.75 ?  139 SER   A HB2  1 
ATOM   3472 H HB2  B SER   A 1 139 ? 16.327 -8.022  -4.146  0.58 19.29 ?  139 SER   A HB2  1 
ATOM   3473 H HB3  A SER   A 1 139 ? 15.204 -8.280  -2.801  0.42 16.75 ?  139 SER   A HB3  1 
ATOM   3474 H HB3  B SER   A 1 139 ? 15.402 -8.199  -2.863  0.58 19.29 ?  139 SER   A HB3  1 
ATOM   3475 H HG   A SER   A 1 139 ? 17.840 -8.338  -2.629  0.42 16.69 ?  139 SER   A HG   1 
ATOM   3476 H HG   B SER   A 1 139 ? 17.421 -7.541  -2.304  0.58 19.43 ?  139 SER   A HG   1 
ATOM   3477 N N    A LEU   A 1 140 ? 14.576 -10.860 -1.698  0.42 13.29 ?  140 LEU   A N    1 
ATOM   3478 N N    B LEU   A 1 140 ? 14.519 -10.970 -1.979  0.58 15.54 ?  140 LEU   A N    1 
ATOM   3479 C CA   A LEU   A 1 140 ? 14.294 -11.683 -0.526  0.42 12.79 ?  140 LEU   A CA   1 
ATOM   3480 C CA   B LEU   A 1 140 ? 14.237 -11.763 -0.786  0.58 15.15 ?  140 LEU   A CA   1 
ATOM   3481 C C    A LEU   A 1 140 ? 14.560 -13.159 -0.809  0.42 12.55 ?  140 LEU   A C    1 
ATOM   3482 C C    B LEU   A 1 140 ? 14.513 -13.241 -1.033  0.58 16.06 ?  140 LEU   A C    1 
ATOM   3483 O O    A LEU   A 1 140 ? 15.124 -13.868 0.034   0.42 13.06 ?  140 LEU   A O    1 
ATOM   3484 O O    B LEU   A 1 140 ? 15.041 -13.934 -0.155  0.58 16.82 ?  140 LEU   A O    1 
ATOM   3485 C CB   A LEU   A 1 140 ? 12.847 -11.473 -0.075  0.42 13.31 ?  140 LEU   A CB   1 
ATOM   3486 C CB   B LEU   A 1 140 ? 12.788 -11.553 -0.348  0.58 15.36 ?  140 LEU   A CB   1 
ATOM   3487 C CG   A LEU   A 1 140 ? 12.377 -12.392 1.059   0.42 13.69 ?  140 LEU   A CG   1 
ATOM   3488 C CG   B LEU   A 1 140 ? 12.304 -12.283 0.911   0.58 15.57 ?  140 LEU   A CG   1 
ATOM   3489 C CD1  A LEU   A 1 140 ? 13.246 -12.211 2.294   0.42 13.56 ?  140 LEU   A CD1  1 
ATOM   3490 C CD1  B LEU   A 1 140 ? 13.162 -11.959 2.129   0.58 15.30 ?  140 LEU   A CD1  1 
ATOM   3491 C CD2  A LEU   A 1 140 ? 10.906 -12.161 1.395   0.42 14.37 ?  140 LEU   A CD2  1 
ATOM   3492 C CD2  B LEU   A 1 140 ? 10.837 -11.952 1.189   0.58 16.53 ?  140 LEU   A CD2  1 
ATOM   3493 H H    A LEU   A 1 140 ? 13.918 -10.388 -1.974  0.42 15.96 ?  140 LEU   A H    1 
ATOM   3494 H H    B LEU   A 1 140 ? 13.828 -10.633 -2.363  0.58 18.66 ?  140 LEU   A H    1 
ATOM   3495 H HA   A LEU   A 1 140 ? 14.870 -11.410 0.205   0.42 15.37 ?  140 LEU   A HA   1 
ATOM   3496 H HA   B LEU   A 1 140 ? 14.812 -11.469 -0.065  0.58 18.19 ?  140 LEU   A HA   1 
ATOM   3497 H HB2  A LEU   A 1 140 ? 12.744 -10.559 0.236   0.42 15.99 ?  140 LEU   A HB2  1 
ATOM   3498 H HB2  B LEU   A 1 140 ? 12.654 -10.611 -0.190  0.58 18.45 ?  140 LEU   A HB2  1 
ATOM   3499 H HB3  A LEU   A 1 140 ? 12.258 -11.626 -0.830  0.42 15.99 ?  140 LEU   A HB3  1 
ATOM   3500 H HB3  B LEU   A 1 140 ? 12.211 -11.844 -1.072  0.58 18.45 ?  140 LEU   A HB3  1 
ATOM   3501 H HG   A LEU   A 1 140 ? 12.461 -13.317 0.776   0.42 16.45 ?  140 LEU   A HG   1 
ATOM   3502 H HG   B LEU   A 1 140 ? 12.359 -13.242 0.764   0.58 18.70 ?  140 LEU   A HG   1 
ATOM   3503 H HD11 A LEU   A 1 140 ? 12.869 -12.730 3.022   0.42 16.29 ?  140 LEU   A HD11 1 
ATOM   3504 H HD11 B LEU   A 1 140 ? 12.780 -12.393 2.910   0.58 18.37 ?  140 LEU   A HD11 1 
ATOM   3505 H HD12 A LEU   A 1 140 ? 14.142 -12.522 2.096   0.42 16.29 ?  140 LEU   A HD12 1 
ATOM   3506 H HD12 B LEU   A 1 140 ? 14.061 -12.286 1.976   0.58 18.37 ?  140 LEU   A HD12 1 
ATOM   3507 H HD13 A LEU   A 1 140 ? 13.261 -11.272 2.530   0.42 16.29 ?  140 LEU   A HD13 1 
ATOM   3508 H HD13 B LEU   A 1 140 ? 13.172 -10.999 2.259   0.58 18.37 ?  140 LEU   A HD13 1 
ATOM   3509 H HD21 A LEU   A 1 140 ? 10.646 -12.761 2.114   0.42 17.26 ?  140 LEU   A HD21 1 
ATOM   3510 H HD21 B LEU   A 1 140 ? 10.550 -12.422 1.990   0.58 19.85 ?  140 LEU   A HD21 1 
ATOM   3511 H HD22 A LEU   A 1 140 ? 10.785 -11.240 1.674   0.42 17.26 ?  140 LEU   A HD22 1 
ATOM   3512 H HD22 B LEU   A 1 140 ? 10.748 -10.996 1.320   0.58 19.85 ?  140 LEU   A HD22 1 
ATOM   3513 H HD23 A LEU   A 1 140 ? 10.369 -12.341 0.607   0.42 17.26 ?  140 LEU   A HD23 1 
ATOM   3514 H HD23 B LEU   A 1 140 ? 10.300 -12.235 0.433   0.58 19.85 ?  140 LEU   A HD23 1 
ATOM   3515 N N    A ARG   A 1 141 ? 14.154 -13.640 -1.987  0.42 12.64 ?  141 ARG   A N    1 
ATOM   3516 N N    B ARG   A 1 141 ? 14.157 -13.741 -2.218  0.58 16.92 ?  141 ARG   A N    1 
ATOM   3517 C CA   A ARG   A 1 141 ? 14.382 -15.038 -2.346  0.42 13.53 ?  141 ARG   A CA   1 
ATOM   3518 C CA   B ARG   A 1 141 ? 14.423 -15.138 -2.543  0.58 18.48 ?  141 ARG   A CA   1 
ATOM   3519 C C    A ARG   A 1 141 ? 15.874 -15.360 -2.339  0.42 13.22 ?  141 ARG   A C    1 
ATOM   3520 C C    B ARG   A 1 141 ? 15.921 -15.426 -2.557  0.58 17.25 ?  141 ARG   A C    1 
ATOM   3521 O O    A ARG   A 1 141 ? 16.315 -16.322 -1.696  0.42 12.83 ?  141 ARG   A O    1 
ATOM   3522 O O    B ARG   A 1 141 ? 16.364 -16.475 -2.074  0.58 16.60 ?  141 ARG   A O    1 
ATOM   3523 C CB   A ARG   A 1 141 ? 13.766 -15.317 -3.722  0.42 14.57 ?  141 ARG   A CB   1 
ATOM   3524 C CB   B ARG   A 1 141 ? 13.791 -15.483 -3.891  0.58 21.40 ?  141 ARG   A CB   1 
ATOM   3525 C CG   A ARG   A 1 141 ? 13.818 -16.776 -4.180  0.42 16.49 ?  141 ARG   A CG   1 
ATOM   3526 C CG   B ARG   A 1 141 ? 12.273 -15.367 -3.924  0.58 24.73 ?  141 ARG   A CG   1 
ATOM   3527 C CD   A ARG   A 1 141 ? 12.779 -17.604 -3.468  0.42 18.57 ?  141 ARG   A CD   1 
ATOM   3528 C CD   B ARG   A 1 141 ? 11.724 -15.832 -5.267  0.58 27.47 ?  141 ARG   A CD   1 
ATOM   3529 N NE   A ARG   A 1 141 ? 13.372 -18.438 -2.433  0.42 19.19 ?  141 ARG   A NE   1 
ATOM   3530 N NE   B ARG   A 1 141 ? 10.310 -16.184 -5.198  0.58 29.60 ?  141 ARG   A NE   1 
ATOM   3531 C CZ   A ARG   A 1 141 ? 12.683 -19.016 -1.459  0.42 19.54 ?  141 ARG   A CZ   1 
ATOM   3532 C CZ   B ARG   A 1 141 ? 9.337  -15.564 -5.849  0.58 31.40 ?  141 ARG   A CZ   1 
ATOM   3533 N NH1  A ARG   A 1 141 ? 11.384 -18.814 -1.319  0.42 19.76 ?  141 ARG   A NH1  1 
ATOM   3534 N NH1  B ARG   A 1 141 ? 9.585  -14.574 -6.688  0.58 31.98 ?  141 ARG   A NH1  1 
ATOM   3535 N NH2  A ARG   A 1 141 ? 13.314 -19.811 -0.602  0.42 19.61 ?  141 ARG   A NH2  1 
ATOM   3536 N NH2  B ARG   A 1 141 ? 8.080  -15.966 -5.668  0.58 32.12 ?  141 ARG   A NH2  1 
ATOM   3537 H H    A ARG   A 1 141 ? 13.748 -13.178 -2.586  0.42 15.19 ?  141 ARG   A H    1 
ATOM   3538 H H    B ARG   A 1 141 ? 13.759 -13.298 -2.836  0.58 20.32 ?  141 ARG   A H    1 
ATOM   3539 H HA   A ARG   A 1 141 ? 13.943 -15.611 -1.700  0.42 16.26 ?  141 ARG   A HA   1 
ATOM   3540 H HA   B ARG   A 1 141 ? 14.016 -15.704 -1.869  0.58 22.19 ?  141 ARG   A HA   1 
ATOM   3541 H HB2  A ARG   A 1 141 ? 12.832 -15.046 -3.706  0.42 17.50 ?  141 ARG   A HB2  1 
ATOM   3542 H HB2  B ARG   A 1 141 ? 14.145 -14.882 -4.564  0.58 25.69 ?  141 ARG   A HB2  1 
ATOM   3543 H HB3  A ARG   A 1 141 ? 14.239 -14.789 -4.383  0.42 17.50 ?  141 ARG   A HB3  1 
ATOM   3544 H HB3  B ARG   A 1 141 ? 14.019 -16.398 -4.116  0.58 25.69 ?  141 ARG   A HB3  1 
ATOM   3545 H HG2  A ARG   A 1 141 ? 13.643 -16.821 -5.134  0.42 19.81 ?  141 ARG   A HG2  1 
ATOM   3546 H HG2  B ARG   A 1 141 ? 11.891 -15.924 -3.229  0.58 29.69 ?  141 ARG   A HG2  1 
ATOM   3547 H HG3  A ARG   A 1 141 ? 14.693 -17.148 -3.984  0.42 19.81 ?  141 ARG   A HG3  1 
ATOM   3548 H HG3  B ARG   A 1 141 ? 12.017 -14.441 -3.794  0.58 29.69 ?  141 ARG   A HG3  1 
ATOM   3549 H HD2  A ARG   A 1 141 ? 12.134 -17.017 -3.044  0.42 22.30 ?  141 ARG   A HD2  1 
ATOM   3550 H HD2  B ARG   A 1 141 ? 11.851 -15.127 -5.917  0.58 32.99 ?  141 ARG   A HD2  1 
ATOM   3551 H HD3  A ARG   A 1 141 ? 12.333 -18.179 -4.112  0.42 22.30 ?  141 ARG   A HD3  1 
ATOM   3552 H HD3  B ARG   A 1 141 ? 12.206 -16.624 -5.544  0.58 32.99 ?  141 ARG   A HD3  1 
ATOM   3553 H HE   A ARG   A 1 141 ? 14.201 -18.653 -2.519  0.42 23.04 ?  141 ARG   A HE   1 
ATOM   3554 H HE   B ARG   A 1 141 ? 10.153 -17.007 -5.046  0.58 35.54 ?  141 ARG   A HE   1 
ATOM   3555 H HH11 A ARG   A 1 141 ? 10.960 -18.310 -1.873  0.42 23.72 ?  141 ARG   A HH11 1 
ATOM   3556 H HH11 B ARG   A 1 141 ? 10.390 -14.305 -6.818  0.58 38.39 ?  141 ARG   A HH11 1 
ATOM   3557 H HH12 A ARG   A 1 141 ? 10.957 -19.198 -0.678  0.42 23.72 ?  141 ARG   A HH12 1 
ATOM   3558 H HH12 B ARG   A 1 141 ? 8.936  -14.199 -7.102  0.58 38.39 ?  141 ARG   A HH12 1 
ATOM   3559 H HH21 A ARG   A 1 141 ? 14.159 -19.946 -0.684  0.42 23.55 ?  141 ARG   A HH21 1 
ATOM   3560 H HH21 B ARG   A 1 141 ? 7.906  -16.611 -5.123  0.58 38.56 ?  141 ARG   A HH21 1 
ATOM   3561 H HH22 A ARG   A 1 141 ? 12.879 -20.183 0.039   0.42 23.55 ?  141 ARG   A HH22 1 
ATOM   3562 H HH22 B ARG   A 1 141 ? 7.440  -15.578 -6.090  0.58 38.56 ?  141 ARG   A HH22 1 
ATOM   3563 N N    A VAL   A 1 142 ? 16.672 -14.558 -3.049  0.42 13.12 ?  142 VAL   A N    1 
ATOM   3564 N N    B VAL   A 1 142 ? 16.721 -14.508 -3.108  0.58 16.34 ?  142 VAL   A N    1 
ATOM   3565 C CA   A VAL   A 1 142 ? 18.115 -14.787 -3.081  0.42 13.64 ?  142 VAL   A CA   1 
ATOM   3566 C CA   B VAL   A 1 142 ? 18.168 -14.709 -3.107  0.58 15.69 ?  142 VAL   A CA   1 
ATOM   3567 C C    A VAL   A 1 142 ? 18.699 -14.712 -1.677  0.42 13.59 ?  142 VAL   A C    1 
ATOM   3568 C C    B VAL   A 1 142 ? 18.697 -14.705 -1.682  0.58 14.53 ?  142 VAL   A C    1 
ATOM   3569 O O    A VAL   A 1 142 ? 19.591 -15.490 -1.318  0.42 13.77 ?  142 VAL   A O    1 
ATOM   3570 O O    B VAL   A 1 142 ? 19.540 -15.532 -1.312  0.58 14.66 ?  142 VAL   A O    1 
ATOM   3571 C CB   A VAL   A 1 142 ? 18.805 -13.813 -4.056  0.42 13.54 ?  142 VAL   A CB   1 
ATOM   3572 C CB   B VAL   A 1 142 ? 18.878 -13.661 -3.985  0.58 15.67 ?  142 VAL   A CB   1 
ATOM   3573 C CG1  A VAL   A 1 142 ? 20.326 -13.923 -3.939  0.42 13.53 ?  142 VAL   A CG1  1 
ATOM   3574 C CG1  B VAL   A 1 142 ? 20.379 -13.932 -4.016  0.58 15.24 ?  142 VAL   A CG1  1 
ATOM   3575 C CG2  A VAL   A 1 142 ? 18.367 -14.091 -5.487  0.42 14.08 ?  142 VAL   A CG2  1 
ATOM   3576 C CG2  B VAL   A 1 142 ? 18.320 -13.672 -5.394  0.58 16.31 ?  142 VAL   A CG2  1 
ATOM   3577 H H    A VAL   A 1 142 ? 16.404 -13.886 -3.516  0.42 15.76 ?  142 VAL   A H    1 
ATOM   3578 H H    B VAL   A 1 142 ? 16.455 -13.775 -3.473  0.58 19.62 ?  142 VAL   A H    1 
ATOM   3579 H HA   A VAL   A 1 142 ? 18.274 -15.682 -3.411  0.42 16.38 ?  142 VAL   A HA   1 
ATOM   3580 H HA   B VAL   A 1 142 ? 18.357 -15.577 -3.485  0.58 18.84 ?  142 VAL   A HA   1 
ATOM   3581 H HB   A VAL   A 1 142 ? 18.553 -12.902 -3.831  0.42 16.27 ?  142 VAL   A HB   1 
ATOM   3582 H HB   B VAL   A 1 142 ? 18.739 -12.775 -3.610  0.58 18.82 ?  142 VAL   A HB   1 
ATOM   3583 H HG11 A VAL   A 1 142 ? 20.732 -13.482 -4.702  0.42 16.25 ?  142 VAL   A HG11 1 
ATOM   3584 H HG11 B VAL   A 1 142 ? 20.784 -13.382 -4.703  0.58 18.30 ?  142 VAL   A HG11 1 
ATOM   3585 H HG12 A VAL   A 1 142 ? 20.616 -13.495 -3.119  0.42 16.25 ?  142 VAL   A HG12 1 
ATOM   3586 H HG12 B VAL   A 1 142 ? 20.760 -13.716 -3.151  0.58 18.30 ?  142 VAL   A HG12 1 
ATOM   3587 H HG13 A VAL   A 1 142 ? 20.573 -14.861 -3.931  0.42 16.25 ?  142 VAL   A HG13 1 
ATOM   3588 H HG13 B VAL   A 1 142 ? 20.522 -14.871 -4.218  0.58 18.30 ?  142 VAL   A HG13 1 
ATOM   3589 H HG21 A VAL   A 1 142 ? 18.819 -13.470 -6.082  0.42 16.91 ?  142 VAL   A HG21 1 
ATOM   3590 H HG21 B VAL   A 1 142 ? 18.812 -13.033 -5.932  0.58 19.59 ?  142 VAL   A HG21 1 
ATOM   3591 H HG22 A VAL   A 1 142 ? 18.606 -15.002 -5.719  0.42 16.91 ?  142 VAL   A HG22 1 
ATOM   3592 H HG22 B VAL   A 1 142 ? 18.422 -14.563 -5.761  0.58 19.59 ?  142 VAL   A HG22 1 
ATOM   3593 H HG23 A VAL   A 1 142 ? 17.407 -13.972 -5.553  0.42 16.91 ?  142 VAL   A HG23 1 
ATOM   3594 H HG23 B VAL   A 1 142 ? 17.383 -13.430 -5.366  0.58 19.59 ?  142 VAL   A HG23 1 
ATOM   3595 N N    . CYS   A 1 143 ? 18.214 -13.773 -0.860  1.00 13.60 ?  143 CYS   A N    1 
ATOM   3596 C CA   . CYS   A 1 143 ? 18.670 -13.697 0.525   1.00 13.85 ?  143 CYS   A CA   1 
ATOM   3597 C C    . CYS   A 1 143 ? 18.429 -15.024 1.243   1.00 13.49 ?  143 CYS   A C    1 
ATOM   3598 O O    . CYS   A 1 143 ? 19.344 -15.601 1.840   1.00 13.49 ?  143 CYS   A O    1 
ATOM   3599 C CB   . CYS   A 1 143 ? 17.937 -12.564 1.240   1.00 13.78 ?  143 CYS   A CB   1 
ATOM   3600 S SG   . CYS   A 1 143 ? 18.416 -12.365 2.970   1.00 14.28 ?  143 CYS   A SG   1 
ATOM   3601 H H    A CYS   A 1 143 ? 17.632 -13.181 -1.078  0.42 16.33 ?  143 CYS   A H    1 
ATOM   3602 H H    B CYS   A 1 143 ? 17.624 -13.186 -1.073  0.58 16.33 ?  143 CYS   A H    1 
ATOM   3603 H HA   . CYS   A 1 143 ? 19.619 -13.512 0.545   1.00 16.63 ?  143 CYS   A HA   1 
ATOM   3604 H HB2  . CYS   A 1 143 ? 18.125 -11.732 0.779   1.00 16.55 ?  143 CYS   A HB2  1 
ATOM   3605 H HB3  . CYS   A 1 143 ? 16.983 -12.743 1.210   1.00 16.55 ?  143 CYS   A HB3  1 
ATOM   3606 H HG   . CYS   A 1 143 ? 17.830 -11.420 3.427   1.00 17.16 ?  143 CYS   A HG   1 
ATOM   3607 N N    . VAL   A 1 144 ? 17.196 -15.534 1.169   1.00 14.23 ?  144 VAL   A N    1 
ATOM   3608 C CA   . VAL   A 1 144 ? 16.833 -16.756 1.876   1.00 15.63 ?  144 VAL   A CA   1 
ATOM   3609 C C    . VAL   A 1 144 ? 17.666 -17.933 1.391   1.00 16.02 ?  144 VAL   A C    1 
ATOM   3610 O O    . VAL   A 1 144 ? 18.031 -18.815 2.178   1.00 16.65 ?  144 VAL   A O    1 
ATOM   3611 C CB   . VAL   A 1 144 ? 15.322 -17.001 1.713   1.00 17.74 ?  144 VAL   A CB   1 
ATOM   3612 C CG1  . VAL   A 1 144 ? 14.963 -18.460 1.969   1.00 19.00 ?  144 VAL   A CG1  1 
ATOM   3613 C CG2  . VAL   A 1 144 ? 14.544 -16.038 2.620   1.00 17.90 ?  144 VAL   A CG2  1 
ATOM   3614 H H    . VAL   A 1 144 ? 16.551 -15.182 0.714   1.00 17.09 ?  144 VAL   A H    1 
ATOM   3615 H HA   . VAL   A 1 144 ? 17.004 -16.635 2.819   1.00 18.78 ?  144 VAL   A HA   1 
ATOM   3616 H HB   . VAL   A 1 144 ? 15.065 -16.794 0.796   1.00 21.30 ?  144 VAL   A HB   1 
ATOM   3617 H HG11 . VAL   A 1 144 ? 14.002 -18.528 2.112   1.00 22.82 ?  144 VAL   A HG11 1 
ATOM   3618 H HG12 . VAL   A 1 144 ? 15.214 -18.990 1.197   1.00 22.82 ?  144 VAL   A HG12 1 
ATOM   3619 H HG13 . VAL   A 1 144 ? 15.432 -18.766 2.757   1.00 22.82 ?  144 VAL   A HG13 1 
ATOM   3620 H HG21 . VAL   A 1 144 ? 13.589 -16.195 2.515   1.00 21.50 ?  144 VAL   A HG21 1 
ATOM   3621 H HG22 . VAL   A 1 144 ? 14.801 -16.193 3.543   1.00 21.50 ?  144 VAL   A HG22 1 
ATOM   3622 H HG23 . VAL   A 1 144 ? 14.753 -15.123 2.370   1.00 21.50 ?  144 VAL   A HG23 1 
ATOM   3623 N N    . ASP   A 1 145 ? 17.957 -17.979 0.094   1.00 16.49 ?  145 ASP   A N    1 
ATOM   3624 C CA   . ASP   A 1 145 ? 18.679 -19.094 -0.509  1.00 16.95 ?  145 ASP   A CA   1 
ATOM   3625 C C    . ASP   A 1 145 ? 20.198 -18.943 -0.440  1.00 16.52 ?  145 ASP   A C    1 
ATOM   3626 O O    . ASP   A 1 145 ? 20.908 -19.853 -0.880  1.00 18.69 ?  145 ASP   A O    1 
ATOM   3627 C CB   . ASP   A 1 145 ? 18.260 -19.255 -1.975  1.00 19.16 ?  145 ASP   A CB   1 
ATOM   3628 C CG   . ASP   A 1 145 ? 16.824 -19.733 -2.133  1.00 21.68 ?  145 ASP   A CG   1 
ATOM   3629 O OD1  . ASP   A 1 145 ? 16.239 -20.245 -1.152  1.00 22.88 ?  145 ASP   A OD1  1 
ATOM   3630 O OD2  . ASP   A 1 145 ? 16.285 -19.584 -3.251  1.00 23.59 -1 145 ASP   A OD2  1 
ATOM   3631 H H    . ASP   A 1 145 ? 17.732 -17.372 -0.471  1.00 19.81 ?  145 ASP   A H    1 
ATOM   3632 H HA   . ASP   A 1 145 ? 18.440 -19.912 -0.042  1.00 20.36 ?  145 ASP   A HA   1 
ATOM   3633 H HB2  . ASP   A 1 145 ? 18.345 -18.395 -2.420  1.00 23.01 ?  145 ASP   A HB2  1 
ATOM   3634 H HB3  . ASP   A 1 145 ? 18.846 -19.903 -2.399  1.00 23.01 ?  145 ASP   A HB3  1 
ATOM   3635 N N    . THR   A 1 146 ? 20.713 -17.833 0.087   1.00 14.16 ?  146 THR   A N    1 
ATOM   3636 C CA   . THR   A 1 146 ? 22.150 -17.567 0.125   1.00 13.79 ?  146 THR   A CA   1 
ATOM   3637 C C    . THR   A 1 146 ? 22.691 -17.373 1.531   1.00 13.38 ?  146 THR   A C    1 
ATOM   3638 O O    . THR   A 1 146 ? 23.763 -17.900 1.858   1.00 14.34 ?  146 THR   A O    1 
ATOM   3639 C CB   . THR   A 1 146 ? 22.479 -16.322 -0.715  1.00 13.71 ?  146 THR   A CB   1 
ATOM   3640 O OG1  . THR   A 1 146 ? 21.975 -16.501 -2.039  1.00 14.61 ?  146 THR   A OG1  1 
ATOM   3641 C CG2  . THR   A 1 146 ? 23.978 -16.086 -0.782  1.00 14.21 ?  146 THR   A CG2  1 
ATOM   3642 H H    . THR   A 1 146 ? 20.234 -17.204 0.441   1.00 17.01 ?  146 THR   A H    1 
ATOM   3643 H HA   . THR   A 1 146 ? 22.615 -18.317 -0.262  1.00 16.56 ?  146 THR   A HA   1 
ATOM   3644 H HB   . THR   A 1 146 ? 22.070 -15.538 -0.317  1.00 16.47 ?  146 THR   A HB   1 
ATOM   3645 H HG1  . THR   A 1 146 ? 21.139 -16.578 -2.019  1.00 17.54 ?  146 THR   A HG1  1 
ATOM   3646 H HG21 . THR   A 1 146 ? 24.184 -15.424 -1.463  1.00 17.07 ?  146 THR   A HG21 1 
ATOM   3647 H HG22 . THR   A 1 146 ? 24.306 -15.761 0.074   1.00 17.07 ?  146 THR   A HG22 1 
ATOM   3648 H HG23 . THR   A 1 146 ? 24.438 -16.911 -1.001  1.00 17.07 ?  146 THR   A HG23 1 
ATOM   3649 N N    . VAL   A 1 147 ? 21.989 -16.607 2.361   1.00 13.24 ?  147 VAL   A N    1 
ATOM   3650 C CA   . VAL   A 1 147 ? 22.467 -16.300 3.703   1.00 13.04 ?  147 VAL   A CA   1 
ATOM   3651 C C    . VAL   A 1 147 ? 22.145 -17.465 4.626   1.00 13.38 ?  147 VAL   A C    1 
ATOM   3652 O O    . VAL   A 1 147 ? 21.004 -17.944 4.669   1.00 14.08 ?  147 VAL   A O    1 
ATOM   3653 C CB   . VAL   A 1 147 ? 21.840 -14.990 4.207   1.00 13.46 ?  147 VAL   A CB   1 
ATOM   3654 C CG1  . VAL   A 1 147 ? 22.363 -14.654 5.576   1.00 14.34 ?  147 VAL   A CG1  1 
ATOM   3655 C CG2  . VAL   A 1 147 ? 22.103 -13.839 3.223   1.00 13.27 ?  147 VAL   A CG2  1 
ATOM   3656 H H    . VAL   A 1 147 ? 21.224 -16.255 2.179   1.00 15.90 ?  147 VAL   A H    1 
ATOM   3657 H HA   . VAL   A 1 147 ? 23.431 -16.183 3.679   1.00 15.67 ?  147 VAL   A HA   1 
ATOM   3658 H HB   . VAL   A 1 147 ? 20.880 -15.111 4.281   1.00 16.17 ?  147 VAL   A HB   1 
ATOM   3659 H HG11 . VAL   A 1 147 ? 22.099 -13.749 5.802   1.00 17.22 ?  147 VAL   A HG11 1 
ATOM   3660 H HG12 . VAL   A 1 147 ? 21.989 -15.276 6.223   1.00 17.22 ?  147 VAL   A HG12 1 
ATOM   3661 H HG13 . VAL   A 1 147 ? 23.330 -14.724 5.571   1.00 17.22 ?  147 VAL   A HG13 1 
ATOM   3662 H HG21 . VAL   A 1 147 ? 21.756 -13.018 3.607   1.00 15.94 ?  147 VAL   A HG21 1 
ATOM   3663 H HG22 . VAL   A 1 147 ? 23.049 -13.766 3.070   1.00 15.94 ?  147 VAL   A HG22 1 
ATOM   3664 H HG23 . VAL   A 1 147 ? 21.638 -14.033 2.391   1.00 15.94 ?  147 VAL   A HG23 1 
ATOM   3665 N N    . ARG   A 1 148 ? 23.157 -17.921 5.364   1.00 13.53 ?  148 ARG   A N    1 
ATOM   3666 C CA   . ARG   A 1 148 ? 23.028 -18.991 6.335   1.00 13.99 ?  148 ARG   A CA   1 
ATOM   3667 C C    . ARG   A 1 148 ? 23.137 -18.512 7.769   1.00 14.34 ?  148 ARG   A C    1 
ATOM   3668 O O    . ARG   A 1 148 ? 22.730 -19.239 8.682   1.00 15.52 ?  148 ARG   A O    1 
ATOM   3669 C CB   . ARG   A 1 148 ? 24.096 -20.067 6.081   1.00 14.71 ?  148 ARG   A CB   1 
ATOM   3670 C CG   . ARG   A 1 148 ? 23.948 -20.733 4.726   1.00 16.21 ?  148 ARG   A CG   1 
ATOM   3671 C CD   . ARG   A 1 148 ? 25.059 -21.756 4.458   1.00 17.41 ?  148 ARG   A CD   1 
ATOM   3672 N NE   . ARG   A 1 148 ? 26.400 -21.177 4.475   1.00 16.94 ?  148 ARG   A NE   1 
ATOM   3673 C CZ   . ARG   A 1 148 ? 26.910 -20.452 3.489   1.00 15.79 ?  148 ARG   A CZ   1 
ATOM   3674 N NH1  . ARG   A 1 148 ? 26.232 -20.226 2.375   1.00 15.68 ?  148 ARG   A NH1  1 
ATOM   3675 N NH2  . ARG   A 1 148 ? 28.122 -19.913 3.634   1.00 16.29 ?  148 ARG   A NH2  1 
ATOM   3676 H H    . ARG   A 1 148 ? 23.966 -17.613 5.301   1.00 16.25 ?  148 ARG   A H    1 
ATOM   3677 H HA   . ARG   A 1 148 ? 22.163 -19.404 6.233   1.00 16.81 ?  148 ARG   A HA   1 
ATOM   3678 H HB2  . ARG   A 1 148 ? 24.977 -19.669 6.119   1.00 17.67 ?  148 ARG   A HB2  1 
ATOM   3679 H HB3  . ARG   A 1 148 ? 24.016 -20.763 6.757   1.00 17.67 ?  148 ARG   A HB3  1 
ATOM   3680 H HG2  . ARG   A 1 148 ? 23.089 -21.187 4.694   1.00 19.46 ?  148 ARG   A HG2  1 
ATOM   3681 H HG3  . ARG   A 1 148 ? 23.983 -20.046 4.040   1.00 19.46 ?  148 ARG   A HG3  1 
ATOM   3682 H HD2  . ARG   A 1 148 ? 25.020 -22.440 5.141   1.00 20.91 ?  148 ARG   A HD2  1 
ATOM   3683 H HD3  . ARG   A 1 148 ? 24.910 -22.148 3.584   1.00 20.91 ?  148 ARG   A HD3  1 
ATOM   3684 H HE   . ARG   A 1 148 ? 26.885 -21.309 5.167   1.00 20.34 ?  148 ARG   A HE   1 
ATOM   3685 H HH11 . ARG   A 1 148 ? 25.449 -20.550 2.269   1.00 18.84 ?  148 ARG   A HH11 1 
ATOM   3686 H HH12 . ARG   A 1 148 ? 26.586 -19.743 1.750   1.00 18.84 ?  148 ARG   A HH12 1 
ATOM   3687 H HH21 . ARG   A 1 148 ? 28.569 -20.048 4.355   1.00 19.57 ?  148 ARG   A HH21 1 
ATOM   3688 H HH22 . ARG   A 1 148 ? 28.464 -19.438 3.001   1.00 19.57 ?  148 ARG   A HH22 1 
ATOM   3689 N N    . THR   A 1 149 ? 23.672 -17.316 7.984   1.00 13.85 ?  149 THR   A N    1 
ATOM   3690 C CA   . THR   A 1 149 ? 23.743 -16.717 9.300   1.00 14.05 ?  149 THR   A CA   1 
ATOM   3691 C C    . THR   A 1 149 ? 22.413 -16.024 9.595   1.00 13.69 ?  149 THR   A C    1 
ATOM   3692 O O    . THR   A 1 149 ? 21.488 -16.015 8.771   1.00 14.49 ?  149 THR   A O    1 
ATOM   3693 C CB   . THR   A 1 149 ? 24.941 -15.776 9.351   1.00 14.47 ?  149 THR   A CB   1 
ATOM   3694 O OG1  . THR   A 1 149 ? 24.805 -14.849 8.270   1.00 14.57 ?  149 THR   A OG1  1 
ATOM   3695 C CG2  . THR   A 1 149 ? 26.252 -16.577 9.237   1.00 15.04 ?  149 THR   A CG2  1 
ATOM   3696 H H    . THR   A 1 149 ? 24.013 -16.814 7.364   1.00 16.64 ?  149 THR   A H    1 
ATOM   3697 H HA   . THR   A 1 149 ? 23.874 -17.421 9.957   1.00 16.87 ?  149 THR   A HA   1 
ATOM   3698 H HB   . THR   A 1 149 ? 24.935 -15.299 10.193  1.00 17.38 ?  149 THR   A HB   1 
ATOM   3699 H HG1  . THR   A 1 149 ? 25.464 -14.325 8.260   1.00 17.50 ?  149 THR   A HG1  1 
ATOM   3700 H HG21 . THR   A 1 149 ? 27.011 -15.982 9.296   1.00 18.07 ?  149 THR   A HG21 1 
ATOM   3701 H HG22 . THR   A 1 149 ? 26.309 -17.232 9.956   1.00 18.07 ?  149 THR   A HG22 1 
ATOM   3702 H HG23 . THR   A 1 149 ? 26.284 -17.050 8.388   1.00 18.07 ?  149 THR   A HG23 1 
ATOM   3703 N N    . ASN   A 1 150 ? 22.277 -15.482 10.799  1.00 14.09 ?  150 ASN   A N    1 
ATOM   3704 C CA   . ASN   A 1 150 ? 20.988 -14.972 11.262  1.00 14.78 ?  150 ASN   A CA   1 
ATOM   3705 C C    . ASN   A 1 150 ? 20.814 -13.536 10.788  1.00 13.67 ?  150 ASN   A C    1 
ATOM   3706 O O    . ASN   A 1 150 ? 21.562 -12.637 11.198  1.00 14.82 ?  150 ASN   A O    1 
ATOM   3707 C CB   . ASN   A 1 150 ? 20.892 -15.076 12.777  1.00 17.31 ?  150 ASN   A CB   1 
ATOM   3708 C CG   . ASN   A 1 150 ? 20.820 -16.505 13.240  1.00 21.23 ?  150 ASN   A CG   1 
ATOM   3709 O OD1  . ASN   A 1 150 ? 20.254 -17.353 12.550  1.00 22.40 ?  150 ASN   A OD1  1 
ATOM   3710 N ND2  . ASN   A 1 150 ? 21.406 -16.793 14.402  1.00 23.88 ?  150 ASN   A ND2  1 
ATOM   3711 H H    . ASN   A 1 150 ? 22.911 -15.405 11.371  1.00 16.93 ?  150 ASN   A H    1 
ATOM   3712 H HA   . ASN   A 1 150 ? 20.271 -15.508 10.881  1.00 17.75 ?  150 ASN   A HA   1 
ATOM   3713 H HB2  . ASN   A 1 150 ? 21.672 -14.670 13.179  1.00 20.79 ?  150 ASN   A HB2  1 
ATOM   3714 H HB3  . ASN   A 1 150 ? 20.085 -14.630 13.083  1.00 20.79 ?  150 ASN   A HB3  1 
ATOM   3715 H HD21 . ASN   A 1 150 ? 21.401 -17.601 14.716  1.00 28.68 ?  150 ASN   A HD21 1 
ATOM   3716 H HD22 . ASN   A 1 150 ? 21.791 -16.170 14.859  1.00 28.68 ?  150 ASN   A HD22 1 
ATOM   3717 N N    . VAL   A 1 151 ? 19.833 -13.312 9.924   1.00 13.37 ?  151 VAL   A N    1 
ATOM   3718 C CA   . VAL   A 1 151 ? 19.632 -12.013 9.308   1.00 13.44 ?  151 VAL   A CA   1 
ATOM   3719 C C    . VAL   A 1 151 ? 18.244 -11.493 9.646   1.00 13.52 ?  151 VAL   A C    1 
ATOM   3720 O O    . VAL   A 1 151 ? 17.236 -12.208 9.497   1.00 14.91 ?  151 VAL   A O    1 
ATOM   3721 C CB   . VAL   A 1 151 ? 19.939 -12.021 7.796   1.00 14.78 ?  151 VAL   A CB   1 
ATOM   3722 C CG1  . VAL   A 1 151 ? 19.126 -13.055 7.055   1.00 16.50 ?  151 VAL   A CG1  1 
ATOM   3723 C CG2  . VAL   A 1 151 ? 19.751 -10.624 7.203   1.00 15.20 ?  151 VAL   A CG2  1 
ATOM   3724 H H    . VAL   A 1 151 ? 19.266 -13.907 9.669   1.00 16.06 ?  151 VAL   A H    1 
ATOM   3725 H HA   . VAL   A 1 151 ? 20.269 -11.391 9.707   1.00 16.15 ?  151 VAL   A HA   1 
ATOM   3726 H HB   . VAL   A 1 151 ? 20.874 -12.254 7.677   1.00 17.75 ?  151 VAL   A HB   1 
ATOM   3727 H HG11 . VAL   A 1 151 ? 19.335 -13.013 6.109   1.00 19.82 ?  151 VAL   A HG11 1 
ATOM   3728 H HG12 . VAL   A 1 151 ? 19.350 -13.941 7.399   1.00 19.82 ?  151 VAL   A HG12 1 
ATOM   3729 H HG13 . VAL   A 1 151 ? 18.182 -12.883 7.194   1.00 19.82 ?  151 VAL   A HG13 1 
ATOM   3730 H HG21 . VAL   A 1 151 ? 20.089 -10.624 6.292   1.00 18.26 ?  151 VAL   A HG21 1 
ATOM   3731 H HG22 . VAL   A 1 151 ? 18.810 -10.401 7.207   1.00 18.26 ?  151 VAL   A HG22 1 
ATOM   3732 H HG23 . VAL   A 1 151 ? 20.250 -9.986  7.737   1.00 18.26 ?  151 VAL   A HG23 1 
ATOM   3733 N N    A TYR   A 1 152 ? 18.208 -10.237 10.091  0.42 13.24 ?  152 TYR   A N    1 
ATOM   3734 N N    B TYR   A 1 152 ? 18.206 -10.257 10.132  0.58 13.16 ?  152 TYR   A N    1 
ATOM   3735 C CA   A TYR   A 1 152 ? 17.004 -9.524  10.496  0.42 12.78 ?  152 TYR   A CA   1 
ATOM   3736 C CA   B TYR   A 1 152 ? 16.983 -9.535  10.450  0.58 12.97 ?  152 TYR   A CA   1 
ATOM   3737 C C    A TYR   A 1 152 ? 16.779 -8.402  9.490   0.42 12.13 ?  152 TYR   A C    1 
ATOM   3738 C C    B TYR   A 1 152 ? 16.805 -8.454  9.393   0.58 12.33 ?  152 TYR   A C    1 
ATOM   3739 O O    A TYR   A 1 152 ? 17.433 -7.357  9.553   0.42 12.18 ?  152 TYR   A O    1 
ATOM   3740 O O    B TYR   A 1 152 ? 17.624 -7.531  9.298   0.58 11.93 ?  152 TYR   A O    1 
ATOM   3741 C CB   A TYR   A 1 152 ? 17.173 -9.008  11.919  0.42 13.57 ?  152 TYR   A CB   1 
ATOM   3742 C CB   B TYR   A 1 152 ? 17.093 -8.947  11.853  0.58 14.01 ?  152 TYR   A CB   1 
ATOM   3743 C CG   A TYR   A 1 152 ? 17.148 -10.138 12.910  0.42 14.32 ?  152 TYR   A CG   1 
ATOM   3744 C CG   B TYR   A 1 152 ? 17.026 -10.013 12.918  0.58 14.63 ?  152 TYR   A CG   1 
ATOM   3745 C CD1  A TYR   A 1 152 ? 18.305 -10.835 13.232  0.42 15.77 ?  152 TYR   A CD1  1 
ATOM   3746 C CD1  B TYR   A 1 152 ? 18.123 -10.819 13.196  0.58 16.53 ?  152 TYR   A CD1  1 
ATOM   3747 C CD2  A TYR   A 1 152 ? 15.957 -10.543 13.492  0.42 14.16 ?  152 TYR   A CD2  1 
ATOM   3748 C CD2  B TYR   A 1 152 ? 15.853 -10.241 13.625  0.58 14.62 ?  152 TYR   A CD2  1 
ATOM   3749 C CE1  A TYR   A 1 152 ? 18.279 -11.892 14.124  0.42 16.85 ?  152 TYR   A CE1  1 
ATOM   3750 C CE1  B TYR   A 1 152 ? 18.058 -11.811 14.159  0.58 18.21 ?  152 TYR   A CE1  1 
ATOM   3751 C CE2  A TYR   A 1 152 ? 15.920 -11.600 14.384  0.42 15.24 ?  152 TYR   A CE2  1 
ATOM   3752 C CE2  B TYR   A 1 152 ? 15.779 -11.230 14.592  0.58 16.80 ?  152 TYR   A CE2  1 
ATOM   3753 C CZ   A TYR   A 1 152 ? 17.084 -12.271 14.699  0.42 16.48 ?  152 TYR   A CZ   1 
ATOM   3754 C CZ   B TYR   A 1 152 ? 16.883 -12.012 14.856  0.58 18.37 ?  152 TYR   A CZ   1 
ATOM   3755 O OH   A TYR   A 1 152 ? 17.049 -13.329 15.585  0.42 17.85 ?  152 TYR   A OH   1 
ATOM   3756 O OH   B TYR   A 1 152 ? 16.820 -12.999 15.816  0.58 20.76 ?  152 TYR   A OH   1 
ATOM   3757 H H    A TYR   A 1 152 ? 18.917 -9.746  10.165  0.42 15.91 ?  152 TYR   A H    1 
ATOM   3758 H H    B TYR   A 1 152 ? 18.920 -9.788  10.288  0.58 15.80 ?  152 TYR   A H    1 
ATOM   3759 H HA   A TYR   A 1 152 ? 16.244 -10.118 10.468  0.42 15.36 ?  152 TYR   A HA   1 
ATOM   3760 H HA   B TYR   A 1 152 ? 16.230 -10.143 10.418  0.58 15.59 ?  152 TYR   A HA   1 
ATOM   3761 H HB2  A TYR   A 1 152 ? 18.028 -8.555  11.996  0.42 16.30 ?  152 TYR   A HB2  1 
ATOM   3762 H HB2  B TYR   A 1 152 ? 17.943 -8.485  11.937  0.58 16.83 ?  152 TYR   A HB2  1 
ATOM   3763 H HB3  A TYR   A 1 152 ? 16.451 -8.399  12.130  0.42 16.30 ?  152 TYR   A HB3  1 
ATOM   3764 H HB3  B TYR   A 1 152 ? 16.361 -8.327  11.992  0.58 16.83 ?  152 TYR   A HB3  1 
ATOM   3765 H HD1  A TYR   A 1 152 ? 19.113 -10.581 12.843  0.42 18.94 ?  152 TYR   A HD1  1 
ATOM   3766 H HD1  B TYR   A 1 152 ? 18.916 -10.683 12.724  0.58 19.85 ?  152 TYR   A HD1  1 
ATOM   3767 H HD2  A TYR   A 1 152 ? 15.169 -10.092 13.276  0.42 17.00 ?  152 TYR   A HD2  1 
ATOM   3768 H HD2  B TYR   A 1 152 ? 15.102 -9.713  13.449  0.58 17.56 ?  152 TYR   A HD2  1 
ATOM   3769 H HE1  A TYR   A 1 152 ? 19.062 -12.343 14.338  0.42 20.24 ?  152 TYR   A HE1  1 
ATOM   3770 H HE1  B TYR   A 1 152 ? 18.806 -12.337 14.334  0.58 21.87 ?  152 TYR   A HE1  1 
ATOM   3771 H HE2  A TYR   A 1 152 ? 15.112 -11.852 14.770  0.42 18.31 ?  152 TYR   A HE2  1 
ATOM   3772 H HE2  B TYR   A 1 152 ? 14.989 -11.369 15.062  0.58 20.17 ?  152 TYR   A HE2  1 
ATOM   3773 H HH   A TYR   A 1 152 ? 16.259 -13.434 15.856  0.42 21.44 ?  152 TYR   A HH   1 
ATOM   3774 H HH   B TYR   A 1 152 ? 16.070 -12.986 16.189  0.58 24.92 ?  152 TYR   A HH   1 
ATOM   3775 N N    A LEU   A 1 153 ? 15.860 -8.638  8.558   0.42 12.13 ?  153 LEU   A N    1 
ATOM   3776 N N    B LEU   A 1 153 ? 15.749 -8.580  8.592   0.58 13.03 ?  153 LEU   A N    1 
ATOM   3777 C CA   A LEU   A 1 153 ? 15.584 -7.707  7.473   0.42 11.92 ?  153 LEU   A CA   1 
ATOM   3778 C CA   B LEU   A 1 153 ? 15.527 -7.732  7.427   0.58 12.85 ?  153 LEU   A CA   1 
ATOM   3779 C C    A LEU   A 1 153 ? 14.601 -6.637  7.924   0.42 12.31 ?  153 LEU   A C    1 
ATOM   3780 C C    B LEU   A 1 153 ? 14.517 -6.645  7.767   0.58 13.00 ?  153 LEU   A C    1 
ATOM   3781 O O    A LEU   A 1 153 ? 13.565 -6.938  8.528   0.42 12.50 ?  153 LEU   A O    1 
ATOM   3782 O O    B LEU   A 1 153 ? 13.374 -6.945  8.136   0.58 13.35 ?  153 LEU   A O    1 
ATOM   3783 C CB   A LEU   A 1 153 ? 14.996 -8.456  6.275   0.42 12.04 ?  153 LEU   A CB   1 
ATOM   3784 C CB   B LEU   A 1 153 ? 15.009 -8.564  6.254   0.58 13.12 ?  153 LEU   A CB   1 
ATOM   3785 C CG   A LEU   A 1 153 ? 15.926 -9.457  5.588   0.42 11.85 ?  153 LEU   A CG   1 
ATOM   3786 C CG   B LEU   A 1 153 ? 16.000 -9.561  5.656   0.58 13.60 ?  153 LEU   A CG   1 
ATOM   3787 C CD1  A LEU   A 1 153 ? 15.109 -10.443 4.774   0.42 11.58 ?  153 LEU   A CD1  1 
ATOM   3788 C CD1  B LEU   A 1 153 ? 15.308 -10.364 4.560   0.58 13.98 ?  153 LEU   A CD1  1 
ATOM   3789 C CD2  A LEU   A 1 153 ? 16.950 -8.752  4.702   0.42 11.42 ?  153 LEU   A CD2  1 
ATOM   3790 C CD2  B LEU   A 1 153 ? 17.248 -8.851  5.127   0.58 13.76 ?  153 LEU   A CD2  1 
ATOM   3791 H H    A LEU   A 1 153 ? 15.373 -9.340  8.538   0.42 14.57 ?  153 LEU   A H    1 
ATOM   3792 H H    B LEU   A 1 153 ? 15.124 -9.165  8.710   0.58 15.65 ?  153 LEU   A H    1 
ATOM   3793 H HA   A LEU   A 1 153 ? 16.402 -7.276  7.193   0.42 14.33 ?  153 LEU   A HA   1 
ATOM   3794 H HA   B LEU   A 1 153 ? 16.359 -7.316  7.171   0.58 15.44 ?  153 LEU   A HA   1 
ATOM   3795 H HB2  A LEU   A 1 153 ? 14.210 -8.944  6.576   0.42 14.46 ?  153 LEU   A HB2  1 
ATOM   3796 H HB2  B LEU   A 1 153 ? 14.233 -9.068  6.555   0.58 15.76 ?  153 LEU   A HB2  1 
ATOM   3797 H HB3  A LEU   A 1 153 ? 14.725 -7.802  5.608   0.42 14.46 ?  153 LEU   A HB3  1 
ATOM   3798 H HB3  B LEU   A 1 153 ? 14.740 -7.958  5.544   0.58 15.76 ?  153 LEU   A HB3  1 
ATOM   3799 H HG   A LEU   A 1 153 ? 16.407 -9.956  6.266   0.42 14.24 ?  153 LEU   A HG   1 
ATOM   3800 H HG   B LEU   A 1 153 ? 16.279 -10.182 6.349   0.58 16.34 ?  153 LEU   A HG   1 
ATOM   3801 H HD11 A LEU   A 1 153 ? 15.712 -11.062 4.336   0.42 13.91 ?  153 LEU   A HD11 1 
ATOM   3802 H HD11 B LEU   A 1 153 ? 15.839 -11.146 4.355   0.58 16.79 ?  153 LEU   A HD11 1 
ATOM   3803 H HD12 A LEU   A 1 153 ? 14.511 -10.921 5.367   0.42 13.91 ?  153 LEU   A HD12 1 
ATOM   3804 H HD12 B LEU   A 1 153 ? 14.430 -10.634 4.875   0.58 16.79 ?  153 LEU   A HD12 1 
ATOM   3805 H HD13 A LEU   A 1 153 ? 14.598 -9.952  4.110   0.42 13.91 ?  153 LEU   A HD13 1 
ATOM   3806 H HD13 B LEU   A 1 153 ? 15.215 -9.805  3.771   0.58 16.79 ?  153 LEU   A HD13 1 
ATOM   3807 H HD21 A LEU   A 1 153 ? 17.576 -9.408  4.365   0.42 13.72 ?  153 LEU   A HD21 1 
ATOM   3808 H HD21 B LEU   A 1 153 ? 17.782 -9.483  4.625   0.58 16.53 ?  153 LEU   A HD21 1 
ATOM   3809 H HD22 A LEU   A 1 153 ? 16.484 -8.326  3.965   0.42 13.72 ?  153 LEU   A HD22 1 
ATOM   3810 H HD22 B LEU   A 1 153 ? 16.974 -8.117  4.558   0.58 16.53 ?  153 LEU   A HD22 1 
ATOM   3811 H HD23 A LEU   A 1 153 ? 17.414 -8.087  5.231   0.42 13.72 ?  153 LEU   A HD23 1 
ATOM   3812 H HD23 B LEU   A 1 153 ? 17.760 -8.512  5.880   0.58 16.53 ?  153 LEU   A HD23 1 
ATOM   3813 N N    . ALA   A 1 154 ? 14.932 -5.389  7.616   1.00 12.86 ?  154 ALA   A N    1 
ATOM   3814 C CA   . ALA   A 1 154 ? 14.066 -4.242  7.833   1.00 13.69 ?  154 ALA   A CA   1 
ATOM   3815 C C    . ALA   A 1 154 ? 13.604 -3.742  6.473   1.00 13.62 ?  154 ALA   A C    1 
ATOM   3816 O O    . ALA   A 1 154 ? 14.429 -3.334  5.644   1.00 14.45 ?  154 ALA   A O    1 
ATOM   3817 C CB   . ALA   A 1 154 ? 14.804 -3.137  8.586   1.00 13.70 ?  154 ALA   A CB   1 
ATOM   3818 H H    A ALA   A 1 154 ? 15.689 -5.174  7.265   0.42 15.45 ?  154 ALA   A H    1 
ATOM   3819 H H    B ALA   A 1 154 ? 15.732 -5.172  7.378   0.58 15.45 ?  154 ALA   A H    1 
ATOM   3820 H HA   . ALA   A 1 154 ? 13.290 -4.503  8.356   1.00 16.44 ?  154 ALA   A HA   1 
ATOM   3821 H HB1  . ALA   A 1 154 ? 14.204 -2.384  8.715   1.00 16.46 ?  154 ALA   A HB1  1 
ATOM   3822 H HB2  . ALA   A 1 154 ? 15.101 -3.475  9.443   1.00 16.46 ?  154 ALA   A HB2  1 
ATOM   3823 H HB3  . ALA   A 1 154 ? 15.572 -2.855  8.058   1.00 16.46 ?  154 ALA   A HB3  1 
ATOM   3824 N N    A VAL   A 1 155 ? 12.290 -3.752  6.276   0.22 13.14 ?  155 VAL   A N    1 
ATOM   3825 N N    B VAL   A 1 155 ? 12.292 -3.814  6.227   0.58 13.28 ?  155 VAL   A N    1 
ATOM   3826 C CA   A VAL   A 1 155 ? 11.637 -3.196  5.102   0.22 13.36 ?  155 VAL   A CA   1 
ATOM   3827 C CA   B VAL   A 1 155 ? 11.672 -3.455  4.951   0.58 14.50 ?  155 VAL   A CA   1 
ATOM   3828 C CA   T VAL   A 1 155 ? 11.296 -3.279  4.475   0.20 16.65 ?  155 VAL   A CA   1 
ATOM   3829 C C    A VAL   A 1 155 ? 10.991 -1.890  5.533   0.22 13.49 ?  155 VAL   A C    1 
ATOM   3830 C C    B VAL   A 1 155 ? 10.915 -2.150  5.162   0.58 15.25 ?  155 VAL   A C    1 
ATOM   3831 C C    T VAL   A 1 155 ? 10.806 -1.965  5.073   0.20 16.11 ?  155 VAL   A C    1 
ATOM   3832 O O    A VAL   A 1 155 ? 10.127 -1.881  6.417   0.22 13.41 ?  155 VAL   A O    1 
ATOM   3833 O O    B VAL   A 1 155 ? 9.962  -2.100  5.945   0.58 14.81 ?  155 VAL   A O    1 
ATOM   3834 O O    T VAL   A 1 155 ? 9.882  -1.936  5.883   0.20 15.96 ?  155 VAL   A O    1 
ATOM   3835 C CB   A VAL   A 1 155 ? 10.588 -4.170  4.546   0.22 13.39 ?  155 VAL   A CB   1 
ATOM   3836 C CB   B VAL   A 1 155 ? 10.739 -4.563  4.422   0.58 14.88 ?  155 VAL   A CB   1 
ATOM   3837 C CB   T VAL   A 1 155 ? 10.176 -4.326  4.370   0.20 16.98 ?  155 VAL   A CB   1 
ATOM   3838 C CG1  A VAL   A 1 155 ? 9.987  -3.622  3.265   0.22 13.62 ?  155 VAL   A CG1  1 
ATOM   3839 C CG1  B VAL   A 1 155 ? 9.960  -4.075  3.200   0.58 16.11 ?  155 VAL   A CG1  1 
ATOM   3840 C CG1  T VAL   A 1 155 ? 9.338  -4.100  3.119   0.20 17.21 ?  155 VAL   A CG1  1 
ATOM   3841 C CG2  A VAL   A 1 155 ? 11.208 -5.542  4.322   0.22 13.50 ?  155 VAL   A CG2  1 
ATOM   3842 C CG2  B VAL   A 1 155 ? 11.534 -5.816  4.052   0.58 16.16 ?  155 VAL   A CG2  1 
ATOM   3843 C CG2  T VAL   A 1 155 ? 10.775 -5.722  4.362   0.20 17.16 ?  155 VAL   A CG2  1 
ATOM   3844 H H    A VAL   A 1 155 ? 11.733 -4.100  6.836   0.22 15.78 ?  155 VAL   A H    1 
ATOM   3845 H H    B VAL   A 1 155 ? 11.716 -4.093  6.808   0.58 15.96 ?  155 VAL   A H    1 
ATOM   3846 H HA   A VAL   A 1 155 ? 12.294 -3.010  4.417   0.22 16.05 ?  155 VAL   A HA   1 
ATOM   3847 H HA   B VAL   A 1 155 ? 12.356 -3.307  4.286   0.58 17.41 ?  155 VAL   A HA   1 
ATOM   3848 H HB   A VAL   A 1 155 ? 9.873  -4.266  5.197   0.22 16.09 ?  155 VAL   A HB   1 
ATOM   3849 H HB   B VAL   A 1 155 ? 10.098 -4.814  5.105   0.58 17.88 ?  155 VAL   A HB   1 
ATOM   3850 H HB   T VAL   A 1 155 ? 9.591  -4.240  5.139   0.20 20.39 ?  155 VAL   A HB   1 
ATOM   3851 H HG11 A VAL   A 1 155 ? 9.403  -4.294  2.882   0.22 16.36 ?  155 VAL   A HG11 1 
ATOM   3852 H HG11 B VAL   A 1 155 ? 9.598  -4.841  2.720   0.58 19.35 ?  155 VAL   A HG11 1 
ATOM   3853 H HG11 T VAL   A 1 155 ? 8.618  -4.752  3.099   0.20 20.67 ?  155 VAL   A HG11 1 
ATOM   3854 H HG12 A VAL   A 1 155 ? 9.479  -2.821  3.470   0.22 16.36 ?  155 VAL   A HG12 1 
ATOM   3855 H HG12 B VAL   A 1 155 ? 9.234  -3.503  3.492   0.58 19.35 ?  155 VAL   A HG12 1 
ATOM   3856 H HG12 T VAL   A 1 155 ? 8.971  -3.203  3.139   0.20 20.67 ?  155 VAL   A HG12 1 
ATOM   3857 H HG13 A VAL   A 1 155 ? 10.703 -3.413  2.647   0.22 16.36 ?  155 VAL   A HG13 1 
ATOM   3858 H HG13 B VAL   A 1 155 ? 10.559 -3.583  2.618   0.58 19.35 ?  155 VAL   A HG13 1 
ATOM   3859 H HG13 T VAL   A 1 155 ? 9.903  -4.210  2.338   0.20 20.67 ?  155 VAL   A HG13 1 
ATOM   3860 H HG21 A VAL   A 1 155 ? 10.571 -6.104  3.859   0.22 16.22 ?  155 VAL   A HG21 1 
ATOM   3861 H HG21 B VAL   A 1 155 ? 10.954 -6.439  3.585   0.58 19.41 ?  155 VAL   A HG21 1 
ATOM   3862 H HG21 T VAL   A 1 155 ? 10.060 -6.374  4.312   0.20 20.60 ?  155 VAL   A HG21 1 
ATOM   3863 H HG22 A VAL   A 1 155 ? 12.012 -5.439  3.786   0.22 16.22 ?  155 VAL   A HG22 1 
ATOM   3864 H HG22 B VAL   A 1 155 ? 12.272 -5.560  3.473   0.58 19.41 ?  155 VAL   A HG22 1 
ATOM   3865 H HG22 T VAL   A 1 155 ? 11.357 -5.809  3.589   0.20 20.60 ?  155 VAL   A HG22 1 
ATOM   3866 H HG23 A VAL   A 1 155 ? 11.434 -5.933  5.181   0.22 16.22 ?  155 VAL   A HG23 1 
ATOM   3867 H HG23 B VAL   A 1 155 ? 11.877 -6.223  4.861   0.58 19.41 ?  155 VAL   A HG23 1 
ATOM   3868 H HG23 T VAL   A 1 155 ? 11.284 -5.845  5.176   0.20 20.60 ?  155 VAL   A HG23 1 
ATOM   3869 N N    A PHE   A 1 156 ? 11.408 -0.784  4.919   0.22 13.65 ?  156 PHE   A N    1 
ATOM   3870 N N    B PHE   A 1 156 ? 11.324 -1.102  4.446   0.58 16.09 ?  156 PHE   A N    1 
ATOM   3871 N N    T PHE   A 1 156 ? 11.455 -0.877  4.658   0.20 15.77 ?  156 PHE   A N    1 
ATOM   3872 C CA   A PHE   A 1 156 ? 10.870 0.514   5.314   0.22 14.25 ?  156 PHE   A CA   1 
ATOM   3873 C CA   B PHE   A 1 156 ? 10.781 0.242   4.665   0.58 17.18 ?  156 PHE   A CA   1 
ATOM   3874 C CA   T PHE   A 1 156 ? 11.050 0.460   5.080   0.20 15.34 ?  156 PHE   A CA   1 
ATOM   3875 C C    A PHE   A 1 156 ? 9.404  0.661   4.912   0.22 13.81 ?  156 PHE   A C    1 
ATOM   3876 C C    B PHE   A 1 156 ? 9.330  0.364   4.198   0.58 18.17 ?  156 PHE   A C    1 
ATOM   3877 C C    T PHE   A 1 156 ? 9.604  0.746   4.698   0.20 14.66 ?  156 PHE   A C    1 
ATOM   3878 O O    A PHE   A 1 156 ? 8.588  1.143   5.705   0.22 13.80 ?  156 PHE   A O    1 
ATOM   3879 O O    B PHE   A 1 156 ? 8.506  0.988   4.875   0.58 18.87 ?  156 PHE   A O    1 
ATOM   3880 O O    T PHE   A 1 156 ? 8.891  1.435   5.436   0.20 14.78 ?  156 PHE   A O    1 
ATOM   3881 C CB   A PHE   A 1 156 ? 11.722 1.638   4.724   0.22 15.18 ?  156 PHE   A CB   1 
ATOM   3882 C CB   B PHE   A 1 156 ? 11.671 1.237   3.917   0.58 17.09 ?  156 PHE   A CB   1 
ATOM   3883 C CB   T PHE   A 1 156 ? 11.991 1.473   4.423   0.20 15.52 ?  156 PHE   A CB   1 
ATOM   3884 C CG   A PHE   A 1 156 ? 11.199 3.014   5.022   0.22 16.41 ?  156 PHE   A CG   1 
ATOM   3885 C CG   B PHE   A 1 156 ? 11.423 2.699   4.241   0.58 18.33 ?  156 PHE   A CG   1 
ATOM   3886 C CG   T PHE   A 1 156 ? 11.561 2.915   4.557   0.20 15.96 ?  156 PHE   A CG   1 
ATOM   3887 C CD1  A PHE   A 1 156 ? 11.058 3.444   6.331   0.22 16.60 ?  156 PHE   A CD1  1 
ATOM   3888 C CD1  B PHE   A 1 156 ? 12.052 3.299   5.325   0.58 19.92 ?  156 PHE   A CD1  1 
ATOM   3889 C CD1  T PHE   A 1 156 ? 11.832 3.630   5.714   0.20 16.13 ?  156 PHE   A CD1  1 
ATOM   3890 C CD2  A PHE   A 1 156 ? 10.858 3.879   3.996   0.22 17.14 ?  156 PHE   A CD2  1 
ATOM   3891 C CD2  B PHE   A 1 156 ? 10.619 3.484   3.425   0.58 19.47 ?  156 PHE   A CD2  1 
ATOM   3892 C CD2  T PHE   A 1 156 ? 10.929 3.565   3.507   0.20 16.17 ?  156 PHE   A CD2  1 
ATOM   3893 C CE1  A PHE   A 1 156 ? 10.578 4.709   6.610   0.22 16.94 ?  156 PHE   A CE1  1 
ATOM   3894 C CE1  B PHE   A 1 156 ? 11.851 4.642   5.614   0.58 21.08 ?  156 PHE   A CE1  1 
ATOM   3895 C CE1  T PHE   A 1 156 ? 11.453 4.960   5.830   0.20 16.56 ?  156 PHE   A CE1  1 
ATOM   3896 C CE2  A PHE   A 1 156 ? 10.377 5.146   4.269   0.22 17.65 ?  156 PHE   A CE2  1 
ATOM   3897 C CE2  B PHE   A 1 156 ? 10.413 4.828   3.710   0.58 21.19 ?  156 PHE   A CE2  1 
ATOM   3898 C CE2  T PHE   A 1 156 ? 10.552 4.893   3.616   0.20 16.53 ?  156 PHE   A CE2  1 
ATOM   3899 C CZ   A PHE   A 1 156 ? 10.239 5.561   5.578   0.22 17.31 ?  156 PHE   A CZ   1 
ATOM   3900 C CZ   B PHE   A 1 156 ? 11.037 5.409   4.804   0.58 21.75 ?  156 PHE   A CZ   1 
ATOM   3901 C CZ   T PHE   A 1 156 ? 10.814 5.591   4.779   0.20 16.85 ?  156 PHE   A CZ   1 
ATOM   3902 H H    A PHE   A 1 156 ? 11.985 -0.758  4.285   0.22 16.40 ?  156 PHE   A H    1 
ATOM   3903 H H    B PHE   A 1 156 ? 11.920 -1.146  3.835   0.58 19.32 ?  156 PHE   A H    1 
ATOM   3904 H H    T PHE   A 1 156 ? 12.123 -0.891  4.122   0.20 18.94 ?  156 PHE   A H    1 
ATOM   3905 H HA   A PHE   A 1 156 ? 10.916 0.592   6.280   0.22 17.12 ?  156 PHE   A HA   1 
ATOM   3906 H HA   B PHE   A 1 156 ? 10.807 0.441   5.609   0.58 20.64 ?  156 PHE   A HA   1 
ATOM   3907 H HA   T PHE   A 1 156 ? 11.141 0.535   6.047   0.20 18.42 ?  156 PHE   A HA   1 
ATOM   3908 H HB2  A PHE   A 1 156 ? 12.620 1.576   5.091   0.22 18.23 ?  156 PHE   A HB2  1 
ATOM   3909 H HB2  B PHE   A 1 156 ? 12.594 1.035   4.125   0.58 20.52 ?  156 PHE   A HB2  1 
ATOM   3910 H HB2  T PHE   A 1 156 ? 12.867 1.386   4.828   0.20 18.65 ?  156 PHE   A HB2  1 
ATOM   3911 H HB3  A PHE   A 1 156 ? 11.754 1.536   3.761   0.22 18.23 ?  156 PHE   A HB3  1 
ATOM   3912 H HB3  B PHE   A 1 156 ? 11.507 1.117   2.974   0.58 20.52 ?  156 PHE   A HB3  1 
ATOM   3913 H HB3  T PHE   A 1 156 ? 12.045 1.268   3.478   0.20 18.65 ?  156 PHE   A HB3  1 
ATOM   3914 H HD1  A PHE   A 1 156 ? 11.288 2.873   7.029   0.22 19.94 ?  156 PHE   A HD1  1 
ATOM   3915 H HD1  B PHE   A 1 156 ? 12.599 2.784   5.879   0.58 23.92 ?  156 PHE   A HD1  1 
ATOM   3916 H HD1  T PHE   A 1 156 ? 12.260 3.208   6.427   0.20 19.38 ?  156 PHE   A HD1  1 
ATOM   3917 H HD2  A PHE   A 1 156 ? 10.951 3.602   3.113   0.22 20.59 ?  156 PHE   A HD2  1 
ATOM   3918 H HD2  B PHE   A 1 156 ? 10.196 3.098   2.696   0.58 23.39 ?  156 PHE   A HD2  1 
ATOM   3919 H HD2  T PHE   A 1 156 ? 10.749 3.099   2.724   0.20 19.43 ?  156 PHE   A HD2  1 
ATOM   3920 H HE1  A PHE   A 1 156 ? 10.488 4.987   7.495   0.22 20.34 ?  156 PHE   A HE1  1 
ATOM   3921 H HE1  B PHE   A 1 156 ? 12.266 5.023   6.355   0.58 25.31 ?  156 PHE   A HE1  1 
ATOM   3922 H HE1  T PHE   A 1 156 ? 11.632 5.425   6.616   0.20 19.89 ?  156 PHE   A HE1  1 
ATOM   3923 H HE2  A PHE   A 1 156 ? 10.151 5.716   3.572   0.22 21.20 ?  156 PHE   A HE2  1 
ATOM   3924 H HE2  B PHE   A 1 156 ? 9.861  5.342   3.169   0.58 25.44 ?  156 PHE   A HE2  1 
ATOM   3925 H HE2  T PHE   A 1 156 ? 10.120 5.313   2.910   0.20 19.86 ?  156 PHE   A HE2  1 
ATOM   3926 H HZ   A PHE   A 1 156 ? 9.918  6.413   5.765   0.22 20.79 ?  156 PHE   A HZ   1 
ATOM   3927 H HZ   B PHE   A 1 156 ? 10.896 6.306   5.004   0.58 26.12 ?  156 PHE   A HZ   1 
ATOM   3928 H HZ   T PHE   A 1 156 ? 10.559 6.480   4.857   0.20 20.23 ?  156 PHE   A HZ   1 
ATOM   3929 N N    A ASP   A 1 157 ? 9.045  0.227   3.703   0.22 13.96 ?  157 ASP   A N    1 
ATOM   3930 N N    B ASP   A 1 157 ? 9.000  -0.234  3.057   0.58 19.95 ?  157 ASP   A N    1 
ATOM   3931 N N    T ASP   A 1 157 ? 9.153  0.212   3.566   0.20 14.61 ?  157 ASP   A N    1 
ATOM   3932 C CA   A ASP   A 1 157 ? 7.718  0.472   3.142   0.22 14.46 ?  157 ASP   A CA   1 
ATOM   3933 C CA   B ASP   A 1 157 ? 7.743  -0.007  2.351   0.58 21.36 ?  157 ASP   A CA   1 
ATOM   3934 C CA   T ASP   A 1 157 ? 7.845  0.517   2.998   0.20 14.67 ?  157 ASP   A CA   1 
ATOM   3935 C C    A ASP   A 1 157 ? 6.737  -0.585  3.641   0.22 14.49 ?  157 ASP   A C    1 
ATOM   3936 C C    B ASP   A 1 157 ? 6.679  -0.983  2.850   0.58 20.07 ?  157 ASP   A C    1 
ATOM   3937 C C    T ASP   A 1 157 ? 6.820  -0.496  3.499   0.20 14.39 ?  157 ASP   A C    1 
ATOM   3938 O O    A ASP   A 1 157 ? 6.941  -1.783  3.416   0.22 14.58 ?  157 ASP   A O    1 
ATOM   3939 O O    B ASP   A 1 157 ? 6.843  -2.198  2.711   0.58 19.09 ?  157 ASP   A O    1 
ATOM   3940 O O    T ASP   A 1 157 ? 6.980  -1.702  3.285   0.20 14.20 ?  157 ASP   A O    1 
ATOM   3941 C CB   A ASP   A 1 157 ? 7.797  0.435   1.616   0.22 15.20 ?  157 ASP   A CB   1 
ATOM   3942 C CB   B ASP   A 1 157 ? 8.021  -0.243  0.867   0.58 24.51 ?  157 ASP   A CB   1 
ATOM   3943 C CB   T ASP   A 1 157 ? 7.958  0.452   1.476   0.20 15.19 ?  157 ASP   A CB   1 
ATOM   3944 C CG   A ASP   A 1 157 ? 6.488  0.841   0.945   0.22 16.30 ?  157 ASP   A CG   1 
ATOM   3945 C CG   B ASP   A 1 157 ? 6.883  0.211   -0.035  0.58 26.97 ?  157 ASP   A CG   1 
ATOM   3946 C CG   T ASP   A 1 157 ? 6.720  0.957   0.771   0.20 15.82 ?  157 ASP   A CG   1 
ATOM   3947 O OD1  A ASP   A 1 157 ? 6.033  1.990   1.134   0.22 17.22 ?  157 ASP   A OD1  1 
ATOM   3948 O OD1  B ASP   A 1 157 ? 5.703  0.038   0.331   0.58 26.96 ?  157 ASP   A OD1  1 
ATOM   3949 O OD1  T ASP   A 1 157 ? 5.630  0.391   0.999   0.20 16.88 ?  157 ASP   A OD1  1 
ATOM   3950 O OD2  A ASP   A 1 157 ? 5.912  0.005   0.217   0.22 16.10 -1 157 ASP   A OD2  1 
ATOM   3951 O OD2  B ASP   A 1 157 ? 7.182  0.750   -1.122  0.58 28.92 -1 157 ASP   A OD2  1 
ATOM   3952 O OD2  T ASP   A 1 157 ? 6.840  1.923   -0.014  0.20 15.05 -1 157 ASP   A OD2  1 
ATOM   3953 H H    A ASP   A 1 157 ? 9.558  -0.227  3.190   0.22 16.77 ?  157 ASP   A H    1 
ATOM   3954 H H    B ASP   A 1 157 ? 9.493  -0.808  2.663   0.58 23.95 ?  157 ASP   A H    1 
ATOM   3955 H H    T ASP   A 1 157 ? 9.607  -0.342  3.094   0.20 17.55 ?  157 ASP   A H    1 
ATOM   3956 H HA   A ASP   A 1 157 ? 7.402  1.347   3.414   0.22 17.37 ?  157 ASP   A HA   1 
ATOM   3957 H HA   B ASP   A 1 157 ? 7.426  0.899   2.478   0.58 25.65 ?  157 ASP   A HA   1 
ATOM   3958 H HA   T ASP   A 1 157 ? 7.566  1.407   3.263   0.20 17.62 ?  157 ASP   A HA   1 
ATOM   3959 H HB2  A ASP   A 1 157 ? 8.514  1.024   1.326   0.22 18.26 ?  157 ASP   A HB2  1 
ATOM   3960 H HB2  B ASP   A 1 157 ? 8.811  0.259   0.629   0.58 29.43 ?  157 ASP   A HB2  1 
ATOM   3961 H HB2  T ASP   A 1 157 ? 8.705  1.001   1.197   0.20 18.24 ?  157 ASP   A HB2  1 
ATOM   3962 H HB3  A ASP   A 1 157 ? 7.992  -0.473  1.332   0.22 18.26 ?  157 ASP   A HB3  1 
ATOM   3963 H HB3  B ASP   A 1 157 ? 8.208  -1.192  0.733   0.58 29.43 ?  157 ASP   A HB3  1 
ATOM   3964 H HB3  T ASP   A 1 157 ? 8.114  -0.473  1.216   0.20 18.24 ?  157 ASP   A HB3  1 
ATOM   3965 N N    A LYS   A 1 158 ? 5.661  -0.140  4.302   0.22 14.95 ?  158 LYS   A N    1 
ATOM   3966 N N    B LYS   A 1 158 ? 5.575  -0.453  3.397   0.58 20.56 ?  158 LYS   A N    1 
ATOM   3967 N N    T LYS   A 1 158 ? 5.758  -0.005  4.149   0.20 15.06 ?  158 LYS   A N    1 
ATOM   3968 C CA   A LYS   A 1 158 ? 4.699  -1.082  4.871   0.22 15.79 ?  158 LYS   A CA   1 
ATOM   3969 C CA   B LYS   A 1 158 ? 4.519  -1.301  3.955   0.58 21.69 ?  158 LYS   A CA   1 
ATOM   3970 C CA   T LYS   A 1 158 ? 4.783  -0.908  4.759   0.20 16.10 ?  158 LYS   A CA   1 
ATOM   3971 C C    A LYS   A 1 158 ? 3.960  -1.849  3.780   0.22 15.88 ?  158 LYS   A C    1 
ATOM   3972 C C    B LYS   A 1 158 ? 3.891  -2.185  2.881   0.58 20.95 ?  158 LYS   A C    1 
ATOM   3973 C C    T LYS   A 1 158 ? 4.037  -1.721  3.707   0.20 16.22 ?  158 LYS   A C    1 
ATOM   3974 O O    A LYS   A 1 158 ? 3.772  -3.066  3.890   0.22 15.96 ?  158 LYS   A O    1 
ATOM   3975 O O    B LYS   A 1 158 ? 3.746  -3.400  3.065   0.58 20.41 ?  158 LYS   A O    1 
ATOM   3976 O O    T LYS   A 1 158 ? 3.834  -2.927  3.879   0.20 16.17 ?  158 LYS   A O    1 
ATOM   3977 C CB   A LYS   A 1 158 ? 3.716  -0.349  5.789   0.22 16.80 ?  158 LYS   A CB   1 
ATOM   3978 C CB   B LYS   A 1 158 ? 3.451  -0.427  4.629   0.58 24.22 ?  158 LYS   A CB   1 
ATOM   3979 C CB   T LYS   A 1 158 ? 3.801  -0.125  5.637   0.20 17.55 ?  158 LYS   A CB   1 
ATOM   3980 C CG   A LYS   A 1 158 ? 2.491  -1.167  6.211   0.22 17.78 ?  158 LYS   A CG   1 
ATOM   3981 C CG   B LYS   A 1 158 ? 2.053  -1.056  4.672   0.58 27.06 ?  158 LYS   A CG   1 
ATOM   3982 C CG   T LYS   A 1 158 ? 2.578  -0.926  6.095   0.20 18.90 ?  158 LYS   A CG   1 
ATOM   3983 C CD   A LYS   A 1 158 ? 2.856  -2.413  7.017   0.22 18.58 ?  158 LYS   A CD   1 
ATOM   3984 C CD   B LYS   A 1 158 ? 1.610  -1.341  6.081   0.58 29.25 ?  158 LYS   A CD   1 
ATOM   3985 C CD   T LYS   A 1 158 ? 2.957  -2.136  6.946   0.20 20.24 ?  158 LYS   A CD   1 
ATOM   3986 C CE   A LYS   A 1 158 ? 1.602  -3.114  7.540   0.22 18.55 ?  158 LYS   A CE   1 
ATOM   3987 C CE   B LYS   A 1 158 ? 1.203  -0.068  6.790   0.58 30.64 ?  158 LYS   A CE   1 
ATOM   3988 C CE   T LYS   A 1 158 ? 1.719  -2.935  7.354   0.20 21.03 ?  158 LYS   A CE   1 
ATOM   3989 N NZ   A LYS   A 1 158 ? 1.886  -4.449  8.138   0.22 18.73 ?  158 LYS   A NZ   1 
ATOM   3990 N NZ   B LYS   A 1 158 ? -0.014 0.535   6.183   0.58 31.59 ?  158 LYS   A NZ   1 
ATOM   3991 N NZ   T LYS   A 1 158 ? 2.053  -4.167  8.126   0.20 21.66 ?  158 LYS   A NZ   1 
ATOM   3992 H H    A LYS   A 1 158 ? 5.470  0.690   4.429   0.22 17.96 ?  158 LYS   A H    1 
ATOM   3993 H H    B LYS   A 1 158 ? 5.405  0.388   3.451   0.58 24.68 ?  158 LYS   A H    1 
ATOM   3994 H H    T LYS   A 1 158 ? 5.580  0.832   4.246   0.20 18.09 ?  158 LYS   A H    1 
ATOM   3995 H HA   A LYS   A 1 158 ? 5.177  -1.725  5.414   0.22 18.96 ?  158 LYS   A HA   1 
ATOM   3996 H HA   B LYS   A 1 158 ? 4.886  -1.876  4.642   0.58 26.05 ?  158 LYS   A HA   1 
ATOM   3997 H HA   T LYS   A 1 158 ? 5.251  -1.529  5.336   0.20 19.34 ?  158 LYS   A HA   1 
ATOM   3998 H HB2  A LYS   A 1 158 ? 4.183  -0.088  6.601   0.22 20.18 ?  158 LYS   A HB2  1 
ATOM   3999 H HB2  B LYS   A 1 158 ? 3.715  -0.248  5.553   0.58 29.08 ?  158 LYS   A HB2  1 
ATOM   4000 H HB2  T LYS   A 1 158 ? 4.265  0.175   6.437   0.20 21.07 ?  158 LYS   A HB2  1 
ATOM   4001 H HB3  A LYS   A 1 158 ? 3.393  0.444   5.333   0.22 20.18 ?  158 LYS   A HB3  1 
ATOM   4002 H HB3  B LYS   A 1 158 ? 3.378  0.419   4.152   0.58 29.08 ?  158 LYS   A HB3  1 
ATOM   4003 H HB3  T LYS   A 1 158 ? 3.477  0.642   5.142   0.20 21.07 ?  158 LYS   A HB3  1 
ATOM   4004 H HG2  A LYS   A 1 158 ? 1.924  -0.613  6.768   0.22 21.35 ?  158 LYS   A HG2  1 
ATOM   4005 H HG2  B LYS   A 1 158 ? 1.432  -0.431  4.272   0.58 32.49 ?  158 LYS   A HG2  1 
ATOM   4006 H HG2  T LYS   A 1 158 ? 2.012  -0.353  6.634   0.20 22.70 ?  158 LYS   A HG2  1 
ATOM   4007 H HG3  A LYS   A 1 158 ? 1.997  -1.449  5.424   0.22 21.35 ?  158 LYS   A HG3  1 
ATOM   4008 H HG3  B LYS   A 1 158 ? 2.004  -1.899  4.202   0.58 32.49 ?  158 LYS   A HG3  1 
ATOM   4009 H HG3  T LYS   A 1 158 ? 2.080  -1.241  5.323   0.20 22.70 ?  158 LYS   A HG3  1 
ATOM   4010 H HD2  A LYS   A 1 158 ? 3.340  -3.034  6.451   0.22 22.32 ?  158 LYS   A HD2  1 
ATOM   4011 H HD2  B LYS   A 1 158 ? 0.847  -1.940  6.051   0.58 35.12 ?  158 LYS   A HD2  1 
ATOM   4012 H HD2  T LYS   A 1 158 ? 3.540  -2.722  6.439   0.20 24.31 ?  158 LYS   A HD2  1 
ATOM   4013 H HD3  A LYS   A 1 158 ? 3.403  -2.155  7.777   0.22 22.32 ?  158 LYS   A HD3  1 
ATOM   4014 H HD3  B LYS   A 1 158 ? 2.341  -1.753  6.569   0.58 35.12 ?  158 LYS   A HD3  1 
ATOM   4015 H HD3  T LYS   A 1 158 ? 3.403  -1.835  7.754   0.20 24.31 ?  158 LYS   A HD3  1 
ATOM   4016 H HE2  A LYS   A 1 158 ? 1.192  -2.560  8.223   0.22 22.27 ?  158 LYS   A HE2  1 
ATOM   4017 H HE2  B LYS   A 1 158 ? 1.013  -0.267  7.718   0.58 36.79 ?  158 LYS   A HE2  1 
ATOM   4018 H HE2  T LYS   A 1 158 ? 1.150  -2.379  7.909   0.20 25.26 ?  158 LYS   A HE2  1 
ATOM   4019 H HE3  A LYS   A 1 158 ? 0.986  -3.242  6.805   0.22 22.27 ?  158 LYS   A HE3  1 
ATOM   4020 H HE3  B LYS   A 1 158 ? 1.924  0.576   6.728   0.58 36.79 ?  158 LYS   A HE3  1 
ATOM   4021 H HE3  T LYS   A 1 158 ? 1.241  -3.205  6.556   0.20 25.26 ?  158 LYS   A HE3  1 
ATOM   4022 H HZ1  A LYS   A 1 158 ? 1.134  -4.820  8.429   0.22 22.49 ?  158 LYS   A HZ1  1 
ATOM   4023 H HZ1  B LYS   A 1 158 ? -0.287 1.223   6.675   0.58 37.93 ?  158 LYS   A HZ1  1 
ATOM   4024 H HZ1  T LYS   A 1 158 ? 1.308  -4.603  8.344   0.20 26.01 ?  158 LYS   A HZ1  1 
ATOM   4025 H HZ2  A LYS   A 1 158 ? 2.256  -4.983  7.527   0.22 22.49 ?  158 LYS   A HZ2  1 
ATOM   4026 H HZ2  B LYS   A 1 158 ? 0.166  0.821   5.360   0.58 37.93 ?  158 LYS   A HZ2  1 
ATOM   4027 H HZ2  T LYS   A 1 158 ? 2.568  -4.703  7.635   0.20 26.01 ?  158 LYS   A HZ2  1 
ATOM   4028 H HZ3  A LYS   A 1 158 ? 2.452  -4.364  8.822   0.22 22.49 ?  158 LYS   A HZ3  1 
ATOM   4029 H HZ3  B LYS   A 1 158 ? -0.666 -0.070  6.144   0.58 37.93 ?  158 LYS   A HZ3  1 
ATOM   4030 H HZ3  T LYS   A 1 158 ? 2.491  -3.952  8.871   0.20 26.01 ?  158 LYS   A HZ3  1 
ATOM   4031 N N    A ASN   A 1 159 ? 3.525  -1.161  2.725   0.22 16.64 ?  159 ASN   A N    1 
ATOM   4032 N N    B ASN   A 1 159 ? 3.447  -1.575  1.779   0.58 21.51 ?  159 ASN   A N    1 
ATOM   4033 N N    T ASN   A 1 159 ? 3.610  -1.086  2.622   0.20 17.04 ?  159 ASN   A N    1 
ATOM   4034 C CA   A ASN   A 1 159 ? 2.850  -1.857  1.635   0.22 16.99 ?  159 ASN   A CA   1 
ATOM   4035 C CA   B ASN   A 1 159 ? 2.848  -2.345  0.694   0.58 22.98 ?  159 ASN   A CA   1 
ATOM   4036 C CA   T ASN   A 1 159 ? 2.878  -1.796  1.579   0.20 17.73 ?  159 ASN   A CA   1 
ATOM   4037 C C    A ASN   A 1 159 ? 3.764  -2.905  1.015   0.22 16.14 ?  159 ASN   A C    1 
ATOM   4038 C C    B ASN   A 1 159 ? 3.780  -3.468  0.267   0.58 21.13 ?  159 ASN   A C    1 
ATOM   4039 C C    T ASN   A 1 159 ? 3.734  -2.892  0.955   0.20 17.72 ?  159 ASN   A C    1 
ATOM   4040 O O    A ASN   A 1 159 ? 3.332  -4.026  0.727   0.22 15.53 ?  159 ASN   A O    1 
ATOM   4041 O O    B ASN   A 1 159 ? 3.356  -4.612  0.065   0.58 21.78 ?  159 ASN   A O    1 
ATOM   4042 O O    T ASN   A 1 159 ? 3.228  -3.947  0.586   0.20 17.62 ?  159 ASN   A O    1 
ATOM   4043 C CB   A ASN   A 1 159 ? 2.367  -0.855  0.586   0.22 18.13 ?  159 ASN   A CB   1 
ATOM   4044 C CB   B ASN   A 1 159 ? 2.560  -1.415  -0.491  0.58 26.40 ?  159 ASN   A CB   1 
ATOM   4045 C CB   T ASN   A 1 159 ? 2.384  -0.826  0.504   0.20 18.45 ?  159 ASN   A CB   1 
ATOM   4046 C CG   A ASN   A 1 159 ? 1.160  -0.062  1.051   0.22 19.46 ?  159 ASN   A CG   1 
ATOM   4047 C CG   B ASN   A 1 159 ? 1.553  -0.327  -0.157  0.58 29.99 ?  159 ASN   A CG   1 
ATOM   4048 C CG   T ASN   A 1 159 ? 1.187  -0.013  0.962   0.20 19.40 ?  159 ASN   A CG   1 
ATOM   4049 O OD1  A ASN   A 1 159 ? 0.302  -0.583  1.760   0.22 20.33 ?  159 ASN   A OD1  1 
ATOM   4050 O OD1  B ASN   A 1 159 ? 1.810  0.859   -0.369  0.58 31.41 ?  159 ASN   A OD1  1 
ATOM   4051 O OD1  T ASN   A 1 159 ? 0.360  -0.492  1.735   0.20 20.09 ?  159 ASN   A OD1  1 
ATOM   4052 N ND2  A ASN   A 1 159 ? 1.088  1.202   0.653   0.22 19.90 ?  159 ASN   A ND2  1 
ATOM   4053 N ND2  B ASN   A 1 159 ? 0.396  -0.729  0.354   0.58 30.86 ?  159 ASN   A ND2  1 
ATOM   4054 N ND2  T ASN   A 1 159 ? 1.089  1.221   0.487   0.20 19.72 ?  159 ASN   A ND2  1 
ATOM   4055 H H    A ASN   A 1 159 ? 3.609  -0.315  2.619   0.22 19.99 ?  159 ASN   A H    1 
ATOM   4056 H H    B ASN   A 1 159 ? 3.491  -0.729  1.636   0.58 25.82 ?  159 ASN   A H    1 
ATOM   4057 H H    T ASN   A 1 159 ? 3.723  -0.251  2.472   0.20 20.46 ?  159 ASN   A H    1 
ATOM   4058 H HA   A ASN   A 1 159 ? 2.071  -2.315  1.988   0.22 20.41 ?  159 ASN   A HA   1 
ATOM   4059 H HA   B ASN   A 1 159 ? 2.003  -2.727  0.982   0.58 27.60 ?  159 ASN   A HA   1 
ATOM   4060 H HA   T ASN   A 1 159 ? 2.103  -2.224  1.973   0.20 21.29 ?  159 ASN   A HA   1 
ATOM   4061 H HB2  A ASN   A 1 159 ? 3.077  -0.227  0.395   0.22 21.77 ?  159 ASN   A HB2  1 
ATOM   4062 H HB2  B ASN   A 1 159 ? 3.384  -0.974  -0.763  0.58 31.70 ?  159 ASN   A HB2  1 
ATOM   4063 H HB2  T ASN   A 1 159 ? 3.097  -0.211  0.282   0.20 22.15 ?  159 ASN   A HB2  1 
ATOM   4064 H HB3  A ASN   A 1 159 ? 2.116  -1.333  -0.219  0.22 21.77 ?  159 ASN   A HB3  1 
ATOM   4065 H HB3  B ASN   A 1 159 ? 2.206  -1.931  -1.233  0.58 31.70 ?  159 ASN   A HB3  1 
ATOM   4066 H HB3  T ASN   A 1 159 ? 2.122  -1.333  -0.281  0.20 22.15 ?  159 ASN   A HB3  1 
ATOM   4067 H HD21 A ASN   A 1 159 ? 0.423  1.691   0.891   0.22 23.90 ?  159 ASN   A HD21 1 
ATOM   4068 H HD21 B ASN   A 1 159 ? -0.213 -0.151  0.550   0.58 37.05 ?  159 ASN   A HD21 1 
ATOM   4069 H HD21 T ASN   A 1 159 ? 0.427  1.717   0.719   0.20 23.68 ?  159 ASN   A HD21 1 
ATOM   4070 H HD22 A ASN   A 1 159 ? 1.709  1.531   0.160   0.22 23.90 ?  159 ASN   A HD22 1 
ATOM   4071 H HD22 B ASN   A 1 159 ? 0.254  -1.564  0.488   0.58 37.05 ?  159 ASN   A HD22 1 
ATOM   4072 H HD22 T ASN   A 1 159 ? 1.687  1.521   -0.048  0.20 23.68 ?  159 ASN   A HD22 1 
ATOM   4073 N N    A LEU   A 1 160 ? 5.039  -2.570  0.823   0.22 15.85 ?  160 LEU   A N    1 
ATOM   4074 N N    B LEU   A 1 160 ? 5.068  -3.159  0.156   0.58 19.28 ?  160 LEU   A N    1 
ATOM   4075 N N    T LEU   A 1 160 ? 5.034  -2.645  0.847   0.20 17.79 ?  160 LEU   A N    1 
ATOM   4076 C CA   A LEU   A 1 160 ? 5.976  -3.563  0.314   0.22 15.72 ?  160 LEU   A CA   1 
ATOM   4077 C CA   B LEU   A 1 160 ? 6.036  -4.165  -0.255  0.58 18.22 ?  160 LEU   A CA   1 
ATOM   4078 C CA   T LEU   A 1 160 ? 5.944  -3.642  0.303   0.20 18.01 ?  160 LEU   A CA   1 
ATOM   4079 C C    A LEU   A 1 160 ? 6.139  -4.710  1.301   0.22 14.78 ?  160 LEU   A C    1 
ATOM   4080 C C    B LEU   A 1 160 ? 6.186  -5.246  0.809   0.58 17.83 ?  160 LEU   A C    1 
ATOM   4081 O O    A LEU   A 1 160 ? 6.186  -5.879  0.902   0.22 14.47 ?  160 LEU   A O    1 
ATOM   4082 O O    B LEU   A 1 160 ? 6.175  -6.441  0.497   0.58 18.61 ?  160 LEU   A O    1 
ATOM   4083 C CB   A LEU   A 1 160 ? 7.325  -2.915  0.017   0.22 16.29 ?  160 LEU   A CB   1 
ATOM   4084 C CB   B LEU   A 1 160 ? 7.375  -3.494  -0.520  0.58 18.87 ?  160 LEU   A CB   1 
ATOM   4085 C CB   T LEU   A 1 160 ? 7.298  -3.016  -0.019  0.20 18.03 ?  160 LEU   A CB   1 
ATOM   4086 C CG   A LEU   A 1 160 ? 8.413  -3.897  -0.417  0.22 16.98 ?  160 LEU   A CG   1 
ATOM   4087 C CG   B LEU   A 1 160 ? 8.510  -4.474  -0.782  0.58 20.09 ?  160 LEU   A CG   1 
ATOM   4088 C CG   T LEU   A 1 160 ? 8.364  -4.012  -0.471  0.20 18.32 ?  160 LEU   A CG   1 
ATOM   4089 C CD1  A LEU   A 1 160 ? 7.960  -4.693  -1.629  0.22 17.40 ?  160 LEU   A CD1  1 
ATOM   4090 C CD1  B LEU   A 1 160 ? 8.219  -5.293  -2.025  0.58 20.82 ?  160 LEU   A CD1  1 
ATOM   4091 C CD1  T LEU   A 1 160 ? 7.913  -4.762  -1.710  0.20 18.59 ?  160 LEU   A CD1  1 
ATOM   4092 C CD2  A LEU   A 1 160 ? 9.707  -3.163  -0.704  0.22 17.21 ?  160 LEU   A CD2  1 
ATOM   4093 C CD2  B LEU   A 1 160 ? 9.823  -3.726  -0.899  0.58 21.06 ?  160 LEU   A CD2  1 
ATOM   4094 C CD2  T LEU   A 1 160 ? 9.666  -3.291  -0.729  0.20 18.44 ?  160 LEU   A CD2  1 
ATOM   4095 H H    A LEU   A 1 160 ? 5.377  -1.799  0.985   0.22 19.04 ?  160 LEU   A H    1 
ATOM   4096 H H    B LEU   A 1 160 ? 5.398  -2.383  0.324   0.58 23.15 ?  160 LEU   A H    1 
ATOM   4097 H H    T LEU   A 1 160 ? 5.412  -1.911  1.082   0.20 21.37 ?  160 LEU   A H    1 
ATOM   4098 H HA   A LEU   A 1 160 ? 5.628  -3.928  -0.511  0.22 18.88 ?  160 LEU   A HA   1 
ATOM   4099 H HA   B LEU   A 1 160 ? 5.730  -4.577  -1.076  0.58 21.88 ?  160 LEU   A HA   1 
ATOM   4100 H HB2  A LEU   A 1 160 ? 7.211  -2.261  -0.692  0.22 19.57 ?  160 LEU   A HB2  1 
ATOM   4101 H HB2  B LEU   A 1 160 ? 7.295  -2.893  -1.283  0.58 22.66 ?  160 LEU   A HB2  1 
ATOM   4102 H HB2  T LEU   A 1 160 ? 7.180  -2.366  -0.730  0.20 21.65 ?  160 LEU   A HB2  1 
ATOM   4103 H HB3  A LEU   A 1 160 ? 7.637  -2.478  0.822   0.22 19.57 ?  160 LEU   A HB3  1 
ATOM   4104 H HB3  B LEU   A 1 160 ? 7.607  -2.996  0.273   0.58 22.66 ?  160 LEU   A HB3  1 
ATOM   4105 H HB3  T LEU   A 1 160 ? 7.631  -2.573  0.777   0.20 21.65 ?  160 LEU   A HB3  1 
ATOM   4106 H HG   A LEU   A 1 160 ? 8.585  -4.522  0.306   0.22 20.40 ?  160 LEU   A HG   1 
ATOM   4107 H HG   B LEU   A 1 160 ? 8.589  -5.081  -0.029  0.58 24.12 ?  160 LEU   A HG   1 
ATOM   4108 H HG   T LEU   A 1 160 ? 8.514  -4.659  0.238   0.20 22.00 ?  160 LEU   A HG   1 
ATOM   4109 H HD11 A LEU   A 1 160 ? 8.713  -5.201  -1.968  0.22 20.90 ?  160 LEU   A HD11 1 
ATOM   4110 H HD11 B LEU   A 1 160 ? 8.996  -5.829  -2.231  0.58 25.00 ?  160 LEU   A HD11 1 
ATOM   4111 H HD11 T LEU   A 1 160 ? 8.648  -5.308  -2.031  0.20 22.32 ?  160 LEU   A HD11 1 
ATOM   4112 H HD12 A LEU   A 1 160 ? 7.248  -5.297  -1.365  0.22 20.90 ?  160 LEU   A HD12 1 
ATOM   4113 H HD12 B LEU   A 1 160 ? 7.455  -5.866  -1.854  0.58 25.00 ?  160 LEU   A HD12 1 
ATOM   4114 H HD12 T LEU   A 1 160 ? 7.158  -5.326  -1.482  0.20 22.32 ?  160 LEU   A HD12 1 
ATOM   4115 H HD13 A LEU   A 1 160 ? 7.642  -4.079  -2.308  0.22 20.90 ?  160 LEU   A HD13 1 
ATOM   4116 H HD13 B LEU   A 1 160 ? 8.024  -4.690  -2.758  0.58 25.00 ?  160 LEU   A HD13 1 
ATOM   4117 H HD13 T LEU   A 1 160 ? 7.657  -4.120  -2.389  0.20 22.32 ?  160 LEU   A HD13 1 
ATOM   4118 H HD21 A LEU   A 1 160 ? 10.382 -3.808  -0.973  0.22 20.67 ?  160 LEU   A HD21 1 
ATOM   4119 H HD21 B LEU   A 1 160 ? 10.536 -4.364  -1.050  0.58 25.29 ?  160 LEU   A HD21 1 
ATOM   4120 H HD21 T LEU   A 1 160 ? 10.295 -3.912  -1.129  0.20 22.14 ?  160 LEU   A HD21 1 
ATOM   4121 H HD22 A LEU   A 1 160 ? 9.556  -2.526  -1.418  0.22 20.67 ?  160 LEU   A HD22 1 
ATOM   4122 H HD22 B LEU   A 1 160 ? 9.768  -3.106  -1.643  0.58 25.29 ?  160 LEU   A HD22 1 
ATOM   4123 H HD22 T LEU   A 1 160 ? 9.500  -2.551  -1.333  0.20 22.14 ?  160 LEU   A HD22 1 
ATOM   4124 H HD23 A LEU   A 1 160 ? 9.994  -2.701  0.099   0.22 20.67 ?  160 LEU   A HD23 1 
ATOM   4125 H HD23 B LEU   A 1 160 ? 9.986  -3.237  -0.075  0.58 25.29 ?  160 LEU   A HD23 1 
ATOM   4126 H HD23 T LEU   A 1 160 ? 10.014 -2.962  0.113   0.20 22.14 ?  160 LEU   A HD23 1 
ATOM   4127 N N    A TYR   A 1 161 ? 6.222  -4.397  2.596   0.42 15.65 ?  161 TYR   A N    1 
ATOM   4128 N N    B TYR   A 1 161 ? 6.350  -4.844  2.071   0.58 18.40 ?  161 TYR   A N    1 
ATOM   4129 C CA   A TYR   A 1 161 ? 6.344  -5.443  3.606   0.42 16.01 ?  161 TYR   A CA   1 
ATOM   4130 C CA   B TYR   A 1 161 ? 6.439  -5.820  3.153   0.58 18.97 ?  161 TYR   A CA   1 
ATOM   4131 C C    A TYR   A 1 161 ? 5.230  -6.476  3.477   0.42 17.43 ?  161 TYR   A C    1 
ATOM   4132 C C    B TYR   A 1 161 ? 5.202  -6.702  3.184   0.58 20.68 ?  161 TYR   A C    1 
ATOM   4133 O O    A TYR   A 1 161 ? 5.488  -7.685  3.477   0.42 16.94 ?  161 TYR   A O    1 
ATOM   4134 O O    B TYR   A 1 161 ? 5.303  -7.935  3.205   0.58 20.52 ?  161 TYR   A O    1 
ATOM   4135 C CB   A TYR   A 1 161 ? 6.369  -4.841  5.014   0.42 16.03 ?  161 TYR   A CB   1 
ATOM   4136 C CB   B TYR   A 1 161 ? 6.600  -5.109  4.497   0.58 18.64 ?  161 TYR   A CB   1 
ATOM   4137 C CG   A TYR   A 1 161 ? 6.317  -5.914  6.076   0.42 15.89 ?  161 TYR   A CG   1 
ATOM   4138 C CG   B TYR   A 1 161 ? 6.440  -6.033  5.688   0.58 19.18 ?  161 TYR   A CG   1 
ATOM   4139 C CD1  A TYR   A 1 161 ? 7.476  -6.536  6.518   0.42 16.04 ?  161 TYR   A CD1  1 
ATOM   4140 C CD1  B TYR   A 1 161 ? 7.501  -6.808  6.132   0.58 19.88 ?  161 TYR   A CD1  1 
ATOM   4141 C CD2  A TYR   A 1 161 ? 5.103  -6.335  6.611   0.42 16.19 ?  161 TYR   A CD2  1 
ATOM   4142 C CD2  B TYR   A 1 161 ? 5.227  -6.124  6.374   0.58 19.54 ?  161 TYR   A CD2  1 
ATOM   4143 C CE1  A TYR   A 1 161 ? 7.429  -7.532  7.470   0.42 16.30 ?  161 TYR   A CE1  1 
ATOM   4144 C CE1  B TYR   A 1 161 ? 7.363  -7.653  7.216   0.58 19.76 ?  161 TYR   A CE1  1 
ATOM   4145 C CE2  A TYR   A 1 161 ? 5.048  -7.332  7.563   0.42 16.25 ?  161 TYR   A CE2  1 
ATOM   4146 C CE2  B TYR   A 1 161 ? 5.083  -6.970  7.467   0.58 19.67 ?  161 TYR   A CE2  1 
ATOM   4147 C CZ   A TYR   A 1 161 ? 6.216  -7.927  7.989   0.42 16.37 ?  161 TYR   A CZ   1 
ATOM   4148 C CZ   B TYR   A 1 161 ? 6.156  -7.731  7.880   0.58 20.17 ?  161 TYR   A CZ   1 
ATOM   4149 O OH   A TYR   A 1 161 ? 6.179  -8.923  8.938   0.42 16.58 ?  161 TYR   A OH   1 
ATOM   4150 O OH   B TYR   A 1 161 ? 6.039  -8.577  8.958   0.58 21.47 ?  161 TYR   A OH   1 
ATOM   4151 H H    A TYR   A 1 161 ? 6.209  -3.599  2.911   0.42 18.79 ?  161 TYR   A H    1 
ATOM   4152 H H    B TYR   A 1 161 ? 6.398  -4.027  2.324   0.58 22.10 ?  161 TYR   A H    1 
ATOM   4153 H HA   A TYR   A 1 161 ? 7.182  -5.908  3.478   0.42 19.23 ?  161 TYR   A HA   1 
ATOM   4154 H HA   B TYR   A 1 161 ? 7.213  -6.387  3.012   0.58 22.78 ?  161 TYR   A HA   1 
ATOM   4155 H HB2  A TYR   A 1 161 ? 7.190  -4.334  5.135   0.42 19.25 ?  161 TYR   A HB2  1 
ATOM   4156 H HB2  B TYR   A 1 161 ? 7.490  -4.720  4.539   0.58 22.38 ?  161 TYR   A HB2  1 
ATOM   4157 H HB3  A TYR   A 1 161 ? 5.600  -4.259  5.134   0.42 19.25 ?  161 TYR   A HB3  1 
ATOM   4158 H HB3  B TYR   A 1 161 ? 5.932  -4.411  4.565   0.58 22.38 ?  161 TYR   A HB3  1 
ATOM   4159 H HD1  A TYR   A 1 161 ? 8.299  -6.274  6.173   0.42 19.26 ?  161 TYR   A HD1  1 
ATOM   4160 H HD1  B TYR   A 1 161 ? 8.317  -6.765  5.689   0.58 23.87 ?  161 TYR   A HD1  1 
ATOM   4161 H HD2  A TYR   A 1 161 ? 4.312  -5.937  6.325   0.42 19.44 ?  161 TYR   A HD2  1 
ATOM   4162 H HD2  B TYR   A 1 161 ? 4.500  -5.609  6.100   0.58 23.47 ?  161 TYR   A HD2  1 
ATOM   4163 H HE1  A TYR   A 1 161 ? 8.217  -7.939  7.760   0.42 19.58 ?  161 TYR   A HE1  1 
ATOM   4164 H HE1  B TYR   A 1 161 ? 8.085  -8.168  7.500   0.58 23.73 ?  161 TYR   A HE1  1 
ATOM   4165 H HE2  A TYR   A 1 161 ? 4.227  -7.603  7.912   0.42 19.52 ?  161 TYR   A HE2  1 
ATOM   4166 H HE2  B TYR   A 1 161 ? 4.267  -7.020  7.919   0.58 23.63 ?  161 TYR   A HE2  1 
ATOM   4167 H HH   A TYR   A 1 161 ? 5.375  -9.073  9.157   0.42 19.91 ?  161 TYR   A HH   1 
ATOM   4168 H HH   B TYR   A 1 161 ? 5.266  -8.524  9.293   0.58 25.78 ?  161 TYR   A HH   1 
ATOM   4169 N N    A ASP   A 1 162 ? 3.978  -6.017  3.369   0.42 18.76 ?  162 ASP   A N    1 
ATOM   4170 N N    B ASP   A 1 162 ? 4.020  -6.075  3.197   0.58 21.83 ?  162 ASP   A N    1 
ATOM   4171 C CA   A ASP   A 1 162 ? 2.859  -6.955  3.290   0.42 19.20 ?  162 ASP   A CA   1 
ATOM   4172 C CA   B ASP   A 1 162 ? 2.766  -6.822  3.227   0.58 23.29 ?  162 ASP   A CA   1 
ATOM   4173 C C    A ASP   A 1 162 ? 2.918  -7.776  2.010   0.42 18.67 ?  162 ASP   A C    1 
ATOM   4174 C C    B ASP   A 1 162 ? 2.716  -7.848  2.103   0.58 23.88 ?  162 ASP   A C    1 
ATOM   4175 O O    A ASP   A 1 162 ? 2.594  -8.970  2.016   0.42 19.19 ?  162 ASP   A O    1 
ATOM   4176 O O    B ASP   A 1 162 ? 2.205  -8.960  2.284   0.58 24.49 ?  162 ASP   A O    1 
ATOM   4177 C CB   A ASP   A 1 162 ? 1.522  -6.217  3.387   0.42 19.91 ?  162 ASP   A CB   1 
ATOM   4178 C CB   B ASP   A 1 162 ? 1.578  -5.856  3.116   0.58 24.29 ?  162 ASP   A CB   1 
ATOM   4179 C CG   A ASP   A 1 162 ? 1.234  -5.702  4.784   0.42 20.60 ?  162 ASP   A CG   1 
ATOM   4180 C CG   B ASP   A 1 162 ? 1.324  -5.065  4.386   0.58 25.28 ?  162 ASP   A CG   1 
ATOM   4181 O OD1  A ASP   A 1 162 ? 1.872  -6.180  5.745   0.42 21.39 ?  162 ASP   A OD1  1 
ATOM   4182 O OD1  B ASP   A 1 162 ? 1.930  -5.382  5.425   0.58 25.17 ?  162 ASP   A OD1  1 
ATOM   4183 O OD2  A ASP   A 1 162 ? 0.345  -4.833  4.920   0.42 20.56 -1 162 ASP   A OD2  1 
ATOM   4184 O OD2  B ASP   A 1 162 ? 0.499  -4.123  4.337   0.58 25.76 -1 162 ASP   A OD2  1 
ATOM   4185 H H    A ASP   A 1 162 ? 3.751  -5.185  3.340   0.42 22.53 ?  162 ASP   A H    1 
ATOM   4186 H H    B ASP   A 1 162 ? 3.923  -5.220  3.193   0.58 26.21 ?  162 ASP   A H    1 
ATOM   4187 H HA   A ASP   A 1 162 ? 2.907  -7.569  4.037   0.42 23.06 ?  162 ASP   A HA   1 
ATOM   4188 H HA   B ASP   A 1 162 ? 2.693  -7.291  4.073   0.58 27.96 ?  162 ASP   A HA   1 
ATOM   4189 H HB2  A ASP   A 1 162 ? 1.526  -5.467  2.771   0.42 23.90 ?  162 ASP   A HB2  1 
ATOM   4190 H HB2  B ASP   A 1 162 ? 1.746  -5.211  2.421   0.58 29.17 ?  162 ASP   A HB2  1 
ATOM   4191 H HB3  A ASP   A 1 162 ? 0.802  -6.828  3.158   0.42 23.90 ?  162 ASP   A HB3  1 
ATOM   4192 H HB3  B ASP   A 1 162 ? 0.772  -6.356  2.932   0.58 29.17 ?  162 ASP   A HB3  1 
ATOM   4193 N N    A LYS   A 1 163 ? 3.328  -7.159  0.901   0.42 19.10 ?  163 LYS   A N    1 
ATOM   4194 N N    B LYS   A 1 163 ? 3.245  -7.494  0.932   0.58 24.95 ?  163 LYS   A N    1 
ATOM   4195 C CA   A LYS   A 1 163 ? 3.460  -7.921  -0.335  0.42 19.33 ?  163 LYS   A CA   1 
ATOM   4196 C CA   B LYS   A 1 163 ? 3.219  -8.409  -0.203  0.58 25.68 ?  163 LYS   A CA   1 
ATOM   4197 C C    A LYS   A 1 163 ? 4.552  -8.975  -0.214  0.42 18.80 ?  163 LYS   A C    1 
ATOM   4198 C C    B LYS   A 1 163 ? 4.320  -9.463  -0.109  0.58 23.47 ?  163 LYS   A C    1 
ATOM   4199 O O    A LYS   A 1 163 ? 4.410  -10.089 -0.731  0.42 18.79 ?  163 LYS   A O    1 
ATOM   4200 O O    B LYS   A 1 163 ? 4.098  -10.626 -0.465  0.58 23.30 ?  163 LYS   A O    1 
ATOM   4201 C CB   A LYS   A 1 163 ? 3.734  -6.983  -1.509  0.42 21.12 ?  163 LYS   A CB   1 
ATOM   4202 C CB   B LYS   A 1 163 ? 3.286  -7.610  -1.509  0.58 28.79 ?  163 LYS   A CB   1 
ATOM   4203 C CG   A LYS   A 1 163 ? 3.698  -7.687  -2.854  0.42 23.50 ?  163 LYS   A CG   1 
ATOM   4204 C CG   B LYS   A 1 163 ? 4.261  -8.150  -2.540  0.58 31.40 ?  163 LYS   A CG   1 
ATOM   4205 C CD   A LYS   A 1 163 ? 4.164  -6.786  -3.977  0.42 25.80 ?  163 LYS   A CD   1 
ATOM   4206 C CD   B LYS   A 1 163 ? 4.713  -7.074  -3.495  0.58 33.78 ?  163 LYS   A CD   1 
ATOM   4207 C CE   A LYS   A 1 163 ? 4.132  -7.518  -5.308  0.42 27.93 ?  163 LYS   A CE   1 
ATOM   4208 C CE   B LYS   A 1 163 ? 3.750  -6.901  -4.648  0.58 35.42 ?  163 LYS   A CE   1 
ATOM   4209 N NZ   A LYS   A 1 163 ? 4.819  -6.752  -6.381  0.42 29.01 ?  163 LYS   A NZ   1 
ATOM   4210 N NZ   B LYS   A 1 163 ? 4.339  -6.036  -5.705  0.58 36.24 ?  163 LYS   A NZ   1 
ATOM   4211 H H    A LYS   A 1 163 ? 3.526  -6.320  0.845   0.42 22.94 ?  163 LYS   A H    1 
ATOM   4212 H H    B LYS   A 1 163 ? 3.613  -6.734  0.772   0.58 29.95 ?  163 LYS   A H    1 
ATOM   4213 H HA   A LYS   A 1 163 ? 2.619  -8.371  -0.508  0.42 23.21 ?  163 LYS   A HA   1 
ATOM   4214 H HA   B LYS   A 1 163 ? 2.375  -8.884  -0.196  0.58 30.84 ?  163 LYS   A HA   1 
ATOM   4215 H HB2  A LYS   A 1 163 ? 3.057  -6.282  -1.522  0.42 25.36 ?  163 LYS   A HB2  1 
ATOM   4216 H HB2  B LYS   A 1 163 ? 2.396  -7.613  -1.914  0.58 34.56 ?  163 LYS   A HB2  1 
ATOM   4217 H HB3  A LYS   A 1 163 ? 4.611  -6.588  -1.400  0.42 25.36 ?  163 LYS   A HB3  1 
ATOM   4218 H HB3  B LYS   A 1 163 ? 3.538  -6.698  -1.304  0.58 34.56 ?  163 LYS   A HB3  1 
ATOM   4219 H HG2  A LYS   A 1 163 ? 4.283  -8.460  -2.826  0.42 28.21 ?  163 LYS   A HG2  1 
ATOM   4220 H HG2  B LYS   A 1 163 ? 5.067  -8.475  -2.121  0.58 37.69 ?  163 LYS   A HG2  1 
ATOM   4221 H HG3  A LYS   A 1 163 ? 2.787  -7.964  -3.043  0.42 28.21 ?  163 LYS   A HG3  1 
ATOM   4222 H HG3  B LYS   A 1 163 ? 3.826  -8.863  -3.037  0.58 37.69 ?  163 LYS   A HG3  1 
ATOM   4223 H HD2  A LYS   A 1 163 ? 3.575  -6.017  -4.037  0.42 30.98 ?  163 LYS   A HD2  1 
ATOM   4224 H HD2  B LYS   A 1 163 ? 4.780  -6.229  -3.019  0.58 40.55 ?  163 LYS   A HD2  1 
ATOM   4225 H HD3  A LYS   A 1 163 ? 5.074  -6.501  -3.804  0.42 30.98 ?  163 LYS   A HD3  1 
ATOM   4226 H HD3  B LYS   A 1 163 ? 5.580  -7.323  -3.846  0.58 40.55 ?  163 LYS   A HD3  1 
ATOM   4227 H HE2  A LYS   A 1 163 ? 4.572  -8.377  -5.214  0.42 33.53 ?  163 LYS   A HE2  1 
ATOM   4228 H HE2  B LYS   A 1 163 ? 3.556  -7.770  -5.034  0.58 42.52 ?  163 LYS   A HE2  1 
ATOM   4229 H HE3  A LYS   A 1 163 ? 3.210  -7.649  -5.574  0.42 33.53 ?  163 LYS   A HE3  1 
ATOM   4230 H HE3  B LYS   A 1 163 ? 2.937  -6.484  -4.326  0.58 42.52 ?  163 LYS   A HE3  1 
ATOM   4231 H HZ1  A LYS   A 1 163 ? 4.786  -7.205  -7.146  0.42 34.82 ?  163 LYS   A HZ1  1 
ATOM   4232 H HZ1  B LYS   A 1 163 ? 3.765  -5.945  -6.376  0.58 43.50 ?  163 LYS   A HZ1  1 
ATOM   4233 H HZ2  A LYS   A 1 163 ? 4.421  -5.964  -6.492  0.42 34.82 ?  163 LYS   A HZ2  1 
ATOM   4234 H HZ2  B LYS   A 1 163 ? 4.528  -5.233  -5.370  0.58 43.50 ?  163 LYS   A HZ2  1 
ATOM   4235 H HZ3  A LYS   A 1 163 ? 5.671  -6.617  -6.160  0.42 34.82 ?  163 LYS   A HZ3  1 
ATOM   4236 H HZ3  B LYS   A 1 163 ? 5.091  -6.403  -6.014  0.58 43.50 ?  163 LYS   A HZ3  1 
ATOM   4237 N N    A LEU   A 1 164 ? 5.650  -8.643  0.465   0.42 17.41 ?  164 LEU   A N    1 
ATOM   4238 N N    B LEU   A 1 164 ? 5.516  -9.080  0.351   0.58 21.92 ?  164 LEU   A N    1 
ATOM   4239 C CA   A LEU   A 1 164 ? 6.729  -9.609  0.644   0.42 17.12 ?  164 LEU   A CA   1 
ATOM   4240 C CA   B LEU   A 1 164 ? 6.603  -10.049 0.458   0.58 21.54 ?  164 LEU   A CA   1 
ATOM   4241 C C    A LEU   A 1 164 ? 6.270  -10.802 1.471   0.42 17.76 ?  164 LEU   A C    1 
ATOM   4242 C C    B LEU   A 1 164 ? 6.239  -11.183 1.408   0.58 21.58 ?  164 LEU   A C    1 
ATOM   4243 O O    A LEU   A 1 164 ? 6.586  -11.952 1.144   0.42 18.04 ?  164 LEU   A O    1 
ATOM   4244 O O    B LEU   A 1 164 ? 6.511  -12.355 1.121   0.58 21.81 ?  164 LEU   A O    1 
ATOM   4245 C CB   A LEU   A 1 164 ? 7.922  -8.931  1.310   0.42 16.16 ?  164 LEU   A CB   1 
ATOM   4246 C CB   B LEU   A 1 164 ? 7.877  -9.354  0.933   0.58 21.22 ?  164 LEU   A CB   1 
ATOM   4247 C CG   A LEU   A 1 164 ? 8.720  -7.973  0.424   0.42 14.88 ?  164 LEU   A CG   1 
ATOM   4248 C CG   B LEU   A 1 164 ? 8.584  -8.449  -0.076  0.58 21.26 ?  164 LEU   A CG   1 
ATOM   4249 C CD1  A LEU   A 1 164 ? 9.684  -7.186  1.281   0.42 14.33 ?  164 LEU   A CD1  1 
ATOM   4250 C CD1  B LEU   A 1 164 ? 9.729  -7.710  0.593   0.58 21.24 ?  164 LEU   A CD1  1 
ATOM   4251 C CD2  A LEU   A 1 164 ? 9.471  -8.725  -0.664  0.42 14.89 ?  164 LEU   A CD2  1 
ATOM   4252 C CD2  B LEU   A 1 164 ? 9.084  -9.282  -1.236  0.58 22.11 ?  164 LEU   A CD2  1 
ATOM   4253 H H    A LEU   A 1 164 ? 5.790  -7.871  0.826   0.42 20.91 ?  164 LEU   A H    1 
ATOM   4254 H H    B LEU   A 1 164 ? 5.717  -8.285  0.611   0.58 26.33 ?  164 LEU   A H    1 
ATOM   4255 H HA   A LEU   A 1 164 ? 7.006  -9.932  -0.224  0.42 20.56 ?  164 LEU   A HA   1 
ATOM   4256 H HA   B LEU   A 1 164 ? 6.774  -10.435 -0.416  0.58 25.87 ?  164 LEU   A HA   1 
ATOM   4257 H HB2  A LEU   A 1 164 ? 7.599  -8.422  2.072   0.42 19.41 ?  164 LEU   A HB2  1 
ATOM   4258 H HB2  B LEU   A 1 164 ? 7.656  -8.804  1.699   0.58 25.48 ?  164 LEU   A HB2  1 
ATOM   4259 H HB3  A LEU   A 1 164 ? 8.531  -9.618  1.615   0.42 19.41 ?  164 LEU   A HB3  1 
ATOM   4260 H HB3  B LEU   A 1 164 ? 8.515  -10.035 1.198   0.58 25.48 ?  164 LEU   A HB3  1 
ATOM   4261 H HG   A LEU   A 1 164 ? 8.111  -7.343  0.002   0.42 17.88 ?  164 LEU   A HG   1 
ATOM   4262 H HG   B LEU   A 1 164 ? 7.956  -7.795  -0.423  0.58 25.53 ?  164 LEU   A HG   1 
ATOM   4263 H HD11 A LEU   A 1 164 ? 10.192 -6.586  0.715   0.42 17.21 ?  164 LEU   A HD11 1 
ATOM   4264 H HD11 B LEU   A 1 164 ? 10.167 -7.143  -0.061  0.58 25.51 ?  164 LEU   A HD11 1 
ATOM   4265 H HD12 A LEU   A 1 164 ? 9.183  -6.679  1.939   0.42 17.21 ?  164 LEU   A HD12 1 
ATOM   4266 H HD12 B LEU   A 1 164 ? 9.376  -7.171  1.317   0.58 25.51 ?  164 LEU   A HD12 1 
ATOM   4267 H HD13 A LEU   A 1 164 ? 10.283 -7.806  1.728   0.42 17.21 ?  164 LEU   A HD13 1 
ATOM   4268 H HD13 B LEU   A 1 164 ? 10.361 -8.360  0.942   0.58 25.51 ?  164 LEU   A HD13 1 
ATOM   4269 H HD21 A LEU   A 1 164 ? 10.056 -8.107  -1.127  0.42 17.88 ?  164 LEU   A HD21 1 
ATOM   4270 H HD21 B LEU   A 1 164 ? 9.643  -8.731  -1.802  0.58 26.55 ?  164 LEU   A HD21 1 
ATOM   4271 H HD22 A LEU   A 1 164 ? 9.991  -9.432  -0.254  0.42 17.88 ?  164 LEU   A HD22 1 
ATOM   4272 H HD22 B LEU   A 1 164 ? 9.596  -10.029 -0.887  0.58 26.55 ?  164 LEU   A HD22 1 
ATOM   4273 H HD23 A LEU   A 1 164 ? 8.828  -9.102  -1.285  0.42 17.88 ?  164 LEU   A HD23 1 
ATOM   4274 H HD23 B LEU   A 1 164 ? 8.323  -9.611  -1.740  0.58 26.55 ?  164 LEU   A HD23 1 
ATOM   4275 N N    A VAL   A 1 165 ? 5.533  -10.548 2.552   0.42 17.40 ?  165 VAL   A N    1 
ATOM   4276 N N    B VAL   A 1 165 ? 5.639  -10.853 2.553   0.58 21.63 ?  165 VAL   A N    1 
ATOM   4277 C CA   A VAL   A 1 165 ? 5.075  -11.635 3.415   0.42 17.54 ?  165 VAL   A CA   1 
ATOM   4278 C CA   B VAL   A 1 165 ? 5.310  -11.876 3.543   0.58 22.18 ?  165 VAL   A CA   1 
ATOM   4279 C C    A VAL   A 1 165 ? 4.049  -12.502 2.690   0.42 17.79 ?  165 VAL   A C    1 
ATOM   4280 C C    B VAL   A 1 165 ? 4.080  -12.685 3.148   0.58 24.19 ?  165 VAL   A C    1 
ATOM   4281 O O    A VAL   A 1 165 ? 4.160  -13.734 2.656   0.42 17.77 ?  165 VAL   A O    1 
ATOM   4282 O O    B VAL   A 1 165 ? 3.886  -13.798 3.657   0.58 24.23 ?  165 VAL   A O    1 
ATOM   4283 C CB   A VAL   A 1 165 ? 4.526  -11.066 4.737   0.42 18.58 ?  165 VAL   A CB   1 
ATOM   4284 C CB   B VAL   A 1 165 ? 5.156  -11.265 4.947   0.58 22.13 ?  165 VAL   A CB   1 
ATOM   4285 C CG1  A VAL   A 1 165 ? 3.830  -12.154 5.543   0.42 18.97 ?  165 VAL   A CG1  1 
ATOM   4286 C CG1  B VAL   A 1 165 ? 6.390  -10.453 5.311   0.58 22.34 ?  165 VAL   A CG1  1 
ATOM   4287 C CG2  A VAL   A 1 165 ? 5.647  -10.425 5.549   0.42 18.06 ?  165 VAL   A CG2  1 
ATOM   4288 C CG2  B VAL   A 1 165 ? 3.911  -10.400 5.028   0.58 22.25 ?  165 VAL   A CG2  1 
ATOM   4289 H H    A VAL   A 1 165 ? 5.284  -9.761  2.807   0.42 20.90 ?  165 VAL   A H    1 
ATOM   4290 H H    B VAL   A 1 165 ? 5.420  -10.053 2.775   0.58 25.98 ?  165 VAL   A H    1 
ATOM   4291 H HA   A VAL   A 1 165 ? 5.831  -12.195 3.634   0.42 21.06 ?  165 VAL   A HA   1 
ATOM   4292 H HA   B VAL   A 1 165 ? 6.045  -12.501 3.587   0.58 26.63 ?  165 VAL   A HA   1 
ATOM   4293 H HB   A VAL   A 1 165 ? 3.872  -10.377 4.543   0.42 22.31 ?  165 VAL   A HB   1 
ATOM   4294 H HB   B VAL   A 1 165 ? 5.072  -11.980 5.600   0.58 26.57 ?  165 VAL   A HB   1 
ATOM   4295 H HG11 A VAL   A 1 165 ? 3.736  -11.856 6.462   0.42 22.78 ?  165 VAL   A HG11 1 
ATOM   4296 H HG11 B VAL   A 1 165 ? 6.320  -10.166 6.235   0.58 26.82 ?  165 VAL   A HG11 1 
ATOM   4297 H HG12 A VAL   A 1 165 ? 2.954  -12.322 5.162   0.42 22.78 ?  165 VAL   A HG12 1 
ATOM   4298 H HG12 B VAL   A 1 165 ? 7.178  -11.006 5.195   0.58 26.82 ?  165 VAL   A HG12 1 
ATOM   4299 H HG13 A VAL   A 1 165 ? 4.367  -12.961 5.513   0.42 22.78 ?  165 VAL   A HG13 1 
ATOM   4300 H HG13 B VAL   A 1 165 ? 6.441  -9.678  4.728   0.58 26.82 ?  165 VAL   A HG13 1 
ATOM   4301 H HG21 A VAL   A 1 165 ? 5.286  -10.092 6.386   0.42 21.68 ?  165 VAL   A HG21 1 
ATOM   4302 H HG21 B VAL   A 1 165 ? 3.853  -10.024 5.919   0.58 26.72 ?  165 VAL   A HG21 1 
ATOM   4303 H HG22 A VAL   A 1 165 ? 6.331  -11.089 5.726   0.42 21.68 ?  165 VAL   A HG22 1 
ATOM   4304 H HG22 B VAL   A 1 165 ? 3.986  -9.692  4.374   0.58 26.72 ?  165 VAL   A HG22 1 
ATOM   4305 H HG23 A VAL   A 1 165 ? 6.026  -9.690  5.039   0.42 21.68 ?  165 VAL   A HG23 1 
ATOM   4306 H HG23 B VAL   A 1 165 ? 3.128  -10.938 4.844   0.58 26.72 ?  165 VAL   A HG23 1 
ATOM   4307 N N    A SER   A 1 166 ? 3.041  -11.870 2.085   0.42 17.80 ?  166 SER   A N    1 
ATOM   4308 N N    B SER   A 1 166 ? 3.241  -12.159 2.258   0.58 26.40 ?  166 SER   A N    1 
ATOM   4309 C CA   A SER   A 1 166 ? 1.941  -12.619 1.484   0.42 19.08 ?  166 SER   A CA   1 
ATOM   4310 C CA   B SER   A 1 166 ? 2.091  -12.892 1.751   0.58 29.10 ?  166 SER   A CA   1 
ATOM   4311 C C    A SER   A 1 166 ? 2.405  -13.496 0.332   0.42 19.11 ?  166 SER   A C    1 
ATOM   4312 C C    B SER   A 1 166 ? 2.414  -13.645 0.467   0.58 31.03 ?  166 SER   A C    1 
ATOM   4313 O O    A SER   A 1 166 ? 1.771  -14.519 0.037   0.42 20.21 ?  166 SER   A O    1 
ATOM   4314 O O    B SER   A 1 166 ? 1.504  -13.940 -0.318  0.58 30.83 ?  166 SER   A O    1 
ATOM   4315 C CB   A SER   A 1 166 ? 0.861  -11.655 0.987   0.42 20.34 ?  166 SER   A CB   1 
ATOM   4316 C CB   B SER   A 1 166 ? 0.910  -11.940 1.548   0.58 30.12 ?  166 SER   A CB   1 
ATOM   4317 O OG   A SER   A 1 166 ? 0.256  -10.960 2.065   0.42 21.87 ?  166 SER   A OG   1 
ATOM   4318 O OG   B SER   A 1 166 ? 0.723  -11.123 2.693   0.58 31.43 ?  166 SER   A OG   1 
ATOM   4319 H H    A SER   A 1 166 ? 2.964  -11.017 2.020   0.42 21.38 ?  166 SER   A H    1 
ATOM   4320 H H    B SER   A 1 166 ? 3.325  -11.368 1.926   0.58 31.69 ?  166 SER   A H    1 
ATOM   4321 H HA   A SER   A 1 166 ? 1.540  -13.193 2.149   0.42 22.91 ?  166 SER   A HA   1 
ATOM   4322 H HA   B SER   A 1 166 ? 1.821  -13.541 2.413   0.58 34.94 ?  166 SER   A HA   1 
ATOM   4323 H HB2  A SER   A 1 166 ? 1.264  -11.012 0.380   0.42 24.43 ?  166 SER   A HB2  1 
ATOM   4324 H HB2  B SER   A 1 166 ? 1.078  -11.373 0.780   0.58 36.16 ?  166 SER   A HB2  1 
ATOM   4325 H HB3  A SER   A 1 166 ? 0.176  -12.160 0.518   0.42 24.43 ?  166 SER   A HB3  1 
ATOM   4326 H HB3  B SER   A 1 166 ? 0.101  -12.458 1.406   0.58 36.16 ?  166 SER   A HB3  1 
ATOM   4327 H HG   A SER   A 1 166 ? 0.842  -10.511 2.474   0.42 26.26 ?  166 SER   A HG   1 
ATOM   4328 H HG   B SER   A 1 166 ? 1.387  -10.619 2.805   0.58 37.73 ?  166 SER   A HG   1 
ATOM   4329 N N    A SER   A 1 167 ? 3.482  -13.108 -0.348  0.42 18.53 ?  167 SER   A N    1 
ATOM   4330 N N    B SER   A 1 167 ? 3.687  -13.974 0.248   0.58 33.33 ?  167 SER   A N    1 
ATOM   4331 C CA   A SER   A 1 167 ? 3.959  -13.838 -1.512  0.42 19.06 ?  167 SER   A CA   1 
ATOM   4332 C CA   B SER   A 1 167 ? 4.153  -14.503 -1.023  0.58 35.80 ?  167 SER   A CA   1 
ATOM   4333 C C    A SER   A 1 167 ? 5.137  -14.753 -1.210  0.42 18.94 ?  167 SER   A C    1 
ATOM   4334 C C    B SER   A 1 167 ? 4.993  -15.762 -0.832  0.58 38.15 ?  167 SER   A C    1 
ATOM   4335 O O    A SER   A 1 167 ? 5.679  -15.355 -2.140  0.42 18.56 ?  167 SER   A O    1 
ATOM   4336 O O    B SER   A 1 167 ? 5.502  -16.053 0.253   0.58 37.75 ?  167 SER   A O    1 
ATOM   4337 C CB   A SER   A 1 167 ? 4.345  -12.864 -2.632  0.42 19.06 ?  167 SER   A CB   1 
ATOM   4338 C CB   B SER   A 1 167 ? 5.017  -13.479 -1.768  0.58 36.10 ?  167 SER   A CB   1 
ATOM   4339 O OG   A SER   A 1 167 ? 5.377  -11.993 -2.212  0.42 19.12 ?  167 SER   A OG   1 
ATOM   4340 O OG   B SER   A 1 167 ? 4.277  -12.322 -2.108  0.58 36.38 ?  167 SER   A OG   1 
ATOM   4341 H H    A SER   A 1 167 ? 3.957  -12.410 -0.157  0.42 22.25 ?  167 SER   A H    1 
ATOM   4342 H H    B SER   A 1 167 ? 4.303  -13.890 0.840   0.58 40.01 ?  167 SER   A H    1 
ATOM   4343 H HA   A SER   A 1 167 ? 3.244  -14.392 -1.846  0.42 22.89 ?  167 SER   A HA   1 
ATOM   4344 H HA   B SER   A 1 167 ? 3.382  -14.710 -1.578  0.58 42.98 ?  167 SER   A HA   1 
ATOM   4345 H HB2  A SER   A 1 167 ? 4.654  -13.370 -3.402  0.42 22.89 ?  167 SER   A HB2  1 
ATOM   4346 H HB2  B SER   A 1 167 ? 5.755  -13.229 -1.191  0.58 43.34 ?  167 SER   A HB2  1 
ATOM   4347 H HB3  A SER   A 1 167 ? 3.564  -12.340 -2.876  0.42 22.89 ?  167 SER   A HB3  1 
ATOM   4348 H HB3  B SER   A 1 167 ? 5.356  -13.890 -2.579  0.58 43.34 ?  167 SER   A HB3  1 
ATOM   4349 H HG   A SER   A 1 167 ? 5.118  -11.536 -1.557  0.42 22.97 ?  167 SER   A HG   1 
ATOM   4350 H HG   B SER   A 1 167 ? 3.917  -12.003 -1.420  0.58 43.68 ?  167 SER   A HG   1 
ATOM   4351 N N    A PHE   A 1 168 ? 5.551  -14.876 0.050   0.42 19.07 ?  168 PHE   A N    1 
ATOM   4352 N N    B PHE   A 1 168 ? 5.123  -16.488 -1.943  0.58 41.15 ?  168 PHE   A N    1 
ATOM   4353 C CA   A PHE   A 1 168 ? 6.737  -15.663 0.364   0.42 20.15 ?  168 PHE   A CA   1 
ATOM   4354 C CA   B PHE   A 1 168 ? 6.008  -17.629 -2.180  0.58 44.37 ?  168 PHE   A CA   1 
ATOM   4355 C C    A PHE   A 1 168 ? 6.426  -17.149 0.287   0.42 22.97 ?  168 PHE   A C    1 
ATOM   4356 C C    B PHE   A 1 168 ? 5.242  -18.941 -2.334  0.58 46.18 ?  168 PHE   A C    1 
ATOM   4357 O O    A PHE   A 1 168 ? 5.444  -17.622 0.867   0.42 24.12 ?  168 PHE   A O    1 
ATOM   4358 O O    B PHE   A 1 168 ? 4.373  -19.050 -3.204  0.58 47.07 ?  168 PHE   A O    1 
ATOM   4359 C CB   A PHE   A 1 168 ? 7.281  -15.334 1.752   0.42 19.00 ?  168 PHE   A CB   1 
ATOM   4360 C CB   B PHE   A 1 168 ? 7.186  -17.752 -1.204  0.58 45.36 ?  168 PHE   A CB   1 
ATOM   4361 C CG   A PHE   A 1 168 ? 8.540  -16.088 2.084   0.42 17.37 ?  168 PHE   A CG   1 
ATOM   4362 C CG   B PHE   A 1 168 ? 8.355  -18.505 -1.787  0.58 46.17 ?  168 PHE   A CG   1 
ATOM   4363 C CD1  A PHE   A 1 168 ? 9.718  -15.802 1.418   0.42 16.51 ?  168 PHE   A CD1  1 
ATOM   4364 C CD1  B PHE   A 1 168 ? 9.169  -17.906 -2.733  0.58 46.44 ?  168 PHE   A CD1  1 
ATOM   4365 C CD2  A PHE   A 1 168 ? 8.550  -17.096 3.038   0.42 16.07 ?  168 PHE   A CD2  1 
ATOM   4366 C CD2  B PHE   A 1 168 ? 8.625  -19.813 -1.416  0.58 46.53 ?  168 PHE   A CD2  1 
ATOM   4367 C CE1  A PHE   A 1 168 ? 10.879 -16.493 1.701   0.42 16.40 ?  168 PHE   A CE1  1 
ATOM   4368 C CE1  B PHE   A 1 168 ? 10.238 -18.592 -3.285  0.58 46.76 ?  168 PHE   A CE1  1 
ATOM   4369 C CE2  A PHE   A 1 168 ? 9.715  -17.788 3.326   0.42 16.24 ?  168 PHE   A CE2  1 
ATOM   4370 C CE2  B PHE   A 1 168 ? 9.694  -20.501 -1.969  0.58 46.69 ?  168 PHE   A CE2  1 
ATOM   4371 C CZ   A PHE   A 1 168 ? 10.874 -17.485 2.656   0.42 16.52 ?  168 PHE   A CZ   1 
ATOM   4372 C CZ   B PHE   A 1 168 ? 10.499 -19.886 -2.905  0.58 46.85 ?  168 PHE   A CZ   1 
ATOM   4373 H H    A PHE   A 1 168 ? 5.170  -14.517 0.730   0.42 22.89 ?  168 PHE   A H    1 
ATOM   4374 H H    B PHE   A 1 168 ? 4.671  -16.304 -2.640  0.58 49.40 ?  168 PHE   A H    1 
ATOM   4375 H HA   A PHE   A 1 168 ? 7.431  -15.467 -0.284  0.42 24.20 ?  168 PHE   A HA   1 
ATOM   4376 H HA   B PHE   A 1 168 ? 6.416  -17.457 -3.036  0.58 53.26 ?  168 PHE   A HA   1 
ATOM   4377 H HB2  A PHE   A 1 168 ? 7.483  -14.386 1.796   0.42 22.82 ?  168 PHE   A HB2  1 
ATOM   4378 H HB2  B PHE   A 1 168 ? 7.506  -16.868 -0.991  0.58 54.45 ?  168 PHE   A HB2  1 
ATOM   4379 H HB3  A PHE   A 1 168 ? 6.615  -15.563 2.417   0.42 22.82 ?  168 PHE   A HB3  1 
ATOM   4380 H HB3  B PHE   A 1 168 ? 6.914  -18.204 -0.391  0.58 54.45 ?  168 PHE   A HB3  1 
ATOM   4381 H HD1  A PHE   A 1 168 ? 9.734  -15.134 0.771   0.42 19.82 ?  168 PHE   A HD1  1 
ATOM   4382 H HD1  B PHE   A 1 168 ? 8.996  -17.030 -3.000  0.58 55.74 ?  168 PHE   A HD1  1 
ATOM   4383 H HD2  A PHE   A 1 168 ? 7.768  -17.304 3.494   0.42 19.30 ?  168 PHE   A HD2  1 
ATOM   4384 H HD2  B PHE   A 1 168 ? 8.088  -20.235 -0.789  0.58 55.86 ?  168 PHE   A HD2  1 
ATOM   4385 H HE1  A PHE   A 1 168 ? 11.667 -16.289 1.249   0.42 19.70 ?  168 PHE   A HE1  1 
ATOM   4386 H HE1  B PHE   A 1 168 ? 10.780 -18.177 -3.921  0.58 56.13 ?  168 PHE   A HE1  1 
ATOM   4387 H HE2  A PHE   A 1 168 ? 9.710  -18.459 3.970   0.42 19.50 ?  168 PHE   A HE2  1 
ATOM   4388 H HE2  B PHE   A 1 168 ? 9.870  -21.377 -1.712  0.58 56.04 ?  168 PHE   A HE2  1 
ATOM   4389 H HZ   A PHE   A 1 168 ? 11.657 -17.952 2.849   0.42 19.84 ?  168 PHE   A HZ   1 
ATOM   4390 H HZ   B PHE   A 1 168 ? 11.217 -20.343 -3.281  0.58 56.24 ?  168 PHE   A HZ   1 
ATOM   4391 N N    A LEU   A 1 169 ? 7.282  -17.884 -0.414  0.42 25.09 ?  169 LEU   A N    1 
ATOM   4392 N N    B LEU   A 1 169 ? 5.554  -19.942 -1.517  0.58 46.70 ?  169 LEU   A N    1 
ATOM   4393 C CA   A LEU   A 1 169 ? 7.114  -19.318 -0.559  0.42 27.78 ?  169 LEU   A CA   1 
ATOM   4394 C CA   B LEU   A 1 169 ? 5.096  -21.300 -1.779  0.58 46.88 ?  169 LEU   A CA   1 
ATOM   4395 C C    A LEU   A 1 169 ? 7.976  -20.044 0.466   0.42 27.60 ?  169 LEU   A C    1 
ATOM   4396 C C    B LEU   A 1 169 ? 5.326  -22.179 -0.556  0.58 46.39 ?  169 LEU   A C    1 
ATOM   4397 O O    A LEU   A 1 169 ? 7.473  -20.508 1.489   0.42 27.45 ?  169 LEU   A O    1 
ATOM   4398 O O    B LEU   A 1 169 ? 4.828  -21.890 0.531   0.58 46.26 ?  169 LEU   A O    1 
ATOM   4399 C CB   A LEU   A 1 169 ? 7.474  -19.746 -1.985  0.42 30.20 ?  169 LEU   A CB   1 
ATOM   4400 C CB   B LEU   A 1 169 ? 5.848  -21.877 -2.984  0.58 47.34 ?  169 LEU   A CB   1 
ATOM   4401 C CG   A LEU   A 1 169 ? 7.098  -21.170 -2.394  0.42 32.33 ?  169 LEU   A CG   1 
ATOM   4402 C CG   B LEU   A 1 169 ? 5.142  -22.901 -3.877  0.58 47.68 ?  169 LEU   A CG   1 
ATOM   4403 C CD1  A LEU   A 1 169 ? 5.648  -21.461 -2.050  0.42 33.16 ?  169 LEU   A CD1  1 
ATOM   4404 C CD1  B LEU   A 1 169 ? 5.469  -22.619 -5.336  0.58 47.71 ?  169 LEU   A CD1  1 
ATOM   4405 C CD2  A LEU   A 1 169 ? 7.343  -21.367 -3.882  0.42 33.10 ?  169 LEU   A CD2  1 
ATOM   4406 C CD2  B LEU   A 1 169 ? 5.546  -24.319 -3.510  0.58 47.79 ?  169 LEU   A CD2  1 
ATOM   4407 O OXT  A LEU   A 1 169 ? 9.191  -20.168 0.312   0.42 27.11 -1 169 LEU   A OXT  1 
ATOM   4408 O OXT  B LEU   A 1 169 ? 6.019  -23.194 -0.621  0.58 46.19 -1 169 LEU   A OXT  1 
ATOM   4409 H H    A LEU   A 1 169 ? 7.972  -17.570 -0.824  0.42 30.12 ?  169 LEU   A H    1 
ATOM   4410 H H    B LEU   A 1 169 ? 6.007  -19.863 -0.793  0.58 56.06 ?  169 LEU   A H    1 
ATOM   4411 H HA   A LEU   A 1 169 ? 6.191  -19.547 -0.386  0.42 33.35 ?  169 LEU   A HA   1 
ATOM   4412 H HA   B LEU   A 1 169 ? 4.149  -21.285 -1.983  0.58 56.28 ?  169 LEU   A HA   1 
ATOM   4413 H HB2  A LEU   A 1 169 ? 7.026  -19.146 -2.603  0.42 36.26 ?  169 LEU   A HB2  1 
ATOM   4414 H HB2  B LEU   A 1 169 ? 6.103  -21.142 -3.557  0.58 56.83 ?  169 LEU   A HB2  1 
ATOM   4415 H HB3  A LEU   A 1 169 ? 8.433  -19.661 -2.095  0.42 36.26 ?  169 LEU   A HB3  1 
ATOM   4416 H HB3  B LEU   A 1 169 ? 6.649  -22.308 -2.651  0.58 56.83 ?  169 LEU   A HB3  1 
ATOM   4417 H HG   A LEU   A 1 169 ? 7.657  -21.799 -1.911  0.42 38.81 ?  169 LEU   A HG   1 
ATOM   4418 H HG   B LEU   A 1 169 ? 4.183  -22.820 -3.762  0.58 57.24 ?  169 LEU   A HG   1 
ATOM   4419 H HD11 A LEU   A 1 169 ? 5.367  -22.260 -2.520  0.42 39.81 ?  169 LEU   A HD11 1 
ATOM   4420 H HD11 B LEU   A 1 169 ? 5.052  -23.296 -5.890  0.58 57.27 ?  169 LEU   A HD11 1 
ATOM   4421 H HD12 A LEU   A 1 169 ? 5.572  -21.596 -1.092  0.42 39.81 ?  169 LEU   A HD12 1 
ATOM   4422 H HD12 B LEU   A 1 169 ? 5.127  -21.742 -5.572  0.58 57.27 ?  169 LEU   A HD12 1 
ATOM   4423 H HD13 A LEU   A 1 169 ? 5.103  -20.707 -2.323  0.42 39.81 ?  169 LEU   A HD13 1 
ATOM   4424 H HD13 B LEU   A 1 169 ? 6.432  -22.641 -5.454  0.58 57.27 ?  169 LEU   A HD13 1 
ATOM   4425 H HD21 A LEU   A 1 169 ? 7.109  -22.277 -4.123  0.42 39.74 ?  169 LEU   A HD21 1 
ATOM   4426 H HD21 B LEU   A 1 169 ? 4.969  -24.943 -3.978  0.58 57.37 ?  169 LEU   A HD21 1 
ATOM   4427 H HD22 A LEU   A 1 169 ? 6.792  -20.741 -4.377  0.42 39.74 ?  169 LEU   A HD22 1 
ATOM   4428 H HD22 B LEU   A 1 169 ? 6.469  -24.463 -3.774  0.58 57.37 ?  169 LEU   A HD22 1 
ATOM   4429 H HD23 A LEU   A 1 169 ? 8.280  -21.205 -4.072  0.42 39.74 ?  169 LEU   A HD23 1 
ATOM   4430 H HD23 B LEU   A 1 169 ? 5.454  -24.436 -2.553  0.58 57.37 ?  169 LEU   A HD23 1 
ATOM   4431 N N    A SER   B 1 1   ? 50.944 -9.232  -23.701 0.42 23.73 ?  1   SER   B N    1 
ATOM   4432 N N    B SER   B 1 1   ? 50.974 -9.717  -23.577 0.58 19.07 ?  1   SER   B N    1 
ATOM   4433 C CA   A SER   B 1 1   ? 51.484 -10.314 -22.850 0.42 24.04 ?  1   SER   B CA   1 
ATOM   4434 C CA   B SER   B 1 1   ? 51.385 -10.649 -22.498 0.58 18.37 ?  1   SER   B CA   1 
ATOM   4435 C C    A SER   B 1 1   ? 50.424 -11.384 -22.632 0.42 23.61 ?  1   SER   B C    1 
ATOM   4436 C C    B SER   B 1 1   ? 50.408 -11.820 -22.347 0.58 16.62 ?  1   SER   B C    1 
ATOM   4437 O O    A SER   B 1 1   ? 49.255 -11.206 -22.993 0.42 23.47 ?  1   SER   B O    1 
ATOM   4438 O O    B SER   B 1 1   ? 49.184 -11.679 -22.483 0.58 18.18 ?  1   SER   B O    1 
ATOM   4439 C CB   A SER   B 1 1   ? 51.961 -9.762  -21.509 0.42 24.53 ?  1   SER   B CB   1 
ATOM   4440 C CB   B SER   B 1 1   ? 51.512 -9.898  -21.176 0.58 20.21 ?  1   SER   B CB   1 
ATOM   4441 O OG   A SER   B 1 1   ? 50.913 -9.750  -20.556 0.42 25.47 ?  1   SER   B OG   1 
ATOM   4442 O OG   B SER   B 1 1   ? 50.243 -9.442  -20.755 0.58 22.17 ?  1   SER   B OG   1 
ATOM   4443 H H1   A SER   B 1 1   ? 50.763 -9.562  -24.507 0.42 28.49 ?  1   SER   B H1   1 
ATOM   4444 H H1   B SER   B 1 1   ? 51.565 -9.056  -23.629 0.58 22.90 ?  1   SER   B H1   1 
ATOM   4445 H H2   A SER   B 1 1   ? 50.205 -8.915  -23.331 0.42 28.49 ?  1   SER   B H2   1 
ATOM   4446 H H2   B SER   B 1 1   ? 50.953 -10.162 -24.345 0.58 22.90 ?  1   SER   B H2   1 
ATOM   4447 H H3   A SER   B 1 1   ? 51.553 -8.591  -23.768 0.42 28.49 ?  1   SER   B H3   1 
ATOM   4448 H H3   B SER   B 1 1   ? 50.173 -9.396  -23.387 0.58 22.90 ?  1   SER   B H3   1 
ATOM   4449 H HA   A SER   B 1 1   ? 52.237 -10.712 -23.306 0.42 28.87 ?  1   SER   B HA   1 
ATOM   4450 H HA   B SER   B 1 1   ? 52.260 -11.000 -22.727 0.58 22.06 ?  1   SER   B HA   1 
ATOM   4451 H HB2  A SER   B 1 1   ? 52.668 -10.329 -21.176 0.42 29.45 ?  1   SER   B HB2  1 
ATOM   4452 H HB2  B SER   B 1 1   ? 51.853 -10.502 -20.504 0.58 24.27 ?  1   SER   B HB2  1 
ATOM   4453 H HB3  A SER   B 1 1   ? 52.294 -8.858  -21.643 0.42 29.45 ?  1   SER   B HB3  1 
ATOM   4454 H HB3  B SER   B 1 1   ? 52.122 -9.146  -21.290 0.58 24.27 ?  1   SER   B HB3  1 
ATOM   4455 H HG   A SER   B 1 1   ? 51.190 -9.427  -19.833 0.42 30.58 ?  1   SER   B HG   1 
ATOM   4456 H HG   B SER   B 1 1   ? 50.320 -8.998  -20.042 0.58 26.62 ?  1   SER   B HG   1 
ATOM   4457 N N    A MET   B 1 2   ? 50.850 -12.498 -22.042 0.42 23.04 ?  2   MET   B N    1 
ATOM   4458 N N    B MET   B 1 2   ? 50.964 -12.989 -22.068 0.58 14.57 ?  2   MET   B N    1 
ATOM   4459 C CA   A MET   B 1 2   ? 50.020 -13.683 -21.863 0.42 22.74 ?  2   MET   B CA   1 
ATOM   4460 C CA   B MET   B 1 2   ? 50.190 -14.227 -22.062 0.58 14.51 ?  2   MET   B CA   1 
ATOM   4461 C C    A MET   B 1 2   ? 49.714 -13.850 -20.379 0.42 20.22 ?  2   MET   B C    1 
ATOM   4462 C C    B MET   B 1 2   ? 49.797 -14.602 -20.635 0.58 15.30 ?  2   MET   B C    1 
ATOM   4463 O O    A MET   B 1 2   ? 50.612 -14.152 -19.587 0.42 19.83 ?  2   MET   B O    1 
ATOM   4464 O O    B MET   B 1 2   ? 50.456 -15.396 -19.968 0.58 18.13 ?  2   MET   B O    1 
ATOM   4465 C CB   A MET   B 1 2   ? 50.754 -14.903 -22.413 0.42 26.09 ?  2   MET   B CB   1 
ATOM   4466 C CB   B MET   B 1 2   ? 50.974 -15.323 -22.749 0.58 16.22 ?  2   MET   B CB   1 
ATOM   4467 C CG   A MET   B 1 2   ? 49.889 -16.143 -22.571 0.42 29.61 ?  2   MET   B CG   1 
ATOM   4468 C CG   B MET   B 1 2   ? 50.143 -16.560 -23.055 0.58 18.60 ?  2   MET   B CG   1 
ATOM   4469 S SD   A MET   B 1 2   ? 50.729 -17.405 -23.538 0.42 33.04 ?  2   MET   B SD   1 
ATOM   4470 S SD   B MET   B 1 2   ? 50.887 -17.597 -24.324 0.58 20.83 ?  2   MET   B SD   1 
ATOM   4471 C CE   A MET   B 1 2   ? 51.221 -16.438 -24.960 0.42 33.76 ?  2   MET   B CE   1 
ATOM   4472 C CE   B MET   B 1 2   ? 52.478 -16.789 -24.455 0.58 21.97 ?  2   MET   B CE   1 
ATOM   4473 H H    A MET   B 1 2   ? 51.653 -12.600 -21.736 0.42 27.66 ?  2   MET   B H    1 
ATOM   4474 H H    B MET   B 1 2   ? 51.809 -13.095 -21.889 0.58 17.50 ?  2   MET   B H    1 
ATOM   4475 H HA   A MET   B 1 2   ? 49.199 -13.585 -22.361 0.42 27.31 ?  2   MET   B HA   1 
ATOM   4476 H HA   B MET   B 1 2   ? 49.393 -14.084 -22.584 0.58 17.43 ?  2   MET   B HA   1 
ATOM   4477 H HB2  A MET   B 1 2   ? 51.113 -14.665 -23.282 0.42 31.33 ?  2   MET   B HB2  1 
ATOM   4478 H HB2  B MET   B 1 2   ? 51.280 -14.936 -23.584 0.58 19.48 ?  2   MET   B HB2  1 
ATOM   4479 H HB3  A MET   B 1 2   ? 51.481 -15.144 -21.821 0.42 31.33 ?  2   MET   B HB3  1 
ATOM   4480 H HB3  B MET   B 1 2   ? 51.727 -15.588 -22.190 0.58 19.48 ?  2   MET   B HB3  1 
ATOM   4481 H HG2  A MET   B 1 2   ? 49.696 -16.517 -21.696 0.42 35.55 ?  2   MET   B HG2  1 
ATOM   4482 H HG2  B MET   B 1 2   ? 50.048 -17.093 -22.248 0.58 22.33 ?  2   MET   B HG2  1 
ATOM   4483 H HG3  A MET   B 1 2   ? 49.065 -15.913 -23.028 0.42 35.55 ?  2   MET   B HG3  1 
ATOM   4484 H HG3  B MET   B 1 2   ? 49.268 -16.280 -23.370 0.58 22.33 ?  2   MET   B HG3  1 
ATOM   4485 H HE1  A MET   B 1 2   ? 51.340 -17.023 -25.717 0.42 40.53 ?  2   MET   B HE1  1 
ATOM   4486 H HE1  B MET   B 1 2   ? 53.053 -17.389 -24.910 0.58 26.38 ?  2   MET   B HE1  1 
ATOM   4487 H HE2  A MET   B 1 2   ? 50.525 -15.786 -25.146 0.42 40.53 ?  2   MET   B HE2  1 
ATOM   4488 H HE2  B MET   B 1 2   ? 52.389 -15.954 -24.961 0.58 26.38 ?  2   MET   B HE2  1 
ATOM   4489 H HE3  A MET   B 1 2   ? 52.053 -15.981 -24.754 0.42 40.53 ?  2   MET   B HE3  1 
ATOM   4490 H HE3  B MET   B 1 2   ? 52.860 -16.619 -23.577 0.58 26.38 ?  2   MET   B HE3  1 
ATOM   4491 N N    A VAL   B 1 3   ? 48.448 -13.660 -20.008 0.42 17.67 ?  3   VAL   B N    1 
ATOM   4492 N N    B VAL   B 1 3   ? 48.680 -14.052 -20.188 0.58 13.95 ?  3   VAL   B N    1 
ATOM   4493 C CA   A VAL   B 1 3   ? 47.983 -13.864 -18.641 0.42 16.74 ?  3   VAL   B CA   1 
ATOM   4494 C CA   B VAL   B 1 3   ? 48.215 -14.216 -18.819 0.58 14.21 ?  3   VAL   B CA   1 
ATOM   4495 C C    A VAL   B 1 3   ? 46.744 -14.749 -18.649 0.42 15.87 ?  3   VAL   B C    1 
ATOM   4496 C C    B VAL   B 1 3   ? 46.941 -15.054 -18.797 0.58 12.88 ?  3   VAL   B C    1 
ATOM   4497 O O    A VAL   B 1 3   ? 45.918 -14.689 -19.563 0.42 16.58 ?  3   VAL   B O    1 
ATOM   4498 O O    B VAL   B 1 3   ? 46.236 -15.197 -19.803 0.58 11.41 ?  3   VAL   B O    1 
ATOM   4499 C CB   A VAL   B 1 3   ? 47.693 -12.537 -17.904 0.42 17.39 ?  3   VAL   B CB   1 
ATOM   4500 C CB   B VAL   B 1 3   ? 47.968 -12.853 -18.156 0.58 15.03 ?  3   VAL   B CB   1 
ATOM   4501 C CG1  A VAL   B 1 3   ? 48.961 -11.696 -17.800 0.42 17.93 ?  3   VAL   B CG1  1 
ATOM   4502 C CG1  B VAL   B 1 3   ? 49.254 -12.048 -18.125 0.58 16.43 ?  3   VAL   B CG1  1 
ATOM   4503 C CG2  A VAL   B 1 3   ? 46.572 -11.767 -18.593 0.42 17.44 ?  3   VAL   B CG2  1 
ATOM   4504 C CG2  B VAL   B 1 3   ? 46.861 -12.104 -18.896 0.58 14.91 ?  3   VAL   B CG2  1 
ATOM   4505 H H    A VAL   B 1 3   ? 47.826 -13.414 -20.555 0.42 21.22 ?  3   VAL   B H    1 
ATOM   4506 H H    B VAL   B 1 3   ? 48.161 -13.582 -20.687 0.58 16.75 ?  3   VAL   B H    1 
ATOM   4507 H HA   A VAL   B 1 3   ? 48.667 -14.331 -18.151 0.42 20.10 ?  3   VAL   B HA   1 
ATOM   4508 H HA   B VAL   B 1 3   ? 48.902 -14.693 -18.317 0.58 17.07 ?  3   VAL   B HA   1 
ATOM   4509 H HB   A VAL   B 1 3   ? 47.398 -12.743 -17.006 0.42 20.89 ?  3   VAL   B HB   1 
ATOM   4510 H HB   B VAL   B 1 3   ? 47.683 -13.011 -17.246 0.58 18.05 ?  3   VAL   B HB   1 
ATOM   4511 H HG11 A VAL   B 1 3   ? 48.757 -10.878 -17.323 0.42 21.53 ?  3   VAL   B HG11 1 
ATOM   4512 H HG11 B VAL   B 1 3   ? 49.086 -11.225 -17.650 0.58 19.73 ?  3   VAL   B HG11 1 
ATOM   4513 H HG12 A VAL   B 1 3   ? 49.634 -12.203 -17.322 0.42 21.53 ?  3   VAL   B HG12 1 
ATOM   4514 H HG12 B VAL   B 1 3   ? 49.937 -12.566 -17.670 0.58 19.73 ?  3   VAL   B HG12 1 
ATOM   4515 H HG13 A VAL   B 1 3   ? 49.276 -11.489 -18.695 0.42 21.53 ?  3   VAL   B HG13 1 
ATOM   4516 H HG13 B VAL   B 1 3   ? 49.529 -11.863 -19.035 0.58 19.73 ?  3   VAL   B HG13 1 
ATOM   4517 H HG21 A VAL   B 1 3   ? 46.508 -10.884 -18.198 0.42 20.94 ?  3   VAL   B HG21 1 
ATOM   4518 H HG21 B VAL   B 1 3   ? 46.798 -11.213 -18.534 0.58 17.91 ?  3   VAL   B HG21 1 
ATOM   4519 H HG22 A VAL   B 1 3   ? 46.771 -11.692 -19.540 0.42 20.94 ?  3   VAL   B HG22 1 
ATOM   4520 H HG22 B VAL   B 1 3   ? 47.077 -12.064 -19.843 0.58 17.91 ?  3   VAL   B HG22 1 
ATOM   4521 H HG23 A VAL   B 1 3   ? 45.734 -12.244 -18.471 0.42 20.94 ?  3   VAL   B HG23 1 
ATOM   4522 H HG23 B VAL   B 1 3   ? 46.019 -12.574 -18.774 0.58 17.91 ?  3   VAL   B HG23 1 
ATOM   4523 N N    . ASN   B 1 4   ? 46.621 -15.577 -17.615 1.00 13.83 ?  4   ASN   B N    1 
ATOM   4524 C CA   . ASN   B 1 4   ? 45.470 -16.458 -17.446 1.00 13.86 ?  4   ASN   B CA   1 
ATOM   4525 C C    . ASN   B 1 4   ? 45.388 -17.450 -18.600 1.00 14.07 ?  4   ASN   B C    1 
ATOM   4526 O O    . ASN   B 1 4   ? 44.331 -17.664 -19.186 1.00 14.68 ?  4   ASN   B O    1 
ATOM   4527 C CB   . ASN   B 1 4   ? 44.163 -15.672 -17.291 1.00 13.50 ?  4   ASN   B CB   1 
ATOM   4528 C CG   . ASN   B 1 4   ? 44.119 -14.876 -15.998 1.00 13.21 ?  4   ASN   B CG   1 
ATOM   4529 O OD1  . ASN   B 1 4   ? 44.389 -15.396 -14.922 1.00 13.49 ?  4   ASN   B OD1  1 
ATOM   4530 N ND2  . ASN   B 1 4   ? 43.796 -13.590 -16.108 1.00 14.66 ?  4   ASN   B ND2  1 
ATOM   4531 H H    A ASN   B 1 4   ? 47.214 -15.656 -17.002 0.42 16.62 ?  4   ASN   B H    1 
ATOM   4532 H H    B ASN   B 1 4   ? 47.066 -15.440 -16.900 0.58 16.62 ?  4   ASN   B H    1 
ATOM   4533 H HA   . ASN   B 1 4   ? 45.604 -16.972 -16.635 1.00 16.65 ?  4   ASN   B HA   1 
ATOM   4534 H HB2  . ASN   B 1 4   ? 44.067 -15.058 -18.034 1.00 16.22 ?  4   ASN   B HB2  1 
ATOM   4535 H HB3  . ASN   B 1 4   ? 43.418 -16.301 -17.287 1.00 16.22 ?  4   ASN   B HB3  1 
ATOM   4536 H HD21 . ASN   B 1 4   ? 43.751 -13.092 -15.408 1.00 17.61 ?  4   ASN   B HD21 1 
ATOM   4537 H HD22 . ASN   B 1 4   ? 43.615 -13.252 -16.882 1.00 17.61 ?  4   ASN   B HD22 1 
ATOM   4538 N N    . SER   B 1 5   ? 46.532 -18.057 -18.931 1.00 14.65 ?  5   SER   B N    1 
ATOM   4539 C CA   . SER   B 1 5   ? 46.632 -18.977 -20.064 1.00 16.61 ?  5   SER   B CA   1 
ATOM   4540 C C    . SER   B 1 5   ? 46.632 -20.386 -19.488 1.00 18.58 ?  5   SER   B C    1 
ATOM   4541 O O    . SER   B 1 5   ? 47.673 -20.980 -19.222 1.00 21.03 ?  5   SER   B O    1 
ATOM   4542 C CB   . SER   B 1 5   ? 47.895 -18.687 -20.874 1.00 19.24 ?  5   SER   B CB   1 
ATOM   4543 O OG   . SER   B 1 5   ? 49.060 -18.890 -20.096 1.00 24.49 ?  5   SER   B OG   1 
ATOM   4544 H H    . SER   B 1 5   ? 47.276 -17.965 -18.506 1.00 17.59 ?  5   SER   B H    1 
ATOM   4545 H HA   . SER   B 1 5   ? 45.862 -18.882 -20.641 1.00 19.95 ?  5   SER   B HA   1 
ATOM   4546 H HB2  . SER   B 1 5   ? 47.915 -19.282 -21.646 1.00 23.11 ?  5   SER   B HB2  1 
ATOM   4547 H HB3  . SER   B 1 5   ? 47.864 -17.766 -21.172 1.00 23.11 ?  5   SER   B HB3  1 
ATOM   4548 H HG   . SER   B 1 5   ? 49.116 -19.698 -19.872 1.00 29.40 ?  5   SER   B HG   1 
ATOM   4549 N N    . PHE   B 1 6   ? 45.430 -20.881 -19.212 1.00 20.77 ?  6   PHE   B N    1 
ATOM   4550 C CA   . PHE   B 1 6   ? 45.226 -22.204 -18.638 1.00 20.32 ?  6   PHE   B CA   1 
ATOM   4551 C C    . PHE   B 1 6   ? 45.140 -23.219 -19.768 1.00 25.51 ?  6   PHE   B C    1 
ATOM   4552 O O    . PHE   B 1 6   ? 44.377 -23.032 -20.720 1.00 28.82 ?  6   PHE   B O    1 
ATOM   4553 C CB   . PHE   B 1 6   ? 43.934 -22.233 -17.816 1.00 18.77 ?  6   PHE   B CB   1 
ATOM   4554 C CG   . PHE   B 1 6   ? 43.953 -21.338 -16.606 1.00 17.41 ?  6   PHE   B CG   1 
ATOM   4555 C CD1  . PHE   B 1 6   ? 44.450 -21.791 -15.398 1.00 15.80 ?  6   PHE   B CD1  1 
ATOM   4556 C CD2  . PHE   B 1 6   ? 43.479 -20.036 -16.682 1.00 17.25 ?  6   PHE   B CD2  1 
ATOM   4557 C CE1  . PHE   B 1 6   ? 44.461 -20.962 -14.282 1.00 14.88 ?  6   PHE   B CE1  1 
ATOM   4558 C CE2  . PHE   B 1 6   ? 43.498 -19.202 -15.577 1.00 17.12 ?  6   PHE   B CE2  1 
ATOM   4559 C CZ   . PHE   B 1 6   ? 43.993 -19.659 -14.379 1.00 15.33 ?  6   PHE   B CZ   1 
ATOM   4560 H H    . PHE   B 1 6   ? 44.695 -20.458 -19.354 1.00 24.94 ?  6   PHE   B H    1 
ATOM   4561 H HA   . PHE   B 1 6   ? 45.964 -22.439 -18.060 1.00 24.40 ?  6   PHE   B HA   1 
ATOM   4562 H HB2  . PHE   B 1 6   ? 43.194 -21.947 -18.379 1.00 22.54 ?  6   PHE   B HB2  1 
ATOM   4563 H HB3  . PHE   B 1 6   ? 43.773 -23.140 -17.507 1.00 22.54 ?  6   PHE   B HB3  1 
ATOM   4564 H HD1  . PHE   B 1 6   ? 44.772 -22.665 -15.331 1.00 18.98 ?  6   PHE   B HD1  1 
ATOM   4565 H HD2  . PHE   B 1 6   ? 43.142 -19.722 -17.486 1.00 20.72 ?  6   PHE   B HD2  1 
ATOM   4566 H HE1  . PHE   B 1 6   ? 44.802 -21.276 -13.472 1.00 17.88 ?  6   PHE   B HE1  1 
ATOM   4567 H HE2  . PHE   B 1 6   ? 43.169 -18.338 -15.645 1.00 20.56 ?  6   PHE   B HE2  1 
ATOM   4568 H HZ   . PHE   B 1 6   ? 43.999 -19.108 -13.629 1.00 18.41 ?  6   PHE   B HZ   1 
ATOM   4569 N N    A SER   B 1 7   ? 45.929 -24.285 -19.664 0.42 26.94 ?  7   SER   B N    1 
ATOM   4570 N N    B SER   B 1 7   ? 45.921 -24.289 -19.661 0.58 26.30 ?  7   SER   B N    1 
ATOM   4571 C CA   A SER   B 1 7   ? 46.014 -25.290 -20.713 0.42 29.74 ?  7   SER   B CA   1 
ATOM   4572 C CA   B SER   B 1 7   ? 46.005 -25.287 -20.716 0.58 29.63 ?  7   SER   B CA   1 
ATOM   4573 C C    A SER   B 1 7   ? 45.918 -26.685 -20.114 0.42 29.52 ?  7   SER   B C    1 
ATOM   4574 C C    B SER   B 1 7   ? 45.928 -26.687 -20.125 0.58 29.30 ?  7   SER   B C    1 
ATOM   4575 O O    A SER   B 1 7   ? 46.524 -26.975 -19.078 0.42 30.24 ?  7   SER   B O    1 
ATOM   4576 O O    B SER   B 1 7   ? 46.559 -26.983 -19.105 0.58 30.11 ?  7   SER   B O    1 
ATOM   4577 C CB   A SER   B 1 7   ? 47.323 -25.149 -21.502 0.42 32.18 ?  7   SER   B CB   1 
ATOM   4578 C CB   B SER   B 1 7   ? 47.307 -25.122 -21.512 0.58 32.72 ?  7   SER   B CB   1 
ATOM   4579 O OG   A SER   B 1 7   ? 47.351 -26.042 -22.603 0.42 33.63 ?  7   SER   B OG   1 
ATOM   4580 O OG   B SER   B 1 7   ? 47.237 -25.811 -22.747 0.58 34.58 ?  7   SER   B OG   1 
ATOM   4581 H H    A SER   B 1 7   ? 46.434 -24.444 -18.985 0.42 32.35 ?  7   SER   B H    1 
ATOM   4582 H H    B SER   B 1 7   ? 46.419 -24.458 -18.978 0.58 31.58 ?  7   SER   B H    1 
ATOM   4583 H HA   A SER   B 1 7   ? 45.277 -25.173 -21.328 0.42 35.71 ?  7   SER   B HA   1 
ATOM   4584 H HA   B SER   B 1 7   ? 45.262 -25.170 -21.328 0.58 35.57 ?  7   SER   B HA   1 
ATOM   4585 H HB2  A SER   B 1 7   ? 47.400 -24.235 -21.828 0.42 38.63 ?  7   SER   B HB2  1 
ATOM   4586 H HB2  B SER   B 1 7   ? 47.460 -24.175 -21.682 0.58 39.29 ?  7   SER   B HB2  1 
ATOM   4587 H HB3  A SER   B 1 7   ? 48.070 -25.352 -20.920 0.42 38.63 ?  7   SER   B HB3  1 
ATOM   4588 H HB3  B SER   B 1 7   ? 48.043 -25.484 -20.995 0.58 39.29 ?  7   SER   B HB3  1 
ATOM   4589 H HG   A SER   B 1 7   ? 48.067 -25.944 -23.033 0.42 40.38 ?  7   SER   B HG   1 
ATOM   4590 H HG   B SER   B 1 7   ? 47.952 -25.705 -23.176 0.58 41.52 ?  7   SER   B HG   1 
ATOM   4591 N N    . GLY   B 1 8   ? 45.152 -27.546 -20.778 1.00 29.01 ?  8   GLY   B N    1 
ATOM   4592 C CA   . GLY   B 1 8   ? 45.060 -28.927 -20.376 1.00 27.75 ?  8   GLY   B CA   1 
ATOM   4593 C C    . GLY   B 1 8   ? 44.102 -29.216 -19.257 1.00 25.94 ?  8   GLY   B C    1 
ATOM   4594 O O    . GLY   B 1 8   ? 44.217 -30.280 -18.635 1.00 27.79 ?  8   GLY   B O    1 
ATOM   4595 H H    A GLY   B 1 8   ? 44.684 -27.343 -21.466 0.42 34.83 ?  8   GLY   B H    1 
ATOM   4596 H H    B GLY   B 1 8   ? 44.673 -27.342 -21.458 0.58 34.83 ?  8   GLY   B H    1 
ATOM   4597 H HA2  . GLY   B 1 8   ? 44.772 -29.454 -21.126 1.00 33.32 ?  8   GLY   B HA2  1 
ATOM   4598 H HA3  . GLY   B 1 8   ? 45.931 -29.233 -20.093 1.00 33.32 ?  8   GLY   B HA3  1 
ATOM   4599 N N    . TYR   B 1 9   ? 43.120 -28.345 -19.008 1.00 23.94 ?  9   TYR   B N    1 
ATOM   4600 C CA   . TYR   B 1 9   ? 42.167 -28.582 -17.934 1.00 22.04 ?  9   TYR   B CA   1 
ATOM   4601 C C    . TYR   B 1 9   ? 40.966 -29.364 -18.422 1.00 21.55 ?  9   TYR   B C    1 
ATOM   4602 O O    . TYR   B 1 9   ? 40.518 -29.217 -19.565 1.00 23.33 ?  9   TYR   B O    1 
ATOM   4603 C CB   . TYR   B 1 9   ? 41.686 -27.280 -17.296 1.00 21.68 ?  9   TYR   B CB   1 
ATOM   4604 C CG   . TYR   B 1 9   ? 42.719 -26.681 -16.381 1.00 20.63 ?  9   TYR   B CG   1 
ATOM   4605 C CD1  . TYR   B 1 9   ? 43.822 -26.021 -16.900 1.00 21.14 ?  9   TYR   B CD1  1 
ATOM   4606 C CD2  . TYR   B 1 9   ? 42.604 -26.788 -15.002 1.00 19.84 ?  9   TYR   B CD2  1 
ATOM   4607 C CE1  . TYR   B 1 9   ? 44.787 -25.481 -16.079 1.00 21.06 ?  9   TYR   B CE1  1 
ATOM   4608 C CE2  . TYR   B 1 9   ? 43.566 -26.246 -14.167 1.00 20.25 ?  9   TYR   B CE2  1 
ATOM   4609 C CZ   . TYR   B 1 9   ? 44.659 -25.588 -14.714 1.00 21.06 ?  9   TYR   B CZ   1 
ATOM   4610 O OH   . TYR   B 1 9   ? 45.627 -25.049 -13.903 1.00 22.12 ?  9   TYR   B OH   1 
ATOM   4611 H H    . TYR   B 1 9   ? 42.950 -27.636 -19.472 1.00 28.75 ?  9   TYR   B H    1 
ATOM   4612 H HA   . TYR   B 1 9   ? 42.583 -29.105 -17.242 1.00 26.46 ?  9   TYR   B HA   1 
ATOM   4613 H HB2  . TYR   B 1 9   ? 41.474 -26.630 -17.986 1.00 26.04 ?  9   TYR   B HB2  1 
ATOM   4614 H HB3  . TYR   B 1 9   ? 40.895 -27.470 -16.766 1.00 26.04 ?  9   TYR   B HB3  1 
ATOM   4615 H HD1  . TYR   B 1 9   ? 43.911 -25.948 -17.823 1.00 25.38 ?  9   TYR   B HD1  1 
ATOM   4616 H HD2  . TYR   B 1 9   ? 41.863 -27.229 -14.635 1.00 23.83 ?  9   TYR   B HD2  1 
ATOM   4617 H HE1  . TYR   B 1 9   ? 45.512 -25.042 -16.444 1.00 25.28 ?  9   TYR   B HE1  1 
ATOM   4618 H HE2  . TYR   B 1 9   ? 43.466 -26.323 -13.243 1.00 24.31 ?  9   TYR   B HE2  1 
ATOM   4619 H HH   . TYR   B 1 9   ? 46.207 -24.682 -14.375 1.00 26.56 ?  9   TYR   B HH   1 
ATOM   4620 N N    A LEU   B 1 10  ? 40.469 -30.234 -17.549 0.42 20.55 ?  10  LEU   B N    1 
ATOM   4621 N N    B LEU   B 1 10  ? 40.433 -30.196 -17.533 0.58 19.89 ?  10  LEU   B N    1 
ATOM   4622 C CA   A LEU   B 1 10  ? 39.265 -31.002 -17.805 0.42 20.70 ?  10  LEU   B CA   1 
ATOM   4623 C CA   B LEU   B 1 10  ? 39.214 -30.943 -17.791 0.58 19.66 ?  10  LEU   B CA   1 
ATOM   4624 C C    A LEU   B 1 10  ? 38.077 -30.236 -17.242 0.42 20.90 ?  10  LEU   B C    1 
ATOM   4625 C C    B LEU   B 1 10  ? 38.036 -30.140 -17.261 0.58 19.27 ?  10  LEU   B C    1 
ATOM   4626 O O    A LEU   B 1 10  ? 38.087 -29.835 -16.075 0.42 20.48 ?  10  LEU   B O    1 
ATOM   4627 O O    B LEU   B 1 10  ? 38.056 -29.691 -16.112 0.58 18.87 ?  10  LEU   B O    1 
ATOM   4628 C CB   A LEU   B 1 10  ? 39.368 -32.367 -17.126 0.42 21.27 ?  10  LEU   B CB   1 
ATOM   4629 C CB   B LEU   B 1 10  ? 39.276 -32.293 -17.076 0.58 20.82 ?  10  LEU   B CB   1 
ATOM   4630 C CG   A LEU   B 1 10  ? 38.214 -33.326 -17.411 0.42 22.08 ?  10  LEU   B CG   1 
ATOM   4631 C CG   B LEU   B 1 10  ? 38.210 -33.310 -17.474 0.58 22.19 ?  10  LEU   B CG   1 
ATOM   4632 C CD1  A LEU   B 1 10  ? 38.232 -33.756 -18.869 0.42 22.56 ?  10  LEU   B CD1  1 
ATOM   4633 C CD1  B LEU   B 1 10  ? 38.543 -33.923 -18.829 0.58 23.00 ?  10  LEU   B CD1  1 
ATOM   4634 C CD2  A LEU   B 1 10  ? 38.284 -34.530 -16.490 0.42 22.26 ?  10  LEU   B CD2  1 
ATOM   4635 C CD2  B LEU   B 1 10  ? 38.055 -34.388 -16.409 0.58 22.73 ?  10  LEU   B CD2  1 
ATOM   4636 H H    A LEU   B 1 10  ? 40.818 -30.402 -16.781 0.42 24.68 ?  10  LEU   B H    1 
ATOM   4637 H H    B LEU   B 1 10  ? 40.753 -30.340 -16.747 0.58 23.89 ?  10  LEU   B H    1 
ATOM   4638 H HA   A LEU   B 1 10  ? 39.137 -31.130 -18.756 0.42 24.86 ?  10  LEU   B HA   1 
ATOM   4639 H HA   B LEU   B 1 10  ? 39.089 -31.089 -18.737 0.58 23.61 ?  10  LEU   B HA   1 
ATOM   4640 H HB2  A LEU   B 1 10  ? 40.185 -32.798 -17.425 0.42 25.54 ?  10  LEU   B HB2  1 
ATOM   4641 H HB2  B LEU   B 1 10  ? 40.139 -32.693 -17.260 0.58 25.01 ?  10  LEU   B HB2  1 
ATOM   4642 H HB3  A LEU   B 1 10  ? 39.406 -32.234 -16.165 0.42 25.54 ?  10  LEU   B HB3  1 
ATOM   4643 H HB3  B LEU   B 1 10  ? 39.188 -32.145 -16.119 0.58 25.01 ?  10  LEU   B HB3  1 
ATOM   4644 H HG   A LEU   B 1 10  ? 37.373 -32.872 -17.243 0.42 26.51 ?  10  LEU   B HG   1 
ATOM   4645 H HG   B LEU   B 1 10  ? 37.357 -32.856 -17.557 0.58 26.65 ?  10  LEU   B HG   1 
ATOM   4646 H HD11 A LEU   B 1 10  ? 37.566 -34.447 -19.002 0.42 27.09 ?  10  LEU   B HD11 1 
ATOM   4647 H HD11 B LEU   B 1 10  ? 37.863 -34.575 -19.057 0.58 27.61 ?  10  LEU   B HD11 1 
ATOM   4648 H HD12 A LEU   B 1 10  ? 38.030 -32.989 -19.426 0.42 27.09 ?  10  LEU   B HD12 1 
ATOM   4649 H HD12 B LEU   B 1 10  ? 38.564 -33.218 -19.495 0.58 27.61 ?  10  LEU   B HD12 1 
ATOM   4650 H HD13 A LEU   B 1 10  ? 39.114 -34.099 -19.084 0.42 27.09 ?  10  LEU   B HD13 1 
ATOM   4651 H HD13 B LEU   B 1 10  ? 39.410 -34.353 -18.774 0.58 27.61 ?  10  LEU   B HD13 1 
ATOM   4652 H HD21 A LEU   B 1 10  ? 37.542 -35.122 -16.691 0.42 26.72 ?  10  LEU   B HD21 1 
ATOM   4653 H HD21 B LEU   B 1 10  ? 37.376 -35.021 -16.696 0.58 27.30 ?  10  LEU   B HD21 1 
ATOM   4654 H HD22 A LEU   B 1 10  ? 39.125 -34.988 -16.636 0.42 26.72 ?  10  LEU   B HD22 1 
ATOM   4655 H HD22 B LEU   B 1 10  ? 38.902 -34.842 -16.293 0.58 27.30 ?  10  LEU   B HD22 1 
ATOM   4656 H HD23 A LEU   B 1 10  ? 38.226 -34.225 -15.571 0.42 26.72 ?  10  LEU   B HD23 1 
ATOM   4657 H HD23 B LEU   B 1 10  ? 37.784 -33.971 -15.576 0.58 27.30 ?  10  LEU   B HD23 1 
ATOM   4658 N N    A LYS   B 1 11  ? 37.060 -30.042 -18.074 0.42 21.76 ?  11  LYS   B N    1 
ATOM   4659 N N    B LYS   B 1 11  ? 37.019 -29.960 -18.100 0.58 20.06 ?  11  LYS   B N    1 
ATOM   4660 C CA   A LYS   B 1 11  ? 35.866 -29.318 -17.672 0.42 23.38 ?  11  LYS   B CA   1 
ATOM   4661 C CA   B LYS   B 1 11  ? 35.803 -29.267 -17.699 0.58 22.70 ?  11  LYS   B CA   1 
ATOM   4662 C C    A LYS   B 1 11  ? 34.991 -30.229 -16.820 0.42 22.27 ?  11  LYS   B C    1 
ATOM   4663 C C    B LYS   B 1 11  ? 34.964 -30.202 -16.836 0.58 22.11 ?  11  LYS   B C    1 
ATOM   4664 O O    A LYS   B 1 11  ? 34.654 -31.343 -17.233 0.42 23.44 ?  11  LYS   B O    1 
ATOM   4665 O O    B LYS   B 1 11  ? 34.630 -31.314 -17.260 0.58 23.70 ?  11  LYS   B O    1 
ATOM   4666 C CB   A LYS   B 1 11  ? 35.115 -28.877 -18.929 0.42 26.54 ?  11  LYS   B CB   1 
ATOM   4667 C CB   B LYS   B 1 11  ? 35.032 -28.853 -18.953 0.58 26.61 ?  11  LYS   B CB   1 
ATOM   4668 C CG   A LYS   B 1 11  ? 34.033 -27.836 -18.719 0.42 29.40 ?  11  LYS   B CG   1 
ATOM   4669 C CG   B LYS   B 1 11  ? 33.867 -27.914 -18.716 0.58 30.26 ?  11  LYS   B CG   1 
ATOM   4670 C CD   A LYS   B 1 11  ? 33.358 -27.502 -20.045 0.42 31.83 ?  11  LYS   B CD   1 
ATOM   4671 C CD   B LYS   B 1 11  ? 33.159 -27.596 -20.028 0.58 33.20 ?  11  LYS   B CD   1 
ATOM   4672 C CE   A LYS   B 1 11  ? 32.327 -26.398 -19.892 0.42 33.58 ?  11  LYS   B CE   1 
ATOM   4673 C CE   B LYS   B 1 11  ? 32.158 -26.466 -19.866 0.58 35.34 ?  11  LYS   B CE   1 
ATOM   4674 N NZ   A LYS   B 1 11  ? 32.957 -25.092 -19.560 0.42 34.50 ?  11  LYS   B NZ   1 
ATOM   4675 N NZ   B LYS   B 1 11  ? 32.830 -25.172 -19.570 0.58 36.41 ?  11  LYS   B NZ   1 
ATOM   4676 H H    A LYS   B 1 11  ? 37.030 -30.330 -18.883 0.42 26.13 ?  11  LYS   B H    1 
ATOM   4677 H H    B LYS   B 1 11  ? 37.000 -30.234 -18.917 0.58 24.09 ?  11  LYS   B H    1 
ATOM   4678 H HA   A LYS   B 1 11  ? 36.105 -28.533 -17.156 0.42 28.07 ?  11  LYS   B HA   1 
ATOM   4679 H HA   B LYS   B 1 11  ? 36.016 -28.472 -17.189 0.58 27.26 ?  11  LYS   B HA   1 
ATOM   4680 H HB2  A LYS   B 1 11  ? 35.758 -28.501 -19.553 0.42 31.86 ?  11  LYS   B HB2  1 
ATOM   4681 H HB2  B LYS   B 1 11  ? 35.644 -28.401 -19.557 0.58 31.95 ?  11  LYS   B HB2  1 
ATOM   4682 H HB3  A LYS   B 1 11  ? 34.695 -29.653 -19.328 0.42 31.86 ?  11  LYS   B HB3  1 
ATOM   4683 H HB3  B LYS   B 1 11  ? 34.679 -29.646 -19.383 0.58 31.95 ?  11  LYS   B HB3  1 
ATOM   4684 H HG2  A LYS   B 1 11  ? 33.361 -28.185 -18.114 0.42 35.29 ?  11  LYS   B HG2  1 
ATOM   4685 H HG2  B LYS   B 1 11  ? 33.229 -28.336 -18.121 0.58 36.32 ?  11  LYS   B HG2  1 
ATOM   4686 H HG3  A LYS   B 1 11  ? 34.426 -27.025 -18.363 0.42 35.29 ?  11  LYS   B HG3  1 
ATOM   4687 H HG3  B LYS   B 1 11  ? 34.192 -27.085 -18.335 0.58 36.32 ?  11  LYS   B HG3  1 
ATOM   4688 H HD2  A LYS   B 1 11  ? 34.029 -27.204 -20.680 0.42 38.21 ?  11  LYS   B HD2  1 
ATOM   4689 H HD2  B LYS   B 1 11  ? 33.818 -27.326 -20.689 0.58 39.86 ?  11  LYS   B HD2  1 
ATOM   4690 H HD3  A LYS   B 1 11  ? 32.909 -28.294 -20.384 0.42 38.21 ?  11  LYS   B HD3  1 
ATOM   4691 H HD3  B LYS   B 1 11  ? 32.682 -28.383 -20.334 0.58 39.86 ?  11  LYS   B HD3  1 
ATOM   4692 H HE2  A LYS   B 1 11  ? 31.841 -26.299 -20.727 0.42 40.31 ?  11  LYS   B HE2  1 
ATOM   4693 H HE2  B LYS   B 1 11  ? 31.655 -26.364 -20.689 0.58 42.42 ?  11  LYS   B HE2  1 
ATOM   4694 H HE3  A LYS   B 1 11  ? 31.715 -26.633 -19.176 0.42 40.31 ?  11  LYS   B HE3  1 
ATOM   4695 H HE3  B LYS   B 1 11  ? 31.560 -26.674 -19.131 0.58 42.42 ?  11  LYS   B HE3  1 
ATOM   4696 H HZ1  A LYS   B 1 11  ? 32.332 -24.463 -19.489 0.42 41.42 ?  11  LYS   B HZ1  1 
ATOM   4697 H HZ1  B LYS   B 1 11  ? 32.227 -24.518 -19.531 0.58 43.70 ?  11  LYS   B HZ1  1 
ATOM   4698 H HZ2  A LYS   B 1 11  ? 33.396 -25.154 -18.789 0.42 41.42 ?  11  LYS   B HZ2  1 
ATOM   4699 H HZ2  B LYS   B 1 11  ? 33.254 -25.220 -18.789 0.58 43.70 ?  11  LYS   B HZ2  1 
ATOM   4700 H HZ3  A LYS   B 1 11  ? 33.529 -24.860 -20.202 0.42 41.42 ?  11  LYS   B HZ3  1 
ATOM   4701 H HZ3  B LYS   B 1 11  ? 33.420 -24.982 -20.209 0.58 43.70 ?  11  LYS   B HZ3  1 
ATOM   4702 N N    . LEU   B 1 12  ? 34.637 -29.765 -15.621 1.00 20.45 ?  12  LEU   B N    1 
ATOM   4703 C CA   . LEU   B 1 12  ? 33.692 -30.475 -14.765 1.00 19.66 ?  12  LEU   B CA   1 
ATOM   4704 C C    . LEU   B 1 12  ? 32.302 -29.864 -14.840 1.00 19.34 ?  12  LEU   B C    1 
ATOM   4705 O O    . LEU   B 1 12  ? 31.315 -30.580 -15.007 1.00 20.13 ?  12  LEU   B O    1 
ATOM   4706 C CB   . LEU   B 1 12  ? 34.164 -30.515 -13.305 1.00 18.86 ?  12  LEU   B CB   1 
ATOM   4707 C CG   . LEU   B 1 12  ? 35.511 -31.188 -13.038 1.00 18.95 ?  12  LEU   B CG   1 
ATOM   4708 C CD1  . LEU   B 1 12  ? 35.891 -31.118 -11.565 1.00 18.79 ?  12  LEU   B CD1  1 
ATOM   4709 C CD2  . LEU   B 1 12  ? 35.504 -32.631 -13.522 1.00 19.54 ?  12  LEU   B CD2  1 
ATOM   4710 H H    A LEU   B 1 12  ? 34.923 -29.028 -15.280 0.42 24.56 ?  12  LEU   B H    1 
ATOM   4711 H H    B LEU   B 1 12  ? 34.950 -29.048 -15.265 0.58 24.56 ?  12  LEU   B H    1 
ATOM   4712 H HA   . LEU   B 1 12  ? 33.607 -31.387 -15.074 1.00 23.61 ?  12  LEU   B HA   1 
ATOM   4713 H HB2  . LEU   B 1 12  ? 34.221 -29.611 -12.980 1.00 22.64 ?  12  LEU   B HB2  1 
ATOM   4714 H HB3  . LEU   B 1 12  ? 33.493 -31.002 -12.790 1.00 22.64 ?  12  LEU   B HB3  1 
ATOM   4715 H HG   . LEU   B 1 12  ? 36.187 -30.717 -13.541 1.00 22.75 ?  12  LEU   B HG   1 
ATOM   4716 H HD11 . LEU   B 1 12  ? 36.753 -31.554 -11.441 1.00 22.56 ?  12  LEU   B HD11 1 
ATOM   4717 H HD12 . LEU   B 1 12  ? 35.953 -30.189 -11.295 1.00 22.56 ?  12  LEU   B HD12 1 
ATOM   4718 H HD13 . LEU   B 1 12  ? 35.217 -31.573 -11.036 1.00 22.56 ?  12  LEU   B HD13 1 
ATOM   4719 H HD21 . LEU   B 1 12  ? 36.327 -33.062 -13.247 1.00 23.46 ?  12  LEU   B HD21 1 
ATOM   4720 H HD22 . LEU   B 1 12  ? 34.743 -33.097 -13.134 1.00 23.46 ?  12  LEU   B HD22 1 
ATOM   4721 H HD23 . LEU   B 1 12  ? 35.434 -32.644 -14.491 1.00 23.46 ?  12  LEU   B HD23 1 
ATOM   4722 N N    . THR   B 1 13  ? 32.214 -28.547 -14.712 1.00 19.54 ?  13  THR   B N    1 
ATOM   4723 C CA   . THR   B 1 13  ? 30.998 -27.791 -14.942 1.00 19.63 ?  13  THR   B CA   1 
ATOM   4724 C C    . THR   B 1 13  ? 31.352 -26.615 -15.844 1.00 21.30 ?  13  THR   B C    1 
ATOM   4725 O O    . THR   B 1 13  ? 32.504 -26.441 -16.261 1.00 22.40 ?  13  THR   B O    1 
ATOM   4726 C CB   . THR   B 1 13  ? 30.389 -27.283 -13.631 1.00 19.08 ?  13  THR   B CB   1 
ATOM   4727 O OG1  . THR   B 1 13  ? 31.236 -26.257 -13.099 1.00 18.09 ?  13  THR   B OG1  1 
ATOM   4728 C CG2  . THR   B 1 13  ? 30.249 -28.411 -12.617 1.00 19.67 ?  13  THR   B CG2  1 
ATOM   4729 H H    . THR   B 1 13  ? 32.872 -28.052 -14.469 1.00 23.46 ?  13  THR   B H    1 
ATOM   4730 H HA   . THR   B 1 13  ? 30.338 -28.349 -15.384 1.00 23.57 ?  13  THR   B HA   1 
ATOM   4731 H HB   . THR   B 1 13  ? 29.498 -26.917 -13.800 1.00 22.91 ?  13  THR   B HB   1 
ATOM   4732 H HG1  . THR   B 1 13  ? 30.905 -25.490 -13.278 1.00 21.73 ?  13  THR   B HG1  1 
ATOM   4733 H HG21 . THR   B 1 13  ? 29.741 -28.110 -11.846 1.00 23.62 ?  13  THR   B HG21 1 
ATOM   4734 H HG22 . THR   B 1 13  ? 29.784 -29.161 -13.023 1.00 23.62 ?  13  THR   B HG22 1 
ATOM   4735 H HG23 . THR   B 1 13  ? 31.124 -28.703 -12.325 1.00 23.62 ?  13  THR   B HG23 1 
ATOM   4736 N N    A ASP   B 1 14  ? 30.352 -25.779 -16.126 0.42 21.97 ?  14  ASP   B N    1 
ATOM   4737 N N    B ASP   B 1 14  ? 30.353 -25.781 -16.132 0.58 21.75 ?  14  ASP   B N    1 
ATOM   4738 C CA   A ASP   B 1 14  ? 30.583 -24.635 -16.999 0.42 23.35 ?  14  ASP   B CA   1 
ATOM   4739 C CA   B ASP   B 1 14  ? 30.591 -24.637 -17.003 0.58 23.38 ?  14  ASP   B CA   1 
ATOM   4740 C C    A ASP   B 1 14  ? 31.664 -23.707 -16.455 0.42 21.61 ?  14  ASP   B C    1 
ATOM   4741 C C    B ASP   B 1 14  ? 31.672 -23.713 -16.457 0.58 21.63 ?  14  ASP   B C    1 
ATOM   4742 O O    A ASP   B 1 14  ? 32.303 -22.990 -17.233 0.42 22.56 ?  14  ASP   B O    1 
ATOM   4743 O O    B ASP   B 1 14  ? 32.319 -23.004 -17.235 0.58 22.92 ?  14  ASP   B O    1 
ATOM   4744 C CB   A ASP   B 1 14  ? 29.283 -23.860 -17.213 0.42 26.48 ?  14  ASP   B CB   1 
ATOM   4745 C CB   B ASP   B 1 14  ? 29.297 -23.857 -17.228 0.58 26.91 ?  14  ASP   B CB   1 
ATOM   4746 C CG   A ASP   B 1 14  ? 28.274 -24.626 -18.062 0.42 29.55 ?  14  ASP   B CG   1 
ATOM   4747 C CG   B ASP   B 1 14  ? 28.434 -24.452 -18.323 0.58 30.50 ?  14  ASP   B CG   1 
ATOM   4748 O OD1  A ASP   B 1 14  ? 28.638 -25.669 -18.648 0.42 30.40 ?  14  ASP   B OD1  1 
ATOM   4749 O OD1  B ASP   B 1 14  ? 28.905 -25.368 -19.033 0.58 31.82 ?  14  ASP   B OD1  1 
ATOM   4750 O OD2  A ASP   B 1 14  ? 27.103 -24.193 -18.131 0.42 30.87 -1 14  ASP   B OD2  1 
ATOM   4751 O OD2  B ASP   B 1 14  ? 27.278 -24.004 -18.476 0.58 31.98 -1 14  ASP   B OD2  1 
ATOM   4752 H H    A ASP   B 1 14  ? 29.550 -25.845 -15.829 0.42 26.38 ?  14  ASP   B H    1 
ATOM   4753 H H    B ASP   B 1 14  ? 29.549 -25.847 -15.836 0.58 26.12 ?  14  ASP   B H    1 
ATOM   4754 H HA   A ASP   B 1 14  ? 30.890 -24.953 -17.858 0.42 28.04 ?  14  ASP   B HA   1 
ATOM   4755 H HA   B ASP   B 1 14  ? 30.904 -24.957 -17.858 0.58 28.08 ?  14  ASP   B HA   1 
ATOM   4756 H HB2  A ASP   B 1 14  ? 28.867 -23.703 -16.354 0.42 31.79 ?  14  ASP   B HB2  1 
ATOM   4757 H HB2  B ASP   B 1 14  ? 28.785 -23.853 -16.406 0.58 32.30 ?  14  ASP   B HB2  1 
ATOM   4758 H HB3  A ASP   B 1 14  ? 29.497 -23.007 -17.636 0.42 31.79 ?  14  ASP   B HB3  1 
ATOM   4759 H HB3  B ASP   B 1 14  ? 29.517 -22.949 -17.490 0.58 32.30 ?  14  ASP   B HB3  1 
ATOM   4760 N N    . ASN   B 1 15  ? 31.882 -23.696 -15.135 1.00 19.68 ?  15  ASN   B N    1 
ATOM   4761 C CA   . ASN   B 1 15  ? 32.852 -22.786 -14.524 1.00 17.28 ?  15  ASN   B CA   1 
ATOM   4762 C C    . ASN   B 1 15  ? 33.940 -23.450 -13.693 1.00 15.64 ?  15  ASN   B C    1 
ATOM   4763 O O    . ASN   B 1 15  ? 34.799 -22.735 -13.167 1.00 15.17 ?  15  ASN   B O    1 
ATOM   4764 C CB   . ASN   B 1 15  ? 32.149 -21.728 -13.657 1.00 17.09 ?  15  ASN   B CB   1 
ATOM   4765 C CG   . ASN   B 1 15  ? 31.522 -22.328 -12.413 1.00 16.96 ?  15  ASN   B CG   1 
ATOM   4766 O OD1  . ASN   B 1 15  ? 30.575 -23.122 -12.501 1.00 19.09 ?  15  ASN   B OD1  1 
ATOM   4767 N ND2  . ASN   B 1 15  ? 32.045 -21.980 -11.252 1.00 15.32 ?  15  ASN   B ND2  1 
ATOM   4768 H H    A ASN   B 1 15  ? 31.462 -24.192 -14.565 0.42 23.64 ?  15  ASN   B H    1 
ATOM   4769 H H    B ASN   B 1 15  ? 31.458 -24.188 -14.565 0.58 23.64 ?  15  ASN   B H    1 
ATOM   4770 H HA   . ASN   B 1 15  ? 33.301 -22.300 -15.221 1.00 20.76 ?  15  ASN   B HA   1 
ATOM   4771 H HB2  . ASN   B 1 15  ? 32.798 -21.053 -13.377 1.00 20.52 ?  15  ASN   B HB2  1 
ATOM   4772 H HB3  . ASN   B 1 15  ? 31.444 -21.296 -14.173 1.00 20.52 ?  15  ASN   B HB3  1 
ATOM   4773 H HD21 . ASN   B 1 15  ? 31.718 -22.290 -10.514 1.00 18.40 ?  15  ASN   B HD21 1 
ATOM   4774 H HD22 . ASN   B 1 15  ? 32.716 -21.433 -11.213 1.00 18.40 ?  15  ASN   B HD22 1 
ATOM   4775 N N    . VAL   B 1 16  ? 33.930 -24.769 -13.524 1.00 15.45 ?  16  VAL   B N    1 
ATOM   4776 C CA   . VAL   B 1 16  ? 34.929 -25.461 -12.715 1.00 14.75 ?  16  VAL   B CA   1 
ATOM   4777 C C    . VAL   B 1 16  ? 35.720 -26.405 -13.608 1.00 15.21 ?  16  VAL   B C    1 
ATOM   4778 O O    . VAL   B 1 16  ? 35.141 -27.286 -14.263 1.00 16.37 ?  16  VAL   B O    1 
ATOM   4779 C CB   . VAL   B 1 16  ? 34.296 -26.216 -11.534 1.00 15.24 ?  16  VAL   B CB   1 
ATOM   4780 C CG1  . VAL   B 1 16  ? 35.358 -26.967 -10.725 1.00 16.19 ?  16  VAL   B CG1  1 
ATOM   4781 C CG2  . VAL   B 1 16  ? 33.516 -25.255 -10.642 1.00 16.59 ?  16  VAL   B CG2  1 
ATOM   4782 H H    . VAL   B 1 16  ? 33.325 -25.291 -13.859 1.00 18.56 ?  16  VAL   B H    1 
ATOM   4783 H HA   . VAL   B 1 16  ? 35.534 -24.808 -12.340 1.00 17.72 ?  16  VAL   B HA   1 
ATOM   4784 H HB   . VAL   B 1 16  ? 33.663 -26.873 -11.875 1.00 18.31 ?  16  VAL   B HB   1 
ATOM   4785 H HG11 . VAL   B 1 16  ? 34.958 -27.285 -9.896  1.00 19.44 ?  16  VAL   B HG11 1 
ATOM   4786 H HG12 . VAL   B 1 16  ? 35.673 -27.724 -11.244 1.00 19.44 ?  16  VAL   B HG12 1 
ATOM   4787 H HG13 . VAL   B 1 16  ? 36.087 -26.365 -10.530 1.00 19.44 ?  16  VAL   B HG13 1 
ATOM   4788 H HG21 . VAL   B 1 16  ? 33.177 -25.738 -9.868  1.00 19.93 ?  16  VAL   B HG21 1 
ATOM   4789 H HG22 . VAL   B 1 16  ? 34.104 -24.543 -10.352 1.00 19.93 ?  16  VAL   B HG22 1 
ATOM   4790 H HG23 . VAL   B 1 16  ? 32.772 -24.885 -11.145 1.00 19.93 ?  16  VAL   B HG23 1 
ATOM   4791 N N    . TYR   B 1 17  ? 37.045 -26.238 -13.589 1.00 15.03 ?  17  TYR   B N    1 
ATOM   4792 C CA   . TYR   B 1 17  ? 37.982 -26.999 -14.400 1.00 15.85 ?  17  TYR   B CA   1 
ATOM   4793 C C    . TYR   B 1 17  ? 39.036 -27.615 -13.488 1.00 14.88 ?  17  TYR   B C    1 
ATOM   4794 O O    . TYR   B 1 17  ? 39.325 -27.082 -12.413 1.00 14.98 ?  17  TYR   B O    1 
ATOM   4795 C CB   . TYR   B 1 17  ? 38.687 -26.081 -15.406 1.00 19.20 ?  17  TYR   B CB   1 
ATOM   4796 C CG   . TYR   B 1 17  ? 37.758 -25.317 -16.320 1.00 23.27 ?  17  TYR   B CG   1 
ATOM   4797 C CD1  . TYR   B 1 17  ? 37.213 -24.100 -15.936 1.00 24.81 ?  17  TYR   B CD1  1 
ATOM   4798 C CD2  . TYR   B 1 17  ? 37.433 -25.813 -17.575 1.00 25.62 ?  17  TYR   B CD2  1 
ATOM   4799 C CE1  . TYR   B 1 17  ? 36.365 -23.397 -16.777 1.00 26.82 ?  17  TYR   B CE1  1 
ATOM   4800 C CE2  . TYR   B 1 17  ? 36.590 -25.120 -18.424 1.00 27.38 ?  17  TYR   B CE2  1 
ATOM   4801 C CZ   . TYR   B 1 17  ? 36.057 -23.912 -18.019 1.00 28.16 ?  17  TYR   B CZ   1 
ATOM   4802 O OH   . TYR   B 1 17  ? 35.218 -23.218 -18.861 1.00 29.41 ?  17  TYR   B OH   1 
ATOM   4803 H H    . TYR   B 1 17  ? 37.434 -25.651 -13.087 1.00 18.05 ?  17  TYR   B H    1 
ATOM   4804 H HA   . TYR   B 1 17  ? 37.506 -27.698 -14.876 1.00 19.04 ?  17  TYR   B HA   1 
ATOM   4805 H HB2  . TYR   B 1 17  ? 39.226 -25.439 -14.921 1.00 23.06 ?  17  TYR   B HB2  1 
ATOM   4806 H HB3  . TYR   B 1 17  ? 39.247 -26.630 -15.966 1.00 23.06 ?  17  TYR   B HB3  1 
ATOM   4807 H HD1  . TYR   B 1 17  ? 37.419 -23.750 -15.100 1.00 29.79 ?  17  TYR   B HD1  1 
ATOM   4808 H HD2  . TYR   B 1 17  ? 37.786 -26.625 -17.852 1.00 30.76 ?  17  TYR   B HD2  1 
ATOM   4809 H HE1  . TYR   B 1 17  ? 36.006 -22.583 -16.506 1.00 32.21 ?  17  TYR   B HE1  1 
ATOM   4810 H HE2  . TYR   B 1 17  ? 36.377 -25.467 -19.262 1.00 32.87 ?  17  TYR   B HE2  1 
ATOM   4811 H HH   . TYR   B 1 17  ? 35.113 -23.643 -19.577 1.00 35.31 ?  17  TYR   B HH   1 
ATOM   4812 N N    . ILE   B 1 18  ? 39.643 -28.725 -13.917 1.00 14.97 ?  18  ILE   B N    1 
ATOM   4813 C CA   . ILE   B 1 18  ? 40.566 -29.447 -13.047 1.00 14.93 ?  18  ILE   B CA   1 
ATOM   4814 C C    . ILE   B 1 18  ? 41.728 -30.013 -13.856 1.00 15.41 ?  18  ILE   B C    1 
ATOM   4815 O O    . ILE   B 1 18  ? 41.571 -30.413 -15.015 1.00 16.74 ?  18  ILE   B O    1 
ATOM   4816 C CB   . ILE   B 1 18  ? 39.813 -30.540 -12.232 1.00 15.14 ?  18  ILE   B CB   1 
ATOM   4817 C CG1  . ILE   B 1 18  ? 40.677 -31.095 -11.094 1.00 15.24 ?  18  ILE   B CG1  1 
ATOM   4818 C CG2  . ILE   B 1 18  ? 39.275 -31.667 -13.144 1.00 15.81 ?  18  ILE   B CG2  1 
ATOM   4819 C CD1  . ILE   B 1 18  ? 39.878 -31.883 -10.061 1.00 16.91 ?  18  ILE   B CD1  1 
ATOM   4820 H H    . ILE   B 1 18  ? 39.532 -29.068 -14.694 1.00 17.98 ?  18  ILE   B H    1 
ATOM   4821 H HA   . ILE   B 1 18  ? 40.922 -28.823 -12.399 1.00 17.93 ?  18  ILE   B HA   1 
ATOM   4822 H HB   . ILE   B 1 18  ? 39.033 -30.128 -11.818 1.00 18.19 ?  18  ILE   B HB   1 
ATOM   4823 H HG12 . ILE   B 1 18  ? 41.341 -31.687 -11.465 1.00 18.31 ?  18  ILE   B HG12 1 
ATOM   4824 H HG13 . ILE   B 1 18  ? 41.096 -30.354 -10.637 1.00 18.31 ?  18  ILE   B HG13 1 
ATOM   4825 H HG21 . ILE   B 1 18  ? 38.709 -32.263 -12.620 1.00 18.99 ?  18  ILE   B HG21 1 
ATOM   4826 H HG22 . ILE   B 1 18  ? 38.749 -31.268 -13.858 1.00 18.99 ?  18  ILE   B HG22 1 
ATOM   4827 H HG23 . ILE   B 1 18  ? 40.019 -32.159 -13.514 1.00 18.99 ?  18  ILE   B HG23 1 
ATOM   4828 H HD11 . ILE   B 1 18  ? 40.474 -32.159 -9.347  1.00 20.31 ?  18  ILE   B HD11 1 
ATOM   4829 H HD12 . ILE   B 1 18  ? 39.174 -31.317 -9.702  1.00 20.31 ?  18  ILE   B HD12 1 
ATOM   4830 H HD13 . ILE   B 1 18  ? 39.487 -32.663 -10.485 1.00 20.31 ?  18  ILE   B HD13 1 
ATOM   4831 N N    . LYS   B 1 19  ? 42.902 -30.047 -13.232 1.00 15.70 ?  19  LYS   B N    1 
ATOM   4832 C CA   . LYS   B 1 19  ? 44.107 -30.525 -13.893 1.00 16.64 ?  19  LYS   B CA   1 
ATOM   4833 C C    . LYS   B 1 19  ? 45.013 -31.203 -12.873 1.00 16.35 ?  19  LYS   B C    1 
ATOM   4834 O O    . LYS   B 1 19  ? 45.108 -30.761 -11.725 1.00 15.96 ?  19  LYS   B O    1 
ATOM   4835 C CB   . LYS   B 1 19  ? 44.864 -29.358 -14.542 1.00 18.23 ?  19  LYS   B CB   1 
ATOM   4836 C CG   . LYS   B 1 19  ? 46.067 -29.777 -15.368 1.00 20.85 ?  19  LYS   B CG   1 
ATOM   4837 C CD   . LYS   B 1 19  ? 46.824 -28.566 -15.901 1.00 22.50 ?  19  LYS   B CD   1 
ATOM   4838 C CE   . LYS   B 1 19  ? 48.028 -28.978 -16.733 1.00 24.25 ?  19  LYS   B CE   1 
ATOM   4839 N NZ   . LYS   B 1 19  ? 48.795 -27.809 -17.243 1.00 25.29 ?  19  LYS   B NZ   1 
ATOM   4840 H H    . LYS   B 1 19  ? 43.005 -29.786 -12.419 1.00 18.86 ?  19  LYS   B H    1 
ATOM   4841 H HA   . LYS   B 1 19  ? 43.852 -31.163 -14.579 1.00 19.98 ?  19  LYS   B HA   1 
ATOM   4842 H HB2  . LYS   B 1 19  ? 44.248 -28.885 -15.124 1.00 21.90 ?  19  LYS   B HB2  1 
ATOM   4843 H HB3  . LYS   B 1 19  ? 45.164 -28.765 -13.834 1.00 21.90 ?  19  LYS   B HB3  1 
ATOM   4844 H HG2  . LYS   B 1 19  ? 46.662 -30.299 -14.811 1.00 25.04 ?  19  LYS   B HG2  1 
ATOM   4845 H HG3  . LYS   B 1 19  ? 45.755 -30.308 -16.119 1.00 25.04 ?  19  LYS   B HG3  1 
ATOM   4846 H HD2  . LYS   B 1 19  ? 46.226 -28.038 -16.457 1.00 27.02 ?  19  LYS   B HD2  1 
ATOM   4847 H HD3  . LYS   B 1 19  ? 47.134 -28.033 -15.149 1.00 27.02 ?  19  LYS   B HD3  1 
ATOM   4848 H HE2  . LYS   B 1 19  ? 48.618 -29.517 -16.183 1.00 29.12 ?  19  LYS   B HE2  1 
ATOM   4849 H HE3  . LYS   B 1 19  ? 47.718 -29.498 -17.493 1.00 29.12 ?  19  LYS   B HE3  1 
ATOM   4850 H HZ1  . LYS   B 1 19  ? 49.456 -28.087 -17.769 1.00 30.37 ?  19  LYS   B HZ1  1 
ATOM   4851 H HZ2  . LYS   B 1 19  ? 48.258 -27.274 -17.712 1.00 30.37 ?  19  LYS   B HZ2  1 
ATOM   4852 H HZ3  . LYS   B 1 19  ? 49.138 -27.350 -16.564 1.00 30.37 ?  19  LYS   B HZ3  1 
ATOM   4853 N N    . ASN   B 1 20  ? 45.696 -32.263 -13.302 1.00 17.91 ?  20  ASN   B N    1 
ATOM   4854 C CA   . ASN   B 1 20  ? 46.719 -32.898 -12.474 1.00 19.04 ?  20  ASN   B CA   1 
ATOM   4855 C C    . ASN   B 1 20  ? 48.000 -32.087 -12.654 1.00 19.70 ?  20  ASN   B C    1 
ATOM   4856 O O    . ASN   B 1 20  ? 48.658 -32.173 -13.695 1.00 21.73 ?  20  ASN   B O    1 
ATOM   4857 C CB   . ASN   B 1 20  ? 46.886 -34.359 -12.894 1.00 21.22 ?  20  ASN   B CB   1 
ATOM   4858 C CG   . ASN   B 1 20  ? 48.071 -35.048 -12.228 1.00 22.50 ?  20  ASN   B CG   1 
ATOM   4859 O OD1  . ASN   B 1 20  ? 48.768 -35.850 -12.864 1.00 24.56 ?  20  ASN   B OD1  1 
ATOM   4860 N ND2  . ASN   B 1 20  ? 48.300 -34.757 -10.954 1.00 22.04 ?  20  ASN   B ND2  1 
ATOM   4861 H H    . ASN   B 1 20  ? 45.580 -32.625 -14.074 1.00 21.51 ?  20  ASN   B H    1 
ATOM   4862 H HA   . ASN   B 1 20  ? 46.437 -32.863 -11.545 1.00 22.87 ?  20  ASN   B HA   1 
ATOM   4863 H HB2  . ASN   B 1 20  ? 46.079 -34.845 -12.652 1.00 25.48 ?  20  ASN   B HB2  1 
ATOM   4864 H HB3  . ASN   B 1 20  ? 47.011 -34.389 -13.854 1.00 25.48 ?  20  ASN   B HB3  1 
ATOM   4865 H HD21 . ASN   B 1 20  ? 48.962 -35.117 -10.543 1.00 26.46 ?  20  ASN   B HD21 1 
ATOM   4866 H HD22 . ASN   B 1 20  ? 47.788 -34.201 -10.534 1.00 26.46 ?  20  ASN   B HD22 1 
ATOM   4867 N N    . ALA   B 1 21  ? 48.352 -31.273 -11.654 1.00 19.24 ?  21  ALA   B N    1 
ATOM   4868 C CA   . ALA   B 1 21  ? 49.491 -30.374 -11.795 1.00 19.78 ?  21  ALA   B CA   1 
ATOM   4869 C C    . ALA   B 1 21  ? 49.944 -29.869 -10.432 1.00 18.04 ?  21  ALA   B C    1 
ATOM   4870 O O    . ALA   B 1 21  ? 49.196 -29.896 -9.451  1.00 17.34 ?  21  ALA   B O    1 
ATOM   4871 C CB   . ALA   B 1 21  ? 49.150 -29.196 -12.708 1.00 21.69 ?  21  ALA   B CB   1 
ATOM   4872 H H    . ALA   B 1 21  ? 47.943 -31.223 -10.890 1.00 23.11 ?  21  ALA   B H    1 
ATOM   4873 H HA   . ALA   B 1 21  ? 50.220 -30.867 -12.189 1.00 23.76 ?  21  ALA   B HA   1 
ATOM   4874 H HB1  . ALA   B 1 21  ? 49.955 -28.674 -12.843 1.00 26.05 ?  21  ALA   B HB1  1 
ATOM   4875 H HB2  . ALA   B 1 21  ? 48.835 -29.543 -13.558 1.00 26.05 ?  21  ALA   B HB2  1 
ATOM   4876 H HB3  . ALA   B 1 21  ? 48.463 -28.657 -12.293 1.00 26.05 ?  21  ALA   B HB3  1 
ATOM   4877 N N    . ASP   B 1 22  ? 51.202 -29.423 -10.406 1.00 17.22 ?  22  ASP   B N    1 
ATOM   4878 C CA   . ASP   B 1 22  ? 51.819 -28.732 -9.280  1.00 16.06 ?  22  ASP   B CA   1 
ATOM   4879 C C    . ASP   B 1 22  ? 51.415 -27.260 -9.369  1.00 14.21 ?  22  ASP   B C    1 
ATOM   4880 O O    . ASP   B 1 22  ? 51.728 -26.591 -10.359 1.00 15.07 ?  22  ASP   B O    1 
ATOM   4881 C CB   . ASP   B 1 22  ? 53.337 -28.910 -9.441  1.00 17.16 ?  22  ASP   B CB   1 
ATOM   4882 C CG   . ASP   B 1 22  ? 54.171 -28.151 -8.416  1.00 18.68 ?  22  ASP   B CG   1 
ATOM   4883 O OD1  . ASP   B 1 22  ? 53.825 -27.021 -8.038  1.00 18.69 ?  22  ASP   B OD1  1 
ATOM   4884 O OD2  . ASP   B 1 22  ? 55.227 -28.686 -8.015  1.00 21.85 -1 22  ASP   B OD2  1 
ATOM   4885 H H    . ASP   B 1 22  ? 51.742 -29.514 -11.070 1.00 20.68 ?  22  ASP   B H    1 
ATOM   4886 H HA   . ASP   B 1 22  ? 51.527 -29.112 -8.434  1.00 19.29 ?  22  ASP   B HA   1 
ATOM   4887 H HB2  . ASP   B 1 22  ? 53.555 -29.847 -9.357  1.00 20.61 ?  22  ASP   B HB2  1 
ATOM   4888 H HB3  . ASP   B 1 22  ? 53.593 -28.587 -10.321 1.00 20.61 ?  22  ASP   B HB3  1 
ATOM   4889 N N    . ILE   B 1 23  ? 50.699 -26.759 -8.354  1.00 13.50 ?  23  ILE   B N    1 
ATOM   4890 C CA   . ILE   B 1 23  ? 50.121 -25.410 -8.433  1.00 13.01 ?  23  ILE   B CA   1 
ATOM   4891 C C    . ILE   B 1 23  ? 51.189 -24.327 -8.579  1.00 12.78 ?  23  ILE   B C    1 
ATOM   4892 O O    . ILE   B 1 23  ? 50.931 -23.281 -9.185  1.00 12.16 ?  23  ILE   B O    1 
ATOM   4893 C CB   . ILE   B 1 23  ? 49.193 -25.149 -7.231  1.00 13.50 ?  23  ILE   B CB   1 
ATOM   4894 C CG1  . ILE   B 1 23  ? 48.372 -23.874 -7.436  1.00 13.63 ?  23  ILE   B CG1  1 
ATOM   4895 C CG2  . ILE   B 1 23  ? 49.966 -25.150 -5.920  1.00 14.34 ?  23  ILE   B CG2  1 
ATOM   4896 C CD1  . ILE   B 1 23  ? 47.254 -23.713 -6.423  1.00 14.67 ?  23  ILE   B CD1  1 
ATOM   4897 H H    . ILE   B 1 23  ? 50.523 -27.178 -7.623  1.00 16.22 ?  23  ILE   B H    1 
ATOM   4898 H HA   . ILE   B 1 23  ? 49.567 -25.370 -9.228  1.00 15.62 ?  23  ILE   B HA   1 
ATOM   4899 H HB   . ILE   B 1 23  ? 48.558 -25.887 -7.197  1.00 16.21 ?  23  ILE   B HB   1 
ATOM   4900 H HG12 . ILE   B 1 23  ? 48.972 -23.107 -7.355  1.00 16.37 ?  23  ILE   B HG12 1 
ATOM   4901 H HG13 . ILE   B 1 23  ? 47.984 -23.886 -8.325  1.00 16.37 ?  23  ILE   B HG13 1 
ATOM   4902 H HG21 . ILE   B 1 23  ? 49.336 -25.117 -5.187  1.00 17.23 ?  23  ILE   B HG21 1 
ATOM   4903 H HG22 . ILE   B 1 23  ? 50.489 -25.968 -5.869  1.00 17.23 ?  23  ILE   B HG22 1 
ATOM   4904 H HG23 . ILE   B 1 23  ? 50.549 -24.382 -5.901  1.00 17.23 ?  23  ILE   B HG23 1 
ATOM   4905 H HD11 . ILE   B 1 23  ? 46.735 -22.929 -6.654  1.00 17.62 ?  23  ILE   B HD11 1 
ATOM   4906 H HD12 . ILE   B 1 23  ? 46.700 -24.504 -6.446  1.00 17.62 ?  23  ILE   B HD12 1 
ATOM   4907 H HD13 . ILE   B 1 23  ? 47.646 -23.604 -5.541  1.00 17.62 ?  23  ILE   B HD13 1 
ATOM   4908 N N    . VAL   B 1 24  ? 52.385 -24.538 -8.015  1.00 12.97 ?  24  VAL   B N    1 
ATOM   4909 C CA   . VAL   B 1 24  ? 53.463 -23.555 -8.169  1.00 13.77 ?  24  VAL   B CA   1 
ATOM   4910 C C    . VAL   B 1 24  ? 53.932 -23.510 -9.615  1.00 13.68 ?  24  VAL   B C    1 
ATOM   4911 O O    . VAL   B 1 24  ? 54.066 -22.435 -10.215 1.00 14.14 ?  24  VAL   B O    1 
ATOM   4912 C CB   . VAL   B 1 24  ? 54.631 -23.864 -7.211  1.00 14.20 ?  24  VAL   B CB   1 
ATOM   4913 C CG1  . VAL   B 1 24  ? 55.840 -22.979 -7.541  1.00 15.39 ?  24  VAL   B CG1  1 
ATOM   4914 C CG2  . VAL   B 1 24  ? 54.199 -23.658 -5.781  1.00 15.08 ?  24  VAL   B CG2  1 
ATOM   4915 H H    . VAL   B 1 24  ? 52.591 -25.229 -7.550  1.00 15.58 ?  24  VAL   B H    1 
ATOM   4916 H HA   . VAL   B 1 24  ? 53.119 -22.681 -7.941  1.00 16.54 ?  24  VAL   B HA   1 
ATOM   4917 H HB   . VAL   B 1 24  ? 54.895 -24.794 -7.315  1.00 17.06 ?  24  VAL   B HB   1 
ATOM   4918 H HG11 . VAL   B 1 24  ? 56.441 -22.973 -6.779  1.00 18.49 ?  24  VAL   B HG11 1 
ATOM   4919 H HG12 . VAL   B 1 24  ? 56.295 -23.336 -8.318  1.00 18.49 ?  24  VAL   B HG12 1 
ATOM   4920 H HG13 . VAL   B 1 24  ? 55.529 -22.077 -7.720  1.00 18.49 ?  24  VAL   B HG13 1 
ATOM   4921 H HG21 . VAL   B 1 24  ? 54.910 -23.947 -5.190  1.00 18.12 ?  24  VAL   B HG21 1 
ATOM   4922 H HG22 . VAL   B 1 24  ? 54.017 -22.714 -5.643  1.00 18.12 ?  24  VAL   B HG22 1 
ATOM   4923 H HG23 . VAL   B 1 24  ? 53.396 -24.177 -5.613  1.00 18.12 ?  24  VAL   B HG23 1 
ATOM   4924 N N    A GLU   B 1 25  ? 54.199 -24.680 -10.199 0.42 15.16 ?  25  GLU   B N    1 
ATOM   4925 N N    B GLU   B 1 25  ? 54.215 -24.682 -10.190 0.58 14.83 ?  25  GLU   B N    1 
ATOM   4926 C CA   A GLU   B 1 25  ? 54.597 -24.722 -11.601 0.42 16.35 ?  25  GLU   B CA   1 
ATOM   4927 C CA   B GLU   B 1 25  ? 54.592 -24.740 -11.596 0.58 15.56 ?  25  GLU   B CA   1 
ATOM   4928 C C    A GLU   B 1 25  ? 53.481 -24.222 -12.507 0.42 15.21 ?  25  GLU   B C    1 
ATOM   4929 C C    B GLU   B 1 25  ? 53.482 -24.193 -12.481 0.58 14.63 ?  25  GLU   B C    1 
ATOM   4930 O O    A GLU   B 1 25  ? 53.745 -23.555 -13.516 0.42 15.98 ?  25  GLU   B O    1 
ATOM   4931 O O    B GLU   B 1 25  ? 53.749 -23.454 -13.437 0.58 15.40 ?  25  GLU   B O    1 
ATOM   4932 C CB   A GLU   B 1 25  ? 55.041 -26.133 -11.987 0.42 19.98 ?  25  GLU   B CB   1 
ATOM   4933 C CB   B GLU   B 1 25  ? 54.965 -26.171 -11.985 0.58 19.38 ?  25  GLU   B CB   1 
ATOM   4934 C CG   A GLU   B 1 25  ? 56.311 -26.570 -11.272 0.42 24.49 ?  25  GLU   B CG   1 
ATOM   4935 C CG   B GLU   B 1 25  ? 56.236 -26.658 -11.305 0.58 25.11 ?  25  GLU   B CG   1 
ATOM   4936 C CD   A GLU   B 1 25  ? 57.409 -25.517 -11.314 0.42 28.16 ?  25  GLU   B CD   1 
ATOM   4937 C CD   B GLU   B 1 25  ? 57.410 -25.713 -11.484 0.58 29.50 ?  25  GLU   B CD   1 
ATOM   4938 O OE1  A GLU   B 1 25  ? 57.746 -25.043 -12.422 0.42 29.47 ?  25  GLU   B OE1  1 
ATOM   4939 O OE1  B GLU   B 1 25  ? 57.838 -25.512 -12.641 0.58 30.77 ?  25  GLU   B OE1  1 
ATOM   4940 O OE2  A GLU   B 1 25  ? 57.929 -25.149 -10.237 0.42 29.30 -1 25  GLU   B OE2  1 
ATOM   4941 O OE2  B GLU   B 1 25  ? 57.907 -25.167 -10.473 0.58 30.99 -1 25  GLU   B OE2  1 
ATOM   4942 H H    A GLU   B 1 25  ? 54.164 -25.447 -9.810  0.42 18.21 ?  25  GLU   B H    1 
ATOM   4943 H H    B GLU   B 1 25  ? 54.196 -25.444 -9.791  0.58 17.81 ?  25  GLU   B H    1 
ATOM   4944 H HA   A GLU   B 1 25  ? 55.339 -24.117 -11.729 0.42 19.64 ?  25  GLU   B HA   1 
ATOM   4945 H HA   B GLU   B 1 25  ? 55.359 -24.171 -11.738 0.58 18.69 ?  25  GLU   B HA   1 
ATOM   4946 H HB2  A GLU   B 1 25  ? 54.335 -26.760 -11.758 0.42 23.99 ?  25  GLU   B HB2  1 
ATOM   4947 H HB2  B GLU   B 1 25  ? 54.242 -26.767 -11.727 0.58 23.28 ?  25  GLU   B HB2  1 
ATOM   4948 H HB3  A GLU   B 1 25  ? 55.207 -26.159 -12.944 0.42 23.99 ?  25  GLU   B HB3  1 
ATOM   4949 H HB3  B GLU   B 1 25  ? 55.099 -26.212 -12.945 0.58 23.28 ?  25  GLU   B HB3  1 
ATOM   4950 H HG2  A GLU   B 1 25  ? 56.105 -26.741 -10.343 0.42 29.41 ?  25  GLU   B HG2  1 
ATOM   4951 H HG2  B GLU   B 1 25  ? 56.071 -26.753 -10.358 0.58 30.15 ?  25  GLU   B HG2  1 
ATOM   4952 H HG3  A GLU   B 1 25  ? 56.652 -27.369 -11.698 0.42 29.41 ?  25  GLU   B HG3  1 
ATOM   4953 H HG3  B GLU   B 1 25  ? 56.500 -27.501 -11.694 0.58 30.15 ?  25  GLU   B HG3  1 
ATOM   4954 N N    . GLU   B 1 26  ? 52.227 -24.521 -12.160 1.00 13.89 ?  26  GLU   B N    1 
ATOM   4955 C CA   . GLU   B 1 26  ? 51.106 -24.001 -12.937 1.00 14.37 ?  26  GLU   B CA   1 
ATOM   4956 C C    . GLU   B 1 26  ? 51.051 -22.484 -12.863 1.00 13.10 ?  26  GLU   B C    1 
ATOM   4957 O O    . GLU   B 1 26  ? 50.858 -21.814 -13.879 1.00 15.15 ?  26  GLU   B O    1 
ATOM   4958 C CB   . GLU   B 1 26  ? 49.782 -24.579 -12.433 1.00 16.07 ?  26  GLU   B CB   1 
ATOM   4959 C CG   . GLU   B 1 26  ? 49.325 -25.841 -13.127 1.00 20.73 ?  26  GLU   B CG   1 
ATOM   4960 C CD   . GLU   B 1 26  ? 49.131 -25.689 -14.632 1.00 22.12 ?  26  GLU   B CD   1 
ATOM   4961 O OE1  . GLU   B 1 26  ? 48.156 -25.057 -15.092 1.00 22.15 ?  26  GLU   B OE1  1 
ATOM   4962 O OE2  . GLU   B 1 26  ? 49.952 -26.255 -15.353 1.00 25.37 -1 26  GLU   B OE2  1 
ATOM   4963 H H    A GLU   B 1 26  ? 51.996 -25.019 -11.492 0.42 16.68 ?  26  GLU   B H    1 
ATOM   4964 H H    B GLU   B 1 26  ? 51.995 -25.033 -11.503 0.58 16.68 ?  26  GLU   B H    1 
ATOM   4965 H HA   . GLU   B 1 26  ? 51.217 -24.258 -13.865 1.00 17.26 ?  26  GLU   B HA   1 
ATOM   4966 H HB2  . GLU   B 1 26  ? 49.873 -24.781 -11.486 1.00 19.30 ?  26  GLU   B HB2  1 
ATOM   4967 H HB3  . GLU   B 1 26  ? 49.090 -23.904 -12.549 1.00 19.30 ?  26  GLU   B HB3  1 
ATOM   4968 H HG2  . GLU   B 1 26  ? 49.996 -26.517 -13.001 1.00 24.89 ?  26  GLU   B HG2  1 
ATOM   4969 H HG3  . GLU   B 1 26  ? 48.479 -26.117 -12.749 1.00 24.89 ?  26  GLU   B HG3  1 
ATOM   4970 N N    . ALA   B 1 27  ? 51.201 -21.923 -11.664 1.00 12.59 ?  27  ALA   B N    1 
ATOM   4971 C CA   . ALA   B 1 27  ? 51.149 -20.474 -11.536 1.00 13.07 ?  27  ALA   B CA   1 
ATOM   4972 C C    . ALA   B 1 27  ? 52.208 -19.812 -12.411 1.00 13.43 ?  27  ALA   B C    1 
ATOM   4973 O O    . ALA   B 1 27  ? 51.933 -18.823 -13.110 1.00 14.40 ?  27  ALA   B O    1 
ATOM   4974 C CB   . ALA   B 1 27  ? 51.311 -20.070 -10.069 1.00 13.47 ?  27  ALA   B CB   1 
ATOM   4975 H H    . ALA   B 1 27  ? 51.326 -22.352 -10.927 1.00 15.12 ?  27  ALA   B H    1 
ATOM   4976 H HA   . ALA   B 1 27  ? 50.283 -20.162 -11.833 1.00 15.70 ?  27  ALA   B HA   1 
ATOM   4977 H HB1  . ALA   B 1 27  ? 51.269 -19.104 -10.001 1.00 16.18 ?  27  ALA   B HB1  1 
ATOM   4978 H HB2  . ALA   B 1 27  ? 50.594 -20.469 -9.551  1.00 16.18 ?  27  ALA   B HB2  1 
ATOM   4979 H HB3  . ALA   B 1 27  ? 52.169 -20.388 -9.745  1.00 16.18 ?  27  ALA   B HB3  1 
ATOM   4980 N N    . LYS   B 1 28  ? 53.429 -20.351 -12.398 1.00 14.53 ?  28  LYS   B N    1 
ATOM   4981 C CA   . LYS   B 1 28  ? 54.500 -19.730 -13.167 1.00 16.38 ?  28  LYS   B CA   1 
ATOM   4982 C C    . LYS   B 1 28  ? 54.243 -19.818 -14.665 1.00 16.69 ?  28  LYS   B C    1 
ATOM   4983 O O    . LYS   B 1 28  ? 54.653 -18.922 -15.415 1.00 18.01 ?  28  LYS   B O    1 
ATOM   4984 C CB   . LYS   B 1 28  ? 55.859 -20.315 -12.760 1.00 19.81 ?  28  LYS   B CB   1 
ATOM   4985 C CG   . LYS   B 1 28  ? 56.242 -19.991 -11.312 1.00 23.65 ?  28  LYS   B CG   1 
ATOM   4986 C CD   . LYS   B 1 28  ? 57.664 -20.409 -10.958 1.00 29.31 ?  28  LYS   B CD   1 
ATOM   4987 C CE   . LYS   B 1 28  ? 57.788 -21.906 -10.806 1.00 33.66 ?  28  LYS   B CE   1 
ATOM   4988 N NZ   . LYS   B 1 28  ? 59.139 -22.286 -10.294 1.00 36.27 ?  28  LYS   B NZ   1 
ATOM   4989 H H    . LYS   B 1 28  ? 53.658 -21.056 -11.954 1.00 17.45 ?  28  LYS   B H    1 
ATOM   4990 H HA   . LYS   B 1 28  ? 54.526 -18.792 -12.944 1.00 19.67 ?  28  LYS   B HA   1 
ATOM   4991 H HB2  . LYS   B 1 28  ? 55.842 -21.279 -12.846 1.00 23.79 ?  28  LYS   B HB2  1 
ATOM   4992 H HB3  . LYS   B 1 28  ? 56.555 -19.945 -13.331 1.00 23.79 ?  28  LYS   B HB3  1 
ATOM   4993 H HG2  . LYS   B 1 28  ? 56.167 -19.031 -11.173 1.00 28.40 ?  28  LYS   B HG2  1 
ATOM   4994 H HG3  . LYS   B 1 28  ? 55.636 -20.456 -10.714 1.00 28.40 ?  28  LYS   B HG3  1 
ATOM   4995 H HD2  . LYS   B 1 28  ? 58.262 -20.121 -11.667 1.00 35.19 ?  28  LYS   B HD2  1 
ATOM   4996 H HD3  . LYS   B 1 28  ? 57.917 -19.992 -10.119 1.00 35.19 ?  28  LYS   B HD3  1 
ATOM   4997 H HE2  . LYS   B 1 28  ? 57.122 -22.221 -10.174 1.00 40.41 ?  28  LYS   B HE2  1 
ATOM   4998 H HE3  . LYS   B 1 28  ? 57.658 -22.329 -11.670 1.00 40.41 ?  28  LYS   B HE3  1 
ATOM   4999 H HZ1  . LYS   B 1 28  ? 59.195 -23.169 -10.210 1.00 43.55 ?  28  LYS   B HZ1  1 
ATOM   5000 H HZ2  . LYS   B 1 28  ? 59.767 -22.007 -10.860 1.00 43.55 ?  28  LYS   B HZ2  1 
ATOM   5001 H HZ3  . LYS   B 1 28  ? 59.279 -21.909 -9.499  1.00 43.55 ?  28  LYS   B HZ3  1 
ATOM   5002 N N    A LYS   B 1 29  ? 53.583 -20.882 -15.122 0.42 17.55 ?  29  LYS   B N    1 
ATOM   5003 N N    B LYS   B 1 29  ? 53.538 -20.860 -15.116 0.58 17.15 ?  29  LYS   B N    1 
ATOM   5004 C CA   A LYS   B 1 29  ? 53.297 -21.020 -16.547 0.42 19.65 ?  29  LYS   B CA   1 
ATOM   5005 C CA   B LYS   B 1 29  ? 53.284 -21.082 -16.538 0.58 19.22 ?  29  LYS   B CA   1 
ATOM   5006 C C    A LYS   B 1 29  ? 52.067 -20.214 -16.958 0.42 17.83 ?  29  LYS   B C    1 
ATOM   5007 C C    B LYS   B 1 29  ? 52.010 -20.404 -17.038 0.58 17.23 ?  29  LYS   B C    1 
ATOM   5008 O O    A LYS   B 1 29  ? 52.108 -19.459 -17.938 0.42 18.65 ?  29  LYS   B O    1 
ATOM   5009 O O    B LYS   B 1 29  ? 51.952 -19.980 -18.199 0.58 17.53 ?  29  LYS   B O    1 
ATOM   5010 C CB   A LYS   B 1 29  ? 53.143 -22.501 -16.912 0.42 23.71 ?  29  LYS   B CB   1 
ATOM   5011 C CB   B LYS   B 1 29  ? 53.184 -22.583 -16.826 0.58 23.59 ?  29  LYS   B CB   1 
ATOM   5012 C CG   A LYS   B 1 29  ? 52.880 -22.746 -18.393 0.42 27.51 ?  29  LYS   B CG   1 
ATOM   5013 C CG   B LYS   B 1 29  ? 52.957 -22.905 -18.299 0.58 27.88 ?  29  LYS   B CG   1 
ATOM   5014 C CD   A LYS   B 1 29  ? 53.067 -24.208 -18.765 0.42 30.43 ?  29  LYS   B CD   1 
ATOM   5015 C CD   B LYS   B 1 29  ? 53.072 -24.395 -18.597 0.58 31.32 ?  29  LYS   B CD   1 
ATOM   5016 C CE   A LYS   B 1 29  ? 52.040 -25.090 -18.081 0.42 32.44 ?  29  LYS   B CE   1 
ATOM   5017 C CE   B LYS   B 1 29  ? 51.850 -25.166 -18.132 0.58 33.73 ?  29  LYS   B CE   1 
ATOM   5018 N NZ   A LYS   B 1 29  ? 52.247 -26.527 -18.408 0.42 33.45 ?  29  LYS   B NZ   1 
ATOM   5019 N NZ   B LYS   B 1 29  ? 51.981 -26.625 -18.417 0.58 34.70 ?  29  LYS   B NZ   1 
ATOM   5020 H H    A LYS   B 1 29  ? 53.307 -21.536 -14.634 0.42 21.07 ?  29  LYS   B H    1 
ATOM   5021 H H    B LYS   B 1 29  ? 53.187 -21.459 -14.608 0.58 20.60 ?  29  LYS   B H    1 
ATOM   5022 H HA   A LYS   B 1 29  ? 54.043 -20.676 -17.049 0.42 23.60 ?  29  LYS   B HA   1 
ATOM   5023 H HA   B LYS   B 1 29  ? 54.031 -20.729 -17.046 0.58 23.09 ?  29  LYS   B HA   1 
ATOM   5024 H HB2  A LYS   B 1 29  ? 53.965 -22.969 -16.680 0.42 28.47 ?  29  LYS   B HB2  1 
ATOM   5025 H HB2  B LYS   B 1 29  ? 54.010 -23.010 -16.552 0.58 28.32 ?  29  LYS   B HB2  1 
ATOM   5026 H HB3  A LYS   B 1 29  ? 52.403 -22.878 -16.413 0.42 28.47 ?  29  LYS   B HB3  1 
ATOM   5027 H HB3  B LYS   B 1 29  ? 52.440 -22.949 -16.323 0.58 28.32 ?  29  LYS   B HB3  1 
ATOM   5028 H HG2  A LYS   B 1 29  ? 51.966 -22.500 -18.601 0.42 33.03 ?  29  LYS   B HG2  1 
ATOM   5029 H HG2  B LYS   B 1 29  ? 52.066 -22.617 -18.553 0.58 33.47 ?  29  LYS   B HG2  1 
ATOM   5030 H HG3  A LYS   B 1 29  ? 53.499 -22.220 -18.922 0.42 33.03 ?  29  LYS   B HG3  1 
ATOM   5031 H HG3  B LYS   B 1 29  ? 53.621 -22.438 -18.830 0.58 33.47 ?  29  LYS   B HG3  1 
ATOM   5032 H HD2  A LYS   B 1 29  ? 52.966 -24.312 -19.725 0.42 36.53 ?  29  LYS   B HD2  1 
ATOM   5033 H HD2  B LYS   B 1 29  ? 53.162 -24.522 -19.556 0.58 37.60 ?  29  LYS   B HD2  1 
ATOM   5034 H HD3  A LYS   B 1 29  ? 53.951 -24.500 -18.488 0.42 36.53 ?  29  LYS   B HD3  1 
ATOM   5035 H HD3  B LYS   B 1 29  ? 53.848 -24.754 -18.139 0.58 37.60 ?  29  LYS   B HD3  1 
ATOM   5036 H HE2  A LYS   B 1 29  ? 52.115 -24.987 -17.120 0.42 38.94 ?  29  LYS   B HE2  1 
ATOM   5037 H HE2  B LYS   B 1 29  ? 51.744 -25.051 -17.175 0.58 40.49 ?  29  LYS   B HE2  1 
ATOM   5038 H HE3  A LYS   B 1 29  ? 51.152 -24.833 -18.377 0.42 38.94 ?  29  LYS   B HE3  1 
ATOM   5039 H HE3  B LYS   B 1 29  ? 51.065 -24.835 -18.598 0.58 40.49 ?  29  LYS   B HE3  1 
ATOM   5040 H HZ1  A LYS   B 1 29  ? 51.634 -27.023 -17.996 0.42 40.16 ?  29  LYS   B HZ1  1 
ATOM   5041 H HZ1  B LYS   B 1 29  ? 51.256 -27.058 -18.137 0.58 41.65 ?  29  LYS   B HZ1  1 
ATOM   5042 H HZ2  A LYS   B 1 29  ? 52.178 -26.651 -19.286 0.42 40.16 ?  29  LYS   B HZ2  1 
ATOM   5043 H HZ2  B LYS   B 1 29  ? 52.077 -26.757 -19.292 0.58 41.65 ?  29  LYS   B HZ2  1 
ATOM   5044 H HZ3  A LYS   B 1 29  ? 53.056 -26.785 -18.141 0.42 40.16 ?  29  LYS   B HZ3  1 
ATOM   5045 H HZ3  B LYS   B 1 29  ? 52.694 -26.954 -17.996 0.58 41.65 ?  29  LYS   B HZ3  1 
ATOM   5046 N N    . VAL   B 1 30  ? 50.974 -20.338 -16.200 1.00 16.25 ?  30  VAL   B N    1 
ATOM   5047 C CA   . VAL   B 1 30  ? 49.688 -19.763 -16.605 1.00 16.26 ?  30  VAL   B CA   1 
ATOM   5048 C C    . VAL   B 1 30  ? 49.672 -18.257 -16.458 1.00 14.83 ?  30  VAL   B C    1 
ATOM   5049 O O    . VAL   B 1 30  ? 48.909 -17.563 -17.151 1.00 15.61 ?  30  VAL   B O    1 
ATOM   5050 C CB   . VAL   B 1 30  ? 48.599 -20.377 -15.700 1.00 19.83 ?  30  VAL   B CB   1 
ATOM   5051 C CG1  . VAL   B 1 30  ? 47.303 -19.584 -15.759 1.00 21.78 ?  30  VAL   B CG1  1 
ATOM   5052 C CG2  . VAL   B 1 30  ? 48.389 -21.848 -16.046 1.00 20.95 ?  30  VAL   B CG2  1 
ATOM   5053 H H    A VAL   B 1 30  ? 50.954 -20.734 -15.433 0.42 19.51 ?  30  VAL   B H    1 
ATOM   5054 H H    B VAL   B 1 30  ? 50.982 -20.638 -15.391 0.58 19.51 ?  30  VAL   B H    1 
ATOM   5055 H HA   . VAL   B 1 30  ? 49.496 -20.003 -17.528 1.00 19.53 ?  30  VAL   B HA   1 
ATOM   5056 H HB   . VAL   B 1 30  ? 48.915 -20.350 -14.784 1.00 23.81 ?  30  VAL   B HB   1 
ATOM   5057 H HG11 . VAL   B 1 30  ? 46.576 -20.174 -15.499 1.00 26.15 ?  30  VAL   B HG11 1 
ATOM   5058 H HG12 . VAL   B 1 30  ? 47.354 -18.840 -15.144 1.00 26.15 ?  30  VAL   B HG12 1 
ATOM   5059 H HG13 . VAL   B 1 30  ? 47.156 -19.276 -16.662 1.00 26.15 ?  30  VAL   B HG13 1 
ATOM   5060 H HG21 . VAL   B 1 30  ? 47.707 -22.222 -15.461 1.00 25.15 ?  30  VAL   B HG21 1 
ATOM   5061 H HG22 . VAL   B 1 30  ? 48.097 -21.923 -16.971 1.00 25.15 ?  30  VAL   B HG22 1 
ATOM   5062 H HG23 . VAL   B 1 30  ? 49.222 -22.332 -15.927 1.00 25.15 ?  30  VAL   B HG23 1 
ATOM   5063 N N    A LYS   B 1 31  ? 50.497 -17.731 -15.560 0.42 15.01 ?  31  LYS   B N    1 
ATOM   5064 N N    B LYS   B 1 31  ? 50.492 -17.733 -15.556 0.58 14.37 ?  31  LYS   B N    1 
ATOM   5065 C CA   A LYS   B 1 31  ? 50.505 -16.317 -15.210 0.42 15.44 ?  31  LYS   B CA   1 
ATOM   5066 C CA   B LYS   B 1 31  ? 50.505 -16.317 -15.210 0.58 14.49 ?  31  LYS   B CA   1 
ATOM   5067 C C    A LYS   B 1 31  ? 49.107 -15.822 -14.827 0.42 13.81 ?  31  LYS   B C    1 
ATOM   5068 C C    B LYS   B 1 31  ? 49.116 -15.806 -14.815 0.58 13.34 ?  31  LYS   B C    1 
ATOM   5069 O O    A LYS   B 1 31  ? 48.549 -14.941 -15.490 0.42 13.88 ?  31  LYS   B O    1 
ATOM   5070 O O    B LYS   B 1 31  ? 48.579 -14.891 -15.446 0.58 13.86 ?  31  LYS   B O    1 
ATOM   5071 C CB   A LYS   B 1 31  ? 51.118 -15.473 -16.319 0.42 17.71 ?  31  LYS   B CB   1 
ATOM   5072 C CB   B LYS   B 1 31  ? 51.122 -15.484 -16.326 0.58 16.25 ?  31  LYS   B CB   1 
ATOM   5073 C CG   A LYS   B 1 31  ? 52.582 -15.836 -16.585 0.42 20.19 ?  31  LYS   B CG   1 
ATOM   5074 C CG   B LYS   B 1 31  ? 52.583 -15.875 -16.599 0.58 18.97 ?  31  LYS   B CG   1 
ATOM   5075 C CD   A LYS   B 1 31  ? 53.191 -15.003 -17.693 0.42 23.15 ?  31  LYS   B CD   1 
ATOM   5076 C CD   B LYS   B 1 31  ? 53.158 -15.195 -17.823 0.58 22.61 ?  31  LYS   B CD   1 
ATOM   5077 C CE   A LYS   B 1 31  ? 54.675 -15.287 -17.837 0.42 25.60 ?  31  LYS   B CE   1 
ATOM   5078 C CE   B LYS   B 1 31  ? 54.666 -15.364 -17.884 0.58 25.54 ?  31  LYS   B CE   1 
ATOM   5079 N NZ   A LYS   B 1 31  ? 55.425 -14.961 -16.590 0.42 26.63 ?  31  LYS   B NZ   1 
ATOM   5080 N NZ   B LYS   B 1 31  ? 55.344 -14.793 -16.682 0.58 26.87 ?  31  LYS   B NZ   1 
ATOM   5081 H H    A LYS   B 1 31  ? 51.089 -18.190 -15.137 0.42 18.03 ?  31  LYS   B H    1 
ATOM   5082 H H    B LYS   B 1 31  ? 51.087 -18.196 -15.134 0.58 17.26 ?  31  LYS   B H    1 
ATOM   5083 H HA   A LYS   B 1 31  ? 51.070 -16.213 -14.435 0.42 18.54 ?  31  LYS   B HA   1 
ATOM   5084 H HA   B LYS   B 1 31  ? 51.070 -16.216 -14.436 0.58 17.40 ?  31  LYS   B HA   1 
ATOM   5085 H HB2  A LYS   B 1 31  ? 50.622 -15.607 -17.140 0.42 21.26 ?  31  LYS   B HB2  1 
ATOM   5086 H HB2  B LYS   B 1 31  ? 50.619 -15.612 -17.142 0.58 19.52 ?  31  LYS   B HB2  1 
ATOM   5087 H HB3  A LYS   B 1 31  ? 51.085 -14.537 -16.059 0.42 21.26 ?  31  LYS   B HB3  1 
ATOM   5088 H HB3  B LYS   B 1 31  ? 51.106 -14.549 -16.063 0.58 19.52 ?  31  LYS   B HB3  1 
ATOM   5089 H HG2  A LYS   B 1 31  ? 53.095 -15.688 -15.774 0.42 24.25 ?  31  LYS   B HG2  1 
ATOM   5090 H HG2  B LYS   B 1 31  ? 53.118 -15.628 -15.829 0.58 22.78 ?  31  LYS   B HG2  1 
ATOM   5091 H HG3  A LYS   B 1 31  ? 52.634 -16.770 -16.844 0.42 24.25 ?  31  LYS   B HG3  1 
ATOM   5092 H HG3  B LYS   B 1 31  ? 52.629 -16.835 -16.737 0.58 22.78 ?  31  LYS   B HG3  1 
ATOM   5093 H HD2  A LYS   B 1 31  ? 52.753 -15.220 -18.529 0.42 27.80 ?  31  LYS   B HD2  1 
ATOM   5094 H HD2  B LYS   B 1 31  ? 52.769 -15.593 -18.617 0.58 27.15 ?  31  LYS   B HD2  1 
ATOM   5095 H HD3  A LYS   B 1 31  ? 53.077 -14.064 -17.483 0.42 27.80 ?  31  LYS   B HD3  1 
ATOM   5096 H HD3  B LYS   B 1 31  ? 52.954 -14.249 -17.784 0.58 27.15 ?  31  LYS   B HD3  1 
ATOM   5097 H HE2  A LYS   B 1 31  ? 54.803 -16.231 -18.028 0.42 30.73 ?  31  LYS   B HE2  1 
ATOM   5098 H HE2  B LYS   B 1 31  ? 54.879 -16.311 -17.931 0.58 30.66 ?  31  LYS   B HE2  1 
ATOM   5099 H HE3  A LYS   B 1 31  ? 55.034 -14.748 -18.557 0.42 30.73 ?  31  LYS   B HE3  1 
ATOM   5100 H HE3  B LYS   B 1 31  ? 55.005 -14.907 -18.669 0.58 30.66 ?  31  LYS   B HE3  1 
ATOM   5101 H HZ1  A LYS   B 1 31  ? 56.300 -15.049 -16.729 0.42 31.98 ?  31  LYS   B HZ1  1 
ATOM   5102 H HZ1  B LYS   B 1 31  ? 56.226 -14.781 -16.806 0.58 32.27 ?  31  LYS   B HZ1  1 
ATOM   5103 H HZ2  A LYS   B 1 31  ? 55.254 -14.124 -16.343 0.42 31.98 ?  31  LYS   B HZ2  1 
ATOM   5104 H HZ2  B LYS   B 1 31  ? 55.061 -13.963 -16.537 0.58 32.27 ?  31  LYS   B HZ2  1 
ATOM   5105 H HZ3  A LYS   B 1 31  ? 55.181 -15.512 -15.933 0.42 31.98 ?  31  LYS   B HZ3  1 
ATOM   5106 H HZ3  B LYS   B 1 31  ? 55.163 -15.289 -15.963 0.58 32.27 ?  31  LYS   B HZ3  1 
ATOM   5107 N N    . PRO   B 1 32  ? 48.524 -16.364 -13.758 1.00 12.87 ?  32  PRO   B N    1 
ATOM   5108 C CA   . PRO   B 1 32  ? 47.156 -15.994 -13.389 1.00 12.48 ?  32  PRO   B CA   1 
ATOM   5109 C C    . PRO   B 1 32  ? 47.103 -14.652 -12.684 1.00 12.66 ?  32  PRO   B C    1 
ATOM   5110 O O    . PRO   B 1 32  ? 48.039 -14.246 -11.993 1.00 13.54 ?  32  PRO   B O    1 
ATOM   5111 C CB   . PRO   B 1 32  ? 46.759 -17.103 -12.408 1.00 13.13 ?  32  PRO   B CB   1 
ATOM   5112 C CG   . PRO   B 1 32  ? 48.072 -17.445 -11.730 1.00 13.07 ?  32  PRO   B CG   1 
ATOM   5113 C CD   . PRO   B 1 32  ? 49.124 -17.311 -12.796 1.00 13.70 ?  32  PRO   B CD   1 
ATOM   5114 H HA   . PRO   B 1 32  ? 46.567 -16.003 -14.167 1.00 15.00 ?  32  PRO   B HA   1 
ATOM   5115 H HB2  . PRO   B 1 32  ? 46.115 -16.760 -11.769 1.00 15.77 ?  32  PRO   B HB2  1 
ATOM   5116 H HB3  . PRO   B 1 32  ? 46.404 -17.865 -12.890 1.00 15.77 ?  32  PRO   B HB3  1 
ATOM   5117 H HG2  . PRO   B 1 32  ? 48.239 -16.824 -11.004 1.00 15.70 ?  32  PRO   B HG2  1 
ATOM   5118 H HG3  . PRO   B 1 32  ? 48.038 -18.358 -11.397 1.00 15.70 ?  32  PRO   B HG3  1 
ATOM   5119 H HD2  . PRO   B 1 32  ? 49.936 -16.939 -12.420 1.00 16.46 ?  32  PRO   B HD2  1 
ATOM   5120 H HD3  . PRO   B 1 32  ? 49.286 -18.169 -13.217 1.00 16.46 ?  32  PRO   B HD3  1 
ATOM   5121 N N    . THR   B 1 33  ? 45.955 -13.984 -12.825 1.00 12.38 ?  33  THR   B N    1 
ATOM   5122 C CA   . THR   B 1 33  ? 45.683 -12.808 -12.004 1.00 12.59 ?  33  THR   B CA   1 
ATOM   5123 C C    . THR   B 1 33  ? 45.645 -13.169 -10.525 1.00 11.94 ?  33  THR   B C    1 
ATOM   5124 O O    . THR   B 1 33  ? 46.130 -12.398 -9.684  1.00 13.21 ?  33  THR   B O    1 
ATOM   5125 C CB   . THR   B 1 33  ? 44.361 -12.154 -12.433 1.00 13.08 ?  33  THR   B CB   1 
ATOM   5126 O OG1  . THR   B 1 33  ? 44.356 -11.908 -13.846 1.00 13.49 ?  33  THR   B OG1  1 
ATOM   5127 C CG2  . THR   B 1 33  ? 44.148 -10.852 -11.697 1.00 14.73 ?  33  THR   B CG2  1 
ATOM   5128 H H    . THR   B 1 33  ? 45.334 -14.193 -13.394 1.00 14.87 ?  33  THR   B H    1 
ATOM   5129 H HA   . THR   B 1 33  ? 46.392 -12.165 -12.153 1.00 15.12 ?  33  THR   B HA   1 
ATOM   5130 H HB   . THR   B 1 33  ? 43.627 -12.760 -12.226 1.00 15.71 ?  33  THR   B HB   1 
ATOM   5131 H HG1  . THR   B 1 33  ? 43.634 -11.543 -14.079 1.00 16.20 ?  33  THR   B HG1  1 
ATOM   5132 H HG21 . THR   B 1 33  ? 43.390 -10.386 -12.067 1.00 17.70 ?  33  THR   B HG21 1 
ATOM   5133 H HG22 . THR   B 1 33  ? 43.987 -11.034 -10.757 1.00 17.70 ?  33  THR   B HG22 1 
ATOM   5134 H HG23 . THR   B 1 33  ? 44.940 -10.300 -11.781 1.00 17.70 ?  33  THR   B HG23 1 
ATOM   5135 N N    . VAL   B 1 34  ? 45.063 -14.327 -10.183 1.00 11.43 ?  34  VAL   B N    1 
ATOM   5136 C CA   . VAL   B 1 34  ? 44.846 -14.713 -8.791  1.00 11.42 ?  34  VAL   B CA   1 
ATOM   5137 C C    . VAL   B 1 34  ? 45.247 -16.164 -8.607  1.00 10.79 ?  34  VAL   B C    1 
ATOM   5138 O O    . VAL   B 1 34  ? 44.732 -17.044 -9.303  1.00 11.47 ?  34  VAL   B O    1 
ATOM   5139 C CB   . VAL   B 1 34  ? 43.373 -14.550 -8.361  1.00 12.80 ?  34  VAL   B CB   1 
ATOM   5140 C CG1  . VAL   B 1 34  ? 43.178 -15.018 -6.923  1.00 13.33 ?  34  VAL   B CG1  1 
ATOM   5141 C CG2  . VAL   B 1 34  ? 42.901 -13.126 -8.545  1.00 13.62 ?  34  VAL   B CG2  1 
ATOM   5142 H H    . VAL   B 1 34  ? 44.796 -14.920 -10.756 1.00 13.73 ?  34  VAL   B H    1 
ATOM   5143 H HA   . VAL   B 1 34  ? 45.402 -14.162 -8.220  1.00 13.72 ?  34  VAL   B HA   1 
ATOM   5144 H HB   . VAL   B 1 34  ? 42.825 -15.104 -8.941  1.00 15.38 ?  34  VAL   B HB   1 
ATOM   5145 H HG11 . VAL   B 1 34  ? 42.338 -14.665 -6.592  1.00 16.02 ?  34  VAL   B HG11 1 
ATOM   5146 H HG12 . VAL   B 1 34  ? 43.159 -15.987 -6.910  1.00 16.02 ?  34  VAL   B HG12 1 
ATOM   5147 H HG13 . VAL   B 1 34  ? 43.912 -14.688 -6.385  1.00 16.02 ?  34  VAL   B HG13 1 
ATOM   5148 H HG21 . VAL   B 1 34  ? 41.976 -13.056 -8.262  1.00 16.35 ?  34  VAL   B HG21 1 
ATOM   5149 H HG22 . VAL   B 1 34  ? 43.455 -12.531 -8.017  1.00 16.35 ?  34  VAL   B HG22 1 
ATOM   5150 H HG23 . VAL   B 1 34  ? 42.969 -12.878 -9.489  1.00 16.35 ?  34  VAL   B HG23 1 
ATOM   5151 N N    . VAL   B 1 35  ? 46.128 -16.421 -7.647  1.00 10.26 ?  35  VAL   B N    1 
ATOM   5152 C CA   . VAL   B 1 35  ? 46.345 -17.768 -7.125  1.00 10.03 ?  35  VAL   B CA   1 
ATOM   5153 C C    . VAL   B 1 35  ? 45.794 -17.814 -5.709  1.00 10.13 ?  35  VAL   B C    1 
ATOM   5154 O O    . VAL   B 1 35  ? 46.014 -16.892 -4.920  1.00 10.27 ?  35  VAL   B O    1 
ATOM   5155 C CB   . VAL   B 1 35  ? 47.825 -18.209 -7.191  1.00 11.13 ?  35  VAL   B CB   1 
ATOM   5156 C CG1  . VAL   B 1 35  ? 48.727 -17.373 -6.276  1.00 11.87 ?  35  VAL   B CG1  1 
ATOM   5157 C CG2  . VAL   B 1 35  ? 47.957 -19.699 -6.882  1.00 11.58 ?  35  VAL   B CG2  1 
ATOM   5158 H H    . VAL   B 1 35  ? 46.619 -15.819 -7.275  1.00 12.32 ?  35  VAL   B H    1 
ATOM   5159 H HA   . VAL   B 1 35  ? 45.829 -18.390 -7.656  1.00 12.05 ?  35  VAL   B HA   1 
ATOM   5160 H HB   . VAL   B 1 35  ? 48.139 -18.080 -8.101  1.00 13.37 ?  35  VAL   B HB   1 
ATOM   5161 H HG11 . VAL   B 1 35  ? 49.648 -17.615 -6.450  1.00 14.26 ?  35  VAL   B HG11 1 
ATOM   5162 H HG12 . VAL   B 1 35  ? 48.579 -16.440 -6.467  1.00 14.26 ?  35  VAL   B HG12 1 
ATOM   5163 H HG13 . VAL   B 1 35  ? 48.498 -17.572 -5.355  1.00 14.26 ?  35  VAL   B HG13 1 
ATOM   5164 H HG21 . VAL   B 1 35  ? 48.883 -19.971 -6.969  1.00 13.91 ?  35  VAL   B HG21 1 
ATOM   5165 H HG22 . VAL   B 1 35  ? 47.654 -19.868 -5.968  1.00 13.91 ?  35  VAL   B HG22 1 
ATOM   5166 H HG23 . VAL   B 1 35  ? 47.406 -20.211 -7.500  1.00 13.91 ?  35  VAL   B HG23 1 
ATOM   5167 N N    . VAL   B 1 36  ? 45.082 -18.891 -5.387  1.00 9.91  ?  36  VAL   B N    1 
ATOM   5168 C CA   . VAL   B 1 36  ? 44.528 -19.088 -4.056  1.00 9.92  ?  36  VAL   B CA   1 
ATOM   5169 C C    . VAL   B 1 36  ? 45.530 -19.849 -3.199  1.00 9.85  ?  36  VAL   B C    1 
ATOM   5170 O O    . VAL   B 1 36  ? 46.069 -20.884 -3.616  1.00 10.65 ?  36  VAL   B O    1 
ATOM   5171 C CB   . VAL   B 1 36  ? 43.191 -19.848 -4.131  1.00 10.10 ?  36  VAL   B CB   1 
ATOM   5172 C CG1  . VAL   B 1 36  ? 42.672 -20.207 -2.744  1.00 11.08 ?  36  VAL   B CG1  1 
ATOM   5173 C CG2  . VAL   B 1 36  ? 42.177 -19.037 -4.902  1.00 11.15 ?  36  VAL   B CG2  1 
ATOM   5174 H H    . VAL   B 1 36  ? 44.915 -19.538 -5.931  1.00 11.91 ?  36  VAL   B H    1 
ATOM   5175 H HA   . VAL   B 1 36  ? 44.362 -18.231 -3.643  1.00 11.92 ?  36  VAL   B HA   1 
ATOM   5176 H HB   . VAL   B 1 36  ? 43.327 -20.677 -4.615  1.00 12.14 ?  36  VAL   B HB   1 
ATOM   5177 H HG11 . VAL   B 1 36  ? 41.735 -20.447 -2.805  1.00 13.32 ?  36  VAL   B HG11 1 
ATOM   5178 H HG12 . VAL   B 1 36  ? 43.183 -20.950 -2.394  1.00 13.32 ?  36  VAL   B HG12 1 
ATOM   5179 H HG13 . VAL   B 1 36  ? 42.773 -19.432 -2.161  1.00 13.32 ?  36  VAL   B HG13 1 
ATOM   5180 H HG21 . VAL   B 1 36  ? 41.332 -19.513 -4.916  1.00 13.40 ?  36  VAL   B HG21 1 
ATOM   5181 H HG22 . VAL   B 1 36  ? 42.069 -18.176 -4.476  1.00 13.40 ?  36  VAL   B HG22 1 
ATOM   5182 H HG23 . VAL   B 1 36  ? 42.499 -18.916 -5.814  1.00 13.40 ?  36  VAL   B HG23 1 
ATOM   5183 N N    . ASN   B 1 37  ? 45.739 -19.360 -1.982  1.00 9.95  ?  37  ASN   B N    1 
ATOM   5184 C CA   . ASN   B 1 37  ? 46.487 -20.075 -0.962  1.00 10.29 ?  37  ASN   B CA   1 
ATOM   5185 C C    . ASN   B 1 37  ? 45.532 -20.743 0.022   1.00 10.51 ?  37  ASN   B C    1 
ATOM   5186 O O    . ASN   B 1 37  ? 44.525 -20.154 0.429   1.00 10.73 ?  37  ASN   B O    1 
ATOM   5187 C CB   . ASN   B 1 37  ? 47.414 -19.130 -0.191  1.00 10.27 ?  37  ASN   B CB   1 
ATOM   5188 C CG   . ASN   B 1 37  ? 48.255 -19.844 0.827   1.00 10.67 ?  37  ASN   B CG   1 
ATOM   5189 O OD1  . ASN   B 1 37  ? 48.586 -21.025 0.657   1.00 11.46 ?  37  ASN   B OD1  1 
ATOM   5190 N ND2  . ASN   B 1 37  ? 48.596 -19.146 1.905   1.00 10.81 ?  37  ASN   B ND2  1 
ATOM   5191 H H    . ASN   B 1 37  ? 45.447 -18.597 -1.708  1.00 11.96 ?  37  ASN   B H    1 
ATOM   5192 H HA   . ASN   B 1 37  ? 47.030 -20.769 -1.374  1.00 12.37 ?  37  ASN   B HA   1 
ATOM   5193 H HB2  . ASN   B 1 37  ? 48.012 -18.701 -0.813  1.00 12.35 ?  37  ASN   B HB2  1 
ATOM   5194 H HB3  . ASN   B 1 37  ? 46.878 -18.474 0.276   1.00 12.35 ?  37  ASN   B HB3  1 
ATOM   5195 H HD21 . ASN   B 1 37  ? 49.085 -19.507 2.518   1.00 12.99 ?  37  ASN   B HD21 1 
ATOM   5196 H HD22 . ASN   B 1 37  ? 48.351 -18.332 1.989   1.00 12.99 ?  37  ASN   B HD22 1 
ATOM   5197 N N    . ALA   B 1 38  ? 45.871 -21.982 0.400   1.00 10.64 ?  38  ALA   B N    1 
ATOM   5198 C CA   . ALA   B 1 38  ? 45.214 -22.716 1.481   1.00 11.22 ?  38  ALA   B CA   1 
ATOM   5199 C C    . ALA   B 1 38  ? 45.797 -22.243 2.812   1.00 10.65 ?  38  ALA   B C    1 
ATOM   5200 O O    . ALA   B 1 38  ? 46.696 -22.861 3.398   1.00 12.01 ?  38  ALA   B O    1 
ATOM   5201 C CB   . ALA   B 1 38  ? 45.417 -24.212 1.287   1.00 12.32 ?  38  ALA   B CB   1 
ATOM   5202 H H    . ALA   B 1 38  ? 46.514 -22.423 0.035   1.00 12.79 ?  38  ALA   B H    1 
ATOM   5203 H HA   . ALA   B 1 38  ? 44.266 -22.524 1.472   1.00 13.48 ?  38  ALA   B HA   1 
ATOM   5204 H HB1  . ALA   B 1 38  ? 44.973 -24.685 2.016   1.00 14.80 ?  38  ALA   B HB1  1 
ATOM   5205 H HB2  . ALA   B 1 38  ? 45.025 -24.477 0.442   1.00 14.80 ?  38  ALA   B HB2  1 
ATOM   5206 H HB3  . ALA   B 1 38  ? 46.363 -24.411 1.296   1.00 14.80 ?  38  ALA   B HB3  1 
ATOM   5207 N N    . ALA   B 1 39  ? 45.285 -21.098 3.280   1.00 10.67 ?  39  ALA   B N    1 
ATOM   5208 C CA   . ALA   B 1 39  ? 45.838 -20.370 4.412   1.00 11.34 ?  39  ALA   B CA   1 
ATOM   5209 C C    . ALA   B 1 39  ? 45.221 -20.824 5.732   1.00 10.78 ?  39  ALA   B C    1 
ATOM   5210 O O    . ALA   B 1 39  ? 44.179 -21.475 5.778   1.00 12.32 ?  39  ALA   B O    1 
ATOM   5211 C CB   . ALA   B 1 39  ? 45.616 -18.865 4.220   1.00 11.43 ?  39  ALA   B CB   1 
ATOM   5212 H H    . ALA   B 1 39  ? 44.597 -20.711 2.931   1.00 12.82 ?  39  ALA   B H    1 
ATOM   5213 H HA   . ALA   B 1 39  ? 46.794 -20.526 4.451   1.00 13.63 ?  39  ALA   B HA   1 
ATOM   5214 H HB1  . ALA   B 1 39  ? 45.993 -18.391 4.978   1.00 13.73 ?  39  ALA   B HB1  1 
ATOM   5215 H HB2  . ALA   B 1 39  ? 46.063 -18.579 3.402   1.00 13.73 ?  39  ALA   B HB2  1 
ATOM   5216 H HB3  . ALA   B 1 39  ? 44.668 -18.688 4.154   1.00 13.73 ?  39  ALA   B HB3  1 
ATOM   5217 N N    . ASN   B 1 40  ? 45.868 -20.421 6.820   1.00 11.70 ?  40  ASN   B N    1 
ATOM   5218 C CA   . ASN   B 1 40  ? 45.299 -20.469 8.159   1.00 12.33 ?  40  ASN   B CA   1 
ATOM   5219 C C    . ASN   B 1 40  ? 45.102 -19.040 8.685   1.00 12.15 ?  40  ASN   B C    1 
ATOM   5220 O O    . ASN   B 1 40  ? 45.504 -18.057 8.049   1.00 12.06 ?  40  ASN   B O    1 
ATOM   5221 C CB   . ASN   B 1 40  ? 46.161 -21.341 9.090   1.00 13.06 ?  40  ASN   B CB   1 
ATOM   5222 C CG   . ASN   B 1 40  ? 47.608 -20.912 9.128   1.00 14.21 ?  40  ASN   B CG   1 
ATOM   5223 O OD1  . ASN   B 1 40  ? 47.913 -19.724 9.196   1.00 16.76 ?  40  ASN   B OD1  1 
ATOM   5224 N ND2  . ASN   B 1 40  ? 48.516 -21.878 9.098   1.00 14.97 ?  40  ASN   B ND2  1 
ATOM   5225 H H    . ASN   B 1 40  ? 46.670 -20.102 6.807   1.00 14.06 ?  40  ASN   B H    1 
ATOM   5226 H HA   . ASN   B 1 40  ? 44.420 -20.869 8.109   1.00 14.81 ?  40  ASN   B HA   1 
ATOM   5227 H HB2  . ASN   B 1 40  ? 45.796 -21.287 9.991   1.00 15.69 ?  40  ASN   B HB2  1 
ATOM   5228 H HB3  . ASN   B 1 40  ? 46.121 -22.256 8.775   1.00 15.69 ?  40  ASN   B HB3  1 
ATOM   5229 H HD21 . ASN   B 1 40  ? 49.354 -21.685 9.129   1.00 17.98 ?  40  ASN   B HD21 1 
ATOM   5230 H HD22 . ASN   B 1 40  ? 48.269 -22.701 9.046   1.00 17.98 ?  40  ASN   B HD22 1 
ATOM   5231 N N    . VAL   B 1 41  ? 44.439 -18.915 9.839   1.00 12.81 ?  41  VAL   B N    1 
ATOM   5232 C CA   . VAL   B 1 41  ? 43.973 -17.593 10.280  1.00 13.06 ?  41  VAL   B CA   1 
ATOM   5233 C C    . VAL   B 1 41  ? 45.120 -16.631 10.558  1.00 12.86 ?  41  VAL   B C    1 
ATOM   5234 O O    . VAL   B 1 41  ? 44.951 -15.408 10.436  1.00 13.18 ?  41  VAL   B O    1 
ATOM   5235 C CB   . VAL   B 1 41  ? 43.009 -17.666 11.483  1.00 15.12 ?  41  VAL   B CB   1 
ATOM   5236 C CG1  . VAL   B 1 41  ? 41.703 -18.357 11.101  1.00 15.40 ?  41  VAL   B CG1  1 
ATOM   5237 C CG2  . VAL   B 1 41  ? 43.675 -18.317 12.690  1.00 15.49 ?  41  VAL   B CG2  1 
ATOM   5238 H H    . VAL   B 1 41  ? 44.238 -19.562 10.366  1.00 15.38 ?  41  VAL   B H    1 
ATOM   5239 H HA   . VAL   B 1 41  ? 43.460 -17.209 9.552   1.00 15.69 ?  41  VAL   B HA   1 
ATOM   5240 H HB   . VAL   B 1 41  ? 42.776 -16.759 11.743  1.00 18.16 ?  41  VAL   B HB   1 
ATOM   5241 H HG11 . VAL   B 1 41  ? 41.110 -18.367 11.869  1.00 18.49 ?  41  VAL   B HG11 1 
ATOM   5242 H HG12 . VAL   B 1 41  ? 41.287 -17.868 10.371  1.00 18.49 ?  41  VAL   B HG12 1 
ATOM   5243 H HG13 . VAL   B 1 41  ? 41.897 -19.265 10.821  1.00 18.49 ?  41  VAL   B HG13 1 
ATOM   5244 H HG21 . VAL   B 1 41  ? 43.036 -18.373 13.416  1.00 18.60 ?  41  VAL   B HG21 1 
ATOM   5245 H HG22 . VAL   B 1 41  ? 43.969 -19.211 12.441  1.00 18.60 ?  41  VAL   B HG22 1 
ATOM   5246 H HG23 . VAL   B 1 41  ? 44.436 -17.782 12.956  1.00 18.60 ?  41  VAL   B HG23 1 
ATOM   5247 N N    A TYR   B 1 42  ? 46.282 -17.143 10.955  0.42 13.28 ?  42  TYR   B N    1 
ATOM   5248 N N    B TYR   B 1 42  ? 46.281 -17.145 10.951  0.58 13.08 ?  42  TYR   B N    1 
ATOM   5249 C CA   A TYR   B 1 42  ? 47.431 -16.292 11.234  0.42 13.44 ?  42  TYR   B CA   1 
ATOM   5250 C CA   B TYR   B 1 42  ? 47.431 -16.302 11.240  0.58 12.93 ?  42  TYR   B CA   1 
ATOM   5251 C C    A TYR   B 1 42  ? 48.404 -16.211 10.058  0.42 12.87 ?  42  TYR   B C    1 
ATOM   5252 C C    B TYR   B 1 42  ? 48.400 -16.207 10.060  0.58 12.73 ?  42  TYR   B C    1 
ATOM   5253 O O    A TYR   B 1 42  ? 49.494 -15.646 10.203  0.42 13.68 ?  42  TYR   B O    1 
ATOM   5254 O O    B TYR   B 1 42  ? 49.480 -15.619 10.199  0.58 13.86 ?  42  TYR   B O    1 
ATOM   5255 C CB   A TYR   B 1 42  ? 48.120 -16.713 12.539  0.42 14.80 ?  42  TYR   B CB   1 
ATOM   5256 C CB   B TYR   B 1 42  ? 48.111 -16.749 12.542  0.58 14.10 ?  42  TYR   B CB   1 
ATOM   5257 C CG   A TYR   B 1 42  ? 47.541 -16.011 13.758  0.42 14.68 ?  42  TYR   B CG   1 
ATOM   5258 C CG   B TYR   B 1 42  ? 47.622 -15.988 13.775  0.58 12.95 ?  42  TYR   B CG   1 
ATOM   5259 C CD1  A TYR   B 1 42  ? 47.736 -14.647 13.950  0.42 13.77 ?  42  TYR   B CD1  1 
ATOM   5260 C CD1  B TYR   B 1 42  ? 47.893 -14.635 13.914  0.58 12.00 ?  42  TYR   B CD1  1 
ATOM   5261 C CD2  A TYR   B 1 42  ? 46.794 -16.699 14.707  0.42 15.63 ?  42  TYR   B CD2  1 
ATOM   5262 C CD2  B TYR   B 1 42  ? 46.901 -16.612 14.793  0.58 13.45 ?  42  TYR   B CD2  1 
ATOM   5263 C CE1  A TYR   B 1 42  ? 47.214 -13.991 15.048  0.42 14.13 ?  42  TYR   B CE1  1 
ATOM   5264 C CE1  B TYR   B 1 42  ? 47.471 -13.922 15.015  0.58 11.39 ?  42  TYR   B CE1  1 
ATOM   5265 C CE2  A TYR   B 1 42  ? 46.268 -16.052 15.812  0.42 15.58 ?  42  TYR   B CE2  1 
ATOM   5266 C CE2  B TYR   B 1 42  ? 46.475 -15.900 15.918  0.58 12.64 ?  42  TYR   B CE2  1 
ATOM   5267 C CZ   A TYR   B 1 42  ? 46.482 -14.698 15.977  0.42 15.26 ?  42  TYR   B CZ   1 
ATOM   5268 C CZ   B TYR   B 1 42  ? 46.763 -14.549 16.018  0.58 11.85 ?  42  TYR   B CZ   1 
ATOM   5269 O OH   A TYR   B 1 42  ? 45.958 -14.050 17.074  0.42 16.72 ?  42  TYR   B OH   1 
ATOM   5270 O OH   B TYR   B 1 42  ? 46.377 -13.799 17.118  0.58 12.67 ?  42  TYR   B OH   1 
ATOM   5271 H H    A TYR   B 1 42  ? 46.426 -17.989 11.063  0.42 15.96 ?  42  TYR   B H    1 
ATOM   5272 H H    B TYR   B 1 42  ? 46.425 -17.993 11.051  0.58 15.72 ?  42  TYR   B H    1 
ATOM   5273 H HA   A TYR   B 1 42  ? 47.095 -15.399 11.378  0.42 16.15 ?  42  TYR   B HA   1 
ATOM   5274 H HA   B TYR   B 1 42  ? 47.097 -15.409 11.393  0.58 15.53 ?  42  TYR   B HA   1 
ATOM   5275 H HB2  A TYR   B 1 42  ? 48.010 -17.668 12.666  0.42 17.77 ?  42  TYR   B HB2  1 
ATOM   5276 H HB2  B TYR   B 1 42  ? 47.932 -17.689 12.690  0.58 16.94 ?  42  TYR   B HB2  1 
ATOM   5277 H HB3  A TYR   B 1 42  ? 49.060 -16.489 12.484  0.42 17.77 ?  42  TYR   B HB3  1 
ATOM   5278 H HB3  B TYR   B 1 42  ? 49.065 -16.601 12.462  0.58 16.94 ?  42  TYR   B HB3  1 
ATOM   5279 H HD1  A TYR   B 1 42  ? 48.233 -14.165 13.325  0.42 16.54 ?  42  TYR   B HD1  1 
ATOM   5280 H HD1  B TYR   B 1 42  ? 48.381 -14.195 13.249  0.58 14.42 ?  42  TYR   B HD1  1 
ATOM   5281 H HD2  A TYR   B 1 42  ? 46.648 -17.610 14.601  0.42 18.78 ?  42  TYR   B HD2  1 
ATOM   5282 H HD2  B TYR   B 1 42  ? 46.706 -17.517 14.725  0.58 16.16 ?  42  TYR   B HD2  1 
ATOM   5283 H HE1  A TYR   B 1 42  ? 47.361 -13.076 15.161  0.42 16.98 ?  42  TYR   B HE1  1 
ATOM   5284 H HE1  B TYR   B 1 42  ? 47.680 -13.013 15.090  0.58 13.68 ?  42  TYR   B HE1  1 
ATOM   5285 H HE2  A TYR   B 1 42  ? 45.773 -16.523 16.442  0.42 18.72 ?  42  TYR   B HE2  1 
ATOM   5286 H HE2  B TYR   B 1 42  ? 45.995 -16.325 16.590  0.58 15.19 ?  42  TYR   B HE2  1 
ATOM   5287 H HH   A TYR   B 1 42  ? 46.166 -13.233 17.056  0.42 20.09 ?  42  TYR   B HH   1 
ATOM   5288 H HH   B TYR   B 1 42  ? 46.625 -13.004 17.039  0.58 15.22 ?  42  TYR   B HH   1 
ATOM   5289 N N    . LEU   B 1 43  ? 48.018 -16.734 8.895   1.00 11.96 ?  43  LEU   B N    1 
ATOM   5290 C CA   . LEU   B 1 43  ? 48.835 -16.650 7.685   1.00 11.79 ?  43  LEU   B CA   1 
ATOM   5291 C C    . LEU   B 1 43  ? 50.250 -17.153 7.936   1.00 12.14 ?  43  LEU   B C    1 
ATOM   5292 O O    . LEU   B 1 43  ? 51.226 -16.559 7.479   1.00 13.15 ?  43  LEU   B O    1 
ATOM   5293 C CB   . LEU   B 1 43  ? 48.855 -15.239 7.090   1.00 12.05 ?  43  LEU   B CB   1 
ATOM   5294 C CG   . LEU   B 1 43  ? 47.505 -14.629 6.706   1.00 12.49 ?  43  LEU   B CG   1 
ATOM   5295 C CD1  . LEU   B 1 43  ? 47.716 -13.231 6.131   1.00 13.96 ?  43  LEU   B CD1  1 
ATOM   5296 C CD2  . LEU   B 1 43  ? 46.742 -15.502 5.733   1.00 13.10 ?  43  LEU   B CD2  1 
ATOM   5297 H H    A LEU   B 1 43  ? 47.283 -17.169 8.783   0.42 14.36 ?  43  LEU   B H    1 
ATOM   5298 H H    B LEU   B 1 43  ? 47.281 -17.165 8.781   0.58 14.36 ?  43  LEU   B H    1 
ATOM   5299 H HA   . LEU   B 1 43  ? 48.440 -17.234 7.020   1.00 14.17 ?  43  LEU   B HA   1 
ATOM   5300 H HB2  . LEU   B 1 43  ? 49.268 -14.647 7.733   1.00 14.47 ?  43  LEU   B HB2  1 
ATOM   5301 H HB3  . LEU   B 1 43  ? 49.393 -15.267 6.283   1.00 14.47 ?  43  LEU   B HB3  1 
ATOM   5302 H HG   . LEU   B 1 43  ? 46.969 -14.538 7.507   1.00 15.01 ?  43  LEU   B HG   1 
ATOM   5303 H HD11 . LEU   B 1 43  ? 46.852 -12.852 5.894   1.00 16.77 ?  43  LEU   B HD11 1 
ATOM   5304 H HD12 . LEU   B 1 43  ? 48.145 -12.672 6.801   1.00 16.77 ?  43  LEU   B HD12 1 
ATOM   5305 H HD13 . LEU   B 1 43  ? 48.277 -13.289 5.343   1.00 16.77 ?  43  LEU   B HD13 1 
ATOM   5306 H HD21 . LEU   B 1 43  ? 45.944 -15.034 5.446   1.00 15.73 ?  43  LEU   B HD21 1 
ATOM   5307 H HD22 . LEU   B 1 43  ? 47.307 -15.695 4.968   1.00 15.73 ?  43  LEU   B HD22 1 
ATOM   5308 H HD23 . LEU   B 1 43  ? 46.497 -16.330 6.178   1.00 15.73 ?  43  LEU   B HD23 1 
ATOM   5309 N N    . LYS   B 1 44  ? 50.355 -18.279 8.644   1.00 12.18 ?  44  LYS   B N    1 
ATOM   5310 C CA   . LYS   B 1 44  ? 51.624 -18.954 8.894   1.00 12.73 ?  44  LYS   B CA   1 
ATOM   5311 C C    . LYS   B 1 44  ? 51.752 -20.076 7.876   1.00 12.38 ?  44  LYS   B C    1 
ATOM   5312 O O    . LYS   B 1 44  ? 51.060 -21.093 7.958   1.00 13.63 ?  44  LYS   B O    1 
ATOM   5313 C CB   . LYS   B 1 44  ? 51.662 -19.457 10.333  1.00 14.12 ?  44  LYS   B CB   1 
ATOM   5314 C CG   . LYS   B 1 44  ? 51.883 -18.334 11.335  1.00 16.56 ?  44  LYS   B CG   1 
ATOM   5315 C CD   . LYS   B 1 44  ? 53.142 -17.547 10.925  1.00 20.78 ?  44  LYS   B CD   1 
ATOM   5316 C CE   . LYS   B 1 44  ? 53.523 -16.427 11.837  1.00 25.00 ?  44  LYS   B CE   1 
ATOM   5317 N NZ   . LYS   B 1 44  ? 54.832 -15.824 11.469  1.00 26.08 ?  44  LYS   B NZ   1 
ATOM   5318 H H    . LYS   B 1 44  ? 49.680 -18.675 9.006   1.00 14.64 ?  44  LYS   B H    1 
ATOM   5319 H HA   . LYS   B 1 44  ? 52.354 -18.352 8.709   1.00 15.29 ?  44  LYS   B HA   1 
ATOM   5320 H HB2  . LYS   B 1 44  ? 50.806 -19.882 10.539  1.00 16.96 ?  44  LYS   B HB2  1 
ATOM   5321 H HB3  . LYS   B 1 44  ? 52.377 -20.102 10.427  1.00 16.96 ?  44  LYS   B HB3  1 
ATOM   5322 H HG2  . LYS   B 1 44  ? 51.125 -17.735 11.335  1.00 19.89 ?  44  LYS   B HG2  1 
ATOM   5323 H HG3  . LYS   B 1 44  ? 52.029 -18.712 12.220  1.00 19.89 ?  44  LYS   B HG3  1 
ATOM   5324 H HD2  . LYS   B 1 44  ? 53.883 -18.182 10.849  1.00 24.95 ?  44  LYS   B HD2  1 
ATOM   5325 H HD3  . LYS   B 1 44  ? 52.985 -17.137 10.060  1.00 24.95 ?  44  LYS   B HD3  1 
ATOM   5326 H HE2  . LYS   B 1 44  ? 52.839 -15.742 11.800  1.00 30.01 ?  44  LYS   B HE2  1 
ATOM   5327 H HE3  . LYS   B 1 44  ? 53.620 -16.781 12.711  1.00 30.01 ?  44  LYS   B HE3  1 
ATOM   5328 H HZ1  . LYS   B 1 44  ? 55.025 -15.160 12.027  1.00 31.32 ?  44  LYS   B HZ1  1 
ATOM   5329 H HZ2  . LYS   B 1 44  ? 55.477 -16.439 11.518  1.00 31.32 ?  44  LYS   B HZ2  1 
ATOM   5330 H HZ3  . LYS   B 1 44  ? 54.807 -15.505 10.637  1.00 31.32 ?  44  LYS   B HZ3  1 
ATOM   5331 N N    . HIS   B 1 45  ? 52.600 -19.855 6.875   1.00 12.05 ?  45  HIS   B N    1 
ATOM   5332 C CA   . HIS   B 1 45  ? 52.624 -20.686 5.674   1.00 12.39 ?  45  HIS   B CA   1 
ATOM   5333 C C    . HIS   B 1 45  ? 53.645 -21.811 5.835   1.00 14.35 ?  45  HIS   B C    1 
ATOM   5334 O O    . HIS   B 1 45  ? 54.712 -21.818 5.230   1.00 17.27 ?  45  HIS   B O    1 
ATOM   5335 C CB   . HIS   B 1 45  ? 52.941 -19.831 4.460   1.00 12.31 ?  45  HIS   B CB   1 
ATOM   5336 C CG   . HIS   B 1 45  ? 52.068 -18.634 4.346   1.00 12.03 ?  45  HIS   B CG   1 
ATOM   5337 N ND1  . HIS   B 1 45  ? 50.692 -18.714 4.311   1.00 12.26 ?  45  HIS   B ND1  1 
ATOM   5338 C CD2  . HIS   B 1 45  ? 52.385 -17.325 4.270   1.00 12.85 ?  45  HIS   B CD2  1 
ATOM   5339 C CE1  . HIS   B 1 45  ? 50.204 -17.489 4.214   1.00 12.33 ?  45  HIS   B CE1  1 
ATOM   5340 N NE2  . HIS   B 1 45  ? 51.208 -16.631 4.180   1.00 12.53 ?  45  HIS   B NE2  1 
ATOM   5341 H H    . HIS   B 1 45  ? 53.173 -19.213 6.862   1.00 14.48 ?  45  HIS   B H    1 
ATOM   5342 H HA   . HIS   B 1 45  ? 51.743 -21.082 5.535   1.00 14.88 ?  45  HIS   B HA   1 
ATOM   5343 H HB2  . HIS   B 1 45  ? 53.864 -19.533 4.514   1.00 14.78 ?  45  HIS   B HB2  1 
ATOM   5344 H HB3  . HIS   B 1 45  ? 52.825 -20.370 3.651   1.00 14.78 ?  45  HIS   B HB3  1 
ATOM   5345 H HD2  . HIS   B 1 45  ? 53.241 -16.956 4.278   1.00 15.44 ?  45  HIS   B HD2  1 
ATOM   5346 H HE1  . HIS   B 1 45  ? 49.301 -17.276 4.163   1.00 14.81 ?  45  HIS   B HE1  1 
ATOM   5347 H HE2  . HIS   B 1 45  ? 51.128 -15.776 4.132   1.00 15.06 ?  45  HIS   B HE2  1 
ATOM   5348 N N    A GLY   B 1 46  ? 53.278 -22.787 6.660   0.42 15.69 ?  46  GLY   B N    1 
ATOM   5349 N N    B GLY   B 1 46  ? 53.287 -22.779 6.670   0.58 15.32 ?  46  GLY   B N    1 
ATOM   5350 C CA   A GLY   B 1 46  ? 54.210 -23.828 7.051   0.42 17.54 ?  46  GLY   B CA   1 
ATOM   5351 C CA   B GLY   B 1 46  ? 54.222 -23.830 7.020   0.58 17.16 ?  46  GLY   B CA   1 
ATOM   5352 C C    A GLY   B 1 46  ? 54.263 -25.062 6.170   0.42 19.41 ?  46  GLY   B C    1 
ATOM   5353 C C    B GLY   B 1 46  ? 54.258 -25.008 6.067   0.58 19.37 ?  46  GLY   B C    1 
ATOM   5354 O O    A GLY   B 1 46  ? 55.353 -25.514 5.803   0.42 21.97 ?  46  GLY   B O    1 
ATOM   5355 O O    B GLY   B 1 46  ? 55.315 -25.352 5.528   0.58 22.32 ?  46  GLY   B O    1 
ATOM   5356 H H    A GLY   B 1 46  ? 52.497 -22.852 7.022   0.42 18.84 ?  46  GLY   B H    1 
ATOM   5357 H H    B GLY   B 1 46  ? 52.516 -22.835 7.056   0.58 18.40 ?  46  GLY   B H    1 
ATOM   5358 H HA2  A GLY   B 1 46  ? 55.101 -23.445 7.081   0.42 21.06 ?  46  GLY   B HA2  1 
ATOM   5359 H HA2  B GLY   B 1 46  ? 55.114 -23.449 7.064   0.58 20.61 ?  46  GLY   B HA2  1 
ATOM   5360 H HA3  A GLY   B 1 46  ? 53.983 -24.123 7.945   0.42 21.06 ?  46  GLY   B HA3  1 
ATOM   5361 H HA3  B GLY   B 1 46  ? 53.998 -24.163 7.903   0.58 20.61 ?  46  GLY   B HA3  1 
ATOM   5362 N N    . GLY   B 1 47  ? 53.109 -25.637 5.836   1.00 19.10 ?  47  GLY   B N    1 
ATOM   5363 C CA   . GLY   B 1 47  ? 53.059 -26.910 5.144   1.00 16.26 ?  47  GLY   B CA   1 
ATOM   5364 C C    . GLY   B 1 47  ? 52.126 -26.884 3.950   1.00 14.56 ?  47  GLY   B C    1 
ATOM   5365 O O    . GLY   B 1 47  ? 51.475 -25.877 3.667   1.00 14.61 ?  47  GLY   B O    1 
ATOM   5366 H H    A GLY   B 1 47  ? 52.334 -25.310 6.017   0.42 22.94 ?  47  GLY   B H    1 
ATOM   5367 H H    B GLY   B 1 47  ? 52.338 -25.342 6.078   0.58 22.94 ?  47  GLY   B H    1 
ATOM   5368 H HA2  . GLY   B 1 47  ? 53.947 -27.152 4.831   1.00 19.53 ?  47  GLY   B HA2  1 
ATOM   5369 H HA3  . GLY   B 1 47  ? 52.755 -27.597 5.755   1.00 19.53 ?  47  GLY   B HA3  1 
ATOM   5370 N N    . GLY   B 1 48  ? 52.076 -28.020 3.262   1.00 13.89 ?  48  GLY   B N    1 
ATOM   5371 C CA   . GLY   B 1 48  ? 51.153 -28.165 2.156   1.00 13.93 ?  48  GLY   B CA   1 
ATOM   5372 C C    . GLY   B 1 48  ? 51.298 -27.060 1.134   1.00 12.88 ?  48  GLY   B C    1 
ATOM   5373 O O    . GLY   B 1 48  ? 52.400 -26.593 0.829   1.00 13.44 ?  48  GLY   B O    1 
ATOM   5374 H H    . GLY   B 1 48  ? 52.558 -28.710 3.416   1.00 16.68 ?  48  GLY   B H    1 
ATOM   5375 H HA2  . GLY   B 1 48  ? 51.310 -29.016 1.710   1.00 16.74 ?  48  GLY   B HA2  1 
ATOM   5376 H HA3  . GLY   B 1 48  ? 50.240 -28.159 2.483   1.00 16.74 ?  48  GLY   B HA3  1 
ATOM   5377 N N    . VAL   B 1 49  ? 50.159 -26.633 0.593   1.00 12.74 ?  49  VAL   B N    1 
ATOM   5378 C CA   . VAL   B 1 49  ? 50.149 -25.602 -0.445  1.00 12.64 ?  49  VAL   B CA   1 
ATOM   5379 C C    . VAL   B 1 49  ? 50.815 -24.321 0.048   1.00 11.76 ?  49  VAL   B C    1 
ATOM   5380 O O    . VAL   B 1 49  ? 51.601 -23.698 -0.676  1.00 12.37 ?  49  VAL   B O    1 
ATOM   5381 C CB   . VAL   B 1 49  ? 48.707 -25.341 -0.932  1.00 13.70 ?  49  VAL   B CB   1 
ATOM   5382 C CG1  . VAL   B 1 49  ? 48.634 -24.089 -1.810  1.00 13.96 ?  49  VAL   B CG1  1 
ATOM   5383 C CG2  . VAL   B 1 49  ? 48.184 -26.560 -1.679  1.00 15.41 ?  49  VAL   B CG2  1 
ATOM   5384 H H    . VAL   B 1 49  ? 49.371 -26.915 0.813   1.00 15.30 ?  49  VAL   B H    1 
ATOM   5385 H HA   . VAL   B 1 49  ? 50.653 -25.922 -1.203  1.00 15.19 ?  49  VAL   B HA   1 
ATOM   5386 H HB   . VAL   B 1 49  ? 48.131 -25.194 -0.163  1.00 16.45 ?  49  VAL   B HB   1 
ATOM   5387 H HG11 . VAL   B 1 49  ? 47.796 -24.093 -2.298  1.00 16.77 ?  49  VAL   B HG11 1 
ATOM   5388 H HG12 . VAL   B 1 49  ? 48.678 -23.299 -1.243  1.00 16.77 ?  49  VAL   B HG12 1 
ATOM   5389 H HG13 . VAL   B 1 49  ? 49.378 -24.093 -2.429  1.00 16.77 ?  49  VAL   B HG13 1 
ATOM   5390 H HG21 . VAL   B 1 49  ? 47.281 -26.383 -1.988  1.00 18.51 ?  49  VAL   B HG21 1 
ATOM   5391 H HG22 . VAL   B 1 49  ? 48.763 -26.736 -2.439  1.00 18.51 ?  49  VAL   B HG22 1 
ATOM   5392 H HG23 . VAL   B 1 49  ? 48.185 -27.322 -1.080  1.00 18.51 ?  49  VAL   B HG23 1 
ATOM   5393 N N    . ALA   B 1 50  ? 50.467 -23.876 1.258   1.00 11.45 ?  50  ALA   B N    1 
ATOM   5394 C CA   . ALA   B 1 50  ? 50.985 -22.598 1.742   1.00 11.39 ?  50  ALA   B CA   1 
ATOM   5395 C C    . ALA   B 1 50  ? 52.503 -22.628 1.855   1.00 11.46 ?  50  ALA   B C    1 
ATOM   5396 O O    . ALA   B 1 50  ? 53.182 -21.666 1.479   1.00 11.76 ?  50  ALA   B O    1 
ATOM   5397 C CB   . ALA   B 1 50  ? 50.343 -22.238 3.077   1.00 12.01 ?  50  ALA   B CB   1 
ATOM   5398 H H    . ALA   B 1 50  ? 49.949 -24.285 1.810   1.00 13.76 ?  50  ALA   B H    1 
ATOM   5399 H HA   . ALA   B 1 50  ? 50.756 -21.903 1.106   1.00 13.68 ?  50  ALA   B HA   1 
ATOM   5400 H HB1  . ALA   B 1 50  ? 50.698 -21.382 3.381   1.00 14.43 ?  50  ALA   B HB1  1 
ATOM   5401 H HB2  . ALA   B 1 50  ? 49.383 -22.168 2.961   1.00 14.43 ?  50  ALA   B HB2  1 
ATOM   5402 H HB3  . ALA   B 1 50  ? 50.550 -22.925 3.728   1.00 14.43 ?  50  ALA   B HB3  1 
ATOM   5403 N N    . GLY   B 1 51  ? 53.054 -23.726 2.362   1.00 12.15 ?  51  GLY   B N    1 
ATOM   5404 C CA   . GLY   B 1 51  ? 54.496 -23.825 2.437   1.00 12.85 ?  51  GLY   B CA   1 
ATOM   5405 C C    . GLY   B 1 51  ? 55.151 -23.783 1.072   1.00 12.41 ?  51  GLY   B C    1 
ATOM   5406 O O    . GLY   B 1 51  ? 56.198 -23.151 0.892   1.00 13.45 ?  51  GLY   B O    1 
ATOM   5407 H H    . GLY   B 1 51  ? 52.628 -24.410 2.664   1.00 14.59 ?  51  GLY   B H    1 
ATOM   5408 H HA2  . GLY   B 1 51  ? 54.848 -23.089 2.966   1.00 15.44 ?  51  GLY   B HA2  1 
ATOM   5409 H HA3  . GLY   B 1 51  ? 54.747 -24.657 2.868   1.00 15.44 ?  51  GLY   B HA3  1 
ATOM   5410 N N    . ALA   B 1 52  ? 54.547 -24.453 0.089   1.00 11.95 ?  52  ALA   B N    1 
ATOM   5411 C CA   . ALA   B 1 52  ? 55.120 -24.461 -1.252  1.00 12.29 ?  52  ALA   B CA   1 
ATOM   5412 C C    . ALA   B 1 52  ? 55.042 -23.080 -1.904  1.00 11.66 ?  52  ALA   B C    1 
ATOM   5413 O O    . ALA   B 1 52  ? 56.011 -22.627 -2.533  1.00 12.93 ?  52  ALA   B O    1 
ATOM   5414 C CB   . ALA   B 1 52  ? 54.420 -25.507 -2.111  1.00 12.83 ?  52  ALA   B CB   1 
ATOM   5415 H H    . ALA   B 1 52  ? 53.813 -24.897 0.171   1.00 14.36 ?  52  ALA   B H    1 
ATOM   5416 H HA   . ALA   B 1 52  ? 56.057 -24.704 -1.187  1.00 14.76 ?  52  ALA   B HA   1 
ATOM   5417 H HB1  . ALA   B 1 52  ? 54.819 -25.501 -2.998  1.00 15.42 ?  52  ALA   B HB1  1 
ATOM   5418 H HB2  . ALA   B 1 52  ? 54.541 -26.379 -1.704  1.00 15.42 ?  52  ALA   B HB2  1 
ATOM   5419 H HB3  . ALA   B 1 52  ? 53.480 -25.292 -2.169  1.00 15.42 ?  52  ALA   B HB3  1 
ATOM   5420 N N    . LEU   B 1 53  ? 53.897 -22.401 -1.789  1.00 11.86 ?  53  LEU   B N    1 
ATOM   5421 C CA   . LEU   B 1 53  ? 53.792 -21.062 -2.363  1.00 11.86 ?  53  LEU   B CA   1 
ATOM   5422 C C    . LEU   B 1 53  ? 54.794 -20.116 -1.708  1.00 11.72 ?  53  LEU   B C    1 
ATOM   5423 O O    . LEU   B 1 53  ? 55.500 -19.365 -2.392  1.00 12.82 ?  53  LEU   B O    1 
ATOM   5424 C CB   . LEU   B 1 53  ? 52.364 -20.519 -2.225  1.00 12.36 ?  53  LEU   B CB   1 
ATOM   5425 C CG   . LEU   B 1 53  ? 51.224 -21.254 -2.944  1.00 12.67 ?  53  LEU   B CG   1 
ATOM   5426 C CD1  . LEU   B 1 53  ? 49.878 -20.635 -2.600  1.00 14.35 ?  53  LEU   B CD1  1 
ATOM   5427 C CD2  . LEU   B 1 53  ? 51.434 -21.274 -4.464  1.00 14.31 ?  53  LEU   B CD2  1 
ATOM   5428 H H    . LEU   B 1 53  ? 53.192 -22.682 -1.387  1.00 14.25 ?  53  LEU   B H    1 
ATOM   5429 H HA   . LEU   B 1 53  ? 54.008 -21.118 -3.312  1.00 14.25 ?  53  LEU   B HA   1 
ATOM   5430 H HB2  . LEU   B 1 53  ? 52.143 -20.521 -1.288  1.00 14.85 ?  53  LEU   B HB2  1 
ATOM   5431 H HB3  . LEU   B 1 53  ? 52.364 -19.616 -2.561  1.00 14.85 ?  53  LEU   B HB3  1 
ATOM   5432 H HG   . LEU   B 1 53  ? 51.205 -22.179 -2.645  1.00 15.22 ?  53  LEU   B HG   1 
ATOM   5433 H HD11 . LEU   B 1 53  ? 49.177 -21.120 -3.068  1.00 17.24 ?  53  LEU   B HD11 1 
ATOM   5434 H HD12 . LEU   B 1 53  ? 49.740 -20.701 -1.643  1.00 17.24 ?  53  LEU   B HD12 1 
ATOM   5435 H HD13 . LEU   B 1 53  ? 49.878 -19.707 -2.875  1.00 17.24 ?  53  LEU   B HD13 1 
ATOM   5436 H HD21 . LEU   B 1 53  ? 50.770 -21.861 -4.872  1.00 17.19 ?  53  LEU   B HD21 1 
ATOM   5437 H HD22 . LEU   B 1 53  ? 51.336 -20.379 -4.815  1.00 17.19 ?  53  LEU   B HD22 1 
ATOM   5438 H HD23 . LEU   B 1 53  ? 52.323 -21.615 -4.664  1.00 17.19 ?  53  LEU   B HD23 1 
ATOM   5439 N N    . ASN   B 1 54  ? 54.874 -20.147 -0.380  1.00 11.63 ?  54  ASN   B N    1 
ATOM   5440 C CA   . ASN   B 1 54  ? 55.787 -19.237 0.300   1.00 11.79 ?  54  ASN   B CA   1 
ATOM   5441 C C    . ASN   B 1 54  ? 57.234 -19.517 -0.086  1.00 12.49 ?  54  ASN   B C    1 
ATOM   5442 O O    . ASN   B 1 54  ? 58.010 -18.584 -0.329  1.00 12.59 ?  54  ASN   B O    1 
ATOM   5443 C CB   . ASN   B 1 54  ? 55.605 -19.303 1.808   1.00 12.95 ?  54  ASN   B CB   1 
ATOM   5444 C CG   . ASN   B 1 54  ? 56.579 -18.386 2.519   1.00 12.88 ?  54  ASN   B CG   1 
ATOM   5445 O OD1  . ASN   B 1 54  ? 56.607 -17.175 2.266   1.00 13.18 ?  54  ASN   B OD1  1 
ATOM   5446 N ND2  . ASN   B 1 54  ? 57.410 -18.954 3.385   1.00 15.00 ?  54  ASN   B ND2  1 
ATOM   5447 H H    . ASN   B 1 54  ? 54.420 -20.667 0.133   1.00 13.97 ?  54  ASN   B H    1 
ATOM   5448 H HA   . ASN   B 1 54  ? 55.576 -18.331 0.018   1.00 14.16 ?  54  ASN   B HA   1 
ATOM   5449 H HB2  . ASN   B 1 54  ? 54.703 -19.023 2.036   1.00 15.55 ?  54  ASN   B HB2  1 
ATOM   5450 H HB3  . ASN   B 1 54  ? 55.763 -20.207 2.112   1.00 15.55 ?  54  ASN   B HB3  1 
ATOM   5451 H HD21 . ASN   B 1 54  ? 57.989 -18.476 3.810   1.00 18.01 ?  54  ASN   B HD21 1 
ATOM   5452 H HD22 . ASN   B 1 54  ? 57.375 -19.803 3.528   1.00 18.01 ?  54  ASN   B HD22 1 
ATOM   5453 N N    . LYS   B 1 55  ? 57.620 -20.794 -0.148  1.00 13.42 ?  55  LYS   B N    1 
ATOM   5454 C CA   . LYS   B 1 55  ? 58.977 -21.139 -0.558  1.00 14.16 ?  55  LYS   B CA   1 
ATOM   5455 C C    . LYS   B 1 55  ? 59.281 -20.602 -1.952  1.00 14.24 ?  55  LYS   B C    1 
ATOM   5456 O O    . LYS   B 1 55  ? 60.389 -20.106 -2.206  1.00 14.90 ?  55  LYS   B O    1 
ATOM   5457 C CB   . LYS   B 1 55  ? 59.173 -22.656 -0.499  1.00 15.94 ?  55  LYS   B CB   1 
ATOM   5458 C CG   . LYS   B 1 55  ? 60.537 -23.128 -0.966  1.00 20.16 ?  55  LYS   B CG   1 
ATOM   5459 C CD   . LYS   B 1 55  ? 60.711 -24.630 -0.771  1.00 24.43 ?  55  LYS   B CD   1 
ATOM   5460 C CE   . LYS   B 1 55  ? 60.811 -25.009 0.708   1.00 27.78 ?  55  LYS   B CE   1 
ATOM   5461 N NZ   . LYS   B 1 55  ? 61.159 -26.439 0.903   1.00 29.80 ?  55  LYS   B NZ   1 
ATOM   5462 H H    . LYS   B 1 55  ? 57.117 -21.468 0.035   1.00 16.13 ?  55  LYS   B H    1 
ATOM   5463 H HA   . LYS   B 1 55  ? 59.601 -20.729 0.055   1.00 17.00 ?  55  LYS   B HA   1 
ATOM   5464 H HB2  . LYS   B 1 55  ? 59.056 -22.939 0.419   1.00 19.14 ?  55  LYS   B HB2  1 
ATOM   5465 H HB3  . LYS   B 1 55  ? 58.506 -23.077 -1.062  1.00 19.14 ?  55  LYS   B HB3  1 
ATOM   5466 H HG2  . LYS   B 1 55  ? 60.637 -22.932 -1.912  1.00 24.21 ?  55  LYS   B HG2  1 
ATOM   5467 H HG3  . LYS   B 1 55  ? 61.224 -22.672 -0.456  1.00 24.21 ?  55  LYS   B HG3  1 
ATOM   5468 H HD2  . LYS   B 1 55  ? 59.947 -25.093 -1.150  1.00 29.33 ?  55  LYS   B HD2  1 
ATOM   5469 H HD3  . LYS   B 1 55  ? 61.527 -24.917 -1.212  1.00 29.33 ?  55  LYS   B HD3  1 
ATOM   5470 H HE2  . LYS   B 1 55  ? 61.500 -24.464 1.125   1.00 33.35 ?  55  LYS   B HE2  1 
ATOM   5471 H HE3  . LYS   B 1 55  ? 59.955 -24.841 1.135   1.00 33.35 ?  55  LYS   B HE3  1 
ATOM   5472 H HZ1  . LYS   B 1 55  ? 61.196 -26.625 1.772   1.00 35.78 ?  55  LYS   B HZ1  1 
ATOM   5473 H HZ2  . LYS   B 1 55  ? 60.542 -26.954 0.522   1.00 35.78 ?  55  LYS   B HZ2  1 
ATOM   5474 H HZ3  . LYS   B 1 55  ? 61.949 -26.611 0.535   1.00 35.78 ?  55  LYS   B HZ3  1 
ATOM   5475 N N    . ALA   B 1 56  ? 58.313 -20.691 -2.874  1.00 13.42 ?  56  ALA   B N    1 
ATOM   5476 C CA   . ALA   B 1 56  ? 58.543 -20.198 -4.226  1.00 14.11 ?  56  ALA   B CA   1 
ATOM   5477 C C    . ALA   B 1 56  ? 58.816 -18.703 -4.231  1.00 14.02 ?  56  ALA   B C    1 
ATOM   5478 O O    . ALA   B 1 56  ? 59.548 -18.212 -5.099  1.00 15.18 ?  56  ALA   B O    1 
ATOM   5479 C CB   . ALA   B 1 56  ? 57.359 -20.538 -5.133  1.00 15.52 ?  56  ALA   B CB   1 
ATOM   5480 H H    . ALA   B 1 56  ? 57.523 -21.017 -2.744  1.00 16.12 ?  56  ALA   B H    1 
ATOM   5481 H HA   . ALA   B 1 56  ? 59.329 -20.630 -4.586  1.00 16.94 ?  56  ALA   B HA   1 
ATOM   5482 H HB1  . ALA   B 1 56  ? 57.543 -20.202 -6.031  1.00 18.64 ?  56  ALA   B HB1  1 
ATOM   5483 H HB2  . ALA   B 1 56  ? 57.255 -21.501 -5.163  1.00 18.64 ?  56  ALA   B HB2  1 
ATOM   5484 H HB3  . ALA   B 1 56  ? 56.559 -20.123 -4.786  1.00 18.64 ?  56  ALA   B HB3  1 
ATOM   5485 N N    . THR   B 1 57  ? 58.244 -17.964 -3.274  1.00 13.46 ?  57  THR   B N    1 
ATOM   5486 C CA   . THR   B 1 57  ? 58.485 -16.530 -3.161  1.00 13.77 ?  57  THR   B CA   1 
ATOM   5487 C C    . THR   B 1 57  ? 59.728 -16.201 -2.345  1.00 14.64 ?  57  THR   B C    1 
ATOM   5488 O O    . THR   B 1 57  ? 59.966 -15.023 -2.056  1.00 14.65 ?  57  THR   B O    1 
ATOM   5489 C CB   . THR   B 1 57  ? 57.286 -15.796 -2.533  1.00 12.93 ?  57  THR   B CB   1 
ATOM   5490 O OG1  . THR   B 1 57  ? 57.254 -16.007 -1.110  1.00 13.35 ?  57  THR   B OG1  1 
ATOM   5491 C CG2  . THR   B 1 57  ? 55.973 -16.213 -3.182  1.00 12.67 ?  57  THR   B CG2  1 
ATOM   5492 H H    . THR   B 1 57  ? 57.700 -18.270 -2.679  1.00 16.16 ?  57  THR   B H    1 
ATOM   5493 H HA   . THR   B 1 57  ? 58.609 -16.164 -4.051  1.00 16.54 ?  57  THR   B HA   1 
ATOM   5494 H HB   . THR   B 1 57  ? 57.391 -14.844 -2.693  1.00 15.53 ?  57  THR   B HB   1 
ATOM   5495 H HG1  . THR   B 1 57  ? 57.184 -16.832 -0.946  1.00 16.04 ?  57  THR   B HG1  1 
ATOM   5496 H HG21 . THR   B 1 57  ? 55.242 -15.675 -2.843  1.00 15.23 ?  57  THR   B HG21 1 
ATOM   5497 H HG22 . THR   B 1 57  ? 56.025 -16.100 -4.146  1.00 15.23 ?  57  THR   B HG22 1 
ATOM   5498 H HG23 . THR   B 1 57  ? 55.786 -17.147 -2.992  1.00 15.23 ?  57  THR   B HG23 1 
ATOM   5499 N N    . ASN   B 1 58  ? 60.513 -17.205 -1.960  1.00 16.04 ?  58  ASN   B N    1 
ATOM   5500 C CA   . ASN   B 1 58  ? 61.705 -16.988 -1.142  1.00 18.99 ?  58  ASN   B CA   1 
ATOM   5501 C C    . ASN   B 1 58  ? 61.362 -16.259 0.157   1.00 16.23 ?  58  ASN   B C    1 
ATOM   5502 O O    . ASN   B 1 58  ? 62.093 -15.372 0.612   1.00 17.42 ?  58  ASN   B O    1 
ATOM   5503 C CB   . ASN   B 1 58  ? 62.799 -16.250 -1.918  1.00 27.90 ?  58  ASN   B CB   1 
ATOM   5504 C CG   . ASN   B 1 58  ? 64.162 -16.381 -1.266  1.00 38.68 ?  58  ASN   B CG   1 
ATOM   5505 O OD1  . ASN   B 1 58  ? 64.500 -17.431 -0.719  1.00 41.78 ?  58  ASN   B OD1  1 
ATOM   5506 N ND2  . ASN   B 1 58  ? 64.949 -15.313 -1.313  1.00 45.62 ?  58  ASN   B ND2  1 
ATOM   5507 H H    . ASN   B 1 58  ? 60.373 -18.034 -2.168  1.00 19.27 ?  58  ASN   B H    1 
ATOM   5508 H HA   . ASN   B 1 58  ? 62.064 -17.864 -0.914  1.00 22.81 ?  58  ASN   B HA   1 
ATOM   5509 H HB2  . ASN   B 1 58  ? 62.860 -16.614 -2.818  1.00 33.50 ?  58  ASN   B HB2  1 
ATOM   5510 H HB3  . ASN   B 1 58  ? 62.577 -15.308 -1.958  1.00 33.50 ?  58  ASN   B HB3  1 
ATOM   5511 H HD21 . ASN   B 1 58  ? 65.731 -15.340 -0.957  1.00 54.77 ?  58  ASN   B HD21 1 
ATOM   5512 H HD22 . ASN   B 1 58  ? 64.677 -14.596 -1.700  1.00 54.77 ?  58  ASN   B HD22 1 
ATOM   5513 N N    . ASN   B 1 59  ? 60.235 -16.635 0.756   1.00 14.83 ?  59  ASN   B N    1 
ATOM   5514 C CA   . ASN   B 1 59  ? 59.756 -16.158 2.050   1.00 14.37 ?  59  ASN   B CA   1 
ATOM   5515 C C    . ASN   B 1 59  ? 59.162 -14.752 1.983   1.00 13.78 ?  59  ASN   B C    1 
ATOM   5516 O O    . ASN   B 1 59  ? 58.717 -14.242 3.016   1.00 14.15 ?  59  ASN   B O    1 
ATOM   5517 C CB   . ASN   B 1 59  ? 60.827 -16.199 3.150   1.00 15.27 ?  59  ASN   B CB   1 
ATOM   5518 C CG   . ASN   B 1 59  ? 60.239 -16.366 4.526   1.00 17.01 ?  59  ASN   B CG   1 
ATOM   5519 O OD1  . ASN   B 1 59  ? 59.404 -17.249 4.763   1.00 16.81 ?  59  ASN   B OD1  1 
ATOM   5520 N ND2  . ASN   B 1 59  ? 60.661 -15.510 5.448   1.00 17.89 ?  59  ASN   B ND2  1 
ATOM   5521 H H    . ASN   B 1 59  ? 59.695 -17.219 0.409   1.00 17.82 ?  59  ASN   B H    1 
ATOM   5522 H HA   . ASN   B 1 59  ? 59.046 -16.757 2.341   1.00 17.26 ?  59  ASN   B HA   1 
ATOM   5523 H HB2  . ASN   B 1 59  ? 61.427 -16.944 2.997   1.00 18.34 ?  59  ASN   B HB2  1 
ATOM   5524 H HB3  . ASN   B 1 59  ? 61.324 -15.365 3.143   1.00 18.34 ?  59  ASN   B HB3  1 
ATOM   5525 H HD21 . ASN   B 1 59  ? 60.364 -15.559 6.255   1.00 21.49 ?  59  ASN   B HD21 1 
ATOM   5526 H HD22 . ASN   B 1 59  ? 61.241 -14.901 5.247   1.00 21.49 ?  59  ASN   B HD22 1 
ATOM   5527 N N    . ALA   B 1 60  ? 59.107 -14.123 0.806   1.00 14.04 ?  60  ALA   B N    1 
ATOM   5528 C CA   . ALA   B 1 60  ? 58.510 -12.794 0.725   1.00 13.70 ?  60  ALA   B CA   1 
ATOM   5529 C C    . ALA   B 1 60  ? 57.038 -12.819 1.122   1.00 12.84 ?  60  ALA   B C    1 
ATOM   5530 O O    . ALA   B 1 60  ? 56.534 -11.865 1.723   1.00 13.98 ?  60  ALA   B O    1 
ATOM   5531 C CB   . ALA   B 1 60  ? 58.670 -12.219 -0.679  1.00 15.24 ?  60  ALA   B CB   1 
ATOM   5532 H H    . ALA   B 1 60  ? 59.411 -14.439 0.065   1.00 16.86 ?  60  ALA   B H    1 
ATOM   5533 H HA   . ALA   B 1 60  ? 58.975 -12.209 1.342   1.00 16.46 ?  60  ALA   B HA   1 
ATOM   5534 H HB1  . ALA   B 1 60  ? 58.267 -11.341 -0.705  1.00 18.31 ?  60  ALA   B HB1  1 
ATOM   5535 H HB2  . ALA   B 1 60  ? 59.617 -12.159 -0.890  1.00 18.31 ?  60  ALA   B HB2  1 
ATOM   5536 H HB3  . ALA   B 1 60  ? 58.229 -12.809 -1.312  1.00 18.31 ?  60  ALA   B HB3  1 
ATOM   5537 N N    . MET   B 1 61  ? 56.328 -13.898 0.776   1.00 12.76 ?  61  MET   B N    1 
ATOM   5538 C CA   . MET   B 1 61  ? 54.928 -14.021 1.160   1.00 12.08 ?  61  MET   B CA   1 
ATOM   5539 C C    . MET   B 1 61  ? 54.777 -14.019 2.680   1.00 12.41 ?  61  MET   B C    1 
ATOM   5540 O O    . MET   B 1 61  ? 53.871 -13.369 3.220   1.00 12.16 ?  61  MET   B O    1 
ATOM   5541 C CB   . MET   B 1 61  ? 54.356 -15.297 0.537   1.00 11.83 ?  61  MET   B CB   1 
ATOM   5542 C CG   . MET   B 1 61  ? 52.907 -15.572 0.913   1.00 11.60 ?  61  MET   B CG   1 
ATOM   5543 S SD   . MET   B 1 61  ? 52.279 -17.093 0.175   1.00 12.55 ?  61  MET   B SD   1 
ATOM   5544 C CE   . MET   B 1 61  ? 52.026 -16.489 -1.494  1.00 13.58 ?  61  MET   B CE   1 
ATOM   5545 H H    . MET   B 1 61  ? 56.638 -14.566 0.316   1.00 15.32 ?  61  MET   B H    1 
ATOM   5546 H HA   . MET   B 1 61  ? 54.440 -13.272 0.789   1.00 14.51 ?  61  MET   B HA   1 
ATOM   5547 H HB2  . MET   B 1 61  ? 54.406 -15.226 -0.429  1.00 14.21 ?  61  MET   B HB2  1 
ATOM   5548 H HB3  . MET   B 1 61  ? 54.892 -16.055 0.834   1.00 14.21 ?  61  MET   B HB3  1 
ATOM   5549 H HG2  . MET   B 1 61  ? 52.843 -15.667 1.879   1.00 13.93 ?  61  MET   B HG2  1 
ATOM   5550 H HG3  . MET   B 1 61  ? 52.359 -14.836 0.613   1.00 13.93 ?  61  MET   B HG3  1 
ATOM   5551 H HE1  . MET   B 1 61  ? 51.646 -17.198 -2.031  1.00 16.32 ?  61  MET   B HE1  1 
ATOM   5552 H HE2  . MET   B 1 61  ? 51.422 -15.729 -1.470  1.00 16.32 ?  61  MET   B HE2  1 
ATOM   5553 H HE3  . MET   B 1 61  ? 52.883 -16.214 -1.863  1.00 16.32 ?  61  MET   B HE3  1 
ATOM   5554 N N    . GLN   B 1 62  ? 55.657 -14.730 3.392   1.00 11.85 ?  62  GLN   B N    1 
ATOM   5555 C CA   . GLN   B 1 62  ? 55.543 -14.782 4.846   1.00 12.38 ?  62  GLN   B CA   1 
ATOM   5556 C C    . GLN   B 1 62  ? 55.814 -13.421 5.476   1.00 12.70 ?  62  GLN   B C    1 
ATOM   5557 O O    . GLN   B 1 62  ? 55.131 -13.027 6.427   1.00 12.96 ?  62  GLN   B O    1 
ATOM   5558 C CB   . GLN   B 1 62  ? 56.496 -15.832 5.425   1.00 13.12 ?  62  GLN   B CB   1 
ATOM   5559 C CG   . GLN   B 1 62  ? 56.269 -16.108 6.910   1.00 13.54 ?  62  GLN   B CG   1 
ATOM   5560 C CD   . GLN   B 1 62  ? 54.887 -16.697 7.144   1.00 12.95 ?  62  GLN   B CD   1 
ATOM   5561 O OE1  . GLN   B 1 62  ? 54.636 -17.847 6.781   1.00 13.25 ?  62  GLN   B OE1  1 
ATOM   5562 N NE2  . GLN   B 1 62  ? 53.972 -15.911 7.702   1.00 13.19 ?  62  GLN   B NE2  1 
ATOM   5563 H H    . GLN   B 1 62  ? 56.309 -15.184 3.063   1.00 14.24 ?  62  GLN   B H    1 
ATOM   5564 H HA   . GLN   B 1 62  ? 54.638 -15.039 5.078   1.00 14.88 ?  62  GLN   B HA   1 
ATOM   5565 H HB2  . GLN   B 1 62  ? 56.373 -16.665 4.944   1.00 15.76 ?  62  GLN   B HB2  1 
ATOM   5566 H HB3  . GLN   B 1 62  ? 57.408 -15.521 5.317   1.00 15.76 ?  62  GLN   B HB3  1 
ATOM   5567 H HG2  . GLN   B 1 62  ? 56.933 -16.744 7.222   1.00 16.26 ?  62  GLN   B HG2  1 
ATOM   5568 H HG3  . GLN   B 1 62  ? 56.333 -15.281 7.408   1.00 16.26 ?  62  GLN   B HG3  1 
ATOM   5569 H HE21 . GLN   B 1 62  ? 54.183 -15.114 7.936   1.00 15.84 ?  62  GLN   B HE21 1 
ATOM   5570 H HE22 . GLN   B 1 62  ? 53.182 -16.213 7.849   1.00 15.84 ?  62  GLN   B HE22 1 
ATOM   5571 N N    . VAL   B 1 63  ? 56.826 -12.704 4.986   1.00 13.24 ?  63  VAL   B N    1 
ATOM   5572 C CA   . VAL   B 1 63  ? 57.127 -11.384 5.536   1.00 14.28 ?  63  VAL   B CA   1 
ATOM   5573 C C    . VAL   B 1 63  ? 55.931 -10.456 5.353   1.00 13.38 ?  63  VAL   B C    1 
ATOM   5574 O O    . VAL   B 1 63  ? 55.506 -9.754  6.283   1.00 14.14 ?  63  VAL   B O    1 
ATOM   5575 C CB   . VAL   B 1 63  ? 58.413 -10.820 4.902   1.00 15.20 ?  63  VAL   B CB   1 
ATOM   5576 C CG1  . VAL   B 1 63  ? 58.623 -9.371  5.330   1.00 15.75 ?  63  VAL   B CG1  1 
ATOM   5577 C CG2  . VAL   B 1 63  ? 59.614 -11.669 5.287   1.00 16.00 ?  63  VAL   B CG2  1 
ATOM   5578 H H    . VAL   B 1 63  ? 57.337 -12.957 4.337   1.00 15.91 ?  63  VAL   B H    1 
ATOM   5579 H HA   . VAL   B 1 63  ? 57.288 -11.478 6.483   1.00 17.15 ?  63  VAL   B HA   1 
ATOM   5580 H HB   . VAL   B 1 63  ? 58.334 -10.843 3.933   1.00 18.25 ?  63  VAL   B HB   1 
ATOM   5581 H HG11 . VAL   B 1 63  ? 59.540 -9.115  5.144   1.00 18.92 ?  63  VAL   B HG11 1 
ATOM   5582 H HG12 . VAL   B 1 63  ? 58.015 -8.801  4.833   1.00 18.92 ?  63  VAL   B HG12 1 
ATOM   5583 H HG13 . VAL   B 1 63  ? 58.447 -9.295  6.281   1.00 18.92 ?  63  VAL   B HG13 1 
ATOM   5584 H HG21 . VAL   B 1 63  ? 60.413 -11.287 4.886   1.00 19.22 ?  63  VAL   B HG21 1 
ATOM   5585 H HG22 . VAL   B 1 63  ? 59.701 -11.665 6.255   1.00 19.22 ?  63  VAL   B HG22 1 
ATOM   5586 H HG23 . VAL   B 1 63  ? 59.482 -12.572 4.969   1.00 19.22 ?  63  VAL   B HG23 1 
ATOM   5587 N N    . GLU   B 1 64  ? 55.363 -10.449 4.150   1.00 13.04 ?  64  GLU   B N    1 
ATOM   5588 C CA   . GLU   B 1 64  ? 54.203 -9.613  3.865   1.00 12.64 ?  64  GLU   B CA   1 
ATOM   5589 C C    . GLU   B 1 64  ? 53.013 -10.018 4.728   1.00 12.45 ?  64  GLU   B C    1 
ATOM   5590 O O    . GLU   B 1 64  ? 52.255 -9.163  5.217   1.00 12.92 ?  64  GLU   B O    1 
ATOM   5591 C CB   . GLU   B 1 64  ? 53.860 -9.766  2.382   1.00 13.03 ?  64  GLU   B CB   1 
ATOM   5592 C CG   . GLU   B 1 64  ? 52.609 -9.024  1.929   1.00 13.27 ?  64  GLU   B CG   1 
ATOM   5593 C CD   . GLU   B 1 64  ? 52.097 -9.518  0.589   1.00 13.95 ?  64  GLU   B CD   1 
ATOM   5594 O OE1  . GLU   B 1 64  ? 52.276 -10.729 0.276   1.00 14.19 ?  64  GLU   B OE1  1 
ATOM   5595 O OE2  . GLU   B 1 64  ? 51.482 -8.698  -0.138  1.00 14.59 -1 64  GLU   B OE2  1 
ATOM   5596 H H    . GLU   B 1 64  ? 55.628 -10.921 3.476   1.00 15.66 ?  64  GLU   B H    1 
ATOM   5597 H HA   . GLU   B 1 64  ? 54.411 -8.684  4.042   1.00 15.18 ?  64  GLU   B HA   1 
ATOM   5598 H HB2  . GLU   B 1 64  ? 54.596 -9.421  1.853   1.00 15.65 ?  64  GLU   B HB2  1 
ATOM   5599 H HB3  . GLU   B 1 64  ? 53.723 -10.701 2.187   1.00 15.65 ?  64  GLU   B HB3  1 
ATOM   5600 H HG2  . GLU   B 1 64  ? 51.891 -9.148  2.575   1.00 15.94 ?  64  GLU   B HG2  1 
ATOM   5601 H HG3  . GLU   B 1 64  ? 52.805 -8.075  1.845   1.00 15.94 ?  64  GLU   B HG3  1 
ATOM   5602 N N    . SER   B 1 65  ? 52.832 -11.327 4.916   1.00 11.93 ?  65  SER   B N    1 
ATOM   5603 C CA   . SER   B 1 65  ? 51.726 -11.842 5.716   1.00 11.91 ?  65  SER   B CA   1 
ATOM   5604 C C    . SER   B 1 65  ? 51.853 -11.439 7.180   1.00 12.33 ?  65  SER   B C    1 
ATOM   5605 O O    . SER   B 1 65  ? 50.855 -11.065 7.809   1.00 12.54 ?  65  SER   B O    1 
ATOM   5606 C CB   . SER   B 1 65  ? 51.662 -13.366 5.591   1.00 12.18 ?  65  SER   B CB   1 
ATOM   5607 O OG   . SER   B 1 65  ? 51.308 -13.774 4.275   1.00 12.34 ?  65  SER   B OG   1 
ATOM   5608 H H    . SER   B 1 65  ? 53.339 -11.946 4.591   1.00 14.33 ?  65  SER   B H    1 
ATOM   5609 H HA   . SER   B 1 65  ? 50.891 -11.485 5.376   1.00 14.31 ?  65  SER   B HA   1 
ATOM   5610 H HB2  . SER   B 1 65  ? 52.531 -13.736 5.820   1.00 14.64 ?  65  SER   B HB2  1 
ATOM   5611 H HB3  . SER   B 1 65  ? 50.994 -13.705 6.214   1.00 14.64 ?  65  SER   B HB3  1 
ATOM   5612 H HG   . SER   B 1 65  ? 51.889 -13.490 3.727   1.00 14.82 ?  65  SER   B HG   1 
ATOM   5613 N N    . ASP   B 1 66  ? 53.057 -11.537 7.754   1.00 12.52 ?  66  ASP   B N    1 
ATOM   5614 C CA   . ASP   B 1 66  ? 53.233 -11.125 9.144   1.00 12.88 ?  66  ASP   B CA   1 
ATOM   5615 C C    . ASP   B 1 66  ? 52.927 -9.643  9.328   1.00 12.98 ?  66  ASP   B C    1 
ATOM   5616 O O    . ASP   B 1 66  ? 52.351 -9.240  10.346  1.00 13.69 ?  66  ASP   B O    1 
ATOM   5617 C CB   . ASP   B 1 66  ? 54.652 -11.433 9.621   1.00 14.02 ?  66  ASP   B CB   1 
ATOM   5618 C CG   . ASP   B 1 66  ? 54.919 -12.931 9.780   1.00 15.45 ?  66  ASP   B CG   1 
ATOM   5619 O OD1  . ASP   B 1 66  ? 53.966 -13.742 9.700   1.00 16.28 ?  66  ASP   B OD1  1 
ATOM   5620 O OD2  . ASP   B 1 66  ? 56.101 -13.285 10.000  1.00 18.56 -1 66  ASP   B OD2  1 
ATOM   5621 H H    . ASP   B 1 66  ? 53.759 -11.837 7.378   1.00 15.04 ?  66  ASP   B H    1 
ATOM   5622 H HA   . ASP   B 1 66  ? 52.621 -11.614 9.712   1.00 15.47 ?  66  ASP   B HA   1 
ATOM   5623 H HB2  . ASP   B 1 66  ? 55.288 -11.081 8.980   1.00 16.84 ?  66  ASP   B HB2  1 
ATOM   5624 H HB3  . ASP   B 1 66  ? 54.798 -11.013 10.490  1.00 16.84 ?  66  ASP   B HB3  1 
ATOM   5625 N N    . ASP   B 1 67  ? 53.305 -8.810  8.359   1.00 12.83 ?  67  ASP   B N    1 
ATOM   5626 C CA   . ASP   B 1 67  ? 52.952 -7.400  8.431   1.00 13.35 ?  67  ASP   B CA   1 
ATOM   5627 C C    . ASP   B 1 67  ? 51.440 -7.195  8.356   1.00 13.31 ?  67  ASP   B C    1 
ATOM   5628 O O    . ASP   B 1 67  ? 50.886 -6.365  9.089   1.00 13.79 ?  67  ASP   B O    1 
ATOM   5629 C CB   . ASP   B 1 67  ? 53.652 -6.640  7.314   1.00 14.96 ?  67  ASP   B CB   1 
ATOM   5630 C CG   . ASP   B 1 67  ? 53.222 -5.200  7.260   1.00 16.44 ?  67  ASP   B CG   1 
ATOM   5631 O OD1  . ASP   B 1 67  ? 53.720 -4.380  8.065   1.00 17.93 ?  67  ASP   B OD1  1 
ATOM   5632 O OD2  . ASP   B 1 67  ? 52.348 -4.897  6.436   1.00 17.44 -1 67  ASP   B OD2  1 
ATOM   5633 H H    . ASP   B 1 67  ? 53.764 -9.032  7.665   1.00 15.41 ?  67  ASP   B H    1 
ATOM   5634 H HA   . ASP   B 1 67  ? 53.264 -7.035  9.276   1.00 16.04 ?  67  ASP   B HA   1 
ATOM   5635 H HB2  . ASP   B 1 67  ? 54.607 -6.666  7.455   1.00 17.97 ?  67  ASP   B HB2  1 
ATOM   5636 H HB3  . ASP   B 1 67  ? 53.429 -7.060  6.461   1.00 17.97 ?  67  ASP   B HB3  1 
ATOM   5637 N N    . TYR   B 1 68  ? 50.758 -7.933  7.468   1.00 13.29 ?  68  TYR   B N    1 
ATOM   5638 C CA   . TYR   B 1 68  ? 49.298 -7.869  7.397   1.00 14.03 ?  68  TYR   B CA   1 
ATOM   5639 C C    . TYR   B 1 68  ? 48.664 -8.194  8.745   1.00 13.24 ?  68  TYR   B C    1 
ATOM   5640 O O    . TYR   B 1 68  ? 47.730 -7.504  9.184   1.00 14.03 ?  68  TYR   B O    1 
ATOM   5641 C CB   . TYR   B 1 68  ? 48.766 -8.818  6.313   1.00 14.47 ?  68  TYR   B CB   1 
ATOM   5642 C CG   . TYR   B 1 68  ? 47.258 -8.972  6.367   1.00 15.13 ?  68  TYR   B CG   1 
ATOM   5643 C CD1  . TYR   B 1 68  ? 46.671 -9.903  7.215   1.00 15.41 ?  68  TYR   B CD1  1 
ATOM   5644 C CD2  . TYR   B 1 68  ? 46.426 -8.160  5.612   1.00 16.08 ?  68  TYR   B CD2  1 
ATOM   5645 C CE1  . TYR   B 1 68  ? 45.306 -10.025 7.310   1.00 16.40 ?  68  TYR   B CE1  1 
ATOM   5646 C CE2  . TYR   B 1 68  ? 45.041 -8.286  5.695   1.00 16.04 ?  68  TYR   B CE2  1 
ATOM   5647 C CZ   . TYR   B 1 68  ? 44.503 -9.222  6.552   1.00 16.33 ?  68  TYR   B CZ   1 
ATOM   5648 O OH   . TYR   B 1 68  ? 43.134 -9.333  6.659   1.00 17.46 ?  68  TYR   B OH   1 
ATOM   5649 H H    . TYR   B 1 68  ? 51.118 -8.482  6.909   1.00 15.97 ?  68  TYR   B H    1 
ATOM   5650 H HA   . TYR   B 1 68  ? 49.041 -6.969  7.166   1.00 16.86 ?  68  TYR   B HA   1 
ATOM   5651 H HB2  . TYR   B 1 68  ? 49.000 -8.461  5.446   1.00 17.38 ?  68  TYR   B HB2  1 
ATOM   5652 H HB3  . TYR   B 1 68  ? 49.164 -9.694  6.437   1.00 17.38 ?  68  TYR   B HB3  1 
ATOM   5653 H HD1  . TYR   B 1 68  ? 47.216 -10.451 7.740   1.00 18.51 ?  68  TYR   B HD1  1 
ATOM   5654 H HD2  . TYR   B 1 68  ? 46.801 -7.519  5.052   1.00 19.31 ?  68  TYR   B HD2  1 
ATOM   5655 H HE1  . TYR   B 1 68  ? 44.929 -10.662 7.874   1.00 19.69 ?  68  TYR   B HE1  1 
ATOM   5656 H HE2  . TYR   B 1 68  ? 44.486 -7.736  5.190   1.00 19.26 ?  68  TYR   B HE2  1 
ATOM   5657 H HH   . TYR   B 1 68  ? 42.751 -8.801  6.128   1.00 20.97 ?  68  TYR   B HH   1 
ATOM   5658 N N    . ILE   B 1 69  ? 49.158 -9.244  9.414   1.00 12.89 ?  69  ILE   B N    1 
ATOM   5659 C CA   . ILE   B 1 69  ? 48.606 -9.653  10.704  1.00 13.10 ?  69  ILE   B CA   1 
ATOM   5660 C C    . ILE   B 1 69  ? 48.859 -8.586  11.761  1.00 13.08 ?  69  ILE   B C    1 
ATOM   5661 O O    . ILE   B 1 69  ? 47.987 -8.276  12.580  1.00 13.27 ?  69  ILE   B O    1 
ATOM   5662 C CB   . ILE   B 1 69  ? 49.191 -11.016 11.124  1.00 13.76 ?  69  ILE   B CB   1 
ATOM   5663 C CG1  . ILE   B 1 69  ? 48.691 -12.147 10.211  1.00 14.10 ?  69  ILE   B CG1  1 
ATOM   5664 C CG2  . ILE   B 1 69  ? 48.877 -11.311 12.586  1.00 14.46 ?  69  ILE   B CG2  1 
ATOM   5665 C CD1  . ILE   B 1 69  ? 47.200 -12.478 10.338  1.00 14.61 ?  69  ILE   B CD1  1 
ATOM   5666 H H    . ILE   B 1 69  ? 49.815 -9.738  9.144   1.00 15.48 ?  69  ILE   B H    1 
ATOM   5667 H HA   . ILE   B 1 69  ? 47.652 -9.761  10.615  1.00 15.74 ?  69  ILE   B HA   1 
ATOM   5668 H HB   . ILE   B 1 69  ? 50.157 -10.975 11.039  1.00 16.53 ?  69  ILE   B HB   1 
ATOM   5669 H HG12 . ILE   B 1 69  ? 48.857 -11.894 9.293   1.00 16.94 ?  69  ILE   B HG12 1 
ATOM   5670 H HG13 . ILE   B 1 69  ? 49.187 -12.956 10.421  1.00 16.94 ?  69  ILE   B HG13 1 
ATOM   5671 H HG21 . ILE   B 1 69  ? 49.017 -12.258 12.755  1.00 17.36 ?  69  ILE   B HG21 1 
ATOM   5672 H HG22 . ILE   B 1 69  ? 49.464 -10.790 13.153  1.00 17.36 ?  69  ILE   B HG22 1 
ATOM   5673 H HG23 . ILE   B 1 69  ? 47.950 -11.082 12.763  1.00 17.36 ?  69  ILE   B HG23 1 
ATOM   5674 H HD11 . ILE   B 1 69  ? 46.989 -13.204 9.727   1.00 17.55 ?  69  ILE   B HD11 1 
ATOM   5675 H HD12 . ILE   B 1 69  ? 47.011 -12.754 11.249  1.00 17.55 ?  69  ILE   B HD12 1 
ATOM   5676 H HD13 . ILE   B 1 69  ? 46.680 -11.695 10.112  1.00 17.55 ?  69  ILE   B HD13 1 
ATOM   5677 N N    . ALA   B 1 70  ? 50.053 -7.994  11.764  1.00 12.79 ?  70  ALA   B N    1 
ATOM   5678 C CA   . ALA   B 1 70  ? 50.347 -6.945  12.735  1.00 12.12 ?  70  ALA   B CA   1 
ATOM   5679 C C    . ALA   B 1 70  ? 49.345 -5.807  12.639  1.00 12.83 ?  70  ALA   B C    1 
ATOM   5680 O O    . ALA   B 1 70  ? 48.955 -5.229  13.656  1.00 13.37 ?  70  ALA   B O    1 
ATOM   5681 C CB   . ALA   B 1 70  ? 51.768 -6.418  12.531  1.00 13.26 ?  70  ALA   B CB   1 
ATOM   5682 H H    . ALA   B 1 70  ? 50.693 -8.175  11.226  1.00 15.36 ?  70  ALA   B H    1 
ATOM   5683 H HA   . ALA   B 1 70  ? 50.299 -7.315  13.630  1.00 14.56 ?  70  ALA   B HA   1 
ATOM   5684 H HB1  . ALA   B 1 70  ? 51.978 -5.778  13.233  1.00 15.93 ?  70  ALA   B HB1  1 
ATOM   5685 H HB2  . ALA   B 1 70  ? 52.395 -7.159  12.572  1.00 15.93 ?  70  ALA   B HB2  1 
ATOM   5686 H HB3  . ALA   B 1 70  ? 51.831 -5.986  11.663  1.00 15.93 ?  70  ALA   B HB3  1 
ATOM   5687 N N    . THR   B 1 71  ? 48.925 -5.466  11.427  1.00 13.56 ?  71  THR   B N    1 
ATOM   5688 C CA   . THR   B 1 71  ? 47.983 -4.369  11.236  1.00 14.90 ?  71  THR   B CA   1 
ATOM   5689 C C    . THR   B 1 71  ? 46.529 -4.785  11.475  1.00 14.71 ?  71  THR   B C    1 
ATOM   5690 O O    . THR   B 1 71  ? 45.748 -4.008  12.046  1.00 16.15 ?  71  THR   B O    1 
ATOM   5691 C CB   . THR   B 1 71  ? 48.156 -3.796  9.829   1.00 17.03 ?  71  THR   B CB   1 
ATOM   5692 O OG1  . THR   B 1 71  ? 49.460 -3.215  9.702   1.00 19.65 ?  71  THR   B OG1  1 
ATOM   5693 C CG2  . THR   B 1 71  ? 47.085 -2.747  9.528   1.00 18.36 ?  71  THR   B CG2  1 
ATOM   5694 H H    . THR   B 1 71  ? 49.167 -5.863  10.698  1.00 16.29 ?  71  THR   B H    1 
ATOM   5695 H HA   . THR   B 1 71  ? 48.195 -3.671  11.867  1.00 17.90 ?  71  THR   B HA   1 
ATOM   5696 H HB   . THR   B 1 71  ? 48.074 -4.505  9.174   1.00 20.45 ?  71  THR   B HB   1 
ATOM   5697 H HG1  . THR   B 1 71  ? 49.554 -2.873  8.937   1.00 23.60 ?  71  THR   B HG1  1 
ATOM   5698 H HG21 . THR   B 1 71  ? 47.347 -2.214  8.759   1.00 22.04 ?  71  THR   B HG21 1 
ATOM   5699 H HG22 . THR   B 1 71  ? 46.238 -3.178  9.333   1.00 22.04 ?  71  THR   B HG22 1 
ATOM   5700 H HG23 . THR   B 1 71  ? 46.972 -2.158  10.291  1.00 22.04 ?  71  THR   B HG23 1 
ATOM   5701 N N    . ASN   B 1 72  ? 46.149 -5.996  11.056  1.00 15.01 ?  72  ASN   B N    1 
ATOM   5702 C CA   . ASN   B 1 72  ? 44.749 -6.381  10.958  1.00 15.77 ?  72  ASN   B CA   1 
ATOM   5703 C C    . ASN   B 1 72  ? 44.313 -7.477  11.920  1.00 16.11 ?  72  ASN   B C    1 
ATOM   5704 O O    . ASN   B 1 72  ? 43.104 -7.641  12.123  1.00 17.52 ?  72  ASN   B O    1 
ATOM   5705 C CB   . ASN   B 1 72  ? 44.436 -6.824  9.522   1.00 16.83 ?  72  ASN   B CB   1 
ATOM   5706 C CG   . ASN   B 1 72  ? 44.690 -5.723  8.516   1.00 17.70 ?  72  ASN   B CG   1 
ATOM   5707 O OD1  . ASN   B 1 72  ? 45.688 -5.737  7.786   1.00 19.76 ?  72  ASN   B OD1  1 
ATOM   5708 N ND2  . ASN   B 1 72  ? 43.824 -4.729  8.513   1.00 19.62 ?  72  ASN   B ND2  1 
ATOM   5709 H H    . ASN   B 1 72  ? 46.700 -6.628  10.834  1.00 18.02 ?  72  ASN   B H    1 
ATOM   5710 H HA   . ASN   B 1 72  ? 44.207 -5.607  11.150  1.00 18.94 ?  72  ASN   B HA   1 
ATOM   5711 H HB2  . ASN   B 1 72  ? 44.998 -7.580  9.290   1.00 20.21 ?  72  ASN   B HB2  1 
ATOM   5712 H HB3  . ASN   B 1 72  ? 43.502 -7.070  9.462   1.00 20.21 ?  72  ASN   B HB3  1 
ATOM   5713 H HD21 . ASN   B 1 72  ? 43.920 -4.074  7.963   1.00 23.56 ?  72  ASN   B HD21 1 
ATOM   5714 H HD22 . ASN   B 1 72  ? 43.143 -4.750  9.039   1.00 23.56 ?  72  ASN   B HD22 1 
ATOM   5715 N N    . GLY   B 1 73  ? 45.237 -8.226  12.509  1.00 14.80 ?  73  GLY   B N    1 
ATOM   5716 C CA   . GLY   B 1 73  ? 44.867 -9.386  13.280  1.00 14.48 ?  73  GLY   B CA   1 
ATOM   5717 C C    . GLY   B 1 73  ? 44.511 -10.556 12.391  1.00 13.12 ?  73  GLY   B C    1 
ATOM   5718 O O    . GLY   B 1 73  ? 44.476 -10.447 11.164  1.00 13.56 ?  73  GLY   B O    1 
ATOM   5719 H H    . GLY   B 1 73  ? 46.086 -8.090  12.465  1.00 17.78 ?  73  GLY   B H    1 
ATOM   5720 H HA2  . GLY   B 1 73  ? 45.604 -9.640  13.859  1.00 17.40 ?  73  GLY   B HA2  1 
ATOM   5721 H HA3  . GLY   B 1 73  ? 44.099 -9.172  13.836  1.00 17.40 ?  73  GLY   B HA3  1 
ATOM   5722 N N    A PRO   B 1 74  ? 44.224 -11.697 13.012  0.42 13.82 ?  74  PRO   B N    1 
ATOM   5723 N N    B PRO   B 1 74  ? 44.226 -11.700 13.012  0.58 13.68 ?  74  PRO   B N    1 
ATOM   5724 C CA   A PRO   B 1 74  ? 43.966 -12.914 12.243  0.42 13.50 ?  74  PRO   B CA   1 
ATOM   5725 C CA   B PRO   B 1 74  ? 43.977 -12.923 12.244  0.58 13.28 ?  74  PRO   B CA   1 
ATOM   5726 C C    A PRO   B 1 74  ? 42.677 -12.813 11.443  0.42 12.78 ?  74  PRO   B C    1 
ATOM   5727 C C    B PRO   B 1 74  ? 42.652 -12.883 11.499  0.58 12.93 ?  74  PRO   B C    1 
ATOM   5728 O O    A PRO   B 1 74  ? 41.778 -12.017 11.733  0.42 13.89 ?  74  PRO   B O    1 
ATOM   5729 O O    B PRO   B 1 74  ? 41.695 -12.207 11.897  0.58 14.24 ?  74  PRO   B O    1 
ATOM   5730 C CB   A PRO   B 1 74  ? 43.864 -13.995 13.326  0.42 14.42 ?  74  PRO   B CB   1 
ATOM   5731 C CB   B PRO   B 1 74  ? 43.967 -14.015 13.323  0.58 14.06 ?  74  PRO   B CB   1 
ATOM   5732 C CG   A PRO   B 1 74  ? 43.409 -13.260 14.543  0.42 15.42 ?  74  PRO   B CG   1 
ATOM   5733 C CG   B PRO   B 1 74  ? 43.564 -13.302 14.569  0.58 15.34 ?  74  PRO   B CG   1 
ATOM   5734 C CD   A PRO   B 1 74  ? 44.074 -11.915 14.461  0.42 14.98 ?  74  PRO   B CD   1 
ATOM   5735 C CD   B PRO   B 1 74  ? 44.202 -11.947 14.462  0.58 14.72 ?  74  PRO   B CD   1 
ATOM   5736 H HA   A PRO   B 1 74  ? 44.712 -13.110 11.651  0.42 16.22 ?  74  PRO   B HA   1 
ATOM   5737 H HA   B PRO   B 1 74  ? 44.706 -13.088 11.617  0.58 15.96 ?  74  PRO   B HA   1 
ATOM   5738 H HB2  A PRO   B 1 74  ? 43.215 -14.664 13.060  0.42 17.32 ?  74  PRO   B HB2  1 
ATOM   5739 H HB2  B PRO   B 1 74  ? 43.321 -14.700 13.086  0.58 16.89 ?  74  PRO   B HB2  1 
ATOM   5740 H HB3  A PRO   B 1 74  ? 44.736 -14.400 13.471  0.42 17.32 ?  74  PRO   B HB3  1 
ATOM   5741 H HB3  B PRO   B 1 74  ? 44.856 -14.398 13.413  0.58 16.89 ?  74  PRO   B HB3  1 
ATOM   5742 H HG2  A PRO   B 1 74  ? 42.444 -13.168 14.525  0.42 18.52 ?  74  PRO   B HG2  1 
ATOM   5743 H HG2  B PRO   B 1 74  ? 42.596 -13.222 14.602  0.58 18.42 ?  74  PRO   B HG2  1 
ATOM   5744 H HG3  A PRO   B 1 74  ? 43.693 -13.738 15.338  0.42 18.52 ?  74  PRO   B HG3  1 
ATOM   5745 H HG3  B PRO   B 1 74  ? 43.895 -13.779 15.344  0.58 18.42 ?  74  PRO   B HG3  1 
ATOM   5746 H HD2  A PRO   B 1 74  ? 43.504 -11.234 14.854  0.42 17.99 ?  74  PRO   B HD2  1 
ATOM   5747 H HD2  B PRO   B 1 74  ? 43.657 -11.281 14.914  0.58 17.68 ?  74  PRO   B HD2  1 
ATOM   5748 H HD3  A PRO   B 1 74  ? 44.943 -11.941 14.895  0.42 17.99 ?  74  PRO   B HD3  1 
ATOM   5749 H HD3  B PRO   B 1 74  ? 45.103 -11.970 14.821  0.58 17.68 ?  74  PRO   B HD3  1 
ATOM   5750 N N    . LEU   B 1 75  ? 42.609 -13.643 10.410  1.00 12.54 ?  75  LEU   B N    1 
ATOM   5751 C CA   . LEU   B 1 75  ? 41.391 -13.820 9.649   1.00 12.38 ?  75  LEU   B CA   1 
ATOM   5752 C C    . LEU   B 1 75  ? 40.401 -14.665 10.447  1.00 13.22 ?  75  LEU   B C    1 
ATOM   5753 O O    . LEU   B 1 75  ? 40.747 -15.297 11.447  1.00 14.30 ?  75  LEU   B O    1 
ATOM   5754 C CB   . LEU   B 1 75  ? 41.700 -14.538 8.338   1.00 12.49 ?  75  LEU   B CB   1 
ATOM   5755 C CG   . LEU   B 1 75  ? 42.541 -13.781 7.308   1.00 14.46 ?  75  LEU   B CG   1 
ATOM   5756 C CD1  . LEU   B 1 75  ? 42.766 -14.612 6.053   1.00 16.33 ?  75  LEU   B CD1  1 
ATOM   5757 C CD2  . LEU   B 1 75  ? 41.910 -12.467 6.952   1.00 18.25 ?  75  LEU   B CD2  1 
ATOM   5758 H H    A LEU   B 1 75  ? 43.267 -14.123 10.130  0.42 15.06 ?  75  LEU   B H    1 
ATOM   5759 H H    B LEU   B 1 75  ? 43.283 -14.076 10.094  0.58 15.06 ?  75  LEU   B H    1 
ATOM   5760 H HA   . LEU   B 1 75  ? 40.986 -12.957 9.455   1.00 14.88 ?  75  LEU   B HA   1 
ATOM   5761 H HB2  . LEU   B 1 75  ? 42.180 -15.359 8.550   1.00 15.01 ?  75  LEU   B HB2  1 
ATOM   5762 H HB3  . LEU   B 1 75  ? 40.860 -14.768 7.909   1.00 15.01 ?  75  LEU   B HB3  1 
ATOM   5763 H HG   . LEU   B 1 75  ? 43.410 -13.593 7.699   1.00 17.37 ?  75  LEU   B HG   1 
ATOM   5764 H HD11 . LEU   B 1 75  ? 43.313 -14.098 5.431   1.00 19.61 ?  75  LEU   B HD11 1 
ATOM   5765 H HD12 . LEU   B 1 75  ? 43.225 -15.431 6.292   1.00 19.61 ?  75  LEU   B HD12 1 
ATOM   5766 H HD13 . LEU   B 1 75  ? 41.911 -14.813 5.648   1.00 19.61 ?  75  LEU   B HD13 1 
ATOM   5767 H HD21 . LEU   B 1 75  ? 42.392 -12.078 6.207   1.00 21.91 ?  75  LEU   B HD21 1 
ATOM   5768 H HD22 . LEU   B 1 75  ? 40.984 -12.619 6.708   1.00 21.91 ?  75  LEU   B HD22 1 
ATOM   5769 H HD23 . LEU   B 1 75  ? 41.956 -11.875 7.721   1.00 21.91 ?  75  LEU   B HD23 1 
ATOM   5770 N N    . LYS   B 1 76  ? 39.156 -14.688 9.974   1.00 14.37 ?  76  LYS   B N    1 
ATOM   5771 C CA   . LYS   B 1 76  ? 38.169 -15.654 10.435  1.00 15.94 ?  76  LYS   B CA   1 
ATOM   5772 C C    . LYS   B 1 76  ? 38.294 -16.941 9.623   1.00 14.29 ?  76  LYS   B C    1 
ATOM   5773 O O    . LYS   B 1 76  ? 38.582 -16.906 8.431   1.00 13.95 ?  76  LYS   B O    1 
ATOM   5774 C CB   . LYS   B 1 76  ? 36.754 -15.100 10.212  1.00 17.56 ?  76  LYS   B CB   1 
ATOM   5775 C CG   . LYS   B 1 76  ? 36.466 -13.734 10.852  1.00 19.39 ?  76  LYS   B CG   1 
ATOM   5776 C CD   . LYS   B 1 76  ? 35.058 -13.211 10.523  1.00 20.07 ?  76  LYS   B CD   1 
ATOM   5777 C CE   . LYS   B 1 76  ? 34.806 -11.850 11.161  1.00 22.02 ?  76  LYS   B CE   1 
ATOM   5778 N NZ   . LYS   B 1 76  ? 33.549 -11.205 10.693  1.00 22.59 ?  76  LYS   B NZ   1 
ATOM   5779 H H    . LYS   B 1 76  ? 38.853 -14.148 9.372   1.00 17.26 ?  76  LYS   B H    1 
ATOM   5780 H HA   . LYS   B 1 76  ? 38.300 -15.856 11.374  1.00 19.14 ?  76  LYS   B HA   1 
ATOM   5781 H HB2  . LYS   B 1 76  ? 36.605 -15.012 9.258   1.00 21.09 ?  76  LYS   B HB2  1 
ATOM   5782 H HB3  . LYS   B 1 76  ? 36.115 -15.731 10.582  1.00 21.09 ?  76  LYS   B HB3  1 
ATOM   5783 H HG2  . LYS   B 1 76  ? 36.541 -13.809 11.815  1.00 23.28 ?  76  LYS   B HG2  1 
ATOM   5784 H HG3  . LYS   B 1 76  ? 37.109 -13.085 10.518  1.00 23.28 ?  76  LYS   B HG3  1 
ATOM   5785 H HD2  . LYS   B 1 76  ? 34.961 -13.120 9.562   1.00 24.10 ?  76  LYS   B HD2  1 
ATOM   5786 H HD3  . LYS   B 1 76  ? 34.395 -13.833 10.868  1.00 24.10 ?  76  LYS   B HD3  1 
ATOM   5787 H HE2  . LYS   B 1 76  ? 34.747 -11.959 12.121  1.00 26.44 ?  76  LYS   B HE2  1 
ATOM   5788 H HE3  . LYS   B 1 76  ? 35.545 -11.261 10.938  1.00 26.44 ?  76  LYS   B HE3  1 
ATOM   5789 H HZ1  . LYS   B 1 76  ? 33.448 -10.413 11.089  1.00 27.13 ?  76  LYS   B HZ1  1 
ATOM   5790 H HZ2  . LYS   B 1 76  ? 33.579 -11.082 9.811   1.00 27.13 ?  76  LYS   B HZ2  1 
ATOM   5791 H HZ3  . LYS   B 1 76  ? 32.851 -11.718 10.890  1.00 27.13 ?  76  LYS   B HZ3  1 
ATOM   5792 N N    . VAL   B 1 77  ? 38.060 -18.086 10.268  1.00 15.65 ?  77  VAL   B N    1 
ATOM   5793 C CA   . VAL   B 1 77  ? 37.854 -19.307 9.495   1.00 15.68 ?  77  VAL   B CA   1 
ATOM   5794 C C    . VAL   B 1 77  ? 36.665 -19.087 8.568   1.00 13.96 ?  77  VAL   B C    1 
ATOM   5795 O O    . VAL   B 1 77  ? 35.600 -18.634 9.008   1.00 14.41 ?  77  VAL   B O    1 
ATOM   5796 C CB   . VAL   B 1 77  ? 37.653 -20.514 10.423  1.00 17.93 ?  77  VAL   B CB   1 
ATOM   5797 C CG1  . VAL   B 1 77  ? 37.367 -21.757 9.593   1.00 18.17 ?  77  VAL   B CG1  1 
ATOM   5798 C CG2  . VAL   B 1 77  ? 38.878 -20.724 11.318  1.00 19.24 ?  77  VAL   B CG2  1 
ATOM   5799 H H    . VAL   B 1 77  ? 38.030 -18.180 11.116  1.00 18.80 ?  77  VAL   B H    1 
ATOM   5800 H HA   . VAL   B 1 77  ? 38.636 -19.474 8.941   1.00 18.83 ?  77  VAL   B HA   1 
ATOM   5801 H HB   . VAL   B 1 77  ? 36.883 -20.350 10.987  1.00 21.54 ?  77  VAL   B HB   1 
ATOM   5802 H HG11 . VAL   B 1 77  ? 37.416 -22.535 10.171  1.00 21.82 ?  77  VAL   B HG11 1 
ATOM   5803 H HG12 . VAL   B 1 77  ? 36.478 -21.691 9.208   1.00 21.82 ?  77  VAL   B HG12 1 
ATOM   5804 H HG13 . VAL   B 1 77  ? 38.029 -21.828 8.889   1.00 21.82 ?  77  VAL   B HG13 1 
ATOM   5805 H HG21 . VAL   B 1 77  ? 38.740 -21.518 11.854  1.00 23.10 ?  77  VAL   B HG21 1 
ATOM   5806 H HG22 . VAL   B 1 77  ? 39.661 -20.829 10.758  1.00 23.10 ?  77  VAL   B HG22 1 
ATOM   5807 H HG23 . VAL   B 1 77  ? 38.981 -19.948 11.891  1.00 23.10 ?  77  VAL   B HG23 1 
ATOM   5808 N N    . GLY   B 1 78  ? 36.848 -19.380 7.275   1.00 13.47 ?  78  GLY   B N    1 
ATOM   5809 C CA   . GLY   B 1 78  ? 35.873 -19.053 6.256   1.00 13.07 ?  78  GLY   B CA   1 
ATOM   5810 C C    . GLY   B 1 78  ? 36.119 -17.740 5.551   1.00 12.45 ?  78  GLY   B C    1 
ATOM   5811 O O    . GLY   B 1 78  ? 35.423 -17.448 4.570   1.00 13.16 ?  78  GLY   B O    1 
ATOM   5812 H H    . GLY   B 1 78  ? 37.544 -19.782 6.961   1.00 16.19 ?  78  GLY   B H    1 
ATOM   5813 H HA2  . GLY   B 1 78  ? 35.868 -19.752 5.585   1.00 15.71 ?  78  GLY   B HA2  1 
ATOM   5814 H HA3  . GLY   B 1 78  ? 34.994 -19.017 6.662   1.00 15.71 ?  78  GLY   B HA3  1 
ATOM   5815 N N    . GLY   B 1 79  ? 37.070 -16.932 6.032   1.00 12.45 ?  79  GLY   B N    1 
ATOM   5816 C CA   . GLY   B 1 79  ? 37.375 -15.643 5.446   1.00 11.82 ?  79  GLY   B CA   1 
ATOM   5817 C C    . GLY   B 1 79  ? 38.614 -15.668 4.562   1.00 11.70 ?  79  GLY   B C    1 
ATOM   5818 O O    . GLY   B 1 79  ? 39.228 -16.706 4.328   1.00 12.30 ?  79  GLY   B O    1 
ATOM   5819 H H    . GLY   B 1 79  ? 37.569 -17.121 6.705   1.00 14.95 ?  79  GLY   B H    1 
ATOM   5820 H HA2  . GLY   B 1 79  ? 36.622 -15.347 4.905   1.00 14.20 ?  79  GLY   B HA2  1 
ATOM   5821 H HA3  . GLY   B 1 79  ? 37.519 -14.993 6.147   1.00 14.20 ?  79  GLY   B HA3  1 
ATOM   5822 N N    . SER   B 1 80  ? 38.986 -14.479 4.081   1.00 11.71 ?  80  SER   B N    1 
ATOM   5823 C CA   . SER   B 1 80  ? 40.094 -14.356 3.143   1.00 11.40 ?  80  SER   B CA   1 
ATOM   5824 C C    . SER   B 1 80  ? 40.676 -12.951 3.190   1.00 11.31 ?  80  SER   B C    1 
ATOM   5825 O O    . SER   B 1 80  ? 40.057 -12.010 3.692   1.00 12.39 ?  80  SER   B O    1 
ATOM   5826 C CB   . SER   B 1 80  ? 39.662 -14.656 1.703   1.00 11.78 ?  80  SER   B CB   1 
ATOM   5827 O OG   . SER   B 1 80  ? 38.819 -13.635 1.194   1.00 12.67 ?  80  SER   B OG   1 
ATOM   5828 H H    . SER   B 1 80  ? 38.610 -13.736 4.276   1.00 14.07 ?  80  SER   B H    1 
ATOM   5829 H HA   . SER   B 1 80  ? 40.787 -14.983 3.394   1.00 13.70 ?  80  SER   B HA   1 
ATOM   5830 H HB2  . SER   B 1 80  ? 40.453 -14.711 1.134   1.00 14.15 ?  80  SER   B HB2  1 
ATOM   5831 H HB3  . SER   B 1 80  ? 39.189 -15.504 1.679   1.00 14.15 ?  80  SER   B HB3  1 
ATOM   5832 H HG   . SER   B 1 80  ? 38.117 -13.584 1.667   1.00 15.22 ?  80  SER   B HG   1 
ATOM   5833 N N    . CYS   B 1 81  ? 41.867 -12.813 2.608   1.00 11.03 ?  81  CYS   B N    1 
ATOM   5834 C CA   . CYS   B 1 81  ? 42.416 -11.502 2.295   1.00 11.57 ?  81  CYS   B CA   1 
ATOM   5835 C C    . CYS   B 1 81  ? 43.188 -11.595 0.989   1.00 10.84 ?  81  CYS   B C    1 
ATOM   5836 O O    . CYS   B 1 81  ? 43.701 -12.656 0.622   1.00 11.60 ?  81  CYS   B O    1 
ATOM   5837 C CB   . CYS   B 1 81  ? 43.309 -10.951 3.416   1.00 11.97 ?  81  CYS   B CB   1 
ATOM   5838 S SG   . CYS   B 1 81  ? 44.824 -11.903 3.675   1.00 12.63 ?  81  CYS   B SG   1 
ATOM   5839 H H    . CYS   B 1 81  ? 42.375 -13.467 2.376   1.00 13.26 ?  81  CYS   B H    1 
ATOM   5840 H HA   . CYS   B 1 81  ? 41.685 -10.876 2.159   1.00 13.91 ?  81  CYS   B HA   1 
ATOM   5841 H HB2  . CYS   B 1 81  ? 43.563 -10.039 3.197   1.00 14.38 ?  81  CYS   B HB2  1 
ATOM   5842 H HB3  . CYS   B 1 81  ? 42.801 -10.954 4.247   1.00 14.38 ?  81  CYS   B HB3  1 
ATOM   5843 H HG   . CYS   B 1 81  ? 45.441 -11.403 4.570   1.00 15.17 ?  81  CYS   B HG   1 
ATOM   5844 N N    . VAL   B 1 82  ? 43.305 -10.456 0.311   1.00 11.30 ?  82  VAL   B N    1 
ATOM   5845 C CA   . VAL   B 1 82  ? 44.074 -10.340 -0.927  1.00 11.08 ?  82  VAL   B CA   1 
ATOM   5846 C C    . VAL   B 1 82  ? 45.415 -9.697  -0.606  1.00 11.11 ?  82  VAL   B C    1 
ATOM   5847 O O    . VAL   B 1 82  ? 45.463 -8.580  -0.078  1.00 12.19 ?  82  VAL   B O    1 
ATOM   5848 C CB   . VAL   B 1 82  ? 43.337 -9.500  -1.983  1.00 12.49 ?  82  VAL   B CB   1 
ATOM   5849 C CG1  . VAL   B 1 82  ? 44.194 -9.339  -3.241  1.00 13.44 ?  82  VAL   B CG1  1 
ATOM   5850 C CG2  . VAL   B 1 82  ? 41.977 -10.100 -2.317  1.00 13.36 ?  82  VAL   B CG2  1 
ATOM   5851 H H    . VAL   B 1 82  ? 42.942 -9.707  0.548   1.00 13.58 ?  82  VAL   B H    1 
ATOM   5852 H HA   . VAL   B 1 82  ? 44.237 -11.221 -1.294  1.00 13.31 ?  82  VAL   B HA   1 
ATOM   5853 H HB   . VAL   B 1 82  ? 43.190 -8.615  -1.624  1.00 15.01 ?  82  VAL   B HB   1 
ATOM   5854 H HG11 . VAL   B 1 82  ? 43.635 -9.013  -3.962  1.00 16.14 ?  82  VAL   B HG11 1 
ATOM   5855 H HG12 . VAL   B 1 82  ? 44.903 -8.695  -3.062  1.00 16.14 ?  82  VAL   B HG12 1 
ATOM   5856 H HG13 . VAL   B 1 82  ? 44.579 -10.195 -3.477  1.00 16.14 ?  82  VAL   B HG13 1 
ATOM   5857 H HG21 . VAL   B 1 82  ? 41.551 -9.559  -3.005  1.00 16.04 ?  82  VAL   B HG21 1 
ATOM   5858 H HG22 . VAL   B 1 82  ? 42.097 -11.006 -2.643  1.00 16.04 ?  82  VAL   B HG22 1 
ATOM   5859 H HG23 . VAL   B 1 82  ? 41.428 -10.105 -1.518  1.00 16.04 ?  82  VAL   B HG23 1 
ATOM   5860 N N    . LEU   B 1 83  ? 46.497 -10.380 -0.974  1.00 10.86 ?  83  LEU   B N    1 
ATOM   5861 C CA   . LEU   B 1 83  ? 47.850 -9.863  -0.850  1.00 10.78 ?  83  LEU   B CA   1 
ATOM   5862 C C    . LEU   B 1 83  ? 48.555 -10.018 -2.197  1.00 11.08 ?  83  LEU   B C    1 
ATOM   5863 O O    . LEU   B 1 83  ? 47.956 -10.441 -3.188  1.00 10.80 ?  83  LEU   B O    1 
ATOM   5864 C CB   . LEU   B 1 83  ? 48.595 -10.539 0.306   1.00 11.28 ?  83  LEU   B CB   1 
ATOM   5865 C CG   . LEU   B 1 83  ? 48.093 -10.182 1.713   1.00 12.66 ?  83  LEU   B CG   1 
ATOM   5866 C CD1  . LEU   B 1 83  ? 48.735 -11.051 2.784   1.00 13.00 ?  83  LEU   B CD1  1 
ATOM   5867 C CD2  . LEU   B 1 83  ? 48.286 -8.688  2.032   1.00 14.15 ?  83  LEU   B CD2  1 
ATOM   5868 H H    . LEU   B 1 83  ? 46.462 -11.176 -1.319  1.00 13.05 ?  83  LEU   B H    1 
ATOM   5869 H HA   . LEU   B 1 83  ? 47.797 -8.920  -0.662  1.00 12.96 ?  83  LEU   B HA   1 
ATOM   5870 H HB2  . LEU   B 1 83  ? 48.518 -11.502 0.203   1.00 13.55 ?  83  LEU   B HB2  1 
ATOM   5871 H HB3  . LEU   B 1 83  ? 49.529 -10.285 0.256   1.00 13.55 ?  83  LEU   B HB3  1 
ATOM   5872 H HG   . LEU   B 1 83  ? 47.143 -10.360 1.742   1.00 15.21 ?  83  LEU   B HG   1 
ATOM   5873 H HD11 . LEU   B 1 83  ? 48.382 -10.791 3.655   1.00 15.62 ?  83  LEU   B HD11 1 
ATOM   5874 H HD12 . LEU   B 1 83  ? 48.518 -11.983 2.614   1.00 15.62 ?  83  LEU   B HD12 1 
ATOM   5875 H HD13 . LEU   B 1 83  ? 49.694 -10.927 2.770   1.00 15.62 ?  83  LEU   B HD13 1 
ATOM   5876 H HD21 . LEU   B 1 83  ? 48.073 -8.534  2.965   1.00 17.00 ?  83  LEU   B HD21 1 
ATOM   5877 H HD22 . LEU   B 1 83  ? 49.207 -8.441  1.856   1.00 17.00 ?  83  LEU   B HD22 1 
ATOM   5878 H HD23 . LEU   B 1 83  ? 47.691 -8.167  1.467   1.00 17.00 ?  83  LEU   B HD23 1 
ATOM   5879 N N    . SER   B 1 84  ? 49.833 -9.650  -2.259  1.00 12.08 ?  84  SER   B N    1 
ATOM   5880 C CA   . SER   B 1 84  ? 50.560 -9.792  -3.515  1.00 12.12 ?  84  SER   B CA   1 
ATOM   5881 C C    . SER   B 1 84  ? 50.735 -11.260 -3.899  1.00 11.25 ?  84  SER   B C    1 
ATOM   5882 O O    . SER   B 1 84  ? 50.843 -12.136 -3.044  1.00 11.55 ?  84  SER   B O    1 
ATOM   5883 C CB   . SER   B 1 84  ? 51.946 -9.162  -3.396  1.00 13.48 ?  84  SER   B CB   1 
ATOM   5884 O OG   . SER   B 1 84  ? 52.693 -9.390  -4.578  1.00 14.79 ?  84  SER   B OG   1 
ATOM   5885 H H    . SER   B 1 84  ? 50.283 -9.314  -1.611  1.00 14.52 ?  84  SER   B H    1 
ATOM   5886 H HA   . SER   B 1 84  ? 50.076 -9.354  -4.224  1.00 14.56 ?  84  SER   B HA   1 
ATOM   5887 H HB2  . SER   B 1 84  ? 51.846 -8.205  -3.267  1.00 16.20 ?  84  SER   B HB2  1 
ATOM   5888 H HB3  . SER   B 1 84  ? 52.415 -9.552  -2.642  1.00 16.20 ?  84  SER   B HB3  1 
ATOM   5889 H HG   . SER   B 1 84  ? 53.464 -9.037  -4.507  1.00 17.76 ?  84  SER   B HG   1 
ATOM   5890 N N    . GLY   B 1 85  ? 50.799 -11.516 -5.198  1.00 12.02 ?  85  GLY   B N    1 
ATOM   5891 C CA   . GLY   B 1 85  ? 51.157 -12.819 -5.705  1.00 13.25 ?  85  GLY   B CA   1 
ATOM   5892 C C    . GLY   B 1 85  ? 52.628 -12.992 -6.015  1.00 12.02 ?  85  GLY   B C    1 
ATOM   5893 O O    . GLY   B 1 85  ? 53.018 -14.071 -6.461  1.00 12.89 ?  85  GLY   B O    1 
ATOM   5894 H H    . GLY   B 1 85  ? 50.634 -10.947 -5.817  1.00 14.44 ?  85  GLY   B H    1 
ATOM   5895 H HA2  . GLY   B 1 85  ? 50.911 -13.499 -5.051  1.00 15.92 ?  85  GLY   B HA2  1 
ATOM   5896 H HA3  . GLY   B 1 85  ? 50.664 -13.002 -6.517  1.00 15.92 ?  85  GLY   B HA3  1 
ATOM   5897 N N    . HIS   B 1 86  ? 53.468 -11.975 -5.804  1.00 12.18 ?  86  HIS   B N    1 
ATOM   5898 C CA   . HIS   B 1 86  ? 54.937 -12.120 -5.887  1.00 12.21 ?  86  HIS   B CA   1 
ATOM   5899 C C    . HIS   B 1 86  ? 55.315 -12.648 -7.269  1.00 12.43 ?  86  HIS   B C    1 
ATOM   5900 O O    . HIS   B 1 86  ? 54.915 -12.056 -8.285  1.00 13.65 ?  86  HIS   B O    1 
ATOM   5901 C CB   . HIS   B 1 86  ? 55.437 -12.945 -4.703  1.00 12.72 ?  86  HIS   B CB   1 
ATOM   5902 C CG   . HIS   B 1 86  ? 55.111 -12.329 -3.385  1.00 13.12 ?  86  HIS   B CG   1 
ATOM   5903 N ND1  . HIS   B 1 86  ? 55.926 -11.401 -2.774  1.00 14.83 ?  86  HIS   B ND1  1 
ATOM   5904 C CD2  . HIS   B 1 86  ? 54.035 -12.485 -2.576  1.00 13.43 ?  86  HIS   B CD2  1 
ATOM   5905 C CE1  . HIS   B 1 86  ? 55.358 -11.009 -1.646  1.00 14.56 ?  86  HIS   B CE1  1 
ATOM   5906 N NE2  . HIS   B 1 86  ? 54.209 -11.643 -1.506  1.00 13.96 ?  86  HIS   B NE2  1 
ATOM   5907 H H    . HIS   B 1 86  ? 53.214 -11.179 -5.608  1.00 14.64 ?  86  HIS   B H    1 
ATOM   5908 H HA   . HIS   B 1 86  ? 55.334 -11.244 -5.802  1.00 14.67 ?  86  HIS   B HA   1 
ATOM   5909 H HB2  . HIS   B 1 86  ? 55.030 -13.826 -4.733  1.00 15.28 ?  86  HIS   B HB2  1 
ATOM   5910 H HB3  . HIS   B 1 86  ? 56.403 -13.028 -4.757  1.00 15.28 ?  86  HIS   B HB3  1 
ATOM   5911 H HD2  . HIS   B 1 86  ? 53.301 -13.047 -2.730  1.00 16.13 ?  86  HIS   B HD2  1 
ATOM   5912 H HE1  . HIS   B 1 86  ? 55.710 -10.407 -1.035  1.00 17.49 ?  86  HIS   B HE1  1 
ATOM   5913 H HE2  . HIS   B 1 86  ? 53.665 -11.578 -0.835  1.00 16.77 ?  86  HIS   B HE2  1 
ATOM   5914 N N    . ASN   B 1 87  ? 56.090 -13.727 -7.365  1.00 12.85 ?  87  ASN   B N    1 
ATOM   5915 C CA   . ASN   B 1 87  ? 56.497 -14.312 -8.634  1.00 13.81 ?  87  ASN   B CA   1 
ATOM   5916 C C    . ASN   B 1 87  ? 55.512 -15.355 -9.149  1.00 13.62 ?  87  ASN   B C    1 
ATOM   5917 O O    . ASN   B 1 87  ? 55.831 -16.059 -10.113 1.00 15.79 ?  87  ASN   B O    1 
ATOM   5918 C CB   . ASN   B 1 87  ? 57.888 -14.945 -8.506  1.00 15.37 ?  87  ASN   B CB   1 
ATOM   5919 C CG   . ASN   B 1 87  ? 57.942 -16.035 -7.447  1.00 16.30 ?  87  ASN   B CG   1 
ATOM   5920 O OD1  . ASN   B 1 87  ? 57.301 -15.927 -6.399  1.00 15.35 ?  87  ASN   B OD1  1 
ATOM   5921 N ND2  . ASN   B 1 87  ? 58.707 -17.102 -7.722  1.00 19.13 ?  87  ASN   B ND2  1 
ATOM   5922 H H    . ASN   B 1 87  ? 56.386 -14.162 -6.686  1.00 15.43 ?  87  ASN   B H    1 
ATOM   5923 H HA   . ASN   B 1 87  ? 56.543 -13.617 -9.300  1.00 16.59 ?  87  ASN   B HA   1 
ATOM   5924 H HB2  . ASN   B 1 87  ? 58.137 -15.341 -9.361  1.00 18.46 ?  87  ASN   B HB2  1 
ATOM   5925 H HB3  . ASN   B 1 87  ? 58.518 -14.256 -8.263  1.00 18.46 ?  87  ASN   B HB3  1 
ATOM   5926 H HD21 . ASN   B 1 87  ? 58.778 -17.743 -7.154  1.00 22.97 ?  87  ASN   B HD21 1 
ATOM   5927 H HD22 . ASN   B 1 87  ? 59.141 -17.144 -8.469  1.00 22.97 ?  87  ASN   B HD22 1 
ATOM   5928 N N    . LEU   B 1 88  ? 54.330 -15.471 -8.535  1.00 12.71 ?  88  LEU   B N    1 
ATOM   5929 C CA   . LEU   B 1 88  ? 53.356 -16.502 -8.874  1.00 12.72 ?  88  LEU   B CA   1 
ATOM   5930 C C    . LEU   B 1 88  ? 52.128 -15.975 -9.595  1.00 12.58 ?  88  LEU   B C    1 
ATOM   5931 O O    . LEU   B 1 88  ? 51.541 -16.697 -10.403 1.00 14.20 ?  88  LEU   B O    1 
ATOM   5932 C CB   . LEU   B 1 88  ? 52.887 -17.191 -7.591  1.00 14.19 ?  88  LEU   B CB   1 
ATOM   5933 C CG   . LEU   B 1 88  ? 54.024 -17.845 -6.813  1.00 16.78 ?  88  LEU   B CG   1 
ATOM   5934 C CD1  . LEU   B 1 88  ? 53.564 -18.303 -5.435  1.00 18.29 ?  88  LEU   B CD1  1 
ATOM   5935 C CD2  . LEU   B 1 88  ? 54.593 -19.000 -7.617  1.00 20.49 ?  88  LEU   B CD2  1 
ATOM   5936 H H    . LEU   B 1 88  ? 54.064 -14.949 -7.901  1.00 15.26 ?  88  LEU   B H    1 
ATOM   5937 H HA   . LEU   B 1 88  ? 53.779 -17.168 -9.435  1.00 15.28 ?  88  LEU   B HA   1 
ATOM   5938 H HB2  . LEU   B 1 88  ? 52.460 -16.539 -7.013  1.00 17.04 ?  88  LEU   B HB2  1 
ATOM   5939 H HB3  . LEU   B 1 88  ? 52.242 -17.889 -7.824  1.00 17.04 ?  88  LEU   B HB3  1 
ATOM   5940 H HG   . LEU   B 1 88  ? 54.726 -17.192 -6.689  1.00 20.16 ?  88  LEU   B HG   1 
ATOM   5941 H HD11 . LEU   B 1 88  ? 54.316 -18.709 -4.975  1.00 21.97 ?  88  LEU   B HD11 1 
ATOM   5942 H HD12 . LEU   B 1 88  ? 53.246 -17.535 -4.937  1.00 21.97 ?  88  LEU   B HD12 1 
ATOM   5943 H HD13 . LEU   B 1 88  ? 52.851 -18.950 -5.541  1.00 21.97 ?  88  LEU   B HD13 1 
ATOM   5944 H HD21 . LEU   B 1 88  ? 55.175 -19.518 -7.044  1.00 24.61 ?  88  LEU   B HD21 1 
ATOM   5945 H HD22 . LEU   B 1 88  ? 53.862 -19.550 -7.937  1.00 24.61 ?  88  LEU   B HD22 1 
ATOM   5946 H HD23 . LEU   B 1 88  ? 55.093 -18.642 -8.367  1.00 24.61 ?  88  LEU   B HD23 1 
ATOM   5947 N N    . ALA   B 1 89  ? 51.708 -14.754 -9.288  1.00 12.16 ?  89  ALA   B N    1 
ATOM   5948 C CA   . ALA   B 1 89  ? 50.435 -14.234 -9.761  1.00 11.48 ?  89  ALA   B CA   1 
ATOM   5949 C C    . ALA   B 1 89  ? 50.428 -12.748 -9.468  1.00 11.83 ?  89  ALA   B C    1 
ATOM   5950 O O    . ALA   B 1 89  ? 51.236 -12.256 -8.684  1.00 12.64 ?  89  ALA   B O    1 
ATOM   5951 C CB   . ALA   B 1 89  ? 49.275 -14.899 -9.023  1.00 11.61 ?  89  ALA   B CB   1 
ATOM   5952 H H    . ALA   B 1 89  ? 52.148 -14.202 -8.805  1.00 14.60 ?  89  ALA   B H    1 
ATOM   5953 H HA   . ALA   B 1 89  ? 50.339 -14.387 -10.723 1.00 13.79 ?  89  ALA   B HA   1 
ATOM   5954 H HB1  . ALA   B 1 89  ? 48.439 -14.544 -9.367  1.00 13.94 ?  89  ALA   B HB1  1 
ATOM   5955 H HB2  . ALA   B 1 89  ? 49.310 -15.859 -9.169  1.00 13.94 ?  89  ALA   B HB2  1 
ATOM   5956 H HB3  . ALA   B 1 89  ? 49.355 -14.704 -8.078  1.00 13.94 ?  89  ALA   B HB3  1 
ATOM   5957 N N    . LYS   B 1 90  ? 49.486 -12.034 -10.066 1.00 12.58 ?  90  LYS   B N    1 
ATOM   5958 C CA   . LYS   B 1 90  ? 49.310 -10.648 -9.652  1.00 12.20 ?  90  LYS   B CA   1 
ATOM   5959 C C    . LYS   B 1 90  ? 48.943 -10.572 -8.172  1.00 12.09 ?  90  LYS   B C    1 
ATOM   5960 O O    . LYS   B 1 90  ? 49.571 -9.828  -7.407  1.00 12.42 ?  90  LYS   B O    1 
ATOM   5961 C CB   . LYS   B 1 90  ? 48.267 -9.964  -10.529 1.00 13.50 ?  90  LYS   B CB   1 
ATOM   5962 C CG   . LYS   B 1 90  ? 47.906 -8.551  -10.094 1.00 14.05 ?  90  LYS   B CG   1 
ATOM   5963 C CD   . LYS   B 1 90  ? 49.076 -7.602  -10.127 1.00 15.58 ?  90  LYS   B CD   1 
ATOM   5964 C CE   . LYS   B 1 90  ? 48.571 -6.226  -9.734  1.00 17.43 ?  90  LYS   B CE   1 
ATOM   5965 N NZ   . LYS   B 1 90  ? 49.641 -5.190  -9.735  1.00 17.24 ?  90  LYS   B NZ   1 
ATOM   5966 H H    . LYS   B 1 90  ? 48.962 -12.317 -10.681 1.00 15.11 ?  90  LYS   B H    1 
ATOM   5967 H HA   . LYS   B 1 90  ? 50.156 -10.184 -9.768  1.00 14.66 ?  90  LYS   B HA   1 
ATOM   5968 H HB2  . LYS   B 1 90  ? 48.613 -9.917  -11.434 1.00 16.22 ?  90  LYS   B HB2  1 
ATOM   5969 H HB3  . LYS   B 1 90  ? 47.460 -10.499 -10.516 1.00 16.22 ?  90  LYS   B HB3  1 
ATOM   5970 H HG2  . LYS   B 1 90  ? 47.228 -8.206  -10.693 1.00 16.88 ?  90  LYS   B HG2  1 
ATOM   5971 H HG3  . LYS   B 1 90  ? 47.559 -8.571  -9.186  1.00 16.88 ?  90  LYS   B HG3  1 
ATOM   5972 H HD2  . LYS   B 1 90  ? 49.755 -7.877  -9.487  1.00 18.72 ?  90  LYS   B HD2  1 
ATOM   5973 H HD3  . LYS   B 1 90  ? 49.446 -7.553  -11.022 1.00 18.72 ?  90  LYS   B HD3  1 
ATOM   5974 H HE2  . LYS   B 1 90  ? 47.884 -5.943  -10.360 1.00 20.94 ?  90  LYS   B HE2  1 
ATOM   5975 H HE3  . LYS   B 1 90  ? 48.199 -6.262  -8.836  1.00 20.94 ?  90  LYS   B HE3  1 
ATOM   5976 H HZ1  . LYS   B 1 90  ? 49.305 -4.395  -9.501  1.00 20.71 ?  90  LYS   B HZ1  1 
ATOM   5977 H HZ2  . LYS   B 1 90  ? 50.282 -5.409  -9.160  1.00 20.71 ?  90  LYS   B HZ2  1 
ATOM   5978 H HZ3  . LYS   B 1 90  ? 49.996 -5.118  -10.550 1.00 20.71 ?  90  LYS   B HZ3  1 
ATOM   5979 N N    . HIS   B 1 91  ? 47.958 -11.369 -7.747  1.00 11.01 ?  91  HIS   B N    1 
ATOM   5980 C CA   . HIS   B 1 91  ? 47.460 -11.392 -6.380  1.00 11.22 ?  91  HIS   B CA   1 
ATOM   5981 C C    . HIS   B 1 91  ? 47.458 -12.821 -5.858  1.00 10.52 ?  91  HIS   B C    1 
ATOM   5982 O O    . HIS   B 1 91  ? 47.228 -13.766 -6.618  1.00 11.12 ?  91  HIS   B O    1 
ATOM   5983 C CB   . HIS   B 1 91  ? 46.010 -10.909 -6.295  1.00 12.52 ?  91  HIS   B CB   1 
ATOM   5984 C CG   . HIS   B 1 91  ? 45.818 -9.491  -6.705  1.00 15.82 ?  91  HIS   B CG   1 
ATOM   5985 N ND1  . HIS   B 1 91  ? 46.446 -8.432  -6.083  1.00 18.69 ?  91  HIS   B ND1  1 
ATOM   5986 C CD2  . HIS   B 1 91  ? 45.024 -8.953  -7.655  1.00 18.78 ?  91  HIS   B CD2  1 
ATOM   5987 C CE1  . HIS   B 1 91  ? 46.066 -7.301  -6.654  1.00 20.14 ?  91  HIS   B CE1  1 
ATOM   5988 N NE2  . HIS   B 1 91  ? 45.198 -7.591  -7.607  1.00 20.48 ?  91  HIS   B NE2  1 
ATOM   5989 H H    . HIS   B 1 91  ? 47.542 -11.922 -8.264  1.00 13.23 ?  91  HIS   B H    1 
ATOM   5990 H HA   . HIS   B 1 91  ? 48.018 -10.834 -5.812  1.00 13.48 ?  91  HIS   B HA   1 
ATOM   5991 H HB2  . HIS   B 1 91  ? 45.464 -11.460 -6.875  1.00 15.04 ?  91  HIS   B HB2  1 
ATOM   5992 H HB3  . HIS   B 1 91  ? 45.708 -10.996 -5.378  1.00 15.04 ?  91  HIS   B HB3  1 
ATOM   5993 H HD1  . HIS   B 1 91  ? 47.009 -8.495  -5.433  1.00 22.44 ?  91  HIS   B HD1  1 
ATOM   5994 H HD2  . HIS   B 1 91  ? 44.472 -9.412  -8.244  1.00 22.55 ?  91  HIS   B HD2  1 
ATOM   5995 H HE1  . HIS   B 1 91  ? 46.355 -6.446  -6.417  1.00 24.18 ?  91  HIS   B HE1  1 
ATOM   5996 N N    . CYS   B 1 92  ? 47.635 -12.957 -4.547  1.00 10.49 ?  92  CYS   B N    1 
ATOM   5997 C CA   . CYS   B 1 92  ? 47.323 -14.188 -3.831  1.00 10.13 ?  92  CYS   B CA   1 
ATOM   5998 C C    . CYS   B 1 92  ? 46.097 -13.949 -2.957  1.00 10.21 ?  92  CYS   B C    1 
ATOM   5999 O O    . CYS   B 1 92  ? 46.097 -13.039 -2.119  1.00 10.85 ?  92  CYS   B O    1 
ATOM   6000 C CB   . CYS   B 1 92  ? 48.497 -14.646 -2.972  1.00 10.90 ?  92  CYS   B CB   1 
ATOM   6001 S SG   . CYS   B 1 92  ? 48.128 -16.179 -2.063  1.00 11.16 ?  92  CYS   B SG   1 
ATOM   6002 H H    . CYS   B 1 92  ? 47.956 -12.332 -4.045  1.00 12.60 ?  92  CYS   B H    1 
ATOM   6003 H HA   . CYS   B 1 92  ? 47.119 -14.881 -4.478  1.00 12.18 ?  92  CYS   B HA   1 
ATOM   6004 H HB2  . CYS   B 1 92  ? 49.261 -14.801 -3.547  1.00 13.10 ?  92  CYS   B HB2  1 
ATOM   6005 H HB3  . CYS   B 1 92  ? 48.697 -13.950 -2.329  1.00 13.10 ?  92  CYS   B HB3  1 
ATOM   6006 H HG   . CYS   B 1 92  ? 49.103 -16.492 -1.434  1.00 13.41 ?  92  CYS   B HG   1 
ATOM   6007 N N    . LEU   B 1 93  ? 45.058 -14.763 -3.156  1.00 9.89  ?  93  LEU   B N    1 
ATOM   6008 C CA   . LEU   B 1 93  ? 43.875 -14.767 -2.304  1.00 10.15 ?  93  LEU   B CA   1 
ATOM   6009 C C    . LEU   B 1 93  ? 44.096 -15.823 -1.231  1.00 9.36  ?  93  LEU   B C    1 
ATOM   6010 O O    . LEU   B 1 93  ? 44.055 -17.023 -1.519  1.00 10.45 ?  93  LEU   B O    1 
ATOM   6011 C CB   . LEU   B 1 93  ? 42.621 -15.069 -3.122  1.00 10.35 ?  93  LEU   B CB   1 
ATOM   6012 C CG   . LEU   B 1 93  ? 41.325 -15.071 -2.308  1.00 11.33 ?  93  LEU   B CG   1 
ATOM   6013 C CD1  . LEU   B 1 93  ? 40.961 -13.678 -1.820  1.00 11.85 ?  93  LEU   B CD1  1 
ATOM   6014 C CD2  . LEU   B 1 93  ? 40.179 -15.670 -3.124  1.00 11.71 ?  93  LEU   B CD2  1 
ATOM   6015 H H    . LEU   B 1 93  ? 45.020 -15.331 -3.807  1.00 11.88 ?  93  LEU   B H    1 
ATOM   6016 H HA   . LEU   B 1 93  ? 43.778 -13.901 -1.883  1.00 12.20 ?  93  LEU   B HA   1 
ATOM   6017 H HB2  . LEU   B 1 93  ? 42.528 -14.394 -3.809  1.00 12.44 ?  93  LEU   B HB2  1 
ATOM   6018 H HB3  . LEU   B 1 93  ? 42.713 -15.941 -3.523  1.00 12.44 ?  93  LEU   B HB3  1 
ATOM   6019 H HG   . LEU   B 1 93  ? 41.439 -15.629 -1.523  1.00 13.62 ?  93  LEU   B HG   1 
ATOM   6020 H HD11 . LEU   B 1 93  ? 40.105 -13.708 -1.373  1.00 14.24 ?  93  LEU   B HD11 1 
ATOM   6021 H HD12 . LEU   B 1 93  ? 41.649 -13.367 -1.216  1.00 14.24 ?  93  LEU   B HD12 1 
ATOM   6022 H HD13 . LEU   B 1 93  ? 40.909 -13.083 -2.593  1.00 14.24 ?  93  LEU   B HD13 1 
ATOM   6023 H HD21 . LEU   B 1 93  ? 39.365 -15.658 -2.588  1.00 14.07 ?  93  LEU   B HD21 1 
ATOM   6024 H HD22 . LEU   B 1 93  ? 40.048 -15.140 -3.926  1.00 14.07 ?  93  LEU   B HD22 1 
ATOM   6025 H HD23 . LEU   B 1 93  ? 40.400 -16.583 -3.361  1.00 14.07 ?  93  LEU   B HD23 1 
ATOM   6026 N N    . HIS   B 1 94  ? 44.370 -15.379 -0.010  1.00 9.63  ?  94  HIS   B N    1 
ATOM   6027 C CA   . HIS   B 1 94  ? 44.583 -16.286 1.109   1.00 9.79  ?  94  HIS   B CA   1 
ATOM   6028 C C    . HIS   B 1 94  ? 43.219 -16.633 1.687   1.00 10.48 ?  94  HIS   B C    1 
ATOM   6029 O O    . HIS   B 1 94  ? 42.548 -15.756 2.234   1.00 11.52 ?  94  HIS   B O    1 
ATOM   6030 C CB   . HIS   B 1 94  ? 45.450 -15.616 2.173   1.00 10.51 ?  94  HIS   B CB   1 
ATOM   6031 C CG   . HIS   B 1 94  ? 46.837 -15.311 1.711   1.00 10.43 ?  94  HIS   B CG   1 
ATOM   6032 N ND1  . HIS   B 1 94  ? 47.864 -16.229 1.798   1.00 10.53 ?  94  HIS   B ND1  1 
ATOM   6033 C CD2  . HIS   B 1 94  ? 47.344 -14.211 1.104   1.00 10.87 ?  94  HIS   B CD2  1 
ATOM   6034 C CE1  . HIS   B 1 94  ? 48.956 -15.680 1.293   1.00 11.00 ?  94  HIS   B CE1  1 
ATOM   6035 N NE2  . HIS   B 1 94  ? 48.668 -14.463 0.859   1.00 11.12 ?  94  HIS   B NE2  1 
ATOM   6036 H H    . HIS   B 1 94  ? 44.444 -14.540 0.193   1.00 11.57 ?  94  HIS   B H    1 
ATOM   6037 H HA   . HIS   B 1 94  ? 45.022 -17.094 0.801   1.00 11.77 ?  94  HIS   B HA   1 
ATOM   6038 H HB2  . HIS   B 1 94  ? 45.037 -14.779 2.432   1.00 12.63 ?  94  HIS   B HB2  1 
ATOM   6039 H HB3  . HIS   B 1 94  ? 45.512 -16.207 2.939   1.00 12.63 ?  94  HIS   B HB3  1 
ATOM   6040 H HD2  . HIS   B 1 94  ? 46.895 -13.437 0.904   1.00 13.07 ?  94  HIS   B HD2  1 
ATOM   6041 H HE1  . HIS   B 1 94  ? 49.786 -16.115 1.240   1.00 13.22 ?  94  HIS   B HE1  1 
ATOM   6042 H HE2  . HIS   B 1 94  ? 49.231 -13.938 0.494   1.00 13.36 ?  94  HIS   B HE2  1 
ATOM   6043 N N    . VAL   B 1 95  ? 42.790 -17.887 1.552   1.00 10.30 ?  95  VAL   B N    1 
ATOM   6044 C CA   . VAL   B 1 95  ? 41.454 -18.318 1.976   1.00 10.45 ?  95  VAL   B CA   1 
ATOM   6045 C C    . VAL   B 1 95  ? 41.606 -19.351 3.076   1.00 10.66 ?  95  VAL   B C    1 
ATOM   6046 O O    . VAL   B 1 95  ? 42.377 -20.304 2.926   1.00 11.29 ?  95  VAL   B O    1 
ATOM   6047 C CB   . VAL   B 1 95  ? 40.642 -18.927 0.818   1.00 10.79 ?  95  VAL   B CB   1 
ATOM   6048 C CG1  . VAL   B 1 95  ? 39.266 -19.386 1.306   1.00 11.94 ?  95  VAL   B CG1  1 
ATOM   6049 C CG2  . VAL   B 1 95  ? 40.509 -17.946 -0.325  1.00 11.05 ?  95  VAL   B CG2  1 
ATOM   6050 H H    . VAL   B 1 95  ? 43.263 -18.523 1.202   1.00 12.38 ?  95  VAL   B H    1 
ATOM   6051 H HA   . VAL   B 1 95  ? 40.969 -17.557 2.328   1.00 12.56 ?  95  VAL   B HA   1 
ATOM   6052 H HB   . VAL   B 1 95  ? 41.109 -19.702 0.483   1.00 12.96 ?  95  VAL   B HB   1 
ATOM   6053 H HG11 . VAL   B 1 95  ? 38.700 -19.565 0.536   1.00 14.35 ?  95  VAL   B HG11 1 
ATOM   6054 H HG12 . VAL   B 1 95  ? 39.366 -20.194 1.833   1.00 14.35 ?  95  VAL   B HG12 1 
ATOM   6055 H HG13 . VAL   B 1 95  ? 38.866 -18.685 1.847   1.00 14.35 ?  95  VAL   B HG13 1 
ATOM   6056 H HG21 . VAL   B 1 95  ? 39.938 -18.337 -1.008  1.00 13.28 ?  95  VAL   B HG21 1 
ATOM   6057 H HG22 . VAL   B 1 95  ? 40.108 -17.126 0.006   1.00 13.28 ?  95  VAL   B HG22 1 
ATOM   6058 H HG23 . VAL   B 1 95  ? 41.385 -17.766 -0.689  1.00 13.28 ?  95  VAL   B HG23 1 
ATOM   6059 N N    . VAL   B 1 96  ? 40.874 -19.175 4.168   1.00 11.27 ?  96  VAL   B N    1 
ATOM   6060 C CA   . VAL   B 1 96  ? 40.949 -20.087 5.312   1.00 11.85 ?  96  VAL   B CA   1 
ATOM   6061 C C    . VAL   B 1 96  ? 39.763 -21.051 5.269   1.00 12.41 ?  96  VAL   B C    1 
ATOM   6062 O O    . VAL   B 1 96  ? 38.641 -20.695 5.646   1.00 12.79 ?  96  VAL   B O    1 
ATOM   6063 C CB   . VAL   B 1 96  ? 40.994 -19.340 6.647   1.00 12.63 ?  96  VAL   B CB   1 
ATOM   6064 C CG1  . VAL   B 1 96  ? 41.147 -20.332 7.797   1.00 13.37 ?  96  VAL   B CG1  1 
ATOM   6065 C CG2  . VAL   B 1 96  ? 42.120 -18.315 6.664   1.00 13.06 ?  96  VAL   B CG2  1 
ATOM   6066 H H    . VAL   B 1 96  ? 40.311 -18.530 4.280   1.00 13.54 ?  96  VAL   B H    1 
ATOM   6067 H HA   . VAL   B 1 96  ? 41.763 -20.611 5.243   1.00 14.24 ?  96  VAL   B HA   1 
ATOM   6068 H HB   . VAL   B 1 96  ? 40.156 -18.867 6.776   1.00 15.17 ?  96  VAL   B HB   1 
ATOM   6069 H HG11 . VAL   B 1 96  ? 41.342 -19.842 8.615   1.00 16.07 ?  96  VAL   B HG11 1 
ATOM   6070 H HG12 . VAL   B 1 96  ? 40.320 -20.828 7.906   1.00 16.07 ?  96  VAL   B HG12 1 
ATOM   6071 H HG13 . VAL   B 1 96  ? 41.876 -20.939 7.599   1.00 16.07 ?  96  VAL   B HG13 1 
ATOM   6072 H HG21 . VAL   B 1 96  ? 42.160 -17.903 7.545   1.00 15.69 ?  96  VAL   B HG21 1 
ATOM   6073 H HG22 . VAL   B 1 96  ? 42.957 -18.761 6.471   1.00 15.69 ?  96  VAL   B HG22 1 
ATOM   6074 H HG23 . VAL   B 1 96  ? 41.940 -17.637 5.995   1.00 15.69 ?  96  VAL   B HG23 1 
ATOM   6075 N N    . GLY   B 1 97  ? 40.003 -22.286 4.835   1.00 12.50 ?  97  GLY   B N    1 
ATOM   6076 C CA   . GLY   B 1 97  ? 39.026 -23.339 4.995   1.00 13.59 ?  97  GLY   B CA   1 
ATOM   6077 C C    . GLY   B 1 97  ? 39.156 -23.951 6.374   1.00 14.90 ?  97  GLY   B C    1 
ATOM   6078 O O    . GLY   B 1 97  ? 40.199 -23.822 7.024   1.00 15.67 ?  97  GLY   B O    1 
ATOM   6079 H H    . GLY   B 1 97  ? 40.735 -22.536 4.436   1.00 15.02 ?  97  GLY   B H    1 
ATOM   6080 H HA2  . GLY   B 1 97  ? 38.134 -22.967 4.876   1.00 16.33 ?  97  GLY   B HA2  1 
ATOM   6081 H HA3  . GLY   B 1 97  ? 39.165 -24.026 4.319   1.00 16.33 ?  97  GLY   B HA3  1 
ATOM   6082 N N    . PRO   B 1 98  ? 38.107 -24.625 6.850   1.00 16.44 ?  98  PRO   B N    1 
ATOM   6083 C CA   . PRO   B 1 98  ? 38.209 -25.328 8.133   1.00 18.13 ?  98  PRO   B CA   1 
ATOM   6084 C C    . PRO   B 1 98  ? 39.239 -26.449 8.079   1.00 18.10 ?  98  PRO   B C    1 
ATOM   6085 O O    . PRO   B 1 98  ? 39.340 -27.177 7.095   1.00 18.09 ?  98  PRO   B O    1 
ATOM   6086 C CB   . PRO   B 1 98  ? 36.792 -25.872 8.350   1.00 19.29 ?  98  PRO   B CB   1 
ATOM   6087 C CG   . PRO   B 1 98  ? 36.197 -25.974 6.996   1.00 18.26 ?  98  PRO   B CG   1 
ATOM   6088 C CD   . PRO   B 1 98  ? 36.782 -24.807 6.224   1.00 17.30 ?  98  PRO   B CD   1 
ATOM   6089 H HA   . PRO   B 1 98  ? 38.436 -24.706 8.834   1.00 21.77 ?  98  PRO   B HA   1 
ATOM   6090 H HB2  . PRO   B 1 98  ? 36.843 -26.749 8.766   1.00 23.17 ?  98  PRO   B HB2  1 
ATOM   6091 H HB3  . PRO   B 1 98  ? 36.288 -25.258 8.898   1.00 23.17 ?  98  PRO   B HB3  1 
ATOM   6092 H HG2  . PRO   B 1 98  ? 36.454 -26.819 6.585   1.00 21.92 ?  98  PRO   B HG2  1 
ATOM   6093 H HG3  . PRO   B 1 98  ? 35.234 -25.902 7.052   1.00 21.92 ?  98  PRO   B HG3  1 
ATOM   6094 H HD2  . PRO   B 1 98  ? 36.864 -25.035 5.279   1.00 20.78 ?  98  PRO   B HD2  1 
ATOM   6095 H HD3  . PRO   B 1 98  ? 36.239 -24.014 6.347   1.00 20.78 ?  98  PRO   B HD3  1 
ATOM   6096 N N    . ASN   B 1 99  ? 40.012 -26.574 9.153   1.00 19.71 ?  99  ASN   B N    1 
ATOM   6097 C CA   . ASN   B 1 99  ? 40.996 -27.647 9.312   1.00 21.13 ?  99  ASN   B CA   1 
ATOM   6098 C C    . ASN   B 1 99  ? 40.387 -28.721 10.211  1.00 23.83 ?  99  ASN   B C    1 
ATOM   6099 O O    . ASN   B 1 99  ? 40.342 -28.570 11.435  1.00 24.40 ?  99  ASN   B O    1 
ATOM   6100 C CB   . ASN   B 1 99  ? 42.280 -27.083 9.909   1.00 21.41 ?  99  ASN   B CB   1 
ATOM   6101 C CG   . ASN   B 1 99  ? 43.414 -28.091 9.923   1.00 22.21 ?  99  ASN   B CG   1 
ATOM   6102 O OD1  . ASN   B 1 99  ? 43.201 -29.273 10.145  1.00 22.52 ?  99  ASN   B OD1  1 
ATOM   6103 N ND2  . ASN   B 1 99  ? 44.620 -27.627 9.678   1.00 22.08 ?  99  ASN   B ND2  1 
ATOM   6104 H H    . ASN   B 1 99  ? 39.983 -26.029 9.816   1.00 23.66 ?  99  ASN   B H    1 
ATOM   6105 H HA   . ASN   B 1 99  ? 41.188 -28.041 8.446   1.00 25.38 ?  99  ASN   B HA   1 
ATOM   6106 H HB2  . ASN   B 1 99  ? 42.556 -26.321 9.391   1.00 25.71 ?  99  ASN   B HB2  1 
ATOM   6107 H HB3  . ASN   B 1 99  ? 42.100 -26.824 10.828  1.00 25.71 ?  99  ASN   B HB3  1 
ATOM   6108 H HD21 . ASN   B 1 99  ? 45.290 -28.164 9.665   1.00 26.51 ?  99  ASN   B HD21 1 
ATOM   6109 H HD22 . ASN   B 1 99  ? 44.726 -26.792 9.529   1.00 26.51 ?  99  ASN   B HD22 1 
ATOM   6110 N N    A VAL   B 1 100 ? 39.902 -29.804 9.597   0.42 26.85 ?  100 VAL   B N    1 
ATOM   6111 N N    B VAL   B 1 100 ? 39.917 -29.808 9.591   0.58 26.37 ?  100 VAL   B N    1 
ATOM   6112 C CA   A VAL   B 1 100 ? 39.263 -30.867 10.370  0.42 29.82 ?  100 VAL   B CA   1 
ATOM   6113 C CA   B VAL   B 1 100 ? 39.293 -30.893 10.345  0.58 28.87 ?  100 VAL   B CA   1 
ATOM   6114 C C    A VAL   B 1 100 ? 40.259 -31.517 11.319  0.42 31.01 ?  100 VAL   B C    1 
ATOM   6115 C C    B VAL   B 1 100 ? 40.310 -31.589 11.245  0.58 28.94 ?  100 VAL   B C    1 
ATOM   6116 O O    A VAL   B 1 100 ? 39.889 -31.957 12.414  0.42 31.68 ?  100 VAL   B O    1 
ATOM   6117 O O    B VAL   B 1 100 ? 39.951 -32.117 12.306  0.58 29.50 ?  100 VAL   B O    1 
ATOM   6118 C CB   A VAL   B 1 100 ? 38.594 -31.890 9.429   0.42 31.41 ?  100 VAL   B CB   1 
ATOM   6119 C CB   B VAL   B 1 100 ? 38.595 -31.870 9.379   0.58 30.98 ?  100 VAL   B CB   1 
ATOM   6120 C CG1  A VAL   B 1 100 ? 38.092 -33.095 10.214  0.42 32.03 ?  100 VAL   B CG1  1 
ATOM   6121 C CG1  B VAL   B 1 100 ? 38.052 -33.074 10.132  0.58 31.94 ?  100 VAL   B CG1  1 
ATOM   6122 C CG2  A VAL   B 1 100 ? 37.448 -31.235 8.673   0.42 31.91 ?  100 VAL   B CG2  1 
ATOM   6123 C CG2  B VAL   B 1 100 ? 37.474 -31.157 8.632   0.58 31.50 ?  100 VAL   B CG2  1 
ATOM   6124 H H    A VAL   B 1 100 ? 39.934 -29.946 8.747   0.42 32.24 ?  100 VAL   B H    1 
ATOM   6125 H H    B VAL   B 1 100 ? 39.942 -29.933 8.736   0.58 31.66 ?  100 VAL   B H    1 
ATOM   6126 H HA   A VAL   B 1 100 ? 38.556 -30.471 10.905  0.42 35.80 ?  100 VAL   B HA   1 
ATOM   6127 H HA   B VAL   B 1 100 ? 38.602 -30.512 10.909  0.58 34.67 ?  100 VAL   B HA   1 
ATOM   6128 H HB   A VAL   B 1 100 ? 39.246 -32.202 8.782   0.42 37.71 ?  100 VAL   B HB   1 
ATOM   6129 H HB   B VAL   B 1 100 ? 39.236 -32.188 8.724   0.58 37.19 ?  100 VAL   B HB   1 
ATOM   6130 H HG11 A VAL   B 1 100 ? 37.491 -33.608 9.650   0.42 38.45 ?  100 VAL   B HG11 1 
ATOM   6131 H HG11 B VAL   B 1 100 ? 37.450 -33.564 9.549   0.58 38.34 ?  100 VAL   B HG11 1 
ATOM   6132 H HG12 A VAL   B 1 100 ? 38.847 -33.644 10.475  0.42 38.45 ?  100 VAL   B HG12 1 
ATOM   6133 H HG12 B VAL   B 1 100 ? 38.791 -33.642 10.396  0.58 38.34 ?  100 VAL   B HG12 1 
ATOM   6134 H HG13 A VAL   B 1 100 ? 37.618 -32.783 11.001  0.42 38.45 ?  100 VAL   B HG13 1 
ATOM   6135 H HG13 B VAL   B 1 100 ? 37.573 -32.764 10.915  0.58 38.34 ?  100 VAL   B HG13 1 
ATOM   6136 H HG21 A VAL   B 1 100 ? 37.029 -31.896 8.100   0.42 38.31 ?  100 VAL   B HG21 1 
ATOM   6137 H HG21 B VAL   B 1 100 ? 37.015 -31.796 8.065   0.58 37.82 ?  100 VAL   B HG21 1 
ATOM   6138 H HG22 A VAL   B 1 100 ? 36.801 -30.895 9.312   0.42 38.31 ?  100 VAL   B HG22 1 
ATOM   6139 H HG22 B VAL   B 1 100 ? 36.855 -30.782 9.278   0.58 37.82 ?  100 VAL   B HG22 1 
ATOM   6140 H HG23 A VAL   B 1 100 ? 37.798 -30.507 8.137   0.42 38.31 ?  100 VAL   B HG23 1 
ATOM   6141 H HG23 B VAL   B 1 100 ? 37.856 -30.449 8.090   0.58 37.82 ?  100 VAL   B HG23 1 
ATOM   6142 N N    A ASN   B 1 101 ? 41.532 -31.590 10.925  0.42 31.79 ?  101 ASN   B N    1 
ATOM   6143 N N    B ASN   B 1 101 ? 41.582 -31.624 10.840  0.58 29.19 ?  101 ASN   B N    1 
ATOM   6144 C CA   A ASN   B 1 101 ? 42.559 -32.115 11.819  0.42 32.81 ?  101 ASN   B CA   1 
ATOM   6145 C CA   B ASN   B 1 101 ? 42.625 -32.156 11.712  0.58 30.18 ?  101 ASN   B CA   1 
ATOM   6146 C C    A ASN   B 1 101 ? 42.750 -31.248 13.056  0.42 34.83 ?  101 ASN   B C    1 
ATOM   6147 C C    B ASN   B 1 101 ? 42.821 -31.314 12.965  0.58 32.61 ?  101 ASN   B C    1 
ATOM   6148 O O    A ASN   B 1 101 ? 43.379 -31.702 14.019  0.42 35.20 ?  101 ASN   B O    1 
ATOM   6149 O O    B ASN   B 1 101 ? 43.501 -31.765 13.896  0.58 33.59 ?  101 ASN   B O    1 
ATOM   6150 C CB   A ASN   B 1 101 ? 43.884 -32.279 11.070  0.42 32.20 ?  101 ASN   B CB   1 
ATOM   6151 C CB   B ASN   B 1 101 ? 43.943 -32.292 10.948  0.58 29.80 ?  101 ASN   B CB   1 
ATOM   6152 C CG   A ASN   B 1 101 ? 43.849 -33.418 10.066  0.42 31.57 ?  101 ASN   B CG   1 
ATOM   6153 C CG   B ASN   B 1 101 ? 43.938 -33.461 9.979   0.58 28.87 ?  101 ASN   B CG   1 
ATOM   6154 O OD1  A ASN   B 1 101 ? 43.166 -34.420 10.273  0.42 31.82 ?  101 ASN   B OD1  1 
ATOM   6155 O OD1  B ASN   B 1 101 ? 43.246 -34.455 10.193  0.58 29.57 ?  101 ASN   B OD1  1 
ATOM   6156 N ND2  A ASN   B 1 101 ? 44.585 -33.267 8.972   0.42 30.94 ?  101 ASN   B ND2  1 
ATOM   6157 N ND2  B ASN   B 1 101 ? 44.710 -33.346 8.906   0.58 28.02 ?  101 ASN   B ND2  1 
ATOM   6158 H H    A ASN   B 1 101 ? 41.818 -31.348 10.151  0.42 38.17 ?  101 ASN   B H    1 
ATOM   6159 H H    B ASN   B 1 101 ? 41.853 -31.364 10.065  0.58 35.05 ?  101 ASN   B H    1 
ATOM   6160 H HA   A ASN   B 1 101 ? 42.283 -32.993 12.117  0.42 39.39 ?  101 ASN   B HA   1 
ATOM   6161 H HA   B ASN   B 1 101 ? 42.358 -33.038 11.996  0.58 36.24 ?  101 ASN   B HA   1 
ATOM   6162 H HB2  A ASN   B 1 101 ? 44.084 -31.462 10.589  0.42 38.66 ?  101 ASN   B HB2  1 
ATOM   6163 H HB2  B ASN   B 1 101 ? 44.106 -31.484 10.438  0.58 35.77 ?  101 ASN   B HB2  1 
ATOM   6164 H HB3  A ASN   B 1 101 ? 44.587 -32.467 11.711  0.42 38.66 ?  101 ASN   B HB3  1 
ATOM   6165 H HB3  B ASN   B 1 101 ? 44.660 -32.433 11.584  0.58 35.77 ?  101 ASN   B HB3  1 
ATOM   6166 H HD21 A ASN   B 1 101 ? 44.595 -33.885 8.374   0.42 37.14 ?  101 ASN   B HD21 1 
ATOM   6167 H HD21 B ASN   B 1 101 ? 44.742 -33.984 8.330   0.58 33.64 ?  101 ASN   B HD21 1 
ATOM   6168 H HD22 A ASN   B 1 101 ? 45.050 -32.553 8.861   0.42 37.14 ?  101 ASN   B HD22 1 
ATOM   6169 H HD22 B ASN   B 1 101 ? 45.180 -32.636 8.789   0.58 33.64 ?  101 ASN   B HD22 1 
ATOM   6170 N N    A LYS   B 1 102 ? 42.234 -30.019 13.049  0.42 36.73 ?  102 LYS   B N    1 
ATOM   6171 N N    B LYS   B 1 102 ? 42.249 -30.108 13.008  0.58 35.42 ?  102 LYS   B N    1 
ATOM   6172 C CA   A LYS   B 1 102 ? 42.177 -29.172 14.232  0.42 38.45 ?  102 LYS   B CA   1 
ATOM   6173 C CA   B LYS   B 1 102 ? 42.186 -29.299 14.218  0.58 37.89 ?  102 LYS   B CA   1 
ATOM   6174 C C    A LYS   B 1 102 ? 40.794 -29.161 14.870  0.42 38.31 ?  102 LYS   B C    1 
ATOM   6175 C C    B LYS   B 1 102 ? 40.780 -29.260 14.806  0.58 37.70 ?  102 LYS   B C    1 
ATOM   6176 O O    A LYS   B 1 102 ? 40.551 -28.369 15.786  0.42 38.25 ?  102 LYS   B O    1 
ATOM   6177 O O    B LYS   B 1 102 ? 40.510 -28.442 15.691  0.58 37.52 ?  102 LYS   B O    1 
ATOM   6178 C CB   A LYS   B 1 102 ? 42.584 -27.738 13.884  0.42 40.24 ?  102 LYS   B CB   1 
ATOM   6179 C CB   B LYS   B 1 102 ? 42.672 -27.876 13.939  0.58 40.53 ?  102 LYS   B CB   1 
ATOM   6180 C CG   A LYS   B 1 102 ? 44.042 -27.555 13.505  0.42 41.77 ?  102 LYS   B CG   1 
ATOM   6181 C CG   B LYS   B 1 102 ? 44.144 -27.768 13.574  0.58 42.75 ?  102 LYS   B CG   1 
ATOM   6182 C CD   A LYS   B 1 102 ? 44.306 -26.104 13.132  0.42 43.20 ?  102 LYS   B CD   1 
ATOM   6183 C CD   B LYS   B 1 102 ? 44.488 -26.352 13.139  0.58 44.85 ?  102 LYS   B CD   1 
ATOM   6184 C CE   A LYS   B 1 102 ? 45.766 -25.851 12.803  0.42 44.07 ?  102 LYS   B CE   1 
ATOM   6185 C CE   B LYS   B 1 102 ? 45.983 -26.165 12.939  0.58 46.29 ?  102 LYS   B CE   1 
ATOM   6186 N NZ   A LYS   B 1 102 ? 45.989 -24.432 12.397  0.42 44.65 ?  102 LYS   B NZ   1 
ATOM   6187 N NZ   B LYS   B 1 102 ? 46.305 -24.777 12.498  0.58 47.27 ?  102 LYS   B NZ   1 
ATOM   6188 H H    A LYS   B 1 102 ? 41.905 -29.647 12.349  0.42 44.09 ?  102 LYS   B H    1 
ATOM   6189 H H    B LYS   B 1 102 ? 41.877 -29.729 12.329  0.58 42.52 ?  102 LYS   B H    1 
ATOM   6190 H HA   A LYS   B 1 102 ? 42.807 -29.506 14.888  0.42 46.16 ?  102 LYS   B HA   1 
ATOM   6191 H HA   B LYS   B 1 102 ? 42.780 -29.686 14.879  0.58 45.49 ?  102 LYS   B HA   1 
ATOM   6192 H HB2  A LYS   B 1 102 ? 42.047 -27.438 13.135  0.42 48.30 ?  102 LYS   B HB2  1 
ATOM   6193 H HB2  B LYS   B 1 102 ? 42.159 -27.511 13.202  0.58 48.65 ?  102 LYS   B HB2  1 
ATOM   6194 H HB3  A LYS   B 1 102 ? 42.411 -27.173 14.654  0.42 48.30 ?  102 LYS   B HB3  1 
ATOM   6195 H HB3  B LYS   B 1 102 ? 42.527 -27.338 14.735  0.58 48.65 ?  102 LYS   B HB3  1 
ATOM   6196 H HG2  A LYS   B 1 102 ? 44.607 -27.788 14.260  0.42 50.15 ?  102 LYS   B HG2  1 
ATOM   6197 H HG2  B LYS   B 1 102 ? 44.687 -27.990 14.347  0.58 51.32 ?  102 LYS   B HG2  1 
ATOM   6198 H HG3  A LYS   B 1 102 ? 44.252 -28.114 12.740  0.42 50.15 ?  102 LYS   B HG3  1 
ATOM   6199 H HG3  B LYS   B 1 102 ? 44.340 -28.371 12.839  0.58 51.32 ?  102 LYS   B HG3  1 
ATOM   6200 H HD2  A LYS   B 1 102 ? 43.776 -25.876 12.352  0.42 51.86 ?  102 LYS   B HD2  1 
ATOM   6201 H HD2  B LYS   B 1 102 ? 44.044 -26.160 12.297  0.58 53.84 ?  102 LYS   B HD2  1 
ATOM   6202 H HD3  A LYS   B 1 102 ? 44.061 -25.535 13.879  0.42 51.86 ?  102 LYS   B HD3  1 
ATOM   6203 H HD3  B LYS   B 1 102 ? 44.192 -25.728 13.820  0.58 53.84 ?  102 LYS   B HD3  1 
ATOM   6204 H HE2  A LYS   B 1 102 ? 46.309 -26.032 13.587  0.42 52.90 ?  102 LYS   B HE2  1 
ATOM   6205 H HE2  B LYS   B 1 102 ? 46.441 -26.332 13.778  0.58 55.56 ?  102 LYS   B HE2  1 
ATOM   6206 H HE3  A LYS   B 1 102 ? 46.035 -26.424 12.068  0.42 52.90 ?  102 LYS   B HE3  1 
ATOM   6207 H HE3  B LYS   B 1 102 ? 46.295 -26.781 12.257  0.58 55.56 ?  102 LYS   B HE3  1 
ATOM   6208 H HZ1  A LYS   B 1 102 ? 46.848 -24.300 12.208  0.42 53.59 ?  102 LYS   B HZ1  1 
ATOM   6209 H HZ1  B LYS   B 1 102 ? 47.183 -24.688 12.387  0.58 56.74 ?  102 LYS   B HZ1  1 
ATOM   6210 H HZ2  A LYS   B 1 102 ? 45.501 -24.243 11.677  0.42 53.59 ?  102 LYS   B HZ2  1 
ATOM   6211 H HZ2  B LYS   B 1 102 ? 45.896 -24.600 11.727  0.58 56.74 ?  102 LYS   B HZ2  1 
ATOM   6212 H HZ3  A LYS   B 1 102 ? 45.750 -23.886 13.058  0.42 53.59 ?  102 LYS   B HZ3  1 
ATOM   6213 H HZ3  B LYS   B 1 102 ? 46.029 -24.192 13.110  0.58 56.74 ?  102 LYS   B HZ3  1 
ATOM   6214 N N    A GLY   B 1 103 ? 39.879 -30.006 14.400  0.42 38.44 ?  103 GLY   B N    1 
ATOM   6215 N N    B GLY   B 1 103 ? 39.874 -30.107 14.321  0.58 38.03 ?  103 GLY   B N    1 
ATOM   6216 C CA   A GLY   B 1 103 ? 38.545 -30.065 14.960  0.42 38.72 ?  103 GLY   B CA   1 
ATOM   6217 C CA   B GLY   B 1 103 ? 38.537 -30.205 14.872  0.58 38.57 ?  103 GLY   B CA   1 
ATOM   6218 C C    A GLY   B 1 103 ? 37.602 -28.982 14.491  0.42 38.73 ?  103 GLY   B C    1 
ATOM   6219 C C    B GLY   B 1 103 ? 37.562 -29.151 14.400  0.58 38.48 ?  103 GLY   B C    1 
ATOM   6220 O O    A GLY   B 1 103 ? 36.482 -28.894 15.006  0.42 38.99 ?  103 GLY   B O    1 
ATOM   6221 O O    B GLY   B 1 103 ? 36.440 -29.096 14.918  0.58 38.71 ?  103 GLY   B O    1 
ATOM   6222 H H    A GLY   B 1 103 ? 40.011 -30.555 13.752  0.42 46.14 ?  103 GLY   B H    1 
ATOM   6223 H H    B GLY   B 1 103 ? 40.014 -30.634 13.659  0.58 45.65 ?  103 GLY   B H    1 
ATOM   6224 H HA2  A GLY   B 1 103 ? 38.150 -30.922 14.740  0.42 46.48 ?  103 GLY   B HA2  1 
ATOM   6225 H HA2  B GLY   B 1 103 ? 38.169 -31.073 14.646  0.58 46.30 ?  103 GLY   B HA2  1 
ATOM   6226 H HA3  A GLY   B 1 103 ? 38.607 -30.003 15.926  0.42 46.48 ?  103 GLY   B HA3  1 
ATOM   6227 H HA3  B GLY   B 1 103 ? 38.591 -30.146 15.839  0.58 46.30 ?  103 GLY   B HA3  1 
ATOM   6228 N N    A GLU   B 1 104 ? 38.014 -28.156 13.533  0.42 38.16 ?  104 GLU   B N    1 
ATOM   6229 N N    B GLU   B 1 104 ? 37.942 -28.322 13.432  0.58 37.60 ?  104 GLU   B N    1 
ATOM   6230 C CA   A GLU   B 1 104 ? 37.170 -27.068 13.065  0.42 37.49 ?  104 GLU   B CA   1 
ATOM   6231 C CA   B GLU   B 1 104 ? 37.091 -27.221 13.009  0.58 36.56 ?  104 GLU   B CA   1 
ATOM   6232 C C    A GLU   B 1 104 ? 35.985 -27.608 12.265  0.42 37.55 ?  104 GLU   B C    1 
ATOM   6233 C C    B GLU   B 1 104 ? 35.903 -27.729 12.193  0.58 36.45 ?  104 GLU   B C    1 
ATOM   6234 O O    A GLU   B 1 104 ? 36.021 -28.707 11.703  0.42 37.70 ?  104 GLU   B O    1 
ATOM   6235 O O    B GLU   B 1 104 ? 35.941 -28.799 11.578  0.58 36.69 ?  104 GLU   B O    1 
ATOM   6236 C CB   A GLU   B 1 104 ? 37.996 -26.079 12.240  0.42 36.91 ?  104 GLU   B CB   1 
ATOM   6237 C CB   B GLU   B 1 104 ? 37.909 -26.197 12.221  0.58 35.89 ?  104 GLU   B CB   1 
ATOM   6238 C CG   A GLU   B 1 104 ? 39.115 -25.428 13.048  0.42 36.32 ?  104 GLU   B CG   1 
ATOM   6239 C CG   B GLU   B 1 104 ? 39.018 -25.578 13.063  0.58 35.04 ?  104 GLU   B CG   1 
ATOM   6240 C CD   A GLU   B 1 104 ? 40.017 -24.533 12.222  0.42 35.83 ?  104 GLU   B CD   1 
ATOM   6241 C CD   B GLU   B 1 104 ? 39.943 -24.664 12.288  0.58 34.21 ?  104 GLU   B CD   1 
ATOM   6242 O OE1  A GLU   B 1 104 ? 39.986 -24.626 10.977  0.42 35.10 ?  104 GLU   B OE1  1 
ATOM   6243 O OE1  B GLU   B 1 104 ? 39.921 -24.687 11.040  0.58 33.43 ?  104 GLU   B OE1  1 
ATOM   6244 O OE2  A GLU   B 1 104 ? 40.766 -23.737 12.826  0.42 35.67 -1 104 GLU   B OE2  1 
ATOM   6245 O OE2  B GLU   B 1 104 ? 40.703 -23.918 12.942  0.58 33.55 -1 104 GLU   B OE2  1 
ATOM   6246 H H    A GLU   B 1 104 ? 38.779 -28.201 13.145  0.42 45.80 ?  104 GLU   B H    1 
ATOM   6247 H H    B GLU   B 1 104 ? 38.689 -28.374 13.011  0.58 45.13 ?  104 GLU   B H    1 
ATOM   6248 H HA   A GLU   B 1 104 ? 36.818 -26.591 13.831  0.42 45.00 ?  104 GLU   B HA   1 
ATOM   6249 H HA   B GLU   B 1 104 ? 36.743 -26.778 13.796  0.58 43.89 ?  104 GLU   B HA   1 
ATOM   6250 H HB2  A GLU   B 1 104 ? 38.400 -26.546 11.494  0.42 44.31 ?  104 GLU   B HB2  1 
ATOM   6251 H HB2  B GLU   B 1 104 ? 38.315 -26.635 11.457  0.58 43.09 ?  104 GLU   B HB2  1 
ATOM   6252 H HB3  A GLU   B 1 104 ? 37.414 -25.374 11.915  0.42 44.31 ?  104 GLU   B HB3  1 
ATOM   6253 H HB3  B GLU   B 1 104 ? 37.320 -25.485 11.923  0.58 43.09 ?  104 GLU   B HB3  1 
ATOM   6254 H HG2  A GLU   B 1 104 ? 38.723 -24.891 13.755  0.42 43.60 ?  104 GLU   B HG2  1 
ATOM   6255 H HG2  B GLU   B 1 104 ? 38.615 -25.057 13.775  0.58 42.06 ?  104 GLU   B HG2  1 
ATOM   6256 H HG3  A GLU   B 1 104 ? 39.674 -26.120 13.430  0.42 43.60 ?  104 GLU   B HG3  1 
ATOM   6257 H HG3  B GLU   B 1 104 ? 39.559 -26.288 13.439  0.58 42.06 ?  104 GLU   B HG3  1 
ATOM   6258 N N    A ASP   B 1 105 ? 34.919 -26.809 12.223  0.42 37.19 ?  105 ASP   B N    1 
ATOM   6259 N N    B ASP   B 1 105 ? 34.833 -26.934 12.197  0.58 35.42 ?  105 ASP   B N    1 
ATOM   6260 C CA   A ASP   B 1 105 ? 33.651 -27.251 11.655  0.42 37.48 ?  105 ASP   B CA   1 
ATOM   6261 C CA   B ASP   B 1 105 ? 33.564 -27.360 11.618  0.58 35.77 ?  105 ASP   B CA   1 
ATOM   6262 C C    A ASP   B 1 105 ? 33.737 -27.288 10.134  0.42 35.84 ?  105 ASP   B C    1 
ATOM   6263 C C    B ASP   B 1 105 ? 33.657 -27.370 10.097  0.58 33.88 ?  105 ASP   B C    1 
ATOM   6264 O O    A ASP   B 1 105 ? 33.986 -26.263 9.491   0.42 35.24 ?  105 ASP   B O    1 
ATOM   6265 O O    B ASP   B 1 105 ? 33.848 -26.322 9.470   0.58 33.05 ?  105 ASP   B O    1 
ATOM   6266 C CB   A ASP   B 1 105 ? 32.533 -26.310 12.102  0.42 39.43 ?  105 ASP   B CB   1 
ATOM   6267 C CB   B ASP   B 1 105 ? 32.447 -26.422 12.074  0.58 38.32 ?  105 ASP   B CB   1 
ATOM   6268 C CG   A ASP   B 1 105 ? 31.162 -26.780 11.660  0.42 41.36 ?  105 ASP   B CG   1 
ATOM   6269 C CG   B ASP   B 1 105 ? 31.066 -26.946 11.724  0.58 40.71 ?  105 ASP   B CG   1 
ATOM   6270 O OD1  A ASP   B 1 105 ? 31.061 -27.897 11.110  0.42 41.83 ?  105 ASP   B OD1  1 
ATOM   6271 O OD1  B ASP   B 1 105 ? 30.974 -27.946 10.982  0.58 41.25 ?  105 ASP   B OD1  1 
ATOM   6272 O OD2  A ASP   B 1 105 ? 30.183 -26.030 11.861  0.42 42.34 -1 105 ASP   B OD2  1 
ATOM   6273 O OD2  B ASP   B 1 105 ? 30.068 -26.362 12.201  0.58 41.51 -1 105 ASP   B OD2  1 
ATOM   6274 H H    A ASP   B 1 105 ? 34.907 -26.003 12.514  0.42 44.64 ?  105 ASP   B H    1 
ATOM   6275 H H    B ASP   B 1 105 ? 34.816 -26.142 12.528  0.58 42.53 ?  105 ASP   B H    1 
ATOM   6276 H HA   A ASP   B 1 105 ? 33.443 -28.143 11.974  0.42 45.00 ?  105 ASP   B HA   1 
ATOM   6277 H HA   B ASP   B 1 105 ? 33.351 -28.257 11.920  0.58 42.94 ?  105 ASP   B HA   1 
ATOM   6278 H HB2  A ASP   B 1 105 ? 32.537 -26.248 13.072  0.42 47.33 ?  105 ASP   B HB2  1 
ATOM   6279 H HB2  B ASP   B 1 105 ? 32.493 -26.315 13.037  0.58 46.00 ?  105 ASP   B HB2  1 
ATOM   6280 H HB3  A ASP   B 1 105 ? 32.678 -25.433 11.715  0.42 47.33 ?  105 ASP   B HB3  1 
ATOM   6281 H HB3  B ASP   B 1 105 ? 32.557 -25.561 11.640  0.58 46.00 ?  105 ASP   B HB3  1 
ATOM   6282 N N    A ILE   B 1 106 ? 33.515 -28.475 9.561   0.42 35.02 ?  106 ILE   B N    1 
ATOM   6283 N N    B ILE   B 1 106 ? 33.494 -28.557 9.507   0.58 33.50 ?  106 ILE   B N    1 
ATOM   6284 C CA   A ILE   B 1 106 ? 33.530 -28.650 8.113   0.42 34.30 ?  106 ILE   B CA   1 
ATOM   6285 C CA   B ILE   B 1 106 ? 33.504 -28.698 8.058   0.58 33.32 ?  106 ILE   B CA   1 
ATOM   6286 C C    A ILE   B 1 106 ? 32.450 -27.820 7.429   0.42 33.11 ?  106 ILE   B C    1 
ATOM   6287 C C    B ILE   B 1 106 ? 32.417 -27.856 7.401   0.58 32.17 ?  106 ILE   B C    1 
ATOM   6288 O O    A ILE   B 1 106 ? 32.565 -27.513 6.238   0.42 32.65 ?  106 ILE   B O    1 
ATOM   6289 O O    B ILE   B 1 106 ? 32.502 -27.560 6.204   0.58 31.04 ?  106 ILE   B O    1 
ATOM   6290 C CB   A ILE   B 1 106 ? 33.406 -30.156 7.779   0.42 34.62 ?  106 ILE   B CB   1 
ATOM   6291 C CB   B ILE   B 1 106 ? 33.388 -30.195 7.685   0.58 33.98 ?  106 ILE   B CB   1 
ATOM   6292 C CG1  A ILE   B 1 106 ? 33.640 -30.414 6.288   0.42 34.54 ?  106 ILE   B CG1  1 
ATOM   6293 C CG1  B ILE   B 1 106 ? 33.721 -30.421 6.209   0.58 34.15 ?  106 ILE   B CG1  1 
ATOM   6294 C CG2  A ILE   B 1 106 ? 32.044 -30.690 8.205   0.42 35.11 ?  106 ILE   B CG2  1 
ATOM   6295 C CG2  B ILE   B 1 106 ? 31.990 -30.714 7.994   0.58 34.73 ?  106 ILE   B CG2  1 
ATOM   6296 C CD1  A ILE   B 1 106 ? 35.006 -29.990 5.804   0.42 34.33 ?  106 ILE   B CD1  1 
ATOM   6297 C CD1  B ILE   B 1 106 ? 35.098 -29.939 5.821   0.58 34.05 ?  106 ILE   B CD1  1 
ATOM   6298 H H    A ILE   B 1 106 ? 33.358 -29.196 9.997   0.42 42.04 ?  106 ILE   B H    1 
ATOM   6299 H H    B ILE   B 1 106 ? 33.377 -29.296 9.930   0.58 40.21 ?  106 ILE   B H    1 
ATOM   6300 H HA   A ILE   B 1 106 ? 34.384 -28.343 7.780   0.42 41.17 ?  106 ILE   B HA   1 
ATOM   6301 H HA   B ILE   B 1 106 ? 34.353 -28.374 7.730   0.58 40.01 ?  106 ILE   B HA   1 
ATOM   6302 H HB   A ILE   B 1 106 ? 34.086 -30.633 8.278   0.42 41.56 ?  106 ILE   B HB   1 
ATOM   6303 H HB   B ILE   B 1 106 ? 34.023 -30.697 8.221   0.58 40.80 ?  106 ILE   B HB   1 
ATOM   6304 H HG12 A ILE   B 1 106 ? 33.552 -31.367 6.120   0.42 41.46 ?  106 ILE   B HG12 1 
ATOM   6305 H HG12 B ILE   B 1 106 ? 33.679 -31.373 6.020   0.58 40.99 ?  106 ILE   B HG12 1 
ATOM   6306 H HG13 A ILE   B 1 106 ? 32.978 -29.930 5.774   0.42 41.46 ?  106 ILE   B HG13 1 
ATOM   6307 H HG13 B ILE   B 1 106 ? 33.075 -29.950 5.663   0.58 40.99 ?  106 ILE   B HG13 1 
ATOM   6308 H HG21 A ILE   B 1 106 ? 32.037 -31.654 8.095   0.42 42.15 ?  106 ILE   B HG21 1 
ATOM   6309 H HG21 B ILE   B 1 106 ? 31.999 -31.683 7.958   0.58 41.69 ?  106 ILE   B HG21 1 
ATOM   6310 H HG22 A ILE   B 1 106 ? 31.893 -30.463 9.136   0.42 42.15 ?  106 ILE   B HG22 1 
ATOM   6311 H HG22 B ILE   B 1 106 ? 31.734 -30.417 8.880   0.58 41.69 ?  106 ILE   B HG22 1 
ATOM   6312 H HG23 A ILE   B 1 106 ? 31.358 -30.289 7.650   0.42 42.15 ?  106 ILE   B HG23 1 
ATOM   6313 H HG23 B ILE   B 1 106 ? 31.370 -30.365 7.335   0.58 41.69 ?  106 ILE   B HG23 1 
ATOM   6314 H HD11 A ILE   B 1 106 ? 35.164 -30.379 4.930   0.42 41.22 ?  106 ILE   B HD11 1 
ATOM   6315 H HD11 B ILE   B 1 106 ? 35.358 -30.363 4.990   0.58 40.87 ?  106 ILE   B HD11 1 
ATOM   6316 H HD12 A ILE   B 1 106 ? 35.034 -29.022 5.744   0.42 41.22 ?  106 ILE   B HD12 1 
ATOM   6317 H HD12 B ILE   B 1 106 ? 35.075 -28.975 5.707   0.58 40.87 ?  106 ILE   B HD12 1 
ATOM   6318 H HD13 A ILE   B 1 106 ? 35.676 -30.305 6.431   0.42 41.22 ?  106 ILE   B HD13 1 
ATOM   6319 H HD13 B ILE   B 1 106 ? 35.725 -30.176 6.523   0.58 40.87 ?  106 ILE   B HD13 1 
ATOM   6320 N N    . GLN   B 1 107 ? 31.398 -27.441 8.158   1.00 32.69 ?  107 GLN   B N    1 
ATOM   6321 C CA   . GLN   B 1 107 ? 30.330 -26.635 7.578   1.00 31.93 ?  107 GLN   B CA   1 
ATOM   6322 C C    . GLN   B 1 107 ? 30.821 -25.271 7.097   1.00 28.43 ?  107 GLN   B C    1 
ATOM   6323 O O    . GLN   B 1 107 ? 30.176 -24.673 6.231   1.00 29.43 ?  107 GLN   B O    1 
ATOM   6324 C CB   . GLN   B 1 107 ? 29.198 -26.468 8.594   1.00 36.72 ?  107 GLN   B CB   1 
ATOM   6325 C CG   . GLN   B 1 107 ? 27.857 -26.069 7.990   1.00 41.29 ?  107 GLN   B CG   1 
ATOM   6326 C CD   . GLN   B 1 107 ? 27.715 -24.569 7.810   1.00 44.79 ?  107 GLN   B CD   1 
ATOM   6327 O OE1  . GLN   B 1 107 ? 28.444 -23.786 8.421   1.00 45.58 ?  107 GLN   B OE1  1 
ATOM   6328 N NE2  . GLN   B 1 107 ? 26.767 -24.161 6.972   1.00 45.75 ?  107 GLN   B NE2  1 
ATOM   6329 H H    A GLN   B 1 107 ? 31.282 -27.635 8.980   0.42 39.25 ?  107 GLN   B H    1 
ATOM   6330 H H    B GLN   B 1 107 ? 31.309 -27.601 8.991   0.58 39.25 ?  107 GLN   B H    1 
ATOM   6331 H HA   . GLN   B 1 107 ? 29.971 -27.104 6.807   1.00 38.33 ?  107 GLN   B HA   1 
ATOM   6332 H HB2  . GLN   B 1 107 ? 29.075 -27.310 9.051   1.00 44.08 ?  107 GLN   B HB2  1 
ATOM   6333 H HB3  . GLN   B 1 107 ? 29.453 -25.782 9.230   1.00 44.08 ?  107 GLN   B HB3  1 
ATOM   6334 H HG2  . GLN   B 1 107 ? 27.763 -26.483 7.118   1.00 49.56 ?  107 GLN   B HG2  1 
ATOM   6335 H HG3  . GLN   B 1 107 ? 27.145 -26.376 8.578   1.00 49.56 ?  107 GLN   B HG3  1 
ATOM   6336 H HE21 . GLN   B 1 107 ? 26.279 -24.737 6.559   1.00 54.92 ?  107 GLN   B HE21 1 
ATOM   6337 H HE22 . GLN   B 1 107 ? 26.643 -23.320 6.841   1.00 54.92 ?  107 GLN   B HE22 1 
ATOM   6338 N N    . LEU   B 1 108 ? 31.952 -24.774 7.615   1.00 24.95 ?  108 LEU   B N    1 
ATOM   6339 C CA   . LEU   B 1 108 ? 32.495 -23.477 7.199   1.00 21.33 ?  108 LEU   B CA   1 
ATOM   6340 C C    . LEU   B 1 108 ? 33.148 -23.517 5.827   1.00 17.91 ?  108 LEU   B C    1 
ATOM   6341 O O    . LEU   B 1 108 ? 33.587 -22.471 5.328   1.00 16.13 ?  108 LEU   B O    1 
ATOM   6342 C CB   . LEU   B 1 108 ? 33.488 -22.967 8.242   1.00 21.54 ?  108 LEU   B CB   1 
ATOM   6343 C CG   . LEU   B 1 108 ? 32.848 -22.405 9.513   1.00 23.24 ?  108 LEU   B CG   1 
ATOM   6344 C CD1  . LEU   B 1 108 ? 33.805 -22.493 10.680  1.00 24.19 ?  108 LEU   B CD1  1 
ATOM   6345 C CD2  . LEU   B 1 108 ? 32.420 -20.960 9.291   1.00 23.94 ?  108 LEU   B CD2  1 
ATOM   6346 H H    . LEU   B 1 108 ? 32.407 -25.165 8.222   1.00 29.95 ?  108 LEU   B H    1 
ATOM   6347 H HA   . LEU   B 1 108 ? 31.765 -22.840 7.160   1.00 25.62 ?  108 LEU   B HA   1 
ATOM   6348 H HB2  . LEU   B 1 108 ? 34.062 -23.700 8.509   1.00 25.87 ?  108 LEU   B HB2  1 
ATOM   6349 H HB3  . LEU   B 1 108 ? 34.017 -22.260 7.847   1.00 25.87 ?  108 LEU   B HB3  1 
ATOM   6350 H HG   . LEU   B 1 108 ? 32.056 -22.920 9.733   1.00 27.90 ?  108 LEU   B HG   1 
ATOM   6351 H HD11 . LEU   B 1 108 ? 33.370 -22.147 11.476  1.00 29.05 ?  108 LEU   B HD11 1 
ATOM   6352 H HD12 . LEU   B 1 108 ? 34.053 -23.420 10.815  1.00 29.05 ?  108 LEU   B HD12 1 
ATOM   6353 H HD13 . LEU   B 1 108 ? 34.595 -21.965 10.481  1.00 29.05 ?  108 LEU   B HD13 1 
ATOM   6354 H HD21 . LEU   B 1 108 ? 32.008 -20.622 10.103  1.00 28.75 ?  108 LEU   B HD21 1 
ATOM   6355 H HD22 . LEU   B 1 108 ? 33.203 -20.429 9.074   1.00 28.75 ?  108 LEU   B HD22 1 
ATOM   6356 H HD23 . LEU   B 1 108 ? 31.784 -20.928 8.560   1.00 28.75 ?  108 LEU   B HD23 1 
ATOM   6357 N N    . LEU   B 1 109 ? 33.194 -24.687 5.200   1.00 16.18 ?  109 LEU   B N    1 
ATOM   6358 C CA   . LEU   B 1 109 ? 33.827 -24.820 3.896   1.00 14.85 ?  109 LEU   B CA   1 
ATOM   6359 C C    . LEU   B 1 109 ? 33.059 -24.065 2.820   1.00 14.40 ?  109 LEU   B C    1 
ATOM   6360 O O    . LEU   B 1 109 ? 33.674 -23.491 1.915   1.00 14.18 ?  109 LEU   B O    1 
ATOM   6361 C CB   . LEU   B 1 109 ? 33.960 -26.303 3.548   1.00 14.90 ?  109 LEU   B CB   1 
ATOM   6362 C CG   . LEU   B 1 109 ? 34.726 -26.665 2.277   1.00 14.28 ?  109 LEU   B CG   1 
ATOM   6363 C CD1  . LEU   B 1 109 ? 36.100 -26.017 2.250   1.00 14.25 ?  109 LEU   B CD1  1 
ATOM   6364 C CD2  . LEU   B 1 109 ? 34.845 -28.192 2.149   1.00 15.85 ?  109 LEU   B CD2  1 
ATOM   6365 H H    . LEU   B 1 109 ? 32.872 -25.416 5.506   1.00 19.43 ?  109 LEU   B H    1 
ATOM   6366 H HA   . LEU   B 1 109 ? 34.720 -24.439 3.936   1.00 17.84 ?  109 LEU   B HA   1 
ATOM   6367 H HB2  . LEU   B 1 109 ? 34.409 -26.743 4.281   1.00 17.89 ?  109 LEU   B HB2  1 
ATOM   6368 H HB3  . LEU   B 1 109 ? 33.067 -26.668 3.451   1.00 17.89 ?  109 LEU   B HB3  1 
ATOM   6369 H HG   . LEU   B 1 109 ? 34.230 -26.356 1.504   1.00 17.15 ?  109 LEU   B HG   1 
ATOM   6370 H HD11 . LEU   B 1 109 ? 36.609 -26.384 1.508   1.00 17.11 ?  109 LEU   B HD11 1 
ATOM   6371 H HD12 . LEU   B 1 109 ? 35.990 -25.064 2.137   1.00 17.11 ?  109 LEU   B HD12 1 
ATOM   6372 H HD13 . LEU   B 1 109 ? 36.553 -26.208 3.085   1.00 17.11 ?  109 LEU   B HD13 1 
ATOM   6373 H HD21 . LEU   B 1 109 ? 35.402 -28.410 1.379   1.00 19.04 ?  109 LEU   B HD21 1 
ATOM   6374 H HD22 . LEU   B 1 109 ? 35.249 -28.554 2.953   1.00 19.04 ?  109 LEU   B HD22 1 
ATOM   6375 H HD23 . LEU   B 1 109 ? 33.960 -28.578 2.025   1.00 19.04 ?  109 LEU   B HD23 1 
ATOM   6376 N N    . LYS   B 1 110 ? 31.726 -24.017 2.904   1.00 14.19 ?  110 LYS   B N    1 
ATOM   6377 C CA   . LYS   B 1 110 ? 30.977 -23.255 1.910   1.00 13.79 ?  110 LYS   B CA   1 
ATOM   6378 C C    . LYS   B 1 110 ? 31.316 -21.770 1.996   1.00 13.52 ?  110 LYS   B C    1 
ATOM   6379 O O    . LYS   B 1 110 ? 31.578 -21.122 0.975   1.00 13.75 ?  110 LYS   B O    1 
ATOM   6380 C CB   . LYS   B 1 110 ? 29.470 -23.493 2.061   1.00 14.82 ?  110 LYS   B CB   1 
ATOM   6381 C CG   . LYS   B 1 110 ? 28.669 -22.913 0.896   1.00 15.23 ?  110 LYS   B CG   1 
ATOM   6382 C CD   . LYS   B 1 110 ? 27.194 -23.332 0.935   1.00 15.31 ?  110 LYS   B CD   1 
ATOM   6383 C CE   . LYS   B 1 110 ? 26.433 -22.814 -0.289  1.00 16.25 ?  110 LYS   B CE   1 
ATOM   6384 N NZ   . LYS   B 1 110 ? 26.788 -23.516 -1.554  1.00 16.47 ?  110 LYS   B NZ   1 
ATOM   6385 H H    . LYS   B 1 110 ? 31.251 -24.404 3.504   1.00 17.04 ?  110 LYS   B H    1 
ATOM   6386 H HA   . LYS   B 1 110 ? 31.229 -23.562 1.028   1.00 16.56 ?  110 LYS   B HA   1 
ATOM   6387 H HB2  . LYS   B 1 110 ? 29.297 -24.448 2.096   1.00 17.80 ?  110 LYS   B HB2  1 
ATOM   6388 H HB3  . LYS   B 1 110 ? 29.157 -23.070 2.877   1.00 17.80 ?  110 LYS   B HB3  1 
ATOM   6389 H HG2  . LYS   B 1 110 ? 28.700 -21.947 0.932   1.00 18.30 ?  110 LYS   B HG2  1 
ATOM   6390 H HG3  . LYS   B 1 110 ? 29.041 -23.231 0.061   1.00 18.30 ?  110 LYS   B HG3  1 
ATOM   6391 H HD2  . LYS   B 1 110 ? 27.130 -24.301 0.944   1.00 18.39 ?  110 LYS   B HD2  1 
ATOM   6392 H HD3  . LYS   B 1 110 ? 26.771 -22.963 1.729   1.00 18.39 ?  110 LYS   B HD3  1 
ATOM   6393 H HE2  . LYS   B 1 110 ? 25.485 -22.931 -0.148  1.00 19.51 ?  110 LYS   B HE2  1 
ATOM   6394 H HE3  . LYS   B 1 110 ? 26.639 -21.872 -0.407  1.00 19.51 ?  110 LYS   B HE3  1 
ATOM   6395 H HZ1  . LYS   B 1 110 ? 26.330 -23.174 -2.233  1.00 19.78 ?  110 LYS   B HZ1  1 
ATOM   6396 H HZ2  . LYS   B 1 110 ? 27.664 -23.416 -1.720  1.00 19.78 ?  110 LYS   B HZ2  1 
ATOM   6397 H HZ3  . LYS   B 1 110 ? 26.610 -24.382 -1.483  1.00 19.78 ?  110 LYS   B HZ3  1 
ATOM   6398 N N    . SER   B 1 111 ? 31.347 -21.220 3.216   1.00 13.65 ?  111 SER   B N    1 
ATOM   6399 C CA   . SER   B 1 111 ? 31.740 -19.822 3.381   1.00 13.56 ?  111 SER   B CA   1 
ATOM   6400 C C    . SER   B 1 111 ? 33.120 -19.570 2.790   1.00 13.05 ?  111 SER   B C    1 
ATOM   6401 O O    . SER   B 1 111 ? 33.354 -18.539 2.146   1.00 13.43 ?  111 SER   B O    1 
ATOM   6402 C CB   . SER   B 1 111 ? 31.744 -19.443 4.859   1.00 14.95 ?  111 SER   B CB   1 
ATOM   6403 O OG   . SER   B 1 111 ? 30.447 -19.477 5.410   1.00 16.24 ?  111 SER   B OG   1 
ATOM   6404 H H    . SER   B 1 111 ? 31.159 -21.633 3.950   1.00 16.39 ?  111 SER   B H    1 
ATOM   6405 H HA   . SER   B 1 111 ? 31.102 -19.258 2.920   1.00 16.29 ?  111 SER   B HA   1 
ATOM   6406 H HB2  . SER   B 1 111 ? 32.301 -20.069 5.345   1.00 17.95 ?  111 SER   B HB2  1 
ATOM   6407 H HB3  . SER   B 1 111 ? 32.102 -18.545 4.950   1.00 17.95 ?  111 SER   B HB3  1 
ATOM   6408 H HG   . SER   B 1 111 ? 30.471 -19.252 6.230   1.00 19.51 ?  111 SER   B HG   1 
ATOM   6409 N N    . ALA   B 1 112 ? 34.051 -20.500 3.004   1.00 13.09 ?  112 ALA   B N    1 
ATOM   6410 C CA   . ALA   B 1 112 ? 35.398 -20.330 2.467   1.00 12.64 ?  112 ALA   B CA   1 
ATOM   6411 C C    . ALA   B 1 112 ? 35.377 -20.243 0.942   1.00 12.53 ?  112 ALA   B C    1 
ATOM   6412 O O    . ALA   B 1 112 ? 35.997 -19.346 0.353   1.00 12.59 ?  112 ALA   B O    1 
ATOM   6413 C CB   . ALA   B 1 112 ? 36.300 -21.461 2.967   1.00 12.86 ?  112 ALA   B CB   1 
ATOM   6414 H H    . ALA   B 1 112 ? 33.930 -21.226 3.453   1.00 15.73 ?  112 ALA   B H    1 
ATOM   6415 H HA   . ALA   B 1 112 ? 35.758 -19.495 2.802   1.00 15.18 ?  112 ALA   B HA   1 
ATOM   6416 H HB1  . ALA   B 1 112 ? 37.193 -21.332 2.610   1.00 15.44 ?  112 ALA   B HB1  1 
ATOM   6417 H HB2  . ALA   B 1 112 ? 36.332 -21.429 3.941   1.00 15.44 ?  112 ALA   B HB2  1 
ATOM   6418 H HB3  . ALA   B 1 112 ? 35.941 -22.309 2.677   1.00 15.44 ?  112 ALA   B HB3  1 
ATOM   6419 N N    . TYR   B 1 113 ? 34.643 -21.151 0.279   1.00 12.41 ?  113 TYR   B N    1 
ATOM   6420 C CA   . TYR   B 1 113 ? 34.560 -21.111 -1.178  1.00 12.40 ?  113 TYR   B CA   1 
ATOM   6421 C C    . TYR   B 1 113 ? 33.857 -19.857 -1.698  1.00 11.91 ?  113 TYR   B C    1 
ATOM   6422 O O    . TYR   B 1 113 ? 34.138 -19.418 -2.822  1.00 11.84 ?  113 TYR   B O    1 
ATOM   6423 C CB   . TYR   B 1 113 ? 33.882 -22.364 -1.721  1.00 12.18 ?  113 TYR   B CB   1 
ATOM   6424 C CG   . TYR   B 1 113 ? 34.845 -23.511 -1.960  1.00 12.70 ?  113 TYR   B CG   1 
ATOM   6425 C CD1  . TYR   B 1 113 ? 35.838 -23.418 -2.928  1.00 13.19 ?  113 TYR   B CD1  1 
ATOM   6426 C CD2  . TYR   B 1 113 ? 34.752 -24.687 -1.237  1.00 13.44 ?  113 TYR   B CD2  1 
ATOM   6427 C CE1  . TYR   B 1 113 ? 36.725 -24.451 -3.156  1.00 13.30 ?  113 TYR   B CE1  1 
ATOM   6428 C CE2  . TYR   B 1 113 ? 35.636 -25.747 -1.465  1.00 13.46 ?  113 TYR   B CE2  1 
ATOM   6429 C CZ   . TYR   B 1 113 ? 36.605 -25.624 -2.431  1.00 13.46 ?  113 TYR   B CZ   1 
ATOM   6430 O OH   . TYR   B 1 113 ? 37.497 -26.639 -2.691  1.00 14.36 ?  113 TYR   B OH   1 
ATOM   6431 H H    . TYR   B 1 113 ? 34.179 -21.778 0.652   1.00 14.91 ?  113 TYR   B H    1 
ATOM   6432 H HA   . TYR   B 1 113 ? 35.463 -21.093 -1.520  1.00 14.90 ?  113 TYR   B HA   1 
ATOM   6433 H HB2  . TYR   B 1 113 ? 33.216 -22.666 -1.083  1.00 14.64 ?  113 TYR   B HB2  1 
ATOM   6434 H HB3  . TYR   B 1 113 ? 33.455 -22.147 -2.565  1.00 14.64 ?  113 TYR   B HB3  1 
ATOM   6435 H HD1  . TYR   B 1 113 ? 35.922 -22.631 -3.424  1.00 15.85 ?  113 TYR   B HD1  1 
ATOM   6436 H HD2  . TYR   B 1 113 ? 34.087 -24.781 -0.596  1.00 16.15 ?  113 TYR   B HD2  1 
ATOM   6437 H HE1  . TYR   B 1 113 ? 37.385 -24.372 -3.813  1.00 15.97 ?  113 TYR   B HE1  1 
ATOM   6438 H HE2  . TYR   B 1 113 ? 35.556 -26.541 -0.981  1.00 16.17 ?  113 TYR   B HE2  1 
ATOM   6439 H HH   . TYR   B 1 113 ? 37.327 -27.304 -2.213  1.00 17.25 ?  113 TYR   B HH   1 
ATOM   6440 N N    . GLU   B 1 114 ? 32.926 -19.280 -0.923  1.00 12.02 ?  114 GLU   B N    1 
ATOM   6441 C CA   . GLU   B 1 114 ? 32.247 -18.061 -1.371  1.00 12.08 ?  114 GLU   B CA   1 
ATOM   6442 C C    . GLU   B 1 114 ? 33.238 -16.943 -1.676  1.00 11.69 ?  114 GLU   B C    1 
ATOM   6443 O O    . GLU   B 1 114 ? 32.968 -16.089 -2.525  1.00 12.27 ?  114 GLU   B O    1 
ATOM   6444 C CB   . GLU   B 1 114 ? 31.194 -17.623 -0.349  1.00 12.25 ?  114 GLU   B CB   1 
ATOM   6445 C CG   . GLU   B 1 114 ? 29.960 -18.544 -0.416  1.00 12.34 ?  114 GLU   B CG   1 
ATOM   6446 C CD   . GLU   B 1 114 ? 28.942 -18.357 0.693   1.00 12.76 ?  114 GLU   B CD   1 
ATOM   6447 O OE1  . GLU   B 1 114 ? 29.240 -17.740 1.736   1.00 13.00 ?  114 GLU   B OE1  1 
ATOM   6448 O OE2  . GLU   B 1 114 ? 27.813 -18.893 0.526   1.00 13.85 -1 114 GLU   B OE2  1 
ATOM   6449 H H    . GLU   B 1 114 ? 32.663 -19.581 -0.158  1.00 14.44 ?  114 GLU   B H    1 
ATOM   6450 H HA   . GLU   B 1 114 ? 31.777 -18.261 -2.194  1.00 14.52 ?  114 GLU   B HA   1 
ATOM   6451 H HB2  . GLU   B 1 114 ? 31.566 -17.679 0.546   1.00 14.71 ?  114 GLU   B HB2  1 
ATOM   6452 H HB3  . GLU   B 1 114 ? 30.910 -16.719 -0.543  1.00 14.71 ?  114 GLU   B HB3  1 
ATOM   6453 H HG2  . GLU   B 1 114 ? 29.503 -18.380 -1.252  1.00 14.83 ?  114 GLU   B HG2  1 
ATOM   6454 H HG3  . GLU   B 1 114 ? 30.264 -19.464 -0.383  1.00 14.83 ?  114 GLU   B HG3  1 
ATOM   6455 N N    . ASN   B 1 115 ? 34.402 -16.938 -1.023  1.00 11.57 ?  115 ASN   B N    1 
ATOM   6456 C CA   . ASN   B 1 115 ? 35.400 -15.909 -1.319  1.00 11.45 ?  115 ASN   B CA   1 
ATOM   6457 C C    . ASN   B 1 115 ? 35.818 -15.938 -2.783  1.00 11.35 ?  115 ASN   B C    1 
ATOM   6458 O O    . ASN   B 1 115 ? 36.200 -14.901 -3.337  1.00 11.74 ?  115 ASN   B O    1 
ATOM   6459 C CB   . ASN   B 1 115 ? 36.638 -16.083 -0.423  1.00 11.88 ?  115 ASN   B CB   1 
ATOM   6460 C CG   . ASN   B 1 115 ? 36.352 -15.805 1.039   1.00 12.60 ?  115 ASN   B CG   1 
ATOM   6461 O OD1  . ASN   B 1 115 ? 36.338 -14.649 1.467   1.00 14.55 ?  115 ASN   B OD1  1 
ATOM   6462 N ND2  . ASN   B 1 115 ? 36.177 -16.862 1.829   1.00 12.89 ?  115 ASN   B ND2  1 
ATOM   6463 H H    . ASN   B 1 115 ? 34.634 -17.502 -0.411  1.00 13.91 ?  115 ASN   B H    1 
ATOM   6464 H HA   . ASN   B 1 115 ? 35.019 -15.040 -1.136  1.00 13.76 ?  115 ASN   B HA   1 
ATOM   6465 H HB2  . ASN   B 1 115 ? 36.965 -16.990 -0.497  1.00 14.27 ?  115 ASN   B HB2  1 
ATOM   6466 H HB3  . ASN   B 1 115 ? 37.327 -15.459 -0.712  1.00 14.27 ?  115 ASN   B HB3  1 
ATOM   6467 H HD21 . ASN   B 1 115 ? 36.029 -16.750 2.672   1.00 15.48 ?  115 ASN   B HD21 1 
ATOM   6468 H HD22 . ASN   B 1 115 ? 36.213 -17.654 1.502   1.00 15.48 ?  115 ASN   B HD22 1 
ATOM   6469 N N    . PHE   B 1 116 ? 35.783 -17.114 -3.418  1.00 11.13 ?  116 PHE   B N    1 
ATOM   6470 C CA   . PHE   B 1 116 ? 36.226 -17.216 -4.804  1.00 11.46 ?  116 PHE   B CA   1 
ATOM   6471 C C    . PHE   B 1 116 ? 35.333 -16.396 -5.729  1.00 10.64 ?  116 PHE   B C    1 
ATOM   6472 O O    . PHE   B 1 116 ? 35.776 -15.961 -6.799  1.00 11.65 ?  116 PHE   B O    1 
ATOM   6473 C CB   . PHE   B 1 116 ? 36.176 -18.665 -5.313  1.00 11.06 ?  116 PHE   B CB   1 
ATOM   6474 C CG   . PHE   B 1 116 ? 37.252 -19.623 -4.774  1.00 10.96 ?  116 PHE   B CG   1 
ATOM   6475 C CD1  . PHE   B 1 116 ? 37.881 -19.450 -3.557  1.00 11.27 ?  116 PHE   B CD1  1 
ATOM   6476 C CD2  . PHE   B 1 116 ? 37.559 -20.760 -5.519  1.00 11.29 ?  116 PHE   B CD2  1 
ATOM   6477 C CE1  . PHE   B 1 116 ? 38.812 -20.386 -3.108  1.00 11.87 ?  116 PHE   B CE1  1 
ATOM   6478 C CE2  . PHE   B 1 116 ? 38.488 -21.691 -5.080  1.00 11.64 ?  116 PHE   B CE2  1 
ATOM   6479 C CZ   . PHE   B 1 116 ? 39.100 -21.512 -3.875  1.00 11.65 ?  116 PHE   B CZ   1 
ATOM   6480 H H    . PHE   B 1 116 ? 35.497 -17.854 -3.075  1.00 13.37 ?  116 PHE   B H    1 
ATOM   6481 H HA   . PHE   B 1 116 ? 37.131 -16.897 -4.883  1.00 13.77 ?  116 PHE   B HA   1 
ATOM   6482 H HB2  . PHE   B 1 116 ? 35.300 -19.041 -5.081  1.00 13.29 ?  116 PHE   B HB2  1 
ATOM   6483 H HB3  . PHE   B 1 116 ? 36.256 -18.653 -6.282  1.00 13.29 ?  116 PHE   B HB3  1 
ATOM   6484 H HD1  . PHE   B 1 116 ? 37.664 -18.711 -3.031  1.00 13.54 ?  116 PHE   B HD1  1 
ATOM   6485 H HD2  . PHE   B 1 116 ? 37.125 -20.894 -6.337  1.00 13.56 ?  116 PHE   B HD2  1 
ATOM   6486 H HE1  . PHE   B 1 116 ? 39.232 -20.264 -2.289  1.00 14.27 ?  116 PHE   B HE1  1 
ATOM   6487 H HE2  . PHE   B 1 116 ? 38.677 -22.432 -5.605  1.00 13.98 ?  116 PHE   B HE2  1 
ATOM   6488 H HZ   . PHE   B 1 116 ? 39.732 -22.121 -3.583  1.00 13.99 ?  116 PHE   B HZ   1 
ATOM   6489 N N    . ASN   B 1 117 ? 34.063 -16.183 -5.351  1.00 11.58 ?  117 ASN   B N    1 
ATOM   6490 C CA   . ASN   B 1 117 ? 33.127 -15.477 -6.220  1.00 12.14 ?  117 ASN   B CA   1 
ATOM   6491 C C    . ASN   B 1 117 ? 33.450 -14.002 -6.378  1.00 12.47 ?  117 ASN   B C    1 
ATOM   6492 O O    . ASN   B 1 117 ? 32.857 -13.353 -7.243  1.00 13.54 ?  117 ASN   B O    1 
ATOM   6493 C CB   . ASN   B 1 117 ? 31.698 -15.686 -5.720  1.00 12.38 ?  117 ASN   B CB   1 
ATOM   6494 C CG   . ASN   B 1 117 ? 31.227 -17.102 -5.967  1.00 12.54 ?  117 ASN   B CG   1 
ATOM   6495 O OD1  . ASN   B 1 117 ? 31.586 -17.704 -6.986  1.00 13.52 ?  117 ASN   B OD1  1 
ATOM   6496 N ND2  . ASN   B 1 117 ? 30.494 -17.670 -5.021  1.00 12.24 ?  117 ASN   B ND2  1 
ATOM   6497 H H    . ASN   B 1 117 ? 33.729 -16.441 -4.593  1.00 13.91 ?  117 ASN   B H    1 
ATOM   6498 H HA   . ASN   B 1 117 ? 33.179 -15.879 -7.095  1.00 14.59 ?  117 ASN   B HA   1 
ATOM   6499 H HB2  . ASN   B 1 117 ? 31.659 -15.512 -4.762  1.00 14.88 ?  117 ASN   B HB2  1 
ATOM   6500 H HB3  . ASN   B 1 117 ? 31.102 -15.073 -6.187  1.00 14.88 ?  117 ASN   B HB3  1 
ATOM   6501 H HD21 . ASN   B 1 117 ? 30.203 -18.476 -5.122  1.00 14.70 ?  117 ASN   B HD21 1 
ATOM   6502 H HD22 . ASN   B 1 117 ? 30.269 -17.225 -4.315  1.00 14.70 ?  117 ASN   B HD22 1 
ATOM   6503 N N    . GLN   B 1 118 ? 34.373 -13.472 -5.591  1.00 12.06 ?  118 GLN   B N    1 
ATOM   6504 C CA   . GLN   B 1 118 ? 34.803 -12.088 -5.728  1.00 12.53 ?  118 GLN   B CA   1 
ATOM   6505 C C    . GLN   B 1 118 ? 35.881 -11.899 -6.797  1.00 12.31 ?  118 GLN   B C    1 
ATOM   6506 O O    . GLN   B 1 118 ? 36.363 -10.776 -6.979  1.00 14.12 ?  118 GLN   B O    1 
ATOM   6507 C CB   . GLN   B 1 118 ? 35.272 -11.558 -4.368  1.00 12.82 ?  118 GLN   B CB   1 
ATOM   6508 C CG   . GLN   B 1 118 ? 34.185 -11.605 -3.302  1.00 13.22 ?  118 GLN   B CG   1 
ATOM   6509 C CD   . GLN   B 1 118 ? 33.032 -10.683 -3.624  1.00 13.23 ?  118 GLN   B CD   1 
ATOM   6510 O OE1  . GLN   B 1 118 ? 33.239 -9.551  -4.057  1.00 14.12 ?  118 GLN   B OE1  1 
ATOM   6511 N NE2  . GLN   B 1 118 ? 31.811 -11.165 -3.434  1.00 13.61 ?  118 GLN   B NE2  1 
ATOM   6512 H H    . GLN   B 1 118 ? 34.783 -13.895 -4.965  1.00 14.48 ?  118 GLN   B H    1 
ATOM   6513 H HA   . GLN   B 1 118 ? 34.044 -11.557 -6.005  1.00 15.05 ?  118 GLN   B HA   1 
ATOM   6514 H HB2  . GLN   B 1 118 ? 36.018 -12.092 -4.059  1.00 15.40 ?  118 GLN   B HB2  1 
ATOM   6515 H HB3  . GLN   B 1 118 ? 35.546 -10.631 -4.467  1.00 15.40 ?  118 GLN   B HB3  1 
ATOM   6516 H HG2  . GLN   B 1 118 ? 33.842 -12.515 -3.241  1.00 15.88 ?  118 GLN   B HG2  1 
ATOM   6517 H HG3  . GLN   B 1 118 ? 34.562 -11.337 -2.452  1.00 15.88 ?  118 GLN   B HG3  1 
ATOM   6518 H HE21 . GLN   B 1 118 ? 31.706 -11.966 -3.133  1.00 16.35 ?  118 GLN   B HE21 1 
ATOM   6519 H HE22 . GLN   B 1 118 ? 31.128 -10.678 -3.607  1.00 16.35 ?  118 GLN   B HE22 1 
ATOM   6520 N N    . HIS   B 1 119 ? 36.235 -12.957 -7.533  1.00 11.74 ?  119 HIS   B N    1 
ATOM   6521 C CA   . HIS   B 1 119 ? 37.280 -12.916 -8.547  1.00 12.16 ?  119 HIS   B CA   1 
ATOM   6522 C C    . HIS   B 1 119 ? 36.793 -13.638 -9.790  1.00 11.87 ?  119 HIS   B C    1 
ATOM   6523 O O    . HIS   B 1 119 ? 36.286 -14.755 -9.693  1.00 13.16 ?  119 HIS   B O    1 
ATOM   6524 C CB   . HIS   B 1 119 ? 38.545 -13.570 -7.991  1.00 12.49 ?  119 HIS   B CB   1 
ATOM   6525 C CG   . HIS   B 1 119 ? 39.039 -12.868 -6.775  1.00 14.02 ?  119 HIS   B CG   1 
ATOM   6526 N ND1  . HIS   B 1 119 ? 39.855 -11.760 -6.845  1.00 15.21 ?  119 HIS   B ND1  1 
ATOM   6527 C CD2  . HIS   B 1 119 ? 38.743 -13.037 -5.466  1.00 15.21 ?  119 HIS   B CD2  1 
ATOM   6528 C CE1  . HIS   B 1 119 ? 40.074 -11.304 -5.627  1.00 16.56 ?  119 HIS   B CE1  1 
ATOM   6529 N NE2  . HIS   B 1 119 ? 39.405 -12.053 -4.772  1.00 16.17 ?  119 HIS   B NE2  1 
ATOM   6530 H H    . HIS   B 1 119 ? 35.855 -13.736 -7.474  1.00 14.11 ?  119 HIS   B H    1 
ATOM   6531 H HA   . HIS   B 1 119 ? 37.475 -11.992 -8.776  1.00 14.61 ?  119 HIS   B HA   1 
ATOM   6532 H HB2  . HIS   B 1 119 ? 38.350 -14.490 -7.753  1.00 15.00 ?  119 HIS   B HB2  1 
ATOM   6533 H HB3  . HIS   B 1 119 ? 39.241 -13.539 -8.665  1.00 15.00 ?  119 HIS   B HB3  1 
ATOM   6534 H HD2  . HIS   B 1 119 ? 38.208 -13.700 -5.101  1.00 18.27 ?  119 HIS   B HD2  1 
ATOM   6535 H HE1  . HIS   B 1 119 ? 40.620 -10.579 -5.411  1.00 19.89 ?  119 HIS   B HE1  1 
ATOM   6536 H HE2  . HIS   B 1 119 ? 39.419 -11.963 -3.916  1.00 19.43 ?  119 HIS   B HE2  1 
ATOM   6537 N N    . GLU   B 1 120 ? 36.968 -13.021 -10.958 1.00 12.90 ?  120 GLU   B N    1 
ATOM   6538 C CA   . GLU   B 1 120 ? 36.381 -13.598 -12.161 1.00 14.30 ?  120 GLU   B CA   1 
ATOM   6539 C C    . GLU   B 1 120 ? 37.049 -14.903 -12.574 1.00 12.76 ?  120 GLU   B C    1 
ATOM   6540 O O    . GLU   B 1 120 ? 36.378 -15.773 -13.144 1.00 13.22 ?  120 GLU   B O    1 
ATOM   6541 C CB   . GLU   B 1 120 ? 36.387 -12.587 -13.304 1.00 18.55 ?  120 GLU   B CB   1 
ATOM   6542 C CG   . GLU   B 1 120 ? 35.441 -11.426 -13.062 1.00 24.98 ?  120 GLU   B CG   1 
ATOM   6543 C CD   . GLU   B 1 120 ? 35.186 -10.589 -14.297 1.00 31.00 ?  120 GLU   B CD   1 
ATOM   6544 O OE1  . GLU   B 1 120 ? 36.141 -10.366 -15.073 1.00 33.10 ?  120 GLU   B OE1  1 
ATOM   6545 O OE2  . GLU   B 1 120 ? 34.029 -10.152 -14.488 1.00 33.44 -1 120 GLU   B OE2  1 
ATOM   6546 H H    . GLU   B 1 120 ? 37.408 -12.287 -11.078 1.00 15.50 ?  120 GLU   B H    1 
ATOM   6547 H HA   . GLU   B 1 120 ? 35.461 -13.811 -11.967 1.00 17.18 ?  120 GLU   B HA   1 
ATOM   6548 H HB2  . GLU   B 1 120 ? 37.277 -12.231 -13.414 1.00 22.27 ?  120 GLU   B HB2  1 
ATOM   6549 H HB3  . GLU   B 1 120 ? 36.104 -13.036 -14.121 1.00 22.27 ?  120 GLU   B HB3  1 
ATOM   6550 H HG2  . GLU   B 1 120 ? 34.584 -11.768 -12.761 1.00 29.99 ?  120 GLU   B HG2  1 
ATOM   6551 H HG3  . GLU   B 1 120 ? 35.821 -10.843 -12.390 1.00 29.99 ?  120 GLU   B HG3  1 
ATOM   6552 N N    . VAL   B 1 121 ? 38.347 -15.058 -12.314 1.00 12.74 ?  121 VAL   B N    1 
ATOM   6553 C CA   . VAL   B 1 121 ? 39.084 -16.272 -12.661 1.00 12.05 ?  121 VAL   B CA   1 
ATOM   6554 C C    . VAL   B 1 121 ? 40.196 -16.479 -11.641 1.00 11.95 ?  121 VAL   B C    1 
ATOM   6555 O O    . VAL   B 1 121 ? 40.887 -15.528 -11.259 1.00 12.80 ?  121 VAL   B O    1 
ATOM   6556 C CB   . VAL   B 1 121 ? 39.598 -16.237 -14.122 1.00 14.38 ?  121 VAL   B CB   1 
ATOM   6557 C CG1  . VAL   B 1 121 ? 40.462 -15.009 -14.394 1.00 15.90 ?  121 VAL   B CG1  1 
ATOM   6558 C CG2  . VAL   B 1 121 ? 40.328 -17.535 -14.480 1.00 15.60 ?  121 VAL   B CG2  1 
ATOM   6559 H H    . VAL   B 1 121 ? 38.839 -14.459 -11.941 1.00 15.31 ?  121 VAL   B H    1 
ATOM   6560 H HA   . VAL   B 1 121 ? 38.471 -17.023 -12.592 1.00 14.47 ?  121 VAL   B HA   1 
ATOM   6561 H HB   . VAL   B 1 121 ? 38.824 -16.180 -14.711 1.00 17.28 ?  121 VAL   B HB   1 
ATOM   6562 H HG11 . VAL   B 1 121 ? 40.769 -15.038 -15.313 1.00 19.09 ?  121 VAL   B HG11 1 
ATOM   6563 H HG12 . VAL   B 1 121 ? 39.929 -14.211 -14.248 1.00 19.09 ?  121 VAL   B HG12 1 
ATOM   6564 H HG13 . VAL   B 1 121 ? 41.218 -15.019 -13.789 1.00 19.09 ?  121 VAL   B HG13 1 
ATOM   6565 H HG21 . VAL   B 1 121 ? 40.539 -17.529 -15.427 1.00 18.74 ?  121 VAL   B HG21 1 
ATOM   6566 H HG22 . VAL   B 1 121 ? 41.146 -17.591 -13.961 1.00 18.74 ?  121 VAL   B HG22 1 
ATOM   6567 H HG23 . VAL   B 1 121 ? 39.755 -18.291 -14.275 1.00 18.74 ?  121 VAL   B HG23 1 
ATOM   6568 N N    . LEU   B 1 122 ? 40.370 -17.731 -11.210 1.00 11.52 ?  122 LEU   B N    1 
ATOM   6569 C CA   . LEU   B 1 122 ? 41.345 -18.086 -10.189 1.00 11.23 ?  122 LEU   B CA   1 
ATOM   6570 C C    . LEU   B 1 122 ? 41.991 -19.423 -10.507 1.00 11.09 ?  122 LEU   B C    1 
ATOM   6571 O O    . LEU   B 1 122 ? 41.325 -20.346 -10.994 1.00 12.45 ?  122 LEU   B O    1 
ATOM   6572 C CB   . LEU   B 1 122 ? 40.703 -18.290 -8.806  1.00 13.59 ?  122 LEU   B CB   1 
ATOM   6573 C CG   . LEU   B 1 122 ? 39.659 -17.285 -8.333  1.00 13.73 ?  122 LEU   B CG   1 
ATOM   6574 C CD1  . LEU   B 1 122 ? 38.273 -17.689 -8.819  1.00 13.42 ?  122 LEU   B CD1  1 
ATOM   6575 C CD2  . LEU   B 1 122 ? 39.690 -17.169 -6.825  1.00 12.89 ?  122 LEU   B CD2  1 
ATOM   6576 H H    . LEU   B 1 122 ? 39.935 -18.413 -11.512 1.00 13.84 ?  122 LEU   B H    1 
ATOM   6577 H HA   . LEU   B 1 122 ? 42.030 -17.396 -10.122 1.00 13.49 ?  122 LEU   B HA   1 
ATOM   6578 H HB2  . LEU   B 1 122 ? 40.276 -19.157 -8.803  1.00 16.32 ?  122 LEU   B HB2  1 
ATOM   6579 H HB3  . LEU   B 1 122 ? 41.411 -18.280 -8.144  1.00 16.32 ?  122 LEU   B HB3  1 
ATOM   6580 H HG   . LEU   B 1 122 ? 39.861 -16.412 -8.710  1.00 16.50 ?  122 LEU   B HG   1 
ATOM   6581 H HD11 . LEU   B 1 122 ? 37.621 -17.059 -8.478  1.00 16.12 ?  122 LEU   B HD11 1 
ATOM   6582 H HD12 . LEU   B 1 122 ? 38.261 -17.682 -9.791  1.00 16.12 ?  122 LEU   B HD12 1 
ATOM   6583 H HD13 . LEU   B 1 122 ? 38.073 -18.581 -8.496  1.00 16.12 ?  122 LEU   B HD13 1 
ATOM   6584 H HD21 . LEU   B 1 122 ? 38.991 -16.553 -6.541  1.00 15.49 ?  122 LEU   B HD21 1 
ATOM   6585 H HD22 . LEU   B 1 122 ? 39.538 -18.041 -6.437  1.00 15.49 ?  122 LEU   B HD22 1 
ATOM   6586 H HD23 . LEU   B 1 122 ? 40.556 -16.827 -6.553  1.00 15.49 ?  122 LEU   B HD23 1 
ATOM   6587 N N    . LEU   B 1 123 ? 43.274 -19.535 -10.138 1.00 10.66 ?  123 LEU   B N    1 
ATOM   6588 C CA   . LEU   B 1 123 ? 43.983 -20.806 -10.014 1.00 11.27 ?  123 LEU   B CA   1 
ATOM   6589 C C    . LEU   B 1 123 ? 43.952 -21.198 -8.541  1.00 10.78 ?  123 LEU   B C    1 
ATOM   6590 O O    . LEU   B 1 123 ? 44.308 -20.373 -7.693  1.00 10.97 ?  123 LEU   B O    1 
ATOM   6591 C CB   . LEU   B 1 123 ? 45.437 -20.619 -10.466 1.00 11.37 ?  123 LEU   B CB   1 
ATOM   6592 C CG   . LEU   B 1 123 ? 46.365 -21.816 -10.241 1.00 11.38 ?  123 LEU   B CG   1 
ATOM   6593 C CD1  . LEU   B 1 123 ? 45.930 -23.053 -11.012 1.00 12.20 ?  123 LEU   B CD1  1 
ATOM   6594 C CD2  . LEU   B 1 123 ? 47.788 -21.421 -10.610 1.00 12.65 ?  123 LEU   B CD2  1 
ATOM   6595 H H    . LEU   B 1 123 ? 43.767 -18.853 -9.929  1.00 12.81 ?  123 LEU   B H    1 
ATOM   6596 H HA   . LEU   B 1 123 ? 43.550 -21.487 -10.548 1.00 13.55 ?  123 LEU   B HA   1 
ATOM   6597 H HB2  . LEU   B 1 123 ? 45.436 -20.423 -11.417 1.00 13.66 ?  123 LEU   B HB2  1 
ATOM   6598 H HB3  . LEU   B 1 123 ? 45.811 -19.864 -9.983  1.00 13.66 ?  123 LEU   B HB3  1 
ATOM   6599 H HG   . LEU   B 1 123 ? 46.360 -22.041 -9.298  1.00 13.68 ?  123 LEU   B HG   1 
ATOM   6600 H HD11 . LEU   B 1 123 ? 46.563 -23.770 -10.842 1.00 14.66 ?  123 LEU   B HD11 1 
ATOM   6601 H HD12 . LEU   B 1 123 ? 45.044 -23.323 -10.709 1.00 14.66 ?  123 LEU   B HD12 1 
ATOM   6602 H HD13 . LEU   B 1 123 ? 45.906 -22.849 -11.957 1.00 14.66 ?  123 LEU   B HD13 1 
ATOM   6603 H HD21 . LEU   B 1 123 ? 48.371 -22.179 -10.471 1.00 15.20 ?  123 LEU   B HD21 1 
ATOM   6604 H HD22 . LEU   B 1 123 ? 47.806 -21.153 -11.545 1.00 15.20 ?  123 LEU   B HD22 1 
ATOM   6605 H HD23 . LEU   B 1 123 ? 48.062 -20.678 -10.050 1.00 15.20 ?  123 LEU   B HD23 1 
ATOM   6606 N N    . ALA   B 1 124 ? 43.507 -22.420 -8.224  1.00 10.73 ?  124 ALA   B N    1 
ATOM   6607 C CA   . ALA   B 1 124 ? 43.256 -22.734 -6.823  1.00 10.65 ?  124 ALA   B CA   1 
ATOM   6608 C C    . ALA   B 1 124 ? 43.530 -24.193 -6.499  1.00 10.52 ?  124 ALA   B C    1 
ATOM   6609 O O    . ALA   B 1 124 ? 43.385 -25.067 -7.363  1.00 11.01 ?  124 ALA   B O    1 
ATOM   6610 C CB   . ALA   B 1 124 ? 41.811 -22.422 -6.442  1.00 11.14 ?  124 ALA   B CB   1 
ATOM   6611 H H    . ALA   B 1 124 ? 43.330 -23.054 -8.795  1.00 12.90 ?  124 ALA   B H    1 
ATOM   6612 H HA   . ALA   B 1 124 ? 43.846 -22.190 -6.292  1.00 12.80 ?  124 ALA   B HA   1 
ATOM   6613 H HB1  . ALA   B 1 124 ? 41.678 -22.643 -5.512  1.00 13.38 ?  124 ALA   B HB1  1 
ATOM   6614 H HB2  . ALA   B 1 124 ? 41.653 -21.474 -6.587  1.00 13.38 ?  124 ALA   B HB2  1 
ATOM   6615 H HB3  . ALA   B 1 124 ? 41.216 -22.944 -7.002  1.00 13.38 ?  124 ALA   B HB3  1 
ATOM   6616 N N    . PRO   B 1 125 ? 43.831 -24.491 -5.235  1.00 11.01 ?  125 PRO   B N    1 
ATOM   6617 C CA   . PRO   B 1 125 ? 43.753 -25.855 -4.705  1.00 11.59 ?  125 PRO   B CA   1 
ATOM   6618 C C    . PRO   B 1 125 ? 42.347 -26.120 -4.162  1.00 11.71 ?  125 PRO   B C    1 
ATOM   6619 O O    . PRO   B 1 125 ? 41.555 -25.204 -3.951  1.00 11.91 ?  125 PRO   B O    1 
ATOM   6620 C CB   . PRO   B 1 125 ? 44.739 -25.792 -3.533  1.00 12.58 ?  125 PRO   B CB   1 
ATOM   6621 C CG   . PRO   B 1 125 ? 44.511 -24.386 -2.974  1.00 12.49 ?  125 PRO   B CG   1 
ATOM   6622 C CD   . PRO   B 1 125 ? 44.138 -23.516 -4.175  1.00 11.64 ?  125 PRO   B CD   1 
ATOM   6623 H HA   . PRO   B 1 125 ? 44.021 -26.525 -5.362  1.00 13.93 ?  125 PRO   B HA   1 
ATOM   6624 H HB2  . PRO   B 1 125 ? 44.515 -26.478 -2.881  1.00 15.11 ?  125 PRO   B HB2  1 
ATOM   6625 H HB3  . PRO   B 1 125 ? 45.647 -25.904 -3.856  1.00 15.11 ?  125 PRO   B HB3  1 
ATOM   6626 H HG2  . PRO   B 1 125 ? 43.785 -24.410 -2.327  1.00 15.01 ?  125 PRO   B HG2  1 
ATOM   6627 H HG3  . PRO   B 1 125 ? 45.328 -24.072 -2.552  1.00 15.01 ?  125 PRO   B HG3  1 
ATOM   6628 H HD2  . PRO   B 1 125 ? 43.362 -22.980 -3.974  1.00 13.98 ?  125 PRO   B HD2  1 
ATOM   6629 H HD3  . PRO   B 1 125 ? 44.899 -22.963 -4.428  1.00 13.98 ?  125 PRO   B HD3  1 
ATOM   6630 N N    . LEU   B 1 126 ? 42.071 -27.389 -3.871  1.00 12.41 ?  126 LEU   B N    1 
ATOM   6631 C CA   . LEU   B 1 126 ? 40.858 -27.744 -3.138  1.00 13.10 ?  126 LEU   B CA   1 
ATOM   6632 C C    . LEU   B 1 126 ? 40.983 -27.341 -1.674  1.00 13.08 ?  126 LEU   B C    1 
ATOM   6633 O O    . LEU   B 1 126 ? 41.893 -27.786 -0.968  1.00 15.54 ?  126 LEU   B O    1 
ATOM   6634 C CB   . LEU   B 1 126 ? 40.603 -29.239 -3.244  1.00 14.05 ?  126 LEU   B CB   1 
ATOM   6635 C CG   . LEU   B 1 126 ? 40.057 -29.741 -4.585  1.00 15.28 ?  126 LEU   B CG   1 
ATOM   6636 C CD1  . LEU   B 1 126 ? 40.093 -31.252 -4.635  1.00 17.32 ?  126 LEU   B CD1  1 
ATOM   6637 C CD2  . LEU   B 1 126 ? 38.650 -29.236 -4.850  1.00 15.54 ?  126 LEU   B CD2  1 
ATOM   6638 H H    . LEU   B 1 126 ? 42.569 -28.062 -4.091  1.00 14.91 ?  126 LEU   B H    1 
ATOM   6639 H HA   . LEU   B 1 126 ? 40.107 -27.270 -3.527  1.00 15.74 ?  126 LEU   B HA   1 
ATOM   6640 H HB2  . LEU   B 1 126 ? 41.432 -29.704 -3.078  1.00 16.88 ?  126 LEU   B HB2  1 
ATOM   6641 H HB3  . LEU   B 1 126 ? 39.952 -29.479 -2.564  1.00 16.88 ?  126 LEU   B HB3  1 
ATOM   6642 H HG   . LEU   B 1 126 ? 40.629 -29.401 -5.295  1.00 18.36 ?  126 LEU   B HG   1 
ATOM   6643 H HD11 . LEU   B 1 126 ? 39.743 -31.545 -5.490  1.00 20.81 ?  126 LEU   B HD11 1 
ATOM   6644 H HD12 . LEU   B 1 126 ? 41.006 -31.550 -4.527  1.00 20.81 ?  126 LEU   B HD12 1 
ATOM   6645 H HD13 . LEU   B 1 126 ? 39.541 -31.600 -3.915  1.00 20.81 ?  126 LEU   B HD13 1 
ATOM   6646 H HD21 . LEU   B 1 126 ? 38.315 -29.652 -5.661  1.00 18.66 ?  126 LEU   B HD21 1 
ATOM   6647 H HD22 . LEU   B 1 126 ? 38.084 -29.470 -4.100  1.00 18.66 ?  126 LEU   B HD22 1 
ATOM   6648 H HD23 . LEU   B 1 126 ? 38.670 -28.271 -4.962  1.00 18.66 ?  126 LEU   B HD23 1 
ATOM   6649 N N    . LEU   B 1 127 ? 40.038 -26.540 -1.200  1.00 13.07 ?  127 LEU   B N    1 
ATOM   6650 C CA   . LEU   B 1 127 ? 40.102 -26.041 0.163   1.00 13.79 ?  127 LEU   B CA   1 
ATOM   6651 C C    . LEU   B 1 127 ? 39.816 -27.153 1.163   1.00 13.39 ?  127 LEU   B C    1 
ATOM   6652 O O    . LEU   B 1 127 ? 39.001 -28.051 0.934   1.00 13.70 ?  127 LEU   B O    1 
ATOM   6653 C CB   . LEU   B 1 127 ? 39.094 -24.909 0.370   1.00 14.03 ?  127 LEU   B CB   1 
ATOM   6654 C CG   . LEU   B 1 127 ? 39.280 -23.660 -0.484  1.00 14.24 ?  127 LEU   B CG   1 
ATOM   6655 C CD1  . LEU   B 1 127 ? 38.170 -22.674 -0.145  1.00 14.79 ?  127 LEU   B CD1  1 
ATOM   6656 C CD2  . LEU   B 1 127 ? 40.663 -23.037 -0.286  1.00 15.25 ?  127 LEU   B CD2  1 
ATOM   6657 H H    . LEU   B 1 127 ? 39.359 -26.253 -1.658  1.00 15.71 ?  127 LEU   B H    1 
ATOM   6658 H HA   . LEU   B 1 127 ? 40.992 -25.686 0.331   1.00 16.57 ?  127 LEU   B HA   1 
ATOM   6659 H HB2  . LEU   B 1 127 ? 38.207 -25.258 0.180   1.00 16.86 ?  127 LEU   B HB2  1 
ATOM   6660 H HB3  . LEU   B 1 127 ? 39.137 -24.634 1.298   1.00 16.86 ?  127 LEU   B HB3  1 
ATOM   6661 H HG   . LEU   B 1 127 ? 39.186 -23.896 -1.419  1.00 17.10 ?  127 LEU   B HG   1 
ATOM   6662 H HD11 . LEU   B 1 127 ? 38.287 -21.869 -0.679  1.00 17.77 ?  127 LEU   B HD11 1 
ATOM   6663 H HD12 . LEU   B 1 127 ? 37.312 -23.076 -0.335  1.00 17.77 ?  127 LEU   B HD12 1 
ATOM   6664 H HD13 . LEU   B 1 127 ? 38.227 -22.445 0.800   1.00 17.77 ?  127 LEU   B HD13 1 
ATOM   6665 H HD21 . LEU   B 1 127 ? 40.698 -22.189 -0.754  1.00 18.32 ?  127 LEU   B HD21 1 
ATOM   6666 H HD22 . LEU   B 1 127 ? 40.812 -22.897 0.663   1.00 18.32 ?  127 LEU   B HD22 1 
ATOM   6667 H HD23 . LEU   B 1 127 ? 41.333 -23.641 -0.641  1.00 18.32 ?  127 LEU   B HD23 1 
ATOM   6668 N N    . SER   B 1 128 ? 40.498 -27.072 2.293   1.00 13.33 ?  128 SER   B N    1 
ATOM   6669 C CA   . SER   B 1 128 ? 40.374 -27.981 3.420   1.00 14.27 ?  128 SER   B CA   1 
ATOM   6670 C C    . SER   B 1 128 ? 40.856 -29.396 3.103   1.00 15.80 ?  128 SER   B C    1 
ATOM   6671 O O    . SER   B 1 128 ? 40.733 -30.279 3.954   1.00 17.95 ?  128 SER   B O    1 
ATOM   6672 C CB   . SER   B 1 128 ? 38.964 -27.970 4.042   1.00 14.32 ?  128 SER   B CB   1 
ATOM   6673 O OG   . SER   B 1 128 ? 38.660 -26.682 4.583   1.00 14.97 ?  128 SER   B OG   1 
ATOM   6674 H H    . SER   B 1 128 ? 41.066 -26.448 2.437   1.00 16.02 ?  128 SER   B H    1 
ATOM   6675 H HA   . SER   B 1 128 ? 40.963 -27.646 4.101   1.00 17.15 ?  128 SER   B HA   1 
ATOM   6676 H HB2  . SER   B 1 128 ? 38.304 -28.203 3.370   1.00 17.20 ?  128 SER   B HB2  1 
ATOM   6677 H HB3  . SER   B 1 128 ? 38.935 -28.628 4.768   1.00 17.20 ?  128 SER   B HB3  1 
ATOM   6678 H HG   . SER   B 1 128 ? 39.232 -26.474 5.161   1.00 17.99 ?  128 SER   B HG   1 
ATOM   6679 N N    . ALA   B 1 129 ? 41.437 -29.627 1.919   1.00 17.03 ?  129 ALA   B N    1 
ATOM   6680 C CA   . ALA   B 1 129 ? 41.987 -30.923 1.556   1.00 17.85 ?  129 ALA   B CA   1 
ATOM   6681 C C    . ALA   B 1 129 ? 43.380 -31.098 2.149   1.00 16.77 ?  129 ALA   B C    1 
ATOM   6682 O O    . ALA   B 1 129 ? 43.944 -30.199 2.790   1.00 16.57 ?  129 ALA   B O    1 
ATOM   6683 C CB   . ALA   B 1 129 ? 42.042 -31.072 0.035   1.00 20.27 ?  129 ALA   B CB   1 
ATOM   6684 H H    . ALA   B 1 129 ? 41.518 -29.035 1.290   1.00 20.45 ?  129 ALA   B H    1 
ATOM   6685 H HA   . ALA   B 1 129 ? 41.415 -31.622 1.903   1.00 21.44 ?  129 ALA   B HA   1 
ATOM   6686 H HB1  . ALA   B 1 129 ? 42.401 -31.948 -0.189  1.00 24.34 ?  129 ALA   B HB1  1 
ATOM   6687 H HB2  . ALA   B 1 129 ? 41.144 -30.986 -0.327  1.00 24.34 ?  129 ALA   B HB2  1 
ATOM   6688 H HB3  . ALA   B 1 129 ? 42.613 -30.380 -0.336  1.00 24.34 ?  129 ALA   B HB3  1 
ATOM   6689 N N    . GLY   B 1 130 ? 43.940 -32.284 1.917   1.00 16.99 ?  130 GLY   B N    1 
ATOM   6690 C CA   . GLY   B 1 130 ? 45.332 -32.526 2.254   1.00 17.75 ?  130 GLY   B CA   1 
ATOM   6691 C C    . GLY   B 1 130 ? 45.560 -32.428 3.745   1.00 17.26 ?  130 GLY   B C    1 
ATOM   6692 O O    . GLY   B 1 130 ? 44.863 -33.066 4.547   1.00 18.57 ?  130 GLY   B O    1 
ATOM   6693 H H    . GLY   B 1 130 ? 43.543 -32.957 1.556   1.00 20.41 ?  130 GLY   B H    1 
ATOM   6694 H HA2  . GLY   B 1 130 ? 45.592 -33.416 1.958   1.00 21.32 ?  130 GLY   B HA2  1 
ATOM   6695 H HA3  . GLY   B 1 130 ? 45.899 -31.878 1.809   1.00 21.32 ?  130 GLY   B HA3  1 
ATOM   6696 N N    . ILE   B 1 131 ? 46.540 -31.605 4.130   1.00 18.14 ?  131 ILE   B N    1 
ATOM   6697 C CA   . ILE   B 1 131 ? 46.913 -31.478 5.531   1.00 19.13 ?  131 ILE   B CA   1 
ATOM   6698 C C    . ILE   B 1 131 ? 45.802 -30.882 6.377   1.00 18.06 ?  131 ILE   B C    1 
ATOM   6699 O O    . ILE   B 1 131 ? 45.874 -30.958 7.605   1.00 19.53 ?  131 ILE   B O    1 
ATOM   6700 C CB   . ILE   B 1 131 ? 48.231 -30.686 5.729   1.00 21.35 ?  131 ILE   B CB   1 
ATOM   6701 C CG1  . ILE   B 1 131 ? 48.051 -29.205 5.365   1.00 22.80 ?  131 ILE   B CG1  1 
ATOM   6702 C CG2  . ILE   B 1 131 ? 49.354 -31.302 4.910   1.00 22.42 ?  131 ILE   B CG2  1 
ATOM   6703 C CD1  . ILE   B 1 131 ? 49.256 -28.334 5.699   1.00 23.92 ?  131 ILE   B CD1  1 
ATOM   6704 H H    . ILE   B 1 131 ? 46.997 -31.103 3.596   1.00 21.78 ?  131 ILE   B H    1 
ATOM   6705 H HA   . ILE   B 1 131 ? 47.074 -32.368 5.871   1.00 22.98 ?  131 ILE   B HA   1 
ATOM   6706 H HB   . ILE   B 1 131 ? 48.474 -30.739 6.669   1.00 25.64 ?  131 ILE   B HB   1 
ATOM   6707 H HG12 . ILE   B 1 131 ? 47.889 -29.141 4.411   1.00 27.37 ?  131 ILE   B HG12 1 
ATOM   6708 H HG13 . ILE   B 1 131 ? 47.290 -28.845 5.850   1.00 27.37 ?  131 ILE   B HG13 1 
ATOM   6709 H HG21 . ILE   B 1 131 ? 50.193 -30.887 5.163   1.00 26.92 ?  131 ILE   B HG21 1 
ATOM   6710 H HG22 . ILE   B 1 131 ? 49.386 -32.253 5.087   1.00 26.92 ?  131 ILE   B HG22 1 
ATOM   6711 H HG23 . ILE   B 1 131 ? 49.176 -31.145 3.969   1.00 26.92 ?  131 ILE   B HG23 1 
ATOM   6712 H HD11 . ILE   B 1 131 ? 49.025 -27.407 5.536   1.00 28.72 ?  131 ILE   B HD11 1 
ATOM   6713 H HD12 . ILE   B 1 131 ? 49.483 -28.460 6.634   1.00 28.72 ?  131 ILE   B HD12 1 
ATOM   6714 H HD13 . ILE   B 1 131 ? 49.999 -28.598 5.138   1.00 28.72 ?  131 ILE   B HD13 1 
ATOM   6715 N N    . PHE   B 1 132 ? 44.770 -30.301 5.756   1.00 17.25 ?  132 PHE   B N    1 
ATOM   6716 C CA   . PHE   B 1 132 ? 43.623 -29.785 6.495   1.00 17.72 ?  132 PHE   B CA   1 
ATOM   6717 C C    . PHE   B 1 132 ? 42.594 -30.863 6.831   1.00 19.40 ?  132 PHE   B C    1 
ATOM   6718 O O    . PHE   B 1 132 ? 41.698 -30.603 7.641   1.00 21.04 ?  132 PHE   B O    1 
ATOM   6719 C CB   . PHE   B 1 132 ? 42.939 -28.665 5.706   1.00 16.93 ?  132 PHE   B CB   1 
ATOM   6720 C CG   . PHE   B 1 132 ? 43.626 -27.323 5.799   1.00 16.37 ?  132 PHE   B CG   1 
ATOM   6721 C CD1  . PHE   B 1 132 ? 44.920 -27.139 5.342   1.00 17.96 ?  132 PHE   B CD1  1 
ATOM   6722 C CD2  . PHE   B 1 132 ? 42.936 -26.228 6.299   1.00 15.78 ?  132 PHE   B CD2  1 
ATOM   6723 C CE1  . PHE   B 1 132 ? 45.533 -25.897 5.428   1.00 18.20 ?  132 PHE   B CE1  1 
ATOM   6724 C CE2  . PHE   B 1 132 ? 43.538 -24.980 6.375   1.00 16.86 ?  132 PHE   B CE2  1 
ATOM   6725 C CZ   . PHE   B 1 132 ? 44.834 -24.818 5.935   1.00 17.90 ?  132 PHE   B CZ   1 
ATOM   6726 H H    . PHE   B 1 132 ? 44.718 -30.194 4.905   1.00 20.71 ?  132 PHE   B H    1 
ATOM   6727 H HA   . PHE   B 1 132 ? 43.941 -29.411 7.331   1.00 21.28 ?  132 PHE   B HA   1 
ATOM   6728 H HB2  . PHE   B 1 132 ? 42.919 -28.919 4.773   1.00 20.34 ?  132 PHE   B HB2  1 
ATOM   6729 H HB3  . PHE   B 1 132 ? 42.036 -28.564 6.042   1.00 20.34 ?  132 PHE   B HB3  1 
ATOM   6730 H HD1  . PHE   B 1 132 ? 45.396 -27.870 5.006   1.00 21.57 ?  132 PHE   B HD1  1 
ATOM   6731 H HD2  . PHE   B 1 132 ? 42.059 -26.336 6.602   1.00 18.96 ?  132 PHE   B HD2  1 
ATOM   6732 H HE1  . PHE   B 1 132 ? 46.405 -25.787 5.131   1.00 21.86 ?  132 PHE   B HE1  1 
ATOM   6733 H HE2  . PHE   B 1 132 ? 43.064 -24.256 6.727   1.00 20.25 ?  132 PHE   B HE2  1 
ATOM   6734 H HZ   . PHE   B 1 132 ? 45.238 -23.981 5.993   1.00 21.50 ?  132 PHE   B HZ   1 
ATOM   6735 N N    . GLY   B 1 133 ? 42.677 -32.054 6.224   1.00 18.87 ?  133 GLY   B N    1 
ATOM   6736 C CA   . GLY   B 1 133 ? 41.963 -33.216 6.719   1.00 20.30 ?  133 GLY   B CA   1 
ATOM   6737 C C    . GLY   B 1 133 ? 40.557 -33.462 6.204   1.00 20.81 ?  133 GLY   B C    1 
ATOM   6738 O O    . GLY   B 1 133 ? 39.969 -34.482 6.572   1.00 22.67 ?  133 GLY   B O    1 
ATOM   6739 H H    . GLY   B 1 133 ? 43.153 -32.208 5.520   1.00 22.66 ?  133 GLY   B H    1 
ATOM   6740 H HA2  . GLY   B 1 133 ? 42.492 -34.006 6.520   1.00 24.38 ?  133 GLY   B HA2  1 
ATOM   6741 H HA3  . GLY   B 1 133 ? 41.901 -33.144 7.683   1.00 24.38 ?  133 GLY   B HA3  1 
ATOM   6742 N N    . ALA   B 1 134 ? 39.986 -32.579 5.388   1.00 19.73 ?  134 ALA   B N    1 
ATOM   6743 C CA   . ALA   B 1 134 ? 38.659 -32.857 4.851   1.00 20.20 ?  134 ALA   B CA   1 
ATOM   6744 C C    . ALA   B 1 134 ? 38.741 -33.853 3.698   1.00 19.49 ?  134 ALA   B C    1 
ATOM   6745 O O    . ALA   B 1 134 ? 39.796 -34.054 3.090   1.00 20.27 ?  134 ALA   B O    1 
ATOM   6746 C CB   . ALA   B 1 134 ? 37.990 -31.575 4.360   1.00 20.61 ?  134 ALA   B CB   1 
ATOM   6747 H H    . ALA   B 1 134 ? 40.330 -31.827 5.149   1.00 23.69 ?  134 ALA   B H    1 
ATOM   6748 H HA   . ALA   B 1 134 ? 38.108 -33.242 5.548   1.00 24.26 ?  134 ALA   B HA   1 
ATOM   6749 H HB1  . ALA   B 1 134 ? 37.096 -31.793 4.044   1.00 24.74 ?  134 ALA   B HB1  1 
ATOM   6750 H HB2  . ALA   B 1 134 ? 37.936 -30.947 5.095   1.00 24.74 ?  134 ALA   B HB2  1 
ATOM   6751 H HB3  . ALA   B 1 134 ? 38.514 -31.201 3.637   1.00 24.74 ?  134 ALA   B HB3  1 
ATOM   6752 N N    . ASP   B 1 135 ? 37.602 -34.469 3.394   1.00 19.72 ?  135 ASP   B N    1 
ATOM   6753 C CA   . ASP   B 1 135 ? 37.516 -35.368 2.250   1.00 20.41 ?  135 ASP   B CA   1 
ATOM   6754 C C    . ASP   B 1 135 ? 37.614 -34.537 0.977   1.00 18.98 ?  135 ASP   B C    1 
ATOM   6755 O O    . ASP   B 1 135 ? 36.754 -33.675 0.744   1.00 18.78 ?  135 ASP   B O    1 
ATOM   6756 C CB   . ASP   B 1 135 ? 36.184 -36.116 2.303   1.00 22.11 ?  135 ASP   B CB   1 
ATOM   6757 C CG   . ASP   B 1 135 ? 36.017 -37.129 1.180   1.00 24.06 ?  135 ASP   B CG   1 
ATOM   6758 O OD1  . ASP   B 1 135 ? 36.869 -37.165 0.268   1.00 23.89 ?  135 ASP   B OD1  1 
ATOM   6759 O OD2  . ASP   B 1 135 ? 35.031 -37.903 1.226   1.00 27.37 -1 135 ASP   B OD2  1 
ATOM   6760 H H    . ASP   B 1 135 ? 36.867 -34.371 3.822   1.00 23.68 ?  135 ASP   B H    1 
ATOM   6761 H HA   . ASP   B 1 135 ? 38.243 -36.008 2.286   1.00 24.51 ?  135 ASP   B HA   1 
ATOM   6762 H HB2  . ASP   B 1 135 ? 36.135 -36.597 3.140   1.00 26.55 ?  135 ASP   B HB2  1 
ATOM   6763 H HB3  . ASP   B 1 135 ? 35.466 -35.477 2.234   1.00 26.55 ?  135 ASP   B HB3  1 
ATOM   6764 N N    . PRO   B 1 136 ? 38.622 -34.748 0.129   1.00 18.75 ?  136 PRO   B N    1 
ATOM   6765 C CA   . PRO   B 1 136 ? 38.711 -33.937 -1.097  1.00 17.73 ?  136 PRO   B CA   1 
ATOM   6766 C C    . PRO   B 1 136 ? 37.512 -34.092 -2.014  1.00 16.73 ?  136 PRO   B C    1 
ATOM   6767 O O    . PRO   B 1 136 ? 37.196 -33.160 -2.758  1.00 15.76 ?  136 PRO   B O    1 
ATOM   6768 C CB   . PRO   B 1 136 ? 40.017 -34.419 -1.750  1.00 18.78 ?  136 PRO   B CB   1 
ATOM   6769 C CG   . PRO   B 1 136 ? 40.236 -35.805 -1.172  1.00 20.60 ?  136 PRO   B CG   1 
ATOM   6770 C CD   . PRO   B 1 136 ? 39.723 -35.720 0.231   1.00 20.19 ?  136 PRO   B CD   1 
ATOM   6771 H HA   . PRO   B 1 136 ? 38.797 -32.999 -0.878  1.00 21.29 ?  136 PRO   B HA   1 
ATOM   6772 H HB2  . PRO   B 1 136 ? 39.916 -34.457 -2.717  1.00 22.55 ?  136 PRO   B HB2  1 
ATOM   6773 H HB3  . PRO   B 1 136 ? 40.742 -33.821 -1.507  1.00 22.55 ?  136 PRO   B HB3  1 
ATOM   6774 H HG2  . PRO   B 1 136 ? 39.729 -36.459 -1.680  1.00 24.74 ?  136 PRO   B HG2  1 
ATOM   6775 H HG3  . PRO   B 1 136 ? 41.180 -36.022 -1.177  1.00 24.74 ?  136 PRO   B HG3  1 
ATOM   6776 H HD2  . PRO   B 1 136 ? 39.390 -36.580 0.524   1.00 24.25 ?  136 PRO   B HD2  1 
ATOM   6777 H HD3  . PRO   B 1 136 ? 40.409 -35.378 0.827   1.00 24.25 ?  136 PRO   B HD3  1 
ATOM   6778 N N    . ILE   B 1 137 ? 36.852 -35.256 -2.008  1.00 16.99 ?  137 ILE   B N    1 
ATOM   6779 C CA   . ILE   B 1 137 ? 35.636 -35.428 -2.803  1.00 17.17 ?  137 ILE   B CA   1 
ATOM   6780 C C    . ILE   B 1 137 ? 34.555 -34.460 -2.333  1.00 16.86 ?  137 ILE   B C    1 
ATOM   6781 O O    . ILE   B 1 137 ? 33.845 -33.841 -3.141  1.00 16.77 ?  137 ILE   B O    1 
ATOM   6782 C CB   . ILE   B 1 137 ? 35.166 -36.897 -2.743  1.00 19.73 ?  137 ILE   B CB   1 
ATOM   6783 C CG1  . ILE   B 1 137 ? 36.167 -37.805 -3.458  1.00 21.80 ?  137 ILE   B CG1  1 
ATOM   6784 C CG2  . ILE   B 1 137 ? 33.777 -37.056 -3.366  1.00 20.64 ?  137 ILE   B CG2  1 
ATOM   6785 C CD1  . ILE   B 1 137 ? 35.852 -39.286 -3.329  1.00 23.96 ?  137 ILE   B CD1  1 
ATOM   6786 H H    . ILE   B 1 137 ? 37.082 -35.956 -1.563  1.00 20.41 ?  137 ILE   B H    1 
ATOM   6787 H HA   . ILE   B 1 137 ? 35.830 -35.225 -3.733  1.00 20.62 ?  137 ILE   B HA   1 
ATOM   6788 H HB   . ILE   B 1 137 ? 35.113 -37.168 -1.817  1.00 23.70 ?  137 ILE   B HB   1 
ATOM   6789 H HG12 . ILE   B 1 137 ? 36.173 -37.589 -4.404  1.00 26.17 ?  137 ILE   B HG12 1 
ATOM   6790 H HG13 . ILE   B 1 137 ? 37.048 -37.659 -3.081  1.00 26.17 ?  137 ILE   B HG13 1 
ATOM   6791 H HG21 . ILE   B 1 137 ? 33.496 -37.982 -3.297  1.00 24.78 ?  137 ILE   B HG21 1 
ATOM   6792 H HG22 . ILE   B 1 137 ? 33.145 -36.501 -2.892  1.00 24.78 ?  137 ILE   B HG22 1 
ATOM   6793 H HG23 . ILE   B 1 137 ? 33.820 -36.794 -4.298  1.00 24.78 ?  137 ILE   B HG23 1 
ATOM   6794 H HD11 . ILE   B 1 137 ? 36.437 -39.771 -3.925  1.00 28.77 ?  137 ILE   B HD11 1 
ATOM   6795 H HD12 . ILE   B 1 137 ? 36.003 -39.564 -2.410  1.00 28.77 ?  137 ILE   B HD12 1 
ATOM   6796 H HD13 . ILE   B 1 137 ? 34.931 -39.455 -3.579  1.00 28.77 ?  137 ILE   B HD13 1 
ATOM   6797 N N    . HIS   B 1 138 ? 34.425 -34.302 -1.020  1.00 17.49 ?  138 HIS   B N    1 
ATOM   6798 C CA   . HIS   B 1 138 ? 33.481 -33.328 -0.490  1.00 17.93 ?  138 HIS   B CA   1 
ATOM   6799 C C    . HIS   B 1 138 ? 33.899 -31.903 -0.824  1.00 16.82 ?  138 HIS   B C    1 
ATOM   6800 O O    . HIS   B 1 138 ? 33.050 -31.062 -1.135  1.00 17.52 ?  138 HIS   B O    1 
ATOM   6801 C CB   . HIS   B 1 138 ? 33.362 -33.493 1.018   1.00 20.01 ?  138 HIS   B CB   1 
ATOM   6802 C CG   . HIS   B 1 138 ? 32.430 -32.510 1.645   1.00 21.59 ?  138 HIS   B CG   1 
ATOM   6803 N ND1  . HIS   B 1 138 ? 31.095 -32.441 1.311   1.00 23.30 ?  138 HIS   B ND1  1 
ATOM   6804 C CD2  . HIS   B 1 138 ? 32.643 -31.529 2.554   1.00 22.17 ?  138 HIS   B CD2  1 
ATOM   6805 C CE1  . HIS   B 1 138 ? 30.519 -31.475 2.003   1.00 23.48 ?  138 HIS   B CE1  1 
ATOM   6806 N NE2  . HIS   B 1 138 ? 31.435 -30.908 2.769   1.00 22.60 ?  138 HIS   B NE2  1 
ATOM   6807 H H    . HIS   B 1 138 ? 34.866 -34.740 -0.427  1.00 21.00 ?  138 HIS   B H    1 
ATOM   6808 H HA   . HIS   B 1 138 ? 32.611 -33.488 -0.883  1.00 21.53 ?  138 HIS   B HA   1 
ATOM   6809 H HB2  . HIS   B 1 138 ? 33.026 -34.382 1.210   1.00 24.03 ?  138 HIS   B HB2  1 
ATOM   6810 H HB3  . HIS   B 1 138 ? 34.234 -33.373 1.419   1.00 24.03 ?  138 HIS   B HB3  1 
ATOM   6811 H HD1  . HIS   B 1 138 ? 30.698 -32.954 0.742   1.00 27.98 ?  138 HIS   B HD1  1 
ATOM   6812 H HD2  . HIS   B 1 138 ? 33.442 -31.327 2.976   1.00 26.62 ?  138 HIS   B HD2  1 
ATOM   6813 H HE1  . HIS   B 1 138 ? 29.616 -31.242 1.960   1.00 28.20 ?  138 HIS   B HE1  1 
ATOM   6814 N N    . SER   B 1 139 ? 35.195 -31.604 -0.757  1.00 15.96 ?  139 SER   B N    1 
ATOM   6815 C CA   . SER   B 1 139 ? 35.639 -30.258 -1.084  1.00 14.97 ?  139 SER   B CA   1 
ATOM   6816 C C    . SER   B 1 139 ? 35.307 -29.913 -2.526  1.00 14.22 ?  139 SER   B C    1 
ATOM   6817 O O    . SER   B 1 139 ? 34.873 -28.794 -2.812  1.00 14.69 ?  139 SER   B O    1 
ATOM   6818 C CB   . SER   B 1 139 ? 37.136 -30.117 -0.817  1.00 16.06 ?  139 SER   B CB   1 
ATOM   6819 O OG   . SER   B 1 139 ? 37.558 -28.787 -1.053  1.00 15.54 ?  139 SER   B OG   1 
ATOM   6820 H H    . SER   B 1 139 ? 35.821 -32.149 -0.541  1.00 19.16 ?  139 SER   B H    1 
ATOM   6821 H HA   . SER   B 1 139 ? 35.171 -29.626 -0.525  1.00 17.98 ?  139 SER   B HA   1 
ATOM   6822 H HB2  . SER   B 1 139 ? 37.310 -30.346 0.109   1.00 19.28 ?  139 SER   B HB2  1 
ATOM   6823 H HB3  . SER   B 1 139 ? 37.625 -30.708 -1.407  1.00 19.28 ?  139 SER   B HB3  1 
ATOM   6824 H HG   . SER   B 1 139 ? 38.382 -28.709 -0.894  1.00 18.67 ?  139 SER   B HG   1 
ATOM   6825 N N    . LEU   B 1 140 ? 35.491 -30.865 -3.447  1.00 13.93 ?  140 LEU   B N    1 
ATOM   6826 C CA   . LEU   B 1 140 ? 35.139 -30.615 -4.838  1.00 14.17 ?  140 LEU   B CA   1 
ATOM   6827 C C    . LEU   B 1 140 ? 33.640 -30.386 -4.982  1.00 14.07 ?  140 LEU   B C    1 
ATOM   6828 O O    . LEU   B 1 140 ? 33.214 -29.501 -5.728  1.00 14.54 ?  140 LEU   B O    1 
ATOM   6829 C CB   . LEU   B 1 140 ? 35.621 -31.776 -5.713  1.00 14.34 ?  140 LEU   B CB   1 
ATOM   6830 C CG   . LEU   B 1 140 ? 35.256 -31.671 -7.185  1.00 14.94 ?  140 LEU   B CG   1 
ATOM   6831 C CD1  . LEU   B 1 140 ? 35.852 -30.418 -7.792  1.00 15.87 ?  140 LEU   B CD1  1 
ATOM   6832 C CD2  . LEU   B 1 140 ? 35.738 -32.909 -7.913  1.00 15.87 ?  140 LEU   B CD2  1 
ATOM   6833 H H    . LEU   B 1 140 ? 35.812 -31.646 -3.299  1.00 16.74 ?  140 LEU   B H    1 
ATOM   6834 H HA   . LEU   B 1 140 ? 35.599 -29.813 -5.143  1.00 17.03 ?  140 LEU   B HA   1 
ATOM   6835 H HB2  . LEU   B 1 140 ? 36.590 -31.831 -5.661  1.00 17.23 ?  140 LEU   B HB2  1 
ATOM   6836 H HB3  . LEU   B 1 140 ? 35.232 -32.600 -5.382  1.00 17.23 ?  140 LEU   B HB3  1 
ATOM   6837 H HG   . LEU   B 1 140 ? 34.295 -31.617 -7.273  1.00 17.94 ?  140 LEU   B HG   1 
ATOM   6838 H HD11 . LEU   B 1 140 ? 35.731 -30.446 -8.752  1.00 19.06 ?  140 LEU   B HD11 1 
ATOM   6839 H HD12 . LEU   B 1 140 ? 35.402 -29.640 -7.424  1.00 19.06 ?  140 LEU   B HD12 1 
ATOM   6840 H HD13 . LEU   B 1 140 ? 36.799 -30.383 -7.578  1.00 19.06 ?  140 LEU   B HD13 1 
ATOM   6841 H HD21 . LEU   B 1 140 ? 35.497 -32.831 -8.851  1.00 19.07 ?  140 LEU   B HD21 1 
ATOM   6842 H HD22 . LEU   B 1 140 ? 36.696 -32.980 -7.818  1.00 19.07 ?  140 LEU   B HD22 1 
ATOM   6843 H HD23 . LEU   B 1 140 ? 35.302 -33.685 -7.525  1.00 19.07 ?  140 LEU   B HD23 1 
ATOM   6844 N N    . ARG   B 1 141 ? 32.832 -31.179 -4.270  1.00 14.99 ?  141 ARG   B N    1 
ATOM   6845 C CA   . ARG   B 1 141 ? 31.384 -30.996 -4.248  1.00 15.94 ?  141 ARG   B CA   1 
ATOM   6846 C C    . ARG   B 1 141 ? 31.010 -29.579 -3.829  1.00 15.41 ?  141 ARG   B C    1 
ATOM   6847 O O    . ARG   B 1 141 ? 30.219 -28.901 -4.503  1.00 15.42 ?  141 ARG   B O    1 
ATOM   6848 C CB   . ARG   B 1 141 ? 30.792 -32.020 -3.272  1.00 17.73 ?  141 ARG   B CB   1 
ATOM   6849 C CG   . ARG   B 1 141 ? 29.330 -31.876 -2.934  1.00 20.14 ?  141 ARG   B CG   1 
ATOM   6850 C CD   . ARG   B 1 141 ? 28.512 -32.509 -3.989  1.00 21.74 ?  141 ARG   B CD   1 
ATOM   6851 N NE   . ARG   B 1 141 ? 28.259 -31.609 -5.102  1.00 21.84 ?  141 ARG   B NE   1 
ATOM   6852 C CZ   . ARG   B 1 141 ? 28.259 -31.971 -6.377  1.00 21.15 ?  141 ARG   B CZ   1 
ATOM   6853 N NH1  . ARG   B 1 141 ? 28.693 -33.162 -6.762  1.00 20.71 ?  141 ARG   B NH1  1 
ATOM   6854 N NH2  . ARG   B 1 141 ? 27.818 -31.112 -7.292  1.00 22.30 ?  141 ARG   B NH2  1 
ATOM   6855 H H    . ARG   B 1 141 ? 33.110 -31.826 -3.786  1.00 18.00 ?  141 ARG   B H    1 
ATOM   6856 H HA   . ARG   B 1 141 ? 31.023 -31.152 -5.128  1.00 19.14 ?  141 ARG   B HA   1 
ATOM   6857 H HB2  . ARG   B 1 141 ? 30.927 -32.901 -3.652  1.00 21.29 ?  141 ARG   B HB2  1 
ATOM   6858 H HB3  . ARG   B 1 141 ? 31.284 -31.958 -2.440  1.00 21.29 ?  141 ARG   B HB3  1 
ATOM   6859 H HG2  . ARG   B 1 141 ? 29.152 -32.317 -2.092  1.00 24.18 ?  141 ARG   B HG2  1 
ATOM   6860 H HG3  . ARG   B 1 141 ? 29.086 -30.932 -2.872  1.00 24.18 ?  141 ARG   B HG3  1 
ATOM   6861 H HD2  . ARG   B 1 141 ? 28.978 -33.295 -4.320  1.00 26.10 ?  141 ARG   B HD2  1 
ATOM   6862 H HD3  . ARG   B 1 141 ? 27.667 -32.769 -3.609  1.00 26.10 ?  141 ARG   B HD3  1 
ATOM   6863 H HE   . ARG   B 1 141 ? 28.075 -30.787 -4.918  1.00 26.22 ?  141 ARG   B HE   1 
ATOM   6864 H HH11 . ARG   B 1 141 ? 28.969 -33.733 -6.184  1.00 24.87 ?  141 ARG   B HH11 1 
ATOM   6865 H HH12 . ARG   B 1 141 ? 28.689 -33.366 -7.595  1.00 24.87 ?  141 ARG   B HH12 1 
ATOM   6866 H HH21 . ARG   B 1 141 ? 27.544 -30.331 -7.056  1.00 26.78 ?  141 ARG   B HH21 1 
ATOM   6867 H HH22 . ARG   B 1 141 ? 27.834 -31.326 -8.126  1.00 26.78 ?  141 ARG   B HH22 1 
ATOM   6868 N N    . VAL   B 1 142 ? 31.548 -29.126 -2.699  1.00 14.89 ?  142 VAL   B N    1 
ATOM   6869 C CA   . VAL   B 1 142 ? 31.221 -27.789 -2.219  1.00 14.87 ?  142 VAL   B CA   1 
ATOM   6870 C C    . VAL   B 1 142 ? 31.709 -26.736 -3.208  1.00 14.62 ?  142 VAL   B C    1 
ATOM   6871 O O    . VAL   B 1 142 ? 31.018 -25.747 -3.473  1.00 14.67 ?  142 VAL   B O    1 
ATOM   6872 C CB   . VAL   B 1 142 ? 31.774 -27.569 -0.797  1.00 15.34 ?  142 VAL   B CB   1 
ATOM   6873 C CG1  . VAL   B 1 142 ? 31.462 -26.154 -0.300  1.00 15.55 ?  142 VAL   B CG1  1 
ATOM   6874 C CG2  . VAL   B 1 142 ? 31.201 -28.605 0.154   1.00 15.99 ?  142 VAL   B CG2  1 
ATOM   6875 H H    . VAL   B 1 142 ? 32.087 -29.568 -2.192  1.00 17.89 ?  142 VAL   B H    1 
ATOM   6876 H HA   . VAL   B 1 142 ? 30.259 -27.706 -2.163  1.00 17.86 ?  142 VAL   B HA   1 
ATOM   6877 H HB   . VAL   B 1 142 ? 32.740 -27.674 -0.811  1.00 18.42 ?  142 VAL   B HB   1 
ATOM   6878 H HG11 . VAL   B 1 142 ? 31.676 -26.099 0.644   1.00 18.68 ?  142 VAL   B HG11 1 
ATOM   6879 H HG12 . VAL   B 1 142 ? 32.003 -25.517 -0.797  1.00 18.68 ?  142 VAL   B HG12 1 
ATOM   6880 H HG13 . VAL   B 1 142 ? 30.522 -25.972 -0.439  1.00 18.68 ?  142 VAL   B HG13 1 
ATOM   6881 H HG21 . VAL   B 1 142 ? 31.510 -28.415 1.051   1.00 19.21 ?  142 VAL   B HG21 1 
ATOM   6882 H HG22 . VAL   B 1 142 ? 30.235 -28.563 0.116   1.00 19.21 ?  142 VAL   B HG22 1 
ATOM   6883 H HG23 . VAL   B 1 142 ? 31.505 -29.486 -0.121  1.00 19.21 ?  142 VAL   B HG23 1 
ATOM   6884 N N    . CYS   B 1 143 ? 32.893 -26.940 -3.783  1.00 13.76 ?  143 CYS   B N    1 
ATOM   6885 C CA   . CYS   B 1 143 ? 33.390 -26.011 -4.793  1.00 13.69 ?  143 CYS   B CA   1 
ATOM   6886 C C    . CYS   B 1 143 ? 32.388 -25.873 -5.933  1.00 13.69 ?  143 CYS   B C    1 
ATOM   6887 O O    . CYS   B 1 143 ? 31.986 -24.763 -6.295  1.00 14.18 ?  143 CYS   B O    1 
ATOM   6888 C CB   . CYS   B 1 143 ? 34.745 -26.500 -5.319  1.00 14.25 ?  143 CYS   B CB   1 
ATOM   6889 S SG   . CYS   B 1 143 ? 35.506 -25.409 -6.545  1.00 14.24 ?  143 CYS   B SG   1 
ATOM   6890 H H    . CYS   B 1 143 ? 33.425 -27.591 -3.607  1.00 16.53 ?  143 CYS   B H    1 
ATOM   6891 H HA   . CYS   B 1 143 ? 33.524 -25.134 -4.393  1.00 16.44 ?  143 CYS   B HA   1 
ATOM   6892 H HB2  . CYS   B 1 143 ? 35.366 -26.578 -4.577  1.00 17.12 ?  143 CYS   B HB2  1 
ATOM   6893 H HB3  . CYS   B 1 143 ? 34.626 -27.366 -5.732  1.00 17.12 ?  143 CYS   B HB3  1 
ATOM   6894 H HG   . CYS   B 1 143 ? 36.578 -25.854 -6.857  1.00 17.10 ?  143 CYS   B HG   1 
ATOM   6895 N N    . VAL   B 1 144 ? 31.986 -26.992 -6.526  1.00 14.38 ?  144 VAL   B N    1 
ATOM   6896 C CA   . VAL   B 1 144 ? 31.092 -26.935 -7.673  1.00 15.77 ?  144 VAL   B CA   1 
ATOM   6897 C C    . VAL   B 1 144 ? 29.746 -26.321 -7.312  1.00 15.56 ?  144 VAL   B C    1 
ATOM   6898 O O    . VAL   B 1 144 ? 29.132 -25.632 -8.135  1.00 17.14 ?  144 VAL   B O    1 
ATOM   6899 C CB   . VAL   B 1 144 ? 30.935 -28.358 -8.224  1.00 18.92 ?  144 VAL   B CB   1 
ATOM   6900 C CG1  . VAL   B 1 144 ? 29.645 -28.511 -9.031  1.00 22.15 ?  144 VAL   B CG1  1 
ATOM   6901 C CG2  . VAL   B 1 144 ? 32.168 -28.765 -9.032  1.00 18.48 ?  144 VAL   B CG2  1 
ATOM   6902 H H    . VAL   B 1 144 ? 32.217 -27.783 -6.286  1.00 17.27 ?  144 VAL   B H    1 
ATOM   6903 H HA   . VAL   B 1 144 ? 31.491 -26.394 -8.369  1.00 18.94 ?  144 VAL   B HA   1 
ATOM   6904 H HB   . VAL   B 1 144 ? 30.872 -28.977 -7.476  1.00 22.72 ?  144 VAL   B HB   1 
ATOM   6905 H HG11 . VAL   B 1 144 ? 29.708 -29.318 -9.576  1.00 26.60 ?  144 VAL   B HG11 1 
ATOM   6906 H HG12 . VAL   B 1 144 ? 28.894 -28.596 -8.422  1.00 26.60 ?  144 VAL   B HG12 1 
ATOM   6907 H HG13 . VAL   B 1 144 ? 29.533 -27.742 -9.603  1.00 26.60 ?  144 VAL   B HG13 1 
ATOM   6908 H HG21 . VAL   B 1 144 ? 32.044 -29.671 -9.366  1.00 22.20 ?  144 VAL   B HG21 1 
ATOM   6909 H HG22 . VAL   B 1 144 ? 32.267 -28.153 -9.779  1.00 22.20 ?  144 VAL   B HG22 1 
ATOM   6910 H HG23 . VAL   B 1 144 ? 32.944 -28.725 -8.460  1.00 22.20 ?  144 VAL   B HG23 1 
ATOM   6911 N N    . ASP   B 1 145 ? 29.272 -26.547 -6.092  1.00 15.44 ?  145 ASP   B N    1 
ATOM   6912 C CA   . ASP   B 1 145 ? 27.962 -26.077 -5.663  1.00 16.72 ?  145 ASP   B CA   1 
ATOM   6913 C C    . ASP   B 1 145 ? 27.992 -24.657 -5.119  1.00 16.40 ?  145 ASP   B C    1 
ATOM   6914 O O    . ASP   B 1 145 ? 26.939 -24.120 -4.767  1.00 18.22 ?  145 ASP   B O    1 
ATOM   6915 C CB   . ASP   B 1 145 ? 27.398 -26.993 -4.572  1.00 18.29 ?  145 ASP   B CB   1 
ATOM   6916 C CG   . ASP   B 1 145 ? 26.998 -28.358 -5.080  1.00 20.52 ?  145 ASP   B CG   1 
ATOM   6917 O OD1  . ASP   B 1 145 ? 26.886 -28.556 -6.307  1.00 20.58 ?  145 ASP   B OD1  1 
ATOM   6918 O OD2  . ASP   B 1 145 ? 26.802 -29.237 -4.222  1.00 22.61 -1 145 ASP   B OD2  1 
ATOM   6919 H H    . ASP   B 1 145 ? 29.706 -26.964 -5.485  1.00 18.55 ?  145 ASP   B H    1 
ATOM   6920 H HA   . ASP   B 1 145 ? 27.359 -26.076 -6.419  1.00 20.09 ?  145 ASP   B HA   1 
ATOM   6921 H HB2  . ASP   B 1 145 ? 28.073 -27.126 -3.897  1.00 21.97 ?  145 ASP   B HB2  1 
ATOM   6922 H HB3  . ASP   B 1 145 ? 26.614 -26.572 -4.190  1.00 21.97 ?  145 ASP   B HB3  1 
ATOM   6923 N N    . THR   B 1 146 ? 29.165 -24.039 -5.026  1.00 14.57 ?  146 THR   B N    1 
ATOM   6924 C CA   . THR   B 1 146 ? 29.319 -22.716 -4.424  1.00 14.18 ?  146 THR   B CA   1 
ATOM   6925 C C    . THR   B 1 146 ? 29.958 -21.698 -5.349  1.00 13.81 ?  146 THR   B C    1 
ATOM   6926 O O    . THR   B 1 146 ? 29.504 -20.538 -5.406  1.00 13.99 ?  146 THR   B O    1 
ATOM   6927 C CB   . THR   B 1 146 ? 30.146 -22.817 -3.131  1.00 14.39 ?  146 THR   B CB   1 
ATOM   6928 O OG1  . THR   B 1 146 ? 29.554 -23.794 -2.267  1.00 14.47 ?  146 THR   B OG1  1 
ATOM   6929 C CG2  . THR   B 1 146 ? 30.213 -21.470 -2.410  1.00 14.73 ?  146 THR   B CG2  1 
ATOM   6930 H H    . THR   B 1 146 ? 29.908 -24.358 -5.315  1.00 17.50 ?  146 THR   B H    1 
ATOM   6931 H HA   . THR   B 1 146 ? 28.449 -22.371 -4.183  1.00 17.04 ?  146 THR   B HA   1 
ATOM   6932 H HB   . THR   B 1 146 ? 31.056 -23.079 -3.348  1.00 17.29 ?  146 THR   B HB   1 
ATOM   6933 H HG1  . THR   B 1 146 ? 29.581 -24.552 -2.640  1.00 17.38 ?  146 THR   B HG1  1 
ATOM   6934 H HG21 . THR   B 1 146 ? 30.583 -21.584 -1.519  1.00 17.70 ?  146 THR   B HG21 1 
ATOM   6935 H HG22 . THR   B 1 146 ? 30.781 -20.850 -2.902  1.00 17.70 ?  146 THR   B HG22 1 
ATOM   6936 H HG23 . THR   B 1 146 ? 29.326 -21.086 -2.333  1.00 17.70 ?  146 THR   B HG23 1 
ATOM   6937 N N    . VAL   B 1 147 ? 31.020 -22.076 -6.040  1.00 12.97 ?  147 VAL   B N    1 
ATOM   6938 C CA   . VAL   B 1 147 ? 31.740 -21.136 -6.885  1.00 12.96 ?  147 VAL   B CA   1 
ATOM   6939 C C    . VAL   B 1 147 ? 31.009 -20.998 -8.209  1.00 13.92 ?  147 VAL   B C    1 
ATOM   6940 O O    . VAL   B 1 147 ? 30.639 -21.999 -8.839  1.00 14.39 ?  147 VAL   B O    1 
ATOM   6941 C CB   . VAL   B 1 147 ? 33.195 -21.588 -7.084  1.00 13.26 ?  147 VAL   B CB   1 
ATOM   6942 C CG1  . VAL   B 1 147 ? 33.960 -20.563 -7.905  1.00 13.40 ?  147 VAL   B CG1  1 
ATOM   6943 C CG2  . VAL   B 1 147 ? 33.874 -21.808 -5.748  1.00 13.35 ?  147 VAL   B CG2  1 
ATOM   6944 H H    . VAL   B 1 147 ? 31.345 -22.875 -6.051  1.00 15.58 ?  147 VAL   B H    1 
ATOM   6945 H HA   . VAL   B 1 147 ? 31.760 -20.265 -6.453  1.00 15.57 ?  147 VAL   B HA   1 
ATOM   6946 H HB   . VAL   B 1 147 ? 33.206 -22.429 -7.572  1.00 15.93 ?  147 VAL   B HB   1 
ATOM   6947 H HG11 . VAL   B 1 147 ? 34.903 -20.786 -7.894  1.00 16.09 ?  147 VAL   B HG11 1 
ATOM   6948 H HG12 . VAL   B 1 147 ? 33.629 -20.571 -8.817  1.00 16.09 ?  147 VAL   B HG12 1 
ATOM   6949 H HG13 . VAL   B 1 147 ? 33.826 -19.684 -7.513  1.00 16.09 ?  147 VAL   B HG13 1 
ATOM   6950 H HG21 . VAL   B 1 147 ? 34.813 -21.994 -5.896  1.00 16.03 ?  147 VAL   B HG21 1 
ATOM   6951 H HG22 . VAL   B 1 147 ? 33.773 -21.008 -5.211  1.00 16.03 ?  147 VAL   B HG22 1 
ATOM   6952 H HG23 . VAL   B 1 147 ? 33.453 -22.561 -5.303  1.00 16.03 ?  147 VAL   B HG23 1 
ATOM   6953 N N    . ARG   B 1 148 ? 30.811 -19.747 -8.634  1.00 13.30 ?  148 ARG   B N    1 
ATOM   6954 C CA   . ARG   B 1 148 ? 30.189 -19.431 -9.910  1.00 13.51 ?  148 ARG   B CA   1 
ATOM   6955 C C    . ARG   B 1 148 ? 31.147 -18.761 -10.884 1.00 13.78 ?  148 ARG   B C    1 
ATOM   6956 O O    . ARG   B 1 148 ? 30.857 -18.734 -12.085 1.00 15.64 ?  148 ARG   B O    1 
ATOM   6957 C CB   . ARG   B 1 148 ? 28.951 -18.544 -9.699  1.00 14.42 ?  148 ARG   B CB   1 
ATOM   6958 C CG   . ARG   B 1 148 ? 27.881 -19.246 -8.880  1.00 15.39 ?  148 ARG   B CG   1 
ATOM   6959 C CD   . ARG   B 1 148 ? 26.668 -18.362 -8.576  1.00 16.77 ?  148 ARG   B CD   1 
ATOM   6960 N NE   . ARG   B 1 148 ? 27.046 -17.162 -7.842  1.00 16.69 ?  148 ARG   B NE   1 
ATOM   6961 C CZ   . ARG   B 1 148 ? 27.352 -17.125 -6.550  1.00 15.61 ?  148 ARG   B CZ   1 
ATOM   6962 N NH1  . ARG   B 1 148 ? 27.283 -18.208 -5.788  1.00 15.51 ?  148 ARG   B NH1  1 
ATOM   6963 N NH2  . ARG   B 1 148 ? 27.747 -15.972 -6.012  1.00 15.12 ?  148 ARG   B NH2  1 
ATOM   6964 H H    . ARG   B 1 148 ? 31.043 -19.042 -8.185  1.00 15.98 ?  148 ARG   B H    1 
ATOM   6965 H HA   . ARG   B 1 148 ? 29.895 -20.255 -10.319 1.00 16.23 ?  148 ARG   B HA   1 
ATOM   6966 H HB2  . ARG   B 1 148 ? 29.211 -17.739 -9.230  1.00 17.33 ?  148 ARG   B HB2  1 
ATOM   6967 H HB3  . ARG   B 1 148 ? 28.572 -18.322 -10.565 1.00 17.33 ?  148 ARG   B HB3  1 
ATOM   6968 H HG2  . ARG   B 1 148 ? 27.571 -20.027 -9.375  1.00 18.49 ?  148 ARG   B HG2  1 
ATOM   6969 H HG3  . ARG   B 1 148 ? 28.269 -19.532 -8.037  1.00 18.49 ?  148 ARG   B HG3  1 
ATOM   6970 H HD2  . ARG   B 1 148 ? 26.258 -18.096 -9.410  1.00 20.14 ?  148 ARG   B HD2  1 
ATOM   6971 H HD3  . ARG   B 1 148 ? 26.040 -18.869 -8.037  1.00 20.14 ?  148 ARG   B HD3  1 
ATOM   6972 H HE   . ARG   B 1 148 ? 27.071 -16.424 -8.277  1.00 20.05 ?  148 ARG   B HE   1 
ATOM   6973 H HH11 . ARG   B 1 148 ? 27.033 -18.961 -6.122  1.00 18.63 ?  148 ARG   B HH11 1 
ATOM   6974 H HH12 . ARG   B 1 148 ? 27.485 -18.160 -4.951  1.00 18.63 ?  148 ARG   B HH12 1 
ATOM   6975 H HH21 . ARG   B 1 148 ? 27.792 -15.266 -6.500  1.00 18.16 ?  148 ARG   B HH21 1 
ATOM   6976 H HH22 . ARG   B 1 148 ? 27.943 -15.932 -5.177  1.00 18.16 ?  148 ARG   B HH22 1 
ATOM   6977 N N    . THR   B 1 149 ? 32.262 -18.217 -10.398 1.00 13.56 ?  149 THR   B N    1 
ATOM   6978 C CA   . THR   B 1 149 ? 33.299 -17.648 -11.245 1.00 13.40 ?  149 THR   B CA   1 
ATOM   6979 C C    . THR   B 1 149 ? 34.186 -18.787 -11.751 1.00 12.77 ?  149 THR   B C    1 
ATOM   6980 O O    . THR   B 1 149 ? 33.978 -19.959 -11.424 1.00 13.41 ?  149 THR   B O    1 
ATOM   6981 C CB   . THR   B 1 149 ? 34.059 -16.590 -10.458 1.00 13.69 ?  149 THR   B CB   1 
ATOM   6982 O OG1  . THR   B 1 149 ? 34.532 -17.200 -9.256  1.00 13.50 ?  149 THR   B OG1  1 
ATOM   6983 C CG2  . THR   B 1 149 ? 33.156 -15.403 -10.133 1.00 14.23 ?  149 THR   B CG2  1 
ATOM   6984 H H    . THR   B 1 149 ? 32.434 -18.155 -9.555  1.00 16.28 ?  149 THR   B H    1 
ATOM   6985 H HA   . THR   B 1 149 ? 32.879 -17.216 -12.010 1.00 16.10 ?  149 THR   B HA   1 
ATOM   6986 H HB   . THR   B 1 149 ? 34.810 -16.283 -10.980 1.00 16.45 ?  149 THR   B HB   1 
ATOM   6987 H HG1  . THR   B 1 149 ? 34.956 -16.635 -8.791  1.00 16.22 ?  149 THR   B HG1  1 
ATOM   6988 H HG21 . THR   B 1 149 ? 33.661 -14.729 -9.649  1.00 17.09 ?  149 THR   B HG21 1 
ATOM   6989 H HG22 . THR   B 1 149 ? 32.813 -15.014 -10.951 1.00 17.09 ?  149 THR   B HG22 1 
ATOM   6990 H HG23 . THR   B 1 149 ? 32.410 -15.690 -9.582  1.00 17.09 ?  149 THR   B HG23 1 
ATOM   6991 N N    . ASN   B 1 150 ? 35.149 -18.464 -12.603 1.00 12.74 ?  150 ASN   B N    1 
ATOM   6992 C CA   . ASN   B 1 150 ? 35.915 -19.491 -13.299 1.00 13.37 ?  150 ASN   B CA   1 
ATOM   6993 C C    . ASN   B 1 150 ? 37.075 -19.950 -12.428 1.00 12.81 ?  150 ASN   B C    1 
ATOM   6994 O O    . ASN   B 1 150 ? 38.013 -19.193 -12.175 1.00 13.61 ?  150 ASN   B O    1 
ATOM   6995 C CB   . ASN   B 1 150 ? 36.385 -18.975 -14.649 1.00 15.29 ?  150 ASN   B CB   1 
ATOM   6996 C CG   . ASN   B 1 150 ? 35.242 -18.752 -15.596 1.00 18.16 ?  150 ASN   B CG   1 
ATOM   6997 O OD1  . ASN   B 1 150 ? 34.328 -19.564 -15.674 1.00 19.34 ?  150 ASN   B OD1  1 
ATOM   6998 N ND2  . ASN   B 1 150 ? 35.271 -17.644 -16.306 1.00 20.85 ?  150 ASN   B ND2  1 
ATOM   6999 H H    . ASN   B 1 150 ? 35.384 -17.656 -12.780 1.00 15.30 ?  150 ASN   B H    1 
ATOM   7000 H HA   . ASN   B 1 150 ? 35.332 -20.256 -13.453 1.00 16.06 ?  150 ASN   B HA   1 
ATOM   7001 H HB2  . ASN   B 1 150 ? 36.838 -18.126 -14.519 1.00 18.37 ?  150 ASN   B HB2  1 
ATOM   7002 H HB3  . ASN   B 1 150 ? 36.990 -19.622 -15.037 1.00 18.37 ?  150 ASN   B HB3  1 
ATOM   7003 H HD21 . ASN   B 1 150 ? 34.639 -17.473 -16.868 1.00 25.04 ?  150 ASN   B HD21 1 
ATOM   7004 H HD22 . ASN   B 1 150 ? 35.922 -17.089 -16.216 1.00 25.04 ?  150 ASN   B HD22 1 
ATOM   7005 N N    . VAL   B 1 151 ? 37.022 -21.192 -11.967 1.00 12.93 ?  151 VAL   B N    1 
ATOM   7006 C CA   . VAL   B 1 151 ? 38.034 -21.730 -11.073 1.00 12.75 ?  151 VAL   B CA   1 
ATOM   7007 C C    . VAL   B 1 151 ? 38.736 -22.900 -11.748 1.00 12.43 ?  151 VAL   B C    1 
ATOM   7008 O O    . VAL   B 1 151 ? 38.093 -23.831 -12.251 1.00 13.95 ?  151 VAL   B O    1 
ATOM   7009 C CB   . VAL   B 1 151 ? 37.482 -22.070 -9.672  1.00 14.00 ?  151 VAL   B CB   1 
ATOM   7010 C CG1  . VAL   B 1 151 ? 36.321 -23.060 -9.725  1.00 15.74 ?  151 VAL   B CG1  1 
ATOM   7011 C CG2  . VAL   B 1 151 ? 38.607 -22.574 -8.781  1.00 13.95 ?  151 VAL   B CG2  1 
ATOM   7012 H H    . VAL   B 1 151 ? 36.392 -21.753 -12.156 1.00 15.53 ?  151 VAL   B H    1 
ATOM   7013 H HA   . VAL   B 1 151 ? 38.703 -21.038 -10.938 1.00 15.32 ?  151 VAL   B HA   1 
ATOM   7014 H HB   . VAL   B 1 151 ? 37.148 -21.252 -9.266  1.00 16.82 ?  151 VAL   B HB   1 
ATOM   7015 H HG11 . VAL   B 1 151 ? 36.017 -23.240 -8.820  1.00 18.90 ?  151 VAL   B HG11 1 
ATOM   7016 H HG12 . VAL   B 1 151 ? 35.600 -22.670 -10.243 1.00 18.90 ?  151 VAL   B HG12 1 
ATOM   7017 H HG13 . VAL   B 1 151 ? 36.625 -23.880 -10.141 1.00 18.90 ?  151 VAL   B HG13 1 
ATOM   7018 H HG21 . VAL   B 1 151 ? 38.285 -22.630 -7.864  1.00 16.75 ?  151 VAL   B HG21 1 
ATOM   7019 H HG22 . VAL   B 1 151 ? 38.887 -23.452 -9.082  1.00 16.75 ?  151 VAL   B HG22 1 
ATOM   7020 H HG23 . VAL   B 1 151 ? 39.353 -21.954 -8.824  1.00 16.75 ?  151 VAL   B HG23 1 
ATOM   7021 N N    . TYR   B 1 152 ? 40.070 -22.823 -11.757 1.00 11.98 ?  152 TYR   B N    1 
ATOM   7022 C CA   . TYR   B 1 152 ? 40.971 -23.810 -12.335 1.00 12.21 ?  152 TYR   B CA   1 
ATOM   7023 C C    . TYR   B 1 152 ? 41.690 -24.490 -11.174 1.00 11.38 ?  152 TYR   B C    1 
ATOM   7024 O O    . TYR   B 1 152 ? 42.538 -23.875 -10.516 1.00 12.02 ?  152 TYR   B O    1 
ATOM   7025 C CB   . TYR   B 1 152 ? 41.937 -23.119 -13.301 1.00 13.25 ?  152 TYR   B CB   1 
ATOM   7026 C CG   . TYR   B 1 152 ? 41.251 -22.653 -14.565 1.00 14.11 ?  152 TYR   B CG   1 
ATOM   7027 C CD1  . TYR   B 1 152 ? 40.614 -21.418 -14.633 1.00 14.50 ?  152 TYR   B CD1  1 
ATOM   7028 C CD2  . TYR   B 1 152 ? 41.224 -23.460 -15.690 1.00 15.17 ?  152 TYR   B CD2  1 
ATOM   7029 C CE1  . TYR   B 1 152 ? 39.970 -21.004 -15.784 1.00 16.13 ?  152 TYR   B CE1  1 
ATOM   7030 C CE2  . TYR   B 1 152 ? 40.575 -23.062 -16.842 1.00 16.61 ?  152 TYR   B CE2  1 
ATOM   7031 C CZ   . TYR   B 1 152 ? 39.957 -21.828 -16.889 1.00 16.65 ?  152 TYR   B CZ   1 
ATOM   7032 O OH   . TYR   B 1 152 ? 39.315 -21.430 -18.041 1.00 19.32 ?  152 TYR   B OH   1 
ATOM   7033 H H    . TYR   B 1 152 ? 40.499 -22.156 -11.407 1.00 14.39 ?  152 TYR   B H    1 
ATOM   7034 H HA   . TYR   B 1 152 ? 40.452 -24.474 -12.820 1.00 14.67 ?  152 TYR   B HA   1 
ATOM   7035 H HB2  . TYR   B 1 152 ? 42.319 -22.344 -12.860 1.00 15.92 ?  152 TYR   B HB2  1 
ATOM   7036 H HB3  . TYR   B 1 152 ? 42.637 -23.743 -13.544 1.00 15.92 ?  152 TYR   B HB3  1 
ATOM   7037 H HD1  . TYR   B 1 152 ? 40.619 -20.863 -13.885 1.00 17.42 ?  152 TYR   B HD1  1 
ATOM   7038 H HD2  . TYR   B 1 152 ? 41.631 -24.301 -15.665 1.00 18.22 ?  152 TYR   B HD2  1 
ATOM   7039 H HE1  . TYR   B 1 152 ? 39.551 -20.174 -15.815 1.00 19.37 ?  152 TYR   B HE1  1 
ATOM   7040 H HE2  . TYR   B 1 152 ? 40.566 -23.617 -17.593 1.00 19.95 ?  152 TYR   B HE2  1 
ATOM   7041 H HH   . TYR   B 1 152 ? 38.984 -20.660 -17.921 1.00 23.20 ?  152 TYR   B HH   1 
ATOM   7042 N N    . LEU   B 1 153 ? 41.307 -25.734 -10.891 1.00 11.80 ?  153 LEU   B N    1 
ATOM   7043 C CA   . LEU   B 1 153 ? 41.812 -26.478 -9.746  1.00 11.57 ?  153 LEU   B CA   1 
ATOM   7044 C C    . LEU   B 1 153 ? 43.040 -27.285 -10.136 1.00 11.92 ?  153 LEU   B C    1 
ATOM   7045 O O    . LEU   B 1 153 ? 43.020 -28.007 -11.132 1.00 13.29 ?  153 LEU   B O    1 
ATOM   7046 C CB   . LEU   B 1 153 ? 40.735 -27.439 -9.236  1.00 11.92 ?  153 LEU   B CB   1 
ATOM   7047 C CG   . LEU   B 1 153 ? 39.483 -26.790 -8.642  1.00 12.79 ?  153 LEU   B CG   1 
ATOM   7048 C CD1  . LEU   B 1 153 ? 38.393 -27.828 -8.472  1.00 13.97 ?  153 LEU   B CD1  1 
ATOM   7049 C CD2  . LEU   B 1 153 ? 39.794 -26.104 -7.311  1.00 13.06 ?  153 LEU   B CD2  1 
ATOM   7050 H H    . LEU   B 1 153 ? 40.738 -26.183 -11.365 1.00 14.18 ?  153 LEU   B H    1 
ATOM   7051 H HA   . LEU   B 1 153 ? 42.039 -25.861 -9.037  1.00 13.90 ?  153 LEU   B HA   1 
ATOM   7052 H HB2  . LEU   B 1 153 ? 40.447 -27.998 -9.970  1.00 14.32 ?  153 LEU   B HB2  1 
ATOM   7053 H HB3  . LEU   B 1 153 ? 41.127 -27.993 -8.540  1.00 14.32 ?  153 LEU   B HB3  1 
ATOM   7054 H HG   . LEU   B 1 153 ? 39.156 -26.107 -9.252  1.00 15.37 ?  153 LEU   B HG   1 
ATOM   7055 H HD11 . LEU   B 1 153 ? 37.593 -27.390 -8.139  1.00 16.78 ?  153 LEU   B HD11 1 
ATOM   7056 H HD12 . LEU   B 1 153 ? 38.219 -28.236 -9.328  1.00 16.78 ?  153 LEU   B HD12 1 
ATOM   7057 H HD13 . LEU   B 1 153 ? 38.697 -28.492 -7.835  1.00 16.78 ?  153 LEU   B HD13 1 
ATOM   7058 H HD21 . LEU   B 1 153 ? 38.980 -25.746 -6.934  1.00 15.69 ?  153 LEU   B HD21 1 
ATOM   7059 H HD22 . LEU   B 1 153 ? 40.184 -26.757 -6.705  1.00 15.69 ?  153 LEU   B HD22 1 
ATOM   7060 H HD23 . LEU   B 1 153 ? 40.433 -25.385 -7.467  1.00 15.69 ?  153 LEU   B HD23 1 
ATOM   7061 N N    . ALA   B 1 154 ? 44.091 -27.184 -9.327  1.00 11.93 ?  154 ALA   B N    1 
ATOM   7062 C CA   . ALA   B 1 154 ? 45.316 -27.948 -9.509  1.00 12.99 ?  154 ALA   B CA   1 
ATOM   7063 C C    . ALA   B 1 154 ? 45.382 -29.017 -8.424  1.00 13.21 ?  154 ALA   B C    1 
ATOM   7064 O O    . ALA   B 1 154 ? 45.315 -28.705 -7.226  1.00 14.67 ?  154 ALA   B O    1 
ATOM   7065 C CB   . ALA   B 1 154 ? 46.538 -27.037 -9.445  1.00 14.26 ?  154 ALA   B CB   1 
ATOM   7066 H H    . ALA   B 1 154 ? 44.105 -26.659 -8.639  1.00 14.34 ?  154 ALA   B H    1 
ATOM   7067 H HA   . ALA   B 1 154 ? 45.299 -28.380 -10.372 1.00 15.61 ?  154 ALA   B HA   1 
ATOM   7068 H HB1  . ALA   B 1 154 ? 47.339 -27.571 -9.570  1.00 17.13 ?  154 ALA   B HB1  1 
ATOM   7069 H HB2  . ALA   B 1 154 ? 46.478 -26.368 -10.148 1.00 17.13 ?  154 ALA   B HB2  1 
ATOM   7070 H HB3  . ALA   B 1 154 ? 46.569 -26.598 -8.579  1.00 17.13 ?  154 ALA   B HB3  1 
ATOM   7071 N N    . VAL   B 1 155 ? 45.494 -30.273 -8.846  1.00 13.39 ?  155 VAL   B N    1 
ATOM   7072 C CA   . VAL   B 1 155 ? 45.596 -31.416 -7.948  1.00 14.21 ?  155 VAL   B CA   1 
ATOM   7073 C C    . VAL   B 1 155 ? 46.929 -32.097 -8.226  1.00 13.59 ?  155 VAL   B C    1 
ATOM   7074 O O    . VAL   B 1 155 ? 47.161 -32.599 -9.335  1.00 15.36 ?  155 VAL   B O    1 
ATOM   7075 C CB   . VAL   B 1 155 ? 44.434 -32.403 -8.150  1.00 15.50 ?  155 VAL   B CB   1 
ATOM   7076 C CG1  . VAL   B 1 155 ? 44.606 -33.587 -7.225  1.00 16.28 ?  155 VAL   B CG1  1 
ATOM   7077 C CG2  . VAL   B 1 155 ? 43.101 -31.705 -7.923  1.00 16.87 ?  155 VAL   B CG2  1 
ATOM   7078 H H    . VAL   B 1 155 ? 45.523 -30.491 -9.679  1.00 16.09 ?  155 VAL   B H    1 
ATOM   7079 H HA   . VAL   B 1 155 ? 45.587 -31.111 -7.028  1.00 17.07 ?  155 VAL   B HA   1 
ATOM   7080 H HB   . VAL   B 1 155 ? 44.452 -32.727 -9.064  1.00 18.62 ?  155 VAL   B HB   1 
ATOM   7081 H HG11 . VAL   B 1 155 ? 43.770 -34.084 -7.188  1.00 19.55 ?  155 VAL   B HG11 1 
ATOM   7082 H HG12 . VAL   B 1 155 ? 45.311 -34.163 -7.563  1.00 19.55 ?  155 VAL   B HG12 1 
ATOM   7083 H HG13 . VAL   B 1 155 ? 44.835 -33.270 -6.337  1.00 19.55 ?  155 VAL   B HG13 1 
ATOM   7084 H HG21 . VAL   B 1 155 ? 42.388 -32.360 -8.003  1.00 20.26 ?  155 VAL   B HG21 1 
ATOM   7085 H HG22 . VAL   B 1 155 ? 43.094 -31.318 -7.036  1.00 20.26 ?  155 VAL   B HG22 1 
ATOM   7086 H HG23 . VAL   B 1 155 ? 42.988 -31.012 -8.591  1.00 20.26 ?  155 VAL   B HG23 1 
ATOM   7087 N N    . PHE   B 1 156 ? 47.793 -32.140 -7.213  1.00 14.14 ?  156 PHE   B N    1 
ATOM   7088 C CA   . PHE   B 1 156 ? 49.169 -32.594 -7.417  1.00 15.00 ?  156 PHE   B CA   1 
ATOM   7089 C C    . PHE   B 1 156 ? 49.260 -34.094 -7.697  1.00 16.69 ?  156 PHE   B C    1 
ATOM   7090 O O    . PHE   B 1 156 ? 49.975 -34.525 -8.613  1.00 18.78 ?  156 PHE   B O    1 
ATOM   7091 C CB   . PHE   B 1 156 ? 50.005 -32.234 -6.193  1.00 14.56 ?  156 PHE   B CB   1 
ATOM   7092 C CG   . PHE   B 1 156 ? 51.429 -32.692 -6.270  1.00 15.62 ?  156 PHE   B CG   1 
ATOM   7093 C CD1  . PHE   B 1 156 ? 52.299 -32.146 -7.199  1.00 17.08 ?  156 PHE   B CD1  1 
ATOM   7094 C CD2  . PHE   B 1 156 ? 51.903 -33.659 -5.407  1.00 15.99 ?  156 PHE   B CD2  1 
ATOM   7095 C CE1  . PHE   B 1 156 ? 53.616 -32.561 -7.267  1.00 18.28 ?  156 PHE   B CE1  1 
ATOM   7096 C CE2  . PHE   B 1 156 ? 53.222 -34.078 -5.474  1.00 17.75 ?  156 PHE   B CE2  1 
ATOM   7097 C CZ   . PHE   B 1 156 ? 54.070 -33.526 -6.410  1.00 18.17 ?  156 PHE   B CZ   1 
ATOM   7098 H H    . PHE   B 1 156 ? 47.608 -31.917 -6.400  1.00 16.99 ?  156 PHE   B H    1 
ATOM   7099 H HA   . PHE   B 1 156 ? 49.537 -32.128 -8.178  1.00 18.02 ?  156 PHE   B HA   1 
ATOM   7100 H HB2  . PHE   B 1 156 ? 50.005 -31.271 -6.095  1.00 17.49 ?  156 PHE   B HB2  1 
ATOM   7101 H HB3  . PHE   B 1 156 ? 49.607 -32.645 -5.410  1.00 17.49 ?  156 PHE   B HB3  1 
ATOM   7102 H HD1  . PHE   B 1 156 ? 51.993 -31.483 -7.789  1.00 20.51 ?  156 PHE   B HD1  1 
ATOM   7103 H HD2  . PHE   B 1 156 ? 51.330 -34.037 -4.780  1.00 19.20 ?  156 PHE   B HD2  1 
ATOM   7104 H HE1  . PHE   B 1 156 ? 54.194 -32.185 -7.899  1.00 21.95 ?  156 PHE   B HE1  1 
ATOM   7105 H HE2  . PHE   B 1 156 ? 53.533 -34.736 -4.893  1.00 21.31 ?  156 PHE   B HE2  1 
ATOM   7106 H HZ   . PHE   B 1 156 ? 54.959 -33.805 -6.454  1.00 21.83 ?  156 PHE   B HZ   1 
ATOM   7107 N N    . ASP   B 1 157 ? 48.600 -34.909 -6.888  1.00 17.38 ?  157 ASP   B N    1 
ATOM   7108 C CA   . ASP   B 1 157 ? 48.732 -36.360 -6.991  1.00 19.03 ?  157 ASP   B CA   1 
ATOM   7109 C C    . ASP   B 1 157 ? 47.815 -36.906 -8.083  1.00 19.22 ?  157 ASP   B C    1 
ATOM   7110 O O    . ASP   B 1 157 ? 46.592 -36.788 -7.975  1.00 18.24 ?  157 ASP   B O    1 
ATOM   7111 C CB   . ASP   B 1 157 ? 48.357 -36.966 -5.646  1.00 21.22 ?  157 ASP   B CB   1 
ATOM   7112 C CG   . ASP   B 1 157 ? 48.487 -38.473 -5.617  1.00 23.39 ?  157 ASP   B CG   1 
ATOM   7113 O OD1  . ASP   B 1 157 ? 48.837 -39.087 -6.654  1.00 23.99 ?  157 ASP   B OD1  1 
ATOM   7114 O OD2  . ASP   B 1 157 ? 48.246 -39.038 -4.534  1.00 25.26 -1 157 ASP   B OD2  1 
ATOM   7115 H H    . ASP   B 1 157 ? 48.068 -34.649 -6.270  1.00 20.87 ?  157 ASP   B H    1 
ATOM   7116 H HA   . ASP   B 1 157 ? 49.652 -36.595 -7.205  1.00 22.85 ?  157 ASP   B HA   1 
ATOM   7117 H HB2  . ASP   B 1 157 ? 48.932 -36.589 -4.964  1.00 25.49 ?  157 ASP   B HB2  1 
ATOM   7118 H HB3  . ASP   B 1 157 ? 47.434 -36.750 -5.457  1.00 25.49 ?  157 ASP   B HB3  1 
ATOM   7119 N N    . LYS   B 1 158 ? 48.406 -37.527 -9.114  1.00 20.42 ?  158 LYS   B N    1 
ATOM   7120 C CA   . LYS   B 1 158 ? 47.628 -38.150 -10.190 1.00 21.61 ?  158 LYS   B CA   1 
ATOM   7121 C C    . LYS   B 1 158 ? 46.566 -39.109 -9.650  1.00 21.35 ?  158 LYS   B C    1 
ATOM   7122 O O    . LYS   B 1 158 ? 45.455 -39.191 -10.190 1.00 21.52 ?  158 LYS   B O    1 
ATOM   7123 C CB   . LYS   B 1 158 ? 48.585 -38.879 -11.147 1.00 23.57 ?  158 LYS   B CB   1 
ATOM   7124 C CG   . LYS   B 1 158 ? 47.912 -39.759 -12.191 1.00 25.91 ?  158 LYS   B CG   1 
ATOM   7125 C CD   . LYS   B 1 158 ? 47.060 -38.957 -13.153 1.00 28.61 ?  158 LYS   B CD   1 
ATOM   7126 C CE   . LYS   B 1 158 ? 46.426 -39.866 -14.198 1.00 30.50 ?  158 LYS   B CE   1 
ATOM   7127 N NZ   . LYS   B 1 158 ? 45.367 -39.174 -14.985 1.00 31.22 ?  158 LYS   B NZ   1 
ATOM   7128 H H    . LYS   B 1 158 ? 49.264 -37.602 -9.213  1.00 24.52 ?  158 LYS   B H    1 
ATOM   7129 H HA   . LYS   B 1 158 ? 47.188 -37.452 -10.704 1.00 25.94 ?  158 LYS   B HA   1 
ATOM   7130 H HB2  . LYS   B 1 158 ? 49.117 -38.219 -11.628 1.00 28.31 ?  158 LYS   B HB2  1 
ATOM   7131 H HB3  . LYS   B 1 158 ? 49.175 -39.445 -10.626 1.00 28.31 ?  158 LYS   B HB3  1 
ATOM   7132 H HG2  . LYS   B 1 158 ? 48.599 -40.210 -12.710 1.00 31.10 ?  158 LYS   B HG2  1 
ATOM   7133 H HG3  . LYS   B 1 158 ? 47.350 -40.417 -11.755 1.00 31.10 ?  158 LYS   B HG3  1 
ATOM   7134 H HD2  . LYS   B 1 158 ? 46.351 -38.512 -12.664 1.00 34.35 ?  158 LYS   B HD2  1 
ATOM   7135 H HD3  . LYS   B 1 158 ? 47.615 -38.306 -13.612 1.00 34.35 ?  158 LYS   B HD3  1 
ATOM   7136 H HE2  . LYS   B 1 158 ? 47.110 -40.168 -14.815 1.00 36.62 ?  158 LYS   B HE2  1 
ATOM   7137 H HE3  . LYS   B 1 158 ? 46.021 -40.628 -13.753 1.00 36.62 ?  158 LYS   B HE3  1 
ATOM   7138 H HZ1  . LYS   B 1 158 ? 45.018 -39.731 -15.584 1.00 37.48 ?  158 LYS   B HZ1  1 
ATOM   7139 H HZ2  . LYS   B 1 158 ? 44.721 -38.890 -14.442 1.00 37.48 ?  158 LYS   B HZ2  1 
ATOM   7140 H HZ3  . LYS   B 1 158 ? 45.715 -38.473 -15.410 1.00 37.48 ?  158 LYS   B HZ3  1 
ATOM   7141 N N    . ASN   B 1 159 ? 46.888 -39.858 -8.596  1.00 21.78 ?  159 ASN   B N    1 
ATOM   7142 C CA   . ASN   B 1 159 ? 45.929 -40.833 -8.083  1.00 22.52 ?  159 ASN   B CA   1 
ATOM   7143 C C    . ASN   B 1 159 ? 44.736 -40.153 -7.406  1.00 20.67 ?  159 ASN   B C    1 
ATOM   7144 O O    . ASN   B 1 159 ? 43.603 -40.646 -7.495  1.00 21.05 ?  159 ASN   B O    1 
ATOM   7145 C CB   . ASN   B 1 159 ? 46.632 -41.803 -7.140  1.00 24.82 ?  159 ASN   B CB   1 
ATOM   7146 C CG   . ASN   B 1 159 ? 47.635 -42.675 -7.856  1.00 27.02 ?  159 ASN   B CG   1 
ATOM   7147 O OD1  . ASN   B 1 159 ? 47.374 -43.161 -8.962  1.00 28.52 ?  159 ASN   B OD1  1 
ATOM   7148 N ND2  . ASN   B 1 159 ? 48.797 -42.874 -7.237  1.00 28.23 ?  159 ASN   B ND2  1 
ATOM   7149 H H    . ASN   B 1 159 ? 47.634 -39.807 -8.177  1.00 26.16 ?  159 ASN   B H    1 
ATOM   7150 H HA   . ASN   B 1 159 ? 45.595 -41.342 -8.839  1.00 27.04 ?  159 ASN   B HA   1 
ATOM   7151 H HB2  . ASN   B 1 159 ? 47.098 -41.297 -6.458  1.00 29.81 ?  159 ASN   B HB2  1 
ATOM   7152 H HB3  . ASN   B 1 159 ? 45.968 -42.378 -6.742  1.00 29.81 ?  159 ASN   B HB3  1 
ATOM   7153 H HD21 . ASN   B 1 159 ? 49.409 -43.362 -7.601  1.00 33.90 ?  159 ASN   B HD21 1 
ATOM   7154 H HD22 . ASN   B 1 159 ? 48.942 -42.523 -6.462  1.00 33.90 ?  159 ASN   B HD22 1 
ATOM   7155 N N    . LEU   B 1 160 ? 44.959 -39.026 -6.725  1.00 19.92 ?  160 LEU   B N    1 
ATOM   7156 C CA   . LEU   B 1 160 ? 43.832 -38.287 -6.171  1.00 18.61 ?  160 LEU   B CA   1 
ATOM   7157 C C    . LEU   B 1 160 ? 43.037 -37.621 -7.279  1.00 17.24 ?  160 LEU   B C    1 
ATOM   7158 O O    . LEU   B 1 160 ? 41.801 -37.614 -7.240  1.00 16.68 ?  160 LEU   B O    1 
ATOM   7159 C CB   . LEU   B 1 160 ? 44.306 -37.249 -5.158  1.00 18.48 ?  160 LEU   B CB   1 
ATOM   7160 C CG   . LEU   B 1 160 ? 43.178 -36.344 -4.639  1.00 17.84 ?  160 LEU   B CG   1 
ATOM   7161 C CD1  . LEU   B 1 160 ? 42.067 -37.176 -3.999  1.00 19.12 ?  160 LEU   B CD1  1 
ATOM   7162 C CD2  . LEU   B 1 160 ? 43.733 -35.306 -3.667  1.00 17.42 ?  160 LEU   B CD2  1 
ATOM   7163 H H    . LEU   B 1 160 ? 45.731 -38.682 -6.582  1.00 23.92 ?  160 LEU   B H    1 
ATOM   7164 H HA   . LEU   B 1 160 ? 43.244 -38.911 -5.725  1.00 22.35 ?  160 LEU   B HA   1 
ATOM   7165 H HB2  . LEU   B 1 160 ? 44.695 -37.715 -4.401  1.00 22.19 ?  160 LEU   B HB2  1 
ATOM   7166 H HB3  . LEU   B 1 160 ? 44.979 -36.688 -5.579  1.00 22.19 ?  160 LEU   B HB3  1 
ATOM   7167 H HG   . LEU   B 1 160 ? 42.795 -35.863 -5.389  1.00 21.43 ?  160 LEU   B HG   1 
ATOM   7168 H HD11 . LEU   B 1 160 ? 41.449 -36.577 -3.557  1.00 22.96 ?  160 LEU   B HD11 1 
ATOM   7169 H HD12 . LEU   B 1 160 ? 41.606 -37.677 -4.691  1.00 22.96 ?  160 LEU   B HD12 1 
ATOM   7170 H HD13 . LEU   B 1 160 ? 42.461 -37.784 -3.355  1.00 22.96 ?  160 LEU   B HD13 1 
ATOM   7171 H HD21 . LEU   B 1 160 ? 43.011 -34.726 -3.387  1.00 20.92 ?  160 LEU   B HD21 1 
ATOM   7172 H HD22 . LEU   B 1 160 ? 44.114 -35.761 -2.903  1.00 20.92 ?  160 LEU   B HD22 1 
ATOM   7173 H HD23 . LEU   B 1 160 ? 44.419 -34.786 -4.121  1.00 20.92 ?  160 LEU   B HD23 1 
ATOM   7174 N N    . TYR   B 1 161 ? 43.730 -37.054 -8.273  1.00 17.89 ?  161 TYR   B N    1 
ATOM   7175 C CA   . TYR   B 1 161 ? 43.056 -36.491 -9.437  1.00 18.10 ?  161 TYR   B CA   1 
ATOM   7176 C C    . TYR   B 1 161 ? 42.103 -37.507 -10.049 1.00 17.36 ?  161 TYR   B C    1 
ATOM   7177 O O    . TYR   B 1 161 ? 40.932 -37.203 -10.299 1.00 17.20 ?  161 TYR   B O    1 
ATOM   7178 C CB   . TYR   B 1 161 ? 44.098 -36.029 -10.466 1.00 18.64 ?  161 TYR   B CB   1 
ATOM   7179 C CG   . TYR   B 1 161 ? 43.518 -35.557 -11.780 1.00 19.61 ?  161 TYR   B CG   1 
ATOM   7180 C CD1  . TYR   B 1 161 ? 43.140 -34.230 -11.949 1.00 19.98 ?  161 TYR   B CD1  1 
ATOM   7181 C CD2  . TYR   B 1 161 ? 43.337 -36.434 -12.849 1.00 20.26 ?  161 TYR   B CD2  1 
ATOM   7182 C CE1  . TYR   B 1 161 ? 42.606 -33.785 -13.138 1.00 20.42 ?  161 TYR   B CE1  1 
ATOM   7183 C CE2  . TYR   B 1 161 ? 42.797 -36.001 -14.044 1.00 21.30 ?  161 TYR   B CE2  1 
ATOM   7184 C CZ   . TYR   B 1 161 ? 42.438 -34.673 -14.185 1.00 21.09 ?  161 TYR   B CZ   1 
ATOM   7185 O OH   . TYR   B 1 161 ? 41.897 -34.229 -15.368 1.00 23.18 ?  161 TYR   B OH   1 
ATOM   7186 H H    . TYR   B 1 161 ? 44.587 -36.994 -8.302  1.00 21.48 ?  161 TYR   B H    1 
ATOM   7187 H HA   . TYR   B 1 161 ? 42.539 -35.718 -9.168  1.00 21.74 ?  161 TYR   B HA   1 
ATOM   7188 H HB2  . TYR   B 1 161 ? 44.603 -35.291 -10.093 1.00 22.39 ?  161 TYR   B HB2  1 
ATOM   7189 H HB3  . TYR   B 1 161 ? 44.695 -36.767 -10.664 1.00 22.39 ?  161 TYR   B HB3  1 
ATOM   7190 H HD1  . TYR   B 1 161 ? 43.257 -33.627 -11.250 1.00 24.00 ?  161 TYR   B HD1  1 
ATOM   7191 H HD2  . TYR   B 1 161 ? 43.575 -37.329 -12.762 1.00 24.33 ?  161 TYR   B HD2  1 
ATOM   7192 H HE1  . TYR   B 1 161 ? 42.360 -32.889 -13.233 1.00 24.53 ?  161 TYR   B HE1  1 
ATOM   7193 H HE2  . TYR   B 1 161 ? 42.677 -36.596 -14.752 1.00 25.57 ?  161 TYR   B HE2  1 
ATOM   7194 H HH   . TYR   B 1 161 ? 41.845 -34.864 -15.918 1.00 27.83 ?  161 TYR   B HH   1 
ATOM   7195 N N    . ASP   B 1 162 ? 42.591 -38.731 -10.276 1.00 18.03 ?  162 ASP   B N    1 
ATOM   7196 C CA   . ASP   B 1 162 ? 41.758 -39.760 -10.888 1.00 18.55 ?  162 ASP   B CA   1 
ATOM   7197 C C    . ASP   B 1 162 ? 40.556 -40.089 -10.014 1.00 17.81 ?  162 ASP   B C    1 
ATOM   7198 O O    . ASP   B 1 162 ? 39.448 -40.291 -10.523 1.00 18.65 ?  162 ASP   B O    1 
ATOM   7199 C CB   . ASP   B 1 162 ? 42.579 -41.028 -11.151 1.00 20.22 ?  162 ASP   B CB   1 
ATOM   7200 C CG   . ASP   B 1 162 ? 43.584 -40.872 -12.279 1.00 21.67 ?  162 ASP   B CG   1 
ATOM   7201 O OD1  . ASP   B 1 162 ? 43.454 -39.931 -13.089 1.00 22.24 ?  162 ASP   B OD1  1 
ATOM   7202 O OD2  . ASP   B 1 162 ? 44.494 -41.733 -12.374 1.00 23.67 -1 162 ASP   B OD2  1 
ATOM   7203 H H    . ASP   B 1 162 ? 43.396 -38.981 -10.092 1.00 21.65 ?  162 ASP   B H    1 
ATOM   7204 H HA   . ASP   B 1 162 ? 41.430 -39.438 -11.740 1.00 22.28 ?  162 ASP   B HA   1 
ATOM   7205 H HB2  . ASP   B 1 162 ? 43.076 -41.261 -10.355 1.00 24.28 ?  162 ASP   B HB2  1 
ATOM   7206 H HB3  . ASP   B 1 162 ? 41.981 -41.751 -11.396 1.00 24.28 ?  162 ASP   B HB3  1 
ATOM   7207 N N    A LYS   B 1 163 ? 40.757 -40.178 -8.699  0.42 17.43 ?  163 LYS   B N    1 
ATOM   7208 N N    B LYS   B 1 163 ? 40.755 -40.161 -8.697  0.58 16.88 ?  163 LYS   B N    1 
ATOM   7209 C CA   A LYS   B 1 163 ? 39.631 -40.443 -7.811  0.42 18.20 ?  163 LYS   B CA   1 
ATOM   7210 C CA   B LYS   B 1 163 ? 39.640 -40.440 -7.796  0.58 17.63 ?  163 LYS   B CA   1 
ATOM   7211 C C    A LYS   B 1 163 ? 38.602 -39.321 -7.886  0.42 16.80 ?  163 LYS   B C    1 
ATOM   7212 C C    B LYS   B 1 163 ? 38.607 -39.319 -7.830  0.58 16.45 ?  163 LYS   B C    1 
ATOM   7213 O O    A LYS   B 1 163 ? 37.392 -39.578 -7.926  0.42 17.35 ?  163 LYS   B O    1 
ATOM   7214 O O    B LYS   B 1 163 ? 37.397 -39.576 -7.765  0.58 17.37 ?  163 LYS   B O    1 
ATOM   7215 C CB   A LYS   B 1 163 ? 40.115 -40.628 -6.374  0.42 21.29 ?  163 LYS   B CB   1 
ATOM   7216 C CB   B LYS   B 1 163 ? 40.149 -40.636 -6.371  0.58 20.95 ?  163 LYS   B CB   1 
ATOM   7217 C CG   A LYS   B 1 163 ? 39.051 -41.214 -5.464  0.42 25.18 ?  163 LYS   B CG   1 
ATOM   7218 C CG   B LYS   B 1 163 ? 39.072 -41.093 -5.409  0.58 25.46 ?  163 LYS   B CG   1 
ATOM   7219 C CD   A LYS   B 1 163 ? 39.457 -41.191 -4.004  0.42 28.56 ?  163 LYS   B CD   1 
ATOM   7220 C CD   B LYS   B 1 163 ? 39.600 -41.278 -4.000  0.58 29.74 ?  163 LYS   B CD   1 
ATOM   7221 C CE   A LYS   B 1 163 ? 38.391 -41.859 -3.149  0.42 31.23 ?  163 LYS   B CE   1 
ATOM   7222 C CE   B LYS   B 1 163 ? 38.516 -41.846 -3.095  0.58 32.92 ?  163 LYS   B CE   1 
ATOM   7223 N NZ   A LYS   B 1 163 ? 38.492 -41.474 -1.717  0.42 32.26 ?  163 LYS   B NZ   1 
ATOM   7224 N NZ   B LYS   B 1 163 ? 38.869 -41.747 -1.654  0.58 34.19 ?  163 LYS   B NZ   1 
ATOM   7225 H H    A LYS   B 1 163 ? 41.520 -40.101 -8.309  0.42 20.93 ?  163 LYS   B H    1 
ATOM   7226 H H    B LYS   B 1 163 ? 41.516 -40.064 -8.310  0.58 20.27 ?  163 LYS   B H    1 
ATOM   7227 H HA   A LYS   B 1 163 ? 39.199 -41.267 -8.088  0.42 21.85 ?  163 LYS   B HA   1 
ATOM   7228 H HA   B LYS   B 1 163 ? 39.206 -41.262 -8.076  0.58 21.17 ?  163 LYS   B HA   1 
ATOM   7229 H HB2  A LYS   B 1 163 ? 40.877 -41.231 -6.372  0.42 25.57 ?  163 LYS   B HB2  1 
ATOM   7230 H HB2  B LYS   B 1 163 ? 40.850 -41.308 -6.375  0.58 25.15 ?  163 LYS   B HB2  1 
ATOM   7231 H HB3  A LYS   B 1 163 ? 40.375 -39.766 -6.016  0.42 25.57 ?  163 LYS   B HB3  1 
ATOM   7232 H HB3  B LYS   B 1 163 ? 40.502 -39.794 -6.045  0.58 25.15 ?  163 LYS   B HB3  1 
ATOM   7233 H HG2  A LYS   B 1 163 ? 38.235 -40.699 -5.555  0.42 30.23 ?  163 LYS   B HG2  1 
ATOM   7234 H HG2  B LYS   B 1 163 ? 38.366 -40.431 -5.380  0.58 30.57 ?  163 LYS   B HG2  1 
ATOM   7235 H HG3  A LYS   B 1 163 ? 38.891 -42.138 -5.717  0.42 30.23 ?  163 LYS   B HG3  1 
ATOM   7236 H HG3  B LYS   B 1 163 ? 38.717 -41.946 -5.712  0.58 30.57 ?  163 LYS   B HG3  1 
ATOM   7237 H HD2  A LYS   B 1 163 ? 40.290 -41.677 -3.891  0.42 34.28 ?  163 LYS   B HD2  1 
ATOM   7238 H HD2  B LYS   B 1 163 ? 40.346 -41.900 -4.012  0.58 35.70 ?  163 LYS   B HD2  1 
ATOM   7239 H HD3  A LYS   B 1 163 ? 39.558 -40.273 -3.709  0.42 34.28 ?  163 LYS   B HD3  1 
ATOM   7240 H HD3  B LYS   B 1 163 ? 39.880 -40.421 -3.644  0.58 35.70 ?  163 LYS   B HD3  1 
ATOM   7241 H HE2  A LYS   B 1 163 ? 37.514 -41.603 -3.473  0.42 37.49 ?  163 LYS   B HE2  1 
ATOM   7242 H HE2  B LYS   B 1 163 ? 37.691 -41.357 -3.239  0.58 39.53 ?  163 LYS   B HE2  1 
ATOM   7243 H HE3  A LYS   B 1 163 ? 38.497 -42.821 -3.209  0.42 37.49 ?  163 LYS   B HE3  1 
ATOM   7244 H HE3  B LYS   B 1 163 ? 38.384 -42.783 -3.310  0.58 39.53 ?  163 LYS   B HE3  1 
ATOM   7245 H HZ1  A LYS   B 1 163 ? 37.854 -41.881 -1.249  0.42 38.73 ?  163 LYS   B HZ1  1 
ATOM   7246 H HZ1  B LYS   B 1 163 ? 38.213 -42.086 -1.156  0.58 41.04 ?  163 LYS   B HZ1  1 
ATOM   7247 H HZ2  A LYS   B 1 163 ? 39.285 -41.712 -1.394  0.42 38.73 ?  163 LYS   B HZ2  1 
ATOM   7248 H HZ2  B LYS   B 1 163 ? 39.617 -42.199 -1.493  0.58 41.04 ?  163 LYS   B HZ2  1 
ATOM   7249 H HZ3  A LYS   B 1 163 ? 38.395 -40.593 -1.633  0.42 38.73 ?  163 LYS   B HZ3  1 
ATOM   7250 H HZ3  B LYS   B 1 163 ? 38.990 -40.895 -1.429  0.58 41.04 ?  163 LYS   B HZ3  1 
ATOM   7251 N N    . LEU   B 1 164 ? 39.069 -38.070 -7.918  1.00 15.51 ?  164 LEU   B N    1 
ATOM   7252 C CA   . LEU   B 1 164 ? 38.159 -36.930 -7.966  1.00 14.93 ?  164 LEU   B CA   1 
ATOM   7253 C C    . LEU   B 1 164 ? 37.367 -36.908 -9.270  1.00 15.66 ?  164 LEU   B C    1 
ATOM   7254 O O    . LEU   B 1 164 ? 36.145 -36.696 -9.268  1.00 17.14 ?  164 LEU   B O    1 
ATOM   7255 C CB   . LEU   B 1 164 ? 38.961 -35.638 -7.809  1.00 14.63 ?  164 LEU   B CB   1 
ATOM   7256 C CG   . LEU   B 1 164 ? 39.510 -35.359 -6.412  1.00 15.42 ?  164 LEU   B CG   1 
ATOM   7257 C CD1  . LEU   B 1 164 ? 40.581 -34.283 -6.465  1.00 15.47 ?  164 LEU   B CD1  1 
ATOM   7258 C CD2  . LEU   B 1 164 ? 38.376 -34.944 -5.475  1.00 17.07 ?  164 LEU   B CD2  1 
ATOM   7259 H H    A LEU   B 1 164 ? 39.906 -37.859 -7.914  0.42 18.63 ?  164 LEU   B H    1 
ATOM   7260 H H    B LEU   B 1 164 ? 39.906 -37.859 -7.949  0.58 18.63 ?  164 LEU   B H    1 
ATOM   7261 H HA   . LEU   B 1 164 ? 37.532 -36.994 -7.236  1.00 17.93 ?  164 LEU   B HA   1 
ATOM   7262 H HB2  . LEU   B 1 164 ? 39.719 -35.671 -8.415  1.00 17.58 ?  164 LEU   B HB2  1 
ATOM   7263 H HB3  . LEU   B 1 164 ? 38.389 -34.894 -8.049  1.00 17.58 ?  164 LEU   B HB3  1 
ATOM   7264 H HG   . LEU   B 1 164 ? 39.910 -36.170 -6.061  1.00 18.52 ?  164 LEU   B HG   1 
ATOM   7265 H HD11 . LEU   B 1 164 ? 40.911 -34.118 -5.566  1.00 18.58 ?  164 LEU   B HD11 1 
ATOM   7266 H HD12 . LEU   B 1 164 ? 41.313 -34.591 -7.029  1.00 18.58 ?  164 LEU   B HD12 1 
ATOM   7267 H HD13 . LEU   B 1 164 ? 40.203 -33.471 -6.833  1.00 18.58 ?  164 LEU   B HD13 1 
ATOM   7268 H HD21 . LEU   B 1 164 ? 38.750 -34.703 -4.614  1.00 20.50 ?  164 LEU   B HD21 1 
ATOM   7269 H HD22 . LEU   B 1 164 ? 37.909 -34.187 -5.858  1.00 20.50 ?  164 LEU   B HD22 1 
ATOM   7270 H HD23 . LEU   B 1 164 ? 37.763 -35.691 -5.369  1.00 20.50 ?  164 LEU   B HD23 1 
ATOM   7271 N N    . VAL   B 1 165 ? 38.053 -37.109 -10.398 1.00 17.29 ?  165 VAL   B N    1 
ATOM   7272 C CA   . VAL   B 1 165 ? 37.392 -37.039 -11.697 1.00 19.36 ?  165 VAL   B CA   1 
ATOM   7273 C C    . VAL   B 1 165 ? 36.473 -38.237 -11.885 1.00 21.75 ?  165 VAL   B C    1 
ATOM   7274 O O    . VAL   B 1 165 ? 35.313 -38.098 -12.294 1.00 23.16 ?  165 VAL   B O    1 
ATOM   7275 C CB   . VAL   B 1 165 ? 38.433 -36.957 -12.829 1.00 20.68 ?  165 VAL   B CB   1 
ATOM   7276 C CG1  . VAL   B 1 165 ? 37.752 -37.094 -14.175 1.00 22.18 ?  165 VAL   B CG1  1 
ATOM   7277 C CG2  . VAL   B 1 165 ? 39.223 -35.666 -12.750 1.00 20.37 ?  165 VAL   B CG2  1 
ATOM   7278 H H    . VAL   B 1 165 ? 38.897 -37.286 -10.438 1.00 20.77 ?  165 VAL   B H    1 
ATOM   7279 H HA   . VAL   B 1 165 ? 36.851 -36.238 -11.735 1.00 23.25 ?  165 VAL   B HA   1 
ATOM   7280 H HB   . VAL   B 1 165 ? 39.062 -37.692 -12.732 1.00 24.83 ?  165 VAL   B HB   1 
ATOM   7281 H HG11 . VAL   B 1 165 ? 38.349 -36.770 -14.864 1.00 26.63 ?  165 VAL   B HG11 1 
ATOM   7282 H HG12 . VAL   B 1 165 ? 37.557 -38.035 -14.331 1.00 26.63 ?  165 VAL   B HG12 1 
ATOM   7283 H HG13 . VAL   B 1 165 ? 36.933 -36.583 -14.170 1.00 26.63 ?  165 VAL   B HG13 1 
ATOM   7284 H HG21 . VAL   B 1 165 ? 39.857 -35.634 -13.484 1.00 24.46 ?  165 VAL   B HG21 1 
ATOM   7285 H HG22 . VAL   B 1 165 ? 38.608 -34.914 -12.817 1.00 24.46 ?  165 VAL   B HG22 1 
ATOM   7286 H HG23 . VAL   B 1 165 ? 39.694 -35.628 -11.904 1.00 24.46 ?  165 VAL   B HG23 1 
ATOM   7287 N N    . SER   B 1 166 ? 36.990 -39.438 -11.597 1.00 22.47 ?  166 SER   B N    1 
ATOM   7288 C CA   . SER   B 1 166 ? 36.235 -40.654 -11.874 1.00 24.05 ?  166 SER   B CA   1 
ATOM   7289 C C    . SER   B 1 166 ? 34.967 -40.725 -11.037 1.00 24.18 ?  166 SER   B C    1 
ATOM   7290 O O    . SER   B 1 166 ? 33.991 -41.343 -11.458 1.00 25.49 ?  166 SER   B O    1 
ATOM   7291 C CB   . SER   B 1 166 ? 37.098 -41.912 -11.668 1.00 25.19 ?  166 SER   B CB   1 
ATOM   7292 O OG   . SER   B 1 166 ? 37.428 -42.109 -10.302 1.00 25.77 ?  166 SER   B OG   1 
ATOM   7293 H H    . SER   B 1 166 ? 37.776 -39.571 -11.262 1.00 26.98 ?  166 SER   B H    1 
ATOM   7294 H HA   . SER   B 1 166 ? 35.977 -40.648 -12.810 1.00 28.88 ?  166 SER   B HA   1 
ATOM   7295 H HB2  . SER   B 1 166 ? 36.612 -42.686 -11.985 1.00 30.25 ?  166 SER   B HB2  1 
ATOM   7296 H HB3  . SER   B 1 166 ? 37.926 -41.817 -12.176 1.00 30.25 ?  166 SER   B HB3  1 
ATOM   7297 H HG   . SER   B 1 166 ? 37.860 -41.444 -10.016 1.00 30.95 ?  166 SER   B HG   1 
ATOM   7298 N N    . SER   B 1 167 ? 34.948 -40.101 -9.862  1.00 22.40 ?  167 SER   B N    1 
ATOM   7299 C CA   . SER   B 1 167 ? 33.789 -40.149 -8.978  1.00 22.28 ?  167 SER   B CA   1 
ATOM   7300 C C    . SER   B 1 167 ? 32.882 -38.921 -9.079  1.00 21.13 ?  167 SER   B C    1 
ATOM   7301 O O    . SER   B 1 167 ? 31.798 -38.920 -8.481  1.00 21.73 ?  167 SER   B O    1 
ATOM   7302 C CB   . SER   B 1 167 ? 34.232 -40.342 -7.520  1.00 22.56 ?  167 SER   B CB   1 
ATOM   7303 O OG   . SER   B 1 167 ? 34.910 -39.184 -7.032  1.00 22.57 ?  167 SER   B OG   1 
ATOM   7304 H H    . SER   B 1 167 ? 35.606 -39.653 -9.553  1.00 26.90 ?  167 SER   B H    1 
ATOM   7305 H HA   . SER   B 1 167 ? 33.254 -40.923 -9.226  1.00 26.76 ?  167 SER   B HA   1 
ATOM   7306 H HB2  . SER   B 1 167 ? 33.442 -40.513 -6.979  1.00 27.09 ?  167 SER   B HB2  1 
ATOM   7307 H HB3  . SER   B 1 167 ? 34.822 -41.121 -7.478  1.00 27.09 ?  167 SER   B HB3  1 
ATOM   7308 H HG   . SER   B 1 167 ? 35.600 -39.063 -7.482  1.00 27.10 ?  167 SER   B HG   1 
ATOM   7309 N N    . PHE   B 1 168 ? 33.276 -37.885 -9.825  1.00 21.25 ?  168 PHE   B N    1 
ATOM   7310 C CA   . PHE   B 1 168 ? 32.443 -36.683 -9.899  1.00 20.11 ?  168 PHE   B CA   1 
ATOM   7311 C C    . PHE   B 1 168 ? 31.132 -36.948 -10.634 1.00 16.92 ?  168 PHE   B C    1 
ATOM   7312 O O    . PHE   B 1 168 ? 30.087 -36.355 -10.301 1.00 17.27 ?  168 PHE   B O    1 
ATOM   7313 C CB   . PHE   B 1 168 ? 33.210 -35.551 -10.581 1.00 20.94 ?  168 PHE   B CB   1 
ATOM   7314 C CG   . PHE   B 1 168 ? 32.397 -34.307 -10.759 1.00 21.14 ?  168 PHE   B CG   1 
ATOM   7315 C CD1  . PHE   B 1 168 ? 32.028 -33.551 -9.655  1.00 22.92 ?  168 PHE   B CD1  1 
ATOM   7316 C CD2  . PHE   B 1 168 ? 31.975 -33.901 -12.012 1.00 20.73 ?  168 PHE   B CD2  1 
ATOM   7317 C CE1  . PHE   B 1 168 ? 31.261 -32.410 -9.794  1.00 22.68 ?  168 PHE   B CE1  1 
ATOM   7318 C CE2  . PHE   B 1 168 ? 31.222 -32.740 -12.163 1.00 20.92 ?  168 PHE   B CE2  1 
ATOM   7319 C CZ   . PHE   B 1 168 ? 30.856 -31.998 -11.048 1.00 21.66 ?  168 PHE   B CZ   1 
ATOM   7320 H H    . PHE   B 1 168 ? 33.996 -37.859 -10.298 1.00 25.52 ?  168 PHE   B H    1 
ATOM   7321 H HA   . PHE   B 1 168 ? 32.226 -36.402 -9.003  1.00 24.15 ?  168 PHE   B HA   1 
ATOM   7322 H HB2  . PHE   B 1 168 ? 33.982 -35.323 -10.036 1.00 25.14 ?  168 PHE   B HB2  1 
ATOM   7323 H HB3  . PHE   B 1 168 ? 33.501 -35.842 -11.457 1.00 25.14 ?  168 PHE   B HB3  1 
ATOM   7324 H HD1  . PHE   B 1 168 ? 32.293 -33.824 -8.809  1.00 27.52 ?  168 PHE   B HD1  1 
ATOM   7325 H HD2  . PHE   B 1 168 ? 32.218 -34.386 -12.764 1.00 24.89 ?  168 PHE   B HD2  1 
ATOM   7326 H HE1  . PHE   B 1 168 ? 31.023 -31.916 -9.045  1.00 27.24 ?  168 PHE   B HE1  1 
ATOM   7327 H HE2  . PHE   B 1 168 ? 30.941 -32.467 -13.010 1.00 25.12 ?  168 PHE   B HE2  1 
ATOM   7328 H HZ   . PHE   B 1 168 ? 30.341 -31.228 -11.148 1.00 26.01 ?  168 PHE   B HZ   1 
ATOM   7329 N N    . LEU   B 1 169 ? 31.176 -37.814 -11.643 1.00 16.79 ?  169 LEU   B N    1 
ATOM   7330 C CA   . LEU   B 1 169 ? 30.003 -38.151 -12.443 1.00 19.17 ?  169 LEU   B CA   1 
ATOM   7331 C C    . LEU   B 1 169 ? 29.991 -39.593 -12.928 1.00 22.63 ?  169 LEU   B C    1 
ATOM   7332 O O    . LEU   B 1 169 ? 29.082 -40.009 -13.647 1.00 25.51 ?  169 LEU   B O    1 
ATOM   7333 C CB   . LEU   B 1 169 ? 29.927 -37.242 -13.665 1.00 21.17 ?  169 LEU   B CB   1 
ATOM   7334 C CG   . LEU   B 1 169 ? 28.703 -36.336 -13.774 1.00 24.61 ?  169 LEU   B CG   1 
ATOM   7335 C CD1  . LEU   B 1 169 ? 28.651 -35.745 -15.161 1.00 25.23 ?  169 LEU   B CD1  1 
ATOM   7336 C CD2  . LEU   B 1 169 ? 27.418 -37.081 -13.462 1.00 24.23 ?  169 LEU   B CD2  1 
ATOM   7337 O OXT  . LEU   B 1 169 ? 30.889 -40.368 -12.640 1.00 23.76 -1 169 LEU   B OXT  1 
ATOM   7338 H H    . LEU   B 1 169 ? 31.892 -38.220 -11.900 1.00 20.17 ?  169 LEU   B H    1 
ATOM   7339 H HA   . LEU   B 1 169 ? 29.217 -38.003 -11.899 1.00 23.02 ?  169 LEU   B HA   1 
ATOM   7340 H HB2  . LEU   B 1 169 ? 30.709 -36.668 -13.673 1.00 25.42 ?  169 LEU   B HB2  1 
ATOM   7341 H HB3  . LEU   B 1 169 ? 29.935 -37.800 -14.460 1.00 25.42 ?  169 LEU   B HB3  1 
ATOM   7342 H HG   . LEU   B 1 169 ? 28.790 -35.606 -13.140 1.00 29.55 ?  169 LEU   B HG   1 
ATOM   7343 H HD11 . LEU   B 1 169 ? 27.896 -35.141 -15.217 1.00 30.29 ?  169 LEU   B HD11 1 
ATOM   7344 H HD12 . LEU   B 1 169 ? 29.476 -35.263 -15.327 1.00 30.29 ?  169 LEU   B HD12 1 
ATOM   7345 H HD13 . LEU   B 1 169 ? 28.552 -36.464 -15.803 1.00 30.29 ?  169 LEU   B HD13 1 
ATOM   7346 H HD21 . LEU   B 1 169 ? 26.678 -36.635 -13.895 1.00 29.09 ?  169 LEU   B HD21 1 
ATOM   7347 H HD22 . LEU   B 1 169 ? 27.497 -37.993 -13.795 1.00 29.09 ?  169 LEU   B HD22 1 
ATOM   7348 H HD23 . LEU   B 1 169 ? 27.286 -37.095 -12.502 1.00 29.09 ?  169 LEU   B HD23 1 
HETATM 7349 C C1   T TFA   C 2 .   ? 12.095 -1.362  1.252   0.20 11.09 ?  201 TFA   A C1   1 
HETATM 7350 C C2   T TFA   C 2 .   ? 12.746 -1.728  -0.109  0.20 13.08 ?  201 TFA   A C2   1 
HETATM 7351 O O    T TFA   C 2 .   ? 12.841 -1.567  2.215   0.20 10.30 ?  201 TFA   A O    1 
HETATM 7352 F F1   T TFA   C 2 .   ? 12.891 -3.063  -0.232  0.20 14.41 ?  201 TFA   A F1   1 
HETATM 7353 F F2   T TFA   C 2 .   ? 11.999 -1.335  -1.153  0.20 12.95 ?  201 TFA   A F2   1 
HETATM 7354 F F3   T TFA   C 2 .   ? 13.951 -1.174  -0.284  0.20 14.48 ?  201 TFA   A F3   1 
HETATM 7355 O OXT  T TFA   C 2 .   ? 10.941 -0.925  1.195   0.20 10.41 ?  201 TFA   A OXT  1 
HETATM 7356 N N2   B A1A8G D 3 .   ? 14.976 -0.204  3.670   0.58 16.74 ?  202 A1A8G A N2   1 
HETATM 7357 C C3   B A1A8G D 3 .   ? 14.210 0.179   -0.650  0.58 20.76 ?  202 A1A8G A C3   1 
HETATM 7358 C C6   B A1A8G D 3 .   ? 12.580 1.817   -2.782  0.58 22.96 ?  202 A1A8G A C6   1 
HETATM 7359 C C9   B A1A8G D 3 .   ? 12.457 1.963   0.197   0.58 21.18 ?  202 A1A8G A C9   1 
HETATM 7360 C C12  B A1A8G D 3 .   ? 14.982 -0.162  5.054   0.58 15.84 ?  202 A1A8G A C12  1 
HETATM 7361 C C14  B A1A8G D 3 .   ? 15.376 2.175   3.654   0.58 14.05 ?  202 A1A8G A C14  1 
HETATM 7362 C C1   B A1A8G D 3 .   ? 16.221 -1.092  0.411   0.58 20.06 ?  202 A1A8G A C1   1 
HETATM 7363 C C10  B A1A8G D 3 .   ? 14.790 2.089   0.697   0.58 18.71 ?  202 A1A8G A C10  1 
HETATM 7364 C C11  B A1A8G D 3 .   ? 15.161 0.941   2.954   0.58 16.67 ?  202 A1A8G A C11  1 
HETATM 7365 C C13  B A1A8G D 3 .   ? 15.353 2.043   5.049   0.58 13.66 ?  202 A1A8G A C13  1 
HETATM 7366 C C15  B A1A8G D 3 .   ? 15.632 3.580   3.412   0.58 13.05 ?  202 A1A8G A C15  1 
HETATM 7367 C C16  B A1A8G D 3 .   ? 15.732 4.234   4.617   0.58 13.00 ?  202 A1A8G A C16  1 
HETATM 7368 C C2   B A1A8G D 3 .   ? 14.889 -0.307  0.702   0.58 19.81 ?  202 A1A8G A C2   1 
HETATM 7369 C C4   B A1A8G D 3 .   ? 13.821 1.678   -0.470  0.58 20.84 ?  202 A1A8G A C4   1 
HETATM 7370 C C5   B A1A8G D 3 .   ? 13.720 2.313   -1.880  0.58 22.44 ?  202 A1A8G A C5   1 
HETATM 7371 C C7   B A1A8G D 3 .   ? 11.209 1.555   -2.081  0.58 22.87 ?  202 A1A8G A C7   1 
HETATM 7372 C C8   B A1A8G D 3 .   ? 11.251 1.332   -0.543  0.58 21.76 ?  202 A1A8G A C8   1 
HETATM 7373 N N1   B A1A8G D 3 .   ? 15.175 0.908   1.507   0.58 18.37 ?  202 A1A8G A N1   1 
HETATM 7374 N N3   B A1A8G D 3 .   ? 15.165 0.927   5.817   0.58 14.33 ?  202 A1A8G A N3   1 
HETATM 7375 N N4   B A1A8G D 3 .   ? 15.568 3.290   5.670   0.58 13.02 ?  202 A1A8G A N4   1 
HETATM 7376 O O1   B A1A8G D 3 .   ? 15.841 -2.344  -0.092  0.58 20.34 ?  202 A1A8G A O1   1 
HETATM 7377 H H6   B A1A8G D 3 .   ? 14.910 0.023   -1.525  0.58 24.92 ?  202 A1A8G A H6   1 
HETATM 7378 H H5   B A1A8G D 3 .   ? 13.328 -0.454  -0.912  0.58 24.92 ?  202 A1A8G A H5   1 
HETATM 7379 H H9   B A1A8G D 3 .   ? 12.430 2.524   -3.646  0.58 27.57 ?  202 A1A8G A H9   1 
HETATM 7380 H H10  B A1A8G D 3 .   ? 12.910 0.890   -3.279  0.58 27.57 ?  202 A1A8G A H10  1 
HETATM 7381 H H15  B A1A8G D 3 .   ? 12.446 1.657   1.253   0.58 25.43 ?  202 A1A8G A H15  1 
HETATM 7382 H H16  B A1A8G D 3 .   ? 12.310 3.084   0.231   0.58 25.43 ?  202 A1A8G A H16  1 
HETATM 7383 H H19  B A1A8G D 3 .   ? 14.811 -1.120  5.630   0.58 19.02 ?  202 A1A8G A H19  1 
HETATM 7384 H H3   B A1A8G D 3 .   ? 16.842 -0.534  -0.332  0.58 24.09 ?  202 A1A8G A H3   1 
HETATM 7385 H H4   B A1A8G D 3 .   ? 16.850 -1.196  1.338   0.58 24.09 ?  202 A1A8G A H4   1 
HETATM 7386 H H18  B A1A8G D 3 .   ? 14.338 2.862   1.322   0.58 22.47 ?  202 A1A8G A H18  1 
HETATM 7387 H H17  B A1A8G D 3 .   ? 15.715 2.542   0.272   0.58 22.47 ?  202 A1A8G A H17  1 
HETATM 7388 H H20  B A1A8G D 3 .   ? 15.718 4.146   2.484   0.58 15.68 ?  202 A1A8G A H20  1 
HETATM 7389 H H21  B A1A8G D 3 .   ? 15.897 5.227   5.012   0.58 15.62 ?  202 A1A8G A H21  1 
HETATM 7390 H H1   B A1A8G D 3 .   ? 14.160 -0.994  1.207   0.58 23.79 ?  202 A1A8G A H1   1 
HETATM 7391 H H8   B A1A8G D 3 .   ? 13.706 3.433   -1.821  0.58 26.94 ?  202 A1A8G A H8   1 
HETATM 7392 H H7   B A1A8G D 3 .   ? 14.668 2.117   -2.428  0.58 26.94 ?  202 A1A8G A H7   1 
HETATM 7393 H H11  B A1A8G D 3 .   ? 10.702 0.683   -2.562  0.58 27.47 ?  202 A1A8G A H11  1 
HETATM 7394 H H12  B A1A8G D 3 .   ? 10.497 2.397   -2.311  0.58 27.47 ?  202 A1A8G A H12  1 
HETATM 7395 H H14  B A1A8G D 3 .   ? 11.175 0.240   -0.315  0.58 26.12 ?  202 A1A8G A H14  1 
HETATM 7396 H H13  B A1A8G D 3 .   ? 10.301 1.721   -0.090  0.58 26.12 ?  202 A1A8G A H13  1 
HETATM 7397 H H22  B A1A8G D 3 .   ? 15.597 3.492   6.585   0.58 15.64 ?  202 A1A8G A H22  1 
HETATM 7398 H H2   B A1A8G D 3 .   ? 16.605 -2.801  -0.499  0.58 24.42 ?  202 A1A8G A H2   1 
HETATM 7399 O O    . HOH   E 4 .   ? -0.457 -2.977  2.759   1.00 45.05 ?  301 HOH   A O    1 
HETATM 7400 O O    . HOH   E 4 .   ? 4.718  3.707   0.272   1.00 28.69 ?  302 HOH   A O    1 
HETATM 7401 O O    . HOH   E 4 .   ? 11.825 0.359   14.433  1.00 34.92 ?  303 HOH   A O    1 
HETATM 7402 O O    A HOH   E 4 .   ? 14.742 -4.587  20.289  0.42 33.89 ?  304 HOH   A O    1 
HETATM 7403 O O    . HOH   E 4 .   ? 15.071 -12.130 18.572  1.00 44.73 ?  305 HOH   A O    1 
HETATM 7404 O O    . HOH   E 4 .   ? 11.867 -10.837 -10.113 1.00 61.84 ?  306 HOH   A O    1 
HETATM 7405 O O    . HOH   E 4 .   ? 14.653 -13.777 16.649  1.00 31.63 ?  307 HOH   A O    1 
HETATM 7406 O O    . HOH   E 4 .   ? 42.529 4.227   5.656   1.00 36.94 ?  308 HOH   A O    1 
HETATM 7407 O O    . HOH   E 4 .   ? 29.076 0.329   -9.873  1.00 22.66 ?  309 HOH   A O    1 
HETATM 7408 O O    . HOH   E 4 .   ? 34.338 -1.817  12.439  1.00 37.80 ?  310 HOH   A O    1 
HETATM 7409 O O    . HOH   E 4 .   ? 25.986 -0.987  -7.668  1.00 24.44 ?  311 HOH   A O    1 
HETATM 7410 O O    . HOH   E 4 .   ? 3.737  -9.270  9.631   1.00 37.47 ?  312 HOH   A O    1 
HETATM 7411 O O    . HOH   E 4 .   ? 22.104 5.423   18.751  1.00 49.78 ?  313 HOH   A O    1 
HETATM 7412 O O    . HOH   E 4 .   ? 10.871 1.747   12.105  1.00 24.41 ?  314 HOH   A O    1 
HETATM 7413 O O    . HOH   E 4 .   ? 39.839 -1.052  -5.083  1.00 21.50 ?  315 HOH   A O    1 
HETATM 7414 O O    . HOH   E 4 .   ? 22.443 -11.950 21.955  1.00 55.43 ?  316 HOH   A O    1 
HETATM 7415 O O    . HOH   E 4 .   ? 9.184  -10.005 19.172  1.00 45.86 ?  317 HOH   A O    1 
HETATM 7416 O O    . HOH   E 4 .   ? 28.001 -6.169  19.542  1.00 45.03 ?  318 HOH   A O    1 
HETATM 7417 O O    . HOH   E 4 .   ? -0.973 -8.714  2.022   1.00 44.09 ?  319 HOH   A O    1 
HETATM 7418 O O    . HOH   E 4 .   ? 14.931 4.067   17.280  1.00 37.21 ?  320 HOH   A O    1 
HETATM 7419 O O    . HOH   E 4 .   ? 37.479 2.799   10.303  1.00 25.34 ?  321 HOH   A O    1 
HETATM 7420 O O    A HOH   E 4 .   ? 14.169 -4.612  -11.868 0.42 23.98 ?  322 HOH   A O    1 
HETATM 7421 O O    . HOH   E 4 .   ? 14.526 -0.535  -12.484 1.00 44.49 ?  323 HOH   A O    1 
HETATM 7422 O O    . HOH   E 4 .   ? 8.156  -21.536 3.787   1.00 54.49 ?  324 HOH   A O    1 
HETATM 7423 O O    . HOH   E 4 .   ? 30.360 -13.303 -8.512  1.00 22.55 ?  325 HOH   A O    1 
HETATM 7424 O O    . HOH   E 4 .   ? 13.610 -15.268 -7.888  1.00 32.56 ?  326 HOH   A O    1 
HETATM 7425 O O    . HOH   E 4 .   ? 18.673 -19.330 13.527  1.00 33.60 ?  327 HOH   A O    1 
HETATM 7426 O O    . HOH   E 4 .   ? 14.538 -21.260 -4.323  1.00 36.85 ?  328 HOH   A O    1 
HETATM 7427 O O    . HOH   E 4 .   ? 43.610 8.263   -3.249  1.00 35.69 ?  329 HOH   A O    1 
HETATM 7428 O O    . HOH   E 4 .   ? 24.143 -7.711  14.370  1.00 16.57 ?  330 HOH   A O    1 
HETATM 7429 O O    . HOH   E 4 .   ? 42.380 10.500  4.861   1.00 18.41 ?  331 HOH   A O    1 
HETATM 7430 O O    . HOH   E 4 .   ? 0.709  -4.532  -0.126  1.00 41.14 ?  332 HOH   A O    1 
HETATM 7431 O O    . HOH   E 4 .   ? 26.960 11.479  1.585   1.00 17.90 ?  333 HOH   A O    1 
HETATM 7432 O O    . HOH   E 4 .   ? 17.098 -17.938 14.929  1.00 29.09 ?  334 HOH   A O    1 
HETATM 7433 O O    A HOH   E 4 .   ? 24.661 2.018   -7.082  0.42 18.45 ?  335 HOH   A O    1 
HETATM 7434 O O    . HOH   E 4 .   ? 30.954 6.189   -12.263 1.00 26.89 ?  336 HOH   A O    1 
HETATM 7435 O O    . HOH   E 4 .   ? 31.622 8.205   14.875  1.00 25.52 ?  337 HOH   A O    1 
HETATM 7436 O O    . HOH   E 4 .   ? 36.279 -5.176  -0.478  1.00 37.61 ?  338 HOH   A O    1 
HETATM 7437 O O    A HOH   E 4 .   ? 28.329 -0.228  -13.415 0.42 24.43 ?  339 HOH   A O    1 
HETATM 7438 O O    . HOH   E 4 .   ? 23.962 -15.804 -9.227  1.00 41.08 ?  340 HOH   A O    1 
HETATM 7439 O O    . HOH   E 4 .   ? 21.376 -2.220  -2.661  1.00 21.16 ?  341 HOH   A O    1 
HETATM 7440 O O    . HOH   E 4 .   ? 31.048 -18.067 7.740   1.00 18.76 ?  342 HOH   A O    1 
HETATM 7441 O O    . HOH   E 4 .   ? 43.467 7.677   2.874   1.00 46.81 ?  343 HOH   A O    1 
HETATM 7442 O O    . HOH   E 4 .   ? 41.565 1.378   5.112   1.00 41.78 ?  344 HOH   A O    1 
HETATM 7443 O O    . HOH   E 4 .   ? 34.136 -1.068  -8.916  1.00 27.00 ?  345 HOH   A O    1 
HETATM 7444 O O    . HOH   E 4 .   ? 22.184 -19.372 11.319  1.00 34.99 ?  346 HOH   A O    1 
HETATM 7445 O O    . HOH   E 4 .   ? 10.040 -21.383 5.560   1.00 24.66 ?  347 HOH   A O    1 
HETATM 7446 O O    . HOH   E 4 .   ? 18.993 -21.950 6.820   1.00 38.50 ?  348 HOH   A O    1 
HETATM 7447 O O    . HOH   E 4 .   ? 44.362 7.236   6.471   1.00 27.29 ?  349 HOH   A O    1 
HETATM 7448 O O    A HOH   E 4 .   ? 14.667 -3.662  2.964   0.42 15.30 ?  350 HOH   A O    1 
HETATM 7449 O O    . HOH   E 4 .   ? 18.512 9.534   8.777   1.00 21.42 ?  351 HOH   A O    1 
HETATM 7450 O O    . HOH   E 4 .   ? 38.534 4.980   7.102   1.00 15.61 ?  352 HOH   A O    1 
HETATM 7451 O O    . HOH   E 4 .   ? 26.714 -3.044  19.624  1.00 36.51 ?  353 HOH   A O    1 
HETATM 7452 O O    . HOH   E 4 .   ? 27.438 13.840  2.755   1.00 32.30 ?  354 HOH   A O    1 
HETATM 7453 O O    B HOH   E 4 .   ? 15.045 -2.830  2.921   0.58 15.53 ?  355 HOH   A O    1 
HETATM 7454 O O    . HOH   E 4 .   ? 24.113 -2.139  -2.271  1.00 12.67 ?  356 HOH   A O    1 
HETATM 7455 O O    A HOH   E 4 .   ? 14.291 0.570   6.660   0.42 19.01 ?  357 HOH   A O    1 
HETATM 7456 O O    . HOH   E 4 .   ? 38.324 10.617  6.920   1.00 51.19 ?  358 HOH   A O    1 
HETATM 7457 O O    . HOH   E 4 .   ? 27.377 -10.509 14.069  1.00 17.19 ?  359 HOH   A O    1 
HETATM 7458 O O    A HOH   E 4 .   ? 13.384 -1.454  -6.666  0.42 17.97 ?  360 HOH   A O    1 
HETATM 7459 O O    . HOH   E 4 .   ? 15.166 -21.458 14.172  1.00 19.11 ?  361 HOH   A O    1 
HETATM 7460 O O    . HOH   E 4 .   ? 24.676 -17.447 12.740  1.00 26.56 ?  362 HOH   A O    1 
HETATM 7461 O O    . HOH   E 4 .   ? 5.355  2.652   4.696   1.00 32.75 ?  363 HOH   A O    1 
HETATM 7462 O O    . HOH   E 4 .   ? 16.633 -22.097 0.832   1.00 34.62 ?  364 HOH   A O    1 
HETATM 7463 O O    . HOH   E 4 .   ? 22.744 12.497  1.522   1.00 15.24 ?  365 HOH   A O    1 
HETATM 7464 O O    . HOH   E 4 .   ? 20.720 -19.730 -5.188  1.00 33.88 ?  366 HOH   A O    1 
HETATM 7465 O O    . HOH   E 4 .   ? 26.980 4.146   -0.751  1.00 12.91 ?  367 HOH   A O    1 
HETATM 7466 O O    A HOH   E 4 .   ? 6.940  -8.156  11.686  0.42 14.47 ?  368 HOH   A O    1 
HETATM 7467 O O    . HOH   E 4 .   ? 21.922 -21.861 8.498   1.00 32.97 ?  369 HOH   A O    1 
HETATM 7468 O O    . HOH   E 4 .   ? 20.111 -12.697 -8.722  1.00 28.94 ?  370 HOH   A O    1 
HETATM 7469 O O    . HOH   E 4 .   ? 21.145 10.299  14.871  1.00 36.08 ?  371 HOH   A O    1 
HETATM 7470 O O    . HOH   E 4 .   ? 31.179 -13.946 -2.482  1.00 14.13 ?  372 HOH   A O    1 
HETATM 7471 O O    . HOH   E 4 .   ? 35.814 -12.615 6.826   1.00 15.87 ?  373 HOH   A O    1 
HETATM 7472 O O    . HOH   E 4 .   ? 30.758 3.112   8.237   1.00 12.33 ?  374 HOH   A O    1 
HETATM 7473 O O    B HOH   E 4 .   ? 12.790 -0.572  -5.179  0.58 33.64 ?  375 HOH   A O    1 
HETATM 7474 O O    . HOH   E 4 .   ? 17.065 -19.247 4.819   1.00 17.13 ?  376 HOH   A O    1 
HETATM 7475 O O    . HOH   E 4 .   ? 30.500 1.950   16.707  1.00 22.00 ?  377 HOH   A O    1 
HETATM 7476 O O    . HOH   E 4 .   ? 33.645 -7.129  4.298   1.00 16.34 ?  378 HOH   A O    1 
HETATM 7477 O O    A HOH   E 4 .   ? 17.540 -1.725  0.319   0.42 18.87 ?  379 HOH   A O    1 
HETATM 7478 O O    . HOH   E 4 .   ? 29.785 -1.963  -12.912 1.00 50.35 ?  380 HOH   A O    1 
HETATM 7479 O O    . HOH   E 4 .   ? 24.374 3.666   -1.854  1.00 18.54 ?  381 HOH   A O    1 
HETATM 7480 O O    . HOH   E 4 .   ? 27.033 2.438   18.616  1.00 38.40 ?  382 HOH   A O    1 
HETATM 7481 O O    . HOH   E 4 .   ? 37.118 -2.941  9.805   1.00 50.64 ?  383 HOH   A O    1 
HETATM 7482 O O    . HOH   E 4 .   ? 7.990  -12.730 -1.206  1.00 39.04 ?  384 HOH   A O    1 
HETATM 7483 O O    . HOH   E 4 .   ? 32.087 -7.384  -9.794  1.00 21.48 ?  385 HOH   A O    1 
HETATM 7484 O O    . HOH   E 4 .   ? 23.496 11.403  3.950   1.00 12.82 ?  386 HOH   A O    1 
HETATM 7485 O O    . HOH   E 4 .   ? 21.329 2.969   -0.314  1.00 14.54 ?  387 HOH   A O    1 
HETATM 7486 O O    . HOH   E 4 .   ? 8.880  -12.001 16.998  1.00 38.86 ?  388 HOH   A O    1 
HETATM 7487 O O    . HOH   E 4 .   ? 37.267 11.991  4.957   1.00 24.65 ?  389 HOH   A O    1 
HETATM 7488 O O    . HOH   E 4 .   ? 28.010 0.799   -7.273  1.00 15.27 ?  390 HOH   A O    1 
HETATM 7489 O O    A HOH   E 4 .   ? 15.823 -0.951  5.139   0.42 20.48 ?  391 HOH   A O    1 
HETATM 7490 O O    . HOH   E 4 .   ? 13.618 -4.603  17.035  1.00 26.99 ?  392 HOH   A O    1 
HETATM 7491 O O    . HOH   E 4 .   ? 27.727 -6.423  -14.191 1.00 35.81 ?  393 HOH   A O    1 
HETATM 7492 O O    . HOH   E 4 .   ? 16.155 16.657  8.561   1.00 44.08 ?  394 HOH   A O    1 
HETATM 7493 O O    . HOH   E 4 .   ? 15.337 -8.078  -10.079 1.00 35.31 ?  395 HOH   A O    1 
HETATM 7494 O O    . HOH   E 4 .   ? 20.602 -19.997 2.758   1.00 21.08 ?  396 HOH   A O    1 
HETATM 7495 O O    . HOH   E 4 .   ? 38.129 -1.348  -1.822  1.00 19.28 ?  397 HOH   A O    1 
HETATM 7496 O O    T HOH   E 4 .   ? 15.443 -0.430  2.253   0.20 11.72 ?  398 HOH   A O    1 
HETATM 7497 O O    . HOH   E 4 .   ? 37.553 -2.091  5.902   1.00 27.20 ?  399 HOH   A O    1 
HETATM 7498 O O    . HOH   E 4 .   ? 41.015 -8.305  -6.844  1.00 38.23 ?  400 HOH   A O    1 
HETATM 7499 O O    . HOH   E 4 .   ? 18.362 -15.831 16.085  1.00 41.86 ?  401 HOH   A O    1 
HETATM 7500 O O    . HOH   E 4 .   ? 32.754 -9.256  5.913   1.00 20.70 ?  402 HOH   A O    1 
HETATM 7501 O O    . HOH   E 4 .   ? 14.091 -23.078 7.359   1.00 21.03 ?  403 HOH   A O    1 
HETATM 7502 O O    . HOH   E 4 .   ? 18.929 -0.669  -1.777  1.00 31.48 ?  404 HOH   A O    1 
HETATM 7503 O O    . HOH   E 4 .   ? 6.354  -5.532  10.814  1.00 19.56 ?  405 HOH   A O    1 
HETATM 7504 O O    A HOH   E 4 .   ? 11.105 -0.388  1.780   0.80 37.34 ?  406 HOH   A O    1 
HETATM 7505 O O    . HOH   E 4 .   ? 17.251 -17.773 -5.278  1.00 34.03 ?  407 HOH   A O    1 
HETATM 7506 O O    . HOH   E 4 .   ? 14.375 -24.620 11.475  1.00 43.32 ?  408 HOH   A O    1 
HETATM 7507 O O    . HOH   E 4 .   ? 45.093 -0.758  3.011   1.00 42.73 ?  409 HOH   A O    1 
HETATM 7508 O O    . HOH   E 4 .   ? 6.491  -3.305  12.479  1.00 31.54 ?  410 HOH   A O    1 
HETATM 7509 O O    A HOH   E 4 .   ? 20.180 4.521   -7.664  0.42 19.02 ?  411 HOH   A O    1 
HETATM 7510 O O    . HOH   E 4 .   ? 15.483 11.746  7.706   1.00 54.89 ?  412 HOH   A O    1 
HETATM 7511 O O    . HOH   E 4 .   ? 15.703 2.229   24.532  1.00 56.81 ?  413 HOH   A O    1 
HETATM 7512 O O    . HOH   E 4 .   ? 21.377 -14.622 17.697  1.00 52.56 ?  414 HOH   A O    1 
HETATM 7513 O O    . HOH   E 4 .   ? 16.059 6.876   2.684   1.00 20.58 ?  415 HOH   A O    1 
HETATM 7514 O O    B HOH   E 4 .   ? 13.332 -3.221  -1.276  0.58 35.99 ?  416 HOH   A O    1 
HETATM 7515 O O    . HOH   E 4 .   ? -1.545 -5.141  7.116   1.00 50.73 ?  417 HOH   A O    1 
HETATM 7516 O O    A HOH   E 4 .   ? 18.691 -2.495  -16.455 0.42 31.76 ?  418 HOH   A O    1 
HETATM 7517 O O    . HOH   E 4 .   ? 35.124 -5.274  -3.027  1.00 19.97 ?  419 HOH   A O    1 
HETATM 7518 O O    . HOH   E 4 .   ? 24.025 -20.261 -1.379  1.00 19.12 ?  420 HOH   A O    1 
HETATM 7519 O O    . HOH   E 4 .   ? 30.276 -12.802 13.596  1.00 19.45 ?  421 HOH   A O    1 
HETATM 7520 O O    . HOH   E 4 .   ? 32.587 -10.590 3.223   1.00 31.26 ?  422 HOH   A O    1 
HETATM 7521 O O    . HOH   E 4 .   ? 30.007 -10.035 13.077  1.00 24.83 ?  423 HOH   A O    1 
HETATM 7522 O O    . HOH   E 4 .   ? 36.688 -5.020  5.469   1.00 25.58 ?  424 HOH   A O    1 
HETATM 7523 O O    . HOH   E 4 .   ? 18.773 -10.447 24.129  1.00 94.60 ?  425 HOH   A O    1 
HETATM 7524 O O    . HOH   E 4 .   ? 10.393 -13.789 -1.952  1.00 24.36 ?  426 HOH   A O    1 
HETATM 7525 O O    . HOH   E 4 .   ? 32.890 -4.509  -9.947  1.00 28.80 ?  427 HOH   A O    1 
HETATM 7526 O O    . HOH   E 4 .   ? 22.500 8.314   18.306  1.00 46.58 ?  428 HOH   A O    1 
HETATM 7527 O O    . HOH   E 4 .   ? 28.799 -10.617 -14.217 1.00 45.24 ?  429 HOH   A O    1 
HETATM 7528 O O    A HOH   E 4 .   ? 7.787  -6.347  -6.672  0.42 32.15 ?  430 HOH   A O    1 
HETATM 7529 O O    . HOH   E 4 .   ? 24.055 4.040   -4.909  1.00 29.15 ?  431 HOH   A O    1 
HETATM 7530 O O    A HOH   E 4 .   ? 10.557 -22.190 -1.392  0.42 33.25 ?  432 HOH   A O    1 
HETATM 7531 O O    . HOH   E 4 .   ? 21.844 -13.970 -8.346  1.00 60.13 ?  433 HOH   A O    1 
HETATM 7532 O O    A HOH   E 4 .   ? 18.913 2.020   -0.872  0.42 12.68 ?  434 HOH   A O    1 
HETATM 7533 O O    . HOH   E 4 .   ? 11.632 -10.589 16.814  1.00 27.16 ?  435 HOH   A O    1 
HETATM 7534 O O    . HOH   E 4 .   ? 16.112 -14.184 20.099  1.00 60.82 ?  436 HOH   A O    1 
HETATM 7535 O O    . HOH   E 4 .   ? 23.499 -20.947 1.307   1.00 20.65 ?  437 HOH   A O    1 
HETATM 7536 O O    A HOH   E 4 .   ? 18.550 4.813   -15.154 0.42 39.94 ?  438 HOH   A O    1 
HETATM 7537 O O    . HOH   E 4 .   ? 37.816 -8.856  -3.473  1.00 24.20 ?  439 HOH   A O    1 
HETATM 7538 O O    . HOH   E 4 .   ? 23.346 7.277   -3.143  1.00 38.27 ?  440 HOH   A O    1 
HETATM 7539 O O    . HOH   E 4 .   ? 23.390 -7.988  17.030  1.00 22.75 ?  441 HOH   A O    1 
HETATM 7540 O O    . HOH   E 4 .   ? 34.351 -8.211  -0.484  1.00 30.69 ?  442 HOH   A O    1 
HETATM 7541 O O    . HOH   E 4 .   ? 16.677 2.796   -1.658  1.00 48.28 ?  443 HOH   A O    1 
HETATM 7542 O O    . HOH   E 4 .   ? 31.376 -12.777 -0.045  1.00 22.00 ?  444 HOH   A O    1 
HETATM 7543 O O    . HOH   E 4 .   ? 20.423 -17.685 24.776  1.00 66.55 ?  445 HOH   A O    1 
HETATM 7544 O O    A HOH   E 4 .   ? 14.058 -0.346  3.322   0.22 28.54 ?  446 HOH   A O    1 
HETATM 7545 O O    . HOH   E 4 .   ? 30.572 14.744  2.712   1.00 19.11 ?  447 HOH   A O    1 
HETATM 7546 O O    B HOH   E 4 .   ? 18.529 1.842   -0.595  0.58 14.34 ?  448 HOH   A O    1 
HETATM 7547 O O    A HOH   E 4 .   ? 9.437  -16.338 -2.126  0.42 35.63 ?  449 HOH   A O    1 
HETATM 7548 O O    . HOH   E 4 .   ? 29.699 -15.949 10.673  1.00 28.97 ?  450 HOH   A O    1 
HETATM 7549 O O    B HOH   E 4 .   ? 20.684 4.273   -2.661  0.58 23.11 ?  451 HOH   A O    1 
HETATM 7550 O O    B HOH   E 4 .   ? 18.030 3.551   -3.134  0.58 34.73 ?  452 HOH   A O    1 
HETATM 7551 O O    B HOH   E 4 .   ? 20.746 6.887   -3.552  0.58 46.40 ?  453 HOH   A O    1 
HETATM 7552 O O    . HOH   E 4 .   ? 25.471 8.320   -4.754  1.00 38.30 ?  454 HOH   A O    1 
HETATM 7553 O O    . HOH   E 4 .   ? 21.454 -9.041  21.356  1.00 66.04 ?  455 HOH   A O    1 
HETATM 7554 O O    . HOH   E 4 .   ? 32.383 -15.865 10.869  1.00 29.38 ?  456 HOH   A O    1 
HETATM 7555 O O    . HOH   E 4 .   ? 20.020 -17.431 -5.070  1.00 32.40 ?  457 HOH   A O    1 
HETATM 7556 O O    B HOH   E 4 .   ? 16.595 5.867   -2.875  0.58 28.77 ?  458 HOH   A O    1 
HETATM 7557 O O    . HOH   E 4 .   ? 24.689 5.670   20.633  1.00 52.23 ?  459 HOH   A O    1 
HETATM 7558 O O    . HOH   E 4 .   ? 27.923 7.183   -6.745  1.00 41.11 ?  460 HOH   A O    1 
HETATM 7559 O O    . HOH   E 4 .   ? 23.241 -22.363 -3.389  1.00 37.08 ?  461 HOH   A O    1 
HETATM 7560 O O    . HOH   E 4 .   ? 24.766 14.741  7.595   1.00 38.50 ?  462 HOH   A O    1 
HETATM 7561 O O    B HOH   E 4 .   ? 12.699 -3.225  1.484   0.58 26.46 ?  463 HOH   A O    1 
HETATM 7562 O O    . HOH   E 4 .   ? 27.431 -11.379 16.564  1.00 41.63 ?  464 HOH   A O    1 
HETATM 7563 O O    . HOH   E 4 .   ? 26.954 11.724  -1.484  1.00 40.25 ?  465 HOH   A O    1 
HETATM 7564 O O    . HOH   E 4 .   ? 16.113 -6.756  -11.964 1.00 56.55 ?  466 HOH   A O    1 
HETATM 7565 O O    . HOH   E 4 .   ? 18.738 10.996  11.102  1.00 32.96 ?  467 HOH   A O    1 
HETATM 7566 O O    . HOH   E 4 .   ? 18.368 -16.125 -8.923  1.00 54.48 ?  468 HOH   A O    1 
HETATM 7567 O O    . HOH   E 4 .   ? 11.898 -13.254 16.181  1.00 56.80 ?  469 HOH   A O    1 
HETATM 7568 O O    . HOH   E 4 .   ? 15.924 -21.606 3.684   1.00 26.74 ?  470 HOH   A O    1 
HETATM 7569 O O    . HOH   E 4 .   ? 23.450 13.701  5.424   1.00 19.59 ?  471 HOH   A O    1 
HETATM 7570 O O    A HOH   E 4 .   ? 11.235 -14.873 -6.274  0.42 28.55 ?  472 HOH   A O    1 
HETATM 7571 O O    A HOH   E 4 .   ? 22.039 5.247   -5.946  0.42 30.42 ?  473 HOH   A O    1 
HETATM 7572 O O    . HOH   E 4 .   ? 25.865 10.956  -3.692  1.00 31.89 ?  474 HOH   A O    1 
HETATM 7573 O O    . HOH   E 4 .   ? 28.755 -4.793  -12.416 1.00 45.98 ?  475 HOH   A O    1 
HETATM 7574 O O    . HOH   E 4 .   ? 41.765 9.211   -3.560  1.00 40.68 ?  476 HOH   A O    1 
HETATM 7575 O O    . HOH   E 4 .   ? 39.844 -7.076  -3.344  1.00 42.66 ?  477 HOH   A O    1 
HETATM 7576 O O    . HOH   E 4 .   ? 12.156 1.587   17.021  1.00 44.01 ?  478 HOH   A O    1 
HETATM 7577 O O    . HOH   E 4 .   ? 44.100 10.051  -2.163  1.00 38.33 ?  479 HOH   A O    1 
HETATM 7578 O O    B HOH   E 4 .   ? 18.285 7.857   -3.936  0.58 32.90 ?  480 HOH   A O    1 
HETATM 7579 O O    . HOH   E 4 .   ? 35.121 7.553   12.176  1.00 47.48 ?  481 HOH   A O    1 
HETATM 7580 O O    . HOH   E 4 .   ? 28.780 8.977   17.674  1.00 47.03 ?  482 HOH   A O    1 
HETATM 7581 O O    . HOH   E 4 .   ? 23.162 11.959  -4.159  1.00 23.88 ?  483 HOH   A O    1 
HETATM 7582 O O    . HOH   E 4 .   ? 15.933 -17.303 -7.111  1.00 38.37 ?  484 HOH   A O    1 
HETATM 7583 O O    . HOH   E 4 .   ? 41.052 -4.020  -0.346  1.00 39.54 ?  485 HOH   A O    1 
HETATM 7584 O O    . HOH   E 4 .   ? 17.356 -18.786 19.785  1.00 55.35 ?  486 HOH   A O    1 
HETATM 7585 O O    . HOH   E 4 .   ? 14.059 -10.304 -11.048 1.00 37.86 ?  487 HOH   A O    1 
HETATM 7586 O O    . HOH   E 4 .   ? 30.670 0.735   19.201  1.00 41.76 ?  488 HOH   A O    1 
HETATM 7587 O O    B HOH   E 4 .   ? 14.814 5.875   -4.883  0.58 29.60 ?  489 HOH   A O    1 
HETATM 7588 O O    . HOH   E 4 .   ? 13.756 -25.018 9.035   1.00 39.38 ?  490 HOH   A O    1 
HETATM 7589 O O    . HOH   E 4 .   ? 16.845 -20.447 16.101  1.00 40.74 ?  491 HOH   A O    1 
HETATM 7590 O O    . HOH   E 4 .   ? 28.880 -8.102  -15.260 1.00 55.85 ?  492 HOH   A O    1 
HETATM 7591 O O    . HOH   E 4 .   ? 39.229 2.377   7.169   1.00 33.69 ?  493 HOH   A O    1 
HETATM 7592 O O    . HOH   E 4 .   ? 23.162 -12.830 19.245  1.00 56.17 ?  494 HOH   A O    1 
HETATM 7593 O O    . HOH   E 4 .   ? 18.479 -23.102 1.837   1.00 54.35 ?  495 HOH   A O    1 
HETATM 7594 O O    . HOH   E 4 .   ? 31.751 -0.672  -10.506 1.00 28.29 ?  496 HOH   A O    1 
HETATM 7595 O O    . HOH   E 4 .   ? 20.685 -16.008 -7.620  1.00 33.06 ?  497 HOH   A O    1 
HETATM 7596 O O    . HOH   E 4 .   ? 25.841 -18.926 -11.934 1.00 44.40 ?  498 HOH   A O    1 
HETATM 7597 O O    . HOH   E 4 .   ? 40.781 -0.230  -7.670  1.00 34.40 ?  499 HOH   A O    1 
HETATM 7598 O O    . HOH   E 4 .   ? 16.263 -23.402 5.760   1.00 31.88 ?  500 HOH   A O    1 
HETATM 7599 O O    . HOH   E 4 .   ? 20.194 -22.357 4.243   1.00 34.17 ?  501 HOH   A O    1 
HETATM 7600 O O    . HOH   E 4 .   ? 39.499 -0.070  6.689   1.00 36.44 ?  502 HOH   A O    1 
HETATM 7601 O O    . HOH   E 4 .   ? 30.850 -5.897  -11.909 1.00 51.68 ?  503 HOH   A O    1 
HETATM 7602 O O    . HOH   E 4 .   ? 30.864 5.733   -14.799 1.00 40.44 ?  504 HOH   A O    1 
HETATM 7603 O O    . HOH   E 4 .   ? 8.145  -3.139  -5.865  1.00 50.26 ?  505 HOH   A O    1 
HETATM 7604 O O    B HOH   E 4 .   ? 14.759 7.839   4.704   0.58 28.38 ?  506 HOH   A O    1 
HETATM 7605 O O    . HOH   E 4 .   ? 37.396 -6.630  7.561   1.00 26.47 ?  507 HOH   A O    1 
HETATM 7606 O O    . HOH   E 4 .   ? 28.976 14.449  0.868   1.00 52.70 ?  508 HOH   A O    1 
HETATM 7607 O O    . HOH   E 4 .   ? 37.935 14.020  6.615   1.00 17.11 ?  509 HOH   A O    1 
HETATM 7608 O O    . HOH   E 4 .   ? 36.469 -6.369  10.271  1.00 49.39 ?  510 HOH   A O    1 
HETATM 7609 O O    . HOH   E 4 .   ? 22.131 -23.987 4.506   1.00 28.20 ?  511 HOH   A O    1 
HETATM 7610 O O    T HOH   E 4 .   ? 11.984 -2.163  -3.802  0.20 15.79 ?  512 HOH   A O    1 
HETATM 7611 O O    B HOH   E 4 .   ? 14.828 7.227   -7.345  0.58 28.35 ?  513 HOH   A O    1 
HETATM 7612 O O    . HOH   E 4 .   ? 17.384 -7.323  -14.238 1.00 59.82 ?  514 HOH   A O    1 
HETATM 7613 O O    A HOH   E 4 .   ? 14.877 8.645   4.742   0.42 31.70 ?  515 HOH   A O    1 
HETATM 7614 O O    . HOH   E 4 .   ? 24.068 8.922   -7.178  1.00 53.65 ?  516 HOH   A O    1 
HETATM 7615 O O    . HOH   E 4 .   ? 15.745 -12.415 27.239  1.00 51.75 ?  517 HOH   A O    1 
HETATM 7616 O O    . HOH   E 4 .   ? 16.351 -21.078 18.678  1.00 42.05 ?  518 HOH   A O    1 
HETATM 7617 O O    B HOH   E 4 .   ? 8.294  7.128   1.930   0.58 34.86 ?  519 HOH   A O    1 
HETATM 7618 O O    . HOH   E 4 .   ? 14.727 -22.715 19.807  1.00 39.90 ?  520 HOH   A O    1 
HETATM 7619 O O    . HOH   F 4 .   ? 29.913 -22.430 5.524   1.00 22.09 ?  201 HOH   B O    1 
HETATM 7620 O O    . HOH   F 4 .   ? 27.685 -29.099 -1.876  1.00 36.49 ?  202 HOH   B O    1 
HETATM 7621 O O    . HOH   F 4 .   ? 38.035 -39.484 -0.151  1.00 44.70 ?  203 HOH   B O    1 
HETATM 7622 O O    . HOH   F 4 .   ? 41.726 -36.096 -17.134 1.00 35.45 ?  204 HOH   B O    1 
HETATM 7623 O O    . HOH   F 4 .   ? 30.109 -26.286 4.209   1.00 30.45 ?  205 HOH   B O    1 
HETATM 7624 O O    . HOH   F 4 .   ? 37.357 -19.731 -18.117 1.00 40.55 ?  206 HOH   B O    1 
HETATM 7625 O O    . HOH   F 4 .   ? 54.583 -9.478  -8.634  1.00 18.71 ?  207 HOH   B O    1 
HETATM 7626 O O    . HOH   F 4 .   ? 59.193 -18.780 6.884   1.00 34.27 ?  208 HOH   B O    1 
HETATM 7627 O O    . HOH   F 4 .   ? 30.978 -28.731 4.414   1.00 32.15 ?  209 HOH   B O    1 
HETATM 7628 O O    . HOH   F 4 .   ? 30.259 -41.007 -8.040  1.00 18.06 ?  210 HOH   B O    1 
HETATM 7629 O O    . HOH   F 4 .   ? 57.759 -24.532 4.965   1.00 39.12 ?  211 HOH   B O    1 
HETATM 7630 O O    . HOH   F 4 .   ? 29.686 -34.007 -0.291  1.00 36.64 ?  212 HOH   B O    1 
HETATM 7631 O O    . HOH   F 4 .   ? 34.878 -24.721 13.854  1.00 37.44 ?  213 HOH   B O    1 
HETATM 7632 O O    . HOH   F 4 .   ? 47.441 -7.356  -3.875  1.00 45.57 ?  214 HOH   B O    1 
HETATM 7633 O O    . HOH   F 4 .   ? 34.608 -36.438 -7.124  1.00 19.86 ?  215 HOH   B O    1 
HETATM 7634 O O    . HOH   F 4 .   ? 49.573 -22.747 -19.776 1.00 49.43 ?  216 HOH   B O    1 
HETATM 7635 O O    . HOH   F 4 .   ? 41.521 -39.206 -14.768 1.00 25.41 ?  217 HOH   B O    1 
HETATM 7636 O O    . HOH   F 4 .   ? 56.730 -30.873 -7.764  1.00 26.79 ?  218 HOH   B O    1 
HETATM 7637 O O    . HOH   F 4 .   ? 56.441 -19.745 7.278   1.00 32.17 ?  219 HOH   B O    1 
HETATM 7638 O O    . HOH   F 4 .   ? 58.245 -12.967 8.430   1.00 26.89 ?  220 HOH   B O    1 
HETATM 7639 O O    . HOH   F 4 .   ? 44.562 -7.312  2.101   1.00 34.53 ?  221 HOH   B O    1 
HETATM 7640 O O    . HOH   F 4 .   ? 26.589 -19.339 -1.814  1.00 15.23 ?  222 HOH   B O    1 
HETATM 7641 O O    . HOH   F 4 .   ? 27.896 -41.849 -15.190 1.00 39.08 ?  223 HOH   B O    1 
HETATM 7642 O O    . HOH   F 4 .   ? 44.949 -43.590 -10.492 1.00 28.06 ?  224 HOH   B O    1 
HETATM 7643 O O    . HOH   F 4 .   ? 41.246 -7.896  5.403   1.00 39.66 ?  225 HOH   B O    1 
HETATM 7644 O O    . HOH   F 4 .   ? 41.450 -9.731  13.125  1.00 22.17 ?  226 HOH   B O    1 
HETATM 7645 O O    . HOH   F 4 .   ? 44.576 -27.763 -0.663  1.00 22.26 ?  227 HOH   B O    1 
HETATM 7646 O O    . HOH   F 4 .   ? 45.212 -34.920 6.769   1.00 45.42 ?  228 HOH   B O    1 
HETATM 7647 O O    . HOH   F 4 .   ? 50.111 -3.421  7.084   1.00 33.02 ?  229 HOH   B O    1 
HETATM 7648 O O    . HOH   F 4 .   ? 35.221 -8.069  -2.951  1.00 18.18 ?  230 HOH   B O    1 
HETATM 7649 O O    . HOH   F 4 .   ? 57.393 -16.311 -12.322 1.00 16.74 ?  231 HOH   B O    1 
HETATM 7650 O O    . HOH   F 4 .   ? 40.676 -16.054 14.058  1.00 20.96 ?  232 HOH   B O    1 
HETATM 7651 O O    . HOH   F 4 .   ? 48.163 -24.679 -17.790 1.00 30.85 ?  233 HOH   B O    1 
HETATM 7652 O O    . HOH   F 4 .   ? 32.223 -9.262  -6.570  1.00 24.72 ?  234 HOH   B O    1 
HETATM 7653 O O    . HOH   F 4 .   ? 29.796 -25.214 -10.747 1.00 18.99 ?  235 HOH   B O    1 
HETATM 7654 O O    . HOH   F 4 .   ? 50.663 -6.110  0.134   1.00 27.86 ?  236 HOH   B O    1 
HETATM 7655 O O    . HOH   F 4 .   ? 41.923 -23.597 9.347   1.00 21.30 ?  237 HOH   B O    1 
HETATM 7656 O O    . HOH   F 4 .   ? 46.369 -1.703  13.378  1.00 28.88 ?  238 HOH   B O    1 
HETATM 7657 O O    . HOH   F 4 .   ? 36.057 -43.440 -8.346  1.00 47.01 ?  239 HOH   B O    1 
HETATM 7658 O O    . HOH   F 4 .   ? 28.561 -19.676 -13.238 1.00 27.14 ?  240 HOH   B O    1 
HETATM 7659 O O    . HOH   F 4 .   ? 32.837 -43.817 -11.263 1.00 24.50 ?  241 HOH   B O    1 
HETATM 7660 O O    . HOH   F 4 .   ? 42.632 -25.387 2.655   1.00 15.86 ?  242 HOH   B O    1 
HETATM 7661 O O    . HOH   F 4 .   ? 47.960 -6.966  15.534  1.00 31.81 ?  243 HOH   B O    1 
HETATM 7662 O O    . HOH   F 4 .   ? 33.615 -16.937 8.154   1.00 20.49 ?  244 HOH   B O    1 
HETATM 7663 O O    . HOH   F 4 .   ? 50.999 -40.012 -8.077  1.00 37.02 ?  245 HOH   B O    1 
HETATM 7664 O O    . HOH   F 4 .   ? 39.339 -10.848 6.081   1.00 23.80 ?  246 HOH   B O    1 
HETATM 7665 O O    . HOH   F 4 .   ? 53.162 -13.431 -20.333 1.00 40.91 ?  247 HOH   B O    1 
HETATM 7666 O O    . HOH   F 4 .   ? 50.836 -13.016 -0.433  1.00 12.33 ?  248 HOH   B O    1 
HETATM 7667 O O    . HOH   F 4 .   ? 55.266 -16.406 -14.248 1.00 20.73 ?  249 HOH   B O    1 
HETATM 7668 O O    . HOH   F 4 .   ? 57.691 -24.427 -3.776  1.00 22.54 ?  250 HOH   B O    1 
HETATM 7669 O O    . HOH   F 4 .   ? 56.257 -23.685 -14.657 1.00 29.05 ?  251 HOH   B O    1 
HETATM 7670 O O    . HOH   F 4 .   ? 42.693 -22.877 3.893   1.00 11.94 ?  252 HOH   B O    1 
HETATM 7671 O O    . HOH   F 4 .   ? 48.668 -36.613 -15.523 1.00 48.99 ?  253 HOH   B O    1 
HETATM 7672 O O    . HOH   F 4 .   ? 43.064 -43.290 -8.113  1.00 29.93 ?  254 HOH   B O    1 
HETATM 7673 O O    . HOH   F 4 .   ? 51.647 -6.550  4.327   1.00 20.41 ?  255 HOH   B O    1 
HETATM 7674 O O    . HOH   F 4 .   ? 40.522 -12.799 -11.562 1.00 15.39 ?  256 HOH   B O    1 
HETATM 7675 O O    . HOH   F 4 .   ? 39.615 -11.143 0.281   1.00 16.00 ?  257 HOH   B O    1 
HETATM 7676 O O    . HOH   F 4 .   ? 57.295 -26.882 -7.618  1.00 45.16 ?  258 HOH   B O    1 
HETATM 7677 O O    . HOH   F 4 .   ? 38.574 -11.120 -2.294  1.00 18.97 ?  259 HOH   B O    1 
HETATM 7678 O O    . HOH   F 4 .   ? 58.272 -10.641 -4.059  1.00 20.82 ?  260 HOH   B O    1 
HETATM 7679 O O    . HOH   F 4 .   ? 25.436 -25.927 -1.235  1.00 33.23 ?  261 HOH   B O    1 
HETATM 7680 O O    . HOH   F 4 .   ? 30.913 -15.716 2.678   1.00 14.17 ?  262 HOH   B O    1 
HETATM 7681 O O    . HOH   F 4 .   ? 48.075 -22.794 5.828   1.00 18.90 ?  263 HOH   B O    1 
HETATM 7682 O O    . HOH   F 4 .   ? 27.163 -31.833 -9.912  1.00 21.50 ?  264 HOH   B O    1 
HETATM 7683 O O    . HOH   F 4 .   ? 30.613 -42.287 -10.623 1.00 33.65 ?  265 HOH   B O    1 
HETATM 7684 O O    . HOH   F 4 .   ? 49.399 -28.765 -6.898  1.00 16.16 ?  266 HOH   B O    1 
HETATM 7685 O O    . HOH   F 4 .   ? 49.545 -0.466  10.231  1.00 29.33 ?  267 HOH   B O    1 
HETATM 7686 O O    . HOH   F 4 .   ? 31.875 -17.910 -14.571 1.00 29.88 ?  268 HOH   B O    1 
HETATM 7687 O O    . HOH   F 4 .   ? 28.522 -30.832 -14.819 1.00 32.10 ?  269 HOH   B O    1 
HETATM 7688 O O    . HOH   F 4 .   ? 34.292 -18.342 11.484  1.00 27.52 ?  270 HOH   B O    1 
HETATM 7689 O O    . HOH   F 4 .   ? 43.241 -32.417 -17.074 1.00 24.19 ?  271 HOH   B O    1 
HETATM 7690 O O    . HOH   F 4 .   ? 57.525 -9.237  1.424   1.00 20.32 ?  272 HOH   B O    1 
HETATM 7691 O O    . HOH   F 4 .   ? 56.947 -8.608  8.428   1.00 19.47 ?  273 HOH   B O    1 
HETATM 7692 O O    . HOH   F 4 .   ? 48.600 -12.171 -14.672 1.00 20.73 ?  274 HOH   B O    1 
HETATM 7693 O O    . HOH   F 4 .   ? 43.530 -15.823 -12.228 1.00 14.18 ?  275 HOH   B O    1 
HETATM 7694 O O    . HOH   F 4 .   ? 28.275 -34.328 -9.309  1.00 20.23 ?  276 HOH   B O    1 
HETATM 7695 O O    . HOH   F 4 .   ? 46.663 -31.284 -4.757  1.00 19.68 ?  277 HOH   B O    1 
HETATM 7696 O O    . HOH   F 4 .   ? 34.529 -12.788 2.613   1.00 22.06 ?  278 HOH   B O    1 
HETATM 7697 O O    . HOH   F 4 .   ? 48.451 -25.078 3.135   1.00 14.21 ?  279 HOH   B O    1 
HETATM 7698 O O    . HOH   F 4 .   ? 38.932 -11.799 12.414  1.00 33.38 ?  280 HOH   B O    1 
HETATM 7699 O O    . HOH   F 4 .   ? 36.858 -12.786 -1.549  1.00 24.47 ?  281 HOH   B O    1 
HETATM 7700 O O    . HOH   F 4 .   ? 50.055 -24.685 5.828   1.00 34.60 ?  282 HOH   B O    1 
HETATM 7701 O O    . HOH   F 4 .   ? 42.350 -10.013 9.314   1.00 19.71 ?  283 HOH   B O    1 
HETATM 7702 O O    . HOH   F 4 .   ? 42.475 -34.692 3.828   1.00 30.23 ?  284 HOH   B O    1 
HETATM 7703 O O    . HOH   F 4 .   ? 51.515 -13.840 11.156  1.00 25.61 ?  285 HOH   B O    1 
HETATM 7704 O O    . HOH   F 4 .   ? 53.812 -12.761 -22.143 1.00 30.83 ?  286 HOH   B O    1 
HETATM 7705 O O    . HOH   F 4 .   ? 51.731 -5.947  -7.938  1.00 38.14 ?  287 HOH   B O    1 
HETATM 7706 O O    . HOH   F 4 .   ? 28.050 -22.870 -7.968  1.00 18.85 ?  288 HOH   B O    1 
HETATM 7707 O O    . HOH   F 4 .   ? 47.003 -29.590 9.859   1.00 31.90 ?  289 HOH   B O    1 
HETATM 7708 O O    . HOH   F 4 .   ? 43.114 -20.081 -20.703 1.00 29.03 ?  290 HOH   B O    1 
HETATM 7709 O O    . HOH   F 4 .   ? 47.138 -34.023 -4.578  1.00 18.83 ?  291 HOH   B O    1 
HETATM 7710 O O    . HOH   F 4 .   ? 45.365 -33.478 -15.888 1.00 24.38 ?  292 HOH   B O    1 
HETATM 7711 O O    . HOH   F 4 .   ? 48.787 -20.087 5.973   1.00 14.44 ?  293 HOH   B O    1 
HETATM 7712 O O    . HOH   F 4 .   ? 27.653 -26.622 -15.588 1.00 34.28 ?  294 HOH   B O    1 
HETATM 7713 O O    . HOH   F 4 .   ? 33.659 -15.309 -13.972 1.00 22.33 ?  295 HOH   B O    1 
HETATM 7714 O O    . HOH   F 4 .   ? 35.029 -33.407 -19.207 1.00 28.18 ?  296 HOH   B O    1 
HETATM 7715 O O    . HOH   F 4 .   ? 57.182 -12.124 12.405  1.00 38.80 ?  297 HOH   B O    1 
HETATM 7716 O O    . HOH   F 4 .   ? 52.582 -35.749 -8.692  1.00 31.41 ?  298 HOH   B O    1 
HETATM 7717 O O    . HOH   F 4 .   ? 53.006 -15.940 -12.772 1.00 19.26 ?  299 HOH   B O    1 
HETATM 7718 O O    . HOH   F 4 .   ? 40.418 -10.924 -9.552  1.00 17.21 ?  300 HOH   B O    1 
HETATM 7719 O O    . HOH   F 4 .   ? 45.910 -40.439 -3.541  1.00 31.97 ?  301 HOH   B O    1 
HETATM 7720 O O    . HOH   F 4 .   ? 51.262 -37.648 -9.608  1.00 28.92 ?  302 HOH   B O    1 
HETATM 7721 O O    . HOH   F 4 .   ? 52.443 -10.398 13.006  1.00 25.94 ?  303 HOH   B O    1 
HETATM 7722 O O    . HOH   F 4 .   ? 62.745 -13.589 4.764   1.00 29.48 ?  304 HOH   B O    1 
HETATM 7723 O O    . HOH   F 4 .   ? 44.694 -27.485 2.030   1.00 16.15 ?  305 HOH   B O    1 
HETATM 7724 O O    . HOH   F 4 .   ? 59.826 -15.201 8.226   1.00 32.88 ?  306 HOH   B O    1 
HETATM 7725 O O    . HOH   F 4 .   ? 43.087 -12.031 -18.473 1.00 21.85 ?  307 HOH   B O    1 
HETATM 7726 O O    . HOH   F 4 .   ? 38.019 -10.293 -10.781 1.00 17.97 ?  308 HOH   B O    1 
HETATM 7727 O O    . HOH   F 4 .   ? 26.023 -21.460 -3.501  1.00 17.92 ?  309 HOH   B O    1 
HETATM 7728 O O    . HOH   F 4 .   ? 44.101 -29.374 -4.611  1.00 24.18 ?  310 HOH   B O    1 
HETATM 7729 O O    . HOH   F 4 .   ? 37.442 -17.910 13.142  1.00 33.71 ?  311 HOH   B O    1 
HETATM 7730 O O    . HOH   F 4 .   ? 60.247 -17.207 -10.232 1.00 37.85 ?  312 HOH   B O    1 
HETATM 7731 O O    . HOH   F 4 .   ? 43.244 -21.484 10.686  1.00 17.21 ?  313 HOH   B O    1 
HETATM 7732 O O    . HOH   F 4 .   ? 43.567 -15.455 18.118  1.00 26.22 ?  314 HOH   B O    1 
HETATM 7733 O O    . HOH   F 4 .   ? 41.857 -8.091  1.360   1.00 23.72 ?  315 HOH   B O    1 
HETATM 7734 O O    . HOH   F 4 .   ? 41.158 -5.525  11.391  1.00 47.21 ?  316 HOH   B O    1 
HETATM 7735 O O    . HOH   F 4 .   ? 48.165 -32.778 -16.558 1.00 44.34 ?  317 HOH   B O    1 
HETATM 7736 O O    . HOH   F 4 .   ? 51.425 -33.081 -10.763 1.00 46.20 ?  318 HOH   B O    1 
HETATM 7737 O O    . HOH   F 4 .   ? 38.346 -12.639 7.985   1.00 18.26 ?  319 HOH   B O    1 
HETATM 7738 O O    . HOH   F 4 .   ? 53.484 -30.261 4.621   1.00 18.72 ?  320 HOH   B O    1 
HETATM 7739 O O    . HOH   F 4 .   ? 35.078 -33.549 4.674   1.00 34.95 ?  321 HOH   B O    1 
HETATM 7740 O O    . HOH   F 4 .   ? 33.649 -31.066 11.100  1.00 39.87 ?  322 HOH   B O    1 
HETATM 7741 O O    . HOH   F 4 .   ? 37.163 -30.685 -20.986 1.00 35.66 ?  323 HOH   B O    1 
HETATM 7742 O O    . HOH   F 4 .   ? 52.564 -29.311 -13.056 1.00 27.28 ?  324 HOH   B O    1 
HETATM 7743 O O    . HOH   F 4 .   ? 32.851 -34.637 -5.839  1.00 17.54 ?  325 HOH   B O    1 
HETATM 7744 O O    . HOH   F 4 .   ? 26.422 -21.039 -6.241  1.00 17.36 ?  326 HOH   B O    1 
HETATM 7745 O O    . HOH   F 4 .   ? 37.308 -35.709 7.217   1.00 35.61 ?  327 HOH   B O    1 
HETATM 7746 O O    . HOH   F 4 .   ? 63.076 -20.075 -0.687  1.00 43.84 ?  328 HOH   B O    1 
HETATM 7747 O O    . HOH   F 4 .   ? 44.019 -1.817  7.768   1.00 49.66 ?  329 HOH   B O    1 
HETATM 7748 O O    . HOH   F 4 .   ? 45.802 -36.388 -16.058 1.00 35.77 ?  330 HOH   B O    1 
HETATM 7749 O O    . HOH   F 4 .   ? 44.742 -24.605 9.600   1.00 25.76 ?  331 HOH   B O    1 
HETATM 7750 O O    . HOH   F 4 .   ? 27.801 -14.751 -9.513  1.00 40.24 ?  332 HOH   B O    1 
HETATM 7751 O O    . HOH   F 4 .   ? 42.545 -9.728  -14.917 1.00 38.72 ?  333 HOH   B O    1 
HETATM 7752 O O    . HOH   F 4 .   ? 36.782 -12.408 4.267   1.00 17.87 ?  334 HOH   B O    1 
HETATM 7753 O O    . HOH   F 4 .   ? 41.386 -24.627 15.809  1.00 49.93 ?  335 HOH   B O    1 
HETATM 7754 O O    . HOH   F 4 .   ? 47.324 -24.524 8.210   1.00 29.77 ?  336 HOH   B O    1 
HETATM 7755 O O    . HOH   F 4 .   ? 57.635 -21.999 3.371   1.00 34.01 ?  337 HOH   B O    1 
HETATM 7756 O O    . HOH   F 4 .   ? 42.998 -43.523 -14.360 1.00 45.98 ?  338 HOH   B O    1 
HETATM 7757 O O    . HOH   F 4 .   ? 43.187 -34.650 0.118   1.00 24.71 ?  339 HOH   B O    1 
HETATM 7758 O O    . HOH   F 4 .   ? 39.651 -23.418 -20.353 1.00 35.44 ?  340 HOH   B O    1 
HETATM 7759 O O    . HOH   F 4 .   ? 37.198 -15.222 -16.638 1.00 44.40 ?  341 HOH   B O    1 
HETATM 7760 O O    . HOH   F 4 .   ? 47.535 -27.478 2.053   1.00 15.77 ?  342 HOH   B O    1 
HETATM 7761 O O    . HOH   F 4 .   ? 38.537 -9.407  -13.275 1.00 28.38 ?  343 HOH   B O    1 
HETATM 7762 O O    . HOH   F 4 .   ? 28.905 -42.858 -12.321 1.00 37.35 ?  344 HOH   B O    1 
HETATM 7763 O O    . HOH   F 4 .   ? 34.470 -10.337 7.763   1.00 23.16 ?  345 HOH   B O    1 
HETATM 7764 O O    . HOH   F 4 .   ? 46.776 -20.020 12.351  1.00 27.71 ?  346 HOH   B O    1 
HETATM 7765 O O    . HOH   F 4 .   ? 37.181 -45.317 -9.721  1.00 37.81 ?  347 HOH   B O    1 
HETATM 7766 O O    . HOH   F 4 .   ? 38.600 -22.594 15.074  1.00 49.72 ?  348 HOH   B O    1 
HETATM 7767 O O    . HOH   F 4 .   ? 33.057 -14.701 1.073   1.00 20.68 ?  349 HOH   B O    1 
HETATM 7768 O O    . HOH   F 4 .   ? 38.690 -12.249 -16.209 1.00 44.66 ?  350 HOH   B O    1 
HETATM 7769 O O    . HOH   F 4 .   ? 40.444 -43.516 -9.073  1.00 27.36 ?  351 HOH   B O    1 
HETATM 7770 O O    . HOH   F 4 .   ? 44.279 -37.328 -17.651 1.00 35.84 ?  352 HOH   B O    1 
HETATM 7771 O O    . HOH   F 4 .   ? 23.378 -23.668 6.845   1.00 36.74 ?  353 HOH   B O    1 
HETATM 7772 O O    . HOH   F 4 .   ? 62.632 -19.972 -4.805  1.00 53.33 ?  354 HOH   B O    1 
HETATM 7773 O O    . HOH   F 4 .   ? 33.967 -9.227  -8.908  1.00 27.00 ?  355 HOH   B O    1 
HETATM 7774 O O    . HOH   F 4 .   ? 39.837 -44.388 -11.232 1.00 42.84 ?  356 HOH   B O    1 
HETATM 7775 O O    . HOH   F 4 .   ? 27.886 -26.606 -0.459  1.00 28.49 ?  357 HOH   B O    1 
HETATM 7776 O O    . HOH   F 4 .   ? 36.395 -8.557  -9.662  1.00 32.40 ?  358 HOH   B O    1 
HETATM 7777 O O    . HOH   F 4 .   ? 55.691 -8.253  10.865  1.00 23.03 ?  359 HOH   B O    1 
HETATM 7778 O O    . HOH   F 4 .   ? 43.331 -12.839 -21.163 1.00 26.73 ?  360 HOH   B O    1 
HETATM 7779 O O    . HOH   F 4 .   ? 56.580 -7.260  3.004   1.00 30.06 ?  361 HOH   B O    1 
HETATM 7780 O O    . HOH   F 4 .   ? 34.189 -7.698  11.446  1.00 41.99 ?  362 HOH   B O    1 
HETATM 7781 O O    . HOH   F 4 .   ? 56.922 -21.616 -16.391 1.00 43.66 ?  363 HOH   B O    1 
HETATM 7782 O O    . HOH   F 4 .   ? 61.605 -19.860 1.899   1.00 40.67 ?  364 HOH   B O    1 
HETATM 7783 O O    . HOH   F 4 .   ? 27.264 -25.951 -11.428 1.00 36.85 ?  365 HOH   B O    1 
HETATM 7784 O O    . HOH   F 4 .   ? 40.279 -8.827  9.791   1.00 39.74 ?  366 HOH   B O    1 
HETATM 7785 O O    . HOH   F 4 .   ? 40.534 -11.320 -14.037 1.00 29.23 ?  367 HOH   B O    1 
HETATM 7786 O O    . HOH   F 4 .   ? 48.341 -26.465 8.860   1.00 50.93 ?  368 HOH   B O    1 
HETATM 7787 O O    . HOH   F 4 .   ? 36.164 -8.649  9.052   1.00 39.26 ?  369 HOH   B O    1 
HETATM 7788 O O    . HOH   F 4 .   ? 54.323 -5.767  3.039   1.00 36.51 ?  370 HOH   B O    1 
HETATM 7789 O O    . HOH   F 4 .   ? 39.949 -7.074  7.756   1.00 39.58 ?  371 HOH   B O    1 
HETATM 7790 O O    . HOH   F 4 .   ? 32.755 -23.655 14.047  1.00 40.27 ?  372 HOH   B O    1 
HETATM 7791 O O    . HOH   F 4 .   ? 58.964 -10.356 9.241   1.00 40.62 ?  373 HOH   B O    1 
HETATM 7792 O O    . HOH   F 4 .   ? 62.926 -12.333 6.984   1.00 41.23 ?  374 HOH   B O    1 
HETATM 7793 O O    . HOH   F 4 .   ? 40.221 -7.847  3.191   1.00 45.27 ?  375 HOH   B O    1 
HETATM 7794 O O    . HOH   F 4 .   ? 56.145 -7.819  -0.595  1.00 35.83 ?  376 HOH   B O    1 
HETATM 7795 O O    . HOH   F 4 .   ? 41.929 -10.023 -17.431 1.00 64.63 ?  377 HOH   B O    1 
HETATM 7796 O O    . HOH   F 4 .   ? 42.016 -6.701  -4.910  1.00 46.67 ?  378 HOH   B O    1 
HETATM 7797 O O    . HOH   F 4 .   ? 36.570 -22.898 13.339  1.00 31.72 ?  379 HOH   B O    1 
HETATM 7798 O O    . HOH   F 4 .   ? 42.831 -17.201 -23.192 1.00 43.92 ?  380 HOH   B O    1 
HETATM 7799 O O    . HOH   F 4 .   ? 52.003 -13.018 13.480  1.00 23.15 ?  381 HOH   B O    1 
HETATM 7800 O O    . HOH   F 4 .   ? 38.056 -10.500 9.999   1.00 26.87 ?  382 HOH   B O    1 
HETATM 7801 O O    . HOH   F 4 .   ? 44.318 -5.688  -3.481  1.00 44.08 ?  383 HOH   B O    1 
HETATM 7802 O O    . HOH   F 4 .   ? 46.628 -5.424  2.899   1.00 35.01 ?  384 HOH   B O    1 
HETATM 7803 O O    . HOH   F 4 .   ? 52.937 -29.891 7.274   1.00 23.82 ?  385 HOH   B O    1 
HETATM 7804 O O    . HOH   F 4 .   ? 39.668 -14.032 15.640  1.00 41.23 ?  386 HOH   B O    1 
HETATM 7805 O O    . HOH   F 4 .   ? 60.496 -22.336 2.967   1.00 39.43 ?  387 HOH   B O    1 
HETATM 7806 O O    . HOH   F 4 .   ? 35.383 -33.715 7.310   1.00 47.48 ?  388 HOH   B O    1 
HETATM 7807 O O    . HOH   F 4 .   ? 23.408 -23.784 1.565   1.00 35.63 ?  389 HOH   B O    1 
HETATM 7808 O O    . HOH   F 4 .   ? 41.088 -9.854  15.894  1.00 40.72 ?  390 HOH   B O    1 
HETATM 7809 O O    . HOH   F 4 .   ? 24.031 -20.931 -7.710  1.00 29.71 ?  391 HOH   B O    1 
HETATM 7810 O O    . HOH   F 4 .   ? 40.868 -6.572  -0.799  1.00 25.49 ?  392 HOH   B O    1 
HETATM 7811 O O    . HOH   F 4 .   ? 35.359 -20.413 13.371  1.00 34.48 ?  393 HOH   B O    1 
HETATM 7812 O O    . HOH   F 4 .   ? 44.212 -31.739 -3.769  1.00 40.84 ?  394 HOH   B O    1 
HETATM 7813 O O    . HOH   F 4 .   ? 28.079 -27.053 2.300   1.00 30.57 ?  395 HOH   B O    1 
HETATM 7814 O O    . HOH   F 4 .   ? 26.776 -28.038 -13.587 1.00 37.04 ?  396 HOH   B O    1 
HETATM 7815 O O    . HOH   F 4 .   ? 24.763 -20.519 -10.585 1.00 44.56 ?  397 HOH   B O    1 
HETATM 7816 O O    . HOH   F 4 .   ? 34.346 -33.468 9.624   1.00 43.35 ?  398 HOH   B O    1 
HETATM 7817 O O    . HOH   F 4 .   ? 50.725 -30.943 8.791   1.00 31.77 ?  399 HOH   B O    1 
HETATM 7818 O O    . HOH   F 4 .   ? 26.885 -30.642 -12.542 1.00 29.96 ?  400 HOH   B O    1 
HETATM 7819 O O    . HOH   F 4 .   ? 57.798 -6.585  -2.286  1.00 36.04 ?  401 HOH   B O    1 
HETATM 7820 O O    . HOH   F 4 .   ? 45.768 -20.041 15.347  1.00 41.02 ?  402 HOH   B O    1 
HETATM 7821 O O    . HOH   F 4 .   ? 41.091 -11.869 -22.384 1.00 33.55 ?  403 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   ? 0.7234 0.7212 0.8331 0.0056  -0.0116 0.0623  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.7340 0.7026 0.8326 -0.0031 -0.0034 0.0593  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.7195 0.7174 0.8239 0.0038  -0.0115 0.0619  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.7291 0.6980 0.8180 -0.0044 -0.0037 0.0597  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.7014 0.6999 0.7811 -0.0035 -0.0144 0.0628  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.7078 0.6769 0.7595 -0.0107 -0.0086 0.0595  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.7046 0.7029 0.7953 -0.0026 -0.0157 0.0645  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.7117 0.6808 0.7738 -0.0101 -0.0096 0.0586  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.7306 0.7282 0.8486 0.0077  -0.0086 0.0608  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.7421 0.7111 0.8487 -0.0007 0.0008  0.0597  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.7344 0.7319 0.8552 0.0092  -0.0075 0.0604  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.7464 0.7152 0.8584 0.0006  0.0024  0.0596  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.7346 0.7321 0.8555 0.0090  -0.0078 0.0609  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.7468 0.7156 0.8589 0.0005  0.0024  0.0604  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.6767 0.6764 0.7149 -0.0126 -0.0154 0.0616  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.6789 0.6477 0.6724 -0.0188 -0.0111 0.0610  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.6481 0.6494 0.6407 -0.0224 -0.0165 0.0588  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.6458 0.6154 0.5769 -0.0276 -0.0140 0.0610  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.6037 0.6131 0.6031 -0.0346 -0.0072 0.0420  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.5986 0.5779 0.5221 -0.0426 0.0063  0.0512  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.6069 0.6150 0.6086 -0.0344 -0.0079 0.0421  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.6012 0.5804 0.5175 -0.0429 0.0074  0.0519  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.6606 0.6562 0.5987 -0.0205 -0.0256 0.0721  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.6574 0.6184 0.5348 -0.0231 -0.0355 0.0715  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.6699 0.6608 0.5596 -0.0193 -0.0333 0.0834  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.6657 0.6198 0.4939 -0.0197 -0.0548 0.0800  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.6735 0.6624 0.5458 -0.0192 -0.0370 0.0879  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.6685 0.6192 0.4769 -0.0181 -0.0646 0.0848  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.6726 0.6621 0.5484 -0.0189 -0.0356 0.0883  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.6677 0.6201 0.4817 -0.0183 -0.0599 0.0835  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.5534 0.5731 0.5537 -0.0482 0.0033  0.0254  5   SER   A N   
60   N N   B SER   A 5   ? 0.5464 0.5362 0.4684 -0.0576 0.0267  0.0425  5   SER   A N   
61   C CA  A SER   A 5   ? 0.5013 0.5319 0.5010 -0.0599 0.0164  0.0113  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.4933 0.4937 0.4199 -0.0718 0.0500  0.0367  5   SER   A CA  
63   C C   A SER   A 5   ? 0.4432 0.4861 0.4381 -0.0706 0.0298  0.0079  5   SER   A C   
64   C C   B SER   A 5   ? 0.4350 0.4456 0.3478 -0.0814 0.0748  0.0355  5   SER   A C   
65   O O   A SER   A 5   ? 0.4456 0.4871 0.4365 -0.0696 0.0320  0.0015  5   SER   A O   
66   O O   B SER   A 5   ? 0.4381 0.4463 0.3330 -0.0821 0.0748  0.0197  5   SER   A O   
67   C CB  A SER   A 5   ? 0.5064 0.5355 0.5138 -0.0599 0.0165  0.0039  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.4990 0.4996 0.4480 -0.0723 0.0484  0.0317  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.5098 0.5375 0.5201 -0.0594 0.0165  -0.0006 5   SER   A OG  
70   O OG  B SER   A 5   ? 0.5031 0.5025 0.4675 -0.0732 0.0451  0.0281  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.3813 0.4386 0.3689 -0.0810 0.0401  0.0136  6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3734 0.3982 0.2767 -0.0912 0.0966  0.0494  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.3219 0.3915 0.3062 -0.0871 0.0457  0.0226  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.3159 0.3555 0.2399 -0.0956 0.1056  0.0504  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.2998 0.3805 0.2923 -0.0954 0.0576  0.0210  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.3017 0.3550 0.2625 -0.0933 0.1242  0.0359  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.3019 0.3812 0.3132 -0.1013 0.0606  0.0241  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.3078 0.3587 0.3003 -0.0903 0.1295  0.0393  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2893 0.3568 0.2660 -0.0802 0.0343  0.0303  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.2809 0.3169 0.2212 -0.0889 0.0778  0.0577  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2609 0.3279 0.2427 -0.0723 0.0252  0.0351  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2509 0.2874 0.2154 -0.0751 0.0514  0.0490  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2491 0.3140 0.2348 -0.0672 0.0153  0.0322  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2385 0.2737 0.2209 -0.0702 0.0355  0.0436  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2542 0.3167 0.2411 -0.0617 0.0319  0.0421  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2468 0.2791 0.2331 -0.0636 0.0448  0.0483  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2446 0.3064 0.2393 -0.0623 0.0184  0.0369  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.2334 0.2669 0.2348 -0.0662 0.0255  0.0450  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2490 0.3107 0.2466 -0.0575 0.0391  0.0427  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2409 0.2743 0.2559 -0.0560 0.0369  0.0424  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2447 0.3052 0.2431 -0.0588 0.0263  0.0358  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.2335 0.2661 0.2479 -0.0644 0.0283  0.0360  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2774 0.3690 0.2677 -0.0948 0.0570  0.0160  7   SER   A N   
122  N N   B SER   A 7   ? 0.2816 0.3483 0.2585 -0.0905 0.1279  0.0128  7   SER   A N   
123  C CA  A SER   A 7   ? 0.2613 0.3616 0.2571 -0.0856 0.0537  0.0009  7   SER   A CA  
124  C CA  B SER   A 7   ? 0.2763 0.3471 0.2719 -0.0799 0.1103  -0.0053 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2404 0.3356 0.2484 -0.0803 0.0617  0.0042  7   SER   A C   
126  C C   B SER   A 7   ? 0.2521 0.3238 0.2346 -0.0713 0.0982  -0.0005 7   SER   A C   
127  O O   A SER   A 7   ? 0.2471 0.3327 0.2564 -0.0804 0.0630  0.0060  7   SER   A O   
128  O O   B SER   A 7   ? 0.2573 0.3197 0.2115 -0.0756 0.0990  0.0002  7   SER   A O   
129  C CB  A SER   A 7   ? 0.2706 0.3782 0.2697 -0.0798 0.0435  -0.0093 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.3016 0.3724 0.3392 -0.0752 0.0981  -0.0148 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.2798 0.3881 0.2758 -0.0760 0.0284  -0.0162 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.3090 0.3761 0.3954 -0.0691 0.0765  -0.0171 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2169 0.3126 0.2371 -0.0743 0.0627  -0.0009 8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2251 0.3050 0.2290 -0.0620 0.0830  0.0067  8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.1984 0.2875 0.2374 -0.0609 0.0569  0.0008  8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2072 0.2804 0.2382 -0.0526 0.0653  0.0208  8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1755 0.2666 0.2289 -0.0459 0.0446  -0.0042 8   GLY   A C   
148  C C   B GLY   A 8   ? 0.1788 0.2580 0.2305 -0.0374 0.0594  0.0345  8   GLY   A C   
149  O O   A GLY   A 8   ? 0.1737 0.2683 0.2539 -0.0354 0.0488  -0.0115 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.1736 0.2596 0.2532 -0.0213 0.0606  0.0276  8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1634 0.2470 0.2125 -0.0309 0.0397  0.0029  9   TYR   A N   
158  N N   B TYR   A 9   ? 0.1710 0.2395 0.2279 -0.0210 0.0523  0.0556  9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1540 0.2254 0.1966 -0.0177 0.0387  0.0136  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.1615 0.2200 0.2195 -0.0188 0.0461  0.0709  9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1512 0.2153 0.1848 -0.0140 0.0439  0.0340  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.1644 0.2040 0.2264 -0.0162 0.0421  0.0747  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1647 0.2272 0.1862 -0.0171 0.0240  0.0356  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.1790 0.2271 0.2471 -0.0185 0.0328  0.0675  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1565 0.2188 0.1926 -0.0029 0.0290  0.0037  9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.1567 0.2304 0.2230 -0.0051 0.0396  0.0647  9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1554 0.2144 0.1926 0.0036  0.0317  -0.0006 9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.1478 0.2372 0.2150 -0.0030 0.0429  0.0514  9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1608 0.2112 0.2002 0.0012  0.0380  -0.0070 9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.1617 0.2466 0.2322 -0.0077 0.0446  0.0472  9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1511 0.2099 0.1946 -0.0035 0.0201  0.0077  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1398 0.2337 0.1976 0.0019  0.0380  0.0454  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1652 0.2115 0.2106 0.0002  0.0258  -0.0056 9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.1672 0.2437 0.2320 -0.0065 0.0459  0.0401  9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1537 0.2094 0.2039 -0.0062 0.0091  0.0054  9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1427 0.2357 0.2051 0.0063  0.0326  0.0453  9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1590 0.2113 0.2242 -0.0112 0.0192  -0.0051 9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1523 0.2344 0.2117 -0.0016 0.0469  0.0507  9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1678 0.2110 0.2538 -0.0209 0.0035  -0.0130 9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.1475 0.2372 0.2192 -0.0083 0.0495  0.0542  9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1552 0.2061 0.1944 -0.0143 0.0327  0.0454  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.1715 0.1890 0.2267 -0.0189 0.0232  0.0743  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1518 0.2017 0.1990 -0.0169 0.0192  0.0550  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1678 0.1815 0.2269 -0.0224 0.0147  0.0791  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1343 0.1961 0.1836 -0.0221 0.0081  0.0429  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1624 0.1710 0.2248 -0.0347 0.0073  0.0771  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1273 0.1896 0.1684 -0.0224 0.0083  0.0355  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1642 0.1565 0.2080 -0.0294 0.0089  0.0653  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1653 0.2033 0.2409 -0.0160 0.0118  0.0650  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1689 0.1795 0.2583 -0.0253 0.0071  0.0820  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1878 0.2110 0.2884 -0.0138 -0.0044 0.0691  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.1844 0.1873 0.3047 -0.0173 -0.0204 0.0912  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.1972 0.2210 0.2982 -0.0174 -0.0064 0.0635  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.1906 0.2026 0.3175 -0.0261 -0.0247 0.0823  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.2088 0.2238 0.3077 -0.0128 -0.0027 0.0641  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.2074 0.1971 0.3192 -0.0152 -0.0244 0.1003  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1402 0.1986 0.1976 -0.0117 0.0121  0.0400  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1736 0.1755 0.2489 -0.0384 0.0065  0.0881  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1363 0.1966 0.2092 -0.0126 0.0051  0.0372  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1688 0.1675 0.2444 -0.0445 0.0052  0.0953  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1285 0.1923 0.2234 -0.0136 -0.0047 0.0402  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1559 0.1629 0.2447 -0.0393 0.0097  0.0719  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1290 0.1978 0.2610 -0.0204 -0.0010 0.0428  11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1529 0.1716 0.2446 -0.0355 0.0156  0.0540  11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1494 0.1964 0.2085 -0.0178 0.0030  0.0103  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1944 0.1646 0.2418 -0.0517 0.0001  0.0822  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1572 0.1988 0.1958 -0.0196 -0.0003 0.0001  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.2080 0.1668 0.2158 -0.0560 -0.0017 0.0836  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.1649 0.1957 0.1897 -0.0151 0.0049  -0.0043 11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.2257 0.1705 0.2147 -0.0449 0.0034  0.0751  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.1724 0.2009 0.1873 -0.0035 0.0085  -0.0015 11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.2402 0.1713 0.2285 -0.0496 0.0043  0.0677  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.1690 0.1969 0.1810 0.0065  -0.0020 0.0101  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.2424 0.1695 0.2208 -0.0479 -0.0052 0.0747  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1340 0.1886 0.2114 -0.0235 -0.0082 0.0246  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1527 0.1668 0.2442 -0.0302 0.0019  0.0604  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1512 0.1933 0.2028 -0.0227 -0.0151 0.0215  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1567 0.1819 0.2288 -0.0204 0.0116  0.0736  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1638 0.1897 0.2160 -0.0277 -0.0204 0.0181  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1596 0.1820 0.2221 -0.0209 0.0238  0.0784  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1731 0.1952 0.2239 -0.0337 -0.0228 0.0063  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1579 0.1829 0.2285 -0.0174 0.0311  0.0769  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1624 0.1921 0.2003 -0.0148 -0.0122 0.0280  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1634 0.1940 0.2373 -0.0207 0.0137  0.0858  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1717 0.1937 0.2146 -0.0045 -0.0004 0.0317  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1703 0.2053 0.2594 -0.0134 0.0169  0.0869  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1856 0.2019 0.2075 -0.0004 0.0023  0.0359  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1768 0.2144 0.2579 -0.0044 0.0307  0.0847  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1669 0.1889 0.2358 0.0018  -0.0070 0.0332  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1722 0.2140 0.2765 -0.0107 0.0071  0.0683  12  LEU   A CD2 
319  N N   A THR   A 13  ? 0.1597 0.1854 0.2247 -0.0246 -0.0200 0.0221  13  THR   A N   
320  N N   B THR   A 13  ? 0.1573 0.1801 0.2232 -0.0210 0.0228  0.0667  13  THR   A N   
321  C CA  A THR   A 13  ? 0.1589 0.1866 0.2340 -0.0261 -0.0083 0.0288  13  THR   A CA  
322  C CA  B THR   A 13  ? 0.1643 0.1846 0.2297 -0.0359 0.0263  0.0617  13  THR   A CA  
323  C C   A THR   A 13  ? 0.1499 0.1837 0.2382 -0.0184 0.0077  0.0354  13  THR   A C   
324  C C   B THR   A 13  ? 0.1680 0.1752 0.2406 -0.0374 0.0221  0.0693  13  THR   A C   
325  O O   A THR   A 13  ? 0.1443 0.1829 0.2428 -0.0177 0.0089  0.0286  13  THR   A O   
326  O O   B THR   A 13  ? 0.1813 0.1785 0.2371 -0.0421 0.0081  0.0731  13  THR   A O   
327  C CB  A THR   A 13  ? 0.1729 0.1913 0.2498 -0.0206 -0.0119 0.0321  13  THR   A CB  
328  C CB  B THR   A 13  ? 0.1699 0.1960 0.2382 -0.0284 0.0307  0.0591  13  THR   A CB  
329  O OG1 A THR   A 13  ? 0.1686 0.1746 0.2607 -0.0205 -0.0211 0.0409  13  THR   A OG1 
330  O OG1 B THR   A 13  ? 0.1537 0.1817 0.2525 -0.0352 0.0351  0.0650  13  THR   A OG1 
331  C CG2 A THR   A 13  ? 0.1804 0.2104 0.2494 -0.0253 -0.0076 0.0291  13  THR   A CG2 
332  C CG2 B THR   A 13  ? 0.1783 0.2192 0.2443 -0.0362 0.0383  0.0480  13  THR   A CG2 
347  N N   A ASP   A 14  ? 0.1479 0.1809 0.2440 -0.0131 0.0177  0.0390  14  ASP   A N   
348  N N   B ASP   A 14  ? 0.1701 0.1664 0.2608 -0.0393 0.0225  0.0678  14  ASP   A N   
349  C CA  A ASP   A 14  ? 0.1572 0.1861 0.2595 -0.0116 0.0041  0.0455  14  ASP   A CA  
350  C CA  B ASP   A 14  ? 0.1756 0.1705 0.2732 -0.0323 0.0126  0.0765  14  ASP   A CA  
351  C C   A ASP   A 14  ? 0.1560 0.1695 0.2412 -0.0130 -0.0039 0.0504  14  ASP   A C   
352  C C   B ASP   A 14  ? 0.1664 0.1646 0.2547 -0.0296 0.0010  0.0742  14  ASP   A C   
353  O O   A ASP   A 14  ? 0.1557 0.1676 0.2287 -0.0073 -0.0072 0.0518  14  ASP   A O   
354  O O   B ASP   A 14  ? 0.1802 0.1641 0.2595 -0.0319 -0.0072 0.0905  14  ASP   A O   
355  C CB  A ASP   A 14  ? 0.1788 0.2110 0.3172 -0.0134 0.0008  0.0552  14  ASP   A CB  
356  C CB  B ASP   A 14  ? 0.2053 0.1900 0.3285 -0.0294 0.0089  0.0885  14  ASP   A CB  
357  C CG  A ASP   A 14  ? 0.2006 0.2379 0.3700 -0.0223 0.0094  0.0617  14  ASP   A CG  
358  C CG  B ASP   A 14  ? 0.2304 0.2398 0.3974 -0.0185 0.0096  0.0766  14  ASP   A CG  
359  O OD1 A ASP   A 14  ? 0.2118 0.2387 0.3920 -0.0167 -0.0018 0.0740  14  ASP   A OD1 
360  O OD1 B ASP   A 14  ? 0.2423 0.2501 0.4217 0.0077  -0.0096 0.0929  14  ASP   A OD1 
361  O OD2 A ASP   A 14  ? 0.2144 0.2539 0.3950 -0.0196 0.0089  0.0503  14  ASP   A OD2 
362  O OD2 B ASP   A 14  ? 0.2453 0.2783 0.4323 -0.0136 0.0087  0.0516  14  ASP   A OD2 
371  N N   . ASN   A 15  ? 0.1545 0.1569 0.2479 -0.0288 -0.0037 0.0648  15  ASN   A N   
372  C CA  . ASN   A 15  ? 0.1559 0.1597 0.2461 -0.0206 -0.0124 0.0535  15  ASN   A CA  
373  C C   . ASN   A 15  ? 0.1463 0.1505 0.2657 -0.0246 0.0068  0.0593  15  ASN   A C   
374  O O   . ASN   A 15  ? 0.1586 0.1531 0.3150 -0.0268 -0.0100 0.0586  15  ASN   A O   
375  C CB  . ASN   A 15  ? 0.1589 0.1603 0.2478 -0.0156 -0.0100 0.0555  15  ASN   A CB  
376  C CG  . ASN   A 15  ? 0.1637 0.1646 0.2534 -0.0169 -0.0006 0.0266  15  ASN   A CG  
377  O OD1 . ASN   A 15  ? 0.1812 0.1694 0.2678 -0.0318 0.0083  0.0374  15  ASN   A OD1 
378  N ND2 . ASN   A 15  ? 0.1649 0.1710 0.2356 -0.0237 0.0058  0.0371  15  ASN   A ND2 
386  N N   A VAL   A 16  ? 0.1436 0.1550 0.2487 -0.0195 -0.0014 0.0531  16  VAL   A N   
387  N N   B VAL   A 16  ? 0.1431 0.1568 0.2532 -0.0196 -0.0030 0.0492  16  VAL   A N   
388  C CA  A VAL   A 16  ? 0.1480 0.1652 0.2319 -0.0171 -0.0005 0.0605  16  VAL   A CA  
389  C CA  B VAL   A 16  ? 0.1496 0.1705 0.2413 -0.0186 0.0004  0.0562  16  VAL   A CA  
390  C C   A VAL   A 16  ? 0.1446 0.1632 0.2282 -0.0287 -0.0002 0.0571  16  VAL   A C   
391  C C   B VAL   A 16  ? 0.1452 0.1651 0.2347 -0.0310 -0.0020 0.0547  16  VAL   A C   
392  O O   A VAL   A 16  ? 0.1427 0.1657 0.2254 -0.0263 0.0083  0.0513  16  VAL   A O   
393  O O   B VAL   A 16  ? 0.1412 0.1667 0.2339 -0.0284 0.0075  0.0468  16  VAL   A O   
394  C CB  A VAL   A 16  ? 0.1607 0.1740 0.2211 -0.0033 0.0035  0.0628  16  VAL   A CB  
395  C CB  B VAL   A 16  ? 0.1675 0.1850 0.2347 -0.0056 0.0117  0.0540  16  VAL   A CB  
396  C CG1 A VAL   A 16  ? 0.1743 0.1839 0.2134 0.0055  0.0112  0.0598  16  VAL   A CG1 
397  C CG1 B VAL   A 16  ? 0.1824 0.1966 0.2305 0.0042  0.0188  0.0465  16  VAL   A CG1 
398  C CG2 A VAL   A 16  ? 0.1645 0.1755 0.2228 -0.0015 0.0107  0.0671  16  VAL   A CG2 
399  C CG2 B VAL   A 16  ? 0.1743 0.1895 0.2376 -0.0054 0.0223  0.0567  16  VAL   A CG2 
418  N N   . TYR   A 17  ? 0.1356 0.1590 0.2274 -0.0320 0.0071  0.0603  17  TYR   A N   
419  C CA  . TYR   A 17  ? 0.1378 0.1611 0.2071 -0.0269 0.0097  0.0595  17  TYR   A CA  
420  C C   . TYR   A 17  ? 0.1502 0.1645 0.2328 -0.0211 0.0107  0.0600  17  TYR   A C   
421  O O   . TYR   A 17  ? 0.1447 0.1604 0.2493 -0.0226 0.0164  0.0718  17  TYR   A O   
422  C CB  . TYR   A 17  ? 0.1629 0.1549 0.2088 -0.0324 -0.0096 0.0622  17  TYR   A CB  
423  C CG  . TYR   A 17  ? 0.1969 0.1752 0.2169 -0.0293 -0.0206 0.0545  17  TYR   A CG  
424  C CD1 . TYR   A 17  ? 0.2093 0.1819 0.2368 -0.0185 -0.0265 0.0527  17  TYR   A CD1 
425  C CD2 . TYR   A 17  ? 0.2154 0.1810 0.2034 -0.0521 -0.0082 0.0528  17  TYR   A CD2 
426  C CE1 . TYR   A 17  ? 0.2261 0.1849 0.2417 -0.0273 -0.0252 0.0484  17  TYR   A CE1 
427  C CE2 . TYR   A 17  ? 0.2319 0.1871 0.2172 -0.0611 -0.0194 0.0305  17  TYR   A CE2 
428  C CZ  . TYR   A 17  ? 0.2513 0.1810 0.2270 -0.0459 -0.0303 0.0462  17  TYR   A CZ  
429  O OH  . TYR   A 17  ? 0.2800 0.1756 0.2434 -0.0487 -0.0321 0.0429  17  TYR   A OH  
440  N N   A ILE   A 18  ? 0.1523 0.1639 0.2241 -0.0263 0.0176  0.0612  18  ILE   A N   
441  N N   B ILE   A 18  ? 0.1444 0.1685 0.2213 -0.0176 0.0127  0.0668  18  ILE   A N   
442  C CA  A ILE   A 18  ? 0.1584 0.1712 0.2089 -0.0273 0.0255  0.0608  18  ILE   A CA  
443  C CA  B ILE   A 18  ? 0.1453 0.1824 0.2010 -0.0100 0.0117  0.0685  18  ILE   A CA  
444  C C   A ILE   A 18  ? 0.1602 0.1793 0.2171 -0.0303 0.0390  0.0648  18  ILE   A C   
445  C C   B ILE   A 18  ? 0.1390 0.1919 0.2014 -0.0100 0.0123  0.0681  18  ILE   A C   
446  O O   A ILE   A 18  ? 0.1576 0.1793 0.2175 -0.0328 0.0397  0.0669  18  ILE   A O   
447  O O   B ILE   A 18  ? 0.1402 0.1982 0.1986 -0.0111 0.0127  0.0603  18  ILE   A O   
448  C CB  A ILE   A 18  ? 0.1677 0.1761 0.1964 -0.0301 0.0208  0.0639  18  ILE   A CB  
449  C CB  B ILE   A 18  ? 0.1557 0.1936 0.1966 -0.0075 0.0105  0.0806  18  ILE   A CB  
450  C CG1 A ILE   A 18  ? 0.1816 0.1903 0.2011 -0.0283 0.0108  0.0630  18  ILE   A CG1 
451  C CG1 B ILE   A 18  ? 0.1717 0.2114 0.2091 0.0009  0.0001  0.0812  18  ILE   A CG1 
452  C CG2 A ILE   A 18  ? 0.1659 0.1817 0.2012 -0.0283 0.0199  0.0567  18  ILE   A CG2 
453  C CG2 B ILE   A 18  ? 0.1581 0.2057 0.2216 -0.0137 0.0057  0.0797  18  ILE   A CG2 
454  C CD1 A ILE   A 18  ? 0.1998 0.2078 0.2217 -0.0205 0.0034  0.0584  18  ILE   A CD1 
455  C CD1 B ILE   A 18  ? 0.1930 0.2299 0.2275 0.0073  -0.0070 0.0778  18  ILE   A CD1 
478  N N   A LYS   A 19  ? 0.1655 0.1848 0.2156 -0.0225 0.0471  0.0648  19  LYS   A N   
479  N N   B LYS   A 19  ? 0.1403 0.1883 0.2085 0.0017  0.0233  0.0730  19  LYS   A N   
480  C CA  A LYS   A 19  ? 0.1761 0.1989 0.2042 -0.0140 0.0501  0.0589  19  LYS   A CA  
481  C CA  B LYS   A 19  ? 0.1504 0.1962 0.2205 0.0108  0.0336  0.0656  19  LYS   A CA  
482  C C   A LYS   A 19  ? 0.1696 0.1985 0.1944 -0.0076 0.0473  0.0480  19  LYS   A C   
483  C C   B LYS   A 19  ? 0.1346 0.1916 0.2402 0.0104  0.0325  0.0612  19  LYS   A C   
484  O O   A LYS   A 19  ? 0.1669 0.2056 0.1897 -0.0095 0.0460  0.0582  19  LYS   A O   
485  O O   B LYS   A 19  ? 0.1273 0.1831 0.2500 0.0160  0.0270  0.0747  19  LYS   A O   
486  C CB  A LYS   A 19  ? 0.1786 0.2086 0.2024 -0.0103 0.0529  0.0615  19  LYS   A CB  
487  C CB  B LYS   A 19  ? 0.1596 0.2034 0.2063 0.0219  0.0457  0.0625  19  LYS   A CB  
488  C CG  A LYS   A 19  ? 0.1908 0.2171 0.2145 0.0011  0.0386  0.0566  19  LYS   A CG  
489  C CG  B LYS   A 19  ? 0.1730 0.2233 0.2300 0.0334  0.0407  0.0438  19  LYS   A CG  
490  C CD  A LYS   A 19  ? 0.1988 0.2207 0.2206 0.0025  0.0317  0.0549  19  LYS   A CD  
491  C CD  B LYS   A 19  ? 0.1849 0.2391 0.2400 0.0364  0.0473  0.0353  19  LYS   A CD  
492  C CE  A LYS   A 19  ? 0.2023 0.2213 0.2312 -0.0045 0.0241  0.0512  19  LYS   A CE  
493  C CE  B LYS   A 19  ? 0.1974 0.2534 0.2453 0.0297  0.0499  0.0380  19  LYS   A CE  
494  N NZ  A LYS   A 19  ? 0.2012 0.2177 0.2365 -0.0137 0.0327  0.0530  19  LYS   A NZ  
495  N NZ  B LYS   A 19  ? 0.2029 0.2610 0.2349 0.0283  0.0488  0.0442  19  LYS   A NZ  
522  N N   A ASN   A 20  ? 0.1702 0.1925 0.1911 -0.0073 0.0291  0.0405  20  ASN   A N   
523  N N   B ASN   A 20  ? 0.1337 0.1965 0.2458 -0.0101 0.0208  0.0695  20  ASN   A N   
524  C CA  A ASN   A 20  ? 0.1737 0.1928 0.1824 0.0042  0.0262  0.0387  20  ASN   A CA  
525  C CA  B ASN   A 20  ? 0.1398 0.2109 0.2355 0.0038  0.0255  0.0598  20  ASN   A CA  
526  C C   A ASN   A 20  ? 0.1846 0.1950 0.1738 -0.0018 0.0243  0.0275  20  ASN   A C   
527  C C   B ASN   A 20  ? 0.1535 0.2203 0.2172 0.0001  0.0333  0.0601  20  ASN   A C   
528  O O   A ASN   A 20  ? 0.1960 0.2060 0.1455 -0.0097 0.0252  0.0318  20  ASN   A O   
529  O O   B ASN   A 20  ? 0.1777 0.2443 0.2318 -0.0105 0.0232  0.0620  20  ASN   A O   
530  C CB  A ASN   A 20  ? 0.1812 0.1917 0.1859 0.0144  0.0258  0.0476  20  ASN   A CB  
531  C CB  B ASN   A 20  ? 0.1447 0.2176 0.2554 0.0066  0.0187  0.0576  20  ASN   A CB  
532  C CG  A ASN   A 20  ? 0.1936 0.1982 0.2041 0.0230  0.0301  0.0413  20  ASN   A CG  
533  C CG  B ASN   A 20  ? 0.1495 0.2311 0.2714 0.0216  0.0176  0.0696  20  ASN   A CG  
534  O OD1 A ASN   A 20  ? 0.2156 0.2230 0.2596 0.0229  0.0325  0.0263  20  ASN   A OD1 
535  O OD1 B ASN   A 20  ? 0.1653 0.2340 0.2862 0.0333  0.0205  0.0787  20  ASN   A OD1 
536  N ND2 A ASN   A 20  ? 0.1953 0.1871 0.2004 0.0273  0.0239  0.0607  20  ASN   A ND2 
537  N ND2 B ASN   A 20  ? 0.1658 0.2304 0.2660 0.0095  0.0223  0.0762  20  ASN   A ND2 
550  N N   A ALA   A 21  ? 0.1841 0.1872 0.1660 -0.0036 0.0157  0.0157  21  ALA   A N   
551  N N   B ALA   A 21  ? 0.1584 0.2072 0.2233 -0.0016 0.0482  0.0383  21  ALA   A N   
552  C CA  A ALA   A 21  ? 0.1893 0.1889 0.1660 -0.0133 -0.0011 0.0134  21  ALA   A CA  
553  C CA  B ALA   A 21  ? 0.1691 0.2005 0.2341 -0.0052 0.0410  0.0359  21  ALA   A CA  
554  C C   A ALA   A 21  ? 0.1928 0.1830 0.1616 -0.0086 0.0088  -0.0074 21  ALA   A C   
555  C C   B ALA   A 21  ? 0.1599 0.1805 0.2191 -0.0053 0.0429  0.0406  21  ALA   A C   
556  O O   A ALA   A 21  ? 0.1940 0.1973 0.1758 -0.0122 0.0142  -0.0208 21  ALA   A O   
557  O O   B ALA   A 21  ? 0.1537 0.1740 0.2237 -0.0003 0.0447  0.0180  21  ALA   A O   
558  C CB  A ALA   A 21  ? 0.1965 0.1976 0.1871 -0.0222 -0.0171 0.0299  21  ALA   A CB  
559  C CB  B ALA   A 21  ? 0.1913 0.2132 0.2591 -0.0079 0.0252  0.0345  21  ALA   A CB  
570  N N   A ASP   A 22  ? 0.2061 0.1717 0.1854 -0.0026 0.0188  -0.0094 22  ASP   A N   
571  N N   B ASP   A 22  ? 0.1654 0.1712 0.2044 -0.0031 0.0463  0.0359  22  ASP   A N   
572  C CA  A ASP   A 22  ? 0.2146 0.1700 0.1986 -0.0013 0.0140  0.0130  22  ASP   A CA  
573  C CA  B ASP   A 22  ? 0.1800 0.1581 0.1909 -0.0014 0.0428  0.0194  22  ASP   A CA  
574  C C   A ASP   A 22  ? 0.2003 0.1683 0.1729 -0.0071 0.0111  0.0182  22  ASP   A C   
575  C C   B ASP   A 22  ? 0.1642 0.1616 0.1698 -0.0118 0.0464  0.0130  22  ASP   A C   
576  O O   A ASP   A 22  ? 0.1977 0.1741 0.1757 -0.0182 0.0122  0.0164  22  ASP   A O   
577  O O   B ASP   A 22  ? 0.1627 0.1763 0.1845 -0.0174 0.0455  -0.0046 22  ASP   A O   
578  C CB  A ASP   A 22  ? 0.2353 0.1753 0.2312 -0.0013 0.0096  0.0106  22  ASP   A CB  
579  C CB  B ASP   A 22  ? 0.2092 0.1599 0.2295 0.0100  0.0431  0.0220  22  ASP   A CB  
580  C CG  A ASP   A 22  ? 0.2461 0.1819 0.2538 -0.0086 -0.0056 0.0242  22  ASP   A CG  
581  C CG  B ASP   A 22  ? 0.2331 0.1621 0.2461 0.0163  0.0403  0.0210  22  ASP   A CG  
582  O OD1 A ASP   A 22  ? 0.2392 0.1746 0.2704 -0.0290 -0.0265 0.0325  22  ASP   A OD1 
583  O OD1 B ASP   A 22  ? 0.2263 0.1491 0.2200 0.0073  0.0349  0.0213  22  ASP   A OD1 
584  O OD2 A ASP   A 22  ? 0.2584 0.1953 0.2581 0.0016  -0.0065 0.0119  22  ASP   A OD2 
585  O OD2 B ASP   A 22  ? 0.2612 0.1842 0.2998 0.0176  0.0463  0.0284  22  ASP   A OD2 
594  N N   A ILE   A 23  ? 0.1985 0.1681 0.1603 -0.0111 0.0088  0.0163  23  ILE   A N   
595  N N   B ILE   A 23  ? 0.1585 0.1579 0.1688 -0.0140 0.0460  0.0140  23  ILE   A N   
596  C CA  A ILE   A 23  ? 0.1919 0.1614 0.1562 -0.0115 0.0194  0.0183  23  ILE   A CA  
597  C CA  B ILE   A 23  ? 0.1534 0.1641 0.1614 -0.0176 0.0448  0.0246  23  ILE   A CA  
598  C C   A ILE   A 23  ? 0.1796 0.1694 0.1625 -0.0098 0.0273  0.0165  23  ILE   A C   
599  C C   B ILE   A 23  ? 0.1552 0.1731 0.1628 -0.0217 0.0345  0.0228  23  ILE   A C   
600  O O   A ILE   A 23  ? 0.1764 0.1807 0.1713 -0.0193 0.0129  0.0005  23  ILE   A O   
601  O O   B ILE   A 23  ? 0.1618 0.1672 0.1761 -0.0120 0.0222  0.0252  23  ILE   A O   
602  C CB  A ILE   A 23  ? 0.1982 0.1610 0.1309 -0.0037 0.0294  0.0129  23  ILE   A CB  
603  C CB  B ILE   A 23  ? 0.1586 0.1640 0.1702 -0.0104 0.0371  0.0217  23  ILE   A CB  
604  C CG1 A ILE   A 23  ? 0.2041 0.1569 0.1358 -0.0094 0.0327  0.0062  23  ILE   A CG1 
605  C CG1 B ILE   A 23  ? 0.1636 0.1618 0.1852 -0.0102 0.0286  0.0109  23  ILE   A CG1 
606  C CG2 A ILE   A 23  ? 0.1996 0.1662 0.1540 0.0039  0.0378  0.0214  23  ILE   A CG2 
607  C CG2 B ILE   A 23  ? 0.1647 0.1619 0.1714 0.0022  0.0436  0.0233  23  ILE   A CG2 
608  C CD1 A ILE   A 23  ? 0.2102 0.1627 0.1507 -0.0122 0.0128  -0.0057 23  ILE   A CD1 
609  C CD1 B ILE   A 23  ? 0.1647 0.1641 0.1932 0.0018  0.0039  0.0011  23  ILE   A CD1 
632  N N   A VAL   A 24  ? 0.1814 0.1754 0.1696 -0.0147 0.0240  0.0133  24  VAL   A N   
633  N N   B VAL   A 24  ? 0.1680 0.1767 0.1608 -0.0332 0.0241  0.0117  24  VAL   A N   
634  C CA  A VAL   A 24  ? 0.1832 0.1896 0.1899 -0.0151 0.0214  0.0038  24  VAL   A CA  
635  C CA  B VAL   A 24  ? 0.1851 0.1832 0.1885 -0.0365 0.0261  0.0091  24  VAL   A CA  
636  C C   A VAL   A 24  ? 0.1846 0.2025 0.2087 -0.0166 0.0089  0.0084  24  VAL   A C   
637  C C   B VAL   A 24  ? 0.1966 0.2003 0.2001 -0.0245 0.0226  0.0062  24  VAL   A C   
638  O O   A VAL   A 24  ? 0.1914 0.2012 0.2174 -0.0147 0.0134  0.0142  24  VAL   A O   
639  O O   B VAL   A 24  ? 0.2081 0.2058 0.2237 -0.0232 0.0223  0.0040  24  VAL   A O   
640  C CB  A VAL   A 24  ? 0.1828 0.1874 0.1781 -0.0130 0.0303  0.0031  24  VAL   A CB  
641  C CB  B VAL   A 24  ? 0.2016 0.1935 0.2052 -0.0335 0.0233  0.0197  24  VAL   A CB  
642  C CG1 A VAL   A 24  ? 0.1826 0.1927 0.1607 -0.0045 0.0375  -0.0117 24  VAL   A CG1 
643  C CG1 B VAL   A 24  ? 0.2245 0.2035 0.2304 -0.0237 0.0124  0.0183  24  VAL   A CG1 
644  C CG2 A VAL   A 24  ? 0.1862 0.1861 0.1860 -0.0127 0.0370  0.0094  24  VAL   A CG2 
645  C CG2 B VAL   A 24  ? 0.2063 0.2018 0.2116 -0.0363 0.0156  0.0160  24  VAL   A CG2 
664  N N   A GLU   A 25  ? 0.1880 0.2223 0.1973 -0.0205 0.0140  -0.0005 25  GLU   A N   
665  N N   B GLU   A 25  ? 0.1892 0.2209 0.2060 -0.0144 0.0405  -0.0025 25  GLU   A N   
666  C CA  A GLU   A 25  ? 0.2051 0.2425 0.2135 -0.0126 0.0186  -0.0031 25  GLU   A CA  
667  C CA  B GLU   A 25  ? 0.1892 0.2435 0.1953 -0.0060 0.0395  -0.0078 25  GLU   A CA  
668  C C   A GLU   A 25  ? 0.1944 0.2375 0.1791 -0.0231 0.0224  -0.0071 25  GLU   A C   
669  C C   B GLU   A 25  ? 0.1810 0.2530 0.1734 -0.0128 0.0559  0.0026  25  GLU   A C   
670  O O   A GLU   A 25  ? 0.1926 0.2476 0.1848 -0.0224 0.0184  -0.0110 25  GLU   A O   
671  O O   B GLU   A 25  ? 0.1982 0.2592 0.1859 -0.0120 0.0498  -0.0006 25  GLU   A O   
672  C CB  A GLU   A 25  ? 0.2269 0.2616 0.2595 -0.0047 0.0138  -0.0014 25  GLU   A CB  
673  C CB  B GLU   A 25  ? 0.2087 0.2559 0.2326 0.0042  0.0374  -0.0084 25  GLU   A CB  
674  C CG  A GLU   A 25  ? 0.2498 0.2794 0.3067 -0.0060 -0.0019 -0.0101 25  GLU   A CG  
675  C CG  B GLU   A 25  ? 0.2503 0.2789 0.3187 0.0034  0.0279  -0.0057 25  GLU   A CG  
676  C CD  A GLU   A 25  ? 0.2693 0.3002 0.3404 -0.0023 -0.0176 -0.0185 25  GLU   A CD  
677  C CD  B GLU   A 25  ? 0.2876 0.3030 0.3946 0.0011  0.0206  -0.0060 25  GLU   A CD  
678  O OE1 A GLU   A 25  ? 0.2803 0.3088 0.3467 0.0019  -0.0322 -0.0289 25  GLU   A OE1 
679  O OE1 B GLU   A 25  ? 0.3030 0.3162 0.4273 0.0005  0.0151  -0.0094 25  GLU   A OE1 
680  O OE2 A GLU   A 25  ? 0.2727 0.3102 0.3559 0.0002  -0.0216 -0.0214 25  GLU   A OE2 
681  O OE2 B GLU   A 25  ? 0.3003 0.3073 0.4262 -0.0039 0.0171  -0.0036 25  GLU   A OE2 
694  N N   A GLU   A 26  ? 0.1895 0.2232 0.1721 -0.0429 0.0256  -0.0060 26  GLU   A N   
695  N N   B GLU   A 26  ? 0.1675 0.2509 0.1885 -0.0131 0.0594  -0.0048 26  GLU   A N   
696  C CA  A GLU   A 26  ? 0.2116 0.2183 0.1664 -0.0548 0.0257  0.0051  26  GLU   A CA  
697  C CA  B GLU   A 26  ? 0.1834 0.2478 0.1866 -0.0153 0.0521  0.0050  26  GLU   A CA  
698  C C   A GLU   A 26  ? 0.2112 0.2146 0.1565 -0.0506 0.0265  0.0062  26  GLU   A C   
699  C C   B GLU   A 26  ? 0.1786 0.2287 0.1748 -0.0062 0.0427  0.0099  26  GLU   A C   
700  O O   A GLU   A 26  ? 0.2148 0.2161 0.1541 -0.0558 0.0167  0.0052  26  GLU   A O   
701  O O   B GLU   A 26  ? 0.1936 0.2317 0.1814 -0.0231 0.0438  0.0121  26  GLU   A O   
702  C CB  A GLU   A 26  ? 0.2301 0.2190 0.1791 -0.0727 0.0351  0.0277  26  GLU   A CB  
703  C CB  B GLU   A 26  ? 0.1998 0.2613 0.2168 -0.0312 0.0347  0.0079  26  GLU   A CB  
704  C CG  A GLU   A 26  ? 0.2458 0.2357 0.2518 -0.0748 0.0343  0.0105  26  GLU   A CG  
705  C CG  B GLU   A 26  ? 0.2097 0.2818 0.2482 -0.0320 0.0380  0.0009  26  GLU   A CG  
706  C CD  A GLU   A 26  ? 0.2525 0.2452 0.2860 -0.0835 0.0477  -0.0039 26  GLU   A CD  
707  C CD  B GLU   A 26  ? 0.2088 0.2950 0.2616 -0.0354 0.0489  0.0070  26  GLU   A CD  
708  O OE1 A GLU   A 26  ? 0.2523 0.2555 0.2955 -0.0758 0.0747  -0.0356 26  GLU   A OE1 
709  O OE1 B GLU   A 26  ? 0.2211 0.3108 0.2599 -0.0269 0.0748  0.0060  26  GLU   A OE1 
710  O OE2 A GLU   A 26  ? 0.2611 0.2547 0.2941 -0.0810 0.0408  0.0041  26  GLU   A OE2 
711  O OE2 B GLU   A 26  ? 0.2045 0.2945 0.2232 -0.0378 0.0573  0.0166  26  GLU   A OE2 
724  N N   A ALA   A 27  ? 0.1979 0.2075 0.1479 -0.0513 0.0315  0.0070  27  ALA   A N   
725  N N   B ALA   A 27  ? 0.1525 0.2072 0.1623 0.0085  0.0240  0.0337  27  ALA   A N   
726  C CA  A ALA   A 27  ? 0.2005 0.2167 0.1672 -0.0507 0.0259  0.0083  27  ALA   A CA  
727  C CA  B ALA   A 27  ? 0.1605 0.2067 0.1659 0.0152  0.0233  0.0343  27  ALA   A CA  
728  C C   A ALA   A 27  ? 0.2123 0.2373 0.1859 -0.0504 0.0202  -0.0016 27  ALA   A C   
729  C C   B ALA   A 27  ? 0.1798 0.2228 0.1539 0.0089  0.0204  0.0246  27  ALA   A C   
730  O O   A ALA   A 27  ? 0.2168 0.2401 0.1886 -0.0526 0.0110  -0.0090 27  ALA   A O   
731  O O   B ALA   A 27  ? 0.1751 0.2250 0.1590 0.0002  0.0207  0.0232  27  ALA   A O   
732  C CB  A ALA   A 27  ? 0.1931 0.2077 0.1676 -0.0560 0.0242  0.0208  27  ALA   A CB  
733  C CB  B ALA   A 27  ? 0.1544 0.2019 0.1894 0.0060  0.0290  0.0331  27  ALA   A CB  
744  N N   A LYS   A 28  ? 0.2332 0.2615 0.2099 -0.0385 0.0093  -0.0169 28  LYS   A N   
745  N N   B LYS   A 28  ? 0.2137 0.2414 0.1703 0.0242  0.0053  0.0005  28  LYS   A N   
746  C CA  A LYS   A 28  ? 0.2619 0.2914 0.2406 -0.0217 0.0051  -0.0289 28  LYS   A CA  
747  C CA  B LYS   A 28  ? 0.2506 0.2777 0.1984 0.0483  -0.0055 -0.0296 28  LYS   A CA  
748  C C   A LYS   A 28  ? 0.2828 0.3172 0.2456 -0.0234 0.0126  -0.0255 28  LYS   A C   
749  C C   B LYS   A 28  ? 0.2719 0.3016 0.1768 0.0584  -0.0055 -0.0210 28  LYS   A C   
750  O O   A LYS   A 28  ? 0.2854 0.3231 0.2694 -0.0232 -0.0008 -0.0241 28  LYS   A O   
751  O O   B LYS   A 28  ? 0.2909 0.3153 0.1869 0.0575  -0.0271 -0.0104 28  LYS   A O   
752  C CB  A LYS   A 28  ? 0.2706 0.3001 0.2743 -0.0068 -0.0058 -0.0336 28  LYS   A CB  
753  C CB  B LYS   A 28  ? 0.2744 0.2971 0.2547 0.0601  -0.0221 -0.0494 28  LYS   A CB  
754  C CG  A LYS   A 28  ? 0.2823 0.3098 0.3110 0.0086  -0.0112 -0.0318 28  LYS   A CG  
755  C CG  B LYS   A 28  ? 0.2929 0.3164 0.3057 0.0629  -0.0366 -0.0581 28  LYS   A CG  
756  C CD  A LYS   A 28  ? 0.2935 0.3239 0.3528 0.0181  -0.0247 -0.0290 28  LYS   A CD  
757  C CD  B LYS   A 28  ? 0.3119 0.3409 0.3822 0.0671  -0.0504 -0.0529 28  LYS   A CD  
758  C CE  A LYS   A 28  ? 0.2992 0.3339 0.3725 0.0233  -0.0362 -0.0292 28  LYS   A CE  
759  C CE  B LYS   A 28  ? 0.3278 0.3583 0.4383 0.0712  -0.0573 -0.0551 28  LYS   A CE  
760  N NZ  A LYS   A 28  ? 0.3049 0.3388 0.3909 0.0273  -0.0390 -0.0329 28  LYS   A NZ  
761  N NZ  B LYS   A 28  ? 0.3356 0.3669 0.4645 0.0718  -0.0668 -0.0549 28  LYS   A NZ  
788  N N   A LYS   A 29  ? 0.2972 0.3381 0.2358 -0.0261 0.0370  -0.0103 29  LYS   A N   
789  N N   B LYS   A 29  ? 0.2704 0.3143 0.1678 0.0669  0.0431  -0.0046 29  LYS   A N   
790  C CA  A LYS   A 29  ? 0.3135 0.3586 0.2489 -0.0249 0.0585  -0.0002 29  LYS   A CA  
791  C CA  B LYS   A 29  ? 0.2791 0.3346 0.1661 0.0675  0.0836  0.0185  29  LYS   A CA  
792  C C   A LYS   A 29  ? 0.3109 0.3480 0.2198 -0.0342 0.0494  0.0074  29  LYS   A C   
793  C C   B LYS   A 29  ? 0.2742 0.3216 0.1462 0.0548  0.0741  0.0347  29  LYS   A C   
794  O O   A LYS   A 29  ? 0.3200 0.3581 0.2313 -0.0278 0.0477  -0.0049 29  LYS   A O   
795  O O   B LYS   A 29  ? 0.2833 0.3343 0.1763 0.0651  0.0525  0.0297  29  LYS   A O   
796  C CB  A LYS   A 29  ? 0.3292 0.3849 0.2995 -0.0161 0.0788  0.0021  29  LYS   A CB  
797  C CB  B LYS   A 29  ? 0.3000 0.3699 0.2157 0.0654  0.1119  0.0286  29  LYS   A CB  
798  C CG  A LYS   A 29  ? 0.3468 0.4085 0.3607 -0.0080 0.0867  0.0016  29  LYS   A CG  
799  C CG  B LYS   A 29  ? 0.3247 0.3999 0.2965 0.0680  0.1217  0.0250  29  LYS   A CG  
800  C CD  A LYS   A 29  ? 0.3625 0.4273 0.4222 -0.0032 0.0886  -0.0001 29  LYS   A CD  
801  C CD  B LYS   A 29  ? 0.3466 0.4223 0.3810 0.0725  0.1208  0.0187  29  LYS   A CD  
802  C CE  A LYS   A 29  ? 0.3749 0.4402 0.4606 -0.0000 0.0891  -0.0002 29  LYS   A CE  
803  C CE  B LYS   A 29  ? 0.3621 0.4387 0.4357 0.0739  0.1227  0.0139  29  LYS   A CE  
804  N NZ  A LYS   A 29  ? 0.3800 0.4461 0.4880 0.0030  0.0874  -0.0022 29  LYS   A NZ  
805  N NZ  B LYS   A 29  ? 0.3705 0.4466 0.4761 0.0757  0.1198  0.0118  29  LYS   A NZ  
832  N N   A VAL   A 30  ? 0.2983 0.3265 0.2133 -0.0497 0.0353  0.0145  30  VAL   A N   
833  N N   B VAL   A 30  ? 0.2584 0.2994 0.1563 0.0315  0.0773  0.0401  30  VAL   A N   
834  C CA  A VAL   A 30  ? 0.2903 0.3058 0.1940 -0.0609 0.0206  0.0213  30  VAL   A CA  
835  C CA  B VAL   A 30  ? 0.2429 0.2798 0.1682 0.0099  0.0596  0.0439  30  VAL   A CA  
836  C C   A VAL   A 30  ? 0.2871 0.2893 0.1578 -0.0540 0.0133  0.0246  30  VAL   A C   
837  C C   B VAL   A 30  ? 0.2411 0.2707 0.1480 0.0007  0.0484  0.0420  30  VAL   A C   
838  O O   A VAL   A 30  ? 0.2894 0.2929 0.1763 -0.0468 0.0085  0.0251  30  VAL   A O   
839  O O   B VAL   A 30  ? 0.2465 0.2759 0.1569 -0.0003 0.0308  0.0426  30  VAL   A O   
840  C CB  A VAL   A 30  ? 0.2865 0.3040 0.2180 -0.0729 0.0160  0.0186  30  VAL   A CB  
841  C CB  B VAL   A 30  ? 0.2361 0.2718 0.2126 -0.0030 0.0487  0.0487  30  VAL   A CB  
842  C CG1 A VAL   A 30  ? 0.2868 0.3014 0.2272 -0.0763 0.0145  0.0126  30  VAL   A CG1 
843  C CG1 B VAL   A 30  ? 0.2408 0.2694 0.2352 -0.0070 0.0378  0.0457  30  VAL   A CG1 
844  C CG2 A VAL   A 30  ? 0.2866 0.3081 0.2399 -0.0753 0.0147  0.0174  30  VAL   A CG2 
845  C CG2 B VAL   A 30  ? 0.2335 0.2732 0.2405 -0.0099 0.0485  0.0597  30  VAL   A CG2 
864  N N   A LYS   A 31  ? 0.2798 0.2686 0.1332 -0.0482 0.0096  0.0197  31  LYS   A N   
865  N N   B LYS   A 31  ? 0.2409 0.2582 0.1574 -0.0016 0.0467  0.0344  31  LYS   A N   
866  C CA  A LYS   A 31  ? 0.2842 0.2681 0.1553 -0.0361 -0.0074 0.0227  31  LYS   A CA  
867  C CA  B LYS   A 31  ? 0.2525 0.2579 0.1700 0.0084  0.0274  0.0211  31  LYS   A CA  
868  C C   A LYS   A 31  ? 0.2614 0.2421 0.1107 -0.0304 -0.0079 0.0446  31  LYS   A C   
869  C C   B LYS   A 31  ? 0.2374 0.2422 0.1464 0.0109  0.0264  0.0331  31  LYS   A C   
870  O O   A LYS   A 31  ? 0.2627 0.2483 0.1100 -0.0198 -0.0171 0.0535  31  LYS   A O   
871  O O   B LYS   A 31  ? 0.2522 0.2473 0.1722 0.0206  0.0203  0.0286  31  LYS   A O   
872  C CB  A LYS   A 31  ? 0.3140 0.2968 0.2604 -0.0313 -0.0215 0.0004  31  LYS   A CB  
873  C CB  B LYS   A 31  ? 0.2832 0.2846 0.2612 0.0088  0.0006  -0.0051 31  LYS   A CB  
874  C CG  A LYS   A 31  ? 0.3428 0.3212 0.3671 -0.0211 -0.0320 -0.0105 31  LYS   A CG  
875  C CG  B LYS   A 31  ? 0.3228 0.3188 0.3828 0.0092  -0.0241 -0.0250 31  LYS   A CG  
876  C CD  A LYS   A 31  ? 0.3677 0.3407 0.4494 -0.0127 -0.0422 -0.0199 31  LYS   A CD  
877  C CD  B LYS   A 31  ? 0.3518 0.3500 0.4729 0.0111  -0.0451 -0.0442 31  LYS   A CD  
878  C CE  A LYS   A 31  ? 0.3831 0.3560 0.5061 -0.0067 -0.0508 -0.0265 31  LYS   A CE  
879  C CE  B LYS   A 31  ? 0.3747 0.3799 0.5383 0.0100  -0.0591 -0.0562 31  LYS   A CE  
880  N NZ  A LYS   A 31  ? 0.3898 0.3596 0.5349 -0.0009 -0.0588 -0.0302 31  LYS   A NZ  
881  N NZ  B LYS   A 31  ? 0.3863 0.3858 0.5766 0.0086  -0.0630 -0.0667 31  LYS   A NZ  
908  N N   A PRO   A 32  ? 0.2361 0.2190 0.0978 -0.0336 -0.0005 0.0345  32  PRO   A N   
909  N N   B PRO   A 32  ? 0.2124 0.2248 0.1261 0.0060  0.0345  0.0302  32  PRO   A N   
910  C CA  A PRO   A 32  ? 0.2263 0.2076 0.1321 -0.0312 -0.0085 0.0377  32  PRO   A CA  
911  C CA  B PRO   A 32  ? 0.2074 0.2198 0.1476 0.0082  0.0251  0.0382  32  PRO   A CA  
912  C C   A PRO   A 32  ? 0.2168 0.1953 0.1407 -0.0275 -0.0095 0.0302  32  PRO   A C   
913  C C   B PRO   A 32  ? 0.2067 0.2114 0.1453 0.0137  0.0133  0.0380  32  PRO   A C   
914  O O   A PRO   A 32  ? 0.2114 0.1839 0.1254 -0.0418 -0.0201 0.0118  32  PRO   A O   
915  O O   B PRO   A 32  ? 0.2066 0.2112 0.1686 0.0068  0.0075  0.0293  32  PRO   A O   
916  C CB  A PRO   A 32  ? 0.2236 0.2184 0.1383 -0.0387 -0.0025 0.0219  32  PRO   A CB  
917  C CB  B PRO   A 32  ? 0.2004 0.2316 0.1622 0.0021  0.0241  0.0261  32  PRO   A CB  
918  C CG  A PRO   A 32  ? 0.2243 0.2267 0.1107 -0.0372 -0.0210 0.0164  32  PRO   A CG  
919  C CG  B PRO   A 32  ? 0.2033 0.2404 0.1445 0.0003  0.0139  0.0175  32  PRO   A CG  
920  C CD  A PRO   A 32  ? 0.2275 0.2213 0.0905 -0.0351 -0.0015 0.0300  32  PRO   A CD  
921  C CD  B PRO   A 32  ? 0.2048 0.2356 0.1279 0.0016  0.0290  0.0193  32  PRO   A CD  
936  N N   A THR   A 33  ? 0.2161 0.1956 0.1397 -0.0170 -0.0088 0.0228  33  THR   A N   
937  N N   B THR   A 33  ? 0.2014 0.2086 0.1351 0.0190  0.0128  0.0321  33  THR   A N   
938  C CA  A THR   A 33  ? 0.2107 0.2007 0.1461 -0.0044 -0.0153 0.0266  33  THR   A CA  
939  C CA  B THR   A 33  ? 0.2047 0.2055 0.1390 0.0231  -0.0042 0.0340  33  THR   A CA  
940  C C   A THR   A 33  ? 0.1938 0.1943 0.1309 -0.0094 -0.0076 0.0179  33  THR   A C   
941  C C   B THR   A 33  ? 0.1840 0.1828 0.1412 0.0115  0.0011  0.0173  33  THR   A C   
942  O O   A THR   A 33  ? 0.1917 0.1966 0.1314 -0.0056 -0.0095 0.0146  33  THR   A O   
943  O O   B THR   A 33  ? 0.1789 0.1708 0.1558 0.0144  0.0006  0.0061  33  THR   A O   
944  C CB  A THR   A 33  ? 0.2257 0.2165 0.1780 0.0077  -0.0074 0.0452  33  THR   A CB  
945  C CB  B THR   A 33  ? 0.2362 0.2292 0.1638 0.0294  0.0069  0.0622  33  THR   A CB  
946  O OG1 A THR   A 33  ? 0.2417 0.2322 0.1995 0.0156  0.0001  0.0516  33  THR   A OG1 
947  O OG1 B THR   A 33  ? 0.2520 0.2571 0.1906 0.0377  -0.0052 0.0679  33  THR   A OG1 
948  C CG2 A THR   A 33  ? 0.2255 0.2227 0.1823 0.0132  -0.0104 0.0407  33  THR   A CG2 
949  C CG2 B THR   A 33  ? 0.2439 0.2346 0.1989 0.0274  0.0153  0.0690  33  THR   A CG2 
964  N N   A VAL   A 34  ? 0.1819 0.1836 0.1144 -0.0194 -0.0000 0.0257  34  VAL   A N   
965  N N   B VAL   A 34  ? 0.1755 0.1801 0.1428 0.0011  -0.0033 0.0315  34  VAL   A N   
966  C CA  A VAL   A 34  ? 0.1764 0.1677 0.1161 -0.0211 -0.0070 0.0319  34  VAL   A CA  
967  C CA  B VAL   A 34  ? 0.1705 0.1679 0.1283 0.0014  -0.0000 0.0306  34  VAL   A CA  
968  C C   A VAL   A 34  ? 0.1663 0.1592 0.1115 -0.0211 0.0020  0.0235  34  VAL   A C   
969  C C   B VAL   A 34  ? 0.1693 0.1625 0.1252 -0.0100 0.0080  0.0246  34  VAL   A C   
970  O O   A VAL   A 34  ? 0.1566 0.1529 0.0980 -0.0180 0.0136  0.0193  34  VAL   A O   
971  O O   B VAL   A 34  ? 0.1727 0.1632 0.1423 -0.0155 0.0089  0.0148  34  VAL   A O   
972  C CB  A VAL   A 34  ? 0.1792 0.1672 0.1129 -0.0247 -0.0027 0.0264  34  VAL   A CB  
973  C CB  B VAL   A 34  ? 0.1712 0.1745 0.1574 0.0036  0.0123  0.0093  34  VAL   A CB  
974  C CG1 A VAL   A 34  ? 0.1822 0.1706 0.1154 -0.0283 -0.0062 0.0204  34  VAL   A CG1 
975  C CG1 B VAL   A 34  ? 0.1792 0.1816 0.1572 0.0019  0.0113  -0.0064 34  VAL   A CG1 
976  C CG2 A VAL   A 34  ? 0.1885 0.1830 0.1375 -0.0140 0.0101  0.0165  34  VAL   A CG2 
977  C CG2 B VAL   A 34  ? 0.1817 0.1918 0.1848 0.0096  0.0189  -0.0002 34  VAL   A CG2 
996  N N   . VAL   A 35  ? 0.1511 0.1608 0.1234 -0.0225 -0.0032 0.0256  35  VAL   A N   
997  C CA  . VAL   A 35  ? 0.1418 0.1534 0.1347 -0.0166 0.0087  0.0197  35  VAL   A CA  
998  C C   . VAL   A 35  ? 0.1414 0.1491 0.1293 -0.0080 0.0078  0.0150  35  VAL   A C   
999  O O   . VAL   A 35  ? 0.1413 0.1652 0.1393 -0.0191 0.0144  0.0180  35  VAL   A O   
1000 C CB  . VAL   A 35  ? 0.1604 0.1544 0.1488 -0.0076 0.0153  0.0178  35  VAL   A CB  
1001 C CG1 . VAL   A 35  ? 0.1704 0.1583 0.1561 -0.0004 0.0120  0.0171  35  VAL   A CG1 
1002 C CG2 . VAL   A 35  ? 0.1566 0.1633 0.1607 -0.0069 0.0112  0.0044  35  VAL   A CG2 
1013 N N   . VAL   A 36  ? 0.1399 0.1444 0.1065 -0.0110 0.0086  0.0162  36  VAL   A N   
1014 C CA  . VAL   A 36  ? 0.1389 0.1311 0.1181 -0.0127 0.0013  0.0125  36  VAL   A CA  
1015 C C   . VAL   A 36  ? 0.1323 0.1357 0.1379 -0.0097 0.0050  0.0234  36  VAL   A C   
1016 O O   . VAL   A 36  ? 0.1298 0.1340 0.1472 -0.0074 0.0119  0.0196  36  VAL   A O   
1017 C CB  . VAL   A 36  ? 0.1400 0.1349 0.1306 -0.0125 0.0086  0.0321  36  VAL   A CB  
1018 C CG1 . VAL   A 36  ? 0.1393 0.1437 0.1487 -0.0221 -0.0006 0.0016  36  VAL   A CG1 
1019 C CG2 . VAL   A 36  ? 0.1362 0.1413 0.1518 -0.0124 0.0069  0.0333  36  VAL   A CG2 
1029 N N   . ASN   A 37  ? 0.1270 0.1243 0.1230 -0.0051 0.0065  0.0205  37  ASN   A N   
1030 C CA  . ASN   A 37  ? 0.1226 0.1267 0.1272 -0.0054 0.0025  0.0243  37  ASN   A CA  
1031 C C   . ASN   A 37  ? 0.1190 0.1308 0.1259 -0.0120 0.0111  0.0342  37  ASN   A C   
1032 O O   . ASN   A 37  ? 0.1346 0.1429 0.1207 -0.0017 0.0088  0.0149  37  ASN   A O   
1033 C CB  . ASN   A 37  ? 0.1277 0.1276 0.1466 -0.0006 0.0033  0.0300  37  ASN   A CB  
1034 C CG  . ASN   A 37  ? 0.1305 0.1263 0.1372 -0.0020 0.0101  0.0162  37  ASN   A CG  
1035 O OD1 . ASN   A 37  ? 0.1276 0.1273 0.1644 0.0004  0.0040  0.0237  37  ASN   A OD1 
1036 N ND2 . ASN   A 37  ? 0.1393 0.1242 0.1474 -0.0037 0.0043  0.0257  37  ASN   A ND2 
1043 N N   A ALA   A 38  ? 0.1255 0.1443 0.1282 -0.0040 0.0047  0.0229  38  ALA   A N   
1044 N N   B ALA   A 38  ? 0.1237 0.1433 0.1442 -0.0009 0.0072  0.0249  38  ALA   A N   
1045 C CA  A ALA   A 38  ? 0.1367 0.1396 0.1201 -0.0024 -0.0056 0.0158  38  ALA   A CA  
1046 C CA  B ALA   A 38  ? 0.1340 0.1375 0.1438 -0.0037 0.0002  0.0222  38  ALA   A CA  
1047 C C   A ALA   A 38  ? 0.1279 0.1336 0.1154 0.0039  -0.0098 0.0116  38  ALA   A C   
1048 C C   B ALA   A 38  ? 0.1335 0.1395 0.1447 0.0022  -0.0075 0.0047  38  ALA   A C   
1049 O O   A ALA   A 38  ? 0.1213 0.1217 0.1042 0.0004  -0.0090 0.0093  38  ALA   A O   
1050 O O   B ALA   A 38  ? 0.1338 0.1333 0.1735 -0.0080 -0.0149 0.0114  38  ALA   A O   
1051 C CB  A ALA   A 38  ? 0.1435 0.1427 0.1194 -0.0144 -0.0145 0.0210  38  ALA   A CB  
1052 C CB  B ALA   A 38  ? 0.1315 0.1438 0.1694 -0.0059 -0.0129 0.0188  38  ALA   A CB  
1063 N N   A ALA   A 39  ? 0.1267 0.1260 0.1388 0.0108  -0.0032 0.0204  39  ALA   A N   
1064 N N   B ALA   A 39  ? 0.1368 0.1355 0.1553 -0.0032 0.0049  0.0167  39  ALA   A N   
1065 C CA  A ALA   A 39  ? 0.1219 0.1340 0.1542 0.0153  0.0031  0.0255  39  ALA   A CA  
1066 C CA  B ALA   A 39  ? 0.1281 0.1337 0.1283 -0.0049 -0.0026 0.0079  39  ALA   A CA  
1067 C C   A ALA   A 39  ? 0.1232 0.1310 0.1412 0.0028  -0.0116 0.0100  39  ALA   A C   
1068 C C   B ALA   A 39  ? 0.1275 0.1186 0.1323 0.0015  -0.0079 0.0057  39  ALA   A C   
1069 O O   A ALA   A 39  ? 0.1339 0.1329 0.1179 -0.0123 -0.0047 0.0285  39  ALA   A O   
1070 O O   B ALA   A 39  ? 0.1462 0.1317 0.1473 0.0053  -0.0072 -0.0039 39  ALA   A O   
1071 C CB  A ALA   A 39  ? 0.1250 0.1521 0.1703 0.0205  -0.0104 0.0207  39  ALA   A CB  
1072 C CB  B ALA   A 39  ? 0.1418 0.1513 0.1377 -0.0076 -0.0136 0.0012  39  ALA   A CB  
1083 N N   A ASN   A 40  ? 0.1273 0.1415 0.1580 -0.0051 -0.0036 0.0056  40  ASN   A N   
1084 N N   B ASN   A 40  ? 0.1275 0.1243 0.1343 -0.0119 0.0164  0.0085  40  ASN   A N   
1085 C CA  A ASN   A 40  ? 0.1305 0.1405 0.1385 -0.0074 -0.0124 0.0047  40  ASN   A CA  
1086 C CA  B ASN   A 40  ? 0.1325 0.1248 0.1320 -0.0022 0.0163  0.0247  40  ASN   A CA  
1087 C C   A ASN   A 40  ? 0.1348 0.1420 0.1322 -0.0069 -0.0132 0.0160  40  ASN   A C   
1088 C C   B ASN   A 40  ? 0.1349 0.1137 0.1100 -0.0044 0.0161  0.0230  40  ASN   A C   
1089 O O   A ASN   A 40  ? 0.1272 0.1533 0.1426 -0.0072 -0.0165 0.0237  40  ASN   A O   
1090 O O   B ASN   A 40  ? 0.1296 0.1208 0.1187 -0.0088 0.0106  0.0211  40  ASN   A O   
1091 C CB  A ASN   A 40  ? 0.1479 0.1470 0.1607 -0.0056 -0.0241 -0.0044 40  ASN   A CB  
1092 C CB  B ASN   A 40  ? 0.1452 0.1399 0.1376 0.0079  0.0125  0.0306  40  ASN   A CB  
1093 C CG  A ASN   A 40  ? 0.1689 0.1456 0.1852 -0.0144 -0.0373 -0.0084 40  ASN   A CG  
1094 C CG  B ASN   A 40  ? 0.1597 0.1462 0.1403 0.0077  0.0323  0.0372  40  ASN   A CG  
1095 O OD1 A ASN   A 40  ? 0.1729 0.1382 0.1918 -0.0211 -0.0513 0.0042  40  ASN   A OD1 
1096 O OD1 B ASN   A 40  ? 0.1682 0.1430 0.1433 0.0028  0.0285  0.0199  40  ASN   A OD1 
1097 N ND2 A ASN   A 40  ? 0.1779 0.1523 0.2054 -0.0156 -0.0420 -0.0305 40  ASN   A ND2 
1098 N ND2 B ASN   A 40  ? 0.1629 0.1600 0.1863 0.0108  0.0462  0.0114  40  ASN   A ND2 
1111 N N   A VAL   A 41  ? 0.1407 0.1398 0.1282 -0.0022 0.0006  0.0211  41  VAL   A N   
1112 N N   B VAL   A 41  ? 0.1342 0.1221 0.1227 0.0032  0.0113  0.0199  41  VAL   A N   
1113 C CA  A VAL   A 41  ? 0.1457 0.1451 0.1071 -0.0059 0.0131  0.0202  41  VAL   A CA  
1114 C CA  B VAL   A 41  ? 0.1394 0.1308 0.1406 0.0071  0.0229  0.0204  41  VAL   A CA  
1115 C C   A VAL   A 41  ? 0.1397 0.1410 0.1116 0.0040  0.0082  0.0162  41  VAL   A C   
1116 C C   B VAL   A 41  ? 0.1443 0.1278 0.1328 0.0043  0.0218  0.0177  41  VAL   A C   
1117 O O   A VAL   A 41  ? 0.1475 0.1437 0.1113 0.0097  -0.0101 0.0028  41  VAL   A O   
1118 O O   B VAL   A 41  ? 0.1562 0.1214 0.1178 0.0015  0.0142  0.0195  41  VAL   A O   
1119 C CB  A VAL   A 41  ? 0.1505 0.1533 0.0936 -0.0180 0.0107  0.0087  41  VAL   A CB  
1120 C CB  B VAL   A 41  ? 0.1540 0.1457 0.1659 0.0069  0.0221  0.0156  41  VAL   A CB  
1121 C CG1 A VAL   A 41  ? 0.1436 0.1458 0.1111 -0.0124 -0.0067 0.0180  41  VAL   A CG1 
1122 C CG1 B VAL   A 41  ? 0.1710 0.1531 0.1841 0.0068  0.0194  0.0100  41  VAL   A CG1 
1123 C CG2 A VAL   A 41  ? 0.1620 0.1669 0.1013 -0.0208 0.0194  0.0077  41  VAL   A CG2 
1124 C CG2 B VAL   A 41  ? 0.1778 0.1573 0.1892 0.0015  0.0294  0.0113  41  VAL   A CG2 
1143 N N   A TYR   A 42  ? 0.1249 0.1329 0.1389 -0.0075 0.0110  0.0189  42  TYR   A N   
1144 N N   B TYR   A 42  ? 0.1327 0.1250 0.1760 0.0003  0.0252  0.0240  42  TYR   A N   
1145 C CA  A TYR   A 42  ? 0.1326 0.1290 0.1455 -0.0088 0.0081  0.0230  42  TYR   A CA  
1146 C CA  B TYR   A 42  ? 0.1356 0.1248 0.1743 -0.0044 0.0177  0.0347  42  TYR   A CA  
1147 C C   A TYR   A 42  ? 0.1320 0.1274 0.1506 -0.0020 0.0180  0.0231  42  TYR   A C   
1148 C C   B TYR   A 42  ? 0.1371 0.1261 0.1582 -0.0092 0.0313  0.0368  42  TYR   A C   
1149 O O   A TYR   A 42  ? 0.1305 0.1287 0.1697 0.0034  0.0120  0.0044  42  TYR   A O   
1150 O O   B TYR   A 42  ? 0.1359 0.1289 0.1591 -0.0214 0.0226  0.0268  42  TYR   A O   
1151 C CB  A TYR   A 42  ? 0.1387 0.1381 0.1479 -0.0088 0.0245  0.0246  42  TYR   A CB  
1152 C CB  B TYR   A 42  ? 0.1480 0.1380 0.1747 -0.0015 0.0242  0.0411  42  TYR   A CB  
1153 C CG  A TYR   A 42  ? 0.1408 0.1469 0.1474 -0.0123 0.0292  0.0224  42  TYR   A CG  
1154 C CG  B TYR   A 42  ? 0.1567 0.1496 0.1803 0.0036  0.0115  0.0473  42  TYR   A CG  
1155 C CD1 A TYR   A 42  ? 0.1416 0.1569 0.1489 -0.0180 0.0309  0.0229  42  TYR   A CD1 
1156 C CD1 B TYR   A 42  ? 0.1590 0.1527 0.1833 -0.0050 0.0260  0.0573  42  TYR   A CD1 
1157 C CD2 A TYR   A 42  ? 0.1398 0.1604 0.1513 -0.0019 0.0263  0.0208  42  TYR   A CD2 
1158 C CD2 B TYR   A 42  ? 0.1695 0.1689 0.1994 0.0142  0.0109  0.0410  42  TYR   A CD2 
1159 C CE1 A TYR   A 42  ? 0.1426 0.1666 0.1510 -0.0010 0.0248  0.0055  42  TYR   A CE1 
1160 C CE1 B TYR   A 42  ? 0.1565 0.1604 0.1716 0.0052  0.0288  0.0578  42  TYR   A CE1 
1161 C CE2 A TYR   A 42  ? 0.1385 0.1651 0.1569 -0.0045 0.0204  0.0210  42  TYR   A CE2 
1162 C CE2 B TYR   A 42  ? 0.1737 0.1756 0.2039 0.0104  0.0170  0.0442  42  TYR   A CE2 
1163 C CZ  A TYR   A 42  ? 0.1413 0.1677 0.1388 -0.0040 0.0213  0.0196  42  TYR   A CZ  
1164 C CZ  B TYR   A 42  ? 0.1693 0.1767 0.1763 0.0040  0.0213  0.0465  42  TYR   A CZ  
1165 O OH  A TYR   A 42  ? 0.1459 0.1795 0.1523 0.0026  0.0019  0.0156  42  TYR   A OH  
1166 O OH  B TYR   A 42  ? 0.1741 0.1969 0.1872 -0.0014 0.0159  0.0363  42  TYR   A OH  
1185 N N   . LEU   A 43  ? 0.1364 0.1278 0.1452 -0.0022 0.0166  0.0174  43  LEU   A N   
1186 C CA  . LEU   A 43  ? 0.1285 0.1271 0.1452 -0.0090 0.0083  0.0121  43  LEU   A CA  
1187 C C   . LEU   A 43  ? 0.1307 0.1282 0.1408 -0.0010 0.0102  0.0102  43  LEU   A C   
1188 O O   . LEU   A 43  ? 0.1505 0.1335 0.1703 0.0033  -0.0005 0.0089  43  LEU   A O   
1189 C CB  . LEU   A 43  ? 0.1289 0.1239 0.1701 -0.0058 0.0103  0.0144  43  LEU   A CB  
1190 C CG  . LEU   A 43  ? 0.1411 0.1299 0.1665 -0.0067 0.0140  0.0152  43  LEU   A CG  
1191 C CD1 . LEU   A 43  ? 0.1435 0.1382 0.1751 -0.0009 -0.0007 0.0295  43  LEU   A CD1 
1192 C CD2 . LEU   A 43  ? 0.1611 0.1313 0.1675 -0.0159 0.0062  0.0312  43  LEU   A CD2 
1205 N N   A LYS   A 44  ? 0.1362 0.1326 0.1455 -0.0031 0.0143  0.0093  44  LYS   A N   
1206 N N   B LYS   A 44  ? 0.1323 0.1286 0.1427 0.0002  0.0062  0.0084  44  LYS   A N   
1207 C CA  A LYS   A 44  ? 0.1525 0.1392 0.1529 -0.0058 0.0275  0.0192  44  LYS   A CA  
1208 C CA  B LYS   A 44  ? 0.1502 0.1327 0.1517 0.0013  0.0142  0.0224  44  LYS   A CA  
1209 C C   A LYS   A 44  ? 0.1399 0.1370 0.1412 -0.0000 0.0145  0.0113  44  LYS   A C   
1210 C C   B LYS   A 44  ? 0.1372 0.1343 0.1505 0.0116  -0.0077 0.0128  44  LYS   A C   
1211 O O   A LYS   A 44  ? 0.1469 0.1507 0.1556 -0.0019 0.0054  0.0006  44  LYS   A O   
1212 O O   B LYS   A 44  ? 0.1421 0.1483 0.1722 0.0041  -0.0077 -0.0053 44  LYS   A O   
1213 C CB  A LYS   A 44  ? 0.1844 0.1506 0.1903 -0.0105 0.0310  0.0301  44  LYS   A CB  
1214 C CB  B LYS   A 44  ? 0.1855 0.1402 0.1931 -0.0002 0.0120  0.0353  44  LYS   A CB  
1215 C CG  A LYS   A 44  ? 0.2192 0.1793 0.2500 -0.0110 0.0512  0.0362  44  LYS   A CG  
1216 C CG  B LYS   A 44  ? 0.2207 0.1802 0.2754 -0.0022 0.0348  0.0405  44  LYS   A CG  
1217 C CD  A LYS   A 44  ? 0.2552 0.2127 0.3341 -0.0001 0.0436  0.0263  44  LYS   A CD  
1218 C CD  B LYS   A 44  ? 0.2582 0.2255 0.3725 0.0005  0.0257  0.0355  44  LYS   A CD  
1219 C CE  A LYS   A 44  ? 0.2705 0.2355 0.3859 0.0057  0.0448  0.0201  44  LYS   A CE  
1220 C CE  B LYS   A 44  ? 0.2753 0.2549 0.4266 -0.0030 0.0215  0.0389  44  LYS   A CE  
1221 N NZ  A LYS   A 44  ? 0.2759 0.2529 0.4123 0.0010  0.0511  0.0156  44  LYS   A NZ  
1222 N NZ  B LYS   A 44  ? 0.2861 0.2777 0.4659 -0.0133 0.0232  0.0380  44  LYS   A NZ  
1249 N N   A HIS   A 45  ? 0.1281 0.1283 0.1321 -0.0056 0.0210  0.0128  45  HIS   A N   
1250 N N   B HIS   A 45  ? 0.1318 0.1299 0.1506 0.0038  -0.0112 0.0095  45  HIS   A N   
1251 C CA  A HIS   A 45  ? 0.1225 0.1265 0.1410 -0.0025 0.0222  0.0105  45  HIS   A CA  
1252 C CA  B HIS   A 45  ? 0.1343 0.1364 0.1643 0.0086  -0.0047 0.0036  45  HIS   A CA  
1253 C C   A HIS   A 45  ? 0.1246 0.1299 0.1483 -0.0055 0.0272  0.0154  45  HIS   A C   
1254 C C   B HIS   A 45  ? 0.1474 0.1391 0.1613 0.0095  -0.0090 0.0057  45  HIS   A C   
1255 O O   A HIS   A 45  ? 0.1349 0.1247 0.1544 -0.0071 0.0337  0.0222  45  HIS   A O   
1256 O O   B HIS   A 45  ? 0.1683 0.1533 0.1787 0.0206  -0.0053 0.0047  45  HIS   A O   
1257 C CB  A HIS   A 45  ? 0.1275 0.1179 0.1236 -0.0053 0.0109  -0.0009 45  HIS   A CB  
1258 C CB  B HIS   A 45  ? 0.1385 0.1272 0.1573 0.0020  -0.0013 0.0017  45  HIS   A CB  
1259 C CG  A HIS   A 45  ? 0.1225 0.1075 0.1261 -0.0111 0.0011  0.0112  45  HIS   A CG  
1260 C CG  B HIS   A 45  ? 0.1272 0.1273 0.1347 -0.0029 0.0027  0.0024  45  HIS   A CG  
1261 N ND1 A HIS   A 45  ? 0.1160 0.1028 0.1158 -0.0112 0.0142  -0.0048 45  HIS   A ND1 
1262 N ND1 B HIS   A 45  ? 0.1237 0.1308 0.1580 0.0017  0.0004  0.0086  45  HIS   A ND1 
1263 C CD2 A HIS   A 45  ? 0.1289 0.1125 0.1423 -0.0104 0.0015  0.0071  45  HIS   A CD2 
1264 C CD2 B HIS   A 45  ? 0.1216 0.1208 0.1323 -0.0024 0.0133  0.0019  45  HIS   A CD2 
1265 C CE1 A HIS   A 45  ? 0.1229 0.1175 0.1443 -0.0096 0.0176  0.0005  45  HIS   A CE1 
1266 C CE1 B HIS   A 45  ? 0.1216 0.1160 0.1216 -0.0023 0.0021  -0.0033 45  HIS   A CE1 
1267 N NE2 A HIS   A 45  ? 0.1327 0.1176 0.1630 0.0075  0.0133  -0.0001 45  HIS   A NE2 
1268 N NE2 B HIS   A 45  ? 0.1246 0.1132 0.1153 0.0014  0.0147  0.0059  45  HIS   A NE2 
1283 N N   A GLY   A 46  ? 0.1302 0.1448 0.1611 0.0027  0.0053  0.0252  46  GLY   A N   
1284 N N   B GLY   A 46  ? 0.1497 0.1373 0.1561 0.0023  -0.0177 0.0167  46  GLY   A N   
1285 C CA  A GLY   A 46  ? 0.1342 0.1500 0.1815 0.0078  -0.0060 0.0290  46  GLY   A CA  
1286 C CA  B GLY   A 46  ? 0.1469 0.1507 0.1728 -0.0033 -0.0114 0.0185  46  GLY   A CA  
1287 C C   A GLY   A 46  ? 0.1417 0.1456 0.1761 0.0217  -0.0180 0.0419  46  GLY   A C   
1288 C C   B GLY   A 46  ? 0.1491 0.1481 0.1749 0.0042  -0.0025 0.0255  46  GLY   A C   
1289 O O   A GLY   A 46  ? 0.1532 0.1494 0.1887 0.0240  -0.0268 0.0533  46  GLY   A O   
1290 O O   B GLY   A 46  ? 0.1590 0.1583 0.2107 0.0056  -0.0051 0.0088  46  GLY   A O   
1297 N N   A GLY   A 47  ? 0.1391 0.1456 0.1872 0.0153  -0.0171 0.0175  47  GLY   A N   
1298 N N   B GLY   A 47  ? 0.1533 0.1565 0.1843 -0.0053 0.0092  0.0174  47  GLY   A N   
1299 C CA  A GLY   A 47  ? 0.1340 0.1444 0.1779 0.0237  -0.0176 0.0158  47  GLY   A CA  
1300 C CA  B GLY   A 47  ? 0.1458 0.1562 0.1675 -0.0061 -0.0131 0.0194  47  GLY   A CA  
1301 C C   A GLY   A 47  ? 0.1267 0.1442 0.1717 0.0149  -0.0043 0.0123  47  GLY   A C   
1302 C C   B GLY   A 47  ? 0.1338 0.1519 0.1392 0.0008  -0.0100 0.0209  47  GLY   A C   
1303 O O   A GLY   A 47  ? 0.1233 0.1305 0.1836 0.0117  0.0030  0.0101  47  GLY   A O   
1304 O O   B GLY   A 47  ? 0.1246 0.1443 0.1684 0.0125  -0.0192 0.0195  47  GLY   A O   
1311 N N   A GLY   A 48  ? 0.1208 0.1519 0.1476 0.0165  -0.0040 0.0063  48  GLY   A N   
1312 N N   B GLY   A 48  ? 0.1325 0.1516 0.1338 0.0059  -0.0039 0.0114  48  GLY   A N   
1313 C CA  A GLY   A 48  ? 0.1207 0.1431 0.1415 0.0065  -0.0036 0.0052  48  GLY   A CA  
1314 C CA  B GLY   A 48  ? 0.1327 0.1372 0.1414 0.0066  -0.0046 -0.0015 48  GLY   A CA  
1315 C C   A GLY   A 48  ? 0.1230 0.1391 0.1459 -0.0024 -0.0002 0.0026  48  GLY   A C   
1316 C C   B GLY   A 48  ? 0.1329 0.1359 0.1298 0.0008  0.0018  0.0007  48  GLY   A C   
1317 O O   A GLY   A 48  ? 0.1375 0.1384 0.1425 0.0020  -0.0004 0.0109  48  GLY   A O   
1318 O O   B GLY   A 48  ? 0.1496 0.1401 0.1436 0.0097  0.0144  -0.0009 48  GLY   A O   
1325 N N   A VAL   A 49  ? 0.1266 0.1404 0.1562 -0.0023 -0.0055 0.0131  49  VAL   A N   
1326 N N   B VAL   A 49  ? 0.1266 0.1351 0.1463 -0.0018 -0.0127 -0.0072 49  VAL   A N   
1327 C CA  A VAL   A 49  ? 0.1325 0.1347 0.1627 -0.0054 -0.0029 0.0093  49  VAL   A CA  
1328 C CA  B VAL   A 49  ? 0.1259 0.1393 0.1497 -0.0105 -0.0042 0.0104  49  VAL   A CA  
1329 C C   A VAL   A 49  ? 0.1282 0.1182 0.1336 -0.0055 -0.0022 0.0073  49  VAL   A C   
1330 C C   B VAL   A 49  ? 0.1345 0.1354 0.1201 -0.0074 -0.0018 0.0012  49  VAL   A C   
1331 O O   A VAL   A 49  ? 0.1245 0.1155 0.1336 -0.0087 -0.0076 -0.0127 49  VAL   A O   
1332 O O   B VAL   A 49  ? 0.1357 0.1512 0.1301 -0.0011 0.0169  0.0094  49  VAL   A O   
1333 C CB  A VAL   A 49  ? 0.1411 0.1435 0.1912 -0.0098 0.0017  -0.0056 49  VAL   A CB  
1334 C CB  B VAL   A 49  ? 0.1202 0.1296 0.1626 -0.0097 -0.0136 0.0130  49  VAL   A CB  
1335 C CG1 A VAL   A 49  ? 0.1484 0.1442 0.2083 -0.0055 0.0076  -0.0135 49  VAL   A CG1 
1336 C CG1 B VAL   A 49  ? 0.1186 0.1337 0.1568 0.0065  -0.0013 0.0195  49  VAL   A CG1 
1337 C CG2 A VAL   A 49  ? 0.1466 0.1487 0.2237 -0.0257 0.0105  -0.0063 49  VAL   A CG2 
1338 C CG2 B VAL   A 49  ? 0.1297 0.1224 0.2009 0.0002  -0.0049 0.0248  49  VAL   A CG2 
1357 N N   A ALA   A 50  ? 0.1222 0.1221 0.1353 -0.0049 -0.0091 0.0082  50  ALA   A N   
1358 N N   B ALA   A 50  ? 0.1289 0.1319 0.1184 0.0049  -0.0138 -0.0017 50  ALA   A N   
1359 C CA  A ALA   A 50  ? 0.1222 0.1174 0.1380 -0.0150 -0.0131 0.0132  50  ALA   A CA  
1360 C CA  B ALA   A 50  ? 0.1237 0.1250 0.1050 0.0003  -0.0109 -0.0023 50  ALA   A CA  
1361 C C   A ALA   A 50  ? 0.1217 0.1201 0.1466 -0.0211 -0.0203 0.0069  50  ALA   A C   
1362 C C   B ALA   A 50  ? 0.1145 0.1299 0.1006 -0.0019 0.0007  0.0051  50  ALA   A C   
1363 O O   A ALA   A 50  ? 0.1298 0.1217 0.1484 -0.0161 -0.0151 0.0057  50  ALA   A O   
1364 O O   B ALA   A 50  ? 0.1180 0.1302 0.1183 0.0030  0.0104  0.0055  50  ALA   A O   
1365 C CB  A ALA   A 50  ? 0.1215 0.1279 0.1448 -0.0110 -0.0013 0.0163  50  ALA   A CB  
1366 C CB  B ALA   A 50  ? 0.1280 0.1274 0.1279 0.0108  0.0052  -0.0082 50  ALA   A CB  
1377 N N   A GLY   A 51  ? 0.1352 0.1184 0.1601 -0.0196 -0.0255 0.0061  51  GLY   A N   
1378 N N   B GLY   A 51  ? 0.1263 0.1303 0.1251 0.0111  -0.0059 0.0021  51  GLY   A N   
1379 C CA  A GLY   A 51  ? 0.1364 0.1201 0.1841 -0.0211 -0.0205 0.0075  51  GLY   A CA  
1380 C CA  B GLY   A 51  ? 0.1275 0.1164 0.1392 0.0068  -0.0113 0.0072  51  GLY   A CA  
1381 C C   A GLY   A 51  ? 0.1300 0.1302 0.1868 -0.0118 -0.0093 -0.0042 51  GLY   A C   
1382 C C   B GLY   A 51  ? 0.1246 0.1130 0.1235 0.0076  -0.0064 -0.0028 51  GLY   A C   
1383 O O   A GLY   A 51  ? 0.1345 0.1388 0.1973 -0.0050 -0.0130 -0.0036 51  GLY   A O   
1384 O O   B GLY   A 51  ? 0.1309 0.1171 0.1354 0.0033  -0.0078 -0.0084 51  GLY   A O   
1391 N N   A ALA   A 52  ? 0.1280 0.1352 0.1827 -0.0134 -0.0009 -0.0064 52  ALA   A N   
1392 N N   B ALA   A 52  ? 0.1304 0.1236 0.1205 0.0086  -0.0062 -0.0125 52  ALA   A N   
1393 C CA  A ALA   A 52  ? 0.1259 0.1327 0.1729 -0.0229 0.0054  -0.0039 52  ALA   A CA  
1394 C CA  B ALA   A 52  ? 0.1299 0.1291 0.1477 0.0036  0.0006  -0.0171 52  ALA   A CA  
1395 C C   A ALA   A 52  ? 0.1240 0.1405 0.1758 -0.0187 0.0161  -0.0067 52  ALA   A C   
1396 C C   B ALA   A 52  ? 0.1312 0.1285 0.1271 0.0023  -0.0025 -0.0134 52  ALA   A C   
1397 O O   A ALA   A 52  ? 0.1212 0.1468 0.1884 -0.0095 0.0333  -0.0112 52  ALA   A O   
1398 O O   B ALA   A 52  ? 0.1411 0.1401 0.1343 0.0007  -0.0064 -0.0128 52  ALA   A O   
1399 C CB  A ALA   A 52  ? 0.1320 0.1474 0.1659 -0.0167 -0.0222 0.0071  52  ALA   A CB  
1400 C CB  B ALA   A 52  ? 0.1334 0.1392 0.1668 0.0098  -0.0059 -0.0059 52  ALA   A CB  
1411 N N   A LEU   A 53  ? 0.1217 0.1418 0.1635 -0.0099 0.0134  -0.0008 53  LEU   A N   
1412 N N   B LEU   A 53  ? 0.1237 0.1304 0.1331 -0.0038 -0.0043 -0.0069 53  LEU   A N   
1413 C CA  A LEU   A 53  ? 0.1354 0.1399 0.1689 -0.0070 0.0114  0.0073  53  LEU   A CA  
1414 C CA  B LEU   A 53  ? 0.1334 0.1315 0.1137 0.0005  -0.0080 -0.0018 53  LEU   A CA  
1415 C C   A LEU   A 53  ? 0.1306 0.1373 0.1563 -0.0019 0.0239  0.0043  53  LEU   A C   
1416 C C   B LEU   A 53  ? 0.1273 0.1387 0.0778 0.0087  -0.0022 0.0166  53  LEU   A C   
1417 O O   A LEU   A 53  ? 0.1379 0.1364 0.1601 -0.0008 0.0271  -0.0019 53  LEU   A O   
1418 O O   B LEU   A 53  ? 0.1329 0.1342 0.1073 0.0117  -0.0077 0.0103  53  LEU   A O   
1419 C CB  A LEU   A 53  ? 0.1429 0.1385 0.1761 -0.0096 0.0141  0.0148  53  LEU   A CB  
1420 C CB  B LEU   A 53  ? 0.1377 0.1412 0.1164 -0.0025 -0.0001 -0.0100 53  LEU   A CB  
1421 C CG  A LEU   A 53  ? 0.1476 0.1357 0.1778 -0.0204 0.0050  0.0209  53  LEU   A CG  
1422 C CG  B LEU   A 53  ? 0.1421 0.1466 0.1235 -0.0138 -0.0114 -0.0011 53  LEU   A CG  
1423 C CD1 A LEU   A 53  ? 0.1518 0.1439 0.1853 -0.0177 -0.0005 0.0220  53  LEU   A CD1 
1424 C CD1 B LEU   A 53  ? 0.1484 0.1465 0.1191 -0.0242 -0.0041 0.0072  53  LEU   A CD1 
1425 C CD2 A LEU   A 53  ? 0.1507 0.1491 0.1606 -0.0169 -0.0028 0.0197  53  LEU   A CD2 
1426 C CD2 B LEU   A 53  ? 0.1453 0.1635 0.1225 -0.0243 -0.0147 0.0102  53  LEU   A CD2 
1449 N N   A ASN   A 54  ? 0.1263 0.1203 0.1617 -0.0135 0.0073  -0.0043 54  ASN   A N   
1450 N N   B ASN   A 54  ? 0.1288 0.1317 0.0954 0.0018  -0.0173 0.0036  54  ASN   A N   
1451 C CA  A ASN   A 54  ? 0.1270 0.1166 0.1644 -0.0122 0.0152  -0.0116 54  ASN   A CA  
1452 C CA  B ASN   A 54  ? 0.1222 0.1416 0.1201 0.0066  -0.0138 -0.0025 54  ASN   A CA  
1453 C C   A ASN   A 54  ? 0.1365 0.1261 0.1620 -0.0104 0.0020  -0.0210 54  ASN   A C   
1454 C C   B ASN   A 54  ? 0.1302 0.1427 0.1015 -0.0037 -0.0086 -0.0049 54  ASN   A C   
1455 O O   A ASN   A 54  ? 0.1393 0.1291 0.1486 -0.0110 -0.0099 -0.0247 54  ASN   A O   
1456 O O   B ASN   A 54  ? 0.1306 0.1520 0.1098 -0.0019 0.0003  -0.0003 54  ASN   A O   
1457 C CB  A ASN   A 54  ? 0.1356 0.1097 0.1693 -0.0305 0.0190  -0.0105 54  ASN   A CB  
1458 C CB  B ASN   A 54  ? 0.1236 0.1410 0.1157 0.0116  -0.0181 -0.0013 54  ASN   A CB  
1459 C CG  A ASN   A 54  ? 0.1478 0.1161 0.1818 -0.0229 0.0249  -0.0034 54  ASN   A CG  
1460 C CG  B ASN   A 54  ? 0.1160 0.1430 0.1183 0.0182  -0.0116 -0.0086 54  ASN   A CG  
1461 O OD1 A ASN   A 54  ? 0.1491 0.1157 0.2108 -0.0276 0.0310  0.0142  54  ASN   A OD1 
1462 O OD1 B ASN   A 54  ? 0.1074 0.1296 0.1330 0.0143  -0.0246 -0.0245 54  ASN   A OD1 
1463 N ND2 A ASN   A 54  ? 0.1520 0.1163 0.1874 -0.0191 0.0160  -0.0004 54  ASN   A ND2 
1464 N ND2 B ASN   A 54  ? 0.1231 0.1491 0.1252 0.0068  -0.0195 0.0027  54  ASN   A ND2 
1477 N N   A LYS   A 55  ? 0.1365 0.1371 0.1719 -0.0016 -0.0069 -0.0188 55  LYS   A N   
1478 N N   B LYS   A 55  ? 0.1278 0.1325 0.1046 -0.0062 -0.0112 0.0025  55  LYS   A N   
1479 C CA  A LYS   A 55  ? 0.1455 0.1499 0.1795 0.0054  -0.0120 -0.0248 55  LYS   A CA  
1480 C CA  B LYS   A 55  ? 0.1461 0.1470 0.1314 0.0076  -0.0089 -0.0171 55  LYS   A CA  
1481 C C   A LYS   A 55  ? 0.1344 0.1522 0.1694 0.0043  -0.0067 -0.0171 55  LYS   A C   
1482 C C   B LYS   A 55  ? 0.1382 0.1497 0.1452 0.0051  -0.0108 -0.0130 55  LYS   A C   
1483 O O   A LYS   A 55  ? 0.1340 0.1634 0.1731 -0.0020 -0.0023 -0.0192 55  LYS   A O   
1484 O O   B LYS   A 55  ? 0.1424 0.1560 0.1361 0.0061  -0.0056 -0.0216 55  LYS   A O   
1485 C CB  A LYS   A 55  ? 0.1504 0.1464 0.1762 0.0212  -0.0193 -0.0337 55  LYS   A CB  
1486 C CB  B LYS   A 55  ? 0.1477 0.1520 0.1479 0.0133  0.0047  -0.0158 55  LYS   A CB  
1487 C CG  A LYS   A 55  ? 0.1701 0.1626 0.1768 0.0347  -0.0322 -0.0323 55  LYS   A CG  
1488 C CG  B LYS   A 55  ? 0.1629 0.1908 0.1908 0.0299  0.0019  -0.0270 55  LYS   A CG  
1489 C CD  A LYS   A 55  ? 0.1888 0.1905 0.2016 0.0496  -0.0452 -0.0218 55  LYS   A CD  
1490 C CD  B LYS   A 55  ? 0.1811 0.2214 0.2244 0.0468  -0.0042 -0.0242 55  LYS   A CD  
1491 C CE  A LYS   A 55  ? 0.2075 0.2248 0.2326 0.0595  -0.0507 -0.0260 55  LYS   A CE  
1492 C CE  B LYS   A 55  ? 0.2104 0.2602 0.2603 0.0611  -0.0038 -0.0258 55  LYS   A CE  
1493 N NZ  A LYS   A 55  ? 0.2183 0.2528 0.2402 0.0611  -0.0654 -0.0217 55  LYS   A NZ  
1494 N NZ  B LYS   A 55  ? 0.2263 0.2873 0.2716 0.0633  -0.0157 -0.0198 55  LYS   A NZ  
1521 N N   . ALA   A 56  ? 0.1419 0.1559 0.1622 -0.0016 -0.0105 -0.0167 56  ALA   A N   
1522 C CA  . ALA   A 56  ? 0.1582 0.1792 0.1441 -0.0092 0.0058  -0.0134 56  ALA   A CA  
1523 C C   . ALA   A 56  ? 0.1587 0.1784 0.1174 -0.0039 -0.0022 -0.0301 56  ALA   A C   
1524 O O   . ALA   A 56  ? 0.1612 0.2070 0.1405 -0.0005 0.0033  -0.0145 56  ALA   A O   
1525 C CB  . ALA   A 56  ? 0.1580 0.1964 0.1615 -0.0153 0.0096  0.0020  56  ALA   A CB  
1532 N N   . THR   A 57  ? 0.1393 0.1688 0.1332 -0.0060 0.0049  -0.0173 57  THR   A N   
1533 C CA  . THR   A 57  ? 0.1398 0.1699 0.1376 -0.0088 0.0016  0.0015  57  THR   A CA  
1534 C C   . THR   A 57  ? 0.1460 0.1755 0.1310 -0.0068 -0.0038 -0.0185 57  THR   A C   
1535 O O   . THR   A 57  ? 0.1501 0.1811 0.1460 -0.0097 -0.0141 -0.0224 57  THR   A O   
1536 C CB  . THR   A 57  ? 0.1339 0.1718 0.1246 -0.0109 -0.0020 -0.0010 57  THR   A CB  
1537 O OG1 . THR   A 57  ? 0.1315 0.1556 0.1305 -0.0073 -0.0008 -0.0103 57  THR   A OG1 
1538 C CG2 . THR   A 57  ? 0.1402 0.1679 0.1264 -0.0047 0.0039  0.0175  57  THR   A CG2 
1546 N N   A ASN   A 58  ? 0.1422 0.1687 0.1673 -0.0044 -0.0014 -0.0199 58  ASN   A N   
1547 N N   B ASN   A 58  ? 0.1459 0.1639 0.1683 -0.0067 0.0049  -0.0235 58  ASN   A N   
1548 C CA  A ASN   A 58  ? 0.1621 0.1668 0.1867 -0.0095 0.0124  -0.0296 58  ASN   A CA  
1549 C CA  B ASN   A 58  ? 0.1774 0.1585 0.1845 -0.0152 0.0287  -0.0378 58  ASN   A CA  
1550 C C   A ASN   A 58  ? 0.1438 0.1542 0.1651 -0.0039 -0.0100 -0.0239 58  ASN   A C   
1551 C C   B ASN   A 58  ? 0.1546 0.1421 0.1709 -0.0034 -0.0025 -0.0214 58  ASN   A C   
1552 O O   A ASN   A 58  ? 0.1400 0.1659 0.1757 -0.0069 -0.0162 -0.0312 58  ASN   A O   
1553 O O   B ASN   A 58  ? 0.1582 0.1407 0.1926 -0.0022 -0.0131 -0.0136 58  ASN   A O   
1554 C CB  A ASN   A 58  ? 0.2012 0.1799 0.2231 -0.0187 0.0289  -0.0361 58  ASN   A CB  
1555 C CB  B ASN   A 58  ? 0.2348 0.1752 0.2141 -0.0304 0.0556  -0.0510 58  ASN   A CB  
1556 C CG  A ASN   A 58  ? 0.2400 0.2041 0.2923 -0.0205 0.0287  -0.0238 58  ASN   A CG  
1557 C CG  B ASN   A 58  ? 0.2944 0.2076 0.2970 -0.0330 0.0589  -0.0376 58  ASN   A CG  
1558 O OD1 A ASN   A 58  ? 0.2605 0.2020 0.3272 -0.0040 0.0518  -0.0085 58  ASN   A OD1 
1559 O OD1 B ASN   A 58  ? 0.3198 0.2029 0.3306 -0.0072 0.0951  -0.0238 58  ASN   A OD1 
1560 N ND2 A ASN   A 58  ? 0.2506 0.2147 0.3173 -0.0191 0.0206  -0.0180 58  ASN   A ND2 
1561 N ND2 B ASN   A 58  ? 0.3161 0.2266 0.3331 -0.0465 0.0427  -0.0354 58  ASN   A ND2 
1574 N N   . ASN   A 59  ? 0.1311 0.1403 0.1615 -0.0083 -0.0104 -0.0129 59  ASN   A N   
1575 C CA  . ASN   A 59  ? 0.1355 0.1301 0.1465 -0.0066 -0.0032 -0.0113 59  ASN   A CA  
1576 C C   . ASN   A 59  ? 0.1336 0.1348 0.1346 -0.0096 0.0021  -0.0129 59  ASN   A C   
1577 O O   . ASN   A 59  ? 0.1368 0.1410 0.1379 -0.0046 0.0024  0.0037  59  ASN   A O   
1578 C CB  . ASN   A 59  ? 0.1436 0.1321 0.1660 0.0038  -0.0226 -0.0175 59  ASN   A CB  
1579 C CG  . ASN   A 59  ? 0.1516 0.1313 0.1523 -0.0023 -0.0205 0.0042  59  ASN   A CG  
1580 O OD1 . ASN   A 59  ? 0.1645 0.1454 0.1532 -0.0135 -0.0212 0.0043  59  ASN   A OD1 
1581 N ND2 . ASN   A 59  ? 0.1729 0.1408 0.1597 -0.0214 -0.0152 0.0027  59  ASN   A ND2 
1589 N N   . ALA   A 60  ? 0.1281 0.1420 0.1556 -0.0082 -0.0029 -0.0026 60  ALA   A N   
1590 C CA  . ALA   A 60  ? 0.1338 0.1412 0.1550 -0.0026 -0.0174 -0.0000 60  ALA   A CA  
1591 C C   . ALA   A 60  ? 0.1335 0.1371 0.1610 -0.0031 -0.0060 0.0011  60  ALA   A C   
1592 O O   . ALA   A 60  ? 0.1258 0.1416 0.1712 -0.0037 -0.0039 -0.0059 60  ALA   A O   
1593 C CB  . ALA   A 60  ? 0.1446 0.1539 0.1662 0.0028  -0.0227 -0.0191 60  ALA   A CB  
1599 N N   . MET   A 61  ? 0.1298 0.1232 0.1505 -0.0089 -0.0006 -0.0043 61  MET   A N   
1600 C CA  . MET   A 61  ? 0.1168 0.1241 0.1619 -0.0127 -0.0029 0.0060  61  MET   A CA  
1601 C C   . MET   A 61  ? 0.1217 0.1300 0.1593 -0.0044 -0.0060 0.0116  61  MET   A C   
1602 O O   . MET   A 61  ? 0.1228 0.1345 0.1722 -0.0055 0.0057  0.0123  61  MET   A O   
1603 C CB  . MET   A 61  ? 0.1357 0.1308 0.1512 -0.0082 0.0033  0.0043  61  MET   A CB  
1604 C CG  . MET   A 61  ? 0.1286 0.1403 0.1555 -0.0144 -0.0083 0.0070  61  MET   A CG  
1605 S SD  . MET   A 61  ? 0.1385 0.1412 0.1820 -0.0121 0.0006  -0.0110 61  MET   A SD  
1606 C CE  . MET   A 61  ? 0.1591 0.1437 0.2130 -0.0225 0.0140  -0.0095 61  MET   A CE  
1616 N N   . GLN   A 62  ? 0.1299 0.1342 0.1577 -0.0089 0.0014  0.0093  62  GLN   A N   
1617 C CA  . GLN   A 62  ? 0.1230 0.1257 0.1562 -0.0068 0.0004  0.0103  62  GLN   A CA  
1618 C C   . GLN   A 62  ? 0.1288 0.1118 0.1554 0.0016  0.0062  -0.0021 62  GLN   A C   
1619 O O   . GLN   A 62  ? 0.1300 0.1305 0.1667 -0.0098 0.0045  -0.0019 62  GLN   A O   
1620 C CB  . GLN   A 62  ? 0.1309 0.1246 0.1546 -0.0132 0.0031  0.0008  62  GLN   A CB  
1621 C CG  . GLN   A 62  ? 0.1277 0.1290 0.1766 -0.0101 0.0010  0.0104  62  GLN   A CG  
1622 C CD  . GLN   A 62  ? 0.1405 0.1289 0.1610 -0.0050 0.0096  0.0118  62  GLN   A CD  
1623 O OE1 . GLN   A 62  ? 0.1442 0.1483 0.1599 -0.0048 -0.0046 0.0100  62  GLN   A OE1 
1624 N NE2 . GLN   A 62  ? 0.1422 0.1353 0.1733 -0.0006 0.0082  0.0046  62  GLN   A NE2 
1633 N N   . VAL   A 63  ? 0.1206 0.1250 0.1811 -0.0103 0.0108  -0.0180 63  VAL   A N   
1634 C CA  . VAL   A 63  ? 0.1332 0.1353 0.1891 -0.0117 0.0020  -0.0134 63  VAL   A CA  
1635 C C   . VAL   A 63  ? 0.1166 0.1379 0.1816 -0.0076 -0.0018 -0.0105 63  VAL   A C   
1636 O O   . VAL   A 63  ? 0.1201 0.1401 0.2101 -0.0122 -0.0007 -0.0086 63  VAL   A O   
1637 C CB  . VAL   A 63  ? 0.1420 0.1456 0.2348 -0.0178 -0.0033 -0.0294 63  VAL   A CB  
1638 C CG1 . VAL   A 63  ? 0.1493 0.1707 0.2819 -0.0202 -0.0105 -0.0493 63  VAL   A CG1 
1639 C CG2 . VAL   A 63  ? 0.1536 0.1364 0.2514 -0.0051 0.0050  -0.0277 63  VAL   A CG2 
1649 N N   A GLU   A 64  ? 0.1265 0.1402 0.1660 -0.0110 0.0019  0.0026  64  GLU   A N   
1650 N N   B GLU   A 64  ? 0.1196 0.1470 0.1668 -0.0081 -0.0069 -0.0055 64  GLU   A N   
1651 C CA  A GLU   A 64  ? 0.1332 0.1352 0.1784 -0.0098 -0.0002 0.0117  64  GLU   A CA  
1652 C CA  B GLU   A 64  ? 0.1192 0.1480 0.1833 -0.0003 -0.0162 -0.0015 64  GLU   A CA  
1653 C C   A GLU   A 64  ? 0.1234 0.1323 0.1670 -0.0026 0.0001  0.0212  64  GLU   A C   
1654 C C   B GLU   A 64  ? 0.1149 0.1410 0.1813 0.0057  -0.0063 0.0124  64  GLU   A C   
1655 O O   A GLU   A 64  ? 0.1310 0.1342 0.1578 -0.0060 -0.0003 0.0202  64  GLU   A O   
1656 O O   B GLU   A 64  ? 0.1229 0.1469 0.1923 0.0062  -0.0011 -0.0006 64  GLU   A O   
1657 C CB  A GLU   A 64  ? 0.1482 0.1342 0.1844 -0.0153 0.0098  0.0217  64  GLU   A CB  
1658 C CB  B GLU   A 64  ? 0.1256 0.1568 0.1845 0.0022  -0.0141 -0.0050 64  GLU   A CB  
1659 C CG  A GLU   A 64  ? 0.1563 0.1358 0.2003 -0.0150 0.0113  0.0167  64  GLU   A CG  
1660 C CG  B GLU   A 64  ? 0.1306 0.1675 0.1920 0.0024  -0.0160 -0.0203 64  GLU   A CG  
1661 C CD  A GLU   A 64  ? 0.1624 0.1352 0.1891 -0.0174 0.0239  0.0168  64  GLU   A CD  
1662 C CD  B GLU   A 64  ? 0.1426 0.1805 0.1935 -0.0067 -0.0106 -0.0181 64  GLU   A CD  
1663 O OE1 A GLU   A 64  ? 0.1630 0.1366 0.2079 -0.0169 0.0466  0.0359  64  GLU   A OE1 
1664 O OE1 B GLU   A 64  ? 0.1501 0.1906 0.2065 -0.0064 -0.0255 -0.0277 64  GLU   A OE1 
1665 O OE2 A GLU   A 64  ? 0.1698 0.1304 0.1594 -0.0174 0.0027  0.0049  64  GLU   A OE2 
1666 O OE2 B GLU   A 64  ? 0.1589 0.1807 0.1905 -0.0157 -0.0100 0.0001  64  GLU   A OE2 
1679 N N   . SER   A 65  ? 0.1155 0.1279 0.1710 0.0001  0.0001  0.0065  65  SER   A N   
1680 C CA  . SER   A 65  ? 0.1286 0.1294 0.1689 -0.0001 -0.0006 0.0003  65  SER   A CA  
1681 C C   . SER   A 65  ? 0.1223 0.1434 0.1594 -0.0127 0.0120  0.0119  65  SER   A C   
1682 O O   . SER   A 65  ? 0.1306 0.1519 0.1836 -0.0068 0.0254  -0.0023 65  SER   A O   
1683 C CB  . SER   A 65  ? 0.1280 0.1285 0.1803 -0.0011 0.0103  0.0101  65  SER   A CB  
1684 O OG  . SER   A 65  ? 0.1267 0.1382 0.1705 -0.0099 0.0109  0.0136  65  SER   A OG  
1691 N N   . ASP   A 66  ? 0.1271 0.1389 0.1699 -0.0064 0.0185  0.0193  66  ASP   A N   
1692 C CA  . ASP   A 66  ? 0.1334 0.1530 0.1883 -0.0046 0.0168  0.0167  66  ASP   A CA  
1693 C C   . ASP   A 66  ? 0.1380 0.1475 0.1761 -0.0076 0.0141  0.0137  66  ASP   A C   
1694 O O   . ASP   A 66  ? 0.1389 0.1580 0.1825 -0.0058 0.0235  0.0261  66  ASP   A O   
1695 C CB  . ASP   A 66  ? 0.1423 0.1623 0.2447 0.0053  0.0236  0.0494  66  ASP   A CB  
1696 C CG  . ASP   A 66  ? 0.1933 0.1872 0.2610 -0.0143 0.0061  0.0747  66  ASP   A CG  
1697 O OD1 . ASP   A 66  ? 0.1881 0.2204 0.2401 -0.0156 0.0088  0.0741  66  ASP   A OD1 
1698 O OD2 . ASP   A 66  ? 0.2154 0.2152 0.3367 0.0057  -0.0122 0.0286  66  ASP   A OD2 
1703 N N   A ASP   A 67  ? 0.1295 0.1497 0.1823 -0.0033 0.0106  0.0155  67  ASP   A N   
1704 N N   B ASP   A 67  ? 0.1337 0.1428 0.1741 -0.0077 0.0006  0.0044  67  ASP   A N   
1705 C CA  A ASP   A 67  ? 0.1237 0.1576 0.2109 0.0007  0.0096  0.0275  67  ASP   A CA  
1706 C CA  B ASP   A 67  ? 0.1315 0.1500 0.1929 -0.0097 -0.0028 0.0075  67  ASP   A CA  
1707 C C   A ASP   A 67  ? 0.1180 0.1534 0.2135 0.0067  0.0218  0.0217  67  ASP   A C   
1708 C C   B ASP   A 67  ? 0.1329 0.1519 0.2066 -0.0034 0.0051  0.0071  67  ASP   A C   
1709 O O   A ASP   A 67  ? 0.1007 0.1566 0.2119 0.0143  0.0293  0.0344  67  ASP   A O   
1710 O O   B ASP   A 67  ? 0.1385 0.1626 0.2149 -0.0062 0.0089  0.0101  67  ASP   A O   
1711 C CB  A ASP   A 67  ? 0.1271 0.1664 0.2267 0.0027  0.0011  0.0418  67  ASP   A CB  
1712 C CB  B ASP   A 67  ? 0.1359 0.1523 0.1929 -0.0099 -0.0087 0.0028  67  ASP   A CB  
1713 C CG  A ASP   A 67  ? 0.1234 0.1756 0.2344 -0.0043 0.0047  0.0524  67  ASP   A CG  
1714 C CG  B ASP   A 67  ? 0.1398 0.1510 0.1952 -0.0207 -0.0150 0.0069  67  ASP   A CG  
1715 O OD1 A ASP   A 67  ? 0.1250 0.1835 0.2552 -0.0029 -0.0015 0.0285  67  ASP   A OD1 
1716 O OD1 B ASP   A 67  ? 0.1408 0.1659 0.2383 -0.0171 -0.0216 0.0144  67  ASP   A OD1 
1717 O OD2 A ASP   A 67  ? 0.1253 0.1815 0.2302 -0.0007 0.0035  0.0603  67  ASP   A OD2 
1718 O OD2 B ASP   A 67  ? 0.1533 0.1517 0.1797 -0.0108 -0.0080 -0.0029 67  ASP   A OD2 
1727 N N   . TYR   A 68  ? 0.1340 0.1443 0.2183 -0.0003 0.0189  0.0171  68  TYR   A N   
1728 C CA  . TYR   A 68  ? 0.1434 0.1343 0.2104 -0.0091 0.0161  0.0226  68  TYR   A CA  
1729 C C   . TYR   A 68  ? 0.1354 0.1345 0.2169 -0.0067 0.0195  0.0093  68  TYR   A C   
1730 O O   . TYR   A 68  ? 0.1371 0.1459 0.2282 0.0031  0.0313  0.0128  68  TYR   A O   
1731 C CB  . TYR   A 68  ? 0.1475 0.1372 0.2077 -0.0045 0.0364  0.0257  68  TYR   A CB  
1732 C CG  . TYR   A 68  ? 0.1514 0.1507 0.2244 -0.0066 0.0479  0.0264  68  TYR   A CG  
1733 C CD1 . TYR   A 68  ? 0.1651 0.1481 0.2299 -0.0213 0.0392  -0.0019 68  TYR   A CD1 
1734 C CD2 . TYR   A 68  ? 0.1691 0.1581 0.2630 -0.0027 0.0442  0.0371  68  TYR   A CD2 
1735 C CE1 . TYR   A 68  ? 0.1678 0.1609 0.2618 -0.0255 0.0287  -0.0055 68  TYR   A CE1 
1736 C CE2 . TYR   A 68  ? 0.1632 0.1618 0.2639 -0.0116 0.0438  0.0296  68  TYR   A CE2 
1737 C CZ  . TYR   A 68  ? 0.1657 0.1574 0.2651 -0.0216 0.0383  -0.0017 68  TYR   A CZ  
1738 O OH  . TYR   A 68  ? 0.1961 0.1628 0.2960 -0.0091 0.0130  -0.0210 68  TYR   A OH  
1749 N N   A ILE   A 69  ? 0.1308 0.1316 0.2064 -0.0045 0.0254  0.0125  69  ILE   A N   
1750 N N   B ILE   A 69  ? 0.1304 0.1369 0.1926 -0.0074 0.0258  0.0118  69  ILE   A N   
1751 C CA  A ILE   A 69  ? 0.1342 0.1334 0.2186 -0.0044 0.0220  0.0051  69  ILE   A CA  
1752 C CA  B ILE   A 69  ? 0.1397 0.1458 0.1949 -0.0051 0.0282  -0.0039 69  ILE   A CA  
1753 C C   A ILE   A 69  ? 0.1334 0.1354 0.2240 0.0001  0.0269  0.0139  69  ILE   A C   
1754 C C   B ILE   A 69  ? 0.1362 0.1456 0.1780 -0.0072 0.0329  -0.0107 69  ILE   A C   
1755 O O   A ILE   A 69  ? 0.1361 0.1400 0.2286 0.0009  0.0253  0.0097  69  ILE   A O   
1756 O O   B ILE   A 69  ? 0.1380 0.1527 0.1939 -0.0132 0.0403  -0.0127 69  ILE   A O   
1757 C CB  A ILE   A 69  ? 0.1422 0.1337 0.2100 -0.0091 0.0246  0.0016  69  ILE   A CB  
1758 C CB  B ILE   A 69  ? 0.1408 0.1524 0.1810 -0.0075 0.0403  0.0010  69  ILE   A CB  
1759 C CG1 A ILE   A 69  ? 0.1376 0.1272 0.2110 -0.0107 0.0274  -0.0061 69  ILE   A CG1 
1760 C CG1 B ILE   A 69  ? 0.1431 0.1470 0.1749 -0.0025 0.0341  -0.0044 69  ILE   A CG1 
1761 C CG2 A ILE   A 69  ? 0.1555 0.1533 0.2365 -0.0034 0.0215  0.0001  69  ILE   A CG2 
1762 C CG2 B ILE   A 69  ? 0.1480 0.1606 0.2029 -0.0068 0.0240  0.0104  69  ILE   A CG2 
1763 C CD1 A ILE   A 69  ? 0.1471 0.1321 0.2110 -0.0067 0.0322  0.0040  69  ILE   A CD1 
1764 C CD1 B ILE   A 69  ? 0.1414 0.1482 0.1926 -0.0117 0.0170  -0.0138 69  ILE   A CD1 
1787 N N   A ALA   A 70  ? 0.1321 0.1418 0.2182 -0.0076 0.0250  0.0313  70  ALA   A N   
1788 N N   B ALA   A 70  ? 0.1405 0.1500 0.1777 -0.0105 0.0251  -0.0004 70  ALA   A N   
1789 C CA  A ALA   A 70  ? 0.1404 0.1479 0.2055 -0.0163 0.0255  0.0346  70  ALA   A CA  
1790 C CA  B ALA   A 70  ? 0.1336 0.1588 0.1729 -0.0231 0.0202  0.0031  70  ALA   A CA  
1791 C C   A ALA   A 70  ? 0.1368 0.1640 0.1881 -0.0099 0.0210  0.0257  70  ALA   A C   
1792 C C   B ALA   A 70  ? 0.1263 0.1669 0.1685 -0.0150 0.0193  -0.0022 70  ALA   A C   
1793 O O   A ALA   A 70  ? 0.1454 0.1851 0.1836 0.0058  0.0113  0.0408  70  ALA   A O   
1794 O O   B ALA   A 70  ? 0.1404 0.1914 0.1894 0.0039  0.0269  0.0046  70  ALA   A O   
1795 C CB  A ALA   A 70  ? 0.1456 0.1497 0.2080 -0.0223 0.0364  0.0322  70  ALA   A CB  
1796 C CB  B ALA   A 70  ? 0.1428 0.1686 0.1884 -0.0298 0.0210  -0.0006 70  ALA   A CB  
1807 N N   A THR   A 71  ? 0.1385 0.1682 0.1745 0.0005  0.0203  0.0359  71  THR   A N   
1808 N N   B THR   A 71  ? 0.1294 0.1664 0.1640 -0.0109 0.0126  -0.0021 71  THR   A N   
1809 C CA  A THR   A 71  ? 0.1473 0.1850 0.1726 0.0066  0.0354  0.0487  71  THR   A CA  
1810 C CA  B THR   A 71  ? 0.1465 0.1849 0.1840 -0.0076 -0.0009 0.0130  71  THR   A CA  
1811 C C   A THR   A 71  ? 0.1326 0.1819 0.1699 0.0171  0.0398  0.0383  71  THR   A C   
1812 C C   B THR   A 71  ? 0.1329 0.1742 0.2130 0.0032  -0.0011 0.0002  71  THR   A C   
1813 O O   A THR   A 71  ? 0.1313 0.1988 0.1746 0.0180  0.0322  0.0374  71  THR   A O   
1814 O O   B THR   A 71  ? 0.1353 0.1806 0.2314 0.0155  0.0100  -0.0119 71  THR   A O   
1815 C CB  A THR   A 71  ? 0.1773 0.2062 0.2010 0.0158  0.0239  0.0518  71  THR   A CB  
1816 C CB  B THR   A 71  ? 0.1856 0.2031 0.2087 -0.0111 0.0128  0.0264  71  THR   A CB  
1817 O OG1 A THR   A 71  ? 0.1918 0.2114 0.1964 0.0118  0.0345  0.0464  71  THR   A OG1 
1818 O OG1 B THR   A 71  ? 0.2104 0.2105 0.2278 -0.0184 0.0193  0.0214  71  THR   A OG1 
1819 C CG2 A THR   A 71  ? 0.1885 0.2170 0.2049 0.0255  0.0090  0.0598  71  THR   A CG2 
1820 C CG2 B THR   A 71  ? 0.1935 0.2132 0.2266 -0.0071 0.0065  0.0407  71  THR   A CG2 
1835 N N   A ASN   A 72  ? 0.1382 0.1655 0.1874 0.0210  0.0334  0.0355  72  ASN   A N   
1836 N N   B ASN   A 72  ? 0.1385 0.1636 0.2200 -0.0119 0.0138  0.0012  72  ASN   A N   
1837 C CA  A ASN   A 72  ? 0.1454 0.1561 0.2019 0.0304  0.0321  0.0319  72  ASN   A CA  
1838 C CA  B ASN   A 72  ? 0.1481 0.1662 0.2446 -0.0037 0.0190  -0.0037 72  ASN   A CA  
1839 C C   A ASN   A 72  ? 0.1572 0.1626 0.1990 0.0100  0.0378  0.0235  72  ASN   A C   
1840 C C   B ASN   A 72  ? 0.1502 0.1680 0.2316 -0.0057 0.0220  -0.0204 72  ASN   A C   
1841 O O   A ASN   A 72  ? 0.1605 0.1649 0.2013 0.0074  0.0288  0.0122  72  ASN   A O   
1842 O O   B ASN   A 72  ? 0.1657 0.1763 0.2511 0.0033  0.0194  -0.0262 72  ASN   A O   
1843 C CB  A ASN   A 72  ? 0.1625 0.1630 0.2095 0.0373  0.0368  0.0432  72  ASN   A CB  
1844 C CB  B ASN   A 72  ? 0.1729 0.1807 0.2535 0.0003  0.0233  0.0023  72  ASN   A CB  
1845 C CG  A ASN   A 72  ? 0.1857 0.1718 0.2129 0.0327  0.0415  0.0500  72  ASN   A CG  
1846 C CG  B ASN   A 72  ? 0.1931 0.1975 0.2781 0.0052  0.0216  0.0016  72  ASN   A CG  
1847 O OD1 A ASN   A 72  ? 0.2033 0.1980 0.2217 0.0361  0.0434  0.0496  72  ASN   A OD1 
1848 O OD1 B ASN   A 72  ? 0.2072 0.2321 0.2888 0.0071  0.0252  -0.0015 72  ASN   A OD1 
1849 N ND2 A ASN   A 72  ? 0.1953 0.1624 0.2061 0.0476  0.0322  0.0555  72  ASN   A ND2 
1850 N ND2 B ASN   A 72  ? 0.2090 0.1976 0.3031 0.0242  0.0200  -0.0057 72  ASN   A ND2 
1863 N N   A GLY   A 73  ? 0.1553 0.1603 0.1861 0.0070  0.0330  0.0331  73  GLY   A N   
1864 N N   B GLY   A 73  ? 0.1388 0.1635 0.2162 -0.0118 0.0310  -0.0210 73  GLY   A N   
1865 C CA  A GLY   A 73  ? 0.1559 0.1592 0.1739 0.0054  0.0335  0.0308  73  GLY   A CA  
1866 C CA  B GLY   A 73  ? 0.1499 0.1631 0.2071 -0.0124 0.0355  -0.0165 73  GLY   A CA  
1867 C C   A GLY   A 73  ? 0.1515 0.1525 0.1653 0.0087  0.0242  0.0270  73  GLY   A C   
1868 C C   B GLY   A 73  ? 0.1531 0.1555 0.1976 -0.0142 0.0345  -0.0015 73  GLY   A C   
1869 O O   A GLY   A 73  ? 0.1542 0.1540 0.1580 0.0132  0.0076  0.0275  73  GLY   A O   
1870 O O   B GLY   A 73  ? 0.1494 0.1604 0.1895 -0.0121 0.0230  -0.0092 73  GLY   A O   
1877 N N   A PRO   A 74  ? 0.1521 0.1539 0.1667 0.0145  0.0228  0.0293  74  PRO   A N   
1878 N N   B PRO   A 74  ? 0.1630 0.1412 0.1786 -0.0184 0.0367  0.0118  74  PRO   A N   
1879 C CA  A PRO   A 74  ? 0.1543 0.1543 0.1866 0.0119  0.0119  0.0274  74  PRO   A CA  
1880 C CA  B PRO   A 74  ? 0.1664 0.1428 0.1819 -0.0050 0.0295  0.0182  74  PRO   A CA  
1881 C C   A PRO   A 74  ? 0.1489 0.1481 0.1736 0.0116  0.0146  0.0264  74  PRO   A C   
1882 C C   B PRO   A 74  ? 0.1626 0.1286 0.1809 -0.0067 0.0353  0.0055  74  PRO   A C   
1883 O O   A PRO   A 74  ? 0.1443 0.1536 0.1589 0.0094  0.0154  0.0357  74  PRO   A O   
1884 O O   B PRO   A 74  ? 0.1581 0.1386 0.1731 0.0051  0.0250  -0.0034 74  PRO   A O   
1885 C CB  A PRO   A 74  ? 0.1666 0.1663 0.2012 0.0163  0.0188  0.0356  74  PRO   A CB  
1886 C CB  B PRO   A 74  ? 0.1817 0.1635 0.2059 0.0026  0.0259  0.0294  74  PRO   A CB  
1887 C CG  A PRO   A 74  ? 0.1760 0.1830 0.2196 0.0204  0.0075  0.0302  74  PRO   A CG  
1888 C CG  B PRO   A 74  ? 0.1990 0.2001 0.2444 -0.0068 0.0127  0.0305  74  PRO   A CG  
1889 C CD  A PRO   A 74  ? 0.1610 0.1725 0.1901 0.0233  0.0169  0.0262  74  PRO   A CD  
1890 C CD  B PRO   A 74  ? 0.1794 0.1655 0.1981 -0.0232 0.0067  0.0239  74  PRO   A CD  
1905 N N   A LEU   A 75  ? 0.1543 0.1464 0.1686 0.0140  0.0225  0.0139  75  LEU   A N   
1906 N N   B LEU   A 75  ? 0.1711 0.1215 0.1780 -0.0068 0.0362  -0.0004 75  LEU   A N   
1907 C CA  A LEU   A 75  ? 0.1563 0.1456 0.1512 0.0129  0.0154  0.0206  75  LEU   A CA  
1908 C CA  B LEU   A 75  ? 0.1742 0.1155 0.1738 -0.0134 0.0207  0.0112  75  LEU   A CA  
1909 C C   A LEU   A 75  ? 0.1620 0.1461 0.1335 0.0040  0.0286  0.0161  75  LEU   A C   
1910 C C   B LEU   A 75  ? 0.1825 0.1267 0.1550 -0.0014 0.0272  0.0119  75  LEU   A C   
1911 O O   A LEU   A 75  ? 0.1631 0.1635 0.1339 0.0133  0.0214  0.0092  75  LEU   A O   
1912 O O   B LEU   A 75  ? 0.1983 0.1313 0.1717 0.0073  0.0184  0.0208  75  LEU   A O   
1913 C CB  A LEU   A 75  ? 0.1582 0.1546 0.1530 0.0220  0.0115  0.0195  75  LEU   A CB  
1914 C CB  B LEU   A 75  ? 0.1792 0.1173 0.1813 -0.0271 0.0123  0.0124  75  LEU   A CB  
1915 C CG  A LEU   A 75  ? 0.1689 0.1745 0.1639 0.0155  0.0158  0.0111  75  LEU   A CG  
1916 C CG  B LEU   A 75  ? 0.1931 0.1379 0.2002 -0.0574 0.0077  0.0120  75  LEU   A CG  
1917 C CD1 A LEU   A 75  ? 0.1691 0.1739 0.1546 0.0173  0.0090  -0.0031 75  LEU   A CD1 
1918 C CD1 B LEU   A 75  ? 0.1944 0.1592 0.1890 -0.0640 0.0019  0.0209  75  LEU   A CD1 
1919 C CD2 A LEU   A 75  ? 0.1740 0.2014 0.1873 0.0264  0.0296  0.0155  75  LEU   A CD2 
1920 C CD2 B LEU   A 75  ? 0.2201 0.1923 0.2620 -0.0360 0.0104  0.0124  75  LEU   A CD2 
1943 N N   . LYS   A 76  ? 0.1805 0.1407 0.1622 -0.0047 0.0147  0.0132  76  LYS   A N   
1944 C CA  . LYS   A 76  ? 0.1771 0.1593 0.1595 -0.0047 0.0157  0.0007  76  LYS   A CA  
1945 C C   . LYS   A 76  ? 0.1741 0.1509 0.1426 -0.0039 0.0143  0.0167  76  LYS   A C   
1946 O O   . LYS   A 76  ? 0.1778 0.1412 0.1551 0.0017  0.0095  0.0185  76  LYS   A O   
1947 C CB  . LYS   A 76  ? 0.1822 0.1740 0.1871 0.0050  0.0114  -0.0220 76  LYS   A CB  
1948 C CG  . LYS   A 76  ? 0.1921 0.1740 0.2330 0.0087  0.0029  -0.0236 76  LYS   A CG  
1949 C CD  . LYS   A 76  ? 0.2074 0.1801 0.2815 0.0170  -0.0128 -0.0163 76  LYS   A CD  
1950 C CE  . LYS   A 76  ? 0.2199 0.1930 0.3372 0.0065  -0.0086 -0.0193 76  LYS   A CE  
1951 N NZ  . LYS   A 76  ? 0.2132 0.1801 0.4047 -0.0095 -0.0088 -0.0335 76  LYS   A NZ  
1966 N N   A VAL   A 77  ? 0.1825 0.1606 0.1428 0.0003  0.0234  0.0195  77  VAL   A N   
1967 N N   B VAL   A 77  ? 0.1871 0.1581 0.1423 -0.0054 0.0275  0.0240  77  VAL   A N   
1968 C CA  A VAL   A 77  ? 0.1813 0.1581 0.1455 0.0030  0.0072  0.0183  77  VAL   A CA  
1969 C CA  B VAL   A 77  ? 0.1874 0.1533 0.1509 -0.0077 0.0019  0.0119  77  VAL   A CA  
1970 C C   A VAL   A 77  ? 0.1742 0.1485 0.1359 0.0062  0.0105  0.0124  77  VAL   A C   
1971 C C   B VAL   A 77  ? 0.1764 0.1434 0.1302 -0.0012 0.0106  0.0055  77  VAL   A C   
1972 O O   A VAL   A 77  ? 0.1751 0.1576 0.1490 0.0072  0.0166  0.0107  77  VAL   A O   
1973 O O   B VAL   A 77  ? 0.1754 0.1516 0.1304 -0.0013 0.0150  -0.0051 77  VAL   A O   
1974 C CB  A VAL   A 77  ? 0.1905 0.1714 0.1482 0.0007  0.0068  0.0284  77  VAL   A CB  
1975 C CB  B VAL   A 77  ? 0.2018 0.1670 0.1670 -0.0167 -0.0064 0.0190  77  VAL   A CB  
1976 C CG1 A VAL   A 77  ? 0.1924 0.1785 0.1720 0.0101  0.0005  0.0242  77  VAL   A CG1 
1977 C CG1 B VAL   A 77  ? 0.2057 0.1790 0.1918 -0.0039 -0.0146 0.0161  77  VAL   A CG1 
1978 C CG2 A VAL   A 77  ? 0.2001 0.1782 0.1574 0.0050  0.0088  0.0335  77  VAL   A CG2 
1979 C CG2 B VAL   A 77  ? 0.2151 0.1749 0.1956 -0.0138 -0.0138 0.0215  77  VAL   A CG2 
1998 N N   . GLY   A 78  ? 0.1706 0.1376 0.1356 0.0007  0.0169  0.0072  78  GLY   A N   
1999 C CA  . GLY   A 78  ? 0.1712 0.1345 0.1630 -0.0039 0.0237  0.0176  78  GLY   A CA  
2000 C C   . GLY   A 78  ? 0.1579 0.1265 0.1543 0.0052  0.0251  0.0257  78  GLY   A C   
2001 O O   . GLY   A 78  ? 0.1544 0.1364 0.1800 0.0005  0.0190  0.0264  78  GLY   A O   
2006 N N   . GLY   A 79  ? 0.1687 0.1272 0.1488 -0.0032 0.0184  0.0246  79  GLY   A N   
2007 C CA  . GLY   A 79  ? 0.1652 0.1406 0.1585 -0.0056 0.0143  0.0194  79  GLY   A CA  
2008 C C   . GLY   A 79  ? 0.1398 0.1308 0.1500 0.0010  0.0183  0.0175  79  GLY   A C   
2009 O O   . GLY   A 79  ? 0.1523 0.1529 0.1539 0.0146  0.0155  0.0171  79  GLY   A O   
2013 N N   . SER   A 80  ? 0.1362 0.1441 0.1788 0.0039  0.0085  0.0044  80  SER   A N   
2014 C CA  . SER   A 80  ? 0.1308 0.1378 0.1583 0.0032  0.0021  0.0114  80  SER   A CA  
2015 C C   . SER   A 80  ? 0.1314 0.1477 0.1557 0.0012  0.0078  0.0164  80  SER   A C   
2016 O O   . SER   A 80  ? 0.1290 0.1657 0.2005 0.0109  0.0126  -0.0026 80  SER   A O   
2017 C CB  . SER   A 80  ? 0.1458 0.1355 0.1813 0.0006  0.0093  0.0164  80  SER   A CB  
2018 O OG  . SER   A 80  ? 0.1805 0.1419 0.2280 -0.0001 0.0067  0.0287  80  SER   A OG  
2024 N N   . CYS   A 81  ? 0.1312 0.1359 0.1603 0.0064  -0.0031 0.0199  81  CYS   A N   
2025 C CA  . CYS   A 81  ? 0.1240 0.1437 0.1652 -0.0009 -0.0024 0.0186  81  CYS   A CA  
2026 C C   . CYS   A 81  ? 0.1240 0.1433 0.1470 -0.0048 0.0076  0.0228  81  CYS   A C   
2027 O O   . CYS   A 81  ? 0.1247 0.1698 0.1750 0.0062  0.0106  0.0305  81  CYS   A O   
2028 C CB  . CYS   A 81  ? 0.1368 0.1467 0.1696 -0.0012 0.0078  0.0206  81  CYS   A CB  
2029 S SG  . CYS   A 81  ? 0.1475 0.1386 0.1759 -0.0130 0.0042  0.0159  81  CYS   A SG  
2035 N N   . VAL   A 82  ? 0.1279 0.1497 0.1452 0.0059  -0.0047 0.0187  82  VAL   A N   
2036 C CA  . VAL   A 82  ? 0.1424 0.1574 0.1559 0.0036  -0.0023 0.0252  82  VAL   A CA  
2037 C C   . VAL   A 82  ? 0.1338 0.1546 0.1670 0.0036  0.0038  0.0270  82  VAL   A C   
2038 O O   . VAL   A 82  ? 0.1327 0.1610 0.1793 0.0090  0.0026  0.0040  82  VAL   A O   
2039 C CB  . VAL   A 82  ? 0.1792 0.1638 0.1719 0.0096  0.0026  0.0336  82  VAL   A CB  
2040 C CG1 . VAL   A 82  ? 0.2056 0.1768 0.1823 0.0143  -0.0042 0.0281  82  VAL   A CG1 
2041 C CG2 . VAL   A 82  ? 0.1849 0.1643 0.2022 -0.0018 0.0032  0.0388  82  VAL   A CG2 
2051 N N   . LEU   A 83  ? 0.1253 0.1514 0.1615 -0.0077 -0.0035 0.0149  83  LEU   A N   
2052 C CA  . LEU   A 83  ? 0.1332 0.1504 0.1470 -0.0116 -0.0077 0.0171  83  LEU   A CA  
2053 C C   . LEU   A 83  ? 0.1459 0.1477 0.1535 -0.0090 -0.0161 0.0212  83  LEU   A C   
2054 O O   . LEU   A 83  ? 0.1529 0.1477 0.1652 -0.0146 -0.0105 0.0231  83  LEU   A O   
2055 C CB  . LEU   A 83  ? 0.1437 0.1590 0.1584 -0.0086 -0.0090 0.0194  83  LEU   A CB  
2056 C CG  . LEU   A 83  ? 0.1571 0.1608 0.1656 -0.0079 -0.0003 0.0123  83  LEU   A CG  
2057 C CD1 . LEU   A 83  ? 0.1624 0.1711 0.1795 -0.0207 0.0017  0.0290  83  LEU   A CD1 
2058 C CD2 . LEU   A 83  ? 0.1517 0.1754 0.1774 -0.0129 0.0102  0.0131  83  LEU   A CD2 
2070 N N   . SER   A 84  ? 0.1507 0.1524 0.1779 -0.0154 -0.0101 0.0228  84  SER   A N   
2071 C CA  . SER   A 84  ? 0.1700 0.1627 0.1410 -0.0027 -0.0087 0.0162  84  SER   A CA  
2072 C C   . SER   A 84  ? 0.1739 0.1635 0.1445 -0.0123 0.0020  0.0088  84  SER   A C   
2073 O O   . SER   A 84  ? 0.1596 0.1700 0.1422 -0.0042 -0.0060 0.0187  84  SER   A O   
2074 C CB  . SER   A 84  ? 0.1699 0.1792 0.1596 0.0026  -0.0168 -0.0009 84  SER   A CB  
2075 O OG  . SER   A 84  ? 0.1726 0.2046 0.1831 -0.0077 -0.0289 -0.0170 84  SER   A OG  
2081 N N   A GLY   A 85  ? 0.1833 0.1687 0.1486 -0.0164 0.0105  0.0068  85  GLY   A N   
2082 N N   B GLY   A 85  ? 0.1839 0.1706 0.1498 -0.0054 0.0090  0.0157  85  GLY   A N   
2083 C CA  A GLY   A 85  ? 0.1822 0.1739 0.1576 -0.0207 0.0146  -0.0054 85  GLY   A CA  
2084 C CA  B GLY   A 85  ? 0.1819 0.1833 0.1633 -0.0014 0.0162  0.0081  85  GLY   A CA  
2085 C C   A GLY   A 85  ? 0.1810 0.1808 0.1437 -0.0223 -0.0018 -0.0021 85  GLY   A C   
2086 C C   B GLY   A 85  ? 0.1797 0.1883 0.1436 0.0110  -0.0043 0.0170  85  GLY   A C   
2087 O O   A GLY   A 85  ? 0.1776 0.1867 0.1445 -0.0256 -0.0031 -0.0230 85  GLY   A O   
2088 O O   B GLY   A 85  ? 0.1790 0.1989 0.1634 0.0147  -0.0035 0.0046  85  GLY   A O   
2095 N N   A HIS   A 86  ? 0.1843 0.1787 0.1389 -0.0240 -0.0053 0.0077  86  HIS   A N   
2096 N N   B HIS   A 86  ? 0.1814 0.1821 0.1416 0.0169  -0.0054 0.0117  86  HIS   A N   
2097 C CA  A HIS   A 86  ? 0.1908 0.1830 0.1330 -0.0289 -0.0049 0.0076  86  HIS   A CA  
2098 C CA  B HIS   A 86  ? 0.1929 0.1871 0.1349 0.0158  0.0011  0.0062  86  HIS   A CA  
2099 C C   A HIS   A 86  ? 0.2076 0.1942 0.1081 -0.0277 0.0019  0.0078  86  HIS   A C   
2100 C C   B HIS   A 86  ? 0.2143 0.2056 0.1439 0.0143  0.0015  0.0069  86  HIS   A C   
2101 O O   A HIS   A 86  ? 0.2110 0.2109 0.1077 -0.0237 0.0037  0.0089  86  HIS   A O   
2102 O O   B HIS   A 86  ? 0.2178 0.2234 0.1671 0.0120  -0.0013 0.0090  86  HIS   A O   
2103 C CB  A HIS   A 86  ? 0.1941 0.1849 0.1649 -0.0299 -0.0111 0.0031  86  HIS   A CB  
2104 C CB  B HIS   A 86  ? 0.1941 0.1878 0.1294 0.0186  0.0078  0.0154  86  HIS   A CB  
2105 C CG  A HIS   A 86  ? 0.1928 0.1841 0.1907 -0.0320 -0.0168 0.0079  86  HIS   A CG  
2106 C CG  B HIS   A 86  ? 0.1922 0.1845 0.1230 0.0211  0.0071  0.0207  86  HIS   A CG  
2107 N ND1 A HIS   A 86  ? 0.1987 0.1840 0.2211 -0.0378 -0.0145 0.0113  86  HIS   A ND1 
2108 N ND1 B HIS   A 86  ? 0.2031 0.1881 0.1516 0.0126  0.0142  0.0083  86  HIS   A ND1 
2109 C CD2 A HIS   A 86  ? 0.1886 0.1830 0.1980 -0.0254 -0.0110 0.0110  86  HIS   A CD2 
2110 C CD2 B HIS   A 86  ? 0.1844 0.1797 0.1108 0.0286  0.0191  0.0231  86  HIS   A CD2 
2111 C CE1 A HIS   A 86  ? 0.1954 0.1771 0.2314 -0.0338 -0.0075 0.0130  86  HIS   A CE1 
2112 C CE1 B HIS   A 86  ? 0.1968 0.1805 0.1512 0.0181  0.0246  0.0070  86  HIS   A CE1 
2113 N NE2 A HIS   A 86  ? 0.1907 0.1798 0.2146 -0.0238 -0.0039 0.0205  86  HIS   A NE2 
2114 N NE2 B HIS   A 86  ? 0.1877 0.1773 0.1282 0.0298  0.0198  0.0176  86  HIS   A NE2 
2129 N N   A ASN   A 87  ? 0.2241 0.1962 0.1279 -0.0133 0.0257  -0.0030 87  ASN   A N   
2130 N N   B ASN   A 87  ? 0.2295 0.2092 0.1585 0.0337  0.0170  -0.0028 87  ASN   A N   
2131 C CA  A ASN   A 87  ? 0.2421 0.2001 0.1313 -0.0072 0.0386  -0.0141 87  ASN   A CA  
2132 C CA  B ASN   A 87  ? 0.2494 0.2259 0.1589 0.0371  0.0258  -0.0080 87  ASN   A CA  
2133 C C   A ASN   A 87  ? 0.2386 0.2068 0.1522 -0.0087 0.0640  -0.0011 87  ASN   A C   
2134 C C   B ASN   A 87  ? 0.2485 0.2407 0.1633 0.0246  0.0515  -0.0076 87  ASN   A C   
2135 O O   A ASN   A 87  ? 0.2549 0.2235 0.1827 -0.0120 0.0904  -0.0120 87  ASN   A O   
2136 O O   B ASN   A 87  ? 0.2767 0.2630 0.1793 0.0078  0.0819  -0.0208 87  ASN   A O   
2137 C CB  A ASN   A 87  ? 0.2552 0.2077 0.1531 -0.0017 0.0388  -0.0170 87  ASN   A CB  
2138 C CB  B ASN   A 87  ? 0.2630 0.2313 0.1782 0.0504  0.0227  0.0002  87  ASN   A CB  
2139 C CG  A ASN   A 87  ? 0.2657 0.2195 0.1505 0.0030  0.0489  -0.0156 87  ASN   A CG  
2140 C CG  B ASN   A 87  ? 0.2779 0.2464 0.1759 0.0563  0.0155  0.0163  87  ASN   A CG  
2141 O OD1 A ASN   A 87  ? 0.2741 0.2255 0.1572 0.0047  0.0532  -0.0054 87  ASN   A OD1 
2142 O OD1 B ASN   A 87  ? 0.2819 0.2463 0.1907 0.0673  0.0133  0.0362  87  ASN   A OD1 
2143 N ND2 A ASN   A 87  ? 0.2728 0.2343 0.1649 0.0071  0.0462  -0.0145 87  ASN   A ND2 
2144 N ND2 B ASN   A 87  ? 0.2897 0.2673 0.1916 0.0551  0.0103  0.0165  87  ASN   A ND2 
2157 N N   A LEU   A 88  ? 0.2165 0.1975 0.1500 -0.0113 0.0441  0.0161  88  LEU   A N   
2158 N N   B LEU   A 88  ? 0.2180 0.2261 0.1501 0.0213  0.0276  -0.0062 88  LEU   A N   
2159 C CA  A LEU   A 88  ? 0.1978 0.1902 0.1508 -0.0155 0.0461  0.0379  88  LEU   A CA  
2160 C CA  B LEU   A 88  ? 0.2026 0.2277 0.1629 0.0127  0.0283  0.0008  88  LEU   A CA  
2161 C C   A LEU   A 88  ? 0.1943 0.1870 0.1422 -0.0172 0.0550  0.0555  88  LEU   A C   
2162 C C   B LEU   A 88  ? 0.1931 0.2303 0.1591 0.0071  0.0267  0.0201  88  LEU   A C   
2163 O O   A LEU   A 88  ? 0.1933 0.1928 0.2003 -0.0139 0.0640  0.0676  88  LEU   A O   
2164 O O   B LEU   A 88  ? 0.1985 0.2301 0.1948 0.0050  0.0237  0.0418  88  LEU   A O   
2165 C CB  A LEU   A 88  ? 0.1847 0.1906 0.1534 -0.0174 0.0059  0.0513  88  LEU   A CB  
2166 C CB  B LEU   A 88  ? 0.1995 0.2295 0.1791 0.0085  0.0115  -0.0020 88  LEU   A CB  
2167 C CG  A LEU   A 88  ? 0.1932 0.1942 0.1778 -0.0210 -0.0181 0.0627  88  LEU   A CG  
2168 C CG  B LEU   A 88  ? 0.2096 0.2316 0.2077 0.0152  0.0118  -0.0061 88  LEU   A CG  
2169 C CD1 A LEU   A 88  ? 0.1943 0.1949 0.1729 -0.0345 -0.0314 0.0610  88  LEU   A CD1 
2170 C CD1 B LEU   A 88  ? 0.2107 0.2274 0.2191 0.0167  0.0145  -0.0208 88  LEU   A CD1 
2171 C CD2 A LEU   A 88  ? 0.2103 0.2045 0.2292 -0.0107 -0.0170 0.0490  88  LEU   A CD2 
2172 C CD2 B LEU   A 88  ? 0.2225 0.2400 0.2133 0.0217  0.0171  -0.0167 88  LEU   A CD2 
2195 N N   A ALA   A 89  ? 0.1993 0.1893 0.1369 -0.0094 0.0399  0.0357  89  ALA   A N   
2196 N N   B ALA   A 89  ? 0.1847 0.2293 0.1531 0.0128  0.0190  0.0020  89  ALA   A N   
2197 C CA  A ALA   A 89  ? 0.2038 0.1869 0.1176 -0.0020 0.0280  0.0307  89  ALA   A CA  
2198 C CA  B ALA   A 89  ? 0.1772 0.2298 0.1491 0.0175  0.0093  0.0059  89  ALA   A CA  
2199 C C   A ALA   A 89  ? 0.2112 0.1824 0.1239 0.0073  0.0103  0.0339  89  ALA   A C   
2200 C C   B ALA   A 89  ? 0.1762 0.2303 0.1607 0.0169  0.0129  0.0044  89  ALA   A C   
2201 O O   A ALA   A 89  ? 0.2081 0.1790 0.1693 -0.0022 -0.0086 0.0115  89  ALA   A O   
2202 O O   B ALA   A 89  ? 0.1725 0.2295 0.2048 0.0034  -0.0039 -0.0105 89  ALA   A O   
2203 C CB  A ALA   A 89  ? 0.1942 0.1859 0.1022 -0.0071 0.0374  0.0295  89  ALA   A CB  
2204 C CB  B ALA   A 89  ? 0.1730 0.2173 0.1560 0.0157  0.0066  -0.0060 89  ALA   A CB  
2215 N N   A LYS   A 90  ? 0.2211 0.1963 0.1375 0.0064  -0.0022 0.0322  90  LYS   A N   
2216 N N   B LYS   A 90  ? 0.1734 0.2315 0.1382 0.0117  0.0033  0.0049  90  LYS   A N   
2217 C CA  A LYS   A 90  ? 0.2306 0.2233 0.1828 0.0084  -0.0097 0.0279  90  LYS   A CA  
2218 C CA  B LYS   A 90  ? 0.1815 0.2290 0.1359 0.0138  -0.0233 0.0215  90  LYS   A CA  
2219 C C   A LYS   A 90  ? 0.2163 0.2211 0.1811 0.0023  -0.0109 0.0129  90  LYS   A C   
2220 C C   B LYS   A 90  ? 0.1561 0.1962 0.1355 0.0112  -0.0269 0.0085  90  LYS   A C   
2221 O O   A LYS   A 90  ? 0.2136 0.2390 0.2134 -0.0002 -0.0160 0.0045  90  LYS   A O   
2222 O O   B LYS   A 90  ? 0.1550 0.1906 0.1566 0.0103  -0.0234 0.0024  90  LYS   A O   
2223 C CB  A LYS   A 90  ? 0.2498 0.2558 0.2298 0.0071  -0.0124 0.0423  90  LYS   A CB  
2224 C CB  B LYS   A 90  ? 0.2087 0.2610 0.1436 0.0071  -0.0366 0.0410  90  LYS   A CB  
2225 C CG  A LYS   A 90  ? 0.2716 0.2856 0.3073 0.0073  -0.0113 0.0498  90  LYS   A CG  
2226 C CG  B LYS   A 90  ? 0.2383 0.2863 0.2497 0.0214  -0.0430 0.0562  90  LYS   A CG  
2227 C CD  A LYS   A 90  ? 0.2905 0.3100 0.3769 0.0050  -0.0087 0.0606  90  LYS   A CD  
2228 C CD  B LYS   A 90  ? 0.2658 0.3090 0.3463 0.0286  -0.0358 0.0649  90  LYS   A CD  
2229 C CE  A LYS   A 90  ? 0.3097 0.3286 0.4284 0.0048  -0.0039 0.0669  90  LYS   A CE  
2230 C CE  B LYS   A 90  ? 0.2887 0.3276 0.4225 0.0343  -0.0227 0.0636  90  LYS   A CE  
2231 N NZ  A LYS   A 90  ? 0.3203 0.3413 0.4678 0.0044  -0.0002 0.0664  90  LYS   A NZ  
2232 N NZ  B LYS   A 90  ? 0.2949 0.3305 0.4709 0.0380  -0.0079 0.0589  90  LYS   A NZ  
2259 N N   A HIS   A 91  ? 0.2066 0.2076 0.1613 0.0005  -0.0128 0.0099  91  HIS   A N   
2260 N N   B HIS   A 91  ? 0.1511 0.1717 0.1145 0.0017  -0.0237 0.0125  91  HIS   A N   
2261 C CA  A HIS   A 91  ? 0.1971 0.1925 0.1562 0.0013  -0.0114 0.0155  91  HIS   A CA  
2262 C CA  B HIS   A 91  ? 0.1474 0.1601 0.1216 0.0068  -0.0131 0.0080  91  HIS   A CA  
2263 C C   A HIS   A 91  ? 0.1685 0.1659 0.1318 -0.0042 -0.0024 0.0238  91  HIS   A C   
2264 C C   B HIS   A 91  ? 0.1465 0.1518 0.1086 -0.0019 -0.0135 0.0078  91  HIS   A C   
2265 O O   A HIS   A 91  ? 0.1553 0.1574 0.1462 -0.0026 0.0121  0.0159  91  HIS   A O   
2266 O O   B HIS   A 91  ? 0.1398 0.1594 0.1380 -0.0071 -0.0061 -0.0032 91  HIS   A O   
2267 C CB  A HIS   A 91  ? 0.2192 0.2181 0.1957 0.0078  -0.0231 0.0105  91  HIS   A CB  
2268 C CB  B HIS   A 91  ? 0.1612 0.1903 0.1667 0.0239  -0.0239 0.0235  91  HIS   A CB  
2269 C CG  A HIS   A 91  ? 0.2536 0.2536 0.2365 0.0127  -0.0439 -0.0028 91  HIS   A CG  
2270 C CG  B HIS   A 91  ? 0.2014 0.2391 0.2188 0.0390  -0.0493 0.0151  91  HIS   A CG  
2271 N ND1 A HIS   A 91  ? 0.2666 0.2752 0.2684 0.0164  -0.0557 -0.0165 91  HIS   A ND1 
2272 N ND1 B HIS   A 91  ? 0.2130 0.2719 0.2748 0.0416  -0.0578 -0.0117 91  HIS   A ND1 
2273 C CD2 A HIS   A 91  ? 0.2703 0.2671 0.2518 0.0158  -0.0563 -0.0042 91  HIS   A CD2 
2274 C CD2 B HIS   A 91  ? 0.2313 0.2586 0.2391 0.0418  -0.0598 0.0193  91  HIS   A CD2 
2275 C CE1 A HIS   A 91  ? 0.2728 0.2799 0.2728 0.0218  -0.0608 -0.0143 91  HIS   A CE1 
2276 C CE1 B HIS   A 91  ? 0.2326 0.2817 0.2827 0.0414  -0.0561 -0.0004 91  HIS   A CE1 
2277 N NE2 A HIS   A 91  ? 0.2793 0.2763 0.2652 0.0238  -0.0638 -0.0114 91  HIS   A NE2 
2278 N NE2 B HIS   A 91  ? 0.2434 0.2777 0.2685 0.0458  -0.0593 0.0060  91  HIS   A NE2 
2293 N N   . CYS   A 92  ? 0.1504 0.1578 0.1253 -0.0078 -0.0039 0.0171  92  CYS   A N   
2294 C CA  . CYS   A 92  ? 0.1391 0.1533 0.1230 -0.0090 0.0074  0.0199  92  CYS   A CA  
2295 C C   . CYS   A 92  ? 0.1390 0.1467 0.1277 -0.0167 0.0063  0.0215  92  CYS   A C   
2296 O O   . CYS   A 92  ? 0.1376 0.1514 0.1514 -0.0088 0.0040  0.0086  92  CYS   A O   
2297 C CB  . CYS   A 92  ? 0.1457 0.1600 0.1476 -0.0104 -0.0036 0.0031  92  CYS   A CB  
2298 S SG  . CYS   A 92  ? 0.1438 0.1451 0.1439 -0.0117 -0.0032 0.0182  92  CYS   A SG  
2305 N N   . LEU   A 93  ? 0.1384 0.1348 0.1332 -0.0082 0.0123  0.0140  93  LEU   A N   
2306 C CA  . LEU   A 93  ? 0.1296 0.1346 0.1313 -0.0043 0.0020  0.0181  93  LEU   A CA  
2307 C C   . LEU   A 93  ? 0.1307 0.1317 0.1335 0.0122  0.0036  0.0217  93  LEU   A C   
2308 O O   . LEU   A 93  ? 0.1238 0.1388 0.1350 0.0038  0.0010  0.0184  93  LEU   A O   
2309 C CB  . LEU   A 93  ? 0.1336 0.1319 0.1357 -0.0031 -0.0039 0.0215  93  LEU   A CB  
2310 C CG  . LEU   A 93  ? 0.1468 0.1321 0.1575 -0.0096 0.0070  0.0275  93  LEU   A CG  
2311 C CD1 . LEU   A 93  ? 0.1551 0.1437 0.1816 0.0024  0.0185  0.0282  93  LEU   A CD1 
2312 C CD2 . LEU   A 93  ? 0.1602 0.1330 0.1845 -0.0111 0.0047  0.0199  93  LEU   A CD2 
2324 N N   . HIS   A 94  ? 0.1280 0.1250 0.1305 -0.0086 0.0071  0.0193  94  HIS   A N   
2325 C CA  . HIS   A 94  ? 0.1273 0.1281 0.1442 -0.0061 0.0035  0.0180  94  HIS   A CA  
2326 C C   . HIS   A 94  ? 0.1272 0.1194 0.1462 -0.0117 -0.0043 0.0210  94  HIS   A C   
2327 O O   . HIS   A 94  ? 0.1221 0.1428 0.1729 -0.0036 0.0024  -0.0022 94  HIS   A O   
2328 C CB  . HIS   A 94  ? 0.1256 0.1266 0.1358 -0.0023 -0.0005 0.0195  94  HIS   A CB  
2329 C CG  . HIS   A 94  ? 0.1258 0.1279 0.1365 -0.0043 -0.0077 0.0109  94  HIS   A CG  
2330 N ND1 . HIS   A 94  ? 0.1241 0.1263 0.1415 -0.0015 -0.0041 0.0208  94  HIS   A ND1 
2331 C CD2 . HIS   A 94  ? 0.1348 0.1381 0.1515 -0.0069 -0.0085 0.0082  94  HIS   A CD2 
2332 C CE1 . HIS   A 94  ? 0.1334 0.1243 0.1446 -0.0085 -0.0178 0.0129  94  HIS   A CE1 
2333 N NE2 . HIS   A 94  ? 0.1425 0.1283 0.1463 -0.0131 -0.0042 -0.0018 94  HIS   A NE2 
2341 N N   A VAL   A 95  ? 0.1211 0.1203 0.1347 -0.0113 0.0012  0.0157  95  VAL   A N   
2342 N N   B VAL   A 95  ? 0.1207 0.1281 0.1278 -0.0065 0.0049  0.0083  95  VAL   A N   
2343 C CA  A VAL   A 95  ? 0.1261 0.1141 0.1295 -0.0096 0.0050  0.0157  95  VAL   A CA  
2344 C CA  B VAL   A 95  ? 0.1310 0.1255 0.1263 -0.0024 0.0110  0.0057  95  VAL   A CA  
2345 C C   A VAL   A 95  ? 0.1197 0.1033 0.1301 -0.0169 0.0013  0.0165  95  VAL   A C   
2346 C C   B VAL   A 95  ? 0.1370 0.1297 0.1317 -0.0090 0.0009  0.0052  95  VAL   A C   
2347 O O   A VAL   A 95  ? 0.1104 0.0924 0.1343 -0.0055 -0.0035 0.0207  95  VAL   A O   
2348 O O   B VAL   A 95  ? 0.1424 0.1348 0.1509 0.0008  -0.0023 -0.0023 95  VAL   A O   
2349 C CB  A VAL   A 95  ? 0.1322 0.1184 0.1215 -0.0122 0.0055  0.0196  95  VAL   A CB  
2350 C CB  B VAL   A 95  ? 0.1326 0.1233 0.1457 -0.0108 0.0054  0.0002  95  VAL   A CB  
2351 C CG1 A VAL   A 95  ? 0.1471 0.1282 0.1353 -0.0114 -0.0050 0.0169  95  VAL   A CG1 
2352 C CG1 B VAL   A 95  ? 0.1397 0.1229 0.1787 -0.0065 0.0040  0.0031  95  VAL   A CG1 
2353 C CG2 A VAL   A 95  ? 0.1319 0.1239 0.1277 -0.0058 0.0237  0.0313  95  VAL   A CG2 
2354 C CG2 B VAL   A 95  ? 0.1426 0.1254 0.1527 -0.0081 0.0004  0.0115  95  VAL   A CG2 
2373 N N   A VAL   A 96  ? 0.1325 0.1157 0.1245 -0.0094 0.0050  0.0176  96  VAL   A N   
2374 N N   B VAL   A 96  ? 0.1469 0.1380 0.1307 0.0035  0.0007  0.0135  96  VAL   A N   
2375 C CA  A VAL   A 96  ? 0.1374 0.1232 0.1256 -0.0107 0.0093  0.0151  96  VAL   A CA  
2376 C CA  B VAL   A 96  ? 0.1529 0.1395 0.1304 0.0004  0.0074  0.0200  96  VAL   A CA  
2377 C C   A VAL   A 96  ? 0.1431 0.1317 0.1356 -0.0130 0.0087  0.0117  96  VAL   A C   
2378 C C   B VAL   A 96  ? 0.1537 0.1417 0.1374 0.0026  0.0025  0.0086  96  VAL   A C   
2379 O O   A VAL   A 96  ? 0.1515 0.1308 0.1550 -0.0247 0.0148  0.0060  96  VAL   A O   
2380 O O   B VAL   A 96  ? 0.1676 0.1423 0.1706 0.0002  0.0131  -0.0068 96  VAL   A O   
2381 C CB  A VAL   A 96  ? 0.1326 0.1238 0.1400 -0.0088 0.0057  0.0068  96  VAL   A CB  
2382 C CB  B VAL   A 96  ? 0.1550 0.1406 0.1346 0.0037  0.0140  0.0221  96  VAL   A CB  
2383 C CG1 A VAL   A 96  ? 0.1470 0.1331 0.1421 -0.0167 -0.0002 0.0026  96  VAL   A CG1 
2384 C CG1 B VAL   A 96  ? 0.1596 0.1402 0.1355 -0.0068 0.0234  0.0241  96  VAL   A CG1 
2385 C CG2 A VAL   A 96  ? 0.1166 0.1151 0.1647 -0.0071 0.0114  0.0043  96  VAL   A CG2 
2386 C CG2 B VAL   A 96  ? 0.1529 0.1416 0.1463 0.0043  0.0144  0.0243  96  VAL   A CG2 
2405 N N   A GLY   A 97  ? 0.1477 0.1364 0.1243 -0.0119 0.0137  0.0084  97  GLY   A N   
2406 N N   B GLY   A 97  ? 0.1545 0.1410 0.1215 0.0001  -0.0065 -0.0008 97  GLY   A N   
2407 C CA  A GLY   A 97  ? 0.1559 0.1372 0.1336 -0.0057 0.0041  0.0052  97  GLY   A CA  
2408 C CA  B GLY   A 97  ? 0.1630 0.1528 0.1186 -0.0002 -0.0009 0.0019  97  GLY   A CA  
2409 C C   A GLY   A 97  ? 0.1556 0.1413 0.1248 -0.0030 -0.0054 0.0021  97  GLY   A C   
2410 C C   B GLY   A 97  ? 0.1603 0.1537 0.1179 0.0002  -0.0003 -0.0074 97  GLY   A C   
2411 O O   A GLY   A 97  ? 0.1590 0.1380 0.1237 0.0042  0.0124  0.0078  97  GLY   A O   
2412 O O   B GLY   A 97  ? 0.1693 0.1509 0.1534 -0.0101 0.0102  0.0065  97  GLY   A O   
2419 N N   A PRO   A 98  ? 0.1572 0.1404 0.1233 -0.0037 -0.0080 0.0060  98  PRO   A N   
2420 N N   B PRO   A 98  ? 0.1710 0.1576 0.1222 0.0127  0.0111  0.0074  98  PRO   A N   
2421 C CA  A PRO   A 98  ? 0.1644 0.1562 0.1251 -0.0075 -0.0055 0.0043  98  PRO   A CA  
2422 C CA  B PRO   A 98  ? 0.1847 0.1703 0.1443 0.0178  0.0083  0.0002  98  PRO   A CA  
2423 C C   A PRO   A 98  ? 0.1703 0.1740 0.1070 -0.0190 -0.0047 0.0194  98  PRO   A C   
2424 C C   B PRO   A 98  ? 0.2038 0.1769 0.1360 0.0223  -0.0012 0.0210  98  PRO   A C   
2425 O O   A PRO   A 98  ? 0.1632 0.1621 0.1302 -0.0181 0.0072  0.0166  98  PRO   A O   
2426 O O   B PRO   A 98  ? 0.2053 0.1807 0.1632 0.0255  0.0096  0.0162  98  PRO   A O   
2427 C CB  A PRO   A 98  ? 0.1688 0.1585 0.1252 0.0065  -0.0043 -0.0174 98  PRO   A CB  
2428 C CB  B PRO   A 98  ? 0.1955 0.1734 0.1529 0.0199  -0.0044 0.0072  98  PRO   A CB  
2429 C CG  A PRO   A 98  ? 0.1688 0.1468 0.1282 0.0098  -0.0039 -0.0196 98  PRO   A CG  
2430 C CG  B PRO   A 98  ? 0.1962 0.1689 0.1587 0.0138  -0.0034 -0.0032 98  PRO   A CG  
2431 C CD  A PRO   A 98  ? 0.1590 0.1383 0.1308 0.0030  -0.0093 -0.0007 98  PRO   A CD  
2432 C CD  B PRO   A 98  ? 0.1841 0.1595 0.1493 0.0125  0.0004  0.0017  98  PRO   A CD  
2447 N N   A ASN   A 99  ? 0.1780 0.2042 0.1195 -0.0170 -0.0050 0.0341  99  ASN   A N   
2448 N N   B ASN   A 99  ? 0.2329 0.1818 0.1427 0.0253  -0.0089 0.0378  99  ASN   A N   
2449 C CA  A ASN   A 99  ? 0.1919 0.2219 0.1290 -0.0153 -0.0126 0.0427  99  ASN   A CA  
2450 C CA  B ASN   A 99  ? 0.2626 0.1950 0.1730 0.0258  -0.0102 0.0499  99  ASN   A CA  
2451 C C   A ASN   A 99  ? 0.2116 0.2440 0.1168 -0.0170 -0.0085 0.0502  99  ASN   A C   
2452 C C   B ASN   A 99  ? 0.2828 0.2291 0.1489 0.0254  -0.0163 0.0418  99  ASN   A C   
2453 O O   A ASN   A 99  ? 0.2201 0.2653 0.1347 -0.0120 -0.0012 0.0324  99  ASN   A O   
2454 O O   B ASN   A 99  ? 0.2812 0.2226 0.1207 0.0263  -0.0219 0.0443  99  ASN   A O   
2455 C CB  A ASN   A 99  ? 0.1926 0.2198 0.1515 -0.0086 -0.0292 0.0438  99  ASN   A CB  
2456 C CB  B ASN   A 99  ? 0.2785 0.1943 0.2316 0.0230  -0.0129 0.0692  99  ASN   A CB  
2457 C CG  A ASN   A 99  ? 0.1998 0.2234 0.1714 0.0011  -0.0347 0.0327  99  ASN   A CG  
2458 C CG  B ASN   A 99  ? 0.2937 0.2057 0.2815 0.0207  -0.0123 0.0643  99  ASN   A CG  
2459 O OD1 A ASN   A 99  ? 0.2090 0.2301 0.1661 0.0017  -0.0194 0.0220  99  ASN   A OD1 
2460 O OD1 B ASN   A 99  ? 0.2915 0.2102 0.2716 0.0278  -0.0164 0.0668  99  ASN   A OD1 
2461 N ND2 A ASN   A 99  ? 0.2071 0.2195 0.1940 0.0080  -0.0295 0.0443  99  ASN   A ND2 
2462 N ND2 B ASN   A 99  ? 0.3055 0.2107 0.3433 0.0193  -0.0166 0.0541  99  ASN   A ND2 
2475 N N   A VAL   A 100 ? 0.2220 0.2519 0.1307 -0.0220 -0.0228 0.0485  100 VAL   A N   
2476 N N   B VAL   A 100 ? 0.3140 0.2811 0.1967 0.0213  -0.0250 0.0229  100 VAL   A N   
2477 C CA  A VAL   A 100 ? 0.2426 0.2725 0.1861 -0.0270 -0.0226 0.0494  100 VAL   A CA  
2478 C CA  B VAL   A 100 ? 0.3454 0.3215 0.2707 0.0267  -0.0329 0.0128  100 VAL   A CA  
2479 C C   A VAL   A 100 ? 0.2600 0.2914 0.1966 -0.0313 -0.0365 0.0658  100 VAL   A C   
2480 C C   B VAL   A 100 ? 0.3646 0.3451 0.2810 0.0374  -0.0426 0.0090  100 VAL   A C   
2481 O O   A VAL   A 100 ? 0.2693 0.2977 0.2272 -0.0370 -0.0142 0.0713  100 VAL   A O   
2482 O O   B VAL   A 100 ? 0.3636 0.3521 0.2646 0.0343  -0.0500 0.0005  100 VAL   A O   
2483 C CB  A VAL   A 100 ? 0.2470 0.2748 0.2165 -0.0276 -0.0062 0.0363  100 VAL   A CB  
2484 C CB  B VAL   A 100 ? 0.3568 0.3339 0.3357 0.0220  -0.0306 0.0148  100 VAL   A CB  
2485 C CG1 A VAL   A 100 ? 0.2468 0.2810 0.2339 -0.0295 0.0046  0.0255  100 VAL   A CG1 
2486 C CG1 B VAL   A 100 ? 0.3595 0.3388 0.3560 0.0207  -0.0373 0.0164  100 VAL   A CG1 
2487 C CG2 A VAL   A 100 ? 0.2521 0.2733 0.2233 -0.0264 0.0027  0.0351  100 VAL   A CG2 
2488 C CG2 B VAL   A 100 ? 0.3616 0.3384 0.3640 0.0200  -0.0231 0.0173  100 VAL   A CG2 
2507 N N   A ASN   A 101 ? 0.2734 0.3048 0.1981 -0.0349 -0.0588 0.0808  101 ASN   A N   
2508 N N   B ASN   A 101 ? 0.3824 0.3575 0.2835 0.0537  -0.0453 0.0189  101 ASN   A N   
2509 C CA  A ASN   A 101 ? 0.2911 0.3180 0.2252 -0.0349 -0.0639 0.0849  101 ASN   A CA  
2510 C CA  B ASN   A 101 ? 0.4040 0.3701 0.2973 0.0693  -0.0420 0.0305  101 ASN   A CA  
2511 C C   A ASN   A 101 ? 0.3039 0.3322 0.2449 -0.0328 -0.0366 0.1029  101 ASN   A C   
2512 C C   B ASN   A 101 ? 0.4213 0.3780 0.3071 0.0664  -0.0231 0.0333  101 ASN   A C   
2513 O O   A ASN   A 101 ? 0.3128 0.3332 0.2621 -0.0308 -0.0318 0.1002  101 ASN   A O   
2514 O O   B ASN   A 101 ? 0.4283 0.3838 0.3135 0.0640  -0.0238 0.0351  101 ASN   A O   
2515 C CB  A ASN   A 101 ? 0.2979 0.3166 0.2260 -0.0399 -0.0804 0.0688  101 ASN   A CB  
2516 C CB  B ASN   A 101 ? 0.4100 0.3741 0.3157 0.0786  -0.0481 0.0345  101 ASN   A CB  
2517 C CG  A ASN   A 101 ? 0.3058 0.3192 0.2297 -0.0484 -0.0864 0.0367  101 ASN   A CG  
2518 C CG  B ASN   A 101 ? 0.4142 0.3720 0.3300 0.0877  -0.0510 0.0373  101 ASN   A CG  
2519 O OD1 A ASN   A 101 ? 0.3060 0.3231 0.2237 -0.0475 -0.0867 0.0221  101 ASN   A OD1 
2520 O OD1 B ASN   A 101 ? 0.4133 0.3699 0.3461 0.0937  -0.0632 0.0437  101 ASN   A OD1 
2521 N ND2 A ASN   A 101 ? 0.3124 0.3190 0.2408 -0.0533 -0.0864 0.0317  101 ASN   A ND2 
2522 N ND2 B ASN   A 101 ? 0.4176 0.3720 0.3319 0.0911  -0.0467 0.0395  101 ASN   A ND2 
2535 N N   A LYS   A 102 ? 0.3065 0.3498 0.2705 -0.0362 -0.0190 0.0994  102 LYS   A N   
2536 N N   B LYS   A 102 ? 0.4262 0.3801 0.3199 0.0692  -0.0047 0.0293  102 LYS   A N   
2537 C CA  A LYS   A 102 ? 0.3127 0.3676 0.2827 -0.0358 -0.0101 0.0886  102 LYS   A CA  
2538 C CA  B LYS   A 102 ? 0.4310 0.3856 0.3017 0.0684  0.0162  0.0366  102 LYS   A CA  
2539 C C   A LYS   A 102 ? 0.3190 0.3803 0.2652 -0.0283 -0.0094 0.0925  102 LYS   A C   
2540 C C   B LYS   A 102 ? 0.4103 0.3638 0.2214 0.0780  0.0197  0.0563  102 LYS   A C   
2541 O O   A LYS   A 102 ? 0.3220 0.3905 0.2844 -0.0249 -0.0140 0.0821  102 LYS   A O   
2542 O O   B LYS   A 102 ? 0.4075 0.3598 0.2479 0.0803  0.0267  0.0614  102 LYS   A O   
2543 C CB  A LYS   A 102 ? 0.3119 0.3729 0.3180 -0.0412 -0.0018 0.0630  102 LYS   A CB  
2544 C CB  B LYS   A 102 ? 0.4536 0.4123 0.3825 0.0601  0.0187  0.0164  102 LYS   A CB  
2545 C CG  A LYS   A 102 ? 0.3123 0.3770 0.3351 -0.0437 0.0030  0.0393  102 LYS   A CG  
2546 C CG  B LYS   A 102 ? 0.4723 0.4350 0.4547 0.0528  0.0148  0.0040  102 LYS   A CG  
2547 C CD  A LYS   A 102 ? 0.3167 0.3828 0.3576 -0.0428 0.0048  0.0184  102 LYS   A CD  
2548 C CD  B LYS   A 102 ? 0.4884 0.4539 0.5173 0.0476  0.0100  -0.0053 102 LYS   A CD  
2549 C CE  A LYS   A 102 ? 0.3215 0.3878 0.3766 -0.0394 0.0064  0.0009  102 LYS   A CE  
2550 C CE  B LYS   A 102 ? 0.5025 0.4668 0.5689 0.0457  0.0071  -0.0097 102 LYS   A CE  
2551 N NZ  A LYS   A 102 ? 0.3260 0.3922 0.3829 -0.0381 0.0083  -0.0153 102 LYS   A NZ  
2552 N NZ  B LYS   A 102 ? 0.5088 0.4736 0.5962 0.0444  0.0080  -0.0126 102 LYS   A NZ  
2579 N N   A GLY   A 103 ? 0.3200 0.3853 0.2727 -0.0222 -0.0136 0.0817  103 GLY   A N   
2580 N N   B GLY   A 103 ? 0.3906 0.3506 0.1373 0.0878  0.0109  0.0450  103 GLY   A N   
2581 C CA  A GLY   A 103 ? 0.3216 0.3851 0.2796 -0.0167 -0.0082 0.0696  103 GLY   A CA  
2582 C CA  B GLY   A 103 ? 0.3701 0.3367 0.1336 0.0919  0.0077  0.0425  103 GLY   A CA  
2583 C C   A GLY   A 103 ? 0.3198 0.3850 0.2886 -0.0164 0.0051  0.0578  103 GLY   A C   
2584 C C   B GLY   A 103 ? 0.3474 0.3196 0.1296 0.0884  0.0021  0.0408  103 GLY   A C   
2585 O O   A GLY   A 103 ? 0.3242 0.3886 0.3123 -0.0090 0.0057  0.0482  103 GLY   A O   
2586 O O   B GLY   A 103 ? 0.3565 0.3228 0.1501 0.0924  0.0013  0.0241  103 GLY   A O   
2593 N N   A GLU   A 104 ? 0.3100 0.3808 0.2667 -0.0259 0.0201  0.0498  104 GLU   A N   
2594 N N   B GLU   A 104 ? 0.3170 0.2973 0.1217 0.0779  -0.0075 0.0575  104 GLU   A N   
2595 C CA  A GLU   A 104 ? 0.3031 0.3758 0.2473 -0.0374 0.0254  0.0359  104 GLU   A CA  
2596 C CA  B GLU   A 104 ? 0.2903 0.2798 0.1246 0.0612  -0.0086 0.0450  104 GLU   A CA  
2597 C C   A GLU   A 104 ? 0.3097 0.3786 0.2583 -0.0332 0.0168  0.0135  104 GLU   A C   
2598 C C   B GLU   A 104 ? 0.2781 0.2806 0.1586 0.0569  -0.0012 0.0182  104 GLU   A C   
2599 O O   A GLU   A 104 ? 0.3087 0.3800 0.2725 -0.0351 0.0115  0.0056  104 GLU   A O   
2600 O O   B GLU   A 104 ? 0.2708 0.2823 0.2099 0.0582  -0.0092 0.0020  104 GLU   A O   
2601 C CB  A GLU   A 104 ? 0.2878 0.3664 0.2224 -0.0545 0.0344  0.0463  104 GLU   A CB  
2602 C CB  B GLU   A 104 ? 0.2848 0.2643 0.1325 0.0389  -0.0046 0.0639  104 GLU   A CB  
2603 C CG  A GLU   A 104 ? 0.2770 0.3577 0.2190 -0.0685 0.0274  0.0512  104 GLU   A CG  
2604 C CG  B GLU   A 104 ? 0.2808 0.2572 0.1734 0.0240  -0.0047 0.0607  104 GLU   A CG  
2605 C CD  A GLU   A 104 ? 0.2666 0.3472 0.2053 -0.0787 0.0191  0.0665  104 GLU   A CD  
2606 C CD  B GLU   A 104 ? 0.2863 0.2539 0.1814 0.0079  -0.0211 0.0624  104 GLU   A CD  
2607 O OE1 A GLU   A 104 ? 0.2610 0.3366 0.1700 -0.0842 0.0093  0.0842  104 GLU   A OE1 
2608 O OE1 B GLU   A 104 ? 0.2914 0.2583 0.1792 0.0052  -0.0330 0.0546  104 GLU   A OE1 
2609 O OE2 A GLU   A 104 ? 0.2674 0.3469 0.2101 -0.0799 0.0242  0.0655  104 GLU   A OE2 
2610 O OE2 B GLU   A 104 ? 0.2947 0.2541 0.1994 -0.0095 -0.0131 0.0601  104 GLU   A OE2 
2623 N N   A ASP   A 105 ? 0.3134 0.3802 0.2633 -0.0271 0.0121  -0.0059 105 ASP   A N   
2624 N N   B ASP   A 105 ? 0.2790 0.2712 0.1611 0.0471  0.0001  0.0114  105 ASP   A N   
2625 C CA  A ASP   A 105 ? 0.3156 0.3805 0.2815 -0.0203 0.0060  -0.0292 105 ASP   A CA  
2626 C CA  B ASP   A 105 ? 0.2861 0.2647 0.1980 0.0391  0.0050  -0.0080 105 ASP   A CA  
2627 C C   A ASP   A 105 ? 0.2986 0.3687 0.2609 -0.0299 -0.0082 -0.0510 105 ASP   A C   
2628 C C   B ASP   A 105 ? 0.2745 0.2414 0.1536 0.0232  0.0036  -0.0159 105 ASP   A C   
2629 O O   A ASP   A 105 ? 0.2982 0.3723 0.2667 -0.0288 -0.0102 -0.0552 105 ASP   A O   
2630 O O   B ASP   A 105 ? 0.2633 0.2161 0.1137 0.0313  0.0052  -0.0150 105 ASP   A O   
2631 C CB  A ASP   A 105 ? 0.3312 0.3901 0.3195 -0.0062 0.0128  -0.0286 105 ASP   A CB  
2632 C CB  B ASP   A 105 ? 0.3063 0.2794 0.2738 0.0495  0.0175  -0.0309 105 ASP   A CB  
2633 C CG  A ASP   A 105 ? 0.3425 0.3979 0.3571 0.0031  0.0137  -0.0286 105 ASP   A CG  
2634 C CG  B ASP   A 105 ? 0.3290 0.2946 0.3402 0.0562  0.0338  -0.0534 105 ASP   A CG  
2635 O OD1 A ASP   A 105 ? 0.3466 0.4015 0.3697 0.0029  0.0071  -0.0376 105 ASP   A OD1 
2636 O OD1 B ASP   A 105 ? 0.3331 0.2965 0.3320 0.0558  0.0346  -0.0666 105 ASP   A OD1 
2637 O OD2 A ASP   A 105 ? 0.3493 0.4007 0.3800 0.0087  0.0201  -0.0196 105 ASP   A OD2 
2638 O OD2 B ASP   A 105 ? 0.3412 0.3036 0.4013 0.0589  0.0384  -0.0511 105 ASP   A OD2 
2647 N N   A ILE   A 106 ? 0.2788 0.3484 0.2383 -0.0421 -0.0313 -0.0727 106 ILE   A N   
2648 N N   B ILE   A 106 ? 0.2760 0.2604 0.1951 0.0017  -0.0062 -0.0160 106 ILE   A N   
2649 C CA  A ILE   A 106 ? 0.2585 0.3273 0.2372 -0.0544 -0.0492 -0.0878 106 ILE   A CA  
2650 C CA  B ILE   A 106 ? 0.2766 0.2709 0.2320 -0.0207 -0.0197 -0.0202 106 ILE   A CA  
2651 C C   A ILE   A 106 ? 0.2517 0.3173 0.2591 -0.0662 -0.0399 -0.0966 106 ILE   A C   
2652 C C   B ILE   A 106 ? 0.2802 0.2526 0.2265 -0.0287 -0.0041 -0.0118 106 ILE   A C   
2653 O O   A ILE   A 106 ? 0.2300 0.3083 0.2555 -0.0778 -0.0348 -0.0928 106 ILE   A O   
2654 O O   B ILE   A 106 ? 0.2635 0.2453 0.2239 -0.0323 0.0040  -0.0044 106 ILE   A O   
2655 C CB  A ILE   A 106 ? 0.2517 0.3193 0.2513 -0.0503 -0.0686 -0.0755 106 ILE   A CB  
2656 C CB  B ILE   A 106 ? 0.2780 0.3031 0.2750 -0.0307 -0.0340 -0.0381 106 ILE   A CB  
2657 C CG1 A ILE   A 106 ? 0.2499 0.3150 0.2703 -0.0401 -0.0629 -0.0579 106 ILE   A CG1 
2658 C CG1 B ILE   A 106 ? 0.2749 0.3176 0.3035 -0.0284 -0.0360 -0.0425 106 ILE   A CG1 
2659 C CG2 A ILE   A 106 ? 0.2527 0.3178 0.2501 -0.0491 -0.0732 -0.0748 106 ILE   A CG2 
2660 C CG2 B ILE   A 106 ? 0.2847 0.3125 0.2849 -0.0382 -0.0390 -0.0476 106 ILE   A CG2 
2661 C CD1 A ILE   A 106 ? 0.2490 0.3131 0.2774 -0.0348 -0.0582 -0.0508 106 ILE   A CD1 
2662 C CD1 B ILE   A 106 ? 0.2744 0.3277 0.3444 -0.0277 -0.0334 -0.0418 106 ILE   A CD1 
2685 N N   A GLN   A 107 ? 0.2734 0.3148 0.2977 -0.0604 -0.0272 -0.1003 107 GLN   A N   
2686 N N   B GLN   A 107 ? 0.3024 0.2473 0.2446 -0.0265 0.0061  -0.0315 107 GLN   A N   
2687 C CA  A GLN   A 107 ? 0.2918 0.3123 0.3381 -0.0468 -0.0087 -0.0953 107 GLN   A CA  
2688 C CA  B GLN   A 107 ? 0.3213 0.2508 0.3008 -0.0251 0.0114  -0.0250 107 GLN   A CA  
2689 C C   A GLN   A 107 ? 0.2670 0.2798 0.3177 -0.0367 0.0127  -0.0764 107 GLN   A C   
2690 C C   B GLN   A 107 ? 0.2878 0.2087 0.2576 -0.0238 0.0228  -0.0113 107 GLN   A C   
2691 O O   A GLN   A 107 ? 0.2735 0.2869 0.3699 -0.0361 0.0288  -0.0763 107 GLN   A O   
2692 O O   B GLN   A 107 ? 0.2860 0.2115 0.2542 -0.0296 0.0153  -0.0101 107 GLN   A O   
2693 C CB  A GLN   A 107 ? 0.3326 0.3436 0.4193 -0.0462 -0.0145 -0.0922 107 GLN   A CB  
2694 C CB  B GLN   A 107 ? 0.3664 0.3026 0.3958 -0.0308 -0.0063 -0.0219 107 GLN   A CB  
2695 C CG  A GLN   A 107 ? 0.3763 0.3832 0.5052 -0.0412 -0.0201 -0.0784 107 GLN   A CG  
2696 C CG  B GLN   A 107 ? 0.4147 0.3628 0.4979 -0.0313 -0.0255 0.0002  107 GLN   A CG  
2697 C CD  A GLN   A 107 ? 0.4104 0.4130 0.5775 -0.0376 -0.0255 -0.0617 107 GLN   A CD  
2698 C CD  B GLN   A 107 ? 0.4530 0.4079 0.5852 -0.0320 -0.0395 0.0200  107 GLN   A CD  
2699 O OE1 A GLN   A 107 ? 0.4168 0.4176 0.6065 -0.0358 -0.0273 -0.0549 107 GLN   A OE1 
2700 O OE1 B GLN   A 107 ? 0.4589 0.4179 0.6138 -0.0315 -0.0436 0.0295  107 GLN   A OE1 
2701 N NE2 A GLN   A 107 ? 0.4161 0.4163 0.6023 -0.0382 -0.0276 -0.0576 107 GLN   A NE2 
2702 N NE2 B GLN   A 107 ? 0.4580 0.4154 0.6109 -0.0333 -0.0464 0.0237  107 GLN   A NE2 
2719 N N   A LEU   A 108 ? 0.2392 0.2413 0.2512 -0.0267 0.0180  -0.0638 108 LEU   A N   
2720 N N   B LEU   A 108 ? 0.2574 0.1823 0.2055 -0.0212 0.0319  -0.0184 108 LEU   A N   
2721 C CA  A LEU   A 108 ? 0.2120 0.2126 0.2108 -0.0079 0.0161  -0.0291 108 LEU   A CA  
2722 C CA  B LEU   A 108 ? 0.2303 0.1746 0.1891 -0.0184 0.0362  -0.0083 108 LEU   A CA  
2723 C C   A LEU   A 108 ? 0.1931 0.1785 0.1942 0.0043  0.0085  -0.0087 108 LEU   A C   
2724 C C   B LEU   A 108 ? 0.2004 0.1521 0.1783 -0.0071 0.0285  0.0125  108 LEU   A C   
2725 O O   A LEU   A 108 ? 0.1917 0.1821 0.2131 0.0108  0.0031  -0.0081 108 LEU   A O   
2726 O O   B LEU   A 108 ? 0.1954 0.1493 0.1956 -0.0056 0.0452  0.0221  108 LEU   A O   
2727 C CB  A LEU   A 108 ? 0.2085 0.2195 0.2018 -0.0061 0.0187  -0.0220 108 LEU   A CB  
2728 C CB  B LEU   A 108 ? 0.2377 0.1914 0.1819 -0.0297 0.0309  -0.0260 108 LEU   A CB  
2729 C CG  A LEU   A 108 ? 0.2090 0.2293 0.2178 0.0027  0.0312  -0.0116 108 LEU   A CG  
2730 C CG  B LEU   A 108 ? 0.2545 0.2180 0.2147 -0.0227 0.0350  -0.0305 108 LEU   A CG  
2731 C CD1 A LEU   A 108 ? 0.2155 0.2350 0.2324 0.0015  0.0405  -0.0064 108 LEU   A CD1 
2732 C CD1 B LEU   A 108 ? 0.2632 0.2289 0.2384 -0.0232 0.0503  -0.0223 108 LEU   A CD1 
2733 C CD2 A LEU   A 108 ? 0.2066 0.2361 0.2347 0.0081  0.0370  -0.0195 108 LEU   A CD2 
2734 C CD2 B LEU   A 108 ? 0.2567 0.2341 0.2321 -0.0247 0.0315  -0.0487 108 LEU   A CD2 
2757 N N   . LEU   A 109 ? 0.1862 0.1536 0.1810 0.0051  0.0102  0.0105  109 LEU   A N   
2758 C CA  . LEU   A 109 ? 0.1691 0.1502 0.1680 0.0054  -0.0037 0.0087  109 LEU   A CA  
2759 C C   . LEU   A 109 ? 0.1561 0.1460 0.1791 -0.0063 0.0106  0.0044  109 LEU   A C   
2760 O O   . LEU   A 109 ? 0.1624 0.1456 0.1867 -0.0037 0.0105  0.0137  109 LEU   A O   
2761 C CB  . LEU   A 109 ? 0.1722 0.1619 0.1833 0.0064  -0.0023 0.0219  109 LEU   A CB  
2762 C CG  . LEU   A 109 ? 0.1697 0.1810 0.2141 0.0055  0.0062  0.0252  109 LEU   A CG  
2763 C CD1 . LEU   A 109 ? 0.1737 0.1768 0.2274 0.0016  0.0038  0.0053  109 LEU   A CD1 
2764 C CD2 . LEU   A 109 ? 0.1717 0.2088 0.2462 0.0057  0.0058  0.0424  109 LEU   A CD2 
2777 N N   . LYS   A 110 ? 0.1673 0.1469 0.1759 -0.0048 0.0010  0.0089  110 LYS   A N   
2778 C CA  . LYS   A 110 ? 0.1533 0.1407 0.1885 -0.0123 -0.0033 0.0107  110 LYS   A CA  
2779 C C   . LYS   A 110 ? 0.1569 0.1349 0.1665 -0.0090 0.0072  -0.0076 110 LYS   A C   
2780 O O   . LYS   A 110 ? 0.1515 0.1324 0.1842 -0.0114 0.0126  0.0014  110 LYS   A O   
2781 C CB  . LYS   A 110 ? 0.1662 0.1541 0.2188 -0.0093 -0.0042 -0.0024 110 LYS   A CB  
2782 C CG  . LYS   A 110 ? 0.1674 0.1487 0.2209 -0.0101 -0.0096 0.0056  110 LYS   A CG  
2783 C CD  . LYS   A 110 ? 0.1648 0.1476 0.2397 -0.0113 0.0026  -0.0038 110 LYS   A CD  
2784 C CE  . LYS   A 110 ? 0.1739 0.1560 0.2655 -0.0109 0.0045  -0.0193 110 LYS   A CE  
2785 N NZ  . LYS   A 110 ? 0.1724 0.1589 0.2731 -0.0203 0.0164  -0.0011 110 LYS   A NZ  
2799 N N   . SER   A 111 ? 0.1594 0.1405 0.1717 -0.0068 -0.0019 0.0037  111 SER   A N   
2800 C CA  . SER   A 111 ? 0.1564 0.1465 0.1672 -0.0023 0.0005  0.0086  111 SER   A CA  
2801 C C   . SER   A 111 ? 0.1454 0.1395 0.1714 -0.0073 0.0032  0.0144  111 SER   A C   
2802 O O   . SER   A 111 ? 0.1568 0.1269 0.1887 -0.0012 0.0129  0.0134  111 SER   A O   
2803 C CB  . SER   A 111 ? 0.1743 0.1687 0.1661 -0.0046 0.0167  -0.0180 111 SER   A CB  
2804 O OG  . SER   A 111 ? 0.2088 0.1868 0.1881 -0.0042 0.0226  -0.0277 111 SER   A OG  
2810 N N   . ALA   A 112 ? 0.1497 0.1334 0.1674 -0.0062 0.0106  0.0082  112 ALA   A N   
2811 C CA  . ALA   A 112 ? 0.1521 0.1305 0.1644 -0.0062 0.0107  0.0028  112 ALA   A CA  
2812 C C   . ALA   A 112 ? 0.1368 0.1270 0.1641 -0.0033 0.0032  0.0121  112 ALA   A C   
2813 O O   . ALA   A 112 ? 0.1448 0.1241 0.1820 -0.0152 0.0157  0.0160  112 ALA   A O   
2814 C CB  . ALA   A 112 ? 0.1685 0.1353 0.1656 -0.0048 0.0036  0.0101  112 ALA   A CB  
2820 N N   . TYR   A 113 ? 0.1307 0.1290 0.1728 -0.0117 0.0133  0.0142  113 TYR   A N   
2821 C CA  . TYR   A 113 ? 0.1326 0.1217 0.1682 -0.0093 0.0106  0.0182  113 TYR   A CA  
2822 C C   . TYR   A 113 ? 0.1314 0.1235 0.1629 -0.0171 0.0131  0.0171  113 TYR   A C   
2823 O O   . TYR   A 113 ? 0.1381 0.1294 0.1738 -0.0014 0.0227  0.0142  113 TYR   A O   
2824 C CB  . TYR   A 113 ? 0.1274 0.1309 0.1814 -0.0025 0.0050  0.0206  113 TYR   A CB  
2825 C CG  . TYR   A 113 ? 0.1320 0.1391 0.1786 -0.0139 0.0164  0.0283  113 TYR   A CG  
2826 C CD1 . TYR   A 113 ? 0.1245 0.1480 0.1743 -0.0003 0.0164  0.0253  113 TYR   A CD1 
2827 C CD2 . TYR   A 113 ? 0.1399 0.1483 0.1945 -0.0189 0.0039  0.0209  113 TYR   A CD2 
2828 C CE1 . TYR   A 113 ? 0.1255 0.1624 0.1922 -0.0012 0.0015  0.0194  113 TYR   A CE1 
2829 C CE2 . TYR   A 113 ? 0.1447 0.1615 0.1864 -0.0106 0.0006  0.0305  113 TYR   A CE2 
2830 C CZ  . TYR   A 113 ? 0.1273 0.1614 0.1996 0.0088  0.0042  0.0298  113 TYR   A CZ  
2831 O OH  . TYR   A 113 ? 0.1411 0.1687 0.2223 0.0187  -0.0050 0.0274  113 TYR   A OH  
2841 N N   . GLU   A 114 ? 0.1282 0.1241 0.1667 -0.0032 0.0123  0.0151  114 GLU   A N   
2842 C CA  . GLU   A 114 ? 0.1383 0.1198 0.1853 -0.0032 0.0091  0.0082  114 GLU   A CA  
2843 C C   . GLU   A 114 ? 0.1325 0.1246 0.1702 -0.0034 0.0121  0.0152  114 GLU   A C   
2844 O O   . GLU   A 114 ? 0.1440 0.1318 0.1699 -0.0036 0.0026  0.0111  114 GLU   A O   
2845 C CB  . GLU   A 114 ? 0.1359 0.1241 0.1951 -0.0103 0.0144  0.0194  114 GLU   A CB  
2846 C CG  . GLU   A 114 ? 0.1476 0.1245 0.2067 -0.0031 0.0202  0.0057  114 GLU   A CG  
2847 C CD  . GLU   A 114 ? 0.1591 0.1218 0.2083 -0.0000 0.0137  0.0008  114 GLU   A CD  
2848 O OE1 . GLU   A 114 ? 0.1624 0.1313 0.2117 -0.0115 0.0192  -0.0033 114 GLU   A OE1 
2849 O OE2 . GLU   A 114 ? 0.1757 0.1372 0.2248 -0.0117 0.0172  -0.0180 114 GLU   A OE2 
2856 N N   . ASN   A 115 ? 0.1355 0.1270 0.1703 -0.0133 0.0074  0.0059  115 ASN   A N   
2857 C CA  . ASN   A 115 ? 0.1416 0.1339 0.1711 -0.0082 0.0164  0.0127  115 ASN   A CA  
2858 C C   . ASN   A 115 ? 0.1431 0.1305 0.1626 -0.0099 0.0007  0.0139  115 ASN   A C   
2859 O O   . ASN   A 115 ? 0.1412 0.1404 0.1690 -0.0104 0.0154  0.0182  115 ASN   A O   
2860 C CB  . ASN   A 115 ? 0.1492 0.1383 0.1706 -0.0142 0.0115  0.0062  115 ASN   A CB  
2861 C CG  . ASN   A 115 ? 0.1469 0.1549 0.1697 -0.0120 0.0229  0.0148  115 ASN   A CG  
2862 O OD1 . ASN   A 115 ? 0.1515 0.2579 0.1920 -0.0093 0.0277  0.0308  115 ASN   A OD1 
2863 N ND2 . ASN   A 115 ? 0.1470 0.1383 0.1739 -0.0115 0.0250  0.0248  115 ASN   A ND2 
2870 N N   . PHE   A 116 ? 0.1265 0.1331 0.1823 0.0007  0.0188  0.0116  116 PHE   A N   
2871 C CA  . PHE   A 116 ? 0.1287 0.1425 0.1611 0.0035  0.0173  0.0118  116 PHE   A CA  
2872 C C   . PHE   A 116 ? 0.1348 0.1488 0.1769 -0.0039 0.0178  0.0152  116 PHE   A C   
2873 O O   . PHE   A 116 ? 0.1354 0.1503 0.1861 0.0071  0.0238  0.0309  116 PHE   A O   
2874 C CB  . PHE   A 116 ? 0.1316 0.1394 0.1630 0.0015  0.0163  0.0215  116 PHE   A CB  
2875 C CG  . PHE   A 116 ? 0.1378 0.1277 0.1607 0.0028  0.0142  0.0211  116 PHE   A CG  
2876 C CD1 . PHE   A 116 ? 0.1390 0.1289 0.1795 0.0001  0.0156  0.0144  116 PHE   A CD1 
2877 C CD2 . PHE   A 116 ? 0.1450 0.1275 0.1792 -0.0043 0.0271  0.0306  116 PHE   A CD2 
2878 C CE1 . PHE   A 116 ? 0.1370 0.1322 0.1873 -0.0150 0.0129  0.0102  116 PHE   A CE1 
2879 C CE2 . PHE   A 116 ? 0.1389 0.1291 0.1945 -0.0053 0.0132  0.0256  116 PHE   A CE2 
2880 C CZ  . PHE   A 116 ? 0.1413 0.1157 0.1853 0.0046  0.0092  0.0157  116 PHE   A CZ  
2890 N N   . ASN   A 117 ? 0.1328 0.1404 0.1807 -0.0076 0.0159  0.0321  117 ASN   A N   
2891 C CA  . ASN   A 117 ? 0.1394 0.1355 0.1929 -0.0033 0.0183  0.0296  117 ASN   A CA  
2892 C C   . ASN   A 117 ? 0.1401 0.1384 0.2099 0.0117  0.0214  0.0321  117 ASN   A C   
2893 O O   . ASN   A 117 ? 0.1508 0.1409 0.2221 0.0070  0.0071  0.0259  117 ASN   A O   
2894 C CB  . ASN   A 117 ? 0.1376 0.1451 0.1880 -0.0072 0.0121  0.0368  117 ASN   A CB  
2895 C CG  . ASN   A 117 ? 0.1389 0.1423 0.2006 -0.0035 0.0160  0.0342  117 ASN   A CG  
2896 O OD1 . ASN   A 117 ? 0.1406 0.1559 0.2258 -0.0057 0.0174  0.0206  117 ASN   A OD1 
2897 N ND2 . ASN   A 117 ? 0.1327 0.1356 0.2023 -0.0117 0.0114  0.0268  117 ASN   A ND2 
2904 N N   . GLN   A 118 ? 0.1329 0.1400 0.2158 0.0035  0.0090  0.0350  118 GLN   A N   
2905 C CA  . GLN   A 118 ? 0.1445 0.1515 0.2127 -0.0006 0.0158  0.0241  118 GLN   A CA  
2906 C C   . GLN   A 118 ? 0.1537 0.1558 0.1958 0.0015  0.0111  0.0330  118 GLN   A C   
2907 O O   . GLN   A 118 ? 0.1430 0.1850 0.2183 0.0027  -0.0056 0.0186  118 GLN   A O   
2908 C CB  . GLN   A 118 ? 0.1420 0.1495 0.2205 -0.0047 0.0305  0.0313  118 GLN   A CB  
2909 C CG  . GLN   A 118 ? 0.1390 0.1548 0.2239 0.0053  0.0174  0.0383  118 GLN   A CG  
2910 C CD  . GLN   A 118 ? 0.1354 0.1614 0.2434 0.0075  0.0151  0.0350  118 GLN   A CD  
2911 O OE1 . GLN   A 118 ? 0.1426 0.1674 0.2519 0.0078  0.0108  0.0202  118 GLN   A OE1 
2912 N NE2 . GLN   A 118 ? 0.1433 0.1640 0.2228 0.0013  0.0185  0.0374  118 GLN   A NE2 
2921 N N   . HIS   A 119 ? 0.1498 0.1520 0.1832 0.0085  0.0091  0.0373  119 HIS   A N   
2922 C CA  . HIS   A 119 ? 0.1566 0.1627 0.1849 0.0050  0.0041  0.0425  119 HIS   A CA  
2923 C C   . HIS   A 119 ? 0.1581 0.1735 0.1806 -0.0012 0.0145  0.0483  119 HIS   A C   
2924 O O   . HIS   A 119 ? 0.1552 0.1796 0.1870 -0.0160 0.0016  0.0373  119 HIS   A O   
2925 C CB  . HIS   A 119 ? 0.1602 0.1585 0.1992 0.0059  0.0249  0.0423  119 HIS   A CB  
2926 C CG  . HIS   A 119 ? 0.1561 0.1641 0.2512 0.0036  0.0229  0.0495  119 HIS   A CG  
2927 N ND1 . HIS   A 119 ? 0.1687 0.1753 0.3252 -0.0071 0.0083  0.0255  119 HIS   A ND1 
2928 C CD2 . HIS   A 119 ? 0.1700 0.1661 0.2758 0.0143  0.0335  0.0573  119 HIS   A CD2 
2929 C CE1 . HIS   A 119 ? 0.1715 0.1738 0.3409 -0.0057 0.0256  0.0418  119 HIS   A CE1 
2930 N NE2 . HIS   A 119 ? 0.1802 0.1701 0.3226 0.0022  0.0423  0.0647  119 HIS   A NE2 
2938 N N   A GLU   A 120 ? 0.1756 0.1948 0.1868 0.0038  0.0131  0.0582  120 GLU   A N   
2939 N N   B GLU   A 120 ? 0.1622 0.1838 0.1808 0.0085  0.0008  0.0709  120 GLU   A N   
2940 C CA  A GLU   A 120 ? 0.2015 0.2213 0.2167 0.0068  0.0117  0.0710  120 GLU   A CA  
2941 C CA  B GLU   A 120 ? 0.1815 0.2056 0.2015 0.0156  0.0031  0.1020  120 GLU   A CA  
2942 C C   A GLU   A 120 ? 0.1876 0.2074 0.1839 -0.0018 0.0100  0.0664  120 GLU   A C   
2943 C C   B GLU   A 120 ? 0.1673 0.1967 0.1938 -0.0007 0.0136  0.0928  120 GLU   A C   
2944 O O   A GLU   A 120 ? 0.1805 0.1975 0.1848 -0.0009 -0.0011 0.0546  120 GLU   A O   
2945 O O   B GLU   A 120 ? 0.1668 0.1950 0.2082 -0.0030 0.0168  0.0869  120 GLU   A O   
2946 C CB  A GLU   A 120 ? 0.2490 0.2647 0.2881 0.0128  0.0115  0.0849  120 GLU   A CB  
2947 C CB  B GLU   A 120 ? 0.2338 0.2474 0.2419 0.0252  0.0055  0.1387  120 GLU   A CB  
2948 C CG  A GLU   A 120 ? 0.3100 0.3110 0.3783 0.0236  0.0070  0.0843  120 GLU   A CG  
2949 C CG  B GLU   A 120 ? 0.3130 0.3002 0.3519 0.0397  0.0079  0.1445  120 GLU   A CG  
2950 C CD  A GLU   A 120 ? 0.3587 0.3496 0.4608 0.0379  0.0083  0.0789  120 GLU   A CD  
2951 C CD  B GLU   A 120 ? 0.3720 0.3434 0.4546 0.0561  0.0182  0.1354  120 GLU   A CD  
2952 O OE1 A GLU   A 120 ? 0.3688 0.3599 0.4816 0.0399  0.0090  0.0775  120 GLU   A OE1 
2953 O OE1 B GLU   A 120 ? 0.3890 0.3540 0.4733 0.0586  0.0252  0.1328  120 GLU   A OE1 
2954 O OE2 A GLU   A 120 ? 0.3737 0.3552 0.4976 0.0398  0.0109  0.0758  120 GLU   A OE2 
2955 O OE2 B GLU   A 120 ? 0.3966 0.3493 0.5058 0.0585  0.0222  0.1300  120 GLU   A OE2 
2968 N N   A VAL   A 121 ? 0.1813 0.2069 0.1627 0.0016  0.0160  0.0609  121 VAL   A N   
2969 N N   B VAL   A 121 ? 0.1565 0.1988 0.1770 0.0096  0.0197  0.0730  121 VAL   A N   
2970 C CA  A VAL   A 121 ? 0.1850 0.2112 0.1566 -0.0058 0.0198  0.0658  121 VAL   A CA  
2971 C CA  B VAL   A 121 ? 0.1614 0.2120 0.1611 -0.0002 0.0321  0.0644  121 VAL   A CA  
2972 C C   A VAL   A 121 ? 0.1754 0.1886 0.1531 -0.0177 0.0141  0.0419  121 VAL   A C   
2973 C C   B VAL   A 121 ? 0.1517 0.1888 0.1460 -0.0035 0.0212  0.0481  121 VAL   A C   
2974 O O   A VAL   A 121 ? 0.1847 0.1805 0.1712 -0.0264 0.0142  0.0204  121 VAL   A O   
2975 O O   B VAL   A 121 ? 0.1387 0.1749 0.1360 0.0070  0.0187  0.0262  121 VAL   A O   
2976 C CB  A VAL   A 121 ? 0.2103 0.2428 0.1910 0.0088  0.0182  0.0781  121 VAL   A CB  
2977 C CB  B VAL   A 121 ? 0.1938 0.2486 0.2054 0.0145  0.0352  0.0596  121 VAL   A CB  
2978 C CG1 A VAL   A 121 ? 0.2106 0.2517 0.1954 0.0159  0.0199  0.0798  121 VAL   A CG1 
2979 C CG1 B VAL   A 121 ? 0.1922 0.2596 0.2113 0.0245  0.0348  0.0555  121 VAL   A CG1 
2980 C CG2 A VAL   A 121 ? 0.2251 0.2560 0.2277 0.0066  0.0138  0.0713  121 VAL   A CG2 
2981 C CG2 B VAL   A 121 ? 0.2125 0.2595 0.2419 0.0102  0.0273  0.0488  121 VAL   A CG2 
3000 N N   . LEU   A 122 ? 0.1530 0.1654 0.1582 -0.0184 0.0142  0.0374  122 LEU   A N   
3001 C CA  . LEU   A 122 ? 0.1532 0.1533 0.1643 -0.0168 0.0298  0.0419  122 LEU   A CA  
3002 C C   . LEU   A 122 ? 0.1542 0.1572 0.1524 -0.0206 0.0189  0.0342  122 LEU   A C   
3003 O O   . LEU   A 122 ? 0.1559 0.1620 0.1837 -0.0236 0.0098  0.0337  122 LEU   A O   
3004 C CB  . LEU   A 122 ? 0.1659 0.1540 0.2035 0.0018  0.0218  0.0455  122 LEU   A CB  
3005 C CG  . LEU   A 122 ? 0.1738 0.1579 0.1972 -0.0095 0.0279  0.0265  122 LEU   A CG  
3006 C CD1 . LEU   A 122 ? 0.1981 0.1633 0.2025 -0.0230 0.0310  0.0262  122 LEU   A CD1 
3007 C CD2 . LEU   A 122 ? 0.1760 0.1457 0.1913 -0.0048 0.0394  0.0246  122 LEU   A CD2 
3020 N N   . LEU   A 123 ? 0.1395 0.1512 0.1628 -0.0221 0.0076  0.0275  123 LEU   A N   
3021 C CA  . LEU   A 123 ? 0.1379 0.1500 0.1646 -0.0220 0.0112  0.0296  123 LEU   A CA  
3022 C C   . LEU   A 123 ? 0.1391 0.1491 0.1531 -0.0086 0.0135  0.0382  123 LEU   A C   
3023 O O   . LEU   A 123 ? 0.1334 0.1600 0.1695 -0.0240 0.0129  0.0375  123 LEU   A O   
3024 C CB  . LEU   A 123 ? 0.1459 0.1639 0.1700 -0.0177 0.0209  0.0255  123 LEU   A CB  
3025 C CG  . LEU   A 123 ? 0.1519 0.1763 0.1797 -0.0147 0.0147  0.0180  123 LEU   A CG  
3026 C CD1 . LEU   A 123 ? 0.1566 0.1884 0.1922 -0.0022 0.0145  0.0103  123 LEU   A CD1 
3027 C CD2 . LEU   A 123 ? 0.1698 0.1732 0.1881 -0.0101 0.0060  0.0242  123 LEU   A CD2 
3039 N N   A ALA   A 124 ? 0.1351 0.1513 0.1364 0.0011  0.0190  0.0333  124 ALA   A N   
3040 N N   B ALA   A 124 ? 0.1443 0.1448 0.1545 -0.0245 0.0179  0.0219  124 ALA   A N   
3041 C CA  A ALA   A 124 ? 0.1221 0.1445 0.1250 0.0217  0.0096  0.0350  124 ALA   A CA  
3042 C CA  B ALA   A 124 ? 0.1383 0.1353 0.1573 -0.0354 0.0064  0.0145  124 ALA   A CA  
3043 C C   A ALA   A 124 ? 0.1265 0.1525 0.1517 0.0155  0.0167  0.0239  124 ALA   A C   
3044 C C   B ALA   A 124 ? 0.1356 0.1241 0.1446 -0.0283 0.0108  0.0200  124 ALA   A C   
3045 O O   A ALA   A 124 ? 0.1276 0.1611 0.1573 0.0128  0.0236  0.0338  124 ALA   A O   
3046 O O   B ALA   A 124 ? 0.1337 0.1296 0.1661 -0.0264 0.0207  0.0174  124 ALA   A O   
3047 C CB  A ALA   A 124 ? 0.1180 0.1401 0.1204 0.0276  0.0100  0.0405  124 ALA   A CB  
3048 C CB  B ALA   A 124 ? 0.1531 0.1349 0.1863 -0.0413 0.0105  0.0141  124 ALA   A CB  
3059 N N   A PRO   A 125 ? 0.1319 0.1593 0.1662 0.0133  0.0198  0.0192  125 PRO   A N   
3060 N N   B PRO   A 125 ? 0.1254 0.1204 0.1262 -0.0196 0.0038  0.0394  125 PRO   A N   
3061 C CA  A PRO   A 125 ? 0.1465 0.1604 0.1738 0.0084  0.0038  0.0111  125 PRO   A CA  
3062 C CA  B PRO   A 125 ? 0.1339 0.1257 0.1297 -0.0121 -0.0102 0.0363  125 PRO   A CA  
3063 C C   A PRO   A 125 ? 0.1382 0.1595 0.1750 0.0093  -0.0027 0.0065  125 PRO   A C   
3064 C C   B PRO   A 125 ? 0.1255 0.1399 0.1424 -0.0097 -0.0082 0.0398  125 PRO   A C   
3065 O O   A PRO   A 125 ? 0.1410 0.1581 0.1850 0.0056  0.0018  -0.0037 125 PRO   A O   
3066 O O   B PRO   A 125 ? 0.1344 0.1404 0.1592 -0.0143 -0.0188 0.0347  125 PRO   A O   
3067 C CB  A PRO   A 125 ? 0.1562 0.1679 0.1754 -0.0001 0.0137  0.0093  125 PRO   A CB  
3068 C CB  B PRO   A 125 ? 0.1356 0.1240 0.1334 -0.0127 0.0016  0.0371  125 PRO   A CB  
3069 C CG  A PRO   A 125 ? 0.1576 0.1670 0.1658 0.0027  0.0078  0.0152  125 PRO   A CG  
3070 C CG  B PRO   A 125 ? 0.1171 0.1220 0.1258 -0.0089 0.0099  0.0298  125 PRO   A CG  
3071 C CD  A PRO   A 125 ? 0.1431 0.1632 0.1658 0.0078  0.0238  0.0127  125 PRO   A CD  
3072 C CD  B PRO   A 125 ? 0.1152 0.1139 0.1225 -0.0138 0.0183  0.0255  125 PRO   A CD  
3087 N N   A LEU   A 126 ? 0.1408 0.1661 0.1696 0.0135  -0.0055 -0.0016 126 LEU   A N   
3088 N N   B LEU   A 126 ? 0.1352 0.1681 0.1627 -0.0013 0.0006  0.0273  126 LEU   A N   
3089 C CA  A LEU   A 126 ? 0.1501 0.1649 0.1685 0.0040  -0.0139 0.0076  126 LEU   A CA  
3090 C CA  B LEU   A 126 ? 0.1449 0.1688 0.1845 -0.0028 -0.0023 0.0410  126 LEU   A CA  
3091 C C   A LEU   A 126 ? 0.1559 0.1573 0.1658 -0.0052 -0.0070 0.0053  126 LEU   A C   
3092 C C   B LEU   A 126 ? 0.1495 0.1709 0.1856 0.0115  0.0047  0.0430  126 LEU   A C   
3093 O O   A LEU   A 126 ? 0.1679 0.1469 0.1700 -0.0133 -0.0001 0.0002  126 LEU   A O   
3094 O O   B LEU   A 126 ? 0.1620 0.1754 0.2308 0.0110  0.0353  0.0542  126 LEU   A O   
3095 C CB  A LEU   A 126 ? 0.1610 0.1790 0.1754 -0.0030 -0.0182 0.0148  126 LEU   A CB  
3096 C CB  B LEU   A 126 ? 0.1648 0.1914 0.2207 -0.0161 0.0003  0.0345  126 LEU   A CB  
3097 C CG  A LEU   A 126 ? 0.1619 0.1980 0.1637 -0.0075 -0.0110 0.0225  126 LEU   A CG  
3098 C CG  B LEU   A 126 ? 0.1701 0.2080 0.2524 -0.0211 0.0032  0.0390  126 LEU   A CG  
3099 C CD1 A LEU   A 126 ? 0.1634 0.2024 0.1914 -0.0044 -0.0012 0.0188  126 LEU   A CD1 
3100 C CD1 B LEU   A 126 ? 0.1730 0.2108 0.2574 -0.0151 -0.0030 0.0374  126 LEU   A CD1 
3101 C CD2 A LEU   A 126 ? 0.1700 0.1952 0.1216 -0.0172 -0.0256 0.0482  126 LEU   A CD2 
3102 C CD2 B LEU   A 126 ? 0.1798 0.2071 0.2693 -0.0275 -0.0033 0.0403  126 LEU   A CD2 
3125 N N   A LEU   A 127 ? 0.1528 0.1613 0.1711 -0.0086 0.0094  0.0009  127 LEU   A N   
3126 N N   B LEU   A 127 ? 0.1523 0.1700 0.1657 0.0142  0.0064  0.0389  127 LEU   A N   
3127 C CA  A LEU   A 127 ? 0.1557 0.1589 0.1652 -0.0051 0.0142  0.0068  127 LEU   A CA  
3128 C CA  B LEU   A 127 ? 0.1564 0.1838 0.1786 0.0082  0.0060  0.0385  127 LEU   A CA  
3129 C C   A LEU   A 127 ? 0.1507 0.1484 0.1458 -0.0140 0.0057  0.0132  127 LEU   A C   
3130 C C   B LEU   A 127 ? 0.1713 0.2026 0.1871 -0.0006 0.0013  0.0446  127 LEU   A C   
3131 O O   A LEU   A 127 ? 0.1529 0.1485 0.1393 -0.0276 -0.0024 0.0138  127 LEU   A O   
3132 O O   B LEU   A 127 ? 0.1836 0.2135 0.1914 -0.0108 -0.0041 0.0495  127 LEU   A O   
3133 C CB  A LEU   A 127 ? 0.1661 0.1659 0.1814 0.0091  0.0156  0.0007  127 LEU   A CB  
3134 C CB  B LEU   A 127 ? 0.1488 0.1848 0.1822 0.0076  0.0055  0.0277  127 LEU   A CB  
3135 C CG  A LEU   A 127 ? 0.1785 0.1595 0.1887 0.0138  0.0098  0.0082  127 LEU   A CG  
3136 C CG  B LEU   A 127 ? 0.1506 0.2010 0.1907 0.0074  0.0071  0.0234  127 LEU   A CG  
3137 C CD1 A LEU   A 127 ? 0.1785 0.1543 0.1852 -0.0013 0.0140  -0.0022 127 LEU   A CD1 
3138 C CD1 B LEU   A 127 ? 0.1509 0.2044 0.2295 0.0207  0.0205  0.0212  127 LEU   A CD1 
3139 C CD2 A LEU   A 127 ? 0.1914 0.1570 0.2196 0.0238  0.0097  0.0190  127 LEU   A CD2 
3140 C CD2 B LEU   A 127 ? 0.1692 0.2161 0.2045 0.0031  0.0003  0.0080  127 LEU   A CD2 
3163 N N   A SER   A 128 ? 0.1488 0.1507 0.1567 -0.0067 0.0029  0.0232  128 SER   A N   
3164 N N   B SER   A 128 ? 0.1829 0.2196 0.1994 0.0028  -0.0058 0.0483  128 SER   A N   
3165 C CA  A SER   A 128 ? 0.1531 0.1657 0.1339 -0.0055 0.0083  0.0199  128 SER   A CA  
3166 C CA  B SER   A 128 ? 0.1938 0.2455 0.2064 0.0047  -0.0142 0.0290  128 SER   A CA  
3167 C C   A SER   A 128 ? 0.1497 0.1623 0.1224 -0.0020 -0.0024 0.0247  128 SER   A C   
3168 C C   B SER   A 128 ? 0.2205 0.2655 0.2405 0.0049  -0.0333 0.0272  128 SER   A C   
3169 O O   A SER   A 128 ? 0.1596 0.1796 0.1191 -0.0004 0.0130  0.0225  128 SER   A O   
3170 O O   B SER   A 128 ? 0.2225 0.2682 0.2546 0.0009  -0.0328 0.0184  128 SER   A O   
3171 C CB  A SER   A 128 ? 0.1585 0.1759 0.1392 -0.0087 0.0028  0.0208  128 SER   A CB  
3172 C CB  B SER   A 128 ? 0.1785 0.2432 0.1724 -0.0016 -0.0218 0.0265  128 SER   A CB  
3173 O OG  A SER   A 128 ? 0.1551 0.1837 0.1572 -0.0059 0.0184  0.0335  128 SER   A OG  
3174 O OG  B SER   A 128 ? 0.1591 0.2393 0.1658 -0.0054 -0.0207 0.0215  128 SER   A OG  
3185 N N   A ALA   A 129 ? 0.1376 0.1594 0.1332 -0.0001 0.0018  0.0364  129 ALA   A N   
3186 N N   B ALA   A 129 ? 0.2461 0.2959 0.2780 0.0175  -0.0399 0.0200  129 ALA   A N   
3187 C CA  A ALA   A 129 ? 0.1304 0.1579 0.1616 0.0013  0.0014  0.0341  129 ALA   A CA  
3188 C CA  B ALA   A 129 ? 0.2726 0.3220 0.3119 0.0270  -0.0373 0.0094  129 ALA   A CA  
3189 C C   A ALA   A 129 ? 0.1352 0.1544 0.1552 0.0063  0.0078  0.0084  129 ALA   A C   
3190 C C   B ALA   A 129 ? 0.2928 0.3346 0.3238 0.0321  -0.0322 0.0007  129 ALA   A C   
3191 O O   A ALA   A 129 ? 0.1448 0.1487 0.1778 -0.0027 0.0104  0.0197  129 ALA   A O   
3192 O O   B ALA   A 129 ? 0.3007 0.3411 0.3470 0.0287  -0.0292 -0.0139 129 ALA   A O   
3193 C CB  A ALA   A 129 ? 0.1253 0.1552 0.1808 0.0064  -0.0068 0.0450  129 ALA   A CB  
3194 C CB  B ALA   A 129 ? 0.2766 0.3278 0.3309 0.0286  -0.0369 0.0105  129 ALA   A CB  
3205 N N   A GLY   A 130 ? 0.1470 0.1539 0.1686 0.0004  0.0154  0.0134  130 GLY   A N   
3206 N N   B GLY   A 130 ? 0.3051 0.3390 0.3064 0.0383  -0.0252 0.0075  130 GLY   A N   
3207 C CA  A GLY   A 130 ? 0.1642 0.1504 0.1720 -0.0016 0.0061  0.0095  130 GLY   A CA  
3208 C CA  B GLY   A 130 ? 0.3176 0.3439 0.3101 0.0412  -0.0240 0.0102  130 GLY   A CA  
3209 C C   A GLY   A 130 ? 0.1827 0.1455 0.1644 -0.0028 -0.0088 0.0120  130 GLY   A C   
3210 C C   B GLY   A 130 ? 0.3251 0.3449 0.3037 0.0460  -0.0248 0.0187  130 GLY   A C   
3211 O O   A GLY   A 130 ? 0.1867 0.1477 0.1600 -0.0033 -0.0187 0.0226  130 GLY   A O   
3212 O O   B GLY   A 130 ? 0.3263 0.3499 0.2814 0.0549  -0.0298 0.0142  130 GLY   A O   
3219 N N   A ILE   A 131 ? 0.2025 0.1505 0.1809 -0.0171 -0.0202 0.0220  131 ILE   A N   
3220 N N   B ILE   A 131 ? 0.3356 0.3449 0.3313 0.0383  -0.0257 0.0229  131 ILE   A N   
3221 C CA  A ILE   A 131 ? 0.2157 0.1625 0.1643 -0.0331 -0.0330 0.0178  131 ILE   A CA  
3222 C CA  B ILE   A 131 ? 0.3512 0.3479 0.3643 0.0275  -0.0193 0.0273  131 ILE   A CA  
3223 C C   A ILE   A 131 ? 0.1960 0.1701 0.1653 -0.0317 -0.0314 0.0406  131 ILE   A C   
3224 C C   B ILE   A 131 ? 0.3534 0.3412 0.3473 0.0224  -0.0231 0.0331  131 ILE   A C   
3225 O O   A ILE   A 131 ? 0.1924 0.1740 0.1517 -0.0307 -0.0432 0.0462  131 ILE   A O   
3226 O O   B ILE   A 131 ? 0.3686 0.3462 0.3482 0.0240  -0.0196 0.0313  131 ILE   A O   
3227 C CB  A ILE   A 131 ? 0.2392 0.1783 0.1720 -0.0372 -0.0343 0.0119  131 ILE   A CB  
3228 C CB  B ILE   A 131 ? 0.3643 0.3572 0.4124 0.0219  -0.0116 0.0238  131 ILE   A CB  
3229 C CG1 A ILE   A 131 ? 0.2499 0.2053 0.1923 -0.0479 -0.0416 0.0030  131 ILE   A CG1 
3230 C CG1 B ILE   A 131 ? 0.3693 0.3642 0.4422 0.0167  -0.0036 0.0224  131 ILE   A CG1 
3231 C CG2 A ILE   A 131 ? 0.2493 0.1775 0.1912 -0.0322 -0.0186 0.0191  131 ILE   A CG2 
3232 C CG2 B ILE   A 131 ? 0.3671 0.3572 0.4203 0.0228  -0.0130 0.0264  131 ILE   A CG2 
3233 C CD1 A ILE   A 131 ? 0.2587 0.2157 0.2221 -0.0523 -0.0375 -0.0079 131 ILE   A CD1 
3234 C CD1 B ILE   A 131 ? 0.3740 0.3700 0.4662 0.0152  -0.0004 0.0199  131 ILE   A CD1 
3257 N N   A PHE   A 132 ? 0.1842 0.1627 0.1569 -0.0309 -0.0115 0.0463  132 PHE   A N   
3258 N N   B PHE   A 132 ? 0.3372 0.3278 0.3322 0.0184  -0.0423 0.0355  132 PHE   A N   
3259 C CA  A PHE   A 132 ? 0.1825 0.1763 0.1645 -0.0250 -0.0054 0.0098  132 PHE   A CA  
3260 C CA  B PHE   A 132 ? 0.3250 0.3187 0.3337 0.0084  -0.0570 0.0303  132 PHE   A CA  
3261 C C   A PHE   A 132 ? 0.1826 0.1894 0.1600 -0.0267 -0.0141 0.0175  132 PHE   A C   
3262 C C   B PHE   A 132 ? 0.3199 0.3171 0.3088 0.0019  -0.0656 0.0435  132 PHE   A C   
3263 O O   A PHE   A 132 ? 0.1868 0.1949 0.1391 -0.0300 -0.0093 -0.0034 132 PHE   A O   
3264 O O   B PHE   A 132 ? 0.3216 0.3119 0.2762 0.0010  -0.0621 0.0476  132 PHE   A O   
3265 C CB  A PHE   A 132 ? 0.1742 0.1592 0.1533 -0.0240 -0.0074 0.0247  132 PHE   A CB  
3266 C CB  B PHE   A 132 ? 0.3177 0.3161 0.3762 0.0143  -0.0740 0.0141  132 PHE   A CB  
3267 C CG  A PHE   A 132 ? 0.1730 0.1554 0.1559 -0.0122 -0.0293 0.0273  132 PHE   A CG  
3268 C CG  B PHE   A 132 ? 0.3160 0.3172 0.4274 0.0178  -0.0795 0.0039  132 PHE   A CG  
3269 C CD1 A PHE   A 132 ? 0.1692 0.1619 0.1597 -0.0033 -0.0436 0.0168  132 PHE   A CD1 
3270 C CD1 B PHE   A 132 ? 0.3194 0.3203 0.4549 0.0185  -0.0790 0.0019  132 PHE   A CD1 
3271 C CD2 A PHE   A 132 ? 0.1775 0.1638 0.1830 -0.0054 -0.0388 0.0344  132 PHE   A CD2 
3272 C CD2 B PHE   A 132 ? 0.3133 0.3176 0.4376 0.0191  -0.0840 -0.0008 132 PHE   A CD2 
3273 C CE1 A PHE   A 132 ? 0.1678 0.1689 0.1576 -0.0022 -0.0470 0.0253  132 PHE   A CE1 
3274 C CE1 B PHE   A 132 ? 0.3208 0.3207 0.4690 0.0169  -0.0777 -0.0051 132 PHE   A CE1 
3275 C CE2 A PHE   A 132 ? 0.1692 0.1608 0.1889 0.0064  -0.0424 0.0342  132 PHE   A CE2 
3276 C CE2 B PHE   A 132 ? 0.3159 0.3188 0.4590 0.0152  -0.0855 -0.0057 132 PHE   A CE2 
3277 C CZ  A PHE   A 132 ? 0.1658 0.1590 0.1634 -0.0084 -0.0470 0.0270  132 PHE   A CZ  
3278 C CZ  B PHE   A 132 ? 0.3162 0.3195 0.4683 0.0146  -0.0878 -0.0084 132 PHE   A CZ  
3297 N N   A GLY   A 133 ? 0.1817 0.1960 0.1635 -0.0285 -0.0302 0.0441  133 GLY   A N   
3298 N N   B GLY   A 133 ? 0.3154 0.3165 0.3172 -0.0046 -0.0696 0.0463  133 GLY   A N   
3299 C CA  A GLY   A 133 ? 0.1887 0.2071 0.1561 -0.0352 -0.0418 0.0316  133 GLY   A CA  
3300 C CA  B GLY   A 133 ? 0.3099 0.3197 0.3335 -0.0099 -0.0785 0.0425  133 GLY   A CA  
3301 C C   A GLY   A 133 ? 0.2009 0.2123 0.1646 -0.0377 -0.0555 0.0113  133 GLY   A C   
3302 C C   B GLY   A 133 ? 0.3067 0.3230 0.3429 -0.0133 -0.0772 0.0464  133 GLY   A C   
3303 O O   A GLY   A 133 ? 0.2086 0.2232 0.1667 -0.0296 -0.0586 -0.0072 133 GLY   A O   
3304 O O   B GLY   A 133 ? 0.3147 0.3363 0.3601 -0.0070 -0.0787 0.0457  133 GLY   A O   
3311 N N   A ALA   A 134 ? 0.2076 0.2104 0.1870 -0.0458 -0.0501 0.0055  134 ALA   A N   
3312 N N   B ALA   A 134 ? 0.2967 0.3130 0.3328 -0.0227 -0.0666 0.0499  134 ALA   A N   
3313 C CA  A ALA   A 134 ? 0.2031 0.2104 0.2196 -0.0429 -0.0508 0.0054  134 ALA   A CA  
3314 C CA  B ALA   A 134 ? 0.2911 0.3117 0.3342 -0.0286 -0.0608 0.0502  134 ALA   A CA  
3315 C C   A ALA   A 134 ? 0.2030 0.2113 0.2250 -0.0379 -0.0544 -0.0062 134 ALA   A C   
3316 C C   B ALA   A 134 ? 0.2855 0.3148 0.3268 -0.0307 -0.0636 0.0527  134 ALA   A C   
3317 O O   A ALA   A 134 ? 0.2109 0.2144 0.2475 -0.0300 -0.0315 -0.0124 134 ALA   A O   
3318 O O   B ALA   A 134 ? 0.2804 0.3175 0.3469 -0.0347 -0.0604 0.0547  134 ALA   A O   
3319 C CB  A ALA   A 134 ? 0.2015 0.2090 0.2542 -0.0471 -0.0508 0.0010  134 ALA   A CB  
3320 C CB  B ALA   A 134 ? 0.2929 0.3099 0.3545 -0.0274 -0.0550 0.0492  134 ALA   A CB  
3331 N N   A ASP   A 135 ? 0.1971 0.2111 0.2247 -0.0387 -0.0594 0.0185  135 ASP   A N   
3332 N N   B ASP   A 135 ? 0.2891 0.3135 0.3131 -0.0225 -0.0566 0.0665  135 ASP   A N   
3333 C CA  A ASP   A 135 ? 0.1894 0.2193 0.2326 -0.0448 -0.0636 0.0394  135 ASP   A CA  
3334 C CA  B ASP   A 135 ? 0.2920 0.3178 0.3227 -0.0145 -0.0487 0.0595  135 ASP   A CA  
3335 C C   A ASP   A 135 ? 0.1682 0.2016 0.2146 -0.0357 -0.0522 0.0559  135 ASP   A C   
3336 C C   B ASP   A 135 ? 0.2793 0.3106 0.2766 -0.0040 -0.0356 0.0716  135 ASP   A C   
3337 O O   A ASP   A 135 ? 0.1561 0.1839 0.2041 -0.0459 -0.0570 0.0583  135 ASP   A O   
3338 O O   B ASP   A 135 ? 0.2740 0.3079 0.2701 -0.0064 -0.0243 0.0630  135 ASP   A O   
3339 C CB  A ASP   A 135 ? 0.2039 0.2428 0.2591 -0.0575 -0.0787 0.0333  135 ASP   A CB  
3340 C CB  B ASP   A 135 ? 0.3084 0.3318 0.3886 -0.0160 -0.0498 0.0334  135 ASP   A CB  
3341 C CG  A ASP   A 135 ? 0.2183 0.2623 0.3036 -0.0636 -0.0756 0.0213  135 ASP   A CG  
3342 C CG  B ASP   A 135 ? 0.3240 0.3462 0.4512 -0.0131 -0.0474 0.0127  135 ASP   A CG  
3343 O OD1 A ASP   A 135 ? 0.2143 0.2647 0.3206 -0.0649 -0.0797 0.0414  135 ASP   A OD1 
3344 O OD1 B ASP   A 135 ? 0.3334 0.3545 0.4853 -0.0154 -0.0389 0.0043  135 ASP   A OD1 
3345 O OD2 A ASP   A 135 ? 0.2449 0.2797 0.3517 -0.0548 -0.0445 0.0056  135 ASP   A OD2 
3346 O OD2 B ASP   A 135 ? 0.3272 0.3494 0.4716 -0.0088 -0.0583 0.0144  135 ASP   A OD2 
3355 N N   A PRO   A 136 ? 0.1619 0.1991 0.2480 -0.0129 -0.0281 0.0658  136 PRO   A N   
3356 N N   B PRO   A 136 ? 0.2730 0.3042 0.2797 0.0083  -0.0235 0.0841  136 PRO   A N   
3357 C CA  A PRO   A 136 ? 0.1503 0.1927 0.2532 0.0004  -0.0163 0.0619  136 PRO   A CA  
3358 C CA  B PRO   A 136 ? 0.2664 0.3019 0.2741 0.0113  -0.0192 0.0857  136 PRO   A CA  
3359 C C   A PRO   A 136 ? 0.1318 0.1890 0.2364 -0.0043 -0.0117 0.0547  136 PRO   A C   
3360 C C   B PRO   A 136 ? 0.2562 0.3044 0.2781 0.0151  -0.0274 0.0779  136 PRO   A C   
3361 O O   A PRO   A 136 ? 0.1170 0.1861 0.2245 -0.0068 -0.0120 0.0521  136 PRO   A O   
3362 O O   B PRO   A 136 ? 0.2499 0.3023 0.2752 0.0194  -0.0329 0.0765  136 PRO   A O   
3363 C CB  A PRO   A 136 ? 0.1640 0.1942 0.2752 0.0075  -0.0001 0.0632  136 PRO   A CB  
3364 C CB  B PRO   A 136 ? 0.2719 0.2977 0.2791 0.0122  -0.0037 0.0907  136 PRO   A CB  
3365 C CG  A PRO   A 136 ? 0.1708 0.1980 0.2797 0.0045  -0.0018 0.0717  136 PRO   A CG  
3366 C CG  B PRO   A 136 ? 0.2762 0.2985 0.2912 0.0145  -0.0045 0.0863  136 PRO   A CG  
3367 C CD  A PRO   A 136 ? 0.1679 0.1996 0.2578 -0.0044 -0.0125 0.0759  136 PRO   A CD  
3368 C CD  B PRO   A 136 ? 0.2758 0.3027 0.2933 0.0101  -0.0117 0.0835  136 PRO   A CD  
3383 N N   A ILE   A 137 ? 0.1332 0.1909 0.2305 -0.0118 -0.0132 0.0539  137 ILE   A N   
3384 N N   B ILE   A 137 ? 0.2550 0.3080 0.2910 0.0156  -0.0310 0.0681  137 ILE   A N   
3385 C CA  A ILE   A 137 ? 0.1394 0.2062 0.2094 -0.0183 -0.0372 0.0554  137 ILE   A CA  
3386 C CA  B ILE   A 137 ? 0.2558 0.3181 0.3074 0.0115  -0.0386 0.0547  137 ILE   A CA  
3387 C C   A ILE   A 137 ? 0.1378 0.2070 0.1785 -0.0187 -0.0373 0.0558  137 ILE   A C   
3388 C C   B ILE   A 137 ? 0.2460 0.3034 0.2835 0.0004  -0.0272 0.0561  137 ILE   A C   
3389 O O   A ILE   A 137 ? 0.1350 0.1878 0.1539 -0.0277 -0.0243 0.0544  137 ILE   A O   
3390 O O   B ILE   A 137 ? 0.2459 0.2992 0.2964 -0.0033 -0.0215 0.0489  137 ILE   A O   
3391 C CB  A ILE   A 137 ? 0.1435 0.2274 0.2422 -0.0211 -0.0538 0.0487  137 ILE   A CB  
3392 C CB  B ILE   A 137 ? 0.2700 0.3407 0.3446 0.0150  -0.0494 0.0458  137 ILE   A CB  
3393 C CG1 A ILE   A 137 ? 0.1558 0.2526 0.2729 -0.0113 -0.0292 0.0451  137 ILE   A CG1 
3394 C CG1 B ILE   A 137 ? 0.2826 0.3569 0.3788 0.0234  -0.0527 0.0375  137 ILE   A CG1 
3395 C CG2 A ILE   A 137 ? 0.1439 0.2281 0.2343 -0.0321 -0.0752 0.0473  137 ILE   A CG2 
3396 C CG2 B ILE   A 137 ? 0.2752 0.3443 0.3468 0.0123  -0.0469 0.0391  137 ILE   A CG2 
3397 C CD1 A ILE   A 137 ? 0.1643 0.2636 0.2918 -0.0040 -0.0141 0.0355  137 ILE   A CD1 
3398 C CD1 B ILE   A 137 ? 0.2952 0.3657 0.4091 0.0259  -0.0451 0.0312  137 ILE   A CD1 
3421 N N   A HIS   A 138 ? 0.1416 0.2222 0.1935 -0.0011 -0.0324 0.0627  138 HIS   A N   
3422 N N   B HIS   A 138 ? 0.2347 0.2947 0.2605 -0.0097 -0.0147 0.0462  138 HIS   A N   
3423 C CA  A HIS   A 138 ? 0.1461 0.2365 0.1887 -0.0066 -0.0212 0.0650  138 HIS   A CA  
3424 C CA  B HIS   A 138 ? 0.2215 0.2858 0.2457 -0.0173 -0.0150 0.0409  138 HIS   A CA  
3425 C C   A HIS   A 138 ? 0.1362 0.2244 0.1780 -0.0017 -0.0241 0.0591  138 HIS   A C   
3426 C C   B HIS   A 138 ? 0.2084 0.2619 0.2231 -0.0133 -0.0204 0.0399  138 HIS   A C   
3427 O O   A HIS   A 138 ? 0.1352 0.2245 0.1800 -0.0020 -0.0219 0.0617  138 HIS   A O   
3428 O O   B HIS   A 138 ? 0.2183 0.2624 0.2324 -0.0162 -0.0151 0.0351  138 HIS   A O   
3429 C CB  A HIS   A 138 ? 0.1711 0.2551 0.1832 -0.0061 -0.0242 0.0656  138 HIS   A CB  
3430 C CB  B HIS   A 138 ? 0.2278 0.3001 0.2416 -0.0224 -0.0262 0.0280  138 HIS   A CB  
3431 C CG  A HIS   A 138 ? 0.1914 0.2634 0.1951 -0.0081 -0.0198 0.0546  138 HIS   A CG  
3432 C CG  B HIS   A 138 ? 0.2306 0.3103 0.2467 -0.0345 -0.0264 0.0060  138 HIS   A CG  
3433 N ND1 A HIS   A 138 ? 0.2062 0.2712 0.2210 -0.0113 -0.0123 0.0390  138 HIS   A ND1 
3434 N ND1 B HIS   A 138 ? 0.2391 0.3181 0.2676 -0.0377 -0.0212 -0.0111 138 HIS   A ND1 
3435 C CD2 A HIS   A 138 ? 0.1970 0.2676 0.1979 -0.0064 -0.0214 0.0518  138 HIS   A CD2 
3436 C CD2 B HIS   A 138 ? 0.2309 0.3171 0.2515 -0.0344 -0.0335 0.0009  138 HIS   A CD2 
3437 C CE1 A HIS   A 138 ? 0.2119 0.2747 0.2300 -0.0084 -0.0137 0.0278  138 HIS   A CE1 
3438 C CE1 B HIS   A 138 ? 0.2402 0.3188 0.2700 -0.0361 -0.0218 -0.0178 138 HIS   A CE1 
3439 N NE2 A HIS   A 138 ? 0.2030 0.2731 0.2021 -0.0060 -0.0136 0.0383  138 HIS   A NE2 
3440 N NE2 B HIS   A 138 ? 0.2330 0.3208 0.2518 -0.0343 -0.0304 -0.0125 138 HIS   A NE2 
3455 N N   A SER   A 139 ? 0.1344 0.2094 0.1885 0.0060  -0.0068 0.0569  139 SER   A N   
3456 N N   B SER   A 139 ? 0.1916 0.2454 0.2070 -0.0093 -0.0144 0.0443  139 SER   A N   
3457 C CA  A SER   A 139 ? 0.1351 0.1952 0.1950 -0.0030 0.0029  0.0582  139 SER   A CA  
3458 C CA  B SER   A 139 ? 0.1806 0.2374 0.2064 -0.0038 -0.0120 0.0448  139 SER   A CA  
3459 C C   A SER   A 139 ? 0.1265 0.1827 0.1905 -0.0024 0.0137  0.0469  139 SER   A C   
3460 C C   B SER   A 139 ? 0.1739 0.2243 0.2154 -0.0049 -0.0201 0.0489  139 SER   A C   
3461 O O   A SER   A 139 ? 0.1096 0.1695 0.1844 -0.0039 0.0153  0.0389  139 SER   A O   
3462 O O   B SER   A 139 ? 0.1726 0.2125 0.2238 -0.0068 -0.0281 0.0534  139 SER   A O   
3463 C CB  A SER   A 139 ? 0.1300 0.1885 0.2113 -0.0105 0.0046  0.0662  139 SER   A CB  
3464 C CB  B SER   A 139 ? 0.1670 0.2373 0.2059 0.0034  0.0117  0.0448  139 SER   A CB  
3465 O OG  A SER   A 139 ? 0.1288 0.1812 0.2181 -0.0126 -0.0087 0.0804  139 SER   A OG  
3466 O OG  B SER   A 139 ? 0.1600 0.2384 0.2162 0.0147  0.0097  0.0443  139 SER   A OG  
3477 N N   A LEU   A 140 ? 0.1322 0.1877 0.1850 -0.0059 0.0139  0.0454  140 LEU   A N   
3478 N N   B LEU   A 140 ? 0.1651 0.2274 0.1978 -0.0061 -0.0314 0.0508  140 LEU   A N   
3479 C CA  A LEU   A 140 ? 0.1277 0.1794 0.1789 -0.0136 0.0080  0.0432  140 LEU   A CA  
3480 C CA  B LEU   A 140 ? 0.1563 0.2171 0.2020 -0.0147 -0.0285 0.0383  140 LEU   A CA  
3481 C C   A LEU   A 140 ? 0.1235 0.1818 0.1713 -0.0178 0.0089  0.0419  140 LEU   A C   
3482 C C   B LEU   A 140 ? 0.1599 0.2228 0.2276 -0.0173 -0.0182 0.0267  140 LEU   A C   
3483 O O   A LEU   A 140 ? 0.1282 0.1812 0.1867 -0.0203 -0.0064 0.0438  140 LEU   A O   
3484 O O   B LEU   A 140 ? 0.1660 0.2224 0.2505 -0.0154 -0.0082 0.0351  140 LEU   A O   
3485 C CB  A LEU   A 140 ? 0.1345 0.1892 0.1822 -0.0135 0.0031  0.0433  140 LEU   A CB  
3486 C CB  B LEU   A 140 ? 0.1576 0.2199 0.2061 -0.0142 -0.0248 0.0391  140 LEU   A CB  
3487 C CG  A LEU   A 140 ? 0.1365 0.1972 0.1865 -0.0163 0.0124  0.0527  140 LEU   A CG  
3488 C CG  B LEU   A 140 ? 0.1561 0.2189 0.2165 -0.0187 -0.0072 0.0562  140 LEU   A CG  
3489 C CD1 A LEU   A 140 ? 0.1373 0.1881 0.1898 -0.0105 0.0091  0.0637  140 LEU   A CD1 
3490 C CD1 B LEU   A 140 ? 0.1610 0.2099 0.2102 -0.0128 0.0039  0.0630  140 LEU   A CD1 
3491 C CD2 A LEU   A 140 ? 0.1502 0.2094 0.1861 -0.0067 0.0125  0.0546  140 LEU   A CD2 
3492 C CD2 B LEU   A 140 ? 0.1646 0.2291 0.2344 -0.0109 -0.0153 0.0563  140 LEU   A CD2 
3515 N N   A ARG   A 141 ? 0.1253 0.1813 0.1737 -0.0159 0.0052  0.0347  141 ARG   A N   
3516 N N   B ARG   A 141 ? 0.1718 0.2255 0.2456 -0.0204 -0.0235 0.0112  141 ARG   A N   
3517 C CA  A ARG   A 141 ? 0.1381 0.1944 0.1817 -0.0207 -0.0060 0.0148  141 ARG   A CA  
3518 C CA  B ARG   A 141 ? 0.1992 0.2387 0.2640 -0.0242 -0.0282 -0.0103 141 ARG   A CA  
3519 C C   A ARG   A 141 ? 0.1381 0.1884 0.1757 -0.0181 -0.0100 0.0179  141 ARG   A C   
3520 C C   B ARG   A 141 ? 0.1870 0.2212 0.2472 -0.0226 -0.0162 -0.0020 141 ARG   A C   
3521 O O   A ARG   A 141 ? 0.1352 0.1778 0.1745 -0.0285 0.0002  0.0102  141 ARG   A O   
3522 O O   B ARG   A 141 ? 0.1833 0.2048 0.2424 -0.0364 0.0042  -0.0128 141 ARG   A O   
3523 C CB  A ARG   A 141 ? 0.1549 0.2083 0.1901 -0.0256 -0.0116 -0.0078 141 ARG   A CB  
3524 C CB  B ARG   A 141 ? 0.2375 0.2652 0.3103 -0.0321 -0.0360 -0.0303 141 ARG   A CB  
3525 C CG  A ARG   A 141 ? 0.1767 0.2303 0.2197 -0.0264 -0.0063 -0.0132 141 ARG   A CG  
3526 C CG  B ARG   A 141 ? 0.2781 0.2942 0.3673 -0.0356 -0.0383 -0.0403 141 ARG   A CG  
3527 C CD  A ARG   A 141 ? 0.1967 0.2536 0.2554 -0.0351 -0.0045 -0.0169 141 ARG   A CD  
3528 C CD  B ARG   A 141 ? 0.3096 0.3187 0.4156 -0.0459 -0.0382 -0.0455 141 ARG   A CD  
3529 N NE  A ARG   A 141 ? 0.1947 0.2697 0.2647 -0.0422 -0.0046 -0.0206 141 ARG   A NE  
3530 N NE  B ARG   A 141 ? 0.3370 0.3366 0.4512 -0.0524 -0.0362 -0.0540 141 ARG   A NE  
3531 C CZ  A ARG   A 141 ? 0.1945 0.2842 0.2639 -0.0525 -0.0065 -0.0230 141 ARG   A CZ  
3532 C CZ  B ARG   A 141 ? 0.3607 0.3509 0.4815 -0.0522 -0.0270 -0.0651 141 ARG   A CZ  
3533 N NH1 A ARG   A 141 ? 0.1864 0.2885 0.2757 -0.0560 -0.0092 -0.0350 141 ARG   A NH1 
3534 N NH1 B ARG   A 141 ? 0.3692 0.3564 0.4896 -0.0557 -0.0216 -0.0682 141 ARG   A NH1 
3535 N NH2 A ARG   A 141 ? 0.1965 0.2894 0.2591 -0.0569 -0.0163 -0.0189 141 ARG   A NH2 
3536 N NH2 B ARG   A 141 ? 0.3692 0.3575 0.4937 -0.0483 -0.0218 -0.0685 141 ARG   A NH2 
3563 N N   A VAL   A 142 ? 0.1391 0.1842 0.1751 -0.0114 -0.0118 0.0185  142 VAL   A N   
3564 N N   B VAL   A 142 ? 0.1748 0.2087 0.2372 -0.0115 -0.0181 0.0057  142 VAL   A N   
3565 C CA  A VAL   A 142 ? 0.1422 0.1805 0.1954 -0.0164 0.0103  0.0138  142 VAL   A CA  
3566 C CA  B VAL   A 142 ? 0.1659 0.1968 0.2334 -0.0108 0.0044  0.0128  142 VAL   A CA  
3567 C C   A VAL   A 142 ? 0.1372 0.1751 0.2042 -0.0214 0.0056  0.0153  142 VAL   A C   
3568 C C   B VAL   A 142 ? 0.1472 0.1851 0.2197 -0.0167 -0.0016 0.0150  142 VAL   A C   
3569 O O   A VAL   A 142 ? 0.1412 0.1721 0.2097 -0.0184 0.0154  0.0170  142 VAL   A O   
3570 O O   B VAL   A 142 ? 0.1514 0.1849 0.2208 -0.0086 0.0026  0.0180  142 VAL   A O   
3571 C CB  A VAL   A 142 ? 0.1416 0.1794 0.1934 -0.0140 0.0070  0.0067  142 VAL   A CB  
3572 C CB  B VAL   A 142 ? 0.1698 0.1987 0.2267 -0.0019 0.0088  0.0278  142 VAL   A CB  
3573 C CG1 A VAL   A 142 ? 0.1405 0.1713 0.2022 -0.0178 0.0091  0.0082  142 VAL   A CG1 
3574 C CG1 B VAL   A 142 ? 0.1618 0.1905 0.2266 -0.0077 0.0194  0.0337  142 VAL   A CG1 
3575 C CG2 A VAL   A 142 ? 0.1420 0.1847 0.2083 -0.0151 0.0108  -0.0067 142 VAL   A CG2 
3576 C CG2 B VAL   A 142 ? 0.1769 0.2038 0.2391 0.0046  0.0010  0.0261  142 VAL   A CG2 
3595 N N   . CYS   A 143 ? 0.1445 0.1760 0.1961 -0.0163 -0.0053 0.0191  143 CYS   A N   
3596 C CA  . CYS   A 143 ? 0.1484 0.1703 0.2074 -0.0154 0.0015  0.0213  143 CYS   A CA  
3597 C C   . CYS   A 143 ? 0.1437 0.1578 0.2111 -0.0220 -0.0043 0.0207  143 CYS   A C   
3598 O O   . CYS   A 143 ? 0.1438 0.1541 0.2148 -0.0142 -0.0012 0.0292  143 CYS   A O   
3599 C CB  . CYS   A 143 ? 0.1504 0.1704 0.2028 -0.0081 0.0160  0.0392  143 CYS   A CB  
3600 S SG  . CYS   A 143 ? 0.1681 0.1716 0.2030 0.0030  0.0084  0.0226  143 CYS   A SG  
3607 N N   . VAL   A 144 ? 0.1406 0.1699 0.2301 -0.0212 0.0005  0.0325  144 VAL   A N   
3608 C CA  . VAL   A 144 ? 0.1493 0.1843 0.2603 -0.0194 0.0260  0.0461  144 VAL   A CA  
3609 C C   . VAL   A 144 ? 0.1610 0.1710 0.2767 -0.0271 -0.0032 0.0314  144 VAL   A C   
3610 O O   . VAL   A 144 ? 0.1812 0.1663 0.2853 -0.0141 0.0036  0.0421  144 VAL   A O   
3611 C CB  . VAL   A 144 ? 0.1677 0.2083 0.2980 -0.0132 0.0269  0.0402  144 VAL   A CB  
3612 C CG1 . VAL   A 144 ? 0.1792 0.2188 0.3239 -0.0238 0.0195  0.0386  144 VAL   A CG1 
3613 C CG2 . VAL   A 144 ? 0.1646 0.2089 0.3067 -0.0101 0.0211  0.0452  144 VAL   A CG2 
3623 N N   . ASP   A 145 ? 0.1721 0.1641 0.2904 -0.0275 -0.0058 0.0224  145 ASP   A N   
3624 C CA  . ASP   A 145 ? 0.1812 0.1715 0.2913 -0.0303 0.0044  0.0051  145 ASP   A CA  
3625 C C   . ASP   A 145 ? 0.1766 0.1576 0.2934 -0.0186 0.0070  -0.0023 145 ASP   A C   
3626 O O   . ASP   A 145 ? 0.1908 0.1666 0.3528 -0.0254 -0.0021 -0.0350 145 ASP   A O   
3627 C CB  . ASP   A 145 ? 0.1990 0.2106 0.3183 -0.0427 -0.0162 -0.0052 145 ASP   A CB  
3628 C CG  . ASP   A 145 ? 0.2225 0.2563 0.3451 -0.0634 -0.0313 0.0010  145 ASP   A CG  
3629 O OD1 . ASP   A 145 ? 0.2273 0.2707 0.3713 -0.0814 -0.0168 -0.0001 145 ASP   A OD1 
3630 O OD2 . ASP   A 145 ? 0.2466 0.2778 0.3719 -0.0780 -0.0522 0.0055  145 ASP   A OD2 
3635 N N   . THR   A 146 ? 0.1613 0.1433 0.2336 -0.0198 0.0109  0.0103  146 THR   A N   
3636 C CA  . THR   A 146 ? 0.1446 0.1481 0.2312 -0.0134 0.0070  0.0157  146 THR   A CA  
3637 C C   . THR   A 146 ? 0.1398 0.1364 0.2321 -0.0078 0.0094  0.0160  146 THR   A C   
3638 O O   . THR   A 146 ? 0.1549 0.1519 0.2380 -0.0005 0.0010  0.0132  146 THR   A O   
3639 C CB  . THR   A 146 ? 0.1448 0.1526 0.2233 -0.0076 0.0169  0.0111  146 THR   A CB  
3640 O OG1 . THR   A 146 ? 0.1541 0.1711 0.2297 -0.0117 0.0100  0.0036  146 THR   A OG1 
3641 C CG2 . THR   A 146 ? 0.1434 0.1497 0.2467 -0.0159 0.0142  0.0177  146 THR   A CG2 
3649 N N   . VAL   A 147 ? 0.1403 0.1420 0.2206 -0.0061 0.0218  0.0243  147 VAL   A N   
3650 C CA  . VAL   A 147 ? 0.1340 0.1438 0.2178 -0.0106 0.0234  0.0272  147 VAL   A CA  
3651 C C   . VAL   A 147 ? 0.1409 0.1406 0.2271 -0.0154 0.0171  0.0216  147 VAL   A C   
3652 O O   . VAL   A 147 ? 0.1481 0.1496 0.2372 -0.0161 0.0192  0.0278  147 VAL   A O   
3653 C CB  . VAL   A 147 ? 0.1474 0.1521 0.2119 -0.0156 0.0132  0.0326  147 VAL   A CB  
3654 C CG1 . VAL   A 147 ? 0.1760 0.1574 0.2114 -0.0084 0.0058  0.0406  147 VAL   A CG1 
3655 C CG2 . VAL   A 147 ? 0.1503 0.1448 0.2090 -0.0081 0.0158  0.0291  147 VAL   A CG2 
3665 N N   . ARG   A 148 ? 0.1362 0.1458 0.2320 -0.0241 0.0264  0.0428  148 ARG   A N   
3666 C CA  . ARG   A 148 ? 0.1576 0.1429 0.2310 -0.0187 0.0186  0.0538  148 ARG   A CA  
3667 C C   . ARG   A 148 ? 0.1691 0.1395 0.2363 -0.0121 0.0159  0.0643  148 ARG   A C   
3668 O O   . ARG   A 148 ? 0.1877 0.1518 0.2501 -0.0156 0.0298  0.0584  148 ARG   A O   
3669 C CB  . ARG   A 148 ? 0.1657 0.1470 0.2461 -0.0130 0.0416  0.0460  148 ARG   A CB  
3670 C CG  . ARG   A 148 ? 0.1753 0.1544 0.2860 -0.0112 0.0600  0.0303  148 ARG   A CG  
3671 C CD  . ARG   A 148 ? 0.1961 0.1541 0.3113 -0.0071 0.0646  0.0478  148 ARG   A CD  
3672 N NE  . ARG   A 148 ? 0.1853 0.1494 0.3089 0.0136  0.0557  0.0605  148 ARG   A NE  
3673 C CZ  . ARG   A 148 ? 0.1730 0.1465 0.2804 0.0112  0.0451  0.0437  148 ARG   A CZ  
3674 N NH1 . ARG   A 148 ? 0.1733 0.1497 0.2730 -0.0079 0.0431  0.0169  148 ARG   A NH1 
3675 N NH2 . ARG   A 148 ? 0.1631 0.1656 0.2904 0.0148  0.0511  0.0476  148 ARG   A NH2 
3689 N N   . THR   A 149 ? 0.1639 0.1503 0.2121 -0.0110 0.0111  0.0595  149 THR   A N   
3690 C CA  . THR   A 149 ? 0.1597 0.1564 0.2176 -0.0105 0.0142  0.0531  149 THR   A CA  
3691 C C   . THR   A 149 ? 0.1512 0.1597 0.2093 -0.0184 0.0091  0.0557  149 THR   A C   
3692 O O   . THR   A 149 ? 0.1513 0.1693 0.2300 -0.0145 0.0092  0.0615  149 THR   A O   
3693 C CB  . THR   A 149 ? 0.1541 0.1725 0.2230 -0.0160 0.0132  0.0476  149 THR   A CB  
3694 O OG1 . THR   A 149 ? 0.1589 0.1600 0.2347 -0.0197 0.0199  0.0452  149 THR   A OG1 
3695 C CG2 . THR   A 149 ? 0.1591 0.1942 0.2183 -0.0114 0.0028  0.0317  149 THR   A CG2 
3703 N N   . ASN   A 150 ? 0.1543 0.1677 0.2136 -0.0147 0.0008  0.0700  150 ASN   A N   
3704 C CA  . ASN   A 150 ? 0.1663 0.1746 0.2206 -0.0121 0.0119  0.0585  150 ASN   A CA  
3705 C C   . ASN   A 150 ? 0.1427 0.1594 0.2174 -0.0182 0.0154  0.0556  150 ASN   A C   
3706 O O   . ASN   A 150 ? 0.1587 0.1688 0.2356 -0.0137 -0.0048 0.0606  150 ASN   A O   
3707 C CB  . ASN   A 150 ? 0.2146 0.2007 0.2426 -0.0169 0.0265  0.0769  150 ASN   A CB  
3708 C CG  . ASN   A 150 ? 0.2740 0.2346 0.2981 -0.0145 0.0229  0.0778  150 ASN   A CG  
3709 O OD1 . ASN   A 150 ? 0.2939 0.2448 0.3125 -0.0185 0.0308  0.0985  150 ASN   A OD1 
3710 N ND2 . ASN   A 150 ? 0.3131 0.2555 0.3388 -0.0085 0.0099  0.0748  150 ASN   A ND2 
3717 N N   . VAL   A 151 ? 0.1472 0.1504 0.2102 -0.0152 0.0060  0.0447  151 VAL   A N   
3718 C CA  . VAL   A 151 ? 0.1541 0.1556 0.2011 -0.0135 0.0099  0.0573  151 VAL   A CA  
3719 C C   . VAL   A 151 ? 0.1507 0.1535 0.2094 -0.0288 0.0093  0.0507  151 VAL   A C   
3720 O O   . VAL   A 151 ? 0.1615 0.1609 0.2442 -0.0245 0.0170  0.0395  151 VAL   A O   
3721 C CB  . VAL   A 151 ? 0.1772 0.1743 0.2101 -0.0084 0.0234  0.0560  151 VAL   A CB  
3722 C CG1 . VAL   A 151 ? 0.1801 0.1985 0.2482 -0.0161 0.0173  0.0455  151 VAL   A CG1 
3723 C CG2 . VAL   A 151 ? 0.1921 0.1727 0.2127 -0.0069 0.0305  0.0502  151 VAL   A CG2 
3733 N N   A TYR   A 152 ? 0.1437 0.1570 0.2025 -0.0234 -0.0006 0.0514  152 TYR   A N   
3734 N N   B TYR   A 152 ? 0.1330 0.1508 0.2161 -0.0246 0.0062  0.0480  152 TYR   A N   
3735 C CA  A TYR   A 152 ? 0.1479 0.1616 0.1762 -0.0221 -0.0022 0.0531  152 TYR   A CA  
3736 C CA  B TYR   A 152 ? 0.1385 0.1545 0.2001 -0.0220 0.0135  0.0471  152 TYR   A CA  
3737 C C   A TYR   A 152 ? 0.1503 0.1578 0.1527 -0.0150 0.0040  0.0545  152 TYR   A C   
3738 C C   B TYR   A 152 ? 0.1399 0.1424 0.1862 -0.0192 0.0314  0.0440  152 TYR   A C   
3739 O O   A TYR   A 152 ? 0.1610 0.1546 0.1472 -0.0109 0.0084  0.0392  152 TYR   A O   
3740 O O   B TYR   A 152 ? 0.1358 0.1273 0.1903 -0.0155 0.0508  0.0278  152 TYR   A O   
3741 C CB  A TYR   A 152 ? 0.1569 0.1714 0.1874 -0.0210 0.0126  0.0585  152 TYR   A CB  
3742 C CB  B TYR   A 152 ? 0.1534 0.1719 0.2071 -0.0121 0.0288  0.0559  152 TYR   A CB  
3743 C CG  A TYR   A 152 ? 0.1692 0.1858 0.1891 -0.0228 0.0272  0.0579  152 TYR   A CG  
3744 C CG  B TYR   A 152 ? 0.1687 0.1944 0.1928 0.0036  0.0299  0.0622  152 TYR   A CG  
3745 C CD1 A TYR   A 152 ? 0.1858 0.2030 0.2104 -0.0154 0.0329  0.0635  152 TYR   A CD1 
3746 C CD1 B TYR   A 152 ? 0.1864 0.2179 0.2238 0.0139  0.0272  0.0683  152 TYR   A CD1 
3747 C CD2 A TYR   A 152 ? 0.1740 0.1844 0.1794 -0.0326 0.0282  0.0518  152 TYR   A CD2 
3748 C CD2 B TYR   A 152 ? 0.1782 0.1999 0.1772 0.0051  0.0271  0.0600  152 TYR   A CD2 
3749 C CE1 A TYR   A 152 ? 0.2076 0.2072 0.2254 -0.0121 0.0345  0.0681  152 TYR   A CE1 
3750 C CE1 B TYR   A 152 ? 0.2128 0.2312 0.2482 0.0201  0.0230  0.0780  152 TYR   A CE1 
3751 C CE2 A TYR   A 152 ? 0.1953 0.1937 0.1902 -0.0307 0.0384  0.0531  152 TYR   A CE2 
3752 C CE2 B TYR   A 152 ? 0.2101 0.2188 0.2094 0.0071  0.0270  0.0714  152 TYR   A CE2 
3753 C CZ  A TYR   A 152 ? 0.2185 0.1997 0.2080 -0.0188 0.0379  0.0728  152 TYR   A CZ  
3754 C CZ  B TYR   A 152 ? 0.2332 0.2312 0.2335 0.0165  0.0286  0.0947  152 TYR   A CZ  
3755 O OH  A TYR   A 152 ? 0.2389 0.2063 0.2330 -0.0072 0.0374  0.0822  152 TYR   A OH  
3756 O OH  B TYR   A 152 ? 0.2669 0.2571 0.2646 0.0238  0.0369  0.1087  152 TYR   A OH  
3775 N N   A LEU   A 153 ? 0.1450 0.1612 0.1546 -0.0113 0.0069  0.0539  153 LEU   A N   
3776 N N   B LEU   A 153 ? 0.1484 0.1514 0.1954 -0.0169 0.0234  0.0397  153 LEU   A N   
3777 C CA  A LEU   A 153 ? 0.1325 0.1596 0.1610 -0.0032 0.0152  0.0503  153 LEU   A CA  
3778 C CA  B LEU   A 153 ? 0.1378 0.1555 0.1949 -0.0140 0.0250  0.0430  153 LEU   A CA  
3779 C C   A LEU   A 153 ? 0.1384 0.1656 0.1636 0.0030  0.0233  0.0496  153 LEU   A C   
3780 C C   B LEU   A 153 ? 0.1417 0.1653 0.1868 -0.0048 0.0274  0.0464  153 LEU   A C   
3781 O O   A LEU   A 153 ? 0.1440 0.1720 0.1591 0.0073  0.0340  0.0468  153 LEU   A O   
3782 O O   B LEU   A 153 ? 0.1426 0.1713 0.1933 -0.0037 0.0343  0.0512  153 LEU   A O   
3783 C CB  A LEU   A 153 ? 0.1279 0.1584 0.1710 0.0028  0.0143  0.0411  153 LEU   A CB  
3784 C CB  B LEU   A 153 ? 0.1351 0.1572 0.2061 -0.0163 0.0133  0.0329  153 LEU   A CB  
3785 C CG  A LEU   A 153 ? 0.1304 0.1504 0.1694 0.0029  0.0136  0.0361  153 LEU   A CG  
3786 C CG  B LEU   A 153 ? 0.1448 0.1576 0.2143 -0.0218 0.0088  0.0297  153 LEU   A CG  
3787 C CD1 A LEU   A 153 ? 0.1330 0.1489 0.1580 0.0004  0.0088  0.0338  153 LEU   A CD1 
3788 C CD1 B LEU   A 153 ? 0.1541 0.1632 0.2138 -0.0259 0.0159  0.0275  153 LEU   A CD1 
3789 C CD2 A LEU   A 153 ? 0.1267 0.1552 0.1521 0.0070  0.0120  0.0308  153 LEU   A CD2 
3790 C CD2 B LEU   A 153 ? 0.1430 0.1657 0.2142 -0.0248 -0.0007 0.0379  153 LEU   A CD2 
3813 N N   . ALA   A 154 ? 0.1423 0.1554 0.1909 -0.0018 0.0280  0.0476  154 ALA   A N   
3814 C CA  . ALA   A 154 ? 0.1537 0.1573 0.2090 0.0026  0.0246  0.0435  154 ALA   A CA  
3815 C C   . ALA   A 154 ? 0.1554 0.1606 0.2014 0.0039  0.0271  0.0581  154 ALA   A C   
3816 O O   . ALA   A 154 ? 0.1684 0.1747 0.2058 0.0025  0.0360  0.0560  154 ALA   A O   
3817 C CB  . ALA   A 154 ? 0.1579 0.1582 0.2045 0.0155  0.0285  0.0359  154 ALA   A CB  
3824 N N   A VAL   A 155 ? 0.1520 0.1617 0.1853 0.0186  0.0160  0.0495  155 VAL   A N   
3825 N N   B VAL   A 155 ? 0.1458 0.1612 0.1977 0.0219  0.0278  0.0768  155 VAL   A N   
3826 C CA  A VAL   A 155 ? 0.1553 0.1684 0.1840 0.0233  -0.0046 0.0395  155 VAL   A CA  
3827 C CA  B VAL   A 155 ? 0.1538 0.1672 0.2298 0.0092  0.0191  0.0841  155 VAL   A CA  
3828 C CA  T VAL   A 155 ? 0.2077 0.2008 0.2241 0.0180  0.0047  0.0302  155 VAL   A CA  
3829 C C   A VAL   A 155 ? 0.1587 0.1717 0.1819 0.0293  -0.0102 0.0360  155 VAL   A C   
3830 C C   B VAL   A 155 ? 0.1592 0.1701 0.2501 0.0040  0.0261  0.0807  155 VAL   A C   
3831 C C   T VAL   A 155 ? 0.2048 0.1944 0.2127 0.0265  0.0121  0.0296  155 VAL   A C   
3832 O O   A VAL   A 155 ? 0.1627 0.1743 0.1727 0.0260  -0.0111 0.0269  155 VAL   A O   
3833 O O   B VAL   A 155 ? 0.1497 0.1752 0.2376 0.0061  0.0436  0.0779  155 VAL   A O   
3834 O O   T VAL   A 155 ? 0.2038 0.1969 0.2058 0.0259  0.0122  0.0291  155 VAL   A O   
3835 C CB  A VAL   A 155 ? 0.1503 0.1680 0.1906 0.0263  -0.0146 0.0391  155 VAL   A CB  
3836 C CB  B VAL   A 155 ? 0.1560 0.1652 0.2443 0.0065  0.0031  0.0731  155 VAL   A CB  
3837 C CB  T VAL   A 155 ? 0.2089 0.2018 0.2345 0.0116  0.0007  0.0312  155 VAL   A CB  
3838 C CG1 A VAL   A 155 ? 0.1632 0.1667 0.1874 0.0286  -0.0207 0.0467  155 VAL   A CG1 
3839 C CG1 B VAL   A 155 ? 0.1745 0.1690 0.2688 0.0041  -0.0052 0.0682  155 VAL   A CG1 
3840 C CG1 T VAL   A 155 ? 0.2091 0.2051 0.2398 0.0130  -0.0036 0.0338  155 VAL   A CG1 
3841 C CG2 A VAL   A 155 ? 0.1437 0.1729 0.1963 0.0276  -0.0249 0.0313  155 VAL   A CG2 
3842 C CG2 B VAL   A 155 ? 0.1717 0.1794 0.2630 0.0150  -0.0084 0.0512  155 VAL   A CG2 
3843 C CG2 T VAL   A 155 ? 0.2087 0.2033 0.2398 0.0099  -0.0010 0.0270  155 VAL   A CG2 
3869 N N   A PHE   A 156 ? 0.1590 0.1739 0.1857 0.0300  0.0034  0.0449  156 PHE   A N   
3870 N N   B PHE   A 156 ? 0.1666 0.1626 0.2821 -0.0097 0.0347  0.0879  156 PHE   A N   
3871 N N   T PHE   A 156 ? 0.1983 0.1869 0.2140 0.0309  0.0227  0.0356  156 PHE   A N   
3872 C CA  A PHE   A 156 ? 0.1694 0.1734 0.1987 0.0411  0.0087  0.0550  156 PHE   A CA  
3873 C CA  B PHE   A 156 ? 0.1866 0.1805 0.2858 -0.0128 0.0087  0.0989  156 PHE   A CA  
3874 C CA  T PHE   A 156 ? 0.1968 0.1791 0.2068 0.0377  0.0276  0.0452  156 PHE   A CA  
3875 C C   A PHE   A 156 ? 0.1621 0.1716 0.1909 0.0466  0.0295  0.0679  156 PHE   A C   
3876 C C   B PHE   A 156 ? 0.1926 0.1978 0.3000 -0.0155 0.0129  0.1081  156 PHE   A C   
3877 C C   T PHE   A 156 ? 0.1846 0.1784 0.1942 0.0428  0.0428  0.0383  156 PHE   A C   
3878 O O   A PHE   A 156 ? 0.1619 0.1714 0.1911 0.0415  0.0466  0.0751  156 PHE   A O   
3879 O O   B PHE   A 156 ? 0.1920 0.2081 0.3167 -0.0188 0.0120  0.0860  156 PHE   A O   
3880 O O   T PHE   A 156 ? 0.1781 0.1801 0.2032 0.0434  0.0578  0.0227  156 PHE   A O   
3881 C CB  A PHE   A 156 ? 0.1833 0.1791 0.2143 0.0419  0.0039  0.0517  156 PHE   A CB  
3882 C CB  B PHE   A 156 ? 0.1912 0.1760 0.2821 -0.0214 -0.0076 0.0959  156 PHE   A CB  
3883 C CB  T PHE   A 156 ? 0.2059 0.1715 0.2124 0.0391  0.0214  0.0610  156 PHE   A CB  
3884 C CG  A PHE   A 156 ? 0.1990 0.1830 0.2415 0.0421  -0.0034 0.0303  156 PHE   A CG  
3885 C CG  B PHE   A 156 ? 0.2079 0.1861 0.3024 -0.0180 -0.0209 0.0883  156 PHE   A CG  
3886 C CG  T PHE   A 156 ? 0.2155 0.1650 0.2258 0.0426  0.0136  0.0665  156 PHE   A CG  
3887 C CD1 A PHE   A 156 ? 0.2041 0.1830 0.2438 0.0443  0.0024  0.0289  156 PHE   A CD1 
3888 C CD1 B PHE   A 156 ? 0.2183 0.2030 0.3354 -0.0117 -0.0169 0.0619  156 PHE   A CD1 
3889 C CD1 T PHE   A 156 ? 0.2220 0.1604 0.2306 0.0463  0.0016  0.0767  156 PHE   A CD1 
3890 C CD2 A PHE   A 156 ? 0.2072 0.1890 0.2551 0.0404  -0.0070 0.0205  156 PHE   A CD2 
3891 C CD2 B PHE   A 156 ? 0.2216 0.1886 0.3298 -0.0158 -0.0227 0.0854  156 PHE   A CD2 
3892 C CD2 T PHE   A 156 ? 0.2194 0.1632 0.2319 0.0414  0.0184  0.0674  156 PHE   A CD2 
3893 C CE1 A PHE   A 156 ? 0.2093 0.1842 0.2500 0.0438  0.0072  0.0211  156 PHE   A CE1 
3894 C CE1 B PHE   A 156 ? 0.2267 0.2128 0.3613 -0.0121 -0.0117 0.0520  156 PHE   A CE1 
3895 C CE1 T PHE   A 156 ? 0.2272 0.1623 0.2398 0.0497  -0.0081 0.0825  156 PHE   A CE1 
3896 C CE2 A PHE   A 156 ? 0.2162 0.1941 0.2605 0.0402  -0.0074 0.0100  156 PHE   A CE2 
3897 C CE2 B PHE   A 156 ? 0.2378 0.2059 0.3613 -0.0158 -0.0240 0.0623  156 PHE   A CE2 
3898 C CE2 T PHE   A 156 ? 0.2268 0.1643 0.2370 0.0419  0.0105  0.0710  156 PHE   A CE2 
3899 C CZ  A PHE   A 156 ? 0.2133 0.1909 0.2534 0.0441  0.0083  0.0111  156 PHE   A CZ  
3900 C CZ  B PHE   A 156 ? 0.2358 0.2140 0.3768 -0.0190 -0.0134 0.0581  156 PHE   A CZ  
3901 C CZ  T PHE   A 156 ? 0.2301 0.1632 0.2469 0.0419  -0.0020 0.0789  156 PHE   A CZ  
3929 N N   A ASP   A 157 ? 0.1555 0.1774 0.1975 0.0573  0.0353  0.0480  157 ASP   A N   
3930 N N   B ASP   A 157 ? 0.2079 0.2294 0.3207 -0.0145 0.0009  0.1208  157 ASP   A N   
3931 N N   T ASP   A 157 ? 0.1849 0.1792 0.1912 0.0448  0.0340  0.0408  157 ASP   A N   
3932 C CA  A ASP   A 157 ? 0.1580 0.1964 0.1950 0.0570  0.0286  0.0438  157 ASP   A CA  
3933 C CA  B ASP   A 157 ? 0.2186 0.2641 0.3289 -0.0102 -0.0018 0.1241  157 ASP   A CA  
3934 C CA  T ASP   A 157 ? 0.1904 0.1887 0.1784 0.0446  0.0203  0.0465  157 ASP   A CA  
3935 C C   A ASP   A 157 ? 0.1489 0.2159 0.1858 0.0500  0.0210  0.0460  157 ASP   A C   
3936 C C   B ASP   A 157 ? 0.2006 0.2681 0.2940 -0.0118 -0.0141 0.1127  157 ASP   A C   
3937 C C   T ASP   A 157 ? 0.1822 0.2048 0.1597 0.0421  0.0151  0.0532  157 ASP   A C   
3938 O O   A ASP   A 157 ? 0.1519 0.2190 0.1832 0.0394  0.0187  0.0500  157 ASP   A O   
3939 O O   B ASP   A 157 ? 0.1868 0.2618 0.2769 -0.0184 -0.0249 0.1166  157 ASP   A O   
3940 O O   T ASP   A 157 ? 0.1802 0.2036 0.1557 0.0344  0.0200  0.0619  157 ASP   A O   
3941 C CB  A ASP   A 157 ? 0.1722 0.1937 0.2116 0.0702  0.0302  0.0445  157 ASP   A CB  
3942 C CB  B ASP   A 157 ? 0.2498 0.2974 0.3842 -0.0013 0.0039  0.1306  157 ASP   A CB  
3943 C CB  T ASP   A 157 ? 0.2050 0.1801 0.1920 0.0527  0.0165  0.0501  157 ASP   A CB  
3944 C CG  A ASP   A 157 ? 0.1908 0.1985 0.2301 0.0765  0.0259  0.0479  157 ASP   A CG  
3945 C CG  B ASP   A 157 ? 0.2744 0.3211 0.4292 0.0120  0.0113  0.1436  157 ASP   A CG  
3946 C CG  T ASP   A 157 ? 0.2207 0.1773 0.2031 0.0564  0.0133  0.0544  157 ASP   A CG  
3947 O OD1 A ASP   A 157 ? 0.2020 0.2032 0.2491 0.0730  0.0152  0.0413  157 ASP   A OD1 
3948 O OD1 B ASP   A 157 ? 0.2728 0.3165 0.4351 0.0281  0.0051  0.1562  157 ASP   A OD1 
3949 O OD1 T ASP   A 157 ? 0.2263 0.1791 0.2359 0.0599  0.0125  0.0408  157 ASP   A OD1 
3950 O OD2 A ASP   A 157 ? 0.1922 0.1933 0.2264 0.0850  0.0261  0.0576  157 ASP   A OD2 
3951 O OD2 B ASP   A 157 ? 0.2894 0.3418 0.4678 0.0104  0.0109  0.1313  157 ASP   A OD2 
3952 O OD2 T ASP   A 157 ? 0.2251 0.1684 0.1785 0.0544  0.0028  0.0656  157 ASP   A OD2 
3965 N N   A LYS   A 158 ? 0.1474 0.2304 0.1902 0.0487  0.0296  0.0437  158 LYS   A N   
3966 N N   B LYS   A 158 ? 0.2088 0.2801 0.2921 -0.0092 -0.0045 0.0912  158 LYS   A N   
3967 N N   T LYS   A 158 ? 0.1856 0.2220 0.1646 0.0432  0.0187  0.0435  158 LYS   A N   
3968 C CA  A LYS   A 158 ? 0.1490 0.2447 0.2062 0.0477  0.0351  0.0442  158 LYS   A CA  
3969 C CA  B LYS   A 158 ? 0.2292 0.3001 0.2948 0.0039  -0.0008 0.0723  158 LYS   A CA  
3970 C CA  T LYS   A 158 ? 0.1892 0.2370 0.1856 0.0462  0.0223  0.0414  158 LYS   A CA  
3971 C C   A LYS   A 158 ? 0.1499 0.2518 0.2018 0.0469  0.0327  0.0484  158 LYS   A C   
3972 C C   B LYS   A 158 ? 0.2165 0.3030 0.2766 0.0085  -0.0022 0.0594  158 LYS   A C   
3973 C C   T LYS   A 158 ? 0.1868 0.2406 0.1887 0.0479  0.0202  0.0364  158 LYS   A C   
3974 O O   A LYS   A 158 ? 0.1451 0.2570 0.2044 0.0426  0.0399  0.0531  158 LYS   A O   
3975 O O   B LYS   A 158 ? 0.2020 0.3100 0.2633 -0.0048 -0.0045 0.0590  158 LYS   A O   
3976 O O   T LYS   A 158 ? 0.1818 0.2405 0.1923 0.0479  0.0228  0.0367  158 LYS   A O   
3977 C CB  A LYS   A 158 ? 0.1513 0.2534 0.2336 0.0418  0.0540  0.0345  158 LYS   A CB  
3978 C CB  B LYS   A 158 ? 0.2612 0.3237 0.3353 0.0093  -0.0145 0.0656  158 LYS   A CB  
3979 C CB  T LYS   A 158 ? 0.1992 0.2491 0.2184 0.0425  0.0357  0.0364  158 LYS   A CB  
3980 C CG  A LYS   A 158 ? 0.1567 0.2607 0.2580 0.0347  0.0663  0.0358  158 LYS   A CG  
3981 C CG  B LYS   A 158 ? 0.2958 0.3475 0.3850 0.0098  -0.0204 0.0497  158 LYS   A CG  
3982 C CG  T LYS   A 158 ? 0.2111 0.2597 0.2474 0.0388  0.0439  0.0398  158 LYS   A CG  
3983 C CD  A LYS   A 158 ? 0.1647 0.2652 0.2761 0.0282  0.0765  0.0399  158 LYS   A CD  
3984 C CD  B LYS   A 158 ? 0.3224 0.3653 0.4237 0.0099  -0.0356 0.0355  158 LYS   A CD  
3985 C CD  T LYS   A 158 ? 0.2259 0.2681 0.2751 0.0384  0.0452  0.0448  158 LYS   A CD  
3986 C CE  A LYS   A 158 ? 0.1643 0.2643 0.2761 0.0205  0.0914  0.0505  158 LYS   A CE  
3987 C CE  B LYS   A 158 ? 0.3401 0.3759 0.4483 0.0093  -0.0472 0.0252  158 LYS   A CE  
3988 C CE  T LYS   A 158 ? 0.2360 0.2722 0.2911 0.0389  0.0452  0.0484  158 LYS   A CE  
3989 N NZ  A LYS   A 158 ? 0.1637 0.2622 0.2856 0.0105  0.1051  0.0576  158 LYS   A NZ  
3990 N NZ  B LYS   A 158 ? 0.3504 0.3825 0.4673 0.0066  -0.0533 0.0196  158 LYS   A NZ  
3991 N NZ  T LYS   A 158 ? 0.2435 0.2738 0.3056 0.0395  0.0448  0.0520  158 LYS   A NZ  
4031 N N   A ASN   A 159 ? 0.1598 0.2504 0.2222 0.0465  0.0137  0.0412  159 ASN   A N   
4032 N N   B ASN   A 159 ? 0.2237 0.3074 0.2860 0.0228  -0.0058 0.0560  159 ASN   A N   
4033 N N   T ASN   A 159 ? 0.1941 0.2417 0.2116 0.0475  0.0092  0.0259  159 ASN   A N   
4034 C CA  A ASN   A 159 ? 0.1718 0.2495 0.2243 0.0472  0.0034  0.0335  159 ASN   A CA  
4035 C CA  B ASN   A 159 ? 0.2407 0.3138 0.3188 0.0281  -0.0072 0.0574  159 ASN   A CA  
4036 C CA  T ASN   A 159 ? 0.2048 0.2441 0.2247 0.0461  0.0077  0.0189  159 ASN   A CA  
4037 C C   A ASN   A 159 ? 0.1712 0.2419 0.2002 0.0514  0.0078  0.0285  159 ASN   A C   
4038 C C   B ASN   A 159 ? 0.2193 0.3025 0.2811 0.0209  -0.0137 0.0623  159 ASN   A C   
4039 C C   T ASN   A 159 ? 0.2132 0.2413 0.2186 0.0450  0.0199  0.0110  159 ASN   A C   
4040 O O   A ASN   A 159 ? 0.1684 0.2369 0.1849 0.0587  -0.0068 0.0227  159 ASN   A O   
4041 O O   B ASN   A 159 ? 0.2187 0.3113 0.2974 0.0271  -0.0273 0.0544  159 ASN   A O   
4042 O O   T ASN   A 159 ? 0.2178 0.2379 0.2138 0.0444  0.0239  0.0018  159 ASN   A O   
4043 C CB  A ASN   A 159 ? 0.1800 0.2564 0.2523 0.0461  -0.0086 0.0313  159 ASN   A CB  
4044 C CB  B ASN   A 159 ? 0.2787 0.3266 0.3977 0.0418  0.0112  0.0512  159 ASN   A CB  
4045 C CB  T ASN   A 159 ? 0.2047 0.2495 0.2467 0.0477  -0.0055 0.0223  159 ASN   A CB  
4046 C CG  A ASN   A 159 ? 0.1943 0.2638 0.2814 0.0442  -0.0117 0.0250  159 ASN   A CG  
4047 C CG  B ASN   A 159 ? 0.3158 0.3436 0.4800 0.0389  0.0309  0.0371  159 ASN   A CG  
4048 C CG  T ASN   A 159 ? 0.2101 0.2544 0.2725 0.0487  -0.0101 0.0216  159 ASN   A CG  
4049 O OD1 A ASN   A 159 ? 0.2041 0.2712 0.2972 0.0391  -0.0050 0.0237  159 ASN   A OD1 
4050 O OD1 B ASN   A 159 ? 0.3279 0.3561 0.5095 0.0309  0.0429  0.0233  159 ASN   A OD1 
4051 O OD1 T ASN   A 159 ? 0.2151 0.2614 0.2869 0.0450  -0.0023 0.0209  159 ASN   A OD1 
4052 N ND2 A ASN   A 159 ? 0.1955 0.2659 0.2947 0.0450  -0.0122 0.0149  159 ASN   A ND2 
4053 N ND2 B ASN   A 159 ? 0.3180 0.3481 0.5064 0.0375  0.0313  0.0345  159 ASN   A ND2 
4054 N ND2 T ASN   A 159 ? 0.2088 0.2554 0.2852 0.0516  -0.0132 0.0147  159 ASN   A ND2 
4073 N N   A LEU   A 160 ? 0.1721 0.2349 0.1952 0.0473  0.0105  0.0360  160 LEU   A N   
4074 N N   B LEU   A 160 ? 0.2041 0.2852 0.2432 0.0134  -0.0006 0.0807  160 LEU   A N   
4075 N N   T LEU   A 160 ? 0.2156 0.2383 0.2222 0.0435  0.0164  0.0171  160 LEU   A N   
4076 C CA  A LEU   A 160 ? 0.1720 0.2326 0.1927 0.0386  0.0277  0.0414  160 LEU   A CA  
4077 C CA  B LEU   A 160 ? 0.1988 0.2758 0.2176 0.0020  0.0211  0.0947  160 LEU   A CA  
4078 C CA  T LEU   A 160 ? 0.2186 0.2371 0.2287 0.0411  0.0216  0.0209  160 LEU   A CA  
4079 C C   A LEU   A 160 ? 0.1585 0.2361 0.1670 0.0324  0.0353  0.0449  160 LEU   A C   
4080 C C   B LEU   A 160 ? 0.1842 0.2743 0.2191 0.0008  0.0086  0.1060  160 LEU   A C   
4081 O O   A LEU   A 160 ? 0.1556 0.2347 0.1596 0.0401  0.0350  0.0348  160 LEU   A O   
4082 O O   B LEU   A 160 ? 0.1929 0.2719 0.2424 -0.0110 -0.0146 0.0802  160 LEU   A O   
4083 C CB  A LEU   A 160 ? 0.1820 0.2281 0.2091 0.0428  0.0348  0.0379  160 LEU   A CB  
4084 C CB  B LEU   A 160 ? 0.2203 0.2755 0.2211 -0.0067 0.0253  0.0942  160 LEU   A CB  
4085 C CB  T LEU   A 160 ? 0.2194 0.2357 0.2300 0.0429  0.0278  0.0219  160 LEU   A CB  
4086 C CG  A LEU   A 160 ? 0.1889 0.2257 0.2306 0.0480  0.0391  0.0328  160 LEU   A CG  
4087 C CG  B LEU   A 160 ? 0.2368 0.2854 0.2412 -0.0050 0.0203  0.0758  160 LEU   A CG  
4088 C CG  T LEU   A 160 ? 0.2205 0.2361 0.2393 0.0451  0.0328  0.0209  160 LEU   A CG  
4089 C CD1 A LEU   A 160 ? 0.1941 0.2243 0.2428 0.0487  0.0399  0.0307  160 LEU   A CD1 
4090 C CD1 B LEU   A 160 ? 0.2423 0.2885 0.2602 0.0008  0.0318  0.0804  160 LEU   A CD1 
4091 C CD1 T LEU   A 160 ? 0.2236 0.2356 0.2471 0.0457  0.0335  0.0220  160 LEU   A CD1 
4092 C CD2 A LEU   A 160 ? 0.1908 0.2260 0.2371 0.0508  0.0451  0.0249  160 LEU   A CD2 
4093 C CD2 B LEU   A 160 ? 0.2488 0.2896 0.2620 -0.0127 0.0193  0.0655  160 LEU   A CD2 
4094 C CD2 T LEU   A 160 ? 0.2209 0.2374 0.2423 0.0449  0.0382  0.0162  160 LEU   A CD2 
4127 N N   A TYR   A 161 ? 0.1578 0.2453 0.1915 0.0225  0.0274  0.0619  161 TYR   A N   
4128 N N   B TYR   A 161 ? 0.1770 0.2803 0.2420 0.0080  0.0127  0.1140  161 TYR   A N   
4129 C CA  A TYR   A 161 ? 0.1460 0.2517 0.2106 0.0131  0.0176  0.0709  161 TYR   A CA  
4130 C CA  B TYR   A 161 ? 0.1793 0.2877 0.2538 -0.0028 0.0059  0.1264  161 TYR   A CA  
4131 C C   A TYR   A 161 ? 0.1418 0.2750 0.2456 0.0041  0.0033  0.0809  161 TYR   A C   
4132 C C   B TYR   A 161 ? 0.1871 0.3128 0.2857 -0.0115 -0.0155 0.1264  161 TYR   A C   
4133 O O   A TYR   A 161 ? 0.1335 0.2831 0.2271 -0.0003 0.0065  0.0835  161 TYR   A O   
4134 O O   B TYR   A 161 ? 0.1905 0.3205 0.2688 -0.0223 -0.0184 0.1254  161 TYR   A O   
4135 C CB  A TYR   A 161 ? 0.1516 0.2465 0.2109 0.0095  0.0324  0.0692  161 TYR   A CB  
4136 C CB  B TYR   A 161 ? 0.1726 0.2783 0.2573 0.0063  0.0288  0.1204  161 TYR   A CB  
4137 C CG  A TYR   A 161 ? 0.1521 0.2362 0.2156 0.0079  0.0236  0.0608  161 TYR   A CG  
4138 C CG  B TYR   A 161 ? 0.1701 0.2711 0.2877 0.0010  0.0197  0.1118  161 TYR   A CG  
4139 C CD1 A TYR   A 161 ? 0.1498 0.2314 0.2281 0.0091  0.0044  0.0458  161 TYR   A CD1 
4140 C CD1 B TYR   A 161 ? 0.1715 0.2720 0.3117 0.0013  0.0106  0.0923  161 TYR   A CD1 
4141 C CD2 A TYR   A 161 ? 0.1587 0.2341 0.2223 0.0112  0.0108  0.0715  161 TYR   A CD2 
4142 C CD2 B TYR   A 161 ? 0.1709 0.2699 0.3018 0.0035  0.0132  0.1210  161 TYR   A CD2 
4143 C CE1 A TYR   A 161 ? 0.1544 0.2281 0.2368 0.0132  -0.0066 0.0557  161 TYR   A CE1 
4144 C CE1 B TYR   A 161 ? 0.1764 0.2685 0.3060 0.0044  0.0131  0.0974  161 TYR   A CE1 
4145 C CE2 A TYR   A 161 ? 0.1615 0.2249 0.2312 0.0116  -0.0159 0.0819  161 TYR   A CE2 
4146 C CE2 B TYR   A 161 ? 0.1781 0.2646 0.3048 0.0016  0.0101  0.1218  161 TYR   A CE2 
4147 C CZ  A TYR   A 161 ? 0.1676 0.2223 0.2322 0.0134  -0.0267 0.0781  161 TYR   A CZ  
4148 C CZ  B TYR   A 161 ? 0.1924 0.2659 0.3080 0.0008  0.0156  0.1130  161 TYR   A CZ  
4149 O OH  A TYR   A 161 ? 0.1829 0.2144 0.2327 0.0131  -0.0481 0.0880  161 TYR   A OH  
4150 O OH  B TYR   A 161 ? 0.2189 0.2658 0.3310 -0.0048 0.0152  0.1168  161 TYR   A OH  
4169 N N   A ASP   A 162 ? 0.1433 0.2873 0.2823 0.0096  0.0127  0.0969  162 ASP   A N   
4170 N N   B ASP   A 162 ? 0.1889 0.3267 0.3137 -0.0082 -0.0136 0.1456  162 ASP   A N   
4171 C CA  A ASP   A 162 ? 0.1381 0.2970 0.2946 0.0044  0.0266  0.0986  162 ASP   A CA  
4172 C CA  B ASP   A 162 ? 0.1948 0.3444 0.3457 -0.0190 -0.0210 0.1388  162 ASP   A CA  
4173 C C   A ASP   A 162 ? 0.1316 0.3072 0.2704 0.0098  0.0252  0.1068  162 ASP   A C   
4174 C C   B ASP   A 162 ? 0.2136 0.3529 0.3406 -0.0322 -0.0319 0.1365  162 ASP   A C   
4175 O O   A ASP   A 162 ? 0.1274 0.3169 0.2847 0.0152  0.0366  0.0922  162 ASP   A O   
4176 O O   B ASP   A 162 ? 0.2227 0.3571 0.3509 -0.0396 -0.0302 0.1317  162 ASP   A O   
4177 C CB  A ASP   A 162 ? 0.1492 0.2922 0.3150 -0.0029 0.0350  0.1055  162 ASP   A CB  
4178 C CB  B ASP   A 162 ? 0.1870 0.3510 0.3849 -0.0179 -0.0154 0.1430  162 ASP   A CB  
4179 C CG  A ASP   A 162 ? 0.1656 0.2907 0.3262 -0.0099 0.0401  0.1187  162 ASP   A CG  
4180 C CG  B ASP   A 162 ? 0.1872 0.3563 0.4171 -0.0160 -0.0007 0.1564  162 ASP   A CG  
4181 O OD1 A ASP   A 162 ? 0.1700 0.2952 0.3475 -0.0144 0.0354  0.1145  162 ASP   A OD1 
4182 O OD1 B ASP   A 162 ? 0.1862 0.3540 0.4163 -0.0100 -0.0044 0.1758  162 ASP   A OD1 
4183 O OD2 A ASP   A 162 ? 0.1751 0.2862 0.3199 -0.0093 0.0528  0.1251  162 ASP   A OD2 
4184 O OD2 B ASP   A 162 ? 0.1922 0.3617 0.4248 -0.0125 0.0149  0.1591  162 ASP   A OD2 
4193 N N   A LYS   A 163 ? 0.1487 0.3106 0.2666 0.0045  0.0027  0.1038  163 LYS   A N   
4194 N N   B LYS   A 163 ? 0.2332 0.3561 0.3587 -0.0405 -0.0506 0.1211  163 LYS   A N   
4195 C CA  A LYS   A 163 ? 0.1644 0.3119 0.2582 -0.0008 -0.0043 0.1026  163 LYS   A CA  
4196 C CA  B LYS   A 163 ? 0.2545 0.3593 0.3620 -0.0494 -0.0438 0.1144  163 LYS   A CA  
4197 C C   A LYS   A 163 ? 0.1643 0.3035 0.2465 -0.0087 0.0086  0.0923  163 LYS   A C   
4198 C C   B LYS   A 163 ? 0.2345 0.3418 0.3154 -0.0676 -0.0386 0.0997  163 LYS   A C   
4199 O O   A LYS   A 163 ? 0.1585 0.3090 0.2466 -0.0151 0.0196  0.0906  163 LYS   A O   
4200 O O   B LYS   A 163 ? 0.2418 0.3395 0.3041 -0.0703 -0.0377 0.1079  163 LYS   A O   
4201 C CB  A LYS   A 163 ? 0.1886 0.3248 0.2892 0.0064  -0.0180 0.0917  163 LYS   A CB  
4202 C CB  B LYS   A 163 ? 0.2894 0.3829 0.4215 -0.0466 -0.0432 0.1048  163 LYS   A CB  
4203 C CG  A LYS   A 163 ? 0.2167 0.3392 0.3369 0.0115  -0.0212 0.0788  163 LYS   A CG  
4204 C CG  B LYS   A 163 ? 0.3147 0.4020 0.4762 -0.0427 -0.0499 0.0966  163 LYS   A CG  
4205 C CD  A LYS   A 163 ? 0.2459 0.3511 0.3834 0.0181  -0.0314 0.0671  163 LYS   A CD  
4206 C CD  B LYS   A 163 ? 0.3363 0.4190 0.5281 -0.0396 -0.0549 0.0871  163 LYS   A CD  
4207 C CE  A LYS   A 163 ? 0.2761 0.3595 0.4256 0.0206  -0.0298 0.0585  163 LYS   A CE  
4208 C CE  B LYS   A 163 ? 0.3518 0.4304 0.5637 -0.0379 -0.0551 0.0823  163 LYS   A CE  
4209 N NZ  A LYS   A 163 ? 0.2842 0.3659 0.4520 0.0208  -0.0277 0.0535  163 LYS   A NZ  
4210 N NZ  B LYS   A 163 ? 0.3592 0.4365 0.5810 -0.0372 -0.0509 0.0797  163 LYS   A NZ  
4237 N N   A LEU   A 164 ? 0.1593 0.2825 0.2198 -0.0123 0.0061  0.0911  164 LEU   A N   
4238 N N   B LEU   A 164 ? 0.2189 0.3302 0.2840 -0.0683 -0.0419 0.0856  164 LEU   A N   
4239 C CA  A LEU   A 164 ? 0.1645 0.2754 0.2105 -0.0104 0.0166  0.0702  164 LEU   A CA  
4240 C CA  B LEU   A 164 ? 0.2229 0.3226 0.2731 -0.0641 -0.0192 0.0806  164 LEU   A CA  
4241 C C   A LEU   A 164 ? 0.1685 0.2837 0.2225 -0.0123 0.0143  0.0671  164 LEU   A C   
4242 C C   B LEU   A 164 ? 0.2243 0.3273 0.2682 -0.0657 -0.0328 0.0849  164 LEU   A C   
4243 O O   A LEU   A 164 ? 0.1660 0.2834 0.2359 -0.0143 0.0301  0.0487  164 LEU   A O   
4244 O O   B LEU   A 164 ? 0.2282 0.3317 0.2688 -0.0602 -0.0260 0.0724  164 LEU   A O   
4245 C CB  A LEU   A 164 ? 0.1688 0.2604 0.1849 -0.0048 0.0230  0.0579  164 LEU   A CB  
4246 C CB  B LEU   A 164 ? 0.2268 0.3109 0.2686 -0.0630 0.0051  0.0670  164 LEU   A CB  
4247 C CG  A LEU   A 164 ? 0.1650 0.2402 0.1603 -0.0086 0.0130  0.0523  164 LEU   A CG  
4248 C CG  B LEU   A 164 ? 0.2277 0.3049 0.2753 -0.0559 0.0165  0.0545  164 LEU   A CG  
4249 C CD1 A LEU   A 164 ? 0.1604 0.2385 0.1455 -0.0032 0.0126  0.0472  164 LEU   A CD1 
4250 C CD1 B LEU   A 164 ? 0.2243 0.3043 0.2786 -0.0537 0.0034  0.0493  164 LEU   A CD1 
4251 C CD2 A LEU   A 164 ? 0.1619 0.2304 0.1733 -0.0212 0.0067  0.0445  164 LEU   A CD2 
4252 C CD2 B LEU   A 164 ? 0.2425 0.3110 0.2865 -0.0439 0.0282  0.0511  164 LEU   A CD2 
4275 N N   A VAL   A 165 ? 0.1637 0.2905 0.2069 -0.0180 0.0154  0.0793  165 VAL   A N   
4276 N N   B VAL   A 165 ? 0.2228 0.3332 0.2659 -0.0685 -0.0412 0.1054  165 VAL   A N   
4277 C CA  A VAL   A 165 ? 0.1712 0.2984 0.1967 -0.0301 0.0149  0.0896  165 VAL   A CA  
4278 C CA  B VAL   A 165 ? 0.2324 0.3416 0.2686 -0.0813 -0.0548 0.1204  165 VAL   A CA  
4279 C C   A VAL   A 165 ? 0.1704 0.3112 0.1943 -0.0398 0.0209  0.0895  165 VAL   A C   
4280 C C   B VAL   A 165 ? 0.2552 0.3607 0.3034 -0.0801 -0.0674 0.1157  165 VAL   A C   
4281 O O   A VAL   A 165 ? 0.1721 0.3175 0.1857 -0.0388 0.0414  0.1002  165 VAL   A O   
4282 O O   B VAL   A 165 ? 0.2565 0.3590 0.3053 -0.0942 -0.0695 0.1310  165 VAL   A O   
4283 C CB  A VAL   A 165 ? 0.1808 0.3023 0.2227 -0.0273 0.0228  0.0758  165 VAL   A CB  
4284 C CB  B VAL   A 165 ? 0.2297 0.3419 0.2693 -0.0816 -0.0656 0.1184  165 VAL   A CB  
4285 C CG1 A VAL   A 165 ? 0.1866 0.3072 0.2270 -0.0269 0.0323  0.0699  165 VAL   A CG1 
4286 C CG1 B VAL   A 165 ? 0.2259 0.3460 0.2767 -0.0814 -0.0640 0.1111  165 VAL   A CG1 
4287 C CG2 A VAL   A 165 ? 0.1784 0.2990 0.2086 -0.0253 0.0321  0.0789  165 VAL   A CG2 
4288 C CG2 B VAL   A 165 ? 0.2371 0.3393 0.2692 -0.0812 -0.0652 0.1226  165 VAL   A CG2 
4307 N N   A SER   A 166 ? 0.1499 0.3191 0.2073 -0.0440 0.0107  0.0618  166 SER   A N   
4308 N N   B SER   A 166 ? 0.2738 0.3862 0.3429 -0.0686 -0.0668 0.0922  166 SER   A N   
4309 C CA  A SER   A 166 ? 0.1501 0.3304 0.2445 -0.0393 -0.0144 0.0357  166 SER   A CA  
4310 C CA  B SER   A 166 ? 0.3068 0.4220 0.3768 -0.0502 -0.0700 0.0641  166 SER   A CA  
4311 C C   A SER   A 166 ? 0.1458 0.3281 0.2521 -0.0313 -0.0193 0.0224  166 SER   A C   
4312 C C   B SER   A 166 ? 0.3482 0.4483 0.3824 -0.0440 -0.0685 0.0417  166 SER   A C   
4313 O O   A SER   A 166 ? 0.1567 0.3314 0.2796 -0.0303 -0.0184 0.0116  166 SER   A O   
4314 O O   B SER   A 166 ? 0.3488 0.4492 0.3736 -0.0430 -0.0798 0.0381  166 SER   A O   
4315 C CB  A SER   A 166 ? 0.1591 0.3419 0.2720 -0.0295 -0.0309 0.0198  166 SER   A CB  
4316 C CB  B SER   A 166 ? 0.3072 0.4320 0.4051 -0.0385 -0.0715 0.0572  166 SER   A CB  
4317 O OG  A SER   A 166 ? 0.1832 0.3489 0.2988 -0.0278 -0.0345 0.0275  166 SER   A OG  
4318 O OG  B SER   A 166 ? 0.3148 0.4438 0.4355 -0.0290 -0.0749 0.0563  166 SER   A OG  
4329 N N   A SER   A 167 ? 0.1461 0.3253 0.2325 -0.0167 -0.0105 0.0200  167 SER   A N   
4330 N N   B SER   A 167 ? 0.3925 0.4744 0.3993 -0.0389 -0.0483 0.0251  167 SER   A N   
4331 C CA  A SER   A 167 ? 0.1748 0.3227 0.2268 -0.0051 -0.0019 0.0157  167 SER   A CA  
4332 C CA  B SER   A 167 ? 0.4368 0.5007 0.4227 -0.0317 -0.0375 0.0137  167 SER   A CA  
4333 C C   A SER   A 167 ? 0.1840 0.3178 0.2177 0.0052  0.0111  0.0089  167 SER   A C   
4334 C C   B SER   A 167 ? 0.4723 0.5226 0.4545 -0.0247 -0.0338 0.0056  167 SER   A C   
4335 O O   A SER   A 167 ? 0.1933 0.3148 0.1970 0.0067  0.0173  0.0103  167 SER   A O   
4336 O O   B SER   A 167 ? 0.4759 0.5250 0.4336 -0.0257 -0.0356 -0.0009 167 SER   A O   
4337 C CB  A SER   A 167 ? 0.1835 0.3229 0.2179 0.0039  0.0034  0.0287  167 SER   A CB  
4338 C CB  B SER   A 167 ? 0.4432 0.5048 0.4237 -0.0285 -0.0322 0.0090  167 SER   A CB  
4339 O OG  A SER   A 167 ? 0.1926 0.3255 0.2086 0.0023  0.0082  0.0348  167 SER   A OG  
4340 O OG  B SER   A 167 ? 0.4488 0.5065 0.4271 -0.0272 -0.0290 0.0071  167 SER   A OG  
4351 N N   A PHE   A 168 ? 0.1859 0.3165 0.2220 0.0089  0.0176  0.0095  168 PHE   A N   
4352 N N   B PHE   A 168 ? 0.5057 0.5418 0.5160 -0.0198 -0.0298 0.0019  168 PHE   A N   
4353 C CA  A PHE   A 168 ? 0.2010 0.3193 0.2453 -0.0007 0.0186  0.0125  168 PHE   A CA  
4354 C CA  B PHE   A 168 ? 0.5409 0.5604 0.5846 -0.0170 -0.0146 0.0008  168 PHE   A CA  
4355 C C   A PHE   A 168 ? 0.2322 0.3450 0.2957 -0.0098 0.0151  0.0092  168 PHE   A C   
4356 C C   B PHE   A 168 ? 0.5628 0.5729 0.6190 -0.0238 -0.0189 -0.0053 168 PHE   A C   
4357 O O   A PHE   A 168 ? 0.2353 0.3490 0.3321 -0.0109 0.0164  0.0179  168 PHE   A O   
4358 O O   B PHE   A 168 ? 0.5657 0.5755 0.6471 -0.0238 -0.0206 -0.0077 168 PHE   A O   
4359 C CB  A PHE   A 168 ? 0.1945 0.2992 0.2283 -0.0087 0.0067  0.0182  168 PHE   A CB  
4360 C CB  B PHE   A 168 ? 0.5501 0.5660 0.6073 -0.0081 0.0134  0.0081  168 PHE   A CB  
4361 C CG  A PHE   A 168 ? 0.1878 0.2833 0.1891 -0.0122 0.0010  0.0277  168 PHE   A CG  
4362 C CG  B PHE   A 168 ? 0.5598 0.5717 0.6226 0.0000  0.0421  0.0172  168 PHE   A CG  
4363 C CD1 A PHE   A 168 ? 0.1811 0.2809 0.1652 -0.0104 -0.0174 0.0359  168 PHE   A CD1 
4364 C CD1 B PHE   A 168 ? 0.5629 0.5733 0.6283 0.0026  0.0546  0.0227  168 PHE   A CD1 
4365 C CD2 A PHE   A 168 ? 0.1782 0.2707 0.1616 -0.0159 0.0227  0.0351  168 PHE   A CD2 
4366 C CD2 B PHE   A 168 ? 0.5637 0.5743 0.6301 0.0028  0.0536  0.0209  168 PHE   A CD2 
4367 C CE1 A PHE   A 168 ? 0.1760 0.2753 0.1718 -0.0143 -0.0259 0.0345  168 PHE   A CE1 
4368 C CE1 B PHE   A 168 ? 0.5654 0.5754 0.6360 0.0045  0.0590  0.0252  168 PHE   A CE1 
4369 C CE2 A PHE   A 168 ? 0.1871 0.2700 0.1598 -0.0203 0.0090  0.0382  168 PHE   A CE2 
4370 C CE2 B PHE   A 168 ? 0.5655 0.5761 0.6323 0.0047  0.0582  0.0240  168 PHE   A CE2 
4371 C CZ  A PHE   A 168 ? 0.1834 0.2719 0.1723 -0.0155 -0.0115 0.0378  168 PHE   A CZ  
4372 C CZ  B PHE   A 168 ? 0.5666 0.5764 0.6370 0.0051  0.0589  0.0257  168 PHE   A CZ  
4391 N N   A LEU   A 169 ? 0.2626 0.3647 0.3260 -0.0223 -0.0041 -0.0063 169 LEU   A N   
4392 N N   B LEU   A 169 ? 0.5788 0.5827 0.6129 -0.0320 -0.0147 -0.0105 169 LEU   A N   
4393 C CA  A LEU   A 169 ? 0.2992 0.3886 0.3678 -0.0307 -0.0131 -0.0117 169 LEU   A CA  
4394 C CA  B LEU   A 169 ? 0.5933 0.5903 0.5976 -0.0393 -0.0050 -0.0150 169 LEU   A CA  
4395 C C   A LEU   A 169 ? 0.3068 0.3943 0.3478 -0.0338 -0.0130 -0.0029 169 LEU   A C   
4396 C C   B LEU   A 169 ? 0.5971 0.5906 0.5750 -0.0452 -0.0026 -0.0132 169 LEU   A C   
4397 O O   A LEU   A 169 ? 0.3121 0.3966 0.3342 -0.0319 -0.0080 -0.0034 169 LEU   A O   
4398 O O   B LEU   A 169 ? 0.5989 0.5908 0.5680 -0.0471 -0.0001 -0.0148 169 LEU   A O   
4399 C CB  A LEU   A 169 ? 0.3237 0.4042 0.4195 -0.0376 -0.0176 -0.0251 169 LEU   A CB  
4400 C CB  B LEU   A 169 ? 0.6027 0.5963 0.5999 -0.0408 0.0052  -0.0208 169 LEU   A CB  
4401 C CG  A LEU   A 169 ? 0.3439 0.4169 0.4675 -0.0427 -0.0242 -0.0414 169 LEU   A CG  
4402 C CG  B LEU   A 169 ? 0.6083 0.6003 0.6031 -0.0420 0.0105  -0.0241 169 LEU   A CG  
4403 C CD1 A LEU   A 169 ? 0.3516 0.4206 0.4879 -0.0435 -0.0270 -0.0466 169 LEU   A CD1 
4404 C CD1 B LEU   A 169 ? 0.6098 0.6015 0.6015 -0.0424 0.0115  -0.0249 169 LEU   A CD1 
4405 C CD2 A LEU   A 169 ? 0.3498 0.4218 0.4860 -0.0451 -0.0236 -0.0465 169 LEU   A CD2 
4406 C CD2 B LEU   A 169 ? 0.6096 0.6018 0.6045 -0.0429 0.0110  -0.0245 169 LEU   A CD2 
4407 O OXT A LEU   A 169 ? 0.3028 0.3959 0.3312 -0.0361 -0.0119 0.0021  169 LEU   A OXT 
4408 O OXT B LEU   A 169 ? 0.5977 0.5901 0.5671 -0.0475 -0.0046 -0.0109 169 LEU   A OXT 
4431 N N   A SER   B 1   ? 0.3425 0.2921 0.2669 -0.1066 -0.0662 0.0105  1   SER   B N   
4432 N N   B SER   B 1   ? 0.2282 0.2083 0.2879 0.0149  -0.0267 -0.0147 1   SER   B N   
4433 C CA  A SER   B 1   ? 0.3388 0.3022 0.2724 -0.1059 -0.0743 0.0127  1   SER   B CA  
4434 C CA  B SER   B 1   ? 0.2172 0.2056 0.2750 0.0063  -0.0435 -0.0299 1   SER   B CA  
4435 C C   A SER   B 1   ? 0.3251 0.3061 0.2658 -0.1169 -0.0722 0.0461  1   SER   B C   
4436 C C   B SER   B 1   ? 0.2017 0.2001 0.2298 0.0139  -0.0490 -0.0332 1   SER   B C   
4437 O O   A SER   B 1   ? 0.3305 0.3069 0.2545 -0.1221 -0.0644 0.0687  1   SER   B O   
4438 O O   B SER   B 1   ? 0.2166 0.2067 0.2676 0.0115  -0.0587 -0.0363 1   SER   B O   
4439 C CB  A SER   B 1   ? 0.3450 0.3010 0.2859 -0.1002 -0.0640 -0.0168 1   SER   B CB  
4440 C CB  B SER   B 1   ? 0.2229 0.2154 0.3295 -0.0033 -0.0679 -0.0504 1   SER   B CB  
4441 O OG  A SER   B 1   ? 0.3480 0.3024 0.3175 -0.0955 -0.0476 -0.0385 1   SER   B OG  
4442 O OG  B SER   B 1   ? 0.2344 0.2355 0.3722 -0.0037 -0.0857 -0.0335 1   SER   B OG  
4457 N N   A MET   B 2   ? 0.3053 0.3009 0.2690 -0.1242 -0.0617 0.0743  2   MET   B N   
4458 N N   B MET   B 2   ? 0.1893 0.1911 0.1731 0.0204  -0.0292 -0.0426 2   MET   B N   
4459 C CA  A MET   B 2   ? 0.2884 0.2970 0.2787 -0.1204 -0.0600 0.0885  2   MET   B CA  
4460 C CA  B MET   B 2   ? 0.2096 0.1956 0.1461 0.0147  -0.0219 -0.0358 2   MET   B CA  
4461 C C   A MET   B 2   ? 0.2540 0.2717 0.2426 -0.1068 -0.0793 0.1022  2   MET   B C   
4462 C C   B MET   B 2   ? 0.2102 0.1974 0.1738 0.0234  -0.0182 -0.0079 2   MET   B C   
4463 O O   A MET   B 2   ? 0.2475 0.2777 0.2280 -0.1059 -0.1038 0.1063  2   MET   B O   
4464 O O   B MET   B 2   ? 0.2375 0.2280 0.2232 0.0418  -0.0166 0.0066  2   MET   B O   
4465 C CB  A MET   B 2   ? 0.3127 0.3287 0.3500 -0.1129 -0.0361 0.0683  2   MET   B CB  
4466 C CB  B MET   B 2   ? 0.2425 0.2095 0.1644 0.0110  -0.0031 -0.0379 2   MET   B CB  
4467 C CG  A MET   B 2   ? 0.3404 0.3597 0.4251 -0.0965 -0.0150 0.0525  2   MET   B CG  
4468 C CG  B MET   B 2   ? 0.2848 0.2197 0.2021 0.0156  -0.0199 -0.0288 2   MET   B CG  
4469 S SD  A MET   B 2   ? 0.3687 0.3910 0.4956 -0.0770 0.0039  0.0376  2   MET   B SD  
4470 S SD  B MET   B 2   ? 0.3359 0.2467 0.2089 0.0113  0.0109  -0.0473 2   MET   B SD  
4471 C CE  A MET   B 2   ? 0.3727 0.3933 0.5168 -0.0771 0.0123  0.0437  2   MET   B CE  
4472 C CE  B MET   B 2   ? 0.3442 0.2561 0.2346 0.0087  0.0243  -0.0566 2   MET   B CE  
4491 N N   A VAL   B 3   ? 0.2193 0.2354 0.2166 -0.1007 -0.0661 0.1151  3   VAL   B N   
4492 N N   B VAL   B 3   ? 0.1866 0.1712 0.1722 -0.0022 -0.0177 0.0082  3   VAL   B N   
4493 C CA  A VAL   B 3   ? 0.2015 0.2079 0.2267 -0.0737 -0.0643 0.0865  3   VAL   B CA  
4494 C CA  B VAL   B 3   ? 0.1850 0.1657 0.1892 -0.0155 -0.0188 0.0027  3   VAL   B CA  
4495 C C   A VAL   B 3   ? 0.1916 0.1952 0.2160 -0.0536 -0.0487 0.0715  3   VAL   B C   
4496 C C   B VAL   B 3   ? 0.1744 0.1595 0.1557 -0.0238 -0.0288 0.0156  3   VAL   B C   
4497 O O   A VAL   B 3   ? 0.1894 0.2014 0.2392 -0.0398 -0.0521 0.0825  3   VAL   B O   
4498 O O   B VAL   B 3   ? 0.1555 0.1500 0.1281 -0.0137 -0.0240 0.0022  3   VAL   B O   
4499 C CB  A VAL   B 3   ? 0.2023 0.1992 0.2593 -0.0640 -0.0525 0.0884  3   VAL   B CB  
4500 C CB  B VAL   B 3   ? 0.1952 0.1707 0.2051 -0.0159 -0.0047 -0.0237 3   VAL   B CB  
4501 C CG1 A VAL   B 3   ? 0.2028 0.1937 0.2847 -0.0613 -0.0447 0.0824  3   VAL   B CG1 
4502 C CG1 B VAL   B 3   ? 0.2052 0.1822 0.2367 -0.0246 -0.0087 -0.0225 3   VAL   B CG1 
4503 C CG2 A VAL   B 3   ? 0.2062 0.1951 0.2612 -0.0570 -0.0359 0.1043  3   VAL   B CG2 
4504 C CG2 B VAL   B 3   ? 0.2030 0.1745 0.1890 -0.0024 0.0177  -0.0459 3   VAL   B CG2 
4523 N N   . ASN   B 4   ? 0.1766 0.1783 0.1707 -0.0416 -0.0479 0.0496  4   ASN   B N   
4524 C CA  . ASN   B 4   ? 0.1848 0.1865 0.1554 -0.0411 -0.0449 0.0332  4   ASN   B CA  
4525 C C   . ASN   B 4   ? 0.1851 0.2017 0.1477 -0.0419 -0.0447 0.0282  4   ASN   B C   
4526 O O   . ASN   B 4   ? 0.1898 0.2021 0.1658 -0.0412 -0.0457 0.0026  4   ASN   B O   
4527 C CB  . ASN   B 4   ? 0.1913 0.1811 0.1406 -0.0436 -0.0452 0.0245  4   ASN   B CB  
4528 C CG  . ASN   B 4   ? 0.1936 0.1742 0.1343 -0.0400 -0.0419 0.0243  4   ASN   B CG  
4529 O OD1 . ASN   B 4   ? 0.1926 0.1721 0.1479 -0.0395 -0.0408 0.0282  4   ASN   B OD1 
4530 N ND2 . ASN   B 4   ? 0.2201 0.1830 0.1540 -0.0206 -0.0225 0.0259  4   ASN   B ND2 
4538 N N   . SER   B 5   ? 0.1824 0.2080 0.1661 -0.0484 -0.0299 0.0198  5   SER   B N   
4539 C CA  . SER   B 5   ? 0.2111 0.2430 0.1771 -0.0477 -0.0146 0.0218  5   SER   B CA  
4540 C C   . SER   B 5   ? 0.2457 0.2414 0.2189 -0.0697 -0.0036 0.0215  5   SER   B C   
4541 O O   . SER   B 5   ? 0.2717 0.2232 0.3039 -0.0462 0.0270  0.0192  5   SER   B O   
4542 C CB  . SER   B 5   ? 0.2247 0.2713 0.2352 -0.0371 -0.0043 0.0269  5   SER   B CB  
4543 O OG  . SER   B 5   ? 0.2638 0.3122 0.3545 -0.0268 -0.0008 0.0360  5   SER   B OG  
4549 N N   . PHE   B 6   ? 0.2803 0.2858 0.2231 -0.0917 0.0089  0.0449  6   PHE   B N   
4550 C CA  . PHE   B 6   ? 0.3066 0.3036 0.1618 -0.1299 0.0085  0.0127  6   PHE   B CA  
4551 C C   . PHE   B 6   ? 0.3778 0.3587 0.2328 -0.1436 0.0614  -0.0296 6   PHE   B C   
4552 O O   . PHE   B 6   ? 0.3906 0.4132 0.2913 -0.1331 0.0439  -0.0397 6   PHE   B O   
4553 C CB  . PHE   B 6   ? 0.2793 0.2854 0.1483 -0.1159 -0.0036 0.0150  6   PHE   B CB  
4554 C CG  . PHE   B 6   ? 0.2435 0.2519 0.1660 -0.0973 -0.0158 0.0188  6   PHE   B CG  
4555 C CD1 . PHE   B 6   ? 0.2348 0.2179 0.1477 -0.0861 -0.0214 0.0112  6   PHE   B CD1 
4556 C CD2 . PHE   B 6   ? 0.2173 0.2489 0.1893 -0.0743 -0.0259 0.0578  6   PHE   B CD2 
4557 C CE1 . PHE   B 6   ? 0.2216 0.1897 0.1541 -0.0610 -0.0285 0.0131  6   PHE   B CE1 
4558 C CE2 . PHE   B 6   ? 0.2024 0.2218 0.2261 -0.0579 -0.0135 0.0588  6   PHE   B CE2 
4559 C CZ  . PHE   B 6   ? 0.2049 0.1987 0.1787 -0.0492 -0.0246 0.0342  6   PHE   B CZ  
4569 N N   A SER   B 7   ? 0.4086 0.3479 0.2672 -0.1555 0.0903  -0.0472 7   SER   B N   
4570 N N   B SER   B 7   ? 0.4119 0.3386 0.2489 -0.1627 0.0923  -0.0597 7   SER   B N   
4571 C CA  A SER   B 7   ? 0.4382 0.3569 0.3350 -0.1496 0.1103  -0.0565 7   SER   B CA  
4572 C CA  B SER   B 7   ? 0.4457 0.3530 0.3270 -0.1550 0.1103  -0.0715 7   SER   B CA  
4573 C C   A SER   B 7   ? 0.4481 0.3426 0.3310 -0.1546 0.1229  -0.0746 7   SER   B C   
4574 C C   B SER   B 7   ? 0.4531 0.3373 0.3227 -0.1584 0.1220  -0.0859 7   SER   B C   
4575 O O   A SER   B 7   ? 0.4557 0.3447 0.3486 -0.1549 0.1278  -0.0733 7   SER   B O   
4576 O O   B SER   B 7   ? 0.4632 0.3364 0.3444 -0.1588 0.1275  -0.0873 7   SER   B O   
4577 C CB  A SER   B 7   ? 0.4502 0.3771 0.3953 -0.1402 0.1197  -0.0469 7   SER   B CB  
4578 C CB  B SER   B 7   ? 0.4616 0.3785 0.4032 -0.1454 0.1211  -0.0633 7   SER   B CB  
4579 O OG  A SER   B 7   ? 0.4575 0.3820 0.4384 -0.1332 0.1208  -0.0389 7   SER   B OG  
4580 O OG  B SER   B 7   ? 0.4717 0.3806 0.4617 -0.1390 0.1218  -0.0548 7   SER   B OG  
4591 N N   . GLY   B 8   ? 0.4529 0.3326 0.3169 -0.1526 0.1307  -0.0881 8   GLY   B N   
4592 C CA  . GLY   B 8   ? 0.4428 0.3098 0.3019 -0.1439 0.1459  -0.0954 8   GLY   B CA  
4593 C C   . GLY   B 8   ? 0.4257 0.2761 0.2837 -0.1416 0.1591  -0.0785 8   GLY   B C   
4594 O O   . GLY   B 8   ? 0.4444 0.2818 0.3297 -0.1366 0.1664  -0.0766 8   GLY   B O   
4599 N N   . TYR   B 9   ? 0.4096 0.2557 0.2444 -0.1220 0.1227  -0.0888 9   TYR   B N   
4600 C CA  . TYR   B 9   ? 0.3870 0.2309 0.2194 -0.0984 0.0835  -0.0566 9   TYR   B CA  
4601 C C   . TYR   B 9   ? 0.3739 0.2277 0.2172 -0.0887 0.0405  -0.0418 9   TYR   B C   
4602 O O   . TYR   B 9   ? 0.3807 0.2459 0.2597 -0.0920 0.0464  -0.0320 9   TYR   B O   
4603 C CB  . TYR   B 9   ? 0.3817 0.2033 0.2389 -0.0945 0.0763  -0.0444 9   TYR   B CB  
4604 C CG  . TYR   B 9   ? 0.3769 0.1818 0.2253 -0.1011 0.0675  -0.0489 9   TYR   B CG  
4605 C CD1 . TYR   B 9   ? 0.3807 0.1774 0.2451 -0.1115 0.0766  -0.0435 9   TYR   B CD1 
4606 C CD2 . TYR   B 9   ? 0.3701 0.1749 0.2090 -0.0867 0.0608  -0.0513 9   TYR   B CD2 
4607 C CE1 . TYR   B 9   ? 0.3707 0.1883 0.2411 -0.1126 0.0845  -0.0668 9   TYR   B CE1 
4608 C CE2 . TYR   B 9   ? 0.3663 0.1771 0.2259 -0.0882 0.0763  -0.0395 9   TYR   B CE2 
4609 C CZ  . TYR   B 9   ? 0.3667 0.1887 0.2447 -0.1019 0.0790  -0.0714 9   TYR   B CZ  
4610 O OH  . TYR   B 9   ? 0.3626 0.2033 0.2744 -0.1106 0.0881  -0.0833 9   TYR   B OH  
4620 N N   A LEU   B 10  ? 0.3667 0.2096 0.2045 -0.0914 0.0133  -0.0362 10  LEU   B N   
4621 N N   B LEU   B 10  ? 0.3569 0.2055 0.1934 -0.0986 0.0215  -0.0414 10  LEU   B N   
4622 C CA  A LEU   B 10  ? 0.3678 0.2051 0.2138 -0.0962 -0.0263 -0.0191 10  LEU   B CA  
4623 C CA  B LEU   B 10  ? 0.3533 0.2017 0.1919 -0.1131 -0.0183 -0.0264 10  LEU   B CA  
4624 C C   A LEU   B 10  ? 0.3637 0.2124 0.2180 -0.0898 -0.0428 -0.0121 10  LEU   B C   
4625 C C   B LEU   B 10  ? 0.3446 0.2053 0.1825 -0.1131 -0.0347 -0.0139 10  LEU   B C   
4626 O O   A LEU   B 10  ? 0.3591 0.2061 0.2131 -0.0844 -0.0497 -0.0101 10  LEU   B O   
4627 O O   B LEU   B 10  ? 0.3324 0.2019 0.1828 -0.1170 -0.0314 -0.0029 10  LEU   B O   
4628 C CB  A LEU   B 10  ? 0.3780 0.2009 0.2293 -0.0980 -0.0471 -0.0022 10  LEU   B CB  
4629 C CB  B LEU   B 10  ? 0.3671 0.2078 0.2163 -0.1131 -0.0414 -0.0133 10  LEU   B CB  
4630 C CG  A LEU   B 10  ? 0.3859 0.2047 0.2482 -0.0937 -0.0673 0.0128  10  LEU   B CG  
4631 C CG  B LEU   B 10  ? 0.3779 0.2202 0.2451 -0.1055 -0.0621 0.0010  10  LEU   B CG  
4632 C CD1 A LEU   B 10  ? 0.3937 0.2094 0.2541 -0.0879 -0.0663 0.0116  10  LEU   B CD1 
4633 C CD1 B LEU   B 10  ? 0.3852 0.2266 0.2620 -0.0968 -0.0570 -0.0013 10  LEU   B CD1 
4634 C CD2 A LEU   B 10  ? 0.3860 0.2034 0.2562 -0.0921 -0.0679 0.0343  10  LEU   B CD2 
4635 C CD2 B LEU   B 10  ? 0.3811 0.2264 0.2562 -0.1027 -0.0593 0.0240  10  LEU   B CD2 
4658 N N   A LYS   B 11  ? 0.3670 0.2338 0.2261 -0.0846 -0.0513 -0.0082 11  LYS   B N   
4659 N N   B LYS   B 11  ? 0.3542 0.2313 0.1767 -0.0997 -0.0552 -0.0128 11  LYS   B N   
4660 C CA  A LYS   B 11  ? 0.3700 0.2530 0.2652 -0.0800 -0.0622 -0.0145 11  LYS   B CA  
4661 C CA  B LYS   B 11  ? 0.3659 0.2563 0.2403 -0.0869 -0.0706 -0.0226 11  LYS   B CA  
4662 C C   A LYS   B 11  ? 0.3501 0.2334 0.2625 -0.0987 -0.0584 -0.0208 11  LYS   B C   
4663 C C   B LYS   B 11  ? 0.3496 0.2357 0.2548 -0.1043 -0.0613 -0.0260 11  LYS   B C   
4664 O O   A LYS   B 11  ? 0.3589 0.2418 0.2898 -0.1108 -0.0610 -0.0405 11  LYS   B O   
4665 O O   B LYS   B 11  ? 0.3607 0.2479 0.2920 -0.1198 -0.0654 -0.0535 11  LYS   B O   
4666 C CB  A LYS   B 11  ? 0.3901 0.2902 0.3280 -0.0575 -0.0653 -0.0174 11  LYS   B CB  
4667 C CB  B LYS   B 11  ? 0.3914 0.2989 0.3208 -0.0573 -0.0753 -0.0268 11  LYS   B CB  
4668 C CG  A LYS   B 11  ? 0.4062 0.3166 0.3942 -0.0429 -0.0645 -0.0168 11  LYS   B CG  
4669 C CG  B LYS   B 11  ? 0.4112 0.3297 0.4086 -0.0390 -0.0745 -0.0254 11  LYS   B CG  
4670 C CD  A LYS   B 11  ? 0.4183 0.3351 0.4557 -0.0339 -0.0613 -0.0194 11  LYS   B CD  
4671 C CD  B LYS   B 11  ? 0.4262 0.3494 0.4858 -0.0282 -0.0713 -0.0296 11  LYS   B CD  
4672 C CE  A LYS   B 11  ? 0.4263 0.3473 0.5021 -0.0295 -0.0600 -0.0226 11  LYS   B CE  
4673 C CE  B LYS   B 11  ? 0.4371 0.3630 0.5425 -0.0222 -0.0696 -0.0310 11  LYS   B CE  
4674 N NZ  A LYS   B 11  ? 0.4316 0.3546 0.5247 -0.0270 -0.0612 -0.0222 11  LYS   B NZ  
4675 N NZ  B LYS   B 11  ? 0.4432 0.3705 0.5695 -0.0198 -0.0723 -0.0300 11  LYS   B NZ  
4702 N N   . LEU   B 12  ? 0.3196 0.2165 0.2411 -0.0997 -0.0627 -0.0203 12  LEU   B N   
4703 C CA  . LEU   B 12  ? 0.2919 0.1954 0.2597 -0.0858 -0.0447 -0.0153 12  LEU   B CA  
4704 C C   . LEU   B 12  ? 0.2745 0.1972 0.2630 -0.0914 -0.0685 -0.0065 12  LEU   B C   
4705 O O   . LEU   B 12  ? 0.2726 0.1993 0.2927 -0.0914 -0.0814 -0.0042 12  LEU   B O   
4706 C CB  . LEU   B 12  ? 0.2832 0.1680 0.2652 -0.0673 -0.0514 -0.0131 12  LEU   B CB  
4707 C CG  . LEU   B 12  ? 0.2817 0.1684 0.2699 -0.0549 -0.0455 -0.0077 12  LEU   B CG  
4708 C CD1 . LEU   B 12  ? 0.2905 0.1670 0.2562 -0.0435 -0.0460 0.0168  12  LEU   B CD1 
4709 C CD2 . LEU   B 12  ? 0.2857 0.1742 0.2825 -0.0569 -0.0350 -0.0228 12  LEU   B CD2 
4722 N N   . THR   B 13  ? 0.2649 0.2020 0.2755 -0.0892 -0.0663 -0.0222 13  THR   B N   
4723 C CA  . THR   B 13  ? 0.2614 0.2143 0.2702 -0.0856 -0.0848 -0.0070 13  THR   B CA  
4724 C C   . THR   B 13  ? 0.2948 0.2287 0.2856 -0.0929 -0.1024 0.0025  13  THR   B C   
4725 O O   . THR   B 13  ? 0.3168 0.2262 0.3081 -0.0880 -0.0758 -0.0031 13  THR   B O   
4726 C CB  . THR   B 13  ? 0.2383 0.2205 0.2661 -0.0759 -0.0757 -0.0056 13  THR   B CB  
4727 O OG1 . THR   B 13  ? 0.2179 0.2051 0.2643 -0.0691 -0.0515 -0.0027 13  THR   B OG1 
4728 C CG2 . THR   B 13  ? 0.2450 0.2285 0.2740 -0.0767 -0.0655 -0.0120 13  THR   B CG2 
4736 N N   A ASP   B 14  ? 0.3012 0.2393 0.2943 -0.0991 -0.1224 0.0115  14  ASP   B N   
4737 N N   B ASP   B 14  ? 0.3030 0.2399 0.2835 -0.1025 -0.1313 0.0163  14  ASP   B N   
4738 C CA  A ASP   B 14  ? 0.3100 0.2497 0.3275 -0.0943 -0.1205 0.0264  14  ASP   B CA  
4739 C CA  B ASP   B 14  ? 0.3164 0.2508 0.3212 -0.0960 -0.1258 0.0390  14  ASP   B CA  
4740 C C   A ASP   B 14  ? 0.3003 0.2320 0.2887 -0.0926 -0.1174 0.0333  14  ASP   B C   
4741 C C   B ASP   B 14  ? 0.3054 0.2329 0.2837 -0.0961 -0.1197 0.0415  14  ASP   B C   
4742 O O   A ASP   B 14  ? 0.3216 0.2465 0.2888 -0.0945 -0.1110 0.0304  14  ASP   B O   
4743 O O   B ASP   B 14  ? 0.3321 0.2520 0.2867 -0.0977 -0.1112 0.0388  14  ASP   B O   
4744 C CB  A ASP   B 14  ? 0.3247 0.2819 0.3995 -0.0882 -0.1246 0.0200  14  ASP   B CB  
4745 C CB  B ASP   B 14  ? 0.3366 0.2875 0.3982 -0.0843 -0.1272 0.0376  14  ASP   B CB  
4746 C CG  A ASP   B 14  ? 0.3417 0.3109 0.4702 -0.0793 -0.1179 0.0077  14  ASP   B CG  
4747 C CG  B ASP   B 14  ? 0.3597 0.3222 0.4771 -0.0699 -0.1127 0.0250  14  ASP   B CG  
4748 O OD1 A ASP   B 14  ? 0.3492 0.3173 0.4887 -0.0863 -0.1201 -0.0025 14  ASP   B OD1 
4749 O OD1 B ASP   B 14  ? 0.3742 0.3333 0.5017 -0.0681 -0.1043 0.0174  14  ASP   B OD1 
4750 O OD2 A ASP   B 14  ? 0.3463 0.3239 0.5029 -0.0769 -0.1106 0.0055  14  ASP   B OD2 
4751 O OD2 B ASP   B 14  ? 0.3673 0.3367 0.5110 -0.0620 -0.1047 0.0233  14  ASP   B OD2 
4760 N N   . ASN   B 15  ? 0.2729 0.2099 0.2651 -0.0777 -0.1172 0.0380  15  ASN   B N   
4761 C CA  . ASN   B 15  ? 0.2290 0.1835 0.2441 -0.0519 -0.0938 0.0128  15  ASN   B CA  
4762 C C   . ASN   B 15  ? 0.2071 0.1661 0.2210 -0.0452 -0.0744 0.0073  15  ASN   B C   
4763 O O   . ASN   B 15  ? 0.1955 0.1528 0.2283 -0.0340 -0.0589 -0.0010 15  ASN   B O   
4764 C CB  . ASN   B 15  ? 0.2185 0.1717 0.2591 -0.0225 -0.0875 0.0159  15  ASN   B CB  
4765 C CG  . ASN   B 15  ? 0.1925 0.1665 0.2856 -0.0351 -0.0565 0.0257  15  ASN   B CG  
4766 O OD1 . ASN   B 15  ? 0.2004 0.2006 0.3244 -0.0572 -0.0650 0.0358  15  ASN   B OD1 
4767 N ND2 . ASN   B 15  ? 0.1823 0.1408 0.2591 -0.0189 -0.0153 -0.0032 15  ASN   B ND2 
4775 N N   . VAL   B 16  ? 0.2028 0.1572 0.2269 -0.0562 -0.0741 0.0092  16  VAL   B N   
4776 C CA  . VAL   B 16  ? 0.2084 0.1531 0.1990 -0.0457 -0.0626 -0.0047 16  VAL   B CA  
4777 C C   . VAL   B 16  ? 0.2137 0.1586 0.2057 -0.0541 -0.0576 0.0018  16  VAL   B C   
4778 O O   . VAL   B 16  ? 0.2137 0.1706 0.2375 -0.0452 -0.0573 -0.0066 16  VAL   B O   
4779 C CB  . VAL   B 16  ? 0.2065 0.1593 0.2133 -0.0302 -0.0519 -0.0085 16  VAL   B CB  
4780 C CG1 . VAL   B 16  ? 0.2090 0.1621 0.2440 -0.0231 -0.0409 0.0107  16  VAL   B CG1 
4781 C CG2 . VAL   B 16  ? 0.2141 0.1643 0.2519 -0.0191 -0.0475 -0.0183 16  VAL   B CG2 
4791 N N   . TYR   B 17  ? 0.2184 0.1729 0.1797 -0.0533 -0.0485 0.0023  17  TYR   B N   
4792 C CA  . TYR   B 17  ? 0.2294 0.1950 0.1778 -0.0711 -0.0537 0.0169  17  TYR   B CA  
4793 C C   . TYR   B 17  ? 0.2232 0.1594 0.1830 -0.0731 -0.0378 0.0005  17  TYR   B C   
4794 O O   . TYR   B 17  ? 0.2183 0.1712 0.1798 -0.0541 -0.0414 -0.0221 17  TYR   B O   
4795 C CB  . TYR   B 17  ? 0.2664 0.2492 0.2138 -0.0664 -0.0574 0.0542  17  TYR   B CB  
4796 C CG  . TYR   B 17  ? 0.2985 0.3129 0.2727 -0.0599 -0.0795 0.0797  17  TYR   B CG  
4797 C CD1 . TYR   B 17  ? 0.3103 0.3370 0.2954 -0.0617 -0.0948 0.1005  17  TYR   B CD1 
4798 C CD2 . TYR   B 17  ? 0.3212 0.3519 0.3004 -0.0462 -0.0951 0.0875  17  TYR   B CD2 
4799 C CE1 . TYR   B 17  ? 0.3304 0.3760 0.3128 -0.0477 -0.1109 0.1030  17  TYR   B CE1 
4800 C CE2 . TYR   B 17  ? 0.3366 0.3865 0.3172 -0.0344 -0.1114 0.0983  17  TYR   B CE2 
4801 C CZ  . TYR   B 17  ? 0.3464 0.3983 0.3255 -0.0332 -0.1138 0.1043  17  TYR   B CZ  
4802 O OH  . TYR   B 17  ? 0.3606 0.4087 0.3481 -0.0192 -0.1182 0.1068  17  TYR   B OH  
4812 N N   . ILE   B 18  ? 0.2385 0.1666 0.1638 -0.0675 -0.0186 -0.0047 18  ILE   B N   
4813 C CA  . ILE   B 18  ? 0.2434 0.1616 0.1622 -0.0617 -0.0093 -0.0200 18  ILE   B CA  
4814 C C   . ILE   B 18  ? 0.2570 0.1640 0.1645 -0.0771 -0.0057 -0.0324 18  ILE   B C   
4815 O O   . ILE   B 18  ? 0.2748 0.1763 0.1851 -0.0726 -0.0008 -0.0400 18  ILE   B O   
4816 C CB  . ILE   B 18  ? 0.2420 0.1589 0.1744 -0.0633 -0.0085 -0.0067 18  ILE   B CB  
4817 C CG1 . ILE   B 18  ? 0.2427 0.1603 0.1761 -0.0596 -0.0040 -0.0128 18  ILE   B CG1 
4818 C CG2 . ILE   B 18  ? 0.2431 0.1705 0.1873 -0.0725 -0.0201 -0.0099 18  ILE   B CG2 
4819 C CD1 . ILE   B 18  ? 0.2448 0.1922 0.2054 -0.0564 -0.0168 0.0200  18  ILE   B CD1 
4831 N N   . LYS   B 19  ? 0.2613 0.1598 0.1756 -0.0543 0.0323  -0.0441 19  LYS   B N   
4832 C CA  . LYS   B 19  ? 0.2582 0.1663 0.2077 -0.0589 0.0276  -0.0508 19  LYS   B CA  
4833 C C   . LYS   B 19  ? 0.2311 0.1673 0.2227 -0.0440 0.0365  -0.0642 19  LYS   B C   
4834 O O   . LYS   B 19  ? 0.2072 0.1763 0.2229 -0.0340 0.0344  -0.0549 19  LYS   B O   
4835 C CB  . LYS   B 19  ? 0.2880 0.1891 0.2157 -0.0669 0.0468  -0.0442 19  LYS   B CB  
4836 C CG  . LYS   B 19  ? 0.3218 0.2162 0.2543 -0.0723 0.0650  -0.0468 19  LYS   B CG  
4837 C CD  . LYS   B 19  ? 0.3527 0.2436 0.2588 -0.0715 0.0806  -0.0525 19  LYS   B CD  
4838 C CE  . LYS   B 19  ? 0.3792 0.2669 0.2753 -0.0785 0.0651  -0.0572 19  LYS   B CE  
4839 N NZ  . LYS   B 19  ? 0.3970 0.2807 0.2834 -0.0848 0.0663  -0.0381 19  LYS   B NZ  
4853 N N   . ASN   B 20  ? 0.2272 0.1874 0.2661 -0.0495 0.0514  -0.0807 20  ASN   B N   
4854 C CA  . ASN   B 20  ? 0.2166 0.2061 0.3008 -0.0444 0.0580  -0.1029 20  ASN   B CA  
4855 C C   . ASN   B 20  ? 0.2163 0.2266 0.3056 -0.0461 0.0774  -0.1081 20  ASN   B C   
4856 O O   . ASN   B 20  ? 0.2399 0.2651 0.3206 -0.0571 0.0749  -0.1070 20  ASN   B O   
4857 C CB  . ASN   B 20  ? 0.2433 0.2173 0.3455 -0.0120 0.0398  -0.1037 20  ASN   B CB  
4858 C CG  . ASN   B 20  ? 0.2692 0.2229 0.3629 0.0223  0.0374  -0.1106 20  ASN   B CG  
4859 O OD1 . ASN   B 20  ? 0.2978 0.2559 0.3794 0.0399  0.0393  -0.1148 20  ASN   B OD1 
4860 N ND2 . ASN   B 20  ? 0.2600 0.2209 0.3564 0.0266  0.0236  -0.0944 20  ASN   B ND2 
4867 N N   . ALA   B 21  ? 0.2181 0.2111 0.3020 -0.0448 0.0824  -0.0972 21  ALA   B N   
4868 C CA  . ALA   B 21  ? 0.2244 0.2121 0.3152 -0.0533 0.0633  -0.0747 21  ALA   B CA  
4869 C C   . ALA   B 21  ? 0.2182 0.1869 0.2804 -0.0446 0.0646  -0.0520 21  ALA   B C   
4870 O O   . ALA   B 21  ? 0.2300 0.1807 0.2480 -0.0454 0.0559  -0.0436 21  ALA   B O   
4871 C CB  . ALA   B 21  ? 0.2407 0.2430 0.3404 -0.0705 0.0571  -0.0495 21  ALA   B CB  
4877 N N   . ASP   B 22  ? 0.2058 0.1673 0.2813 -0.0374 0.0554  -0.0462 22  ASP   B N   
4878 C CA  . ASP   B 22  ? 0.1940 0.1528 0.2634 -0.0206 0.0396  -0.0262 22  ASP   B CA  
4879 C C   . ASP   B 22  ? 0.1897 0.1523 0.1978 -0.0289 0.0291  -0.0100 22  ASP   B C   
4880 O O   . ASP   B 22  ? 0.1992 0.1575 0.2159 -0.0180 0.0224  -0.0126 22  ASP   B O   
4881 C CB  . ASP   B 22  ? 0.2000 0.1582 0.2939 -0.0060 0.0349  -0.0153 22  ASP   B CB  
4882 C CG  . ASP   B 22  ? 0.1968 0.1827 0.3304 0.0020  0.0230  -0.0126 22  ASP   B CG  
4883 O OD1 . ASP   B 22  ? 0.2113 0.1763 0.3224 0.0006  -0.0125 -0.0101 22  ASP   B OD1 
4884 O OD2 . ASP   B 22  ? 0.2067 0.2142 0.4092 0.0019  -0.0009 -0.0286 22  ASP   B OD2 
4889 N N   . ILE   B 23  ? 0.1948 0.1497 0.1684 -0.0191 0.0024  0.0111  23  ILE   B N   
4890 C CA  . ILE   B 23  ? 0.1873 0.1425 0.1642 -0.0222 0.0069  0.0034  23  ILE   B CA  
4891 C C   . ILE   B 23  ? 0.1822 0.1525 0.1510 -0.0068 -0.0011 0.0018  23  ILE   B C   
4892 O O   . ILE   B 23  ? 0.1637 0.1477 0.1507 -0.0126 -0.0026 0.0036  23  ILE   B O   
4893 C CB  . ILE   B 23  ? 0.1793 0.1521 0.1814 -0.0279 -0.0024 0.0140  23  ILE   B CB  
4894 C CG1 . ILE   B 23  ? 0.1833 0.1588 0.1757 -0.0151 0.0045  0.0238  23  ILE   B CG1 
4895 C CG2 . ILE   B 23  ? 0.1867 0.1844 0.1739 -0.0140 -0.0093 0.0123  23  ILE   B CG2 
4896 C CD1 . ILE   B 23  ? 0.1912 0.1762 0.1901 -0.0149 0.0024  0.0305  23  ILE   B CD1 
4908 N N   . VAL   B 24  ? 0.1779 0.1492 0.1659 -0.0140 -0.0042 0.0060  24  VAL   B N   
4909 C CA  . VAL   B 24  ? 0.1805 0.1532 0.1897 -0.0090 -0.0254 0.0027  24  VAL   B CA  
4910 C C   . VAL   B 24  ? 0.1733 0.1593 0.1872 -0.0144 -0.0115 -0.0036 24  VAL   B C   
4911 O O   . VAL   B 24  ? 0.1688 0.1711 0.1974 -0.0162 -0.0019 0.0101  24  VAL   B O   
4912 C CB  . VAL   B 24  ? 0.1813 0.1768 0.1815 -0.0047 -0.0192 -0.0007 24  VAL   B CB  
4913 C CG1 . VAL   B 24  ? 0.1781 0.1838 0.2230 -0.0205 -0.0299 -0.0111 24  VAL   B CG1 
4914 C CG2 . VAL   B 24  ? 0.1886 0.2123 0.1722 0.0045  -0.0191 -0.0042 24  VAL   B CG2 
4924 N N   A GLU   B 25  ? 0.1954 0.1748 0.2057 -0.0078 0.0012  0.0001  25  GLU   B N   
4925 N N   B GLU   B 25  ? 0.1929 0.1736 0.1970 -0.0056 0.0067  -0.0091 25  GLU   B N   
4926 C CA  A GLU   B 25  ? 0.2085 0.1977 0.2150 -0.0109 0.0124  -0.0044 25  GLU   B CA  
4927 C CA  B GLU   B 25  ? 0.2003 0.1992 0.1916 -0.0125 0.0224  -0.0245 25  GLU   B CA  
4928 C C   A GLU   B 25  ? 0.2048 0.1888 0.1844 -0.0195 0.0137  -0.0006 25  GLU   B C   
4929 C C   B GLU   B 25  ? 0.1987 0.1909 0.1663 -0.0209 0.0168  -0.0133 25  GLU   B C   
4930 O O   A GLU   B 25  ? 0.2089 0.1982 0.1999 -0.0192 0.0180  0.0041  25  GLU   B O   
4931 O O   B GLU   B 25  ? 0.1989 0.2007 0.1854 -0.0232 0.0215  -0.0167 25  GLU   B O   
4932 C CB  A GLU   B 25  ? 0.2408 0.2390 0.2793 0.0027  0.0203  -0.0041 25  GLU   B CB  
4933 C CB  B GLU   B 25  ? 0.2328 0.2529 0.2508 0.0009  0.0409  -0.0312 25  GLU   B CB  
4934 C CG  A GLU   B 25  ? 0.2725 0.2881 0.3699 0.0084  0.0136  -0.0061 25  GLU   B CG  
4935 C CG  B GLU   B 25  ? 0.2657 0.3256 0.3627 0.0048  0.0321  -0.0304 25  GLU   B CG  
4936 C CD  A GLU   B 25  ? 0.2996 0.3301 0.4402 0.0068  0.0070  -0.0082 25  GLU   B CD  
4937 C CD  B GLU   B 25  ? 0.2952 0.3814 0.4443 0.0036  0.0255  -0.0340 25  GLU   B CD  
4938 O OE1 A GLU   B 25  ? 0.3125 0.3414 0.4658 0.0087  0.0102  -0.0077 25  GLU   B OE1 
4939 O OE1 B GLU   B 25  ? 0.3077 0.3944 0.4671 0.0092  0.0319  -0.0386 25  GLU   B OE1 
4940 O OE2 A GLU   B 25  ? 0.3087 0.3405 0.4641 0.0055  0.0010  -0.0138 25  GLU   B OE2 
4941 O OE2 B GLU   B 25  ? 0.3070 0.3981 0.4724 0.0035  0.0180  -0.0361 25  GLU   B OE2 
4954 N N   . GLU   B 26  ? 0.1972 0.1683 0.1622 -0.0333 0.0167  -0.0104 26  GLU   B N   
4955 C CA  . GLU   B 26  ? 0.1998 0.1818 0.1643 -0.0477 0.0065  -0.0021 26  GLU   B CA  
4956 C C   . GLU   B 26  ? 0.1772 0.1729 0.1475 -0.0302 0.0127  0.0129  26  GLU   B C   
4957 O O   . GLU   B 26  ? 0.2080 0.2061 0.1614 -0.0270 0.0075  0.0217  26  GLU   B O   
4958 C CB  . GLU   B 26  ? 0.2387 0.2043 0.1677 -0.0522 0.0166  0.0142  26  GLU   B CB  
4959 C CG  . GLU   B 26  ? 0.2900 0.2474 0.2501 -0.0577 0.0251  -0.0263 26  GLU   B CG  
4960 C CD  . GLU   B 26  ? 0.3185 0.2654 0.2567 -0.0904 0.0268  -0.0667 26  GLU   B CD  
4961 O OE1 . GLU   B 26  ? 0.3385 0.2379 0.2651 -0.0987 0.1054  -0.0522 26  GLU   B OE1 
4962 O OE2 . GLU   B 26  ? 0.3274 0.3183 0.3182 -0.0825 0.0285  -0.0553 26  GLU   B OE2 
4970 N N   . ALA   B 27  ? 0.1665 0.1545 0.1573 -0.0271 0.0072  0.0115  27  ALA   B N   
4971 C CA  . ALA   B 27  ? 0.1670 0.1581 0.1713 -0.0181 0.0026  0.0232  27  ALA   B CA  
4972 C C   . ALA   B 27  ? 0.1664 0.1651 0.1790 -0.0112 0.0040  0.0306  27  ALA   B C   
4973 O O   . ALA   B 27  ? 0.1633 0.1828 0.2012 -0.0073 -0.0006 0.0422  27  ALA   B O   
4974 C CB  . ALA   B 27  ? 0.1860 0.1522 0.1737 -0.0247 0.0006  0.0197  27  ALA   B CB  
4980 N N   . LYS   B 28  ? 0.1643 0.1746 0.2132 -0.0131 0.0092  0.0417  28  LYS   B N   
4981 C CA  . LYS   B 28  ? 0.1805 0.2079 0.2338 -0.0080 0.0414  0.0670  28  LYS   B CA  
4982 C C   . LYS   B 28  ? 0.2049 0.2163 0.2131 -0.0009 0.0407  0.0519  28  LYS   B C   
4983 O O   . LYS   B 28  ? 0.2248 0.2260 0.2335 -0.0079 0.0565  0.0491  28  LYS   B O   
4984 C CB  . LYS   B 28  ? 0.2059 0.2535 0.2931 -0.0004 0.0697  0.0966  28  LYS   B CB  
4985 C CG  . LYS   B 28  ? 0.2350 0.3094 0.3543 0.0059  0.0764  0.1229  28  LYS   B CG  
4986 C CD  . LYS   B 28  ? 0.2928 0.3839 0.4370 0.0094  0.0986  0.1406  28  LYS   B CD  
4987 C CE  . LYS   B 28  ? 0.3355 0.4353 0.5082 0.0221  0.0980  0.1497  28  LYS   B CE  
4988 N NZ  . LYS   B 28  ? 0.3805 0.4571 0.5406 0.0326  0.0943  0.1608  28  LYS   B NZ  
5002 N N   A LYS   B 29  ? 0.2200 0.2339 0.2128 -0.0001 0.0332  0.0399  29  LYS   B N   
5003 N N   B LYS   B 29  ? 0.2223 0.2283 0.2011 0.0110  0.0404  0.0336  29  LYS   B N   
5004 C CA  A LYS   B 29  ? 0.2505 0.2566 0.2395 -0.0042 0.0182  0.0300  29  LYS   B CA  
5005 C CA  B LYS   B 29  ? 0.2608 0.2465 0.2231 0.0154  0.0313  0.0224  29  LYS   B CA  
5006 C C   A LYS   B 29  ? 0.2409 0.2439 0.1928 -0.0101 0.0108  0.0293  29  LYS   B C   
5007 C C   B LYS   B 29  ? 0.2542 0.2303 0.1703 0.0136  0.0364  0.0226  29  LYS   B C   
5008 O O   A LYS   B 29  ? 0.2450 0.2542 0.2093 -0.0176 0.0007  0.0321  29  LYS   B O   
5009 O O   B LYS   B 29  ? 0.2713 0.2265 0.1681 0.0270  0.0473  0.0113  29  LYS   B O   
5010 C CB  A LYS   B 29  ? 0.2906 0.2908 0.3196 -0.0015 0.0110  0.0189  29  LYS   B CB  
5011 C CB  B LYS   B 29  ? 0.3074 0.2807 0.3082 0.0179  0.0174  0.0102  29  LYS   B CB  
5012 C CG  A LYS   B 29  ? 0.3224 0.3195 0.4032 -0.0033 0.0121  0.0145  29  LYS   B CG  
5013 C CG  B LYS   B 29  ? 0.3434 0.3126 0.4032 0.0145  0.0141  0.0071  29  LYS   B CG  
5014 C CD  A LYS   B 29  ? 0.3479 0.3396 0.4687 -0.0071 0.0191  0.0099  29  LYS   B CD  
5015 C CD  B LYS   B 29  ? 0.3746 0.3368 0.4785 0.0080  0.0186  0.0001  29  LYS   B CD  
5016 C CE  A LYS   B 29  ? 0.3675 0.3547 0.5103 -0.0109 0.0287  0.0067  29  LYS   B CE  
5017 C CE  B LYS   B 29  ? 0.4017 0.3545 0.5255 0.0021  0.0263  -0.0046 29  LYS   B CE  
5018 N NZ  A LYS   B 29  ? 0.3745 0.3615 0.5349 -0.0126 0.0329  0.0036  29  LYS   B NZ  
5019 N NZ  B LYS   B 29  ? 0.4061 0.3618 0.5504 -0.0021 0.0303  -0.0085 29  LYS   B NZ  
5046 N N   . VAL   B 30  ? 0.2230 0.2236 0.1707 -0.0108 0.0166  0.0202  30  VAL   B N   
5047 C CA  . VAL   B 30  ? 0.2095 0.2137 0.1945 -0.0224 -0.0150 0.0220  30  VAL   B CA  
5048 C C   . VAL   B 30  ? 0.1875 0.2029 0.1730 -0.0218 -0.0138 0.0232  30  VAL   B C   
5049 O O   . VAL   B 30  ? 0.1953 0.2199 0.1780 -0.0299 -0.0248 0.0415  30  VAL   B O   
5050 C CB  . VAL   B 30  ? 0.2253 0.2194 0.3087 -0.0482 -0.0339 0.0522  30  VAL   B CB  
5051 C CG1 . VAL   B 30  ? 0.2530 0.2426 0.3320 -0.0404 -0.0111 0.0406  30  VAL   B CG1 
5052 C CG2 . VAL   B 30  ? 0.2335 0.2155 0.3468 -0.0593 -0.0500 0.0332  30  VAL   B CG2 
5063 N N   A LYS   B 31  ? 0.1873 0.1895 0.1934 -0.0267 -0.0101 0.0259  31  LYS   B N   
5064 N N   B LYS   B 31  ? 0.1810 0.1739 0.1909 -0.0324 -0.0068 0.0264  31  LYS   B N   
5065 C CA  A LYS   B 31  ? 0.1841 0.1939 0.2085 -0.0239 -0.0177 0.0369  31  LYS   B CA  
5066 C CA  B LYS   B 31  ? 0.1708 0.1757 0.2040 -0.0279 -0.0180 0.0412  31  LYS   B CA  
5067 C C   A LYS   B 31  ? 0.1760 0.1700 0.1789 -0.0229 -0.0245 0.0324  31  LYS   B C   
5068 C C   B LYS   B 31  ? 0.1670 0.1566 0.1834 -0.0206 -0.0283 0.0456  31  LYS   B C   
5069 O O   A LYS   B 31  ? 0.1731 0.1795 0.1746 -0.0248 -0.0224 0.0220  31  LYS   B O   
5070 O O   B LYS   B 31  ? 0.1626 0.1708 0.1933 -0.0184 -0.0296 0.0549  31  LYS   B O   
5071 C CB  A LYS   B 31  ? 0.1920 0.2294 0.2514 -0.0219 0.0066  0.0473  31  LYS   B CB  
5072 C CB  B LYS   B 31  ? 0.1677 0.2118 0.2381 -0.0296 0.0190  0.0424  31  LYS   B CB  
5073 C CG  A LYS   B 31  ? 0.2110 0.2639 0.2923 -0.0220 0.0178  0.0545  31  LYS   B CG  
5074 C CG  B LYS   B 31  ? 0.1865 0.2555 0.2787 -0.0323 0.0306  0.0403  31  LYS   B CG  
5075 C CD  A LYS   B 31  ? 0.2333 0.3026 0.3438 -0.0189 0.0207  0.0584  31  LYS   B CD  
5076 C CD  B LYS   B 31  ? 0.2127 0.3065 0.3400 -0.0316 0.0260  0.0398  31  LYS   B CD  
5077 C CE  A LYS   B 31  ? 0.2503 0.3299 0.3925 -0.0152 0.0155  0.0572  31  LYS   B CE  
5078 C CE  B LYS   B 31  ? 0.2294 0.3334 0.4076 -0.0288 0.0133  0.0363  31  LYS   B CE  
5079 N NZ  A LYS   B 31  ? 0.2658 0.3385 0.4075 -0.0066 0.0094  0.0524  31  LYS   B NZ  
5080 N NZ  B LYS   B 31  ? 0.2498 0.3450 0.4264 -0.0169 -0.0011 0.0288  31  LYS   B NZ  
5107 N N   . PRO   B 32  ? 0.1769 0.1532 0.1590 -0.0300 -0.0319 0.0389  32  PRO   B N   
5108 C CA  . PRO   B 32  ? 0.1868 0.1558 0.1317 -0.0391 -0.0323 0.0165  32  PRO   B CA  
5109 C C   . PRO   B 32  ? 0.1907 0.1510 0.1395 -0.0367 -0.0504 0.0215  32  PRO   B C   
5110 O O   . PRO   B 32  ? 0.1950 0.1481 0.1712 -0.0338 -0.0529 0.0228  32  PRO   B O   
5111 C CB  . PRO   B 32  ? 0.2008 0.1500 0.1481 -0.0443 -0.0227 0.0010  32  PRO   B CB  
5112 C CG  . PRO   B 32  ? 0.2150 0.1394 0.1422 -0.0270 -0.0462 0.0039  32  PRO   B CG  
5113 C CD  . PRO   B 32  ? 0.1992 0.1508 0.1706 -0.0195 -0.0414 0.0174  32  PRO   B CD  
5121 N N   . THR   B 33  ? 0.1953 0.1358 0.1391 -0.0328 -0.0395 0.0126  33  THR   B N   
5122 C CA  . THR   B 33  ? 0.2020 0.1414 0.1347 -0.0307 -0.0320 0.0238  33  THR   B CA  
5123 C C   . THR   B 33  ? 0.2000 0.1336 0.1201 -0.0347 -0.0341 0.0073  33  THR   B C   
5124 O O   . THR   B 33  ? 0.2225 0.1392 0.1401 -0.0439 -0.0398 0.0085  33  THR   B O   
5125 C CB  . THR   B 33  ? 0.2160 0.1527 0.1282 -0.0197 -0.0361 0.0257  33  THR   B CB  
5126 O OG1 . THR   B 33  ? 0.2016 0.1587 0.1523 -0.0191 -0.0402 0.0216  33  THR   B OG1 
5127 C CG2 . THR   B 33  ? 0.2378 0.1577 0.1642 -0.0109 -0.0274 0.0115  33  THR   B CG2 
5135 N N   . VAL   B 34  ? 0.1814 0.1302 0.1225 -0.0330 -0.0330 0.0034  34  VAL   B N   
5136 C CA  . VAL   B 34  ? 0.1771 0.1382 0.1185 -0.0312 -0.0256 0.0023  34  VAL   B CA  
5137 C C   . VAL   B 34  ? 0.1657 0.1281 0.1161 -0.0323 -0.0219 0.0081  34  VAL   B C   
5138 O O   . VAL   B 34  ? 0.1821 0.1356 0.1183 -0.0277 -0.0279 0.0038  34  VAL   B O   
5139 C CB  . VAL   B 34  ? 0.1924 0.1559 0.1382 -0.0102 -0.0245 0.0057  34  VAL   B CB  
5140 C CG1 . VAL   B 34  ? 0.1915 0.1696 0.1456 -0.0147 -0.0139 0.0019  34  VAL   B CG1 
5141 C CG2 . VAL   B 34  ? 0.1891 0.1618 0.1664 -0.0110 -0.0239 0.0100  34  VAL   B CG2 
5151 N N   . VAL   B 35  ? 0.1624 0.1300 0.0973 -0.0299 -0.0161 0.0102  35  VAL   B N   
5152 C CA  . VAL   B 35  ? 0.1516 0.1319 0.0976 -0.0294 -0.0121 0.0109  35  VAL   B CA  
5153 C C   . VAL   B 35  ? 0.1422 0.1220 0.1208 -0.0197 -0.0214 -0.0010 35  VAL   B C   
5154 O O   . VAL   B 35  ? 0.1495 0.1264 0.1143 -0.0241 -0.0036 -0.0065 35  VAL   B O   
5155 C CB  . VAL   B 35  ? 0.1529 0.1521 0.1177 -0.0253 0.0047  0.0020  35  VAL   B CB  
5156 C CG1 . VAL   B 35  ? 0.1470 0.1695 0.1343 -0.0288 -0.0040 -0.0039 35  VAL   B CG1 
5157 C CG2 . VAL   B 35  ? 0.1528 0.1543 0.1330 -0.0201 -0.0038 0.0036  35  VAL   B CG2 
5167 N N   . VAL   B 36  ? 0.1405 0.1291 0.1069 -0.0204 -0.0149 0.0083  36  VAL   B N   
5168 C CA  . VAL   B 36  ? 0.1347 0.1287 0.1135 -0.0193 -0.0091 -0.0015 36  VAL   B CA  
5169 C C   . VAL   B 36  ? 0.1341 0.1347 0.1055 -0.0082 -0.0107 0.0101  36  VAL   B C   
5170 O O   . VAL   B 36  ? 0.1463 0.1354 0.1228 -0.0128 -0.0072 -0.0041 36  VAL   B O   
5171 C CB  . VAL   B 36  ? 0.1370 0.1324 0.1143 -0.0202 -0.0028 -0.0004 36  VAL   B CB  
5172 C CG1 . VAL   B 36  ? 0.1349 0.1474 0.1388 -0.0065 -0.0036 0.0070  36  VAL   B CG1 
5173 C CG2 . VAL   B 36  ? 0.1436 0.1444 0.1357 -0.0203 -0.0145 0.0028  36  VAL   B CG2 
5183 N N   . ASN   B 37  ? 0.1403 0.1324 0.1053 -0.0059 -0.0181 0.0074  37  ASN   B N   
5184 C CA  . ASN   B 37  ? 0.1468 0.1296 0.1146 -0.0066 -0.0165 0.0045  37  ASN   B CA  
5185 C C   . ASN   B 37  ? 0.1460 0.1314 0.1221 -0.0013 -0.0088 0.0083  37  ASN   B C   
5186 O O   . ASN   B 37  ? 0.1472 0.1379 0.1226 0.0023  -0.0019 0.0086  37  ASN   B O   
5187 C CB  . ASN   B 37  ? 0.1475 0.1283 0.1146 -0.0002 -0.0200 0.0096  37  ASN   B CB  
5188 C CG  . ASN   B 37  ? 0.1482 0.1366 0.1207 0.0003  -0.0039 -0.0033 37  ASN   B CG  
5189 O OD1 . ASN   B 37  ? 0.1588 0.1425 0.1341 0.0108  -0.0145 -0.0051 37  ASN   B OD1 
5190 N ND2 . ASN   B 37  ? 0.1557 0.1308 0.1243 0.0063  -0.0187 -0.0014 37  ASN   B ND2 
5197 N N   . ALA   B 38  ? 0.1681 0.1291 0.1072 0.0125  0.0044  0.0050  38  ALA   B N   
5198 C CA  . ALA   B 38  ? 0.1778 0.1379 0.1106 -0.0006 0.0090  0.0049  38  ALA   B CA  
5199 C C   . ALA   B 38  ? 0.1684 0.1342 0.1018 0.0025  0.0052  0.0105  38  ALA   B C   
5200 O O   . ALA   B 38  ? 0.1826 0.1471 0.1268 0.0089  -0.0046 0.0104  38  ALA   B O   
5201 C CB  . ALA   B 38  ? 0.1958 0.1437 0.1287 -0.0062 0.0175  0.0011  38  ALA   B CB  
5207 N N   . ALA   B 39  ? 0.1651 0.1363 0.1039 0.0135  -0.0000 0.0050  39  ALA   B N   
5208 C CA  . ALA   B 39  ? 0.1737 0.1415 0.1158 0.0162  -0.0125 -0.0025 39  ALA   B CA  
5209 C C   . ALA   B 39  ? 0.1783 0.1539 0.0775 0.0145  -0.0123 0.0047  39  ALA   B C   
5210 O O   . ALA   B 39  ? 0.1884 0.1593 0.1203 -0.0008 -0.0166 0.0038  39  ALA   B O   
5211 C CB  . ALA   B 39  ? 0.1585 0.1402 0.1354 0.0047  -0.0124 0.0080  39  ALA   B CB  
5217 N N   . ASN   B 40  ? 0.1761 0.1768 0.0917 0.0053  -0.0004 -0.0020 40  ASN   B N   
5218 C CA  . ASN   B 40  ? 0.1843 0.1775 0.1067 0.0133  -0.0098 -0.0073 40  ASN   B CA  
5219 C C   . ASN   B 40  ? 0.1928 0.1759 0.0928 0.0246  -0.0084 0.0011  40  ASN   B C   
5220 O O   . ASN   B 40  ? 0.1846 0.1670 0.1067 0.0242  -0.0057 -0.0038 40  ASN   B O   
5221 C CB  . ASN   B 40  ? 0.1940 0.1778 0.1243 0.0280  -0.0156 0.0077  40  ASN   B CB  
5222 C CG  . ASN   B 40  ? 0.2037 0.1836 0.1527 0.0225  -0.0246 0.0122  40  ASN   B CG  
5223 O OD1 . ASN   B 40  ? 0.2061 0.1715 0.2593 0.0163  -0.0421 0.0204  40  ASN   B OD1 
5224 N ND2 . ASN   B 40  ? 0.2062 0.1886 0.1739 0.0183  -0.0177 0.0122  40  ASN   B ND2 
5231 N N   . VAL   B 41  ? 0.2053 0.1756 0.1056 0.0328  0.0073  -0.0020 41  VAL   B N   
5232 C CA  . VAL   B 41  ? 0.2041 0.1828 0.1093 0.0246  0.0004  -0.0086 41  VAL   B CA  
5233 C C   . VAL   B 41  ? 0.1966 0.1849 0.1071 0.0327  -0.0119 -0.0047 41  VAL   B C   
5234 O O   . VAL   B 41  ? 0.1906 0.1886 0.1216 0.0265  -0.0081 -0.0058 41  VAL   B O   
5235 C CB  . VAL   B 41  ? 0.2266 0.2031 0.1447 0.0062  0.0227  -0.0147 41  VAL   B CB  
5236 C CG1 . VAL   B 41  ? 0.2277 0.2048 0.1525 -0.0132 0.0329  -0.0259 41  VAL   B CG1 
5237 C CG2 . VAL   B 41  ? 0.2321 0.2209 0.1356 -0.0050 0.0307  -0.0194 41  VAL   B CG2 
5247 N N   A TYR   B 42  ? 0.2020 0.1865 0.1163 0.0349  -0.0171 -0.0070 42  TYR   B N   
5248 N N   B TYR   B 42  ? 0.2052 0.1822 0.1096 0.0311  -0.0238 -0.0104 42  TYR   B N   
5249 C CA  A TYR   B 42  ? 0.2024 0.1876 0.1207 0.0388  -0.0243 -0.0134 42  TYR   B CA  
5250 C CA  B TYR   B 42  ? 0.2067 0.1793 0.1052 0.0331  -0.0365 -0.0199 42  TYR   B CA  
5251 C C   A TYR   B 42  ? 0.1917 0.1814 0.1158 0.0331  -0.0233 -0.0127 42  TYR   B C   
5252 C C   B TYR   B 42  ? 0.1938 0.1776 0.1123 0.0303  -0.0296 -0.0131 42  TYR   B C   
5253 O O   A TYR   B 42  ? 0.1922 0.1881 0.1396 0.0349  -0.0307 -0.0193 42  TYR   B O   
5254 O O   B TYR   B 42  ? 0.1952 0.1833 0.1483 0.0314  -0.0420 -0.0170 42  TYR   B O   
5255 C CB  A TYR   B 42  ? 0.2099 0.2060 0.1463 0.0329  -0.0230 0.0001  42  TYR   B CB  
5256 C CB  B TYR   B 42  ? 0.2150 0.1944 0.1264 0.0178  -0.0427 -0.0046 42  TYR   B CB  
5257 C CG  A TYR   B 42  ? 0.1966 0.2139 0.1473 0.0259  -0.0104 0.0115  42  TYR   B CG  
5258 C CG  B TYR   B 42  ? 0.1933 0.1921 0.1065 -0.0039 -0.0452 -0.0005 42  TYR   B CG  
5259 C CD1 A TYR   B 42  ? 0.1830 0.2142 0.1260 0.0191  0.0037  0.0204  42  TYR   B CD1 
5260 C CD1 B TYR   B 42  ? 0.1761 0.1864 0.0935 -0.0235 -0.0262 0.0040  42  TYR   B CD1 
5261 C CD2 A TYR   B 42  ? 0.1964 0.2130 0.1846 0.0295  -0.0058 0.0164  42  TYR   B CD2 
5262 C CD2 B TYR   B 42  ? 0.1914 0.1775 0.1420 -0.0049 -0.0401 -0.0071 42  TYR   B CD2 
5263 C CE1 A TYR   B 42  ? 0.1856 0.2171 0.1342 0.0172  0.0022  0.0184  42  TYR   B CE1 
5264 C CE1 B TYR   B 42  ? 0.1733 0.1795 0.0799 -0.0329 -0.0207 -0.0004 42  TYR   B CE1 
5265 C CE2 A TYR   B 42  ? 0.1947 0.2195 0.1780 0.0186  0.0149  0.0227  42  TYR   B CE2 
5266 C CE2 B TYR   B 42  ? 0.1846 0.1803 0.1155 -0.0175 -0.0143 0.0073  42  TYR   B CE2 
5267 C CZ  A TYR   B 42  ? 0.1957 0.2243 0.1597 0.0199  0.0212  0.0160  42  TYR   B CZ  
5268 C CZ  B TYR   B 42  ? 0.1748 0.1794 0.0959 -0.0228 -0.0132 -0.0010 42  TYR   B CZ  
5269 O OH  A TYR   B 42  ? 0.2197 0.2420 0.1738 0.0216  0.0432  0.0182  42  TYR   B OH  
5270 O OH  B TYR   B 42  ? 0.1788 0.1736 0.1291 -0.0288 -0.0138 -0.0060 42  TYR   B OH  
5289 N N   . LEU   B 43  ? 0.1856 0.1668 0.1020 0.0229  -0.0218 -0.0126 43  LEU   B N   
5290 C CA  . LEU   B 43  ? 0.1773 0.1608 0.1099 0.0139  -0.0205 -0.0091 43  LEU   B CA  
5291 C C   . LEU   B 43  ? 0.1815 0.1633 0.1165 0.0153  -0.0185 -0.0075 43  LEU   B C   
5292 O O   . LEU   B 43  ? 0.1792 0.1660 0.1545 0.0198  -0.0272 -0.0026 43  LEU   B O   
5293 C CB  . LEU   B 43  ? 0.1758 0.1513 0.1306 0.0096  -0.0200 -0.0114 43  LEU   B CB  
5294 C CG  . LEU   B 43  ? 0.1789 0.1496 0.1463 0.0046  -0.0313 -0.0165 43  LEU   B CG  
5295 C CD1 . LEU   B 43  ? 0.1863 0.1575 0.1866 -0.0049 -0.0517 -0.0212 43  LEU   B CD1 
5296 C CD2 . LEU   B 43  ? 0.1858 0.1526 0.1592 0.0003  -0.0270 -0.0138 43  LEU   B CD2 
5309 N N   . LYS   B 44  ? 0.1793 0.1620 0.1216 0.0194  -0.0138 -0.0090 44  LYS   B N   
5310 C CA  . LYS   B 44  ? 0.1986 0.1729 0.1120 0.0216  -0.0162 -0.0150 44  LYS   B CA  
5311 C C   . LYS   B 44  ? 0.1951 0.1665 0.1088 0.0264  -0.0181 -0.0100 44  LYS   B C   
5312 O O   . LYS   B 44  ? 0.2139 0.1621 0.1418 0.0189  -0.0087 -0.0080 44  LYS   B O   
5313 C CB  . LYS   B 44  ? 0.2195 0.1884 0.1285 0.0377  -0.0259 -0.0147 44  LYS   B CB  
5314 C CG  . LYS   B 44  ? 0.2548 0.2160 0.1582 0.0232  -0.0487 -0.0056 44  LYS   B CG  
5315 C CD  . LYS   B 44  ? 0.2925 0.2425 0.2544 -0.0052 -0.0692 -0.0102 44  LYS   B CD  
5316 C CE  . LYS   B 44  ? 0.3287 0.2740 0.3471 -0.0101 -0.0792 -0.0056 44  LYS   B CE  
5317 N NZ  . LYS   B 44  ? 0.3325 0.2817 0.3768 -0.0079 -0.0952 0.0082  44  LYS   B NZ  
5331 N N   . HIS   B 45  ? 0.1839 0.1750 0.0990 0.0150  -0.0180 0.0054  45  HIS   B N   
5332 C CA  . HIS   B 45  ? 0.1878 0.1701 0.1127 0.0151  -0.0141 -0.0143 45  HIS   B CA  
5333 C C   . HIS   B 45  ? 0.1985 0.1841 0.1627 0.0305  -0.0266 -0.0121 45  HIS   B C   
5334 O O   . HIS   B 45  ? 0.2177 0.2138 0.2248 0.0574  0.0111  -0.0067 45  HIS   B O   
5335 C CB  . HIS   B 45  ? 0.1750 0.1756 0.1170 0.0176  -0.0099 -0.0137 45  HIS   B CB  
5336 C CG  . HIS   B 45  ? 0.1707 0.1620 0.1245 0.0075  -0.0112 0.0024  45  HIS   B CG  
5337 N ND1 . HIS   B 45  ? 0.1797 0.1511 0.1349 0.0098  -0.0205 -0.0067 45  HIS   B ND1 
5338 C CD2 . HIS   B 45  ? 0.1903 0.1638 0.1342 -0.0089 -0.0143 0.0014  45  HIS   B CD2 
5339 C CE1 . HIS   B 45  ? 0.1992 0.1379 0.1313 0.0058  -0.0321 -0.0084 45  HIS   B CE1 
5340 N NE2 . HIS   B 45  ? 0.2047 0.1523 0.1192 0.0045  -0.0232 -0.0087 45  HIS   B NE2 
5348 N N   A GLY   B 46  ? 0.2091 0.1852 0.2017 0.0305  -0.0411 -0.0042 46  GLY   B N   
5349 N N   B GLY   B 46  ? 0.2085 0.1811 0.1924 0.0341  -0.0468 0.0058  46  GLY   B N   
5350 C CA  A GLY   B 46  ? 0.2252 0.1931 0.2480 0.0206  -0.0466 -0.0001 46  GLY   B CA  
5351 C CA  B GLY   B 46  ? 0.2287 0.1913 0.2320 0.0243  -0.0570 0.0158  46  GLY   B CA  
5352 C C   A GLY   B 46  ? 0.2341 0.2066 0.2969 0.0242  -0.0393 -0.0005 46  GLY   B C   
5353 C C   B GLY   B 46  ? 0.2405 0.2103 0.2851 0.0305  -0.0460 0.0182  46  GLY   B C   
5354 O O   A GLY   B 46  ? 0.2401 0.2192 0.3753 0.0266  -0.0179 -0.0267 46  GLY   B O   
5355 O O   B GLY   B 46  ? 0.2548 0.2310 0.3624 0.0311  -0.0148 0.0022  46  GLY   B O   
5362 N N   . GLY   B 47  ? 0.2375 0.2132 0.2751 0.0078  -0.0310 0.0003  47  GLY   B N   
5363 C CA  . GLY   B 47  ? 0.2145 0.1831 0.2203 -0.0028 -0.0311 -0.0083 47  GLY   B CA  
5364 C C   . GLY   B 47  ? 0.1950 0.1696 0.1885 0.0007  -0.0139 0.0000  47  GLY   B C   
5365 O O   . GLY   B 47  ? 0.2015 0.1559 0.1978 0.0068  -0.0214 0.0087  47  GLY   B O   
5370 N N   . GLY   B 48  ? 0.1784 0.1557 0.1935 0.0055  -0.0241 0.0089  48  GLY   B N   
5371 C CA  . GLY   B 48  ? 0.1728 0.1564 0.2002 -0.0009 -0.0102 0.0060  48  GLY   B CA  
5372 C C   . GLY   B 48  ? 0.1616 0.1543 0.1736 0.0033  -0.0045 -0.0059 48  GLY   B C   
5373 O O   . GLY   B 48  ? 0.1557 0.1545 0.2005 0.0056  -0.0176 0.0064  48  GLY   B O   
5377 N N   . VAL   B 49  ? 0.1583 0.1542 0.1715 0.0101  0.0023  0.0043  49  VAL   B N   
5378 C CA  . VAL   B 49  ? 0.1638 0.1672 0.1493 0.0192  -0.0111 -0.0209 49  VAL   B CA  
5379 C C   . VAL   B 49  ? 0.1567 0.1565 0.1337 0.0186  -0.0064 -0.0089 49  VAL   B C   
5380 O O   . VAL   B 49  ? 0.1683 0.1581 0.1438 0.0120  -0.0101 -0.0032 49  VAL   B O   
5381 C CB  . VAL   B 49  ? 0.1706 0.1857 0.1641 0.0042  -0.0203 -0.0211 49  VAL   B CB  
5382 C CG1 . VAL   B 49  ? 0.1736 0.1924 0.1645 0.0196  -0.0231 -0.0085 49  VAL   B CG1 
5383 C CG2 . VAL   B 49  ? 0.1855 0.2132 0.1868 -0.0040 -0.0330 -0.0292 49  VAL   B CG2 
5393 N N   . ALA   B 50  ? 0.1573 0.1510 0.1269 0.0059  -0.0006 0.0011  50  ALA   B N   
5394 C CA  . ALA   B 50  ? 0.1623 0.1344 0.1360 0.0137  -0.0091 0.0043  50  ALA   B CA  
5395 C C   . ALA   B 50  ? 0.1627 0.1429 0.1297 0.0132  -0.0029 -0.0010 50  ALA   B C   
5396 O O   . ALA   B 50  ? 0.1673 0.1450 0.1345 0.0091  0.0025  -0.0066 50  ALA   B O   
5397 C CB  . ALA   B 50  ? 0.1700 0.1450 0.1413 0.0054  -0.0172 0.0044  50  ALA   B CB  
5403 N N   . GLY   B 51  ? 0.1644 0.1537 0.1435 0.0158  -0.0237 0.0107  51  GLY   B N   
5404 C CA  . GLY   B 51  ? 0.1618 0.1607 0.1657 0.0195  -0.0245 0.0013  51  GLY   B CA  
5405 C C   . GLY   B 51  ? 0.1625 0.1533 0.1558 0.0197  -0.0136 -0.0009 51  GLY   B C   
5406 O O   . GLY   B 51  ? 0.1575 0.1711 0.1826 0.0139  -0.0125 -0.0189 51  GLY   B O   
5410 N N   . ALA   B 52  ? 0.1564 0.1543 0.1435 0.0181  -0.0111 -0.0120 52  ALA   B N   
5411 C CA  . ALA   B 52  ? 0.1605 0.1636 0.1427 0.0197  -0.0033 -0.0178 52  ALA   B CA  
5412 C C   . ALA   B 52  ? 0.1524 0.1636 0.1270 0.0153  0.0041  -0.0172 52  ALA   B C   
5413 O O   . ALA   B 52  ? 0.1532 0.1668 0.1712 0.0104  0.0006  -0.0161 52  ALA   B O   
5414 C CB  . ALA   B 52  ? 0.1758 0.1597 0.1520 0.0127  -0.0015 -0.0202 52  ALA   B CB  
5420 N N   . LEU   B 53  ? 0.1469 0.1593 0.1443 0.0073  -0.0006 0.0016  53  LEU   B N   
5421 C CA  . LEU   B 53  ? 0.1522 0.1645 0.1341 0.0095  -0.0032 -0.0033 53  LEU   B CA  
5422 C C   . LEU   B 53  ? 0.1514 0.1590 0.1347 0.0128  0.0046  -0.0070 53  LEU   B C   
5423 O O   . LEU   B 53  ? 0.1499 0.1734 0.1636 0.0051  0.0053  0.0028  53  LEU   B O   
5424 C CB  . LEU   B 53  ? 0.1529 0.1745 0.1422 0.0169  -0.0031 0.0062  53  LEU   B CB  
5425 C CG  . LEU   B 53  ? 0.1513 0.1771 0.1529 0.0063  -0.0069 0.0269  53  LEU   B CG  
5426 C CD1 . LEU   B 53  ? 0.1591 0.1997 0.1864 0.0164  0.0051  0.0013  53  LEU   B CD1 
5427 C CD2 . LEU   B 53  ? 0.1646 0.2067 0.1725 -0.0056 -0.0059 -0.0079 53  LEU   B CD2 
5439 N N   . ASN   B 54  ? 0.1546 0.1469 0.1404 0.0087  -0.0032 0.0005  54  ASN   B N   
5440 C CA  . ASN   B 54  ? 0.1558 0.1641 0.1280 0.0150  -0.0111 -0.0062 54  ASN   B CA  
5441 C C   . ASN   B 54  ? 0.1561 0.1613 0.1572 0.0138  0.0013  -0.0117 54  ASN   B C   
5442 O O   . ASN   B 54  ? 0.1524 0.1661 0.1598 0.0099  0.0005  -0.0140 54  ASN   B O   
5443 C CB  . ASN   B 54  ? 0.1574 0.1754 0.1591 0.0081  -0.0058 -0.0042 54  ASN   B CB  
5444 C CG  . ASN   B 54  ? 0.1544 0.1787 0.1565 0.0109  -0.0146 -0.0048 54  ASN   B CG  
5445 O OD1 . ASN   B 54  ? 0.1534 0.1726 0.1748 0.0041  -0.0135 -0.0277 54  ASN   B OD1 
5446 N ND2 . ASN   B 54  ? 0.1798 0.2031 0.1869 0.0098  -0.0289 0.0052  54  ASN   B ND2 
5453 N N   . LYS   B 55  ? 0.1546 0.1731 0.1824 0.0177  -0.0065 -0.0141 55  LYS   B N   
5454 C CA  . LYS   B 55  ? 0.1568 0.1859 0.1952 0.0201  -0.0076 -0.0172 55  LYS   B CA  
5455 C C   . LYS   B 55  ? 0.1507 0.1907 0.1996 0.0198  0.0037  -0.0180 55  LYS   B C   
5456 O O   . LYS   B 55  ? 0.1506 0.2082 0.2072 0.0134  0.0058  -0.0247 55  LYS   B O   
5457 C CB  . LYS   B 55  ? 0.1740 0.1960 0.2355 0.0390  0.0076  -0.0002 55  LYS   B CB  
5458 C CG  . LYS   B 55  ? 0.2112 0.2341 0.3208 0.0429  0.0183  0.0137  55  LYS   B CG  
5459 C CD  . LYS   B 55  ? 0.2567 0.2640 0.4075 0.0550  0.0415  0.0217  55  LYS   B CD  
5460 C CE  . LYS   B 55  ? 0.2859 0.2884 0.4811 0.0546  0.0585  0.0337  55  LYS   B CE  
5461 N NZ  . LYS   B 55  ? 0.2892 0.3112 0.5318 0.0478  0.0427  0.0525  55  LYS   B NZ  
5475 N N   . ALA   B 56  ? 0.1499 0.1801 0.1800 0.0085  0.0051  -0.0167 56  ALA   B N   
5476 C CA  . ALA   B 56  ? 0.1687 0.1967 0.1705 0.0074  0.0014  -0.0216 56  ALA   B CA  
5477 C C   . ALA   B 56  ? 0.1705 0.1975 0.1648 0.0043  0.0089  -0.0068 56  ALA   B C   
5478 O O   . ALA   B 56  ? 0.1733 0.2070 0.1966 0.0029  0.0254  -0.0091 56  ALA   B O   
5479 C CB  . ALA   B 56  ? 0.1945 0.2142 0.1810 -0.0050 -0.0008 -0.0179 56  ALA   B CB  
5485 N N   . THR   B 57  ? 0.1587 0.1834 0.1691 -0.0015 0.0127  -0.0167 57  THR   B N   
5486 C CA  . THR   B 57  ? 0.1634 0.1837 0.1761 -0.0078 0.0149  -0.0115 57  THR   B CA  
5487 C C   . THR   B 57  ? 0.1590 0.1958 0.2013 -0.0028 0.0212  -0.0245 57  THR   B C   
5488 O O   . THR   B 57  ? 0.1666 0.1869 0.2032 -0.0148 0.0100  -0.0225 57  THR   B O   
5489 C CB  . THR   B 57  ? 0.1692 0.1661 0.1559 -0.0069 0.0054  0.0067  57  THR   B CB  
5490 O OG1 . THR   B 57  ? 0.1749 0.1557 0.1768 -0.0063 0.0043  -0.0041 57  THR   B OG1 
5491 C CG2 . THR   B 57  ? 0.1622 0.1691 0.1503 -0.0021 0.0191  0.0066  57  THR   B CG2 
5499 N N   . ASN   B 58  ? 0.1528 0.2227 0.2341 -0.0059 0.0056  -0.0395 58  ASN   B N   
5500 C CA  . ASN   B 58  ? 0.1882 0.2721 0.2613 -0.0173 0.0427  -0.0272 58  ASN   B CA  
5501 C C   . ASN   B 58  ? 0.1580 0.2469 0.2118 -0.0076 -0.0008 -0.0305 58  ASN   B C   
5502 O O   . ASN   B 58  ? 0.1584 0.2596 0.2437 -0.0084 -0.0076 -0.0429 58  ASN   B O   
5503 C CB  . ASN   B 58  ? 0.3068 0.3647 0.3887 -0.0330 0.0964  -0.0024 58  ASN   B CB  
5504 C CG  . ASN   B 58  ? 0.4400 0.4651 0.5645 -0.0393 0.1203  0.0265  58  ASN   B CG  
5505 O OD1 . ASN   B 58  ? 0.4573 0.4864 0.6436 -0.0426 0.1235  0.0376  58  ASN   B OD1 
5506 N ND2 . ASN   B 58  ? 0.5585 0.5585 0.6166 -0.0423 0.1305  0.0353  58  ASN   B ND2 
5513 N N   . ASN   B 59  ? 0.1526 0.2225 0.1884 -0.0048 -0.0039 -0.0164 59  ASN   B N   
5514 C CA  . ASN   B 59  ? 0.1577 0.2165 0.1719 -0.0044 -0.0135 -0.0044 59  ASN   B CA  
5515 C C   . ASN   B 59  ? 0.1532 0.2042 0.1663 -0.0079 -0.0171 -0.0142 59  ASN   B C   
5516 O O   . ASN   B 59  ? 0.1570 0.2039 0.1766 -0.0076 -0.0128 -0.0095 59  ASN   B O   
5517 C CB  . ASN   B 59  ? 0.1690 0.2297 0.1816 0.0064  -0.0252 -0.0107 59  ASN   B CB  
5518 C CG  . ASN   B 59  ? 0.1845 0.2460 0.2158 0.0109  -0.0362 -0.0107 59  ASN   B CG  
5519 O OD1 . ASN   B 59  ? 0.1790 0.2546 0.2050 0.0146  -0.0290 0.0071  59  ASN   B OD1 
5520 N ND2 . ASN   B 59  ? 0.1912 0.2534 0.2353 0.0087  -0.0450 -0.0244 59  ASN   B ND2 
5527 N N   . ALA   B 60  ? 0.1616 0.1870 0.1847 -0.0068 -0.0002 -0.0180 60  ALA   B N   
5528 C CA  . ALA   B 60  ? 0.1650 0.1797 0.1760 -0.0089 0.0004  -0.0107 60  ALA   B CA  
5529 C C   . ALA   B 60  ? 0.1728 0.1645 0.1505 -0.0026 -0.0089 -0.0065 60  ALA   B C   
5530 O O   . ALA   B 60  ? 0.1705 0.1746 0.1863 -0.0093 0.0008  -0.0127 60  ALA   B O   
5531 C CB  . ALA   B 60  ? 0.1778 0.1895 0.2118 -0.0190 0.0059  -0.0085 60  ALA   B CB  
5537 N N   . MET   B 61  ? 0.1640 0.1572 0.1635 -0.0048 0.0009  -0.0029 61  MET   B N   
5538 C CA  . MET   B 61  ? 0.1550 0.1542 0.1497 0.0039  -0.0141 -0.0036 61  MET   B CA  
5539 C C   . MET   B 61  ? 0.1521 0.1614 0.1581 -0.0017 -0.0146 -0.0035 61  MET   B C   
5540 O O   . MET   B 61  ? 0.1494 0.1649 0.1479 0.0094  -0.0137 -0.0272 61  MET   B O   
5541 C CB  . MET   B 61  ? 0.1503 0.1576 0.1417 0.0063  -0.0149 -0.0139 61  MET   B CB  
5542 C CG  . MET   B 61  ? 0.1493 0.1570 0.1344 0.0052  -0.0070 0.0000  61  MET   B CG  
5543 S SD  . MET   B 61  ? 0.1529 0.1568 0.1672 -0.0004 -0.0088 -0.0154 61  MET   B SD  
5544 C CE  . MET   B 61  ? 0.1534 0.1804 0.1823 -0.0003 -0.0066 -0.0289 61  MET   B CE  
5554 N N   . GLN   B 62  ? 0.1530 0.1570 0.1404 0.0060  -0.0173 -0.0076 62  GLN   B N   
5555 C CA  . GLN   B 62  ? 0.1612 0.1634 0.1459 0.0097  -0.0144 -0.0034 62  GLN   B CA  
5556 C C   . GLN   B 62  ? 0.1641 0.1727 0.1459 0.0049  -0.0225 -0.0141 62  GLN   B C   
5557 O O   . GLN   B 62  ? 0.1708 0.1766 0.1451 0.0052  -0.0290 -0.0113 62  GLN   B O   
5558 C CB  . GLN   B 62  ? 0.1747 0.1726 0.1513 0.0115  -0.0263 0.0010  62  GLN   B CB  
5559 C CG  . GLN   B 62  ? 0.1830 0.1806 0.1507 0.0047  -0.0284 -0.0201 62  GLN   B CG  
5560 C CD  . GLN   B 62  ? 0.1756 0.1777 0.1388 0.0120  -0.0308 -0.0070 62  GLN   B CD  
5561 O OE1 . GLN   B 62  ? 0.1709 0.1701 0.1623 0.0142  -0.0337 -0.0125 62  GLN   B OE1 
5562 N NE2 . GLN   B 62  ? 0.1781 0.1825 0.1403 0.0183  -0.0272 -0.0175 62  GLN   B NE2 
5571 N N   . VAL   B 63  ? 0.1603 0.1720 0.1707 0.0038  -0.0196 -0.0256 63  VAL   B N   
5572 C CA  . VAL   B 63  ? 0.1756 0.1789 0.1879 -0.0070 -0.0251 -0.0258 63  VAL   B CA  
5573 C C   . VAL   B 63  ? 0.1722 0.1681 0.1679 -0.0087 -0.0360 -0.0327 63  VAL   B C   
5574 O O   . VAL   B 63  ? 0.1845 0.1720 0.1807 0.0020  -0.0485 -0.0261 63  VAL   B O   
5575 C CB  . VAL   B 63  ? 0.1692 0.1888 0.2194 -0.0054 -0.0325 -0.0268 63  VAL   B CB  
5576 C CG1 . VAL   B 63  ? 0.1813 0.1860 0.2311 -0.0172 -0.0109 -0.0181 63  VAL   B CG1 
5577 C CG2 . VAL   B 63  ? 0.1608 0.2085 0.2387 0.0040  -0.0420 -0.0322 63  VAL   B CG2 
5587 N N   . GLU   B 64  ? 0.1713 0.1582 0.1658 0.0031  -0.0320 -0.0268 64  GLU   B N   
5588 C CA  . GLU   B 64  ? 0.1664 0.1579 0.1558 -0.0069 -0.0328 -0.0157 64  GLU   B CA  
5589 C C   . GLU   B 64  ? 0.1609 0.1593 0.1528 0.0028  -0.0284 -0.0193 64  GLU   B C   
5590 O O   . GLU   B 64  ? 0.1726 0.1637 0.1545 -0.0000 -0.0342 -0.0226 64  GLU   B O   
5591 C CB  . GLU   B 64  ? 0.1668 0.1693 0.1589 -0.0132 -0.0297 -0.0150 64  GLU   B CB  
5592 C CG  . GLU   B 64  ? 0.1822 0.1690 0.1530 -0.0123 -0.0297 -0.0238 64  GLU   B CG  
5593 C CD  . GLU   B 64  ? 0.1832 0.1801 0.1667 -0.0223 -0.0267 -0.0061 64  GLU   B CD  
5594 O OE1 . GLU   B 64  ? 0.1846 0.1916 0.1630 -0.0220 -0.0198 -0.0326 64  GLU   B OE1 
5595 O OE2 . GLU   B 64  ? 0.2071 0.1861 0.1612 -0.0302 -0.0348 -0.0110 64  GLU   B OE2 
5602 N N   . SER   B 65  ? 0.1628 0.1553 0.1351 -0.0034 -0.0203 -0.0228 65  SER   B N   
5603 C CA  . SER   B 65  ? 0.1616 0.1509 0.1400 0.0100  -0.0255 -0.0232 65  SER   B CA  
5604 C C   . SER   B 65  ? 0.1638 0.1542 0.1505 0.0186  -0.0343 -0.0240 65  SER   B C   
5605 O O   . SER   B 65  ? 0.1628 0.1584 0.1553 0.0087  -0.0285 -0.0225 65  SER   B O   
5606 C CB  . SER   B 65  ? 0.1656 0.1504 0.1470 0.0006  -0.0147 -0.0175 65  SER   B CB  
5607 O OG  . SER   B 65  ? 0.1688 0.1594 0.1406 -0.0010 -0.0188 -0.0285 65  SER   B OG  
5613 N N   . ASP   B 66  ? 0.1761 0.1622 0.1374 0.0111  -0.0392 -0.0222 66  ASP   B N   
5614 C CA  . ASP   B 66  ? 0.1821 0.1668 0.1405 0.0133  -0.0377 -0.0085 66  ASP   B CA  
5615 C C   . ASP   B 66  ? 0.1857 0.1682 0.1394 0.0026  -0.0300 -0.0221 66  ASP   B C   
5616 O O   . ASP   B 66  ? 0.1956 0.1751 0.1494 0.0115  -0.0308 -0.0321 66  ASP   B O   
5617 C CB  . ASP   B 66  ? 0.1917 0.1791 0.1619 0.0171  -0.0598 -0.0270 66  ASP   B CB  
5618 C CG  . ASP   B 66  ? 0.2106 0.1943 0.1819 0.0257  -0.0648 -0.0138 66  ASP   B CG  
5619 O OD1 . ASP   B 66  ? 0.2345 0.1913 0.1926 0.0182  -0.0527 -0.0117 66  ASP   B OD1 
5620 O OD2 . ASP   B 66  ? 0.2259 0.2183 0.2608 0.0429  -0.0546 -0.0108 66  ASP   B OD2 
5625 N N   . ASP   B 67  ? 0.1788 0.1666 0.1419 0.0056  -0.0286 -0.0342 67  ASP   B N   
5626 C CA  . ASP   B 67  ? 0.2008 0.1620 0.1445 0.0025  -0.0328 -0.0149 67  ASP   B CA  
5627 C C   . ASP   B 67  ? 0.1966 0.1648 0.1443 0.0126  -0.0282 -0.0222 67  ASP   B C   
5628 O O   . ASP   B 67  ? 0.1901 0.1690 0.1649 0.0050  -0.0185 -0.0416 67  ASP   B O   
5629 C CB  . ASP   B 67  ? 0.2262 0.1661 0.1761 -0.0044 -0.0478 -0.0219 67  ASP   B CB  
5630 C CG  . ASP   B 67  ? 0.2623 0.1750 0.1871 -0.0005 -0.0749 -0.0300 67  ASP   B CG  
5631 O OD1 . ASP   B 67  ? 0.2867 0.1816 0.2130 -0.0021 -0.0657 -0.0268 67  ASP   B OD1 
5632 O OD2 . ASP   B 67  ? 0.2723 0.1843 0.2061 0.0138  -0.0746 -0.0165 67  ASP   B OD2 
5637 N N   . TYR   B 68  ? 0.1917 0.1693 0.1440 0.0085  -0.0293 -0.0299 68  TYR   B N   
5638 C CA  . TYR   B 68  ? 0.1868 0.1778 0.1686 0.0169  -0.0444 -0.0419 68  TYR   B CA  
5639 C C   . TYR   B 68  ? 0.1772 0.1678 0.1581 0.0171  -0.0386 -0.0445 68  TYR   B C   
5640 O O   . TYR   B 68  ? 0.1796 0.1799 0.1736 0.0219  -0.0349 -0.0428 68  TYR   B O   
5641 C CB  . TYR   B 68  ? 0.1922 0.1911 0.1666 0.0317  -0.0541 -0.0445 68  TYR   B CB  
5642 C CG  . TYR   B 68  ? 0.2007 0.2048 0.1693 0.0283  -0.0448 -0.0534 68  TYR   B CG  
5643 C CD1 . TYR   B 68  ? 0.2065 0.2118 0.1671 0.0080  -0.0437 -0.0490 68  TYR   B CD1 
5644 C CD2 . TYR   B 68  ? 0.2091 0.2199 0.1818 0.0256  -0.0559 -0.0500 68  TYR   B CD2 
5645 C CE1 . TYR   B 68  ? 0.2115 0.2271 0.1843 0.0074  -0.0373 -0.0612 68  TYR   B CE1 
5646 C CE2 . TYR   B 68  ? 0.2013 0.2222 0.1859 0.0190  -0.0459 -0.0599 68  TYR   B CE2 
5647 C CZ  . TYR   B 68  ? 0.1958 0.2282 0.1966 0.0130  -0.0353 -0.0583 68  TYR   B CZ  
5648 O OH  . TYR   B 68  ? 0.1907 0.2426 0.2302 0.0058  -0.0208 -0.0337 68  TYR   B OH  
5658 N N   . ILE   B 69  ? 0.1667 0.1578 0.1652 0.0146  -0.0357 -0.0332 69  ILE   B N   
5659 C CA  . ILE   B 69  ? 0.1712 0.1653 0.1612 0.0045  -0.0337 -0.0239 69  ILE   B CA  
5660 C C   . ILE   B 69  ? 0.1695 0.1600 0.1672 0.0044  -0.0419 -0.0255 69  ILE   B C   
5661 O O   . ILE   B 69  ? 0.1763 0.1661 0.1616 0.0067  -0.0322 -0.0256 69  ILE   B O   
5662 C CB  . ILE   B 69  ? 0.1784 0.1601 0.1843 0.0065  -0.0153 -0.0288 69  ILE   B CB  
5663 C CG1 . ILE   B 69  ? 0.1790 0.1628 0.1940 -0.0072 -0.0081 -0.0307 69  ILE   B CG1 
5664 C CG2 . ILE   B 69  ? 0.1830 0.1695 0.1967 0.0036  -0.0109 -0.0268 69  ILE   B CG2 
5665 C CD1 . ILE   B 69  ? 0.1817 0.1739 0.1994 -0.0154 -0.0203 -0.0475 69  ILE   B CD1 
5677 N N   . ALA   B 70  ? 0.1628 0.1639 0.1591 0.0131  -0.0351 -0.0186 70  ALA   B N   
5678 C CA  . ALA   B 70  ? 0.1714 0.1663 0.1227 0.0003  -0.0395 -0.0246 70  ALA   B CA  
5679 C C   . ALA   B 70  ? 0.1787 0.1623 0.1462 -0.0040 -0.0323 -0.0261 70  ALA   B C   
5680 O O   . ALA   B 70  ? 0.1831 0.1623 0.1627 -0.0030 -0.0317 -0.0193 70  ALA   B O   
5681 C CB  . ALA   B 70  ? 0.1780 0.1743 0.1514 -0.0058 -0.0220 -0.0333 70  ALA   B CB  
5687 N N   . THR   B 71  ? 0.1922 0.1651 0.1580 0.0065  -0.0428 -0.0320 71  THR   B N   
5688 C CA  . THR   B 71  ? 0.2066 0.1766 0.1830 0.0128  -0.0566 -0.0287 71  THR   B CA  
5689 C C   . THR   B 71  ? 0.1951 0.1752 0.1888 0.0312  -0.0630 -0.0418 71  THR   B C   
5690 O O   . THR   B 71  ? 0.2057 0.1828 0.2250 0.0307  -0.0509 -0.0562 71  THR   B O   
5691 C CB  . THR   B 71  ? 0.2342 0.1977 0.2152 0.0129  -0.0596 0.0001  71  THR   B CB  
5692 O OG1 . THR   B 71  ? 0.2560 0.2268 0.2638 -0.0029 -0.0566 0.0376  71  THR   B OG1 
5693 C CG2 . THR   B 71  ? 0.2548 0.1973 0.2453 0.0132  -0.0456 0.0126  71  THR   B CG2 
5701 N N   . ASN   B 72  ? 0.1924 0.1806 0.1972 0.0148  -0.0617 -0.0667 72  ASN   B N   
5702 C CA  . ASN   B 72  ? 0.1914 0.1841 0.2235 0.0334  -0.0529 -0.0777 72  ASN   B CA  
5703 C C   . ASN   B 72  ? 0.1853 0.1980 0.2288 0.0240  -0.0350 -0.0784 72  ASN   B C   
5704 O O   . ASN   B 72  ? 0.1803 0.2199 0.2657 0.0200  -0.0266 -0.0818 72  ASN   B O   
5705 C CB  . ASN   B 72  ? 0.2032 0.2046 0.2316 0.0276  -0.0685 -0.0667 72  ASN   B CB  
5706 C CG  . ASN   B 72  ? 0.2206 0.2262 0.2257 0.0453  -0.0822 -0.0394 72  ASN   B CG  
5707 O OD1 . ASN   B 72  ? 0.2608 0.2581 0.2320 0.0324  -0.0609 -0.0516 72  ASN   B OD1 
5708 N ND2 . ASN   B 72  ? 0.2261 0.2289 0.2906 0.0616  -0.0786 0.0041  72  ASN   B ND2 
5715 N N   . GLY   B 73  ? 0.1768 0.1979 0.1879 0.0144  -0.0449 -0.0666 73  GLY   B N   
5716 C CA  . GLY   B 73  ? 0.1716 0.2121 0.1665 0.0071  -0.0161 -0.0553 73  GLY   B CA  
5717 C C   . GLY   B 73  ? 0.1739 0.2125 0.1122 0.0124  -0.0233 -0.0424 73  GLY   B C   
5718 O O   . GLY   B 73  ? 0.1730 0.1927 0.1497 0.0211  -0.0252 -0.0373 73  GLY   B O   
5722 N N   A PRO   B 74  ? 0.1735 0.2201 0.1317 0.0105  -0.0215 -0.0310 74  PRO   B N   
5723 N N   B PRO   B 74  ? 0.1731 0.2230 0.1237 0.0123  -0.0208 -0.0291 74  PRO   B N   
5724 C CA  A PRO   B 74  ? 0.1695 0.2154 0.1281 0.0135  -0.0132 -0.0221 74  PRO   B CA  
5725 C CA  B PRO   B 74  ? 0.1697 0.2194 0.1157 0.0181  -0.0105 -0.0160 74  PRO   B CA  
5726 C C   A PRO   B 74  ? 0.1641 0.1983 0.1231 0.0116  -0.0102 -0.0232 74  PRO   B C   
5727 C C   B PRO   B 74  ? 0.1651 0.2022 0.1240 0.0175  -0.0161 -0.0144 74  PRO   B C   
5728 O O   A PRO   B 74  ? 0.1654 0.1957 0.1667 0.0101  0.0019  -0.0348 74  PRO   B O   
5729 O O   B PRO   B 74  ? 0.1691 0.2023 0.1694 0.0208  -0.0194 -0.0247 74  PRO   B O   
5730 C CB  A PRO   B 74  ? 0.1762 0.2345 0.1373 0.0064  -0.0134 -0.0094 74  PRO   B CB  
5731 C CB  B PRO   B 74  ? 0.1794 0.2426 0.1121 0.0081  -0.0073 -0.0008 74  PRO   B CB  
5732 C CG  A PRO   B 74  ? 0.1913 0.2434 0.1512 0.0018  -0.0148 -0.0101 74  PRO   B CG  
5733 C CG  B PRO   B 74  ? 0.1983 0.2531 0.1313 0.0010  -0.0075 -0.0020 74  PRO   B CG  
5734 C CD  A PRO   B 74  ? 0.1907 0.2375 0.1410 0.0071  -0.0100 -0.0153 74  PRO   B CD  
5735 C CD  B PRO   B 74  ? 0.1952 0.2448 0.1192 0.0078  -0.0006 -0.0094 74  PRO   B CD  
5750 N N   . LEU   B 75  ? 0.1705 0.1870 0.1189 0.0168  -0.0216 -0.0196 75  LEU   B N   
5751 C CA  . LEU   B 75  ? 0.1783 0.1814 0.1107 0.0093  -0.0234 -0.0025 75  LEU   B CA  
5752 C C   . LEU   B 75  ? 0.1908 0.1982 0.1134 0.0155  -0.0188 0.0049  75  LEU   B C   
5753 O O   . LEU   B 75  ? 0.2047 0.2145 0.1243 0.0003  -0.0062 0.0084  75  LEU   B O   
5754 C CB  . LEU   B 75  ? 0.1745 0.1791 0.1211 -0.0006 -0.0304 0.0067  75  LEU   B CB  
5755 C CG  . LEU   B 75  ? 0.2118 0.1936 0.1439 -0.0263 -0.0157 0.0002  75  LEU   B CG  
5756 C CD1 . LEU   B 75  ? 0.2509 0.2134 0.1561 -0.0317 0.0043  -0.0036 75  LEU   B CD1 
5757 C CD2 . LEU   B 75  ? 0.2513 0.2156 0.2264 -0.0165 -0.0053 0.0117  75  LEU   B CD2 
5770 N N   . LYS   B 76  ? 0.1892 0.2141 0.1428 0.0122  -0.0053 0.0162  76  LYS   B N   
5771 C CA  . LYS   B 76  ? 0.2049 0.2227 0.1780 0.0014  0.0172  0.0015  76  LYS   B CA  
5772 C C   . LYS   B 76  ? 0.1945 0.2088 0.1396 0.0011  0.0231  0.0228  76  LYS   B C   
5773 O O   . LYS   B 76  ? 0.1995 0.1823 0.1485 -0.0041 0.0203  0.0126  76  LYS   B O   
5774 C CB  . LYS   B 76  ? 0.2158 0.2277 0.2236 0.0012  0.0303  -0.0425 76  LYS   B CB  
5775 C CG  . LYS   B 76  ? 0.2141 0.2533 0.2692 0.0030  0.0121  -0.0486 76  LYS   B CG  
5776 C CD  . LYS   B 76  ? 0.2054 0.2550 0.3021 0.0096  0.0188  -0.0639 76  LYS   B CD  
5777 C CE  . LYS   B 76  ? 0.2119 0.2669 0.3580 0.0100  0.0136  -0.0738 76  LYS   B CE  
5778 N NZ  . LYS   B 76  ? 0.2130 0.2703 0.3751 0.0028  -0.0124 -0.0881 76  LYS   B NZ  
5792 N N   . VAL   B 77  ? 0.2085 0.2278 0.1585 0.0047  0.0121  0.0223  77  VAL   B N   
5793 C CA  . VAL   B 77  ? 0.2126 0.2183 0.1648 0.0076  0.0156  0.0595  77  VAL   B CA  
5794 C C   . VAL   B 77  ? 0.1951 0.1887 0.1464 0.0159  0.0340  0.0433  77  VAL   B C   
5795 O O   . VAL   B 77  ? 0.1906 0.1903 0.1666 0.0144  0.0416  0.0272  77  VAL   B O   
5796 C CB  . VAL   B 77  ? 0.2389 0.2268 0.2157 0.0086  0.0228  0.0780  77  VAL   B CB  
5797 C CG1 . VAL   B 77  ? 0.2361 0.2091 0.2452 0.0056  0.0291  0.0901  77  VAL   B CG1 
5798 C CG2 . VAL   B 77  ? 0.2561 0.2392 0.2356 0.0079  0.0045  0.0837  77  VAL   B CG2 
5808 N N   . GLY   B 78  ? 0.1821 0.1686 0.1613 0.0115  0.0200  0.0264  78  GLY   B N   
5809 C CA  . GLY   B 78  ? 0.1843 0.1628 0.1497 0.0050  0.0281  0.0217  78  GLY   B CA  
5810 C C   . GLY   B 78  ? 0.1711 0.1585 0.1435 0.0100  0.0222  0.0239  78  GLY   B C   
5811 O O   . GLY   B 78  ? 0.1743 0.1577 0.1679 0.0121  0.0213  0.0279  78  GLY   B O   
5815 N N   . GLY   B 79  ? 0.1609 0.1676 0.1444 0.0079  0.0151  0.0137  79  GLY   B N   
5816 C CA  . GLY   B 79  ? 0.1572 0.1561 0.1357 0.0060  0.0073  0.0159  79  GLY   B CA  
5817 C C   . GLY   B 79  ? 0.1536 0.1536 0.1372 0.0130  0.0105  0.0071  79  GLY   B C   
5818 O O   . GLY   B 79  ? 0.1626 0.1511 0.1536 0.0149  0.0205  0.0093  79  GLY   B O   
5822 N N   . SER   B 80  ? 0.1545 0.1469 0.1436 0.0084  0.0243  0.0079  80  SER   B N   
5823 C CA  . SER   B 80  ? 0.1507 0.1483 0.1341 0.0001  0.0010  -0.0008 80  SER   B CA  
5824 C C   . SER   B 80  ? 0.1515 0.1468 0.1315 0.0088  0.0025  -0.0023 80  SER   B C   
5825 O O   . SER   B 80  ? 0.1596 0.1515 0.1598 0.0128  0.0079  -0.0011 80  SER   B O   
5826 C CB  . SER   B 80  ? 0.1541 0.1510 0.1423 0.0043  0.0040  0.0089  80  SER   B CB  
5827 O OG  . SER   B 80  ? 0.1583 0.1592 0.1638 -0.0030 -0.0073 0.0065  80  SER   B OG  
5833 N N   . CYS   B 81  ? 0.1521 0.1275 0.1396 0.0107  -0.0034 -0.0019 81  CYS   B N   
5834 C CA  . CYS   B 81  ? 0.1611 0.1315 0.1472 0.0029  -0.0131 -0.0092 81  CYS   B CA  
5835 C C   . CYS   B 81  ? 0.1472 0.1393 0.1256 -0.0042 -0.0135 -0.0003 81  CYS   B C   
5836 O O   . CYS   B 81  ? 0.1681 0.1282 0.1443 0.0043  -0.0008 -0.0024 81  CYS   B O   
5837 C CB  . CYS   B 81  ? 0.1709 0.1421 0.1418 -0.0079 -0.0164 -0.0033 81  CYS   B CB  
5838 S SG  . CYS   B 81  ? 0.1700 0.1621 0.1478 -0.0013 -0.0280 -0.0102 81  CYS   B SG  
5844 N N   . VAL   B 82  ? 0.1478 0.1378 0.1437 -0.0078 -0.0066 0.0027  82  VAL   B N   
5845 C CA  . VAL   B 82  ? 0.1527 0.1409 0.1273 -0.0055 -0.0153 0.0093  82  VAL   B CA  
5846 C C   . VAL   B 82  ? 0.1582 0.1308 0.1331 -0.0092 -0.0143 0.0071  82  VAL   B C   
5847 O O   . VAL   B 82  ? 0.1690 0.1295 0.1646 -0.0060 -0.0079 -0.0186 82  VAL   B O   
5848 C CB  . VAL   B 82  ? 0.1579 0.1632 0.1536 -0.0077 -0.0230 0.0120  82  VAL   B CB  
5849 C CG1 . VAL   B 82  ? 0.1672 0.1811 0.1622 -0.0015 -0.0168 0.0094  82  VAL   B CG1 
5850 C CG2 . VAL   B 82  ? 0.1687 0.1684 0.1704 -0.0075 -0.0255 0.0272  82  VAL   B CG2 
5860 N N   . LEU   B 83  ? 0.1496 0.1286 0.1344 -0.0136 -0.0285 -0.0061 83  LEU   B N   
5861 C CA  . LEU   B 83  ? 0.1549 0.1404 0.1145 -0.0146 -0.0276 -0.0130 83  LEU   B CA  
5862 C C   . LEU   B 83  ? 0.1567 0.1367 0.1276 -0.0143 -0.0267 -0.0044 83  LEU   B C   
5863 O O   . LEU   B 83  ? 0.1598 0.1461 0.1044 -0.0227 -0.0119 0.0045  83  LEU   B O   
5864 C CB  . LEU   B 83  ? 0.1578 0.1518 0.1189 -0.0115 -0.0259 -0.0110 83  LEU   B CB  
5865 C CG  . LEU   B 83  ? 0.1771 0.1639 0.1402 -0.0113 -0.0189 -0.0099 83  LEU   B CG  
5866 C CD1 . LEU   B 83  ? 0.1808 0.1669 0.1461 -0.0071 -0.0263 0.0075  83  LEU   B CD1 
5867 C CD2 . LEU   B 83  ? 0.1960 0.1664 0.1752 -0.0038 -0.0223 -0.0224 83  LEU   B CD2 
5879 N N   . SER   B 84  ? 0.1635 0.1505 0.1451 -0.0252 -0.0248 0.0013  84  SER   B N   
5880 C CA  . SER   B 84  ? 0.1633 0.1640 0.1331 -0.0331 -0.0263 0.0080  84  SER   B CA  
5881 C C   . SER   B 84  ? 0.1576 0.1784 0.0913 -0.0259 -0.0219 0.0170  84  SER   B C   
5882 O O   . SER   B 84  ? 0.1729 0.1591 0.1067 -0.0179 -0.0124 -0.0014 84  SER   B O   
5883 C CB  . SER   B 84  ? 0.1787 0.1656 0.1680 -0.0283 0.0035  -0.0032 84  SER   B CB  
5884 O OG  . SER   B 84  ? 0.1756 0.1823 0.2040 -0.0418 -0.0063 0.0084  84  SER   B OG  
5890 N N   . GLY   B 85  ? 0.1586 0.1947 0.1034 -0.0231 -0.0159 0.0115  85  GLY   B N   
5891 C CA  . GLY   B 85  ? 0.1684 0.1997 0.1354 -0.0372 0.0052  -0.0188 85  GLY   B CA  
5892 C C   . GLY   B 85  ? 0.1617 0.1815 0.1133 -0.0397 -0.0021 -0.0003 85  GLY   B C   
5893 O O   . GLY   B 85  ? 0.1775 0.1804 0.1319 -0.0513 0.0151  -0.0205 85  GLY   B O   
5897 N N   . HIS   B 86  ? 0.1607 0.1678 0.1344 -0.0326 -0.0153 0.0056  86  HIS   B N   
5898 C CA  . HIS   B 86  ? 0.1580 0.1758 0.1303 -0.0330 -0.0226 0.0030  86  HIS   B CA  
5899 C C   . HIS   B 86  ? 0.1542 0.1859 0.1321 -0.0426 -0.0086 0.0299  86  HIS   B C   
5900 O O   . HIS   B 86  ? 0.1744 0.1936 0.1505 -0.0388 0.0057  0.0166  86  HIS   B O   
5901 C CB  . HIS   B 86  ? 0.1671 0.1789 0.1371 -0.0145 -0.0163 -0.0051 86  HIS   B CB  
5902 C CG  . HIS   B 86  ? 0.1737 0.1806 0.1440 -0.0060 -0.0228 -0.0002 86  HIS   B CG  
5903 N ND1 . HIS   B 86  ? 0.1792 0.2059 0.1786 -0.0255 -0.0174 -0.0103 86  HIS   B ND1 
5904 C CD2 . HIS   B 86  ? 0.1830 0.1844 0.1429 0.0006  -0.0097 -0.0043 86  HIS   B CD2 
5905 C CE1 . HIS   B 86  ? 0.1868 0.2042 0.1622 -0.0156 -0.0043 -0.0320 86  HIS   B CE1 
5906 N NE2 . HIS   B 86  ? 0.1848 0.1925 0.1532 0.0070  -0.0086 -0.0075 86  HIS   B NE2 
5914 N N   . ASN   B 87  ? 0.1585 0.1760 0.1536 -0.0277 0.0017  0.0073  87  ASN   B N   
5915 C CA  . ASN   B 87  ? 0.1763 0.1920 0.1563 -0.0261 0.0252  0.0112  87  ASN   B CA  
5916 C C   . ASN   B 87  ? 0.1984 0.1835 0.1357 -0.0326 0.0370  0.0098  87  ASN   B C   
5917 O O   . ASN   B 87  ? 0.2274 0.1953 0.1772 -0.0336 0.0607  -0.0088 87  ASN   B O   
5918 C CB  . ASN   B 87  ? 0.1734 0.2239 0.1866 -0.0254 0.0300  0.0050  87  ASN   B CB  
5919 C CG  . ASN   B 87  ? 0.1777 0.2455 0.1963 0.0092  0.0312  0.0276  87  ASN   B CG  
5920 O OD1 . ASN   B 87  ? 0.1731 0.2238 0.1862 0.0107  0.0457  0.0296  87  ASN   B OD1 
5921 N ND2 . ASN   B 87  ? 0.2180 0.2611 0.2476 0.0194  0.0417  0.0313  87  ASN   B ND2 
5928 N N   . LEU   B 88  ? 0.1827 0.1728 0.1273 -0.0341 0.0209  0.0042  88  LEU   B N   
5929 C CA  . LEU   B 88  ? 0.1979 0.1581 0.1275 -0.0392 0.0050  0.0028  88  LEU   B CA  
5930 C C   . LEU   B 88  ? 0.1969 0.1530 0.1282 -0.0407 -0.0012 -0.0097 88  LEU   B C   
5931 O O   . LEU   B 88  ? 0.2189 0.1624 0.1581 -0.0187 -0.0222 -0.0222 88  LEU   B O   
5932 C CB  . LEU   B 88  ? 0.2243 0.1741 0.1407 -0.0526 -0.0154 -0.0009 88  LEU   B CB  
5933 C CG  . LEU   B 88  ? 0.2610 0.2049 0.1717 -0.0433 -0.0294 0.0171  88  LEU   B CG  
5934 C CD1 . LEU   B 88  ? 0.2634 0.2361 0.1955 -0.0545 -0.0249 0.0439  88  LEU   B CD1 
5935 C CD2 . LEU   B 88  ? 0.3018 0.2343 0.2424 -0.0030 -0.0543 0.0028  88  LEU   B CD2 
5947 N N   . ALA   B 89  ? 0.1733 0.1629 0.1256 -0.0468 0.0123  -0.0097 89  ALA   B N   
5948 C CA  . ALA   B 89  ? 0.1698 0.1531 0.1132 -0.0448 0.0023  0.0065  89  ALA   B CA  
5949 C C   . ALA   B 89  ? 0.1810 0.1490 0.1194 -0.0465 0.0178  0.0057  89  ALA   B C   
5950 O O   . ALA   B 89  ? 0.1633 0.1590 0.1579 -0.0436 0.0164  -0.0268 89  ALA   B O   
5951 C CB  . ALA   B 89  ? 0.1632 0.1529 0.1249 -0.0416 0.0064  0.0010  89  ALA   B CB  
5957 N N   . LYS   B 90  ? 0.2087 0.1403 0.1289 -0.0495 -0.0034 0.0024  90  LYS   B N   
5958 C CA  . LYS   B 90  ? 0.2161 0.1436 0.1039 -0.0423 -0.0055 -0.0003 90  LYS   B CA  
5959 C C   . LYS   B 90  ? 0.1945 0.1296 0.1352 -0.0339 -0.0062 -0.0053 90  LYS   B C   
5960 O O   . LYS   B 90  ? 0.1936 0.1446 0.1337 -0.0435 -0.0002 -0.0084 90  LYS   B O   
5961 C CB  . LYS   B 90  ? 0.2194 0.1503 0.1434 -0.0384 -0.0020 0.0128  90  LYS   B CB  
5962 C CG  . LYS   B 90  ? 0.2154 0.1637 0.1549 -0.0288 0.0163  0.0024  90  LYS   B CG  
5963 C CD  . LYS   B 90  ? 0.2358 0.1742 0.1821 -0.0172 0.0225  -0.0072 90  LYS   B CD  
5964 C CE  . LYS   B 90  ? 0.2544 0.1834 0.2246 -0.0106 0.0289  -0.0151 90  LYS   B CE  
5965 N NZ  . LYS   B 90  ? 0.2678 0.1778 0.2095 -0.0164 0.0510  -0.0229 90  LYS   B NZ  
5979 N N   . HIS   B 91  ? 0.1700 0.1310 0.1174 -0.0309 -0.0122 0.0018  91  HIS   B N   
5980 C CA  . HIS   B 91  ? 0.1646 0.1293 0.1324 -0.0236 -0.0163 -0.0033 91  HIS   B CA  
5981 C C   . HIS   B 91  ? 0.1551 0.1374 0.1074 -0.0253 -0.0087 -0.0028 91  HIS   B C   
5982 O O   . HIS   B 91  ? 0.1723 0.1441 0.1063 -0.0262 -0.0130 -0.0014 91  HIS   B O   
5983 C CB  . HIS   B 91  ? 0.1823 0.1292 0.1641 -0.0114 -0.0093 0.0049  91  HIS   B CB  
5984 C CG  . HIS   B 91  ? 0.2167 0.1597 0.2247 -0.0032 0.0208  0.0116  91  HIS   B CG  
5985 N ND1 . HIS   B 91  ? 0.2462 0.1617 0.3022 -0.0019 0.0258  -0.0010 91  HIS   B ND1 
5986 C CD2 . HIS   B 91  ? 0.2271 0.1908 0.2955 0.0115  0.0039  0.0636  91  HIS   B CD2 
5987 C CE1 . HIS   B 91  ? 0.2484 0.1798 0.3369 0.0071  0.0307  0.0164  91  HIS   B CE1 
5988 N NE2 . HIS   B 91  ? 0.2485 0.1969 0.3326 0.0133  0.0197  0.0704  91  HIS   B NE2 
5996 N N   . CYS   B 92  ? 0.1531 0.1357 0.1097 -0.0289 -0.0153 -0.0099 92  CYS   B N   
5997 C CA  . CYS   B 92  ? 0.1505 0.1273 0.1073 -0.0236 -0.0114 -0.0032 92  CYS   B CA  
5998 C C   . CYS   B 92  ? 0.1485 0.1283 0.1112 -0.0156 -0.0165 -0.0019 92  CYS   B C   
5999 O O   . CYS   B 92  ? 0.1493 0.1436 0.1192 -0.0152 -0.0101 0.0005  92  CYS   B O   
6000 C CB  . CYS   B 92  ? 0.1539 0.1382 0.1221 -0.0179 -0.0172 -0.0046 92  CYS   B CB  
6001 S SG  . CYS   B 92  ? 0.1502 0.1422 0.1315 -0.0112 -0.0147 0.0041  92  CYS   B SG  
6007 N N   . LEU   B 93  ? 0.1456 0.1293 0.1007 -0.0074 -0.0135 -0.0017 93  LEU   B N   
6008 C CA  . LEU   B 93  ? 0.1418 0.1327 0.1113 -0.0051 -0.0068 0.0045  93  LEU   B CA  
6009 C C   . LEU   B 93  ? 0.1331 0.1253 0.0974 -0.0041 -0.0123 0.0078  93  LEU   B C   
6010 O O   . LEU   B 93  ? 0.1430 0.1304 0.1235 -0.0068 -0.0053 -0.0055 93  LEU   B O   
6011 C CB  . LEU   B 93  ? 0.1488 0.1255 0.1189 -0.0026 -0.0165 0.0058  93  LEU   B CB  
6012 C CG  . LEU   B 93  ? 0.1401 0.1424 0.1481 -0.0085 -0.0080 0.0150  93  LEU   B CG  
6013 C CD1 . LEU   B 93  ? 0.1460 0.1520 0.1523 0.0031  -0.0079 -0.0005 93  LEU   B CD1 
6014 C CD2 . LEU   B 93  ? 0.1431 0.1469 0.1549 -0.0011 -0.0203 0.0025  93  LEU   B CD2 
6026 N N   . HIS   B 94  ? 0.1450 0.1293 0.0915 -0.0071 -0.0108 0.0037  94  HIS   B N   
6027 C CA  . HIS   B 94  ? 0.1504 0.1319 0.0897 0.0028  -0.0030 0.0064  94  HIS   B CA  
6028 C C   . HIS   B 94  ? 0.1402 0.1357 0.1221 0.0031  0.0021  0.0086  94  HIS   B C   
6029 O O   . HIS   B 94  ? 0.1365 0.1420 0.1593 0.0011  0.0106  -0.0048 94  HIS   B O   
6030 C CB  . HIS   B 94  ? 0.1422 0.1289 0.1285 0.0071  -0.0144 -0.0018 94  HIS   B CB  
6031 C CG  . HIS   B 94  ? 0.1418 0.1312 0.1231 -0.0054 -0.0219 -0.0075 94  HIS   B CG  
6032 N ND1 . HIS   B 94  ? 0.1442 0.1407 0.1152 0.0004  -0.0240 -0.0046 94  HIS   B ND1 
6033 C CD2 . HIS   B 94  ? 0.1440 0.1344 0.1348 0.0028  -0.0113 -0.0001 94  HIS   B CD2 
6034 C CE1 . HIS   B 94  ? 0.1492 0.1368 0.1319 -0.0064 -0.0217 0.0050  94  HIS   B CE1 
6035 N NE2 . HIS   B 94  ? 0.1451 0.1403 0.1371 -0.0096 -0.0154 -0.0019 94  HIS   B NE2 
6043 N N   . VAL   B 95  ? 0.1340 0.1264 0.1309 0.0012  -0.0034 0.0078  95  VAL   B N   
6044 C CA  . VAL   B 95  ? 0.1404 0.1393 0.1174 0.0049  0.0078  0.0161  95  VAL   B CA  
6045 C C   . VAL   B 95  ? 0.1477 0.1376 0.1197 0.0088  0.0163  0.0138  95  VAL   B C   
6046 O O   . VAL   B 95  ? 0.1503 0.1412 0.1373 0.0090  0.0073  0.0188  95  VAL   B O   
6047 C CB  . VAL   B 95  ? 0.1507 0.1395 0.1196 -0.0037 -0.0073 0.0104  95  VAL   B CB  
6048 C CG1 . VAL   B 95  ? 0.1589 0.1498 0.1452 -0.0081 0.0023  0.0090  95  VAL   B CG1 
6049 C CG2 . VAL   B 95  ? 0.1538 0.1400 0.1260 0.0048  -0.0048 0.0070  95  VAL   B CG2 
6059 N N   . VAL   B 96  ? 0.1658 0.1407 0.1216 0.0108  0.0071  0.0196  96  VAL   B N   
6060 C CA  . VAL   B 96  ? 0.1782 0.1497 0.1224 0.0145  0.0073  0.0206  96  VAL   B CA  
6061 C C   . VAL   B 96  ? 0.1819 0.1500 0.1394 0.0051  0.0133  0.0190  96  VAL   B C   
6062 O O   . VAL   B 96  ? 0.1829 0.1568 0.1463 -0.0010 0.0271  0.0112  96  VAL   B O   
6063 C CB  . VAL   B 96  ? 0.1904 0.1748 0.1145 0.0146  0.0047  0.0156  96  VAL   B CB  
6064 C CG1 . VAL   B 96  ? 0.1882 0.1890 0.1309 0.0272  0.0051  0.0142  96  VAL   B CG1 
6065 C CG2 . VAL   B 96  ? 0.1940 0.1718 0.1303 0.0070  0.0069  0.0056  96  VAL   B CG2 
6075 N N   . GLY   B 97  ? 0.1872 0.1543 0.1335 0.0036  0.0037  0.0228  97  GLY   B N   
6076 C CA  . GLY   B 97  ? 0.2154 0.1568 0.1443 0.0056  0.0062  0.0293  97  GLY   B CA  
6077 C C   . GLY   B 97  ? 0.2546 0.1631 0.1486 0.0113  0.0036  0.0191  97  GLY   B C   
6078 O O   . GLY   B 97  ? 0.2766 0.1736 0.1454 -0.0004 -0.0112 0.0098  97  GLY   B O   
6082 N N   . PRO   B 98  ? 0.2785 0.1741 0.1721 0.0221  0.0305  0.0414  98  PRO   B N   
6083 C CA  . PRO   B 98  ? 0.2935 0.1986 0.1967 0.0358  0.0571  0.0408  98  PRO   B CA  
6084 C C   . PRO   B 98  ? 0.3129 0.2089 0.1660 0.0626  0.0711  0.0705  98  PRO   B C   
6085 O O   . PRO   B 98  ? 0.2909 0.1973 0.1993 0.0503  0.0684  0.0669  98  PRO   B O   
6086 C CB  . PRO   B 98  ? 0.2831 0.2128 0.2372 0.0307  0.0768  0.0511  98  PRO   B CB  
6087 C CG  . PRO   B 98  ? 0.2802 0.1927 0.2208 0.0279  0.0657  0.0795  98  PRO   B CG  
6088 C CD  . PRO   B 98  ? 0.2694 0.1809 0.2071 0.0362  0.0467  0.0554  98  PRO   B CD  
6096 N N   . ASN   B 99  ? 0.3315 0.2419 0.1754 0.0979  0.0789  0.0527  99  ASN   B N   
6097 C CA  . ASN   B 99  ? 0.3610 0.2626 0.1794 0.1081  0.0641  0.0841  99  ASN   B CA  
6098 C C   . ASN   B 99  ? 0.3845 0.3036 0.2176 0.1000  0.0933  0.1190  99  ASN   B C   
6099 O O   . ASN   B 99  ? 0.3901 0.3171 0.2199 0.1148  0.0847  0.1221  99  ASN   B O   
6100 C CB  . ASN   B 99  ? 0.3682 0.2546 0.1908 0.1154  0.0470  0.0712  99  ASN   B CB  
6101 C CG  . ASN   B 99  ? 0.3755 0.2606 0.2076 0.1004  0.0428  0.0587  99  ASN   B CG  
6102 O OD1 . ASN   B 99  ? 0.3738 0.2573 0.2247 0.0994  0.0560  0.0731  99  ASN   B OD1 
6103 N ND2 . ASN   B 99  ? 0.3719 0.2551 0.2120 0.0991  0.0093  0.0439  99  ASN   B ND2 
6110 N N   A VAL   B 100 ? 0.4045 0.3264 0.2894 0.0782  0.0823  0.1241  100 VAL   B N   
6111 N N   B VAL   B 100 ? 0.3990 0.3139 0.2890 0.0829  0.0917  0.1433  100 VAL   B N   
6112 C CA  A VAL   B 100 ? 0.4265 0.3498 0.3568 0.0535  0.0639  0.1300  100 VAL   B CA  
6113 C CA  B VAL   B 100 ? 0.4183 0.3242 0.3546 0.0615  0.0791  0.1681  100 VAL   B CA  
6114 C C   A VAL   B 100 ? 0.4439 0.3695 0.3650 0.0467  0.0519  0.1315  100 VAL   B C   
6115 C C   B VAL   B 100 ? 0.4320 0.3301 0.3374 0.0659  0.0670  0.1884  100 VAL   B C   
6116 O O   A VAL   B 100 ? 0.4480 0.3778 0.3780 0.0449  0.0585  0.1275  100 VAL   B O   
6117 O O   B VAL   B 100 ? 0.4364 0.3397 0.3448 0.0628  0.0945  0.1842  100 VAL   B O   
6118 C CB  A VAL   B 100 ? 0.4307 0.3528 0.4101 0.0336  0.0592  0.1383  100 VAL   B CB  
6119 C CB  B VAL   B 100 ? 0.4219 0.3289 0.4263 0.0299  0.0824  0.1817  100 VAL   B CB  
6120 C CG1 A VAL   B 100 ? 0.4329 0.3544 0.4297 0.0291  0.0568  0.1392  100 VAL   B CG1 
6121 C CG1 B VAL   B 100 ? 0.4255 0.3319 0.4561 0.0241  0.0794  0.1804  100 VAL   B CG1 
6122 C CG2 A VAL   B 100 ? 0.4313 0.3547 0.4264 0.0253  0.0596  0.1405  100 VAL   B CG2 
6123 C CG2 B VAL   B 100 ? 0.4217 0.3306 0.4445 0.0164  0.0884  0.1853  100 VAL   B CG2 
6142 N N   A ASN   B 101 ? 0.4577 0.3829 0.3674 0.0426  0.0338  0.1258  101 ASN   B N   
6143 N N   B ASN   B 101 ? 0.4423 0.3326 0.3343 0.0746  0.0274  0.1883  101 ASN   B N   
6144 C CA  A ASN   B 101 ? 0.4733 0.3982 0.3751 0.0357  0.0192  0.1128  101 ASN   B CA  
6145 C CA  B ASN   B 101 ? 0.4633 0.3431 0.3404 0.0770  0.0117  0.1920  101 ASN   B CA  
6146 C C   A ASN   B 101 ? 0.4970 0.4236 0.4028 0.0284  0.0135  0.1035  101 ASN   B C   
6147 C C   B ASN   B 101 ? 0.4964 0.3803 0.3625 0.0684  0.0050  0.1878  101 ASN   B C   
6148 O O   A ASN   B 101 ? 0.4986 0.4268 0.4122 0.0320  0.0146  0.0967  101 ASN   B O   
6149 O O   B ASN   B 101 ? 0.4985 0.3898 0.3882 0.0731  0.0117  0.1616  101 ASN   B O   
6150 C CB  A ASN   B 101 ? 0.4662 0.3899 0.3673 0.0339  0.0146  0.0999  101 ASN   B CB  
6151 C CB  B ASN   B 101 ? 0.4556 0.3298 0.3468 0.0784  0.0145  0.1668  101 ASN   B CB  
6152 C CG  A ASN   B 101 ? 0.4597 0.3818 0.3580 0.0325  0.0144  0.0935  101 ASN   B CG  
6153 C CG  B ASN   B 101 ? 0.4463 0.3122 0.3384 0.0806  0.0210  0.1610  101 ASN   B CG  
6154 O OD1 A ASN   B 101 ? 0.4593 0.3808 0.3687 0.0310  0.0196  0.0912  101 ASN   B OD1 
6155 O OD1 B ASN   B 101 ? 0.4462 0.3139 0.3634 0.0756  0.0367  0.1472  101 ASN   B OD1 
6156 N ND2 A ASN   B 101 ? 0.4562 0.3775 0.3417 0.0330  0.0115  0.0900  101 ASN   B ND2 
6157 N ND2 B ASN   B 101 ? 0.4417 0.3036 0.3193 0.0832  0.0196  0.1539  101 ASN   B ND2 
6170 N N   A LYS   B 102 ? 0.5172 0.4466 0.4317 0.0174  0.0137  0.0908  102 LYS   B N   
6171 N N   B LYS   B 102 ? 0.5256 0.4176 0.4024 0.0499  0.0059  0.1667  102 LYS   B N   
6172 C CA  A LYS   B 102 ? 0.5357 0.4694 0.4559 0.0064  0.0167  0.0756  102 LYS   B CA  
6173 C CA  B LYS   B 102 ? 0.5527 0.4568 0.4303 0.0298  0.0073  0.1422  102 LYS   B CA  
6174 C C   A LYS   B 102 ? 0.5410 0.4746 0.4400 0.0074  0.0196  0.0907  102 LYS   B C   
6175 C C   B LYS   B 102 ? 0.5589 0.4655 0.4079 0.0221  0.0109  0.1652  102 LYS   B C   
6176 O O   A LYS   B 102 ? 0.5452 0.4758 0.4323 0.0059  0.0113  0.0931  102 LYS   B O   
6177 O O   B LYS   B 102 ? 0.5643 0.4658 0.3956 0.0210  -0.0046 0.1744  102 LYS   B O   
6178 C CB  A LYS   B 102 ? 0.5466 0.4855 0.4967 -0.0046 0.0235  0.0423  102 LYS   B CB  
6179 C CB  B LYS   B 102 ? 0.5701 0.4852 0.4844 0.0182  0.0142  0.0879  102 LYS   B CB  
6180 C CG  A LYS   B 102 ? 0.5560 0.4991 0.5322 -0.0137 0.0314  0.0117  102 LYS   B CG  
6181 C CG  B LYS   B 102 ? 0.5850 0.5078 0.5316 0.0095  0.0194  0.0420  102 LYS   B CG  
6182 C CD  A LYS   B 102 ? 0.5652 0.5109 0.5653 -0.0202 0.0379  -0.0126 102 LYS   B CD  
6183 C CD  B LYS   B 102 ? 0.5990 0.5267 0.5784 0.0035  0.0242  0.0067  102 LYS   B CD  
6184 C CE  A LYS   B 102 ? 0.5713 0.5189 0.5841 -0.0258 0.0429  -0.0309 102 LYS   B CE  
6185 C CE  B LYS   B 102 ? 0.6087 0.5421 0.6080 -0.0022 0.0273  -0.0184 102 LYS   B CE  
6186 N NZ  A LYS   B 102 ? 0.5751 0.5241 0.5972 -0.0281 0.0448  -0.0423 102 LYS   B NZ  
6187 N NZ  B LYS   B 102 ? 0.6147 0.5502 0.6310 -0.0048 0.0279  -0.0329 102 LYS   B NZ  
6214 N N   A GLY   B 103 ? 0.5404 0.4779 0.4421 0.0109  0.0325  0.0951  103 GLY   B N   
6215 N N   B GLY   B 103 ? 0.5573 0.4719 0.4157 0.0158  0.0326  0.1670  103 GLY   B N   
6216 C CA  A GLY   B 103 ? 0.5387 0.4799 0.4525 0.0153  0.0466  0.0924  103 GLY   B CA  
6217 C CA  B GLY   B 103 ? 0.5540 0.4765 0.4349 0.0118  0.0525  0.1577  103 GLY   B CA  
6218 C C   A GLY   B 103 ? 0.5347 0.4798 0.4572 0.0196  0.0585  0.0864  103 GLY   B C   
6219 C C   B GLY   B 103 ? 0.5474 0.4764 0.4382 0.0076  0.0693  0.1483  103 GLY   B C   
6220 O O   A GLY   B 103 ? 0.5373 0.4825 0.4617 0.0192  0.0620  0.0929  103 GLY   B O   
6221 O O   B GLY   B 103 ? 0.5506 0.4799 0.4403 0.0063  0.0726  0.1623  103 GLY   B O   
6228 N N   A GLU   B 104 ? 0.5267 0.4753 0.4477 0.0237  0.0667  0.0697  104 GLU   B N   
6229 N N   B GLU   B 104 ? 0.5352 0.4699 0.4235 0.0041  0.0818  0.1207  104 GLU   B N   
6230 C CA  A GLU   B 104 ? 0.5180 0.4706 0.4356 0.0302  0.0726  0.0513  104 GLU   B CA  
6231 C CA  B GLU   B 104 ? 0.5225 0.4625 0.4041 0.0045  0.0916  0.0916  104 GLU   B CA  
6232 C C   A GLU   B 104 ? 0.5164 0.4706 0.4396 0.0213  0.1095  0.0552  104 GLU   B C   
6233 C C   B GLU   B 104 ? 0.5179 0.4622 0.4049 -0.0020 0.1446  0.0987  104 GLU   B C   
6234 O O   A GLU   B 104 ? 0.5163 0.4723 0.4438 0.0199  0.1107  0.0590  104 GLU   B O   
6235 O O   B GLU   B 104 ? 0.5173 0.4641 0.4124 -0.0046 0.1467  0.1039  104 GLU   B O   
6236 C CB  A GLU   B 104 ? 0.5123 0.4640 0.4262 0.0454  0.0411  0.0242  104 GLU   B CB  
6237 C CB  B GLU   B 104 ? 0.5171 0.4531 0.3936 0.0115  0.0467  0.0487  104 GLU   B CB  
6238 C CG  A GLU   B 104 ? 0.5067 0.4588 0.4145 0.0607  0.0073  -0.0038 104 GLU   B CG  
6239 C CG  B GLU   B 104 ? 0.5114 0.4451 0.3748 0.0192  0.0008  0.0050  104 GLU   B CG  
6240 C CD  A GLU   B 104 ? 0.5022 0.4545 0.4046 0.0732  -0.0200 -0.0250 104 GLU   B CD  
6241 C CD  B GLU   B 104 ? 0.5066 0.4382 0.3550 0.0244  -0.0351 -0.0278 104 GLU   B CD  
6242 O OE1 A GLU   B 104 ? 0.4986 0.4499 0.3850 0.0789  -0.0218 -0.0323 104 GLU   B OE1 
6243 O OE1 B GLU   B 104 ? 0.5026 0.4329 0.3348 0.0271  -0.0392 -0.0381 104 GLU   B OE1 
6244 O OE2 A GLU   B 104 ? 0.5011 0.4553 0.3990 0.0766  -0.0391 -0.0368 104 GLU   B OE2 
6245 O OE2 B GLU   B 104 ? 0.5042 0.4372 0.3335 0.0234  -0.0620 -0.0453 104 GLU   B OE2 
6258 N N   A ASP   B 105 ? 0.5121 0.4682 0.4327 0.0146  0.1433  0.0531  105 ASP   B N   
6259 N N   B ASP   B 105 ? 0.5093 0.4588 0.3779 -0.0048 0.1955  0.0972  105 ASP   B N   
6260 C CA  A ASP   B 105 ? 0.5111 0.4672 0.4459 0.0077  0.1681  0.0403  105 ASP   B CA  
6261 C CA  B ASP   B 105 ? 0.5046 0.4586 0.3958 -0.0057 0.2244  0.0719  105 ASP   B CA  
6262 C C   A ASP   B 105 ? 0.4989 0.4518 0.4113 -0.0064 0.1840  0.0376  105 ASP   B C   
6263 C C   B ASP   B 105 ? 0.4870 0.4399 0.3603 -0.0188 0.2320  0.0692  105 ASP   B C   
6264 O O   A ASP   B 105 ? 0.4970 0.4505 0.3914 -0.0022 0.1936  0.0444  105 ASP   B O   
6265 O O   B ASP   B 105 ? 0.4723 0.4355 0.3480 -0.0154 0.2235  0.0721  105 ASP   B O   
6266 C CB  A ASP   B 105 ? 0.5193 0.4791 0.4996 0.0152  0.1731  0.0271  105 ASP   B CB  
6267 C CB  B ASP   B 105 ? 0.5174 0.4738 0.4649 0.0063  0.2288  0.0430  105 ASP   B CB  
6268 C CG  A ASP   B 105 ? 0.5267 0.4887 0.5560 0.0186  0.1778  0.0182  105 ASP   B CG  
6269 C CG  B ASP   B 105 ? 0.5265 0.4853 0.5349 0.0112  0.2336  0.0262  105 ASP   B CG  
6270 O OD1 A ASP   B 105 ? 0.5273 0.4908 0.5711 0.0176  0.1857  0.0207  105 ASP   B OD1 
6271 O OD1 B ASP   B 105 ? 0.5266 0.4883 0.5523 0.0093  0.2440  0.0283  105 ASP   B OD1 
6272 O OD2 A ASP   B 105 ? 0.5304 0.4935 0.5847 0.0227  0.1746  0.0107  105 ASP   B OD2 
6273 O OD2 B ASP   B 105 ? 0.5279 0.4901 0.5592 0.0154  0.2369  0.0159  105 ASP   B OD2 
6282 N N   A ILE   B 106 ? 0.4860 0.4353 0.4092 -0.0227 0.1868  0.0315  106 ILE   B N   
6283 N N   B ILE   B 106 ? 0.4789 0.4239 0.3699 -0.0324 0.2311  0.0603  106 ILE   B N   
6284 C CA  A ILE   B 106 ? 0.4680 0.4185 0.4166 -0.0378 0.1976  0.0233  106 ILE   B CA  
6285 C CA  B ILE   B 106 ? 0.4632 0.4087 0.3944 -0.0445 0.2313  0.0420  106 ILE   B CA  
6286 C C   A ILE   B 106 ? 0.4434 0.4072 0.4076 -0.0421 0.2139  0.0236  106 ILE   B C   
6287 C C   B ILE   B 106 ? 0.4363 0.4003 0.3858 -0.0459 0.2318  0.0358  106 ILE   B C   
6288 O O   A ILE   B 106 ? 0.4398 0.3996 0.4011 -0.0492 0.2215  0.0288  106 ILE   B O   
6289 O O   B ILE   B 106 ? 0.4232 0.3906 0.3656 -0.0513 0.2194  0.0444  106 ILE   B O   
6290 C CB  A ILE   B 106 ? 0.4737 0.4135 0.4283 -0.0457 0.1916  0.0190  106 ILE   B CB  
6291 C CB  B ILE   B 106 ? 0.4736 0.4026 0.4151 -0.0522 0.2329  0.0365  106 ILE   B CB  
6292 C CG1 A ILE   B 106 ? 0.4751 0.4108 0.4263 -0.0445 0.1825  0.0129  106 ILE   B CG1 
6293 C CG1 B ILE   B 106 ? 0.4786 0.4014 0.4173 -0.0451 0.2202  0.0246  106 ILE   B CG1 
6294 C CG2 A ILE   B 106 ? 0.4769 0.4148 0.4424 -0.0486 0.1919  0.0187  106 ILE   B CG2 
6295 C CG2 B ILE   B 106 ? 0.4786 0.4043 0.4366 -0.0570 0.2344  0.0359  106 ILE   B CG2 
6296 C CD1 A ILE   B 106 ? 0.4741 0.4083 0.4221 -0.0437 0.1797  0.0125  106 ILE   B CD1 
6297 C CD1 B ILE   B 106 ? 0.4795 0.3994 0.4148 -0.0408 0.2161  0.0226  106 ILE   B CD1 
6320 N N   . GLN   B 107 ? 0.4210 0.4032 0.4180 -0.0420 0.2177  0.0263  107 GLN   B N   
6321 C CA  . GLN   B 107 ? 0.3850 0.4003 0.4279 -0.0327 0.2067  0.0199  107 GLN   B CA  
6322 C C   . GLN   B 107 ? 0.3358 0.3617 0.3828 -0.0102 0.1779  0.0055  107 GLN   B C   
6323 O O   . GLN   B 107 ? 0.3232 0.3684 0.4267 0.0084  0.1450  -0.0291 107 GLN   B O   
6324 C CB  . GLN   B 107 ? 0.4201 0.4458 0.5293 -0.0338 0.1761  0.0196  107 GLN   B CB  
6325 C CG  . GLN   B 107 ? 0.4576 0.4936 0.6175 -0.0314 0.1344  0.0172  107 GLN   B CG  
6326 C CD  . GLN   B 107 ? 0.4867 0.5288 0.6862 -0.0323 0.1006  0.0176  107 GLN   B CD  
6327 O OE1 . GLN   B 107 ? 0.4912 0.5330 0.7076 -0.0324 0.0986  0.0192  107 GLN   B OE1 
6328 N NE2 . GLN   B 107 ? 0.4931 0.5338 0.7116 -0.0309 0.0824  0.0178  107 GLN   B NE2 
6338 N N   . LEU   B 108 ? 0.2985 0.3253 0.3241 0.0136  0.1531  0.0101  108 LEU   B N   
6339 C CA  . LEU   B 108 ? 0.2698 0.2847 0.2562 0.0234  0.1143  0.0281  108 LEU   B CA  
6340 C C   . LEU   B 108 ? 0.2160 0.2279 0.2367 0.0192  0.0676  0.0209  108 LEU   B C   
6341 O O   . LEU   B 108 ? 0.2019 0.2059 0.2050 0.0249  0.0443  0.0228  108 LEU   B O   
6342 C CB  . LEU   B 108 ? 0.2862 0.2996 0.2326 0.0229  0.1173  0.0491  108 LEU   B CB  
6343 C CG  . LEU   B 108 ? 0.3034 0.3268 0.2527 0.0233  0.0980  0.0360  108 LEU   B CG  
6344 C CD1 . LEU   B 108 ? 0.3196 0.3454 0.2542 0.0228  0.0904  0.0362  108 LEU   B CD1 
6345 C CD2 . LEU   B 108 ? 0.3123 0.3317 0.2657 0.0342  0.0708  0.0156  108 LEU   B CD2 
6357 N N   . LEU   B 109 ? 0.1901 0.1950 0.2297 0.0106  0.0559  0.0191  109 LEU   B N   
6358 C CA  . LEU   B 109 ? 0.1661 0.1583 0.2399 0.0067  0.0498  0.0289  109 LEU   B CA  
6359 C C   . LEU   B 109 ? 0.1631 0.1404 0.2437 0.0039  0.0388  0.0256  109 LEU   B C   
6360 O O   . LEU   B 109 ? 0.1679 0.1367 0.2344 0.0012  0.0420  0.0349  109 LEU   B O   
6361 C CB  . LEU   B 109 ? 0.1745 0.1440 0.2475 -0.0017 0.0378  0.0350  109 LEU   B CB  
6362 C CG  . LEU   B 109 ? 0.1681 0.1416 0.2327 -0.0001 0.0386  0.0135  109 LEU   B CG  
6363 C CD1 . LEU   B 109 ? 0.1662 0.1568 0.2183 0.0020  0.0274  0.0170  109 LEU   B CD1 
6364 C CD2 . LEU   B 109 ? 0.1882 0.1500 0.2641 -0.0080 0.0277  0.0217  109 LEU   B CD2 
6376 N N   . LYS   B 110 ? 0.1573 0.1457 0.2361 -0.0090 0.0417  0.0145  110 LYS   B N   
6377 C CA  . LYS   B 110 ? 0.1556 0.1418 0.2265 -0.0071 0.0418  0.0238  110 LYS   B CA  
6378 C C   . LYS   B 110 ? 0.1542 0.1427 0.2169 -0.0094 0.0449  0.0138  110 LYS   B C   
6379 O O   . LYS   B 110 ? 0.1518 0.1482 0.2223 -0.0083 0.0382  0.0129  110 LYS   B O   
6380 C CB  . LYS   B 110 ? 0.1705 0.1401 0.2524 0.0009  0.0427  0.0202  110 LYS   B CB  
6381 C CG  . LYS   B 110 ? 0.1632 0.1482 0.2675 -0.0046 0.0181  0.0262  110 LYS   B CG  
6382 C CD  . LYS   B 110 ? 0.1549 0.1399 0.2870 -0.0117 0.0221  0.0151  110 LYS   B CD  
6383 C CE  . LYS   B 110 ? 0.1574 0.1593 0.3006 -0.0016 0.0175  0.0107  110 LYS   B CE  
6384 N NZ  . LYS   B 110 ? 0.1574 0.1812 0.2872 0.0002  0.0078  0.0185  110 LYS   B NZ  
6398 N N   . SER   B 111 ? 0.1576 0.1414 0.2195 -0.0083 0.0417  0.0129  111 SER   B N   
6399 C CA  . SER   B 111 ? 0.1646 0.1458 0.2050 0.0008  0.0419  0.0187  111 SER   B CA  
6400 C C   . SER   B 111 ? 0.1526 0.1452 0.1981 -0.0054 0.0282  0.0077  111 SER   B C   
6401 O O   . SER   B 111 ? 0.1541 0.1463 0.2100 -0.0125 0.0189  0.0053  111 SER   B O   
6402 C CB  . SER   B 111 ? 0.1795 0.1675 0.2209 0.0086  0.0539  0.0222  111 SER   B CB  
6403 O OG  . SER   B 111 ? 0.1917 0.1935 0.2320 0.0193  0.0576  0.0337  111 SER   B OG  
6409 N N   . ALA   B 112 ? 0.1429 0.1435 0.2111 0.0067  0.0380  0.0156  112 ALA   B N   
6410 C CA  . ALA   B 112 ? 0.1494 0.1479 0.1828 0.0043  0.0182  0.0092  112 ALA   B CA  
6411 C C   . ALA   B 112 ? 0.1479 0.1367 0.1914 0.0044  0.0186  0.0068  112 ALA   B C   
6412 O O   . ALA   B 112 ? 0.1467 0.1414 0.1905 -0.0037 0.0159  0.0051  112 ALA   B O   
6413 C CB  . ALA   B 112 ? 0.1575 0.1512 0.1798 0.0057  0.0111  0.0186  112 ALA   B CB  
6419 N N   . TYR   B 113 ? 0.1413 0.1274 0.2031 0.0024  0.0133  0.0181  113 TYR   B N   
6420 C CA  . TYR   B 113 ? 0.1407 0.1280 0.2025 -0.0009 0.0145  0.0118  113 TYR   B CA  
6421 C C   . TYR   B 113 ? 0.1341 0.1307 0.1876 -0.0108 0.0134  0.0064  113 TYR   B C   
6422 O O   . TYR   B 113 ? 0.1388 0.1296 0.1815 -0.0052 0.0065  -0.0057 113 TYR   B O   
6423 C CB  . TYR   B 113 ? 0.1375 0.1218 0.2036 -0.0041 0.0235  0.0146  113 TYR   B CB  
6424 C CG  . TYR   B 113 ? 0.1415 0.1249 0.2163 -0.0059 0.0141  0.0109  113 TYR   B CG  
6425 C CD1 . TYR   B 113 ? 0.1466 0.1286 0.2260 -0.0038 0.0253  0.0220  113 TYR   B CD1 
6426 C CD2 . TYR   B 113 ? 0.1589 0.1253 0.2265 -0.0122 0.0165  0.0128  113 TYR   B CD2 
6427 C CE1 . TYR   B 113 ? 0.1501 0.1372 0.2179 -0.0071 0.0320  0.0091  113 TYR   B CE1 
6428 C CE2 . TYR   B 113 ? 0.1533 0.1219 0.2363 -0.0038 0.0205  0.0134  113 TYR   B CE2 
6429 C CZ  . TYR   B 113 ? 0.1478 0.1310 0.2326 0.0009  0.0259  0.0122  113 TYR   B CZ  
6430 O OH  . TYR   B 113 ? 0.1567 0.1298 0.2591 0.0065  0.0347  0.0081  113 TYR   B OH  
6440 N N   . GLU   B 114 ? 0.1380 0.1200 0.1988 -0.0055 0.0140  0.0085  114 GLU   B N   
6441 C CA  . GLU   B 114 ? 0.1370 0.1212 0.2009 0.0029  0.0017  0.0073  114 GLU   B CA  
6442 C C   . GLU   B 114 ? 0.1373 0.1206 0.1861 -0.0007 0.0122  0.0049  114 GLU   B C   
6443 O O   . GLU   B 114 ? 0.1376 0.1310 0.1974 0.0010  0.0026  0.0179  114 GLU   B O   
6444 C CB  . GLU   B 114 ? 0.1397 0.1246 0.2010 0.0001  0.0273  0.0140  114 GLU   B CB  
6445 C CG  . GLU   B 114 ? 0.1452 0.1171 0.2066 -0.0015 0.0070  -0.0002 114 GLU   B CG  
6446 C CD  . GLU   B 114 ? 0.1390 0.1262 0.2196 -0.0063 0.0144  0.0028  114 GLU   B CD  
6447 O OE1 . GLU   B 114 ? 0.1388 0.1380 0.2173 -0.0055 0.0279  0.0065  114 GLU   B OE1 
6448 O OE2 . GLU   B 114 ? 0.1427 0.1507 0.2330 -0.0190 0.0225  0.0023  114 GLU   B OE2 
6455 N N   . ASN   B 115 ? 0.1401 0.1203 0.1793 -0.0022 -0.0010 0.0018  115 ASN   B N   
6456 C CA  . ASN   B 115 ? 0.1383 0.1299 0.1670 -0.0089 0.0102  0.0094  115 ASN   B CA  
6457 C C   . ASN   B 115 ? 0.1306 0.1209 0.1799 -0.0121 -0.0002 0.0061  115 ASN   B C   
6458 O O   . ASN   B 115 ? 0.1430 0.1238 0.1795 -0.0130 0.0005  0.0047  115 ASN   B O   
6459 C CB  . ASN   B 115 ? 0.1490 0.1394 0.1630 -0.0077 0.0173  -0.0033 115 ASN   B CB  
6460 C CG  . ASN   B 115 ? 0.1592 0.1501 0.1695 -0.0074 0.0009  0.0011  115 ASN   B CG  
6461 O OD1 . ASN   B 115 ? 0.1957 0.1612 0.1959 -0.0073 0.0147  -0.0079 115 ASN   B OD1 
6462 N ND2 . ASN   B 115 ? 0.1573 0.1585 0.1738 -0.0061 -0.0011 0.0224  115 ASN   B ND2 
6469 N N   . PHE   B 116 ? 0.1333 0.1262 0.1633 -0.0081 -0.0031 -0.0004 116 PHE   B N   
6470 C CA  . PHE   B 116 ? 0.1390 0.1335 0.1629 -0.0118 -0.0054 0.0010  116 PHE   B CA  
6471 C C   . PHE   B 116 ? 0.1319 0.1199 0.1523 -0.0119 -0.0072 0.0030  116 PHE   B C   
6472 O O   . PHE   B 116 ? 0.1483 0.1345 0.1599 -0.0064 -0.0080 0.0058  116 PHE   B O   
6473 C CB  . PHE   B 116 ? 0.1311 0.1330 0.1562 -0.0133 -0.0024 0.0021  116 PHE   B CB  
6474 C CG  . PHE   B 116 ? 0.1265 0.1333 0.1566 -0.0152 0.0045  0.0025  116 PHE   B CG  
6475 C CD1 . PHE   B 116 ? 0.1364 0.1316 0.1602 -0.0061 -0.0042 0.0038  116 PHE   B CD1 
6476 C CD2 . PHE   B 116 ? 0.1346 0.1507 0.1435 -0.0090 0.0008  -0.0050 116 PHE   B CD2 
6477 C CE1 . PHE   B 116 ? 0.1523 0.1391 0.1597 -0.0001 -0.0167 0.0041  116 PHE   B CE1 
6478 C CE2 . PHE   B 116 ? 0.1362 0.1474 0.1587 -0.0065 -0.0032 0.0054  116 PHE   B CE2 
6479 C CZ  . PHE   B 116 ? 0.1381 0.1439 0.1605 -0.0032 -0.0065 0.0062  116 PHE   B CZ  
6489 N N   . ASN   B 117 ? 0.1391 0.1226 0.1781 -0.0088 -0.0153 0.0113  117 ASN   B N   
6490 C CA  . ASN   B 117 ? 0.1462 0.1311 0.1842 -0.0059 -0.0116 0.0020  117 ASN   B CA  
6491 C C   . ASN   B 117 ? 0.1545 0.1324 0.1871 -0.0085 -0.0223 0.0108  117 ASN   B C   
6492 O O   . ASN   B 117 ? 0.1590 0.1339 0.2217 -0.0068 -0.0396 0.0141  117 ASN   B O   
6493 C CB  . ASN   B 117 ? 0.1465 0.1272 0.1967 -0.0027 -0.0072 0.0040  117 ASN   B CB  
6494 C CG  . ASN   B 117 ? 0.1387 0.1314 0.2063 0.0020  -0.0032 0.0019  117 ASN   B CG  
6495 O OD1 . ASN   B 117 ? 0.1621 0.1376 0.2138 -0.0204 -0.0005 -0.0020 117 ASN   B OD1 
6496 N ND2 . ASN   B 117 ? 0.1491 0.1322 0.1837 -0.0064 0.0010  -0.0014 117 ASN   B ND2 
6503 N N   . GLN   B 118 ? 0.1512 0.1294 0.1775 -0.0134 -0.0112 -0.0025 118 GLN   B N   
6504 C CA  . GLN   B 118 ? 0.1569 0.1289 0.1903 -0.0062 -0.0121 -0.0078 118 GLN   B CA  
6505 C C   . GLN   B 118 ? 0.1466 0.1242 0.1969 -0.0040 -0.0093 -0.0021 118 GLN   B C   
6506 O O   . GLN   B 118 ? 0.1765 0.1236 0.2364 -0.0096 -0.0038 0.0104  118 GLN   B O   
6507 C CB  . GLN   B 118 ? 0.1580 0.1324 0.1966 -0.0047 -0.0116 -0.0133 118 GLN   B CB  
6508 C CG  . GLN   B 118 ? 0.1666 0.1394 0.1962 0.0036  -0.0130 -0.0154 118 GLN   B CG  
6509 C CD  . GLN   B 118 ? 0.1709 0.1314 0.2005 -0.0006 -0.0089 -0.0104 118 GLN   B CD  
6510 O OE1 . GLN   B 118 ? 0.1726 0.1298 0.2342 -0.0028 0.0034  -0.0029 118 GLN   B OE1 
6511 N NE2 . GLN   B 118 ? 0.1794 0.1339 0.2039 0.0084  -0.0140 0.0012  118 GLN   B NE2 
6520 N N   . HIS   B 119 ? 0.1571 0.1273 0.1617 -0.0148 -0.0135 0.0111  119 HIS   B N   
6521 C CA  . HIS   B 119 ? 0.1671 0.1385 0.1565 -0.0115 -0.0200 0.0144  119 HIS   B CA  
6522 C C   . HIS   B 119 ? 0.1702 0.1349 0.1458 -0.0063 -0.0401 0.0148  119 HIS   B C   
6523 O O   . HIS   B 119 ? 0.1823 0.1398 0.1779 -0.0331 -0.0299 0.0073  119 HIS   B O   
6524 C CB  . HIS   B 119 ? 0.1699 0.1559 0.1487 -0.0003 -0.0201 0.0038  119 HIS   B CB  
6525 C CG  . HIS   B 119 ? 0.1674 0.1868 0.1786 0.0012  -0.0427 -0.0144 119 HIS   B CG  
6526 N ND1 . HIS   B 119 ? 0.1691 0.1973 0.2114 -0.0058 -0.0469 -0.0332 119 HIS   B ND1 
6527 C CD2 . HIS   B 119 ? 0.1874 0.2077 0.1827 0.0366  -0.0464 -0.0260 119 HIS   B CD2 
6528 C CE1 . HIS   B 119 ? 0.1944 0.2147 0.2200 0.0198  -0.0523 -0.0368 119 HIS   B CE1 
6529 N NE2 . HIS   B 119 ? 0.2052 0.2237 0.1857 0.0375  -0.0529 -0.0420 119 HIS   B NE2 
6537 N N   . GLU   B 120 ? 0.1962 0.1417 0.1522 -0.0221 -0.0442 0.0211  120 GLU   B N   
6538 C CA  . GLU   B 120 ? 0.2250 0.1520 0.1663 -0.0142 -0.0510 0.0296  120 GLU   B CA  
6539 C C   . GLU   B 120 ? 0.1962 0.1377 0.1509 -0.0127 -0.0343 0.0210  120 GLU   B C   
6540 O O   . GLU   B 120 ? 0.1884 0.1566 0.1574 -0.0176 -0.0398 0.0137  120 GLU   B O   
6541 C CB  . GLU   B 120 ? 0.2873 0.1847 0.2327 0.0043  -0.0820 0.0436  120 GLU   B CB  
6542 C CG  . GLU   B 120 ? 0.3403 0.2734 0.3354 0.0167  -0.1103 0.0527  120 GLU   B CG  
6543 C CD  . GLU   B 120 ? 0.3825 0.3442 0.4512 0.0226  -0.1110 0.0649  120 GLU   B CD  
6544 O OE1 . GLU   B 120 ? 0.4010 0.3616 0.4952 0.0169  -0.0970 0.0757  120 GLU   B OE1 
6545 O OE2 . GLU   B 120 ? 0.3985 0.3691 0.5030 0.0238  -0.1157 0.0646  120 GLU   B OE2 
6552 N N   . VAL   B 121 ? 0.1883 0.1439 0.1521 -0.0222 -0.0273 0.0158  121 VAL   B N   
6553 C CA  . VAL   B 121 ? 0.1719 0.1457 0.1401 -0.0219 -0.0375 0.0173  121 VAL   B CA  
6554 C C   . VAL   B 121 ? 0.1704 0.1431 0.1404 -0.0244 -0.0257 0.0099  121 VAL   B C   
6555 O O   . VAL   B 121 ? 0.1838 0.1434 0.1589 -0.0376 -0.0298 0.0103  121 VAL   B O   
6556 C CB  . VAL   B 121 ? 0.2031 0.1883 0.1552 -0.0157 -0.0427 0.0187  121 VAL   B CB  
6557 C CG1 . VAL   B 121 ? 0.2109 0.1991 0.1940 -0.0282 -0.0244 0.0097  121 VAL   B CG1 
6558 C CG2 . VAL   B 121 ? 0.2319 0.2133 0.1476 -0.0006 -0.0243 -0.0030 121 VAL   B CG2 
6568 N N   . LEU   B 122 ? 0.1596 0.1407 0.1373 -0.0205 -0.0324 0.0127  122 LEU   B N   
6569 C CA  . LEU   B 122 ? 0.1573 0.1540 0.1153 -0.0175 -0.0239 0.0086  122 LEU   B CA  
6570 C C   . LEU   B 122 ? 0.1550 0.1304 0.1358 -0.0243 -0.0216 0.0108  122 LEU   B C   
6571 O O   . LEU   B 122 ? 0.1667 0.1311 0.1751 -0.0353 -0.0313 0.0050  122 LEU   B O   
6572 C CB  . LEU   B 122 ? 0.1733 0.1703 0.1725 -0.0032 -0.0255 0.0137  122 LEU   B CB  
6573 C CG  . LEU   B 122 ? 0.1582 0.1826 0.1809 -0.0166 -0.0107 0.0135  122 LEU   B CG  
6574 C CD1 . LEU   B 122 ? 0.1632 0.1913 0.1554 -0.0363 -0.0179 0.0092  122 LEU   B CD1 
6575 C CD2 . LEU   B 122 ? 0.1581 0.1888 0.1430 -0.0141 -0.0074 -0.0016 122 LEU   B CD2 
6587 N N   . LEU   B 123 ? 0.1552 0.1249 0.1251 -0.0225 -0.0223 0.0159  123 LEU   B N   
6588 C CA  . LEU   B 123 ? 0.1578 0.1324 0.1382 -0.0293 -0.0204 -0.0003 123 LEU   B CA  
6589 C C   . LEU   B 123 ? 0.1567 0.1277 0.1252 -0.0256 -0.0251 0.0030  123 LEU   B C   
6590 O O   . LEU   B 123 ? 0.1625 0.1301 0.1242 -0.0319 -0.0138 0.0013  123 LEU   B O   
6591 C CB  . LEU   B 123 ? 0.1595 0.1336 0.1390 -0.0195 -0.0168 -0.0064 123 LEU   B CB  
6592 C CG  . LEU   B 123 ? 0.1566 0.1356 0.1403 -0.0147 -0.0060 0.0041  123 LEU   B CG  
6593 C CD1 . LEU   B 123 ? 0.1731 0.1407 0.1499 -0.0205 0.0028  -0.0047 123 LEU   B CD1 
6594 C CD2 . LEU   B 123 ? 0.1718 0.1411 0.1678 -0.0150 -0.0083 0.0052  123 LEU   B CD2 
6606 N N   . ALA   B 124 ? 0.1514 0.1296 0.1269 -0.0265 -0.0143 -0.0038 124 ALA   B N   
6607 C CA  . ALA   B 124 ? 0.1440 0.1257 0.1349 -0.0156 -0.0111 -0.0003 124 ALA   B CA  
6608 C C   . ALA   B 124 ? 0.1411 0.1220 0.1366 -0.0209 -0.0151 -0.0056 124 ALA   B C   
6609 O O   . ALA   B 124 ? 0.1536 0.1294 0.1356 -0.0231 -0.0151 0.0036  124 ALA   B O   
6610 C CB  . ALA   B 124 ? 0.1476 0.1267 0.1489 -0.0084 -0.0022 0.0021  124 ALA   B CB  
6616 N N   . PRO   B 125 ? 0.1523 0.1292 0.1369 -0.0186 -0.0209 0.0103  125 PRO   B N   
6617 C CA  . PRO   B 125 ? 0.1617 0.1327 0.1461 -0.0185 -0.0151 0.0179  125 PRO   B CA  
6618 C C   . PRO   B 125 ? 0.1585 0.1300 0.1562 -0.0115 0.0038  0.0053  125 PRO   B C   
6619 O O   . PRO   B 125 ? 0.1523 0.1333 0.1669 -0.0101 0.0062  0.0174  125 PRO   B O   
6620 C CB  . PRO   B 125 ? 0.1617 0.1569 0.1592 -0.0194 -0.0296 0.0289  125 PRO   B CB  
6621 C CG  . PRO   B 125 ? 0.1629 0.1615 0.1502 -0.0278 -0.0210 0.0237  125 PRO   B CG  
6622 C CD  . PRO   B 125 ? 0.1611 0.1402 0.1409 -0.0346 -0.0159 0.0108  125 PRO   B CD  
6630 N N   . LEU   B 126 ? 0.1686 0.1207 0.1824 -0.0222 0.0214  0.0171  126 LEU   B N   
6631 C CA  . LEU   B 126 ? 0.1735 0.1404 0.1839 -0.0179 0.0288  0.0144  126 LEU   B CA  
6632 C C   . LEU   B 126 ? 0.1711 0.1447 0.1812 -0.0011 0.0242  0.0279  126 LEU   B C   
6633 O O   . LEU   B 126 ? 0.1948 0.1847 0.2109 0.0282  -0.0030 -0.0045 126 LEU   B O   
6634 C CB  . LEU   B 126 ? 0.1872 0.1424 0.2044 -0.0314 0.0344  0.0122  126 LEU   B CB  
6635 C CG  . LEU   B 126 ? 0.2025 0.1546 0.2236 -0.0339 0.0284  -0.0012 126 LEU   B CG  
6636 C CD1 . LEU   B 126 ? 0.2177 0.1584 0.2822 -0.0334 0.0188  -0.0045 126 LEU   B CD1 
6637 C CD2 . LEU   B 126 ? 0.1979 0.1613 0.2312 -0.0386 0.0157  -0.0102 126 LEU   B CD2 
6649 N N   . LEU   B 127 ? 0.1647 0.1312 0.2008 -0.0001 0.0328  0.0089  127 LEU   B N   
6650 C CA  . LEU   B 127 ? 0.1678 0.1406 0.2157 -0.0050 0.0355  0.0118  127 LEU   B CA  
6651 C C   . LEU   B 127 ? 0.1560 0.1373 0.2153 -0.0065 0.0292  0.0211  127 LEU   B C   
6652 O O   . LEU   B 127 ? 0.1607 0.1379 0.2219 -0.0146 0.0158  0.0209  127 LEU   B O   
6653 C CB  . LEU   B 127 ? 0.1843 0.1410 0.2079 -0.0032 0.0355  0.0147  127 LEU   B CB  
6654 C CG  . LEU   B 127 ? 0.1938 0.1377 0.2093 -0.0028 0.0373  0.0160  127 LEU   B CG  
6655 C CD1 . LEU   B 127 ? 0.1952 0.1473 0.2196 0.0066  0.0306  0.0205  127 LEU   B CD1 
6656 C CD2 . LEU   B 127 ? 0.2025 0.1453 0.2316 -0.0172 0.0402  0.0156  127 LEU   B CD2 
6668 N N   . SER   B 128 ? 0.1629 0.1300 0.2137 -0.0029 0.0092  0.0233  128 SER   B N   
6669 C CA  . SER   B 128 ? 0.1798 0.1458 0.2168 0.0067  -0.0017 0.0270  128 SER   B CA  
6670 C C   . SER   B 128 ? 0.1984 0.1454 0.2565 0.0038  -0.0219 0.0294  128 SER   B C   
6671 O O   . SER   B 128 ? 0.2202 0.1549 0.3070 0.0044  -0.0165 0.0435  128 SER   B O   
6672 C CB  . SER   B 128 ? 0.1879 0.1483 0.2078 0.0027  0.0146  0.0428  128 SER   B CB  
6673 O OG  . SER   B 128 ? 0.1908 0.1627 0.2155 0.0135  0.0168  0.0360  128 SER   B OG  
6679 N N   . ALA   B 129 ? 0.2075 0.1589 0.2806 0.0261  -0.0041 0.0055  129 ALA   B N   
6680 C CA  . ALA   B 129 ? 0.2208 0.1681 0.2895 0.0376  -0.0100 0.0018  129 ALA   B CA  
6681 C C   . ALA   B 129 ? 0.2111 0.1564 0.2696 0.0280  0.0068  -0.0037 129 ALA   B C   
6682 O O   . ALA   B 129 ? 0.2045 0.1620 0.2630 0.0217  0.0014  -0.0002 129 ALA   B O   
6683 C CB  . ALA   B 129 ? 0.2470 0.1968 0.3265 0.0387  0.0002  -0.0111 129 ALA   B CB  
6689 N N   . GLY   B 130 ? 0.2059 0.1604 0.2794 0.0317  0.0100  0.0015  130 GLY   B N   
6690 C CA  . GLY   B 130 ? 0.2158 0.1711 0.2876 0.0280  0.0333  0.0084  130 GLY   B CA  
6691 C C   . GLY   B 130 ? 0.2265 0.1697 0.2595 0.0183  0.0252  0.0302  130 GLY   B C   
6692 O O   . GLY   B 130 ? 0.2375 0.1928 0.2752 0.0198  0.0080  0.0410  130 GLY   B O   
6696 N N   . ILE   B 131 ? 0.2228 0.1921 0.2743 0.0256  0.0149  0.0188  131 ILE   B N   
6697 C CA  . ILE   B 131 ? 0.2470 0.2030 0.2770 0.0262  0.0070  0.0291  131 ILE   B CA  
6698 C C   . ILE   B 131 ? 0.2516 0.1940 0.2405 0.0215  0.0012  0.0312  131 ILE   B C   
6699 O O   . ILE   B 131 ? 0.2797 0.2155 0.2468 0.0184  -0.0133 0.0366  131 ILE   B O   
6700 C CB  . ILE   B 131 ? 0.2553 0.2310 0.3249 0.0165  -0.0020 0.0224  131 ILE   B CB  
6701 C CG1 . ILE   B 131 ? 0.2633 0.2543 0.3486 -0.0137 -0.0147 0.0341  131 ILE   B CG1 
6702 C CG2 . ILE   B 131 ? 0.2524 0.2477 0.3516 0.0293  0.0059  0.0048  131 ILE   B CG2 
6703 C CD1 . ILE   B 131 ? 0.2627 0.2737 0.3724 -0.0259 -0.0288 0.0386  131 ILE   B CD1 
6715 N N   . PHE   B 132 ? 0.2451 0.1765 0.2337 0.0187  0.0312  0.0276  132 PHE   B N   
6716 C CA  . PHE   B 132 ? 0.2566 0.1778 0.2388 0.0091  0.0548  0.0289  132 PHE   B CA  
6717 C C   . PHE   B 132 ? 0.2718 0.1967 0.2687 0.0158  0.0651  0.0304  132 PHE   B C   
6718 O O   . PHE   B 132 ? 0.2872 0.2228 0.2894 0.0135  0.0807  0.0191  132 PHE   B O   
6719 C CB  . PHE   B 132 ? 0.2454 0.1782 0.2198 0.0080  0.0489  0.0187  132 PHE   B CB  
6720 C CG  . PHE   B 132 ? 0.2288 0.1814 0.2118 0.0189  0.0279  0.0286  132 PHE   B CG  
6721 C CD1 . PHE   B 132 ? 0.2375 0.1805 0.2644 0.0067  0.0328  0.0295  132 PHE   B CD1 
6722 C CD2 . PHE   B 132 ? 0.2204 0.1895 0.1899 0.0271  0.0210  0.0419  132 PHE   B CD2 
6723 C CE1 . PHE   B 132 ? 0.2344 0.1839 0.2734 0.0017  0.0241  0.0279  132 PHE   B CE1 
6724 C CE2 . PHE   B 132 ? 0.2288 0.1985 0.2133 0.0205  0.0075  0.0427  132 PHE   B CE2 
6725 C CZ  . PHE   B 132 ? 0.2317 0.1953 0.2532 0.0119  0.0036  0.0406  132 PHE   B CZ  
6735 N N   . GLY   B 133 ? 0.2625 0.1845 0.2701 0.0021  0.0456  0.0520  133 GLY   B N   
6736 C CA  . GLY   B 133 ? 0.2786 0.1952 0.2976 -0.0113 0.0393  0.0553  133 GLY   B CA  
6737 C C   . GLY   B 133 ? 0.2806 0.2040 0.3061 -0.0355 0.0556  0.0641  133 GLY   B C   
6738 O O   . GLY   B 133 ? 0.2961 0.2226 0.3426 -0.0554 0.0494  0.0671  133 GLY   B O   
6742 N N   . ALA   B 134 ? 0.2651 0.2046 0.2800 -0.0305 0.0565  0.0387  134 ALA   B N   
6743 C CA  . ALA   B 134 ? 0.2681 0.2036 0.2960 -0.0200 0.0609  0.0344  134 ALA   B CA  
6744 C C   . ALA   B 134 ? 0.2712 0.1885 0.2808 -0.0148 0.0489  0.0497  134 ALA   B C   
6745 O O   . ALA   B 134 ? 0.2674 0.2074 0.2954 0.0061  0.0408  0.0468  134 ALA   B O   
6746 C CB  . ALA   B 134 ? 0.2633 0.2058 0.3138 -0.0197 0.0577  0.0265  134 ALA   B CB  
6752 N N   . ASP   B 135 ? 0.2839 0.1821 0.2833 -0.0160 0.0269  0.0575  135 ASP   B N   
6753 C CA  . ASP   B 135 ? 0.2923 0.1728 0.3104 -0.0172 0.0158  0.0637  135 ASP   B CA  
6754 C C   . ASP   B 135 ? 0.2623 0.1607 0.2981 -0.0056 0.0082  0.0559  135 ASP   B C   
6755 O O   . ASP   B 135 ? 0.2452 0.1615 0.3070 -0.0048 0.0162  0.0506  135 ASP   B O   
6756 C CB  . ASP   B 135 ? 0.3273 0.1802 0.3328 -0.0377 0.0112  0.0680  135 ASP   B CB  
6757 C CG  . ASP   B 135 ? 0.3509 0.1910 0.3724 -0.0604 0.0089  0.0583  135 ASP   B CG  
6758 O OD1 . ASP   B 135 ? 0.3588 0.1842 0.3649 -0.0407 -0.0111 0.0509  135 ASP   B OD1 
6759 O OD2 . ASP   B 135 ? 0.3705 0.2296 0.4400 -0.0744 0.0214  0.0352  135 ASP   B OD2 
6764 N N   . PRO   B 136 ? 0.2479 0.1653 0.2993 0.0178  -0.0135 0.0350  136 PRO   B N   
6765 C CA  . PRO   B 136 ? 0.2224 0.1583 0.2930 0.0133  -0.0077 0.0300  136 PRO   B CA  
6766 C C   . PRO   B 136 ? 0.2007 0.1412 0.2936 0.0117  -0.0032 0.0287  136 PRO   B C   
6767 O O   . PRO   B 136 ? 0.1761 0.1462 0.2766 0.0067  0.0002  0.0165  136 PRO   B O   
6768 C CB  . PRO   B 136 ? 0.2243 0.1791 0.3102 0.0347  -0.0190 0.0217  136 PRO   B CB  
6769 C CG  . PRO   B 136 ? 0.2506 0.1962 0.3359 0.0320  -0.0031 0.0120  136 PRO   B CG  
6770 C CD  . PRO   B 136 ? 0.2568 0.1901 0.3204 0.0350  0.0025  0.0252  136 PRO   B CD  
6778 N N   . ILE   B 137 ? 0.2188 0.1279 0.2990 0.0075  0.0017  0.0206  137 ILE   B N   
6779 C CA  . ILE   B 137 ? 0.2198 0.1259 0.3068 -0.0036 0.0076  0.0059  137 ILE   B CA  
6780 C C   . ILE   B 137 ? 0.2046 0.1380 0.2981 -0.0091 0.0255  0.0147  137 ILE   B C   
6781 O O   . ILE   B 137 ? 0.2052 0.1355 0.2965 -0.0105 0.0211  0.0113  137 ILE   B O   
6782 C CB  . ILE   B 137 ? 0.2516 0.1382 0.3600 -0.0108 0.0117  0.0098  137 ILE   B CB  
6783 C CG1 . ILE   B 137 ? 0.2787 0.1563 0.3932 0.0001  0.0109  0.0034  137 ILE   B CG1 
6784 C CG2 . ILE   B 137 ? 0.2584 0.1420 0.3837 -0.0296 0.0122  0.0128  137 ILE   B CG2 
6785 C CD1 . ILE   B 137 ? 0.3020 0.1757 0.4328 0.0069  0.0058  0.0072  137 ILE   B CD1 
6797 N N   . HIS   B 138 ? 0.2106 0.1445 0.3093 -0.0076 0.0535  0.0178  138 HIS   B N   
6798 C CA  . HIS   B 138 ? 0.2260 0.1474 0.3079 -0.0108 0.0582  0.0196  138 HIS   B CA  
6799 C C   . HIS   B 138 ? 0.2069 0.1458 0.2864 -0.0092 0.0470  0.0395  138 HIS   B C   
6800 O O   . HIS   B 138 ? 0.2025 0.1557 0.3075 -0.0021 0.0467  0.0411  138 HIS   B O   
6801 C CB  . HIS   B 138 ? 0.2637 0.1597 0.3369 -0.0215 0.0850  0.0264  138 HIS   B CB  
6802 C CG  . HIS   B 138 ? 0.2895 0.1808 0.3501 -0.0177 0.1105  0.0386  138 HIS   B CG  
6803 N ND1 . HIS   B 138 ? 0.3006 0.1996 0.3851 -0.0148 0.1175  0.0372  138 HIS   B ND1 
6804 C CD2 . HIS   B 138 ? 0.3085 0.1909 0.3431 -0.0177 0.1180  0.0420  138 HIS   B CD2 
6805 C CE1 . HIS   B 138 ? 0.3052 0.2007 0.3864 -0.0092 0.1213  0.0410  138 HIS   B CE1 
6806 N NE2 . HIS   B 138 ? 0.3123 0.1909 0.3557 -0.0069 0.1245  0.0304  138 HIS   B NE2 
6814 N N   . SER   B 139 ? 0.2038 0.1360 0.2665 0.0024  0.0382  0.0216  139 SER   B N   
6815 C CA  . SER   B 139 ? 0.1966 0.1284 0.2437 0.0023  0.0361  0.0119  139 SER   B CA  
6816 C C   . SER   B 139 ? 0.1774 0.1261 0.2371 -0.0120 0.0199  0.0113  139 SER   B C   
6817 O O   . SER   B 139 ? 0.1630 0.1326 0.2624 -0.0125 0.0098  0.0167  139 SER   B O   
6818 C CB  . SER   B 139 ? 0.2059 0.1409 0.2632 -0.0004 0.0153  -0.0029 139 SER   B CB  
6819 O OG  . SER   B 139 ? 0.2004 0.1333 0.2568 -0.0043 -0.0046 0.0228  139 SER   B OG  
6825 N N   . LEU   B 140 ? 0.1725 0.1209 0.2359 -0.0120 0.0288  0.0042  140 LEU   B N   
6826 C CA  . LEU   B 140 ? 0.1679 0.1279 0.2428 -0.0066 0.0214  0.0108  140 LEU   B CA  
6827 C C   . LEU   B 140 ? 0.1678 0.1234 0.2434 -0.0098 0.0173  0.0076  140 LEU   B C   
6828 O O   . LEU   B 140 ? 0.1693 0.1358 0.2475 -0.0124 0.0066  0.0089  140 LEU   B O   
6829 C CB  . LEU   B 140 ? 0.1636 0.1256 0.2559 -0.0134 0.0320  0.0018  140 LEU   B CB  
6830 C CG  . LEU   B 140 ? 0.1814 0.1308 0.2552 -0.0063 0.0095  0.0093  140 LEU   B CG  
6831 C CD1 . LEU   B 140 ? 0.1926 0.1298 0.2806 -0.0137 0.0150  0.0043  140 LEU   B CD1 
6832 C CD2 . LEU   B 140 ? 0.1964 0.1447 0.2621 -0.0124 -0.0009 -0.0038 140 LEU   B CD2 
6844 N N   . ARG   B 141 ? 0.1705 0.1283 0.2707 -0.0060 0.0208  0.0080  141 ARG   B N   
6845 C CA  . ARG   B 141 ? 0.1732 0.1249 0.3075 -0.0139 0.0342  0.0007  141 ARG   B CA  
6846 C C   . ARG   B 141 ? 0.1619 0.1305 0.2932 -0.0179 0.0169  0.0045  141 ARG   B C   
6847 O O   . ARG   B 141 ? 0.1583 0.1274 0.3002 -0.0201 0.0075  -0.0136 141 ARG   B O   
6848 C CB  . ARG   B 141 ? 0.1827 0.1476 0.3433 -0.0243 0.0422  -0.0013 141 ARG   B CB  
6849 C CG  . ARG   B 141 ? 0.2220 0.1801 0.3629 -0.0175 0.0372  -0.0151 141 ARG   B CG  
6850 C CD  . ARG   B 141 ? 0.2641 0.2012 0.3607 -0.0260 0.0292  -0.0208 141 ARG   B CD  
6851 N NE  . ARG   B 141 ? 0.2871 0.2012 0.3414 -0.0481 0.0365  -0.0183 141 ARG   B NE  
6852 C CZ  . ARG   B 141 ? 0.3072 0.1843 0.3120 -0.0499 0.0413  -0.0320 141 ARG   B CZ  
6853 N NH1 . ARG   B 141 ? 0.3219 0.1786 0.2864 -0.0404 0.0411  -0.0180 141 ARG   B NH1 
6854 N NH2 . ARG   B 141 ? 0.3096 0.2010 0.3368 -0.0324 0.0217  -0.0147 141 ARG   B NH2 
6868 N N   . VAL   B 142 ? 0.1623 0.1327 0.2708 -0.0089 0.0277  -0.0005 142 VAL   B N   
6869 C CA  . VAL   B 142 ? 0.1542 0.1294 0.2814 -0.0101 0.0274  -0.0099 142 VAL   B CA  
6870 C C   . VAL   B 142 ? 0.1543 0.1257 0.2756 -0.0084 0.0140  0.0009  142 VAL   B C   
6871 O O   . VAL   B 142 ? 0.1608 0.1295 0.2672 -0.0030 0.0183  0.0042  142 VAL   B O   
6872 C CB  . VAL   B 142 ? 0.1661 0.1414 0.2753 -0.0068 0.0345  0.0026  142 VAL   B CB  
6873 C CG1 . VAL   B 142 ? 0.1625 0.1436 0.2847 -0.0042 0.0307  0.0017  142 VAL   B CG1 
6874 C CG2 . VAL   B 142 ? 0.1970 0.1332 0.2774 0.0039  0.0283  0.0147  142 VAL   B CG2 
6884 N N   . CYS   B 143 ? 0.1495 0.1302 0.2430 0.0024  0.0095  0.0190  143 CYS   B N   
6885 C CA  . CYS   B 143 ? 0.1411 0.1268 0.2522 -0.0056 0.0087  0.0036  143 CYS   B CA  
6886 C C   . CYS   B 143 ? 0.1422 0.1231 0.2550 -0.0111 -0.0023 -0.0058 143 CYS   B C   
6887 O O   . CYS   B 143 ? 0.1417 0.1377 0.2593 -0.0050 -0.0085 -0.0152 143 CYS   B O   
6888 C CB  . CYS   B 143 ? 0.1520 0.1334 0.2561 -0.0052 0.0047  0.0070  143 CYS   B CB  
6889 S SG  . CYS   B 143 ? 0.1579 0.1509 0.2322 -0.0099 0.0061  0.0037  143 CYS   B SG  
6895 N N   . VAL   B 144 ? 0.1448 0.1241 0.2774 -0.0114 -0.0115 -0.0099 144 VAL   B N   
6896 C CA  . VAL   B 144 ? 0.1560 0.1438 0.2994 -0.0268 -0.0192 -0.0205 144 VAL   B CA  
6897 C C   . VAL   B 144 ? 0.1502 0.1440 0.2972 -0.0161 -0.0129 0.0018  144 VAL   B C   
6898 O O   . VAL   B 144 ? 0.1642 0.1599 0.3271 -0.0006 -0.0071 0.0102  144 VAL   B O   
6899 C CB  . VAL   B 144 ? 0.1834 0.1673 0.3681 -0.0265 -0.0247 -0.0435 144 VAL   B CB  
6900 C CG1 . VAL   B 144 ? 0.2117 0.2107 0.4193 -0.0242 -0.0152 -0.0443 144 VAL   B CG1 
6901 C CG2 . VAL   B 144 ? 0.1898 0.1665 0.3460 -0.0141 -0.0499 -0.0393 144 VAL   B CG2 
6911 N N   . ASP   B 145 ? 0.1521 0.1344 0.3001 -0.0098 -0.0001 -0.0158 145 ASP   B N   
6912 C CA  . ASP   B 145 ? 0.1568 0.1374 0.3412 -0.0085 0.0103  -0.0135 145 ASP   B CA  
6913 C C   . ASP   B 145 ? 0.1438 0.1447 0.3346 -0.0145 0.0083  -0.0123 145 ASP   B C   
6914 O O   . ASP   B 145 ? 0.1470 0.1535 0.3919 -0.0163 0.0109  -0.0167 145 ASP   B O   
6915 C CB  . ASP   B 145 ? 0.1627 0.1410 0.3912 -0.0211 0.0221  0.0055  145 ASP   B CB  
6916 C CG  . ASP   B 145 ? 0.1786 0.1522 0.4489 -0.0284 0.0270  0.0080  145 ASP   B CG  
6917 O OD1 . ASP   B 145 ? 0.1799 0.1597 0.4423 -0.0301 -0.0235 -0.0019 145 ASP   B OD1 
6918 O OD2 . ASP   B 145 ? 0.2073 0.1600 0.4918 -0.0356 0.0446  0.0127  145 ASP   B OD2 
6923 N N   . THR   B 146 ? 0.1418 0.1319 0.2797 -0.0164 -0.0001 -0.0021 146 THR   B N   
6924 C CA  . THR   B 146 ? 0.1390 0.1312 0.2687 -0.0120 0.0167  0.0008  146 THR   B CA  
6925 C C   . THR   B 146 ? 0.1425 0.1274 0.2547 -0.0057 0.0044  0.0071  146 THR   B C   
6926 O O   . THR   B 146 ? 0.1479 0.1318 0.2518 -0.0098 0.0059  0.0040  146 THR   B O   
6927 C CB  . THR   B 146 ? 0.1494 0.1363 0.2612 -0.0106 0.0257  0.0071  146 THR   B CB  
6928 O OG1 . THR   B 146 ? 0.1550 0.1354 0.2594 -0.0050 0.0226  0.0145  146 THR   B OG1 
6929 C CG2 . THR   B 146 ? 0.1619 0.1456 0.2523 -0.0116 0.0142  0.0057  146 THR   B CG2 
6937 N N   . VAL   B 147 ? 0.1500 0.1280 0.2148 -0.0064 0.0106  0.0011  147 VAL   B N   
6938 C CA  . VAL   B 147 ? 0.1499 0.1259 0.2166 -0.0087 -0.0065 -0.0023 147 VAL   B CA  
6939 C C   . VAL   B 147 ? 0.1513 0.1318 0.2458 -0.0226 -0.0178 -0.0072 147 VAL   B C   
6940 O O   . VAL   B 147 ? 0.1590 0.1370 0.2508 -0.0213 -0.0350 -0.0018 147 VAL   B O   
6941 C CB  . VAL   B 147 ? 0.1539 0.1438 0.2063 -0.0060 -0.0117 -0.0023 147 VAL   B CB  
6942 C CG1 . VAL   B 147 ? 0.1490 0.1575 0.2026 -0.0096 -0.0202 0.0060  147 VAL   B CG1 
6943 C CG2 . VAL   B 147 ? 0.1553 0.1463 0.2055 -0.0156 0.0058  0.0023  147 VAL   B CG2 
6953 N N   . ARG   B 148 ? 0.1488 0.1279 0.2288 -0.0135 -0.0153 -0.0072 148 ARG   B N   
6954 C CA  . ARG   B 148 ? 0.1524 0.1422 0.2186 -0.0088 -0.0329 -0.0121 148 ARG   B CA  
6955 C C   . ARG   B 148 ? 0.1565 0.1495 0.2177 -0.0085 -0.0479 -0.0003 148 ARG   B C   
6956 O O   . ARG   B 148 ? 0.1811 0.1829 0.2301 -0.0330 -0.0454 0.0118  148 ARG   B O   
6957 C CB  . ARG   B 148 ? 0.1579 0.1546 0.2355 -0.0057 -0.0255 -0.0097 148 ARG   B CB  
6958 C CG  . ARG   B 148 ? 0.1636 0.1800 0.2411 -0.0100 -0.0336 -0.0283 148 ARG   B CG  
6959 C CD  . ARG   B 148 ? 0.1700 0.1978 0.2693 0.0095  -0.0343 -0.0408 148 ARG   B CD  
6960 N NE  . ARG   B 148 ? 0.1725 0.1919 0.2698 0.0223  -0.0406 -0.0444 148 ARG   B NE  
6961 C CZ  . ARG   B 148 ? 0.1621 0.1795 0.2514 0.0173  -0.0322 -0.0312 148 ARG   B CZ  
6962 N NH1 . ARG   B 148 ? 0.1514 0.1840 0.2538 0.0134  -0.0130 -0.0254 148 ARG   B NH1 
6963 N NH2 . ARG   B 148 ? 0.1779 0.1646 0.2320 0.0194  -0.0251 -0.0315 148 ARG   B NH2 
6977 N N   . THR   B 149 ? 0.1607 0.1416 0.2128 -0.0117 -0.0319 0.0083  149 THR   B N   
6978 C CA  . THR   B 149 ? 0.1705 0.1436 0.1951 -0.0201 -0.0329 0.0127  149 THR   B CA  
6979 C C   . THR   B 149 ? 0.1642 0.1468 0.1742 -0.0248 -0.0336 0.0018  149 THR   B C   
6980 O O   . THR   B 149 ? 0.1733 0.1444 0.1919 -0.0255 -0.0267 0.0120  149 THR   B O   
6981 C CB  . THR   B 149 ? 0.1762 0.1419 0.2023 -0.0194 -0.0372 0.0003  149 THR   B CB  
6982 O OG1 . THR   B 149 ? 0.1738 0.1459 0.1932 -0.0172 -0.0436 -0.0029 149 THR   B OG1 
6983 C CG2 . THR   B 149 ? 0.1835 0.1502 0.2069 -0.0066 -0.0189 0.0085  149 THR   B CG2 
6991 N N   . ASN   B 150 ? 0.1724 0.1470 0.1645 -0.0239 -0.0376 0.0068  150 ASN   B N   
6992 C CA  . ASN   B 150 ? 0.1898 0.1645 0.1535 -0.0310 -0.0415 0.0072  150 ASN   B CA  
6993 C C   . ASN   B 150 ? 0.1770 0.1532 0.1565 -0.0307 -0.0328 0.0026  150 ASN   B C   
6994 O O   . ASN   B 150 ? 0.1864 0.1418 0.1888 -0.0397 -0.0438 0.0013  150 ASN   B O   
6995 C CB  . ASN   B 150 ? 0.2154 0.1959 0.1697 -0.0329 -0.0470 0.0184  150 ASN   B CB  
6996 C CG  . ASN   B 150 ? 0.2411 0.2376 0.2115 -0.0306 -0.0711 0.0467  150 ASN   B CG  
6997 O OD1 . ASN   B 150 ? 0.2523 0.2532 0.2292 -0.0412 -0.0789 0.0373  150 ASN   B OD1 
6998 N ND2 . ASN   B 150 ? 0.2572 0.2575 0.2776 -0.0179 -0.0709 0.0883  150 ASN   B ND2 
7005 N N   . VAL   B 151 ? 0.1716 0.1496 0.1698 -0.0365 -0.0461 0.0098  151 VAL   B N   
7006 C CA  . VAL   B 151 ? 0.1724 0.1463 0.1657 -0.0337 -0.0331 0.0081  151 VAL   B CA  
7007 C C   . VAL   B 151 ? 0.1802 0.1428 0.1492 -0.0389 -0.0287 0.0097  151 VAL   B C   
7008 O O   . VAL   B 151 ? 0.1816 0.1518 0.1967 -0.0347 -0.0257 -0.0035 151 VAL   B O   
7009 C CB  . VAL   B 151 ? 0.1845 0.1573 0.1902 -0.0161 -0.0304 0.0009  151 VAL   B CB  
7010 C CG1 . VAL   B 151 ? 0.1987 0.1692 0.2300 -0.0201 -0.0163 -0.0112 151 VAL   B CG1 
7011 C CG2 . VAL   B 151 ? 0.1857 0.1773 0.1668 -0.0017 -0.0260 0.0204  151 VAL   B CG2 
7021 N N   . TYR   B 152 ? 0.1670 0.1362 0.1520 -0.0317 -0.0228 0.0090  152 TYR   B N   
7022 C CA  . TYR   B 152 ? 0.1667 0.1530 0.1442 -0.0373 -0.0335 0.0031  152 TYR   B CA  
7023 C C   . TYR   B 152 ? 0.1673 0.1365 0.1286 -0.0301 -0.0203 -0.0068 152 TYR   B C   
7024 O O   . TYR   B 152 ? 0.1773 0.1385 0.1409 -0.0306 -0.0203 0.0034  152 TYR   B O   
7025 C CB  . TYR   B 152 ? 0.1899 0.1707 0.1429 -0.0378 -0.0168 0.0211  152 TYR   B CB  
7026 C CG  . TYR   B 152 ? 0.2070 0.1771 0.1521 -0.0576 -0.0278 0.0058  152 TYR   B CG  
7027 C CD1 . TYR   B 152 ? 0.2161 0.1929 0.1420 -0.0554 -0.0310 0.0224  152 TYR   B CD1 
7028 C CD2 . TYR   B 152 ? 0.2286 0.1888 0.1590 -0.0603 -0.0129 0.0063  152 TYR   B CD2 
7029 C CE1 . TYR   B 152 ? 0.2357 0.2148 0.1622 -0.0546 -0.0498 0.0302  152 TYR   B CE1 
7030 C CE2 . TYR   B 152 ? 0.2441 0.2183 0.1689 -0.0669 -0.0325 0.0118  152 TYR   B CE2 
7031 C CZ  . TYR   B 152 ? 0.2438 0.2378 0.1511 -0.0625 -0.0528 0.0390  152 TYR   B CZ  
7032 O OH  . TYR   B 152 ? 0.2639 0.2773 0.1929 -0.0488 -0.0681 0.0488  152 TYR   B OH  
7042 N N   . LEU   B 153 ? 0.1738 0.1308 0.1437 -0.0373 -0.0273 0.0011  153 LEU   B N   
7043 C CA  . LEU   B 153 ? 0.1706 0.1258 0.1432 -0.0302 -0.0111 -0.0052 153 LEU   B CA  
7044 C C   . LEU   B 153 ? 0.1700 0.1301 0.1529 -0.0253 -0.0085 -0.0170 153 LEU   B C   
7045 O O   . LEU   B 153 ? 0.1795 0.1553 0.1701 -0.0134 -0.0164 -0.0293 153 LEU   B O   
7046 C CB  . LEU   B 153 ? 0.1712 0.1287 0.1531 -0.0320 -0.0093 0.0006  153 LEU   B CB  
7047 C CG  . LEU   B 153 ? 0.1625 0.1365 0.1871 -0.0293 -0.0058 -0.0061 153 LEU   B CG  
7048 C CD1 . LEU   B 153 ? 0.1713 0.1494 0.2101 -0.0307 -0.0053 0.0044  153 LEU   B CD1 
7049 C CD2 . LEU   B 153 ? 0.1622 0.1432 0.1909 -0.0209 0.0082  0.0116  153 LEU   B CD2 
7061 N N   . ALA   B 154 ? 0.1640 0.1322 0.1572 -0.0116 -0.0087 -0.0187 154 ALA   B N   
7062 C CA  . ALA   B 154 ? 0.1690 0.1460 0.1786 -0.0124 -0.0084 -0.0170 154 ALA   B CA  
7063 C C   . ALA   B 154 ? 0.1795 0.1528 0.1696 -0.0087 -0.0207 -0.0241 154 ALA   B C   
7064 O O   . ALA   B 154 ? 0.2130 0.1506 0.1939 -0.0019 -0.0073 -0.0001 154 ALA   B O   
7065 C CB  . ALA   B 154 ? 0.1770 0.1566 0.2081 -0.0081 0.0012  -0.0251 154 ALA   B CB  
7071 N N   . VAL   B 155 ? 0.1521 0.1439 0.2128 -0.0148 0.0015  -0.0178 155 VAL   B N   
7072 C CA  . VAL   B 155 ? 0.1520 0.1412 0.2467 -0.0158 -0.0119 -0.0088 155 VAL   B CA  
7073 C C   . VAL   B 155 ? 0.1552 0.1405 0.2207 -0.0075 -0.0057 -0.0135 155 VAL   B C   
7074 O O   . VAL   B 155 ? 0.1718 0.1535 0.2582 0.0024  -0.0043 -0.0443 155 VAL   B O   
7075 C CB  . VAL   B 155 ? 0.1582 0.1536 0.2770 -0.0080 -0.0158 0.0167  155 VAL   B CB  
7076 C CG1 . VAL   B 155 ? 0.1690 0.1582 0.2913 -0.0161 -0.0094 0.0137  155 VAL   B CG1 
7077 C CG2 . VAL   B 155 ? 0.1588 0.1731 0.3091 -0.0044 -0.0165 0.0449  155 VAL   B CG2 
7087 N N   . PHE   B 156 ? 0.1455 0.1533 0.2386 -0.0016 0.0002  -0.0123 156 PHE   B N   
7088 C CA  . PHE   B 156 ? 0.1457 0.1575 0.2667 0.0098  -0.0082 -0.0275 156 PHE   B CA  
7089 C C   . PHE   B 156 ? 0.1501 0.1674 0.3166 0.0125  -0.0091 -0.0418 156 PHE   B C   
7090 O O   . PHE   B 156 ? 0.1729 0.1925 0.3482 0.0211  0.0087  -0.0609 156 PHE   B O   
7091 C CB  . PHE   B 156 ? 0.1484 0.1551 0.2498 0.0017  -0.0065 -0.0160 156 PHE   B CB  
7092 C CG  . PHE   B 156 ? 0.1637 0.1708 0.2589 0.0054  -0.0078 0.0012  156 PHE   B CG  
7093 C CD1 . PHE   B 156 ? 0.1636 0.1906 0.2948 0.0152  0.0072  0.0246  156 PHE   B CD1 
7094 C CD2 . PHE   B 156 ? 0.1695 0.1823 0.2557 0.0132  -0.0110 0.0079  156 PHE   B CD2 
7095 C CE1 . PHE   B 156 ? 0.1738 0.2084 0.3124 0.0130  0.0042  0.0312  156 PHE   B CE1 
7096 C CE2 . PHE   B 156 ? 0.1749 0.2060 0.2935 0.0152  -0.0149 0.0127  156 PHE   B CE2 
7097 C CZ  . PHE   B 156 ? 0.1610 0.2139 0.3157 0.0132  -0.0153 0.0125  156 PHE   B CZ  
7107 N N   . ASP   B 157 ? 0.1548 0.1514 0.3542 0.0168  -0.0270 -0.0131 157 ASP   B N   
7108 C CA  . ASP   B 157 ? 0.1732 0.1607 0.3889 0.0144  -0.0311 -0.0253 157 ASP   B CA  
7109 C C   . ASP   B 157 ? 0.1663 0.1640 0.3998 0.0039  -0.0229 -0.0536 157 ASP   B C   
7110 O O   . ASP   B 157 ? 0.1452 0.1671 0.3807 0.0083  -0.0186 -0.0431 157 ASP   B O   
7111 C CB  . ASP   B 157 ? 0.2077 0.1846 0.4141 0.0096  -0.0533 -0.0083 157 ASP   B CB  
7112 C CG  . ASP   B 157 ? 0.2504 0.1968 0.4416 0.0032  -0.0494 -0.0081 157 ASP   B CG  
7113 O OD1 . ASP   B 157 ? 0.2562 0.1932 0.4622 0.0178  -0.0370 0.0030  157 ASP   B OD1 
7114 O OD2 . ASP   B 157 ? 0.2782 0.2191 0.4624 0.0028  -0.0351 -0.0022 157 ASP   B OD2 
7119 N N   . LYS   B 158 ? 0.1721 0.1930 0.4106 0.0016  -0.0094 -0.0783 158 LYS   B N   
7120 C CA  . LYS   B 158 ? 0.1889 0.2212 0.4108 0.0006  0.0116  -0.1042 158 LYS   B CA  
7121 C C   . LYS   B 158 ? 0.1850 0.2098 0.4162 0.0053  0.0024  -0.0963 158 LYS   B C   
7122 O O   . LYS   B 158 ? 0.1800 0.2147 0.4229 -0.0020 0.0033  -0.1023 158 LYS   B O   
7123 C CB  . LYS   B 158 ? 0.2141 0.2699 0.4118 0.0050  0.0257  -0.1327 158 LYS   B CB  
7124 C CG  . LYS   B 158 ? 0.2484 0.3282 0.4077 0.0093  0.0271  -0.1574 158 LYS   B CG  
7125 C CD  . LYS   B 158 ? 0.2796 0.3936 0.4139 0.0065  0.0245  -0.1574 158 LYS   B CD  
7126 C CE  . LYS   B 158 ? 0.3017 0.4284 0.4288 0.0077  0.0288  -0.1503 158 LYS   B CE  
7127 N NZ  . LYS   B 158 ? 0.3039 0.4565 0.4259 0.0057  0.0384  -0.1508 158 LYS   B NZ  
7141 N N   . ASN   B 159 ? 0.1879 0.1985 0.4412 0.0026  -0.0150 -0.0776 159 ASN   B N   
7142 C CA  . ASN   B 159 ? 0.2127 0.1913 0.4518 0.0207  -0.0476 -0.0617 159 ASN   B CA  
7143 C C   . ASN   B 159 ? 0.1876 0.1607 0.4371 0.0075  -0.0665 -0.0537 159 ASN   B C   
7144 O O   . ASN   B 159 ? 0.1898 0.1559 0.4540 -0.0065 -0.0749 -0.0268 159 ASN   B O   
7145 C CB  . ASN   B 159 ? 0.2513 0.2161 0.4759 0.0450  -0.0648 -0.0571 159 ASN   B CB  
7146 C CG  . ASN   B 159 ? 0.2795 0.2421 0.5051 0.0564  -0.0818 -0.0610 159 ASN   B CG  
7147 O OD1 . ASN   B 159 ? 0.2985 0.2656 0.5198 0.0714  -0.0836 -0.0709 159 ASN   B OD1 
7148 N ND2 . ASN   B 159 ? 0.2866 0.2682 0.5180 0.0623  -0.0977 -0.0592 159 ASN   B ND2 
7155 N N   . LEU   B 160 ? 0.1717 0.1627 0.4223 0.0039  -0.0597 -0.0496 160 LEU   B N   
7156 C CA  . LEU   B 160 ? 0.1653 0.1617 0.3802 0.0070  -0.0461 -0.0231 160 LEU   B CA  
7157 C C   . LEU   B 160 ? 0.1562 0.1516 0.3472 0.0022  -0.0287 -0.0319 160 LEU   B C   
7158 O O   . LEU   B 160 ? 0.1454 0.1639 0.3243 -0.0017 -0.0345 -0.0095 160 LEU   B O   
7159 C CB  . LEU   B 160 ? 0.1628 0.1767 0.3626 -0.0009 -0.0494 -0.0062 160 LEU   B CB  
7160 C CG  . LEU   B 160 ? 0.1589 0.1916 0.3274 0.0027  -0.0429 0.0101  160 LEU   B CG  
7161 C CD1 . LEU   B 160 ? 0.1792 0.2097 0.3374 -0.0084 -0.0168 0.0190  160 LEU   B CD1 
7162 C CD2 . LEU   B 160 ? 0.1604 0.1923 0.3091 0.0210  -0.0392 0.0033  160 LEU   B CD2 
7174 N N   . TYR   B 161 ? 0.1598 0.1552 0.3646 -0.0086 -0.0125 -0.0567 161 TYR   B N   
7175 C CA  . TYR   B 161 ? 0.1738 0.1622 0.3517 -0.0195 0.0226  -0.0573 161 TYR   B CA  
7176 C C   . TYR   B 161 ? 0.1808 0.1559 0.3231 -0.0068 0.0319  -0.0400 161 TYR   B C   
7177 O O   . TYR   B 161 ? 0.1836 0.1635 0.3065 -0.0289 0.0213  -0.0345 161 TYR   B O   
7178 C CB  . TYR   B 161 ? 0.1839 0.1638 0.3607 -0.0300 0.0430  -0.0680 161 TYR   B CB  
7179 C CG  . TYR   B 161 ? 0.2148 0.1683 0.3619 -0.0433 0.0514  -0.0592 161 TYR   B CG  
7180 C CD1 . TYR   B 161 ? 0.2252 0.1749 0.3591 -0.0449 0.0496  -0.0584 161 TYR   B CD1 
7181 C CD2 . TYR   B 161 ? 0.2415 0.1800 0.3483 -0.0318 0.0426  -0.0649 161 TYR   B CD2 
7182 C CE1 . TYR   B 161 ? 0.2455 0.1904 0.3401 -0.0448 0.0458  -0.0646 161 TYR   B CE1 
7183 C CE2 . TYR   B 161 ? 0.2622 0.1965 0.3505 -0.0302 0.0417  -0.0613 161 TYR   B CE2 
7184 C CZ  . TYR   B 161 ? 0.2652 0.1992 0.3367 -0.0471 0.0366  -0.0601 161 TYR   B CZ  
7185 O OH  . TYR   B 161 ? 0.2925 0.2279 0.3602 -0.0535 0.0354  -0.0577 161 TYR   B OH  
7195 N N   . ASP   B 162 ? 0.1832 0.1579 0.3440 -0.0100 0.0103  -0.0642 162 ASP   B N   
7196 C CA  . ASP   B 162 ? 0.1927 0.1619 0.3503 -0.0101 -0.0011 -0.0651 162 ASP   B CA  
7197 C C   . ASP   B 162 ? 0.1863 0.1538 0.3367 -0.0128 -0.0086 -0.0356 162 ASP   B C   
7198 O O   . ASP   B 162 ? 0.1921 0.1613 0.3551 -0.0240 -0.0305 -0.0165 162 ASP   B O   
7199 C CB  . ASP   B 162 ? 0.2108 0.1826 0.3748 -0.0050 -0.0146 -0.0879 162 ASP   B CB  
7200 C CG  . ASP   B 162 ? 0.2199 0.2054 0.3982 0.0105  -0.0068 -0.1022 162 ASP   B CG  
7201 O OD1 . ASP   B 162 ? 0.2296 0.2327 0.3825 -0.0004 0.0126  -0.0880 162 ASP   B OD1 
7202 O OD2 . ASP   B 162 ? 0.2263 0.2321 0.4410 0.0273  -0.0048 -0.0871 162 ASP   B OD2 
7207 N N   A LYS   B 163 ? 0.1849 0.1499 0.3275 -0.0136 -0.0154 -0.0261 163 LYS   B N   
7208 N N   B LYS   B 163 ? 0.1799 0.1389 0.3226 -0.0173 -0.0162 -0.0244 163 LYS   B N   
7209 C CA  A LYS   B 163 ? 0.1916 0.1697 0.3301 -0.0152 -0.0138 -0.0103 163 LYS   B CA  
7210 C CA  B LYS   B 163 ? 0.1866 0.1601 0.3230 -0.0222 -0.0137 -0.0019 163 LYS   B CA  
7211 C C   A LYS   B 163 ? 0.1670 0.1546 0.3166 -0.0163 -0.0186 0.0007  163 LYS   B C   
7212 C C   B LYS   B 163 ? 0.1609 0.1500 0.3140 -0.0187 -0.0209 0.0131  163 LYS   B C   
7213 O O   A LYS   B 163 ? 0.1698 0.1613 0.3283 -0.0230 -0.0230 0.0030  163 LYS   B O   
7214 O O   B LYS   B 163 ? 0.1628 0.1618 0.3353 -0.0237 -0.0287 0.0255  163 LYS   B O   
7215 C CB  A LYS   B 163 ? 0.2337 0.2104 0.3649 -0.0131 -0.0120 -0.0012 163 LYS   B CB  
7216 C CB  B LYS   B 163 ? 0.2353 0.2021 0.3585 -0.0238 -0.0104 0.0131  163 LYS   B CB  
7217 C CG  A LYS   B 163 ? 0.2917 0.2603 0.4046 -0.0122 -0.0060 -0.0002 163 LYS   B CG  
7218 C CG  B LYS   B 163 ? 0.3096 0.2569 0.4010 -0.0247 -0.0026 0.0134  163 LYS   B CG  
7219 C CD  A LYS   B 163 ? 0.3321 0.3063 0.4466 -0.0153 -0.0041 -0.0031 163 LYS   B CD  
7220 C CD  B LYS   B 163 ? 0.3672 0.3112 0.4515 -0.0305 -0.0010 0.0114  163 LYS   B CD  
7221 C CE  A LYS   B 163 ? 0.3697 0.3402 0.4766 -0.0172 -0.0001 -0.0048 163 LYS   B CE  
7222 C CE  B LYS   B 163 ? 0.4097 0.3541 0.4872 -0.0349 0.0036  0.0097  163 LYS   B CE  
7223 N NZ  A LYS   B 163 ? 0.3860 0.3444 0.4952 -0.0182 0.0017  -0.0084 163 LYS   B NZ  
7224 N NZ  B LYS   B 163 ? 0.4357 0.3562 0.5072 -0.0365 0.0056  0.0043  163 LYS   B NZ  
7251 N N   . LEU   B 164 ? 0.1539 0.1404 0.2950 -0.0158 -0.0220 0.0038  164 LEU   B N   
7252 C CA  . LEU   B 164 ? 0.1496 0.1418 0.2757 -0.0104 -0.0209 0.0059  164 LEU   B CA  
7253 C C   . LEU   B 164 ? 0.1654 0.1478 0.2820 -0.0101 -0.0325 0.0200  164 LEU   B C   
7254 O O   . LEU   B 164 ? 0.1705 0.1717 0.3090 -0.0131 -0.0373 0.0304  164 LEU   B O   
7255 C CB  . LEU   B 164 ? 0.1499 0.1392 0.2669 -0.0119 -0.0048 -0.0007 164 LEU   B CB  
7256 C CG  . LEU   B 164 ? 0.1614 0.1564 0.2681 -0.0091 -0.0087 0.0082  164 LEU   B CG  
7257 C CD1 . LEU   B 164 ? 0.1630 0.1580 0.2666 -0.0222 -0.0158 -0.0044 164 LEU   B CD1 
7258 C CD2 . LEU   B 164 ? 0.1813 0.1790 0.2884 -0.0051 -0.0062 0.0017  164 LEU   B CD2 
7271 N N   . VAL   B 165 ? 0.1982 0.1544 0.3044 -0.0248 -0.0458 0.0013  165 VAL   B N   
7272 C CA  . VAL   B 165 ? 0.2420 0.1618 0.3319 -0.0481 -0.0816 0.0102  165 VAL   B CA  
7273 C C   . VAL   B 165 ? 0.2805 0.1766 0.3692 -0.0548 -0.1094 0.0321  165 VAL   B C   
7274 O O   . VAL   B 165 ? 0.3083 0.1984 0.3733 -0.0558 -0.1230 0.0331  165 VAL   B O   
7275 C CB  . VAL   B 165 ? 0.2677 0.1744 0.3435 -0.0224 -0.0548 -0.0092 165 VAL   B CB  
7276 C CG1 . VAL   B 165 ? 0.2860 0.1882 0.3685 -0.0175 -0.0383 -0.0052 165 VAL   B CG1 
7277 C CG2 . VAL   B 165 ? 0.2628 0.1699 0.3412 -0.0174 -0.0437 -0.0117 165 VAL   B CG2 
7287 N N   . SER   B 166 ? 0.2900 0.1605 0.4032 -0.0566 -0.1301 0.0059  166 SER   B N   
7288 C CA  . SER   B 166 ? 0.2852 0.1709 0.4579 -0.0442 -0.1052 -0.0085 166 SER   B CA  
7289 C C   . SER   B 166 ? 0.2612 0.1874 0.4702 -0.0565 -0.0910 0.0116  166 SER   B C   
7290 O O   . SER   B 166 ? 0.2586 0.2082 0.5016 -0.0759 -0.1018 -0.0249 166 SER   B O   
7291 C CB  . SER   B 166 ? 0.2877 0.1718 0.4977 -0.0447 -0.0941 -0.0203 166 SER   B CB  
7292 O OG  . SER   B 166 ? 0.2770 0.1757 0.5266 -0.0362 -0.1061 -0.0131 166 SER   B OG  
7298 N N   . SER   B 167 ? 0.2420 0.1774 0.4316 -0.0552 -0.0994 0.0496  167 SER   B N   
7299 C CA  . SER   B 167 ? 0.2340 0.1903 0.4223 -0.0452 -0.0754 0.0572  167 SER   B CA  
7300 C C   . SER   B 167 ? 0.2184 0.1939 0.3905 -0.0618 -0.0721 0.0696  167 SER   B C   
7301 O O   . SER   B 167 ? 0.2237 0.2137 0.3884 -0.0579 -0.0693 0.0695  167 SER   B O   
7302 C CB  . SER   B 167 ? 0.2213 0.1938 0.4421 -0.0435 -0.0467 0.0621  167 SER   B CB  
7303 O OG  . SER   B 167 ? 0.2163 0.2110 0.4304 -0.0431 -0.0341 0.0558  167 SER   B OG  
7309 N N   . PHE   B 168 ? 0.2212 0.1937 0.3925 -0.0556 -0.0583 0.0724  168 PHE   B N   
7310 C CA  . PHE   B 168 ? 0.2256 0.1888 0.3496 -0.0558 -0.0492 0.0438  168 PHE   B CA  
7311 C C   . PHE   B 168 ? 0.1956 0.1725 0.2749 -0.0236 -0.0376 0.0252  168 PHE   B C   
7312 O O   . PHE   B 168 ? 0.2279 0.1653 0.2630 -0.0031 -0.0078 -0.0012 168 PHE   B O   
7313 C CB  . PHE   B 168 ? 0.2441 0.1962 0.3553 -0.0670 -0.0598 0.0630  168 PHE   B CB  
7314 C CG  . PHE   B 168 ? 0.2754 0.1808 0.3470 -0.0624 -0.0562 0.0396  168 PHE   B CG  
7315 C CD1 . PHE   B 168 ? 0.3042 0.1901 0.3767 -0.0577 -0.0570 0.0263  168 PHE   B CD1 
7316 C CD2 . PHE   B 168 ? 0.2658 0.1747 0.3471 -0.0584 -0.0549 0.0413  168 PHE   B CD2 
7317 C CE1 . PHE   B 168 ? 0.3118 0.1901 0.3600 -0.0538 -0.0483 0.0371  168 PHE   B CE1 
7318 C CE2 . PHE   B 168 ? 0.2873 0.1777 0.3297 -0.0459 -0.0604 0.0285  168 PHE   B CE2 
7319 C CZ  . PHE   B 168 ? 0.3026 0.1781 0.3424 -0.0378 -0.0645 0.0460  168 PHE   B CZ  
7329 N N   . LEU   B 169 ? 0.2003 0.1834 0.2542 -0.0069 -0.0143 0.0133  169 LEU   B N   
7330 C CA  . LEU   B 169 ? 0.2308 0.2052 0.2925 -0.0053 -0.0024 -0.0262 169 LEU   B CA  
7331 C C   . LEU   B 169 ? 0.2646 0.2335 0.3618 0.0165  -0.0089 -0.0576 169 LEU   B C   
7332 O O   . LEU   B 169 ? 0.2824 0.2585 0.4282 0.0110  -0.0130 -0.0777 169 LEU   B O   
7333 C CB  . LEU   B 169 ? 0.2495 0.2504 0.3046 -0.0088 0.0063  0.0061  169 LEU   B CB  
7334 C CG  . LEU   B 169 ? 0.2858 0.2910 0.3582 -0.0017 0.0195  0.0105  169 LEU   B CG  
7335 C CD1 . LEU   B 169 ? 0.2957 0.3060 0.3569 -0.0074 0.0168  0.0235  169 LEU   B CD1 
7336 C CD2 . LEU   B 169 ? 0.2775 0.2934 0.3496 0.0152  0.0489  -0.0027 169 LEU   B CD2 
7337 O OXT . LEU   B 169 ? 0.2891 0.2513 0.3624 0.0507  0.0045  -0.0563 169 LEU   B OXT 
7349 C C1  T TFA   C .   ? 0.1351 0.1434 0.1428 -0.0263 0.0229  0.0177  201 TFA   A C1  
7350 C C2  T TFA   C .   ? 0.1646 0.1605 0.1720 -0.0259 0.0061  0.0098  201 TFA   A C2  
7351 O O   T TFA   C .   ? 0.1286 0.1282 0.1347 -0.0318 0.0298  0.0226  201 TFA   A O   
7352 F F1  T TFA   C .   ? 0.1704 0.1597 0.2177 -0.0219 -0.0152 0.0151  201 TFA   A F1  
7353 F F2  T TFA   C .   ? 0.1728 0.1684 0.1510 -0.0301 -0.0005 0.0179  201 TFA   A F2  
7354 F F3  T TFA   C .   ? 0.1804 0.1720 0.1978 -0.0292 0.0247  -0.0033 201 TFA   A F3  
7355 O OXT T TFA   C .   ? 0.1175 0.1376 0.1404 -0.0094 0.0253  0.0183  201 TFA   A OXT 
7356 N N2  B A1A8G D .   ? 0.1908 0.1842 0.2612 0.0032  -0.0210 0.0122  202 A1A8G A N2  
7357 C C3  B A1A8G D .   ? 0.2693 0.2328 0.2865 0.0174  -0.0152 -0.0101 202 A1A8G A C3  
7358 C C6  B A1A8G D .   ? 0.3071 0.2609 0.3044 0.0362  -0.0027 0.0077  202 A1A8G A C6  
7359 C C9  B A1A8G D .   ? 0.2910 0.2419 0.2718 0.0419  -0.0023 0.0122  202 A1A8G A C9  
7360 C C12 B A1A8G D .   ? 0.1788 0.1741 0.2487 0.0028  -0.0053 0.0397  202 A1A8G A C12 
7361 C C14 B A1A8G D .   ? 0.1691 0.1738 0.1908 0.0151  -0.0071 0.0372  202 A1A8G A C14 
7362 C C1  B A1A8G D .   ? 0.2545 0.2244 0.2833 0.0057  -0.0166 -0.0147 202 A1A8G A C1  
7363 C C10 B A1A8G D .   ? 0.2519 0.2028 0.2561 0.0267  -0.0106 0.0024  202 A1A8G A C10 
7364 C C11 B A1A8G D .   ? 0.2013 0.1932 0.2390 0.0165  -0.0156 0.0148  202 A1A8G A C11 
7365 C C13 B A1A8G D .   ? 0.1630 0.1577 0.1983 0.0058  0.0044  0.0396  202 A1A8G A C13 
7366 C C15 B A1A8G D .   ? 0.1501 0.1738 0.1720 0.0157  0.0138  0.0344  202 A1A8G A C15 
7367 C C16 B A1A8G D .   ? 0.1500 0.1622 0.1819 0.0026  -0.0092 0.0386  202 A1A8G A C16 
7368 C C2  B A1A8G D .   ? 0.2510 0.2184 0.2834 0.0140  -0.0204 -0.0095 202 A1A8G A C2  
7369 C C4  B A1A8G D .   ? 0.2791 0.2349 0.2780 0.0292  -0.0088 -0.0001 202 A1A8G A C4  
7370 C C5  B A1A8G D .   ? 0.3009 0.2462 0.3054 0.0311  -0.0026 0.0046  202 A1A8G A C5  
7371 C C7  B A1A8G D .   ? 0.3057 0.2636 0.2998 0.0404  -0.0016 0.0114  202 A1A8G A C7  
7372 C C8  B A1A8G D .   ? 0.3021 0.2523 0.2722 0.0430  -0.0032 0.0209  202 A1A8G A C8  
7373 N N1  B A1A8G D .   ? 0.2340 0.2027 0.2611 0.0151  -0.0250 0.0042  202 A1A8G A N1  
7374 N N3  B A1A8G D .   ? 0.1724 0.1609 0.2111 -0.0002 0.0068  0.0472  202 A1A8G A N3  
7375 N N4  B A1A8G D .   ? 0.1570 0.1519 0.1859 0.0036  -0.0117 0.0432  202 A1A8G A N4  
7376 O O1  B A1A8G D .   ? 0.2475 0.2286 0.2967 -0.0049 -0.0181 -0.0139 202 A1A8G A O1  
7399 O O   . HOH   E .   ? 0.3325 0.6897 0.6896 0.1981  0.0284  0.1886  301 HOH   A O   
7400 O O   . HOH   E .   ? 0.4064 0.2520 0.4317 -0.0648 -0.1102 0.0214  302 HOH   A O   
7401 O O   . HOH   E .   ? 0.4520 0.3772 0.4975 -0.0098 0.1736  -0.0206 303 HOH   A O   
7402 O O   A HOH   E .   ? 0.3099 0.5404 0.4375 -0.0519 -0.0158 0.1731  304 HOH   A O   
7403 O O   . HOH   E .   ? 0.5299 0.4980 0.6715 -0.0490 0.0838  0.2073  305 HOH   A O   
7404 O O   . HOH   E .   ? 0.6688 0.8715 0.8095 -0.1303 -0.1376 -0.0538 306 HOH   A O   
7405 O O   . HOH   E .   ? 0.4152 0.3723 0.4143 -0.1475 -0.0121 0.1376  307 HOH   A O   
7406 O O   . HOH   E .   ? 0.4253 0.4355 0.5426 0.2317  0.1269  0.1314  308 HOH   A O   
7407 O O   . HOH   E .   ? 0.3362 0.3381 0.1866 -0.0351 0.0407  0.0700  309 HOH   A O   
7408 O O   . HOH   E .   ? 0.6718 0.4446 0.3198 0.1547  -0.0599 0.0809  310 HOH   A O   
7409 O O   . HOH   E .   ? 0.2938 0.3553 0.2797 -0.1382 -0.0765 0.1618  311 HOH   A O   
7410 O O   . HOH   E .   ? 0.3326 0.5018 0.5893 0.0256  0.1098  0.2984  312 HOH   A O   
7411 O O   . HOH   E .   ? 0.5934 0.7975 0.5007 -0.0416 0.2666  -0.1602 313 HOH   A O   
7412 O O   . HOH   E .   ? 0.2505 0.3426 0.3344 -0.0233 0.0976  -0.0160 314 HOH   A O   
7413 O O   . HOH   E .   ? 0.2076 0.1922 0.4172 0.0139  0.1009  -0.0083 315 HOH   A O   
7414 O O   . HOH   E .   ? 0.6855 0.5994 0.8214 -0.1406 -0.0837 0.1017  316 HOH   A O   
7415 O O   . HOH   E .   ? 0.5735 0.5281 0.6408 -0.0922 0.2030  0.2419  317 HOH   A O   
7416 O O   . HOH   E .   ? 0.6634 0.6761 0.3713 -0.1121 -0.1010 0.1138  318 HOH   A O   
7417 O O   . HOH   E .   ? 0.7049 0.4894 0.4810 0.0459  0.0300  -0.0454 319 HOH   A O   
7418 O O   . HOH   E .   ? 0.4493 0.5312 0.4334 0.2039  0.0052  -0.1301 320 HOH   A O   
7419 O O   . HOH   E .   ? 0.2478 0.3401 0.3748 -0.0363 -0.0927 0.1141  321 HOH   A O   
7420 O O   A HOH   E .   ? 0.3205 0.3566 0.2341 -0.0621 0.0090  0.0180  322 HOH   A O   
7421 O O   . HOH   E .   ? 0.5412 0.8120 0.3374 -0.0816 -0.0901 -0.0726 323 HOH   A O   
7422 O O   . HOH   E .   ? 0.7397 0.6350 0.6955 -0.1040 -0.1252 0.1419  324 HOH   A O   
7423 O O   . HOH   E .   ? 0.2021 0.3129 0.3418 0.0457  -0.0325 -0.0209 325 HOH   A O   
7424 O O   . HOH   E .   ? 0.4160 0.3728 0.4483 -0.0783 -0.0371 -0.0424 326 HOH   A O   
7425 O O   . HOH   E .   ? 0.4215 0.4131 0.4420 -0.1866 -0.1204 0.2103  327 HOH   A O   
7426 O O   . HOH   E .   ? 0.4305 0.4364 0.5333 -0.1342 -0.1181 -0.0949 328 HOH   A O   
7427 O O   . HOH   E .   ? 0.3125 0.6486 0.3950 0.0189  0.0401  0.2810  329 HOH   A O   
7428 O O   . HOH   E .   ? 0.2496 0.1950 0.1850 -0.0468 0.0254  0.0279  330 HOH   A O   
7429 O O   . HOH   E .   ? 0.2239 0.1728 0.3027 -0.0398 0.0096  0.0046  331 HOH   A O   
7430 O O   . HOH   E .   ? 0.3068 0.7946 0.4619 0.0470  -0.0436 0.0990  332 HOH   A O   
7431 O O   . HOH   E .   ? 0.2368 0.1971 0.2464 0.0481  -0.0506 -0.0156 333 HOH   A O   
7432 O O   . HOH   E .   ? 0.3004 0.2925 0.5125 -0.0278 -0.1253 0.1259  334 HOH   A O   
7433 O O   A HOH   E .   ? 0.1840 0.1914 0.3254 0.0134  -0.0616 0.0500  335 HOH   A O   
7434 O O   . HOH   E .   ? 0.4468 0.2853 0.2897 -0.1002 0.0139  0.0319  336 HOH   A O   
7435 O O   . HOH   E .   ? 0.3452 0.3915 0.2329 -0.1147 -0.0176 -0.0560 337 HOH   A O   
7436 O O   . HOH   E .   ? 0.3319 0.4328 0.6642 -0.1013 0.2247  -0.1037 338 HOH   A O   
7437 O O   A HOH   E .   ? 0.3359 0.3499 0.2422 -0.1254 0.0028  0.0828  339 HOH   A O   
7438 O O   . HOH   E .   ? 0.5638 0.3961 0.6011 0.2012  -0.1052 -0.0019 340 HOH   A O   
7439 O O   . HOH   E .   ? 0.1924 0.2297 0.3821 0.0075  -0.0527 -0.0523 341 HOH   A O   
7440 O O   . HOH   E .   ? 0.2423 0.2060 0.2645 0.0388  0.0342  0.0280  342 HOH   A O   
7441 O O   . HOH   E .   ? 0.4387 0.8771 0.4626 0.1874  -0.0578 0.0470  343 HOH   A O   
7442 O O   . HOH   E .   ? 0.3859 0.8575 0.3442 -0.1156 0.0073  0.1021  344 HOH   A O   
7443 O O   . HOH   E .   ? 0.3700 0.4394 0.2167 -0.0431 0.0906  0.0348  345 HOH   A O   
7444 O O   . HOH   E .   ? 0.6881 0.3168 0.3245 0.0385  -0.0141 0.0973  346 HOH   A O   
7445 O O   . HOH   E .   ? 0.3321 0.2589 0.3462 -0.0372 0.0635  -0.0449 347 HOH   A O   
7446 O O   . HOH   E .   ? 0.5481 0.2258 0.6888 0.1006  -0.0841 -0.0433 348 HOH   A O   
7447 O O   . HOH   E .   ? 0.2443 0.4064 0.3861 0.1039  -0.0734 -0.0625 349 HOH   A O   
7448 O O   A HOH   E .   ? 0.1469 0.2502 0.1842 0.0678  0.0368  0.0626  350 HOH   A O   
7449 O O   . HOH   E .   ? 0.1878 0.2658 0.3602 0.0345  0.0556  -0.0487 351 HOH   A O   
7450 O O   . HOH   E .   ? 0.1504 0.2022 0.2407 -0.0025 -0.0084 0.0514  352 HOH   A O   
7451 O O   . HOH   E .   ? 0.4916 0.4945 0.4011 -0.0006 -0.1797 -0.0180 353 HOH   A O   
7452 O O   . HOH   E .   ? 0.6145 0.2045 0.4083 0.0022  -0.1992 0.0507  354 HOH   A O   
7453 O O   B HOH   E .   ? 0.1912 0.2056 0.1934 0.0218  -0.0032 0.0302  355 HOH   A O   
7454 O O   . HOH   E .   ? 0.1482 0.1436 0.1897 0.0007  0.0068  0.0177  356 HOH   A O   
7455 O O   A HOH   E .   ? 0.1730 0.3009 0.2483 0.0192  0.0542  0.0425  357 HOH   A O   
7456 O O   . HOH   E .   ? 0.7075 0.8258 0.4115 0.1935  -0.0354 -0.0621 358 HOH   A O   
7457 O O   . HOH   E .   ? 0.1916 0.2194 0.2423 -0.0061 -0.0306 0.0434  359 HOH   A O   
7458 O O   A HOH   E .   ? 0.1970 0.2076 0.2783 -0.0181 -0.0434 0.0519  360 HOH   A O   
7459 O O   . HOH   E .   ? 0.2232 0.2225 0.2804 -0.0230 -0.0370 0.0736  361 HOH   A O   
7460 O O   . HOH   E .   ? 0.3537 0.2559 0.3995 -0.0051 0.0031  0.1043  362 HOH   A O   
7461 O O   . HOH   E .   ? 0.3115 0.4024 0.5304 0.0617  0.1150  -0.0195 363 HOH   A O   
7462 O O   . HOH   E .   ? 0.4441 0.3048 0.5663 -0.1095 -0.0057 -0.0430 364 HOH   A O   
7463 O O   . HOH   E .   ? 0.1832 0.1784 0.2173 0.0084  -0.0257 0.0248  365 HOH   A O   
7464 O O   . HOH   E .   ? 0.3365 0.4130 0.5376 -0.1676 -0.1001 0.0175  366 HOH   A O   
7465 O O   . HOH   E .   ? 0.1790 0.1502 0.1613 -0.0201 0.0125  -0.0009 367 HOH   A O   
7466 O O   A HOH   E .   ? 0.1636 0.1688 0.2174 -0.0149 0.0342  0.0760  368 HOH   A O   
7467 O O   . HOH   E .   ? 0.5225 0.2748 0.4555 -0.1813 0.1008  0.0231  369 HOH   A O   
7468 O O   . HOH   E .   ? 0.2462 0.3510 0.5023 -0.0436 0.0724  -0.0761 370 HOH   A O   
7469 O O   . HOH   E .   ? 0.3481 0.6740 0.3488 0.1366  0.1093  -0.0694 371 HOH   A O   
7470 O O   . HOH   E .   ? 0.1694 0.1522 0.2154 -0.0119 0.0276  -0.0092 372 HOH   A O   
7471 O O   . HOH   E .   ? 0.1545 0.1985 0.2501 0.0068  0.0013  0.0069  373 HOH   A O   
7472 O O   . HOH   E .   ? 0.1513 0.1548 0.1625 0.0011  -0.0180 -0.0006 374 HOH   A O   
7473 O O   B HOH   E .   ? 0.2696 0.6017 0.4069 0.0581  -0.1182 -0.1011 375 HOH   A O   
7474 O O   . HOH   E .   ? 0.1857 0.1878 0.2774 -0.0271 0.0181  0.0299  376 HOH   A O   
7475 O O   . HOH   E .   ? 0.3079 0.2396 0.2885 -0.0447 -0.1160 0.0410  377 HOH   A O   
7476 O O   . HOH   E .   ? 0.1800 0.1936 0.2474 -0.0223 0.0202  0.0241  378 HOH   A O   
7477 O O   A HOH   E .   ? 0.3120 0.1819 0.2229 -0.0192 0.0291  -0.0019 379 HOH   A O   
7478 O O   . HOH   E .   ? 0.6217 0.7321 0.5594 -0.1002 0.0778  0.1500  380 HOH   A O   
7479 O O   . HOH   E .   ? 0.2463 0.2323 0.2259 -0.0274 0.0224  0.0007  381 HOH   A O   
7480 O O   . HOH   E .   ? 0.5397 0.7073 0.2121 0.0150  -0.0069 -0.0433 382 HOH   A O   
7481 O O   . HOH   E .   ? 0.4387 0.8246 0.6608 -0.1101 -0.1694 0.1160  383 HOH   A O   
7482 O O   . HOH   E .   ? 0.3277 0.7579 0.3978 -0.0031 -0.0648 -0.0389 384 HOH   A O   
7483 O O   . HOH   E .   ? 0.3147 0.2965 0.2051 0.0147  0.0579  0.0230  385 HOH   A O   
7484 O O   . HOH   E .   ? 0.1468 0.1484 0.1921 0.0022  -0.0171 0.0097  386 HOH   A O   
7485 O O   . HOH   E .   ? 0.1650 0.1869 0.2007 0.0251  -0.0394 -0.0334 387 HOH   A O   
7486 O O   . HOH   E .   ? 0.6070 0.4819 0.3875 -0.1836 -0.1061 0.1584  388 HOH   A O   
7487 O O   . HOH   E .   ? 0.3722 0.2047 0.3596 -0.0951 0.1242  -0.0293 389 HOH   A O   
7488 O O   . HOH   E .   ? 0.2141 0.1789 0.1872 -0.0160 0.0149  0.0242  390 HOH   A O   
7489 O O   A HOH   E .   ? 0.1770 0.2475 0.3535 -0.0174 0.0161  -0.0070 391 HOH   A O   
7490 O O   . HOH   E .   ? 0.2874 0.3871 0.3510 -0.0887 0.1174  -0.0172 392 HOH   A O   
7491 O O   . HOH   E .   ? 0.3416 0.6732 0.3457 -0.0344 -0.0085 0.1263  393 HOH   A O   
7492 O O   . HOH   E .   ? 0.5280 0.6267 0.5203 0.1884  -0.0545 -0.1678 394 HOH   A O   
7493 O O   . HOH   E .   ? 0.5487 0.4193 0.3736 -0.0745 -0.1356 -0.0182 395 HOH   A O   
7494 O O   . HOH   E .   ? 0.2533 0.1816 0.3662 0.0045  -0.0418 0.0066  396 HOH   A O   
7495 O O   . HOH   E .   ? 0.2483 0.2084 0.2760 -0.0590 -0.0007 0.0457  397 HOH   A O   
7496 O O   T HOH   E .   ? 0.1242 0.0776 0.2433 -0.0070 -0.0073 0.0297  398 HOH   A O   
7497 O O   . HOH   E .   ? 0.2514 0.3912 0.3908 -0.0346 0.1038  -0.0518 399 HOH   A O   
7498 O O   . HOH   E .   ? 0.2508 0.3584 0.8432 -0.0387 0.0545  -0.0297 400 HOH   A O   
7499 O O   . HOH   E .   ? 0.4694 0.5252 0.5958 -0.1116 -0.0817 -0.1097 401 HOH   A O   
7500 O O   . HOH   E .   ? 0.1939 0.2058 0.3869 0.0420  0.1049  0.1057  402 HOH   A O   
7501 O O   . HOH   E .   ? 0.3115 0.2184 0.2693 -0.0205 0.0402  0.0251  403 HOH   A O   
7502 O O   . HOH   E .   ? 0.2530 0.5319 0.4113 0.0904  -0.1324 -0.0100 404 HOH   A O   
7503 O O   . HOH   E .   ? 0.1688 0.2732 0.3012 0.0019  0.0698  0.0791  405 HOH   A O   
7504 O O   A HOH   E .   ? 0.4259 0.5211 0.4718 0.2086  0.0450  0.1115  406 HOH   A O   
7505 O O   . HOH   E .   ? 0.3185 0.5228 0.4516 -0.0884 0.0425  -0.0491 407 HOH   A O   
7506 O O   . HOH   E .   ? 0.4844 0.5001 0.6616 0.0919  0.1973  -0.1547 408 HOH   A O   
7507 O O   . HOH   E .   ? 0.6991 0.3916 0.5327 0.1554  -0.1060 0.1583  409 HOH   A O   
7508 O O   . HOH   E .   ? 0.3325 0.4148 0.4510 -0.0244 0.1417  -0.0169 410 HOH   A O   
7509 O O   A HOH   E .   ? 0.2673 0.2079 0.2475 -0.0082 -0.0374 0.0413  411 HOH   A O   
7510 O O   . HOH   E .   ? 0.5434 0.7667 0.7753 -0.0975 -0.1205 0.3848  412 HOH   A O   
7511 O O   . HOH   E .   ? 0.6852 0.8004 0.6731 0.1970  -0.0433 0.1815  413 HOH   A O   
7512 O O   . HOH   E .   ? 0.5845 0.6617 0.7508 -0.0717 -0.0753 0.1870  414 HOH   A O   
7513 O O   . HOH   E .   ? 0.2299 0.2077 0.3443 0.0185  -0.0955 0.0160  415 HOH   A O   
7514 O O   B HOH   E .   ? 0.5398 0.3937 0.4340 -0.1803 0.1521  0.0674  416 HOH   A O   
7515 O O   . HOH   E .   ? 0.7226 0.6555 0.5495 -0.0127 0.1897  0.2590  417 HOH   A O   
7516 O O   A HOH   E .   ? 0.4869 0.4060 0.3138 -0.1397 0.0043  0.1382  418 HOH   A O   
7517 O O   . HOH   E .   ? 0.3941 0.1407 0.2241 -0.0161 -0.0856 0.0249  419 HOH   A O   
7518 O O   . HOH   E .   ? 0.1742 0.1722 0.3801 0.0135  0.0071  0.0172  420 HOH   A O   
7519 O O   . HOH   E .   ? 0.2037 0.2681 0.2670 0.0025  -0.0285 0.0598  421 HOH   A O   
7520 O O   . HOH   E .   ? 0.4108 0.2444 0.5326 -0.0912 -0.2514 0.1123  422 HOH   A O   
7521 O O   . HOH   E .   ? 0.2014 0.2617 0.4802 -0.0115 -0.0254 0.0582  423 HOH   A O   
7522 O O   . HOH   E .   ? 0.2560 0.4501 0.2659 0.1767  0.0387  0.0652  424 HOH   A O   
7523 O O   . HOH   E .   ? 1.3075 1.2408 1.0460 -0.0359 -0.0552 0.0162  425 HOH   A O   
7524 O O   . HOH   E .   ? 0.2443 0.3214 0.3601 -0.0288 0.0060  0.0050  426 HOH   A O   
7525 O O   . HOH   E .   ? 0.2946 0.6061 0.1937 -0.0435 0.0607  0.0568  427 HOH   A O   
7526 O O   . HOH   E .   ? 0.6086 0.7352 0.4261 0.0860  0.2741  -0.0086 428 HOH   A O   
7527 O O   . HOH   E .   ? 0.4624 0.8305 0.4261 0.1896  -0.0573 -0.0012 429 HOH   A O   
7528 O O   A HOH   E .   ? 0.2898 0.4286 0.5033 -0.0599 -0.1096 0.1709  430 HOH   A O   
7529 O O   . HOH   E .   ? 0.2234 0.3568 0.5274 0.0227  -0.1026 -0.0385 431 HOH   A O   
7530 O O   A HOH   E .   ? 0.4034 0.4177 0.4421 -0.0386 0.0608  -0.0697 432 HOH   A O   
7531 O O   . HOH   E .   ? 0.7363 0.7771 0.7714 0.4148  0.1754  0.0819  433 HOH   A O   
7532 O O   A HOH   E .   ? 0.1631 0.2033 0.1153 0.0481  0.0345  0.0079  434 HOH   A O   
7533 O O   . HOH   E .   ? 0.3881 0.3604 0.2836 -0.0945 -0.0381 0.0528  435 HOH   A O   
7534 O O   . HOH   E .   ? 0.7474 0.7967 0.7666 -0.0256 -0.0334 -0.0450 436 HOH   A O   
7535 O O   . HOH   E .   ? 0.2544 0.1887 0.3415 0.0165  0.0196  -0.0084 437 HOH   A O   
7536 O O   A HOH   E .   ? 0.5029 0.6502 0.3643 0.1231  -0.1214 0.1827  438 HOH   A O   
7537 O O   . HOH   E .   ? 0.2025 0.2362 0.4806 -0.0251 -0.0949 0.0663  439 HOH   A O   
7538 O O   . HOH   E .   ? 0.3204 0.4327 0.7010 -0.0165 0.0633  -0.2501 440 HOH   A O   
7539 O O   . HOH   E .   ? 0.4047 0.2762 0.1835 -0.0766 0.0213  0.0572  441 HOH   A O   
7540 O O   . HOH   E .   ? 0.4447 0.3881 0.3334 0.2411  -0.0764 -0.0362 442 HOH   A O   
7541 O O   . HOH   E .   ? 0.9413 0.4213 0.4718 -0.1623 0.1094  -0.1323 443 HOH   A O   
7542 O O   . HOH   E .   ? 0.2545 0.2984 0.2829 -0.0015 0.0059  -0.0831 444 HOH   A O   
7543 O O   . HOH   E .   ? 0.9383 0.7385 0.8520 0.1428  0.0223  -0.0832 445 HOH   A O   
7544 O O   A HOH   E .   ? 0.3908 0.3887 0.3048 0.0173  0.0414  -0.0374 446 HOH   A O   
7545 O O   . HOH   E .   ? 0.2163 0.2251 0.2848 -0.0083 -0.0108 0.0570  447 HOH   A O   
7546 O O   B HOH   E .   ? 0.1613 0.1814 0.2020 -0.0153 -0.0164 0.0386  448 HOH   A O   
7547 O O   A HOH   E .   ? 0.4430 0.4065 0.5043 -0.0881 0.2323  -0.0400 449 HOH   A O   
7548 O O   . HOH   E .   ? 0.3042 0.3924 0.4042 0.0615  0.0279  0.0998  450 HOH   A O   
7549 O O   B HOH   E .   ? 0.3568 0.1695 0.3518 -0.0011 0.0161  -0.0172 451 HOH   A O   
7550 O O   B HOH   E .   ? 0.5258 0.3799 0.4141 -0.0393 0.0939  -0.1734 452 HOH   A O   
7551 O O   B HOH   E .   ? 0.6815 0.5526 0.5290 0.0297  0.0580  -0.0633 453 HOH   A O   
7552 O O   . HOH   E .   ? 0.4900 0.4429 0.5225 0.2437  -0.0976 0.0755  454 HOH   A O   
7553 O O   . HOH   E .   ? 0.9043 0.7340 0.8708 -0.1351 0.1391  -0.1338 455 HOH   A O   
7554 O O   . HOH   E .   ? 0.4350 0.3200 0.3612 0.0053  0.0428  -0.0105 456 HOH   A O   
7555 O O   . HOH   E .   ? 0.4024 0.3222 0.5064 -0.0362 -0.0546 -0.1520 457 HOH   A O   
7556 O O   B HOH   E .   ? 0.3985 0.3716 0.3230 0.0960  -0.1314 -0.0239 458 HOH   A O   
7557 O O   . HOH   E .   ? 0.7586 0.7555 0.4705 0.0381  -0.1105 -0.0089 459 HOH   A O   
7558 O O   . HOH   E .   ? 0.4178 0.6485 0.4957 0.0210  0.0118  0.1322  460 HOH   A O   
7559 O O   . HOH   E .   ? 0.4085 0.4736 0.5269 -0.1727 0.0616  -0.1399 461 HOH   A O   
7560 O O   . HOH   E .   ? 0.3033 0.5223 0.6371 0.0760  -0.1107 0.1700  462 HOH   A O   
7561 O O   B HOH   E .   ? 0.2178 0.2739 0.5136 -0.0007 0.0181  0.1333  463 HOH   A O   
7562 O O   . HOH   E .   ? 0.4457 0.6980 0.4380 -0.0768 -0.1411 0.2386  464 HOH   A O   
7563 O O   . HOH   E .   ? 0.4608 0.4944 0.5741 -0.0938 0.1094  -0.0315 465 HOH   A O   
7564 O O   . HOH   E .   ? 0.7160 0.7545 0.6783 -0.1394 -0.0777 -0.0937 466 HOH   A O   
7565 O O   . HOH   E .   ? 0.2586 0.4716 0.5219 0.0733  -0.0202 -0.2057 467 HOH   A O   
7566 O O   . HOH   E .   ? 0.6607 0.7599 0.6493 0.1137  0.1338  0.0410  468 HOH   A O   
7567 O O   . HOH   E .   ? 0.8479 0.7586 0.5517 0.1439  0.1642  0.2419  469 HOH   A O   
7568 O O   . HOH   E .   ? 0.3104 0.3068 0.3990 -0.1165 0.0776  -0.0280 470 HOH   A O   
7569 O O   . HOH   E .   ? 0.2839 0.1780 0.2823 0.0190  -0.0989 -0.0349 471 HOH   A O   
7570 O O   A HOH   E .   ? 0.3388 0.4256 0.3204 0.0159  -0.0398 0.0401  472 HOH   A O   
7571 O O   A HOH   E .   ? 0.2687 0.4268 0.4602 0.0772  -0.1785 -0.1060 473 HOH   A O   
7572 O O   . HOH   E .   ? 0.3764 0.3592 0.4761 0.0465  0.1452  0.1034  474 HOH   A O   
7573 O O   . HOH   E .   ? 0.7999 0.4532 0.4937 -0.0303 0.1227  0.0547  475 HOH   A O   
7574 O O   . HOH   E .   ? 0.3886 0.7020 0.4551 0.2484  0.1503  0.2606  476 HOH   A O   
7575 O O   . HOH   E .   ? 0.6069 0.3958 0.6181 0.1756  0.0088  0.2215  477 HOH   A O   
7576 O O   . HOH   E .   ? 0.6171 0.5171 0.5379 -0.0784 0.0990  -0.0336 478 HOH   A O   
7577 O O   . HOH   E .   ? 0.5319 0.4919 0.4324 -0.1687 0.1544  0.1450  479 HOH   A O   
7578 O O   B HOH   E .   ? 0.2773 0.6390 0.3337 -0.0117 -0.0875 0.0252  480 HOH   A O   
7579 O O   . HOH   E .   ? 0.5726 0.6679 0.5636 -0.0843 -0.1297 0.0272  481 HOH   A O   
7580 O O   . HOH   E .   ? 0.4951 0.5657 0.7260 -0.1809 -0.0922 -0.0921 482 HOH   A O   
7581 O O   . HOH   E .   ? 0.2912 0.3246 0.2918 0.0816  0.0127  0.0260  483 HOH   A O   
7582 O O   . HOH   E .   ? 0.5913 0.5373 0.3291 -0.0358 -0.0301 0.0350  484 HOH   A O   
7583 O O   . HOH   E .   ? 0.5484 0.4191 0.5348 0.0180  -0.0526 -0.0981 485 HOH   A O   
7584 O O   . HOH   E .   ? 0.7422 0.5697 0.7912 -0.1527 0.0355  -0.0989 486 HOH   A O   
7585 O O   . HOH   E .   ? 0.5276 0.5250 0.3858 0.0497  -0.0023 -0.0163 487 HOH   A O   
7586 O O   . HOH   E .   ? 0.8270 0.4123 0.3475 0.0147  -0.1493 0.0541  488 HOH   A O   
7587 O O   B HOH   E .   ? 0.3865 0.4645 0.2737 0.1173  -0.1204 -0.1107 489 HOH   A O   
7588 O O   . HOH   E .   ? 0.5472 0.4699 0.4793 0.0846  0.1052  0.2347  490 HOH   A O   
7589 O O   . HOH   E .   ? 0.7984 0.3572 0.3923 0.0425  -0.1543 0.0685  491 HOH   A O   
7590 O O   . HOH   E .   ? 0.5549 0.6847 0.8824 -0.0383 0.2219  -0.1345 492 HOH   A O   
7591 O O   . HOH   E .   ? 0.2638 0.2253 0.7911 0.0138  -0.1211 -0.0188 493 HOH   A O   
7592 O O   . HOH   E .   ? 0.8178 0.7391 0.5773 -0.0708 0.2436  0.1329  494 HOH   A O   
7593 O O   . HOH   E .   ? 0.6300 0.7613 0.6737 0.2223  -0.1199 -0.0528 495 HOH   A O   
7594 O O   . HOH   E .   ? 0.4512 0.3281 0.2956 -0.0922 0.1422  -0.0530 496 HOH   A O   
7595 O O   . HOH   E .   ? 0.3743 0.5242 0.3577 -0.0103 -0.0745 -0.0134 497 HOH   A O   
7596 O O   . HOH   E .   ? 0.6019 0.6264 0.4588 0.0024  -0.1177 -0.0344 498 HOH   A O   
7597 O O   . HOH   E .   ? 0.4175 0.3303 0.5593 0.0494  0.2551  0.1094  499 HOH   A O   
7598 O O   . HOH   E .   ? 0.2925 0.2904 0.6283 0.0158  0.0413  -0.0197 500 HOH   A O   
7599 O O   . HOH   E .   ? 0.3481 0.2311 0.7192 -0.0133 0.1028  0.0204  501 HOH   A O   
7600 O O   . HOH   E .   ? 0.2722 0.4411 0.6714 -0.0086 -0.1294 0.0649  502 HOH   A O   
7601 O O   . HOH   E .   ? 0.4249 0.9079 0.6307 -0.1329 -0.0629 0.2340  503 HOH   A O   
7602 O O   . HOH   E .   ? 0.6997 0.2859 0.5509 -0.0439 0.1362  0.0582  504 HOH   A O   
7603 O O   . HOH   E .   ? 0.6333 0.6814 0.5949 0.0511  -0.1504 -0.0436 505 HOH   A O   
7604 O O   B HOH   E .   ? 0.2227 0.4577 0.3979 0.0254  0.0318  0.0829  506 HOH   A O   
7605 O O   . HOH   E .   ? 0.2655 0.3829 0.3574 0.0732  -0.0290 0.1135  507 HOH   A O   
7606 O O   . HOH   E .   ? 0.6498 0.8675 0.4850 0.1160  0.0116  0.2636  508 HOH   A O   
7607 O O   . HOH   E .   ? 0.2506 0.2217 0.1779 -0.0439 0.0029  0.0149  509 HOH   A O   
7608 O O   . HOH   E .   ? 0.5256 0.8651 0.4857 0.3279  -0.0891 0.0740  510 HOH   A O   
7609 O O   . HOH   E .   ? 0.3458 0.2676 0.4583 -0.0115 0.0334  0.0740  511 HOH   A O   
7610 O O   T HOH   E .   ? 0.1171 0.2240 0.2590 -0.0398 -0.0279 0.0614  512 HOH   A O   
7611 O O   B HOH   E .   ? 0.2945 0.2895 0.4933 -0.0497 -0.0531 0.0148  513 HOH   A O   
7612 O O   . HOH   E .   ? 0.6928 0.9223 0.6579 -0.1146 -0.1352 -0.1289 514 HOH   A O   
7613 O O   A HOH   E .   ? 0.3612 0.5410 0.3022 0.1889  -0.0445 0.0761  515 HOH   A O   
7614 O O   . HOH   E .   ? 0.5096 0.9686 0.5603 0.2032  0.1069  -0.0718 516 HOH   A O   
7615 O O   . HOH   E .   ? 0.6058 0.7751 0.5855 -0.1234 -0.0759 0.1008  517 HOH   A O   
7616 O O   . HOH   E .   ? 0.5450 0.5477 0.5050 0.0684  0.0937  0.1401  518 HOH   A O   
7617 O O   B HOH   E .   ? 0.5266 0.3471 0.4510 0.1278  0.0526  0.1414  519 HOH   A O   
7618 O O   . HOH   E .   ? 0.3260 0.4852 0.7048 -0.0470 -0.0828 0.3355  520 HOH   A O   
7619 O O   . HOH   F .   ? 0.2373 0.2804 0.3216 0.0063  0.0816  0.0231  201 HOH   B O   
7620 O O   . HOH   F .   ? 0.3108 0.3001 0.7753 -0.0028 -0.0465 0.0317  202 HOH   B O   
7621 O O   . HOH   F .   ? 0.7926 0.4461 0.4595 -0.0121 0.0399  -0.0304 203 HOH   B O   
7622 O O   . HOH   F .   ? 0.4791 0.4022 0.4655 -0.0281 0.0104  -0.2038 204 HOH   B O   
7623 O O   . HOH   F .   ? 0.3458 0.2099 0.6014 0.0196  0.2284  0.0714  205 HOH   B O   
7624 O O   . HOH   F .   ? 0.5127 0.6637 0.3642 0.2602  0.0624  0.1234  206 HOH   B O   
7625 O O   . HOH   F .   ? 0.1885 0.2234 0.2991 -0.0108 0.0276  -0.0211 207 HOH   B O   
7626 O O   . HOH   F .   ? 0.3371 0.6197 0.3453 0.0494  -0.0190 0.2115  208 HOH   B O   
7627 O O   . HOH   F .   ? 0.3711 0.2496 0.6009 -0.0398 0.2429  0.0151  209 HOH   B O   
7628 O O   . HOH   F .   ? 0.1831 0.2191 0.2842 -0.0282 -0.0123 0.0163  210 HOH   B O   
7629 O O   . HOH   F .   ? 0.4028 0.5639 0.5198 0.2661  0.0781  -0.0040 211 HOH   B O   
7630 O O   . HOH   F .   ? 0.4519 0.4109 0.5293 -0.1808 0.0130  0.0724  212 HOH   B O   
7631 O O   . HOH   F .   ? 0.6649 0.4630 0.2947 -0.1051 0.0379  0.0512  213 HOH   B O   
7632 O O   . HOH   F .   ? 0.6375 0.3879 0.7060 0.0874  -0.1017 0.2494  214 HOH   B O   
7633 O O   . HOH   F .   ? 0.1828 0.2232 0.3485 -0.0114 0.0122  -0.0317 215 HOH   B O   
7634 O O   . HOH   F .   ? 0.6137 0.5949 0.6696 0.2281  0.1740  0.0004  216 HOH   B O   
7635 O O   . HOH   F .   ? 0.2443 0.2369 0.4842 -0.0332 -0.0025 -0.0779 217 HOH   B O   
7636 O O   . HOH   F .   ? 0.3582 0.2914 0.3684 0.0183  -0.1113 0.0031  218 HOH   B O   
7637 O O   . HOH   F .   ? 0.2884 0.2878 0.6460 0.0775  -0.1008 0.0611  219 HOH   B O   
7638 O O   . HOH   F .   ? 0.2464 0.4223 0.3529 -0.0125 -0.0514 0.0638  220 HOH   B O   
7639 O O   . HOH   F .   ? 0.5391 0.4401 0.3326 0.0818  0.0690  -0.1436 221 HOH   B O   
7640 O O   . HOH   F .   ? 0.1752 0.1552 0.2483 -0.0311 0.0130  0.0071  222 HOH   B O   
7641 O O   . HOH   F .   ? 0.2902 0.6554 0.5394 -0.0152 0.1411  -0.2109 223 HOH   B O   
7642 O O   . HOH   F .   ? 0.3078 0.2714 0.4869 0.0429  -0.0487 -0.0759 224 HOH   B O   
7643 O O   . HOH   F .   ? 0.4740 0.6031 0.4297 0.2852  -0.1210 -0.0194 225 HOH   B O   
7644 O O   . HOH   F .   ? 0.2483 0.2744 0.3196 0.0096  0.0301  -0.0876 226 HOH   B O   
7645 O O   . HOH   F .   ? 0.2331 0.3871 0.2258 -0.0237 -0.0134 0.0511  227 HOH   B O   
7646 O O   . HOH   F .   ? 0.7476 0.5713 0.4068 0.0066  0.1388  0.0138  228 HOH   B O   
7647 O O   . HOH   F .   ? 0.4165 0.4366 0.4015 0.1852  -0.0243 0.0125  229 HOH   B O   
7648 O O   . HOH   F .   ? 0.2341 0.1408 0.3160 0.0084  -0.0600 -0.0085 230 HOH   B O   
7649 O O   . HOH   F .   ? 0.2228 0.1738 0.2393 -0.0198 0.0706  -0.0020 231 HOH   B O   
7650 O O   . HOH   F .   ? 0.3092 0.3093 0.1778 0.0157  0.0281  0.0183  232 HOH   B O   
7651 O O   . HOH   F .   ? 0.5813 0.2851 0.3055 -0.1304 0.1035  -0.0691 233 HOH   B O   
7652 O O   . HOH   F .   ? 0.4632 0.2324 0.2435 0.1575  0.0753  0.0461  234 HOH   B O   
7653 O O   . HOH   F .   ? 0.1755 0.1888 0.3573 -0.0313 -0.0174 0.0308  235 HOH   B O   
7654 O O   . HOH   F .   ? 0.5248 0.2149 0.3189 0.0097  -0.0691 0.0007  236 HOH   B O   
7655 O O   . HOH   F .   ? 0.3911 0.2410 0.1771 0.0267  -0.0521 0.0012  237 HOH   B O   
7656 O O   . HOH   F .   ? 0.3529 0.2674 0.4769 0.0919  -0.1669 -0.1719 238 HOH   B O   
7657 O O   . HOH   F .   ? 0.3783 0.5712 0.8366 0.0407  0.1186  -0.0069 239 HOH   B O   
7658 O O   . HOH   F .   ? 0.2554 0.4250 0.3508 -0.0526 -0.0935 -0.0910 240 HOH   B O   
7659 O O   . HOH   F .   ? 0.2729 0.3222 0.3357 -0.1201 0.0133  -0.0120 241 HOH   B O   
7660 O O   . HOH   F .   ? 0.1708 0.1632 0.2684 -0.0026 0.0125  -0.0075 242 HOH   B O   
7661 O O   . HOH   F .   ? 0.6027 0.3687 0.2374 -0.0725 -0.0720 -0.1055 243 HOH   B O   
7662 O O   . HOH   F .   ? 0.2021 0.2958 0.2807 0.0467  0.0573  0.0875  244 HOH   B O   
7663 O O   . HOH   F .   ? 0.2461 0.5498 0.6107 0.1288  -0.0294 -0.1620 245 HOH   B O   
7664 O O   . HOH   F .   ? 0.3241 0.3401 0.2402 -0.0661 0.0321  -0.0268 246 HOH   B O   
7665 O O   . HOH   F .   ? 0.4080 0.4970 0.6495 -0.0819 -0.0766 -0.1835 247 HOH   B O   
7666 O O   . HOH   F .   ? 0.1673 0.1530 0.1482 -0.0062 -0.0079 -0.0068 248 HOH   B O   
7667 O O   . HOH   F .   ? 0.2825 0.2654 0.2397 -0.0398 0.0281  -0.0156 249 HOH   B O   
7668 O O   . HOH   F .   ? 0.2909 0.2348 0.3308 0.0695  0.1029  -0.0099 250 HOH   B O   
7669 O O   . HOH   F .   ? 0.3231 0.3539 0.4268 0.0237  0.1593  0.0096  251 HOH   B O   
7670 O O   . HOH   F .   ? 0.1724 0.1391 0.1424 0.0037  -0.0080 0.0025  252 HOH   B O   
7671 O O   . HOH   F .   ? 0.8257 0.4883 0.5472 0.1355  0.0730  -0.1229 253 HOH   B O   
7672 O O   . HOH   F .   ? 0.2967 0.1735 0.6668 -0.0162 -0.0735 -0.0138 254 HOH   B O   
7673 O O   . HOH   F .   ? 0.3898 0.1869 0.1989 0.0143  -0.0890 -0.0179 255 HOH   B O   
7674 O O   . HOH   F .   ? 0.2319 0.1516 0.2014 -0.0343 -0.0465 0.0268  256 HOH   B O   
7675 O O   . HOH   F .   ? 0.2155 0.1929 0.1994 -0.0303 -0.0389 0.0103  257 HOH   B O   
7676 O O   . HOH   F .   ? 0.5518 0.5479 0.6161 0.1572  -0.1513 -0.1207 258 HOH   B O   
7677 O O   . HOH   F .   ? 0.2479 0.2278 0.2450 0.0820  -0.0818 -0.0633 259 HOH   B O   
7678 O O   . HOH   F .   ? 0.2495 0.3029 0.2385 -0.0598 0.0257  0.0483  260 HOH   B O   
7679 O O   . HOH   F .   ? 0.5478 0.3191 0.3955 -0.2324 0.0204  0.0058  261 HOH   B O   
7680 O O   . HOH   F .   ? 0.1529 0.1690 0.2164 -0.0079 0.0103  0.0101  262 HOH   B O   
7681 O O   . HOH   F .   ? 0.2909 0.2411 0.1860 0.0329  0.0108  0.0076  263 HOH   B O   
7682 O O   . HOH   F .   ? 0.2272 0.2035 0.3864 0.0118  -0.0425 -0.0518 264 HOH   B O   
7683 O O   . HOH   F .   ? 0.5476 0.3874 0.3434 0.0599  -0.0094 -0.0489 265 HOH   B O   
7684 O O   . HOH   F .   ? 0.2263 0.1571 0.2305 -0.0380 -0.0081 0.0132  266 HOH   B O   
7685 O O   . HOH   F .   ? 0.4458 0.2757 0.3928 -0.0199 -0.1416 -0.0262 267 HOH   B O   
7686 O O   . HOH   F .   ? 0.3464 0.4494 0.3394 -0.0291 -0.1070 0.0874  268 HOH   B O   
7687 O O   . HOH   F .   ? 0.2229 0.4878 0.5089 -0.0581 -0.0332 -0.1366 269 HOH   B O   
7688 O O   . HOH   F .   ? 0.3775 0.4438 0.2245 0.0041  0.1066  0.0126  270 HOH   B O   
7689 O O   . HOH   F .   ? 0.3316 0.2954 0.2921 -0.0761 0.0489  -0.0384 271 HOH   B O   
7690 O O   . HOH   F .   ? 0.2689 0.2052 0.2981 -0.0594 0.0041  -0.0218 272 HOH   B O   
7691 O O   . HOH   F .   ? 0.2272 0.2796 0.2332 -0.0244 -0.0589 -0.0708 273 HOH   B O   
7692 O O   . HOH   F .   ? 0.2459 0.2022 0.3396 -0.0387 -0.0070 0.0647  274 HOH   B O   
7693 O O   . HOH   F .   ? 0.1924 0.1867 0.1599 -0.0478 -0.0393 0.0080  275 HOH   B O   
7694 O O   . HOH   F .   ? 0.2085 0.1595 0.4007 -0.0065 -0.0613 -0.0141 276 HOH   B O   
7695 O O   . HOH   F .   ? 0.2079 0.2979 0.2421 0.0502  -0.0315 -0.0335 277 HOH   B O   
7696 O O   . HOH   F .   ? 0.2630 0.2839 0.2914 -0.0105 0.0395  -0.0726 278 HOH   B O   
7697 O O   . HOH   F .   ? 0.1917 0.1580 0.1903 0.0114  0.0088  -0.0030 279 HOH   B O   
7698 O O   . HOH   F .   ? 0.2416 0.4000 0.6268 0.0029  0.0282  -0.0597 280 HOH   B O   
7699 O O   . HOH   F .   ? 0.3176 0.2067 0.4055 -0.0734 -0.1618 0.0528  281 HOH   B O   
7700 O O   . HOH   F .   ? 0.6000 0.4070 0.3077 0.2735  0.1376  0.1062  282 HOH   B O   
7701 O O   . HOH   F .   ? 0.2463 0.2846 0.2180 -0.0230 -0.0756 0.0064  283 HOH   B O   
7702 O O   . HOH   F .   ? 0.3753 0.2340 0.5393 0.0297  0.1115  0.0801  284 HOH   B O   
7703 O O   . HOH   F .   ? 0.2605 0.4954 0.2172 -0.0989 -0.0393 -0.0604 285 HOH   B O   
7704 O O   . HOH   F .   ? 0.2122 0.5417 0.4175 -0.0642 0.0083  -0.1012 286 HOH   B O   
7705 O O   . HOH   F .   ? 0.4590 0.4836 0.5068 0.1801  -0.0408 0.0907  287 HOH   B O   
7706 O O   . HOH   F .   ? 0.1893 0.1654 0.3614 -0.0197 -0.0012 0.0017  288 HOH   B O   
7707 O O   . HOH   F .   ? 0.3919 0.3718 0.4484 0.1208  -0.0445 -0.0810 289 HOH   B O   
7708 O O   . HOH   F .   ? 0.3502 0.5539 0.1990 -0.1392 -0.0382 0.0870  290 HOH   B O   
7709 O O   . HOH   F .   ? 0.1972 0.2281 0.2901 0.0195  0.0039  0.0122  291 HOH   B O   
7710 O O   . HOH   F .   ? 0.3678 0.2906 0.2680 -0.0527 0.0474  -0.1190 292 HOH   B O   
7711 O O   . HOH   F .   ? 0.1892 0.2232 0.1362 0.0031  -0.0224 0.0032  293 HOH   B O   
7712 O O   . HOH   F .   ? 0.2792 0.4849 0.5383 -0.0591 -0.1344 0.0658  294 HOH   B O   
7713 O O   . HOH   F .   ? 0.2659 0.2907 0.2919 0.0052  -0.0895 0.0201  295 HOH   B O   
7714 O O   . HOH   F .   ? 0.4122 0.3322 0.3266 0.0437  -0.0114 -0.0556 296 HOH   B O   
7715 O O   . HOH   F .   ? 0.4783 0.5623 0.4335 0.0498  -0.1573 0.0047  297 HOH   B O   
7716 O O   . HOH   F .   ? 0.2169 0.3104 0.6661 0.0644  -0.0593 -0.1336 298 HOH   B O   
7717 O O   . HOH   F .   ? 0.2826 0.2322 0.2170 -0.0945 0.0047  0.0103  299 HOH   B O   
7718 O O   . HOH   F .   ? 0.2124 0.1841 0.2574 -0.0401 -0.0108 -0.0205 300 HOH   B O   
7719 O O   . HOH   F .   ? 0.3415 0.2875 0.5856 -0.0387 -0.0630 0.1688  301 HOH   B O   
7720 O O   . HOH   F .   ? 0.1906 0.3642 0.5440 0.0420  -0.0163 -0.1470 302 HOH   B O   
7721 O O   . HOH   F .   ? 0.4803 0.2581 0.2474 0.0509  -0.1383 -0.0091 303 HOH   B O   
7722 O O   . HOH   F .   ? 0.2399 0.3923 0.4879 -0.0293 -0.0738 -0.0511 304 HOH   B O   
7723 O O   . HOH   F .   ? 0.2050 0.1794 0.2293 0.0129  0.0097  0.0241  305 HOH   B O   
7724 O O   . HOH   F .   ? 0.2812 0.7519 0.2164 0.0896  -0.0412 -0.0727 306 HOH   B O   
7725 O O   . HOH   F .   ? 0.3283 0.2914 0.2105 0.0450  -0.0273 0.0494  307 HOH   B O   
7726 O O   . HOH   F .   ? 0.2686 0.1551 0.2592 -0.0263 -0.0186 0.0269  308 HOH   B O   
7727 O O   . HOH   F .   ? 0.1810 0.1595 0.3403 -0.0048 0.0028  0.0015  309 HOH   B O   
7728 O O   . HOH   F .   ? 0.3668 0.2077 0.3441 0.0747  0.1380  0.0451  310 HOH   B O   
7729 O O   . HOH   F .   ? 0.4471 0.6040 0.2296 0.0272  0.1075  0.0899  311 HOH   B O   
7730 O O   . HOH   F .   ? 0.5589 0.3142 0.5650 0.1575  0.3000  0.1571  312 HOH   B O   
7731 O O   . HOH   F .   ? 0.2646 0.1966 0.1927 -0.0025 0.0261  0.0198  313 HOH   B O   
7732 O O   . HOH   F .   ? 0.4769 0.3151 0.2041 0.1038  -0.1009 -0.0421 314 HOH   B O   
7733 O O   . HOH   F .   ? 0.4085 0.2210 0.2718 0.1282  0.0915  0.0344  315 HOH   B O   
7734 O O   . HOH   F .   ? 0.3137 0.7684 0.7116 0.1685  -0.0956 -0.1466 316 HOH   B O   
7735 O O   . HOH   F .   ? 0.7132 0.4484 0.5229 0.1423  0.2072  0.0214  317 HOH   B O   
7736 O O   . HOH   F .   ? 0.3628 0.4625 0.9300 0.0029  -0.1007 0.2672  318 HOH   B O   
7737 O O   . HOH   F .   ? 0.1890 0.2879 0.2167 -0.0062 -0.0177 0.0669  319 HOH   B O   
7738 O O   . HOH   F .   ? 0.2129 0.1660 0.3325 0.0321  -0.0806 0.0087  320 HOH   B O   
7739 O O   . HOH   F .   ? 0.4100 0.4498 0.4680 -0.1618 0.1699  -0.0589 321 HOH   B O   
7740 O O   . HOH   F .   ? 0.6303 0.4177 0.4667 0.1087  0.2016  0.2141  322 HOH   B O   
7741 O O   . HOH   F .   ? 0.6412 0.4475 0.2662 0.0362  -0.0696 -0.1043 323 HOH   B O   
7742 O O   . HOH   F .   ? 0.3409 0.2892 0.4065 -0.0629 0.1694  -0.1032 324 HOH   B O   
7743 O O   . HOH   F .   ? 0.1739 0.1828 0.3099 -0.0210 -0.0169 0.0204  325 HOH   B O   
7744 O O   . HOH   F .   ? 0.1778 0.1681 0.3139 -0.0066 0.0018  -0.0136 326 HOH   B O   
7745 O O   . HOH   F .   ? 0.4829 0.3860 0.4841 -0.1015 0.0282  0.1472  327 HOH   B O   
7746 O O   . HOH   F .   ? 0.5018 0.4388 0.7251 0.0834  0.0276  -0.0317 328 HOH   B O   
7747 O O   . HOH   F .   ? 0.6024 0.5754 0.7091 0.2227  -0.0865 0.1798  329 HOH   B O   
7748 O O   . HOH   F .   ? 0.5445 0.3584 0.4562 -0.0148 0.1173  -0.1677 330 HOH   B O   
7749 O O   . HOH   F .   ? 0.4012 0.2770 0.3006 0.0781  -0.0206 0.0622  331 HOH   B O   
7750 O O   . HOH   F .   ? 0.7854 0.2517 0.4919 0.0413  -0.1348 -0.0430 332 HOH   B O   
7751 O O   . HOH   F .   ? 0.4770 0.5641 0.4298 0.1141  -0.1016 0.0852  333 HOH   B O   
7752 O O   . HOH   F .   ? 0.1970 0.2119 0.2699 0.0357  0.0418  0.0228  334 HOH   B O   
7753 O O   . HOH   F .   ? 0.6376 0.6448 0.6147 -0.1342 -0.0996 0.2398  335 HOH   B O   
7754 O O   . HOH   F .   ? 0.2860 0.2158 0.6295 0.0026  0.0069  0.0563  336 HOH   B O   
7755 O O   . HOH   F .   ? 0.2981 0.3643 0.6299 -0.0683 -0.2023 0.1666  337 HOH   B O   
7756 O O   . HOH   F .   ? 0.6526 0.4448 0.6496 -0.1136 -0.1425 -0.1460 338 HOH   B O   
7757 O O   . HOH   F .   ? 0.2264 0.3614 0.3510 0.0515  -0.0210 -0.1108 339 HOH   B O   
7758 O O   . HOH   F .   ? 0.5184 0.4812 0.3471 -0.0208 -0.1312 0.0084  340 HOH   B O   
7759 O O   . HOH   F .   ? 0.4679 0.7980 0.4210 -0.0834 -0.1224 0.2093  341 HOH   B O   
7760 O O   . HOH   F .   ? 0.2007 0.1582 0.2403 0.0059  -0.0159 0.0131  342 HOH   B O   
7761 O O   . HOH   F .   ? 0.4642 0.2808 0.3334 0.0171  0.0416  0.1182  343 HOH   B O   
7762 O O   . HOH   F .   ? 0.3505 0.3942 0.6744 -0.1412 -0.1048 0.0153  344 HOH   B O   
7763 O O   . HOH   F .   ? 0.2778 0.2028 0.3995 0.0327  -0.1008 -0.0582 345 HOH   B O   
7764 O O   . HOH   F .   ? 0.4171 0.3224 0.3135 0.0688  -0.1136 -0.0739 346 HOH   B O   
7765 O O   . HOH   F .   ? 0.4112 0.5874 0.4381 -0.1510 -0.1195 -0.0504 347 HOH   B O   
7766 O O   . HOH   F .   ? 0.6356 0.5206 0.7330 -0.1321 0.1386  0.0838  348 HOH   B O   
7767 O O   . HOH   F .   ? 0.2260 0.2309 0.3288 -0.0144 0.0807  -0.0209 349 HOH   B O   
7768 O O   . HOH   F .   ? 0.8621 0.5280 0.3067 0.1247  0.0007  0.1250  350 HOH   B O   
7769 O O   . HOH   F .   ? 0.2943 0.2300 0.5152 -0.0317 -0.0561 -0.0449 351 HOH   B O   
7770 O O   . HOH   F .   ? 0.3533 0.5183 0.4901 -0.1436 0.0231  -0.0639 352 HOH   B O   
7771 O O   . HOH   F .   ? 0.5582 0.3140 0.5237 -0.1169 0.1811  0.0132  353 HOH   B O   
7772 O O   . HOH   F .   ? 0.4859 0.6724 0.8680 0.0522  0.1470  -0.1101 354 HOH   B O   
7773 O O   . HOH   F .   ? 0.2053 0.4636 0.3570 0.0665  -0.0362 -0.1052 355 HOH   B O   
7774 O O   . HOH   F .   ? 0.3910 0.5510 0.6855 -0.0637 -0.1339 0.0220  356 HOH   B O   
7775 O O   . HOH   F .   ? 0.2683 0.3527 0.4615 0.0193  0.0176  -0.0162 357 HOH   B O   
7776 O O   . HOH   F .   ? 0.5313 0.3386 0.3611 -0.0163 0.0950  -0.0617 358 HOH   B O   
7777 O O   . HOH   F .   ? 0.3690 0.2095 0.2966 -0.0712 0.0140  -0.0684 359 HOH   B O   
7778 O O   . HOH   F .   ? 0.2991 0.3254 0.3913 -0.0293 -0.0774 0.0023  360 HOH   B O   
7779 O O   . HOH   F .   ? 0.4269 0.2877 0.4275 -0.0981 -0.0322 -0.0363 361 HOH   B O   
7780 O O   . HOH   F .   ? 0.5166 0.4911 0.5877 0.2390  -0.1333 0.1054  362 HOH   B O   
7781 O O   . HOH   F .   ? 0.5815 0.4276 0.6499 0.0564  0.2273  0.2079  363 HOH   B O   
7782 O O   . HOH   F .   ? 0.6862 0.3639 0.4953 0.0585  -0.1686 -0.1034 364 HOH   B O   
7783 O O   . HOH   F .   ? 0.2426 0.5034 0.6540 -0.1129 -0.0580 -0.0674 365 HOH   B O   
7784 O O   . HOH   F .   ? 0.4487 0.7958 0.2656 0.2961  0.0016  0.0319  366 HOH   B O   
7785 O O   . HOH   F .   ? 0.6103 0.2501 0.2503 -0.0230 0.0131  0.0518  367 HOH   B O   
7786 O O   . HOH   F .   ? 0.6787 0.6341 0.6223 -0.0830 -0.0843 -0.1288 368 HOH   B O   
7787 O O   . HOH   F .   ? 0.4134 0.4672 0.6112 0.2067  -0.1690 -0.0470 369 HOH   B O   
7788 O O   . HOH   F .   ? 0.5826 0.3351 0.4694 -0.1158 0.0289  -0.0144 370 HOH   B O   
7789 O O   . HOH   F .   ? 0.4002 0.6441 0.4594 0.2671  0.1031  0.1803  371 HOH   B O   
7790 O O   . HOH   F .   ? 0.5743 0.4981 0.4576 0.1024  0.0184  0.0716  372 HOH   B O   
7791 O O   . HOH   F .   ? 0.5753 0.6814 0.2866 0.2317  -0.0909 0.0630  373 HOH   B O   
7792 O O   . HOH   F .   ? 0.4818 0.5390 0.5456 -0.0361 -0.0368 -0.0186 374 HOH   B O   
7793 O O   . HOH   F .   ? 0.4103 0.6464 0.6635 0.0920  -0.1426 0.0278  375 HOH   B O   
7794 O O   . HOH   F .   ? 0.6553 0.4087 0.2973 -0.1197 -0.0996 -0.0596 376 HOH   B O   
7795 O O   . HOH   F .   ? 1.0330 0.8114 0.6111 0.2669  -0.1078 -0.0784 377 HOH   B O   
7796 O O   . HOH   F .   ? 0.4700 0.6480 0.6552 0.0981  -0.0392 0.2614  378 HOH   B O   
7797 O O   . HOH   F .   ? 0.3381 0.6451 0.2220 -0.0694 0.0077  -0.0263 379 HOH   B O   
7798 O O   . HOH   F .   ? 0.5005 0.8167 0.3517 -0.1566 0.0049  -0.1744 380 HOH   B O   
7799 O O   . HOH   F .   ? 0.2590 0.4058 0.2150 0.0521  -0.0383 -0.0537 381 HOH   B O   
7800 O O   . HOH   F .   ? 0.2481 0.3915 0.3814 0.0345  -0.0586 -0.0289 382 HOH   B O   
7801 O O   . HOH   F .   ? 0.7144 0.3804 0.5800 0.0060  -0.1092 0.0632  383 HOH   B O   
7802 O O   . HOH   F .   ? 0.5926 0.3197 0.4179 -0.0010 -0.0120 -0.0866 384 HOH   B O   
7803 O O   . HOH   F .   ? 0.2978 0.2704 0.3367 -0.0070 0.0232  -0.0127 385 HOH   B O   
7804 O O   . HOH   F .   ? 0.3744 0.7262 0.4659 -0.0303 0.1441  0.0334  386 HOH   B O   
7805 O O   . HOH   F .   ? 0.2552 0.8315 0.4115 0.0840  -0.0264 0.1099  387 HOH   B O   
7806 O O   . HOH   F .   ? 0.7469 0.5487 0.5085 -0.0989 0.0177  0.1093  388 HOH   B O   
7807 O O   . HOH   F .   ? 0.5087 0.3266 0.5183 -0.1940 0.0153  0.0487  389 HOH   B O   
7808 O O   . HOH   F .   ? 0.6753 0.4927 0.3792 0.1766  -0.0353 -0.0616 390 HOH   B O   
7809 O O   . HOH   F .   ? 0.2275 0.4026 0.4986 -0.0495 -0.0803 -0.0130 391 HOH   B O   
7810 O O   . HOH   F .   ? 0.4004 0.2558 0.3122 0.0962  -0.0329 0.0416  392 HOH   B O   
7811 O O   . HOH   F .   ? 0.4398 0.5523 0.3180 -0.0366 0.1462  -0.0684 393 HOH   B O   
7812 O O   . HOH   F .   ? 0.6175 0.4697 0.4645 0.0590  0.0597  0.0872  394 HOH   B O   
7813 O O   . HOH   F .   ? 0.4191 0.2245 0.5180 -0.0440 0.0419  0.0853  395 HOH   B O   
7814 O O   . HOH   F .   ? 0.2778 0.4054 0.7242 -0.1224 -0.1159 0.0973  396 HOH   B O   
7815 O O   . HOH   F .   ? 0.4801 0.6952 0.5178 0.0853  0.0419  -0.1197 397 HOH   B O   
7816 O O   . HOH   F .   ? 0.6163 0.5278 0.5030 0.0969  0.1065  0.0931  398 HOH   B O   
7817 O O   . HOH   F .   ? 0.3677 0.4545 0.3849 -0.0087 0.0412  -0.0880 399 HOH   B O   
7818 O O   . HOH   F .   ? 0.2166 0.2736 0.6482 -0.0444 -0.0855 -0.0370 400 HOH   B O   
7819 O O   . HOH   F .   ? 0.6246 0.4208 0.3239 -0.2435 -0.0291 0.0822  401 HOH   B O   
7820 O O   . HOH   F .   ? 0.6292 0.4652 0.4643 -0.1611 -0.1321 0.2435  402 HOH   B O   
7821 O O   . HOH   F .   ? 0.4779 0.5012 0.2957 0.1759  -0.0267 -0.0480 403 HOH   B O   
# 
