data_7HE2
# 
_entry.id   7HE2 
# 
_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   7HE2         pdb_00007he2 10.2210/pdb7he2/pdb 
WWPDB D_1001407356 ?            ?                   
# 
_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                        7HE2 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                       18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'DIMETHYL SULFOXIDE'                                                             78.133    2   ? ? ? ? 
3 non-polymer syn '[(2R,4R)-4-methoxy-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' 248.281   1   ? ? ? ? 
4 water       nat water                                                                            18.015    431 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DIMETHYL SULFOXIDE'                                                             DMS   
3 '[(2R,4R)-4-methoxy-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' A1A9E 
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 
A1A9E non-polymer         . '[(2R,4R)-4-methoxy-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' ? 'C12 H16 N4 O2'  
248.281 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                             ? 'C2 H6 O S'      
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                        ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                  ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                          ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                        ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                            ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                       ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                          ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                           ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                       ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                    ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                          ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                           ? 'C3 H7 N O3'     
105.093 
THR   'L-peptide linking' y THREONINE                                                                        ? 'C4 H9 N O3'     
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                         ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                           ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 DMS   1   301 301  DMS   DMS A . 
D 2 DMS   1   302 401  DMS   DMS A . 
E 3 A1A9E 1   303 201  A1A9E LA1 A . 
F 4 HOH   1   401 247  HOH   HOH A . 
F 4 HOH   2   402 292  HOH   HOH A . 
F 4 HOH   3   403 229  HOH   HOH A . 
F 4 HOH   4   404 155  HOH   HOH A . 
F 4 HOH   5   405 196  HOH   HOH A . 
F 4 HOH   6   406 151  HOH   HOH A . 
F 4 HOH   7   407 1290 HOH   HOH A . 
F 4 HOH   8   408 625  HOH   HOH A . 
F 4 HOH   9   409 409  HOH   HOH A . 
F 4 HOH   10  410 96   HOH   HOH A . 
F 4 HOH   11  411 337  HOH   HOH A . 
F 4 HOH   12  412 1283 HOH   HOH A . 
F 4 HOH   13  413 209  HOH   HOH A . 
F 4 HOH   14  414 19   HOH   HOH A . 
F 4 HOH   15  415 1295 HOH   HOH A . 
F 4 HOH   16  416 76   HOH   HOH A . 
F 4 HOH   17  417 225  HOH   HOH A . 
F 4 HOH   18  418 109  HOH   HOH A . 
F 4 HOH   19  419 136  HOH   HOH A . 
F 4 HOH   20  420 93   HOH   HOH A . 
F 4 HOH   21  421 396  HOH   HOH A . 
F 4 HOH   22  422 49   HOH   HOH A . 
F 4 HOH   23  423 86   HOH   HOH A . 
F 4 HOH   24  424 18   HOH   HOH A . 
F 4 HOH   25  425 1300 HOH   HOH A . 
F 4 HOH   26  426 15   HOH   HOH A . 
F 4 HOH   27  427 15   HOH   HOH A . 
F 4 HOH   28  428 39   HOH   HOH A . 
F 4 HOH   29  429 124  HOH   HOH A . 
F 4 HOH   30  430 236  HOH   HOH A . 
F 4 HOH   31  431 140  HOH   HOH A . 
F 4 HOH   32  432 57   HOH   HOH A . 
F 4 HOH   33  433 33   HOH   HOH A . 
F 4 HOH   34  434 241  HOH   HOH A . 
F 4 HOH   35  435 105  HOH   HOH A . 
F 4 HOH   36  436 68   HOH   HOH A . 
F 4 HOH   37  437 36   HOH   HOH A . 
F 4 HOH   38  438 165  HOH   HOH A . 
F 4 HOH   39  439 320  HOH   HOH A . 
F 4 HOH   40  440 21   HOH   HOH A . 
F 4 HOH   41  441 148  HOH   HOH A . 
F 4 HOH   42  442 661  HOH   HOH A . 
F 4 HOH   43  443 1310 HOH   HOH A . 
F 4 HOH   44  444 17   HOH   HOH A . 
F 4 HOH   45  445 8    HOH   HOH A . 
F 4 HOH   46  446 469  HOH   HOH A . 
F 4 HOH   47  447 192  HOH   HOH A . 
F 4 HOH   48  448 662  HOH   HOH A . 
F 4 HOH   49  449 333  HOH   HOH A . 
F 4 HOH   50  450 1238 HOH   HOH A . 
F 4 HOH   51  451 42   HOH   HOH A . 
F 4 HOH   52  452 24   HOH   HOH A . 
F 4 HOH   53  453 964  HOH   HOH A . 
F 4 HOH   54  454 939  HOH   HOH A . 
F 4 HOH   55  455 630  HOH   HOH A . 
F 4 HOH   56  456 162  HOH   HOH A . 
F 4 HOH   57  457 102  HOH   HOH A . 
F 4 HOH   58  458 115  HOH   HOH A . 
F 4 HOH   59  459 164  HOH   HOH A . 
F 4 HOH   60  460 159  HOH   HOH A . 
F 4 HOH   61  461 169  HOH   HOH A . 
F 4 HOH   62  462 92   HOH   HOH A . 
F 4 HOH   63  463 14   HOH   HOH A . 
F 4 HOH   64  464 81   HOH   HOH A . 
F 4 HOH   65  465 139  HOH   HOH A . 
F 4 HOH   66  466 186  HOH   HOH A . 
F 4 HOH   67  467 66   HOH   HOH A . 
F 4 HOH   68  468 12   HOH   HOH A . 
F 4 HOH   69  469 2    HOH   HOH A . 
F 4 HOH   70  470 56   HOH   HOH A . 
F 4 HOH   71  471 19   HOH   HOH A . 
F 4 HOH   72  472 354  HOH   HOH A . 
F 4 HOH   73  473 45   HOH   HOH A . 
F 4 HOH   74  474 34   HOH   HOH A . 
F 4 HOH   75  475 195  HOH   HOH A . 
F 4 HOH   76  476 5    HOH   HOH A . 
F 4 HOH   77  477 138  HOH   HOH A . 
F 4 HOH   78  478 134  HOH   HOH A . 
F 4 HOH   79  479 218  HOH   HOH A . 
F 4 HOH   80  480 78   HOH   HOH A . 
F 4 HOH   81  481 35   HOH   HOH A . 
F 4 HOH   82  482 493  HOH   HOH A . 
F 4 HOH   83  483 1309 HOH   HOH A . 
F 4 HOH   84  484 46   HOH   HOH A . 
F 4 HOH   85  485 461  HOH   HOH A . 
F 4 HOH   86  486 154  HOH   HOH A . 
F 4 HOH   87  487 405  HOH   HOH A . 
F 4 HOH   88  488 1315 HOH   HOH A . 
F 4 HOH   89  489 1    HOH   HOH A . 
F 4 HOH   90  490 366  HOH   HOH A . 
F 4 HOH   91  491 116  HOH   HOH A . 
F 4 HOH   92  492 296  HOH   HOH A . 
F 4 HOH   93  493 153  HOH   HOH A . 
F 4 HOH   94  494 303  HOH   HOH A . 
F 4 HOH   95  495 6    HOH   HOH A . 
F 4 HOH   96  496 27   HOH   HOH A . 
F 4 HOH   97  497 22   HOH   HOH A . 
F 4 HOH   98  498 3    HOH   HOH A . 
F 4 HOH   99  499 58   HOH   HOH A . 
F 4 HOH   100 500 281  HOH   HOH A . 
F 4 HOH   101 501 85   HOH   HOH A . 
F 4 HOH   102 502 1301 HOH   HOH A . 
F 4 HOH   103 503 2    HOH   HOH A . 
F 4 HOH   104 504 212  HOH   HOH A . 
F 4 HOH   105 505 121  HOH   HOH A . 
F 4 HOH   106 506 122  HOH   HOH A . 
F 4 HOH   107 507 10   HOH   HOH A . 
F 4 HOH   108 508 278  HOH   HOH A . 
F 4 HOH   109 509 6    HOH   HOH A . 
F 4 HOH   110 510 4    HOH   HOH A . 
F 4 HOH   111 511 1296 HOH   HOH A . 
F 4 HOH   112 512 381  HOH   HOH A . 
F 4 HOH   113 513 74   HOH   HOH A . 
F 4 HOH   114 514 67   HOH   HOH A . 
F 4 HOH   115 515 952  HOH   HOH A . 
F 4 HOH   116 516 1279 HOH   HOH A . 
F 4 HOH   117 517 582  HOH   HOH A . 
F 4 HOH   118 518 8    HOH   HOH A . 
F 4 HOH   119 519 397  HOH   HOH A . 
F 4 HOH   120 520 123  HOH   HOH A . 
F 4 HOH   121 521 53   HOH   HOH A . 
F 4 HOH   122 522 12   HOH   HOH A . 
F 4 HOH   123 523 1222 HOH   HOH A . 
F 4 HOH   124 524 25   HOH   HOH A . 
F 4 HOH   125 525 1275 HOH   HOH A . 
F 4 HOH   126 526 26   HOH   HOH A . 
F 4 HOH   127 527 51   HOH   HOH A . 
F 4 HOH   128 528 132  HOH   HOH A . 
F 4 HOH   129 529 1068 HOH   HOH A . 
F 4 HOH   130 530 83   HOH   HOH A . 
F 4 HOH   131 531 199  HOH   HOH A . 
F 4 HOH   132 532 125  HOH   HOH A . 
F 4 HOH   133 533 95   HOH   HOH A . 
F 4 HOH   134 534 351  HOH   HOH A . 
F 4 HOH   135 535 11   HOH   HOH A . 
F 4 HOH   136 536 24   HOH   HOH A . 
F 4 HOH   137 537 1289 HOH   HOH A . 
F 4 HOH   138 538 70   HOH   HOH A . 
F 4 HOH   139 539 13   HOH   HOH A . 
F 4 HOH   140 540 20   HOH   HOH A . 
F 4 HOH   141 541 1313 HOH   HOH A . 
F 4 HOH   142 542 393  HOH   HOH A . 
F 4 HOH   143 543 7    HOH   HOH A . 
F 4 HOH   144 544 1308 HOH   HOH A . 
F 4 HOH   145 545 156  HOH   HOH A . 
F 4 HOH   146 546 1189 HOH   HOH A . 
F 4 HOH   147 547 71   HOH   HOH A . 
F 4 HOH   148 548 944  HOH   HOH A . 
F 4 HOH   149 549 80   HOH   HOH A . 
F 4 HOH   150 550 16   HOH   HOH A . 
F 4 HOH   151 551 79   HOH   HOH A . 
F 4 HOH   152 552 188  HOH   HOH A . 
F 4 HOH   153 553 94   HOH   HOH A . 
F 4 HOH   154 554 23   HOH   HOH A . 
F 4 HOH   155 555 104  HOH   HOH A . 
F 4 HOH   156 556 3    HOH   HOH A . 
F 4 HOH   157 557 4    HOH   HOH A . 
F 4 HOH   158 558 40   HOH   HOH A . 
F 4 HOH   159 559 7    HOH   HOH A . 
F 4 HOH   160 560 97   HOH   HOH A . 
F 4 HOH   161 561 576  HOH   HOH A . 
F 4 HOH   162 562 1286 HOH   HOH A . 
F 4 HOH   163 563 726  HOH   HOH A . 
F 4 HOH   164 564 330  HOH   HOH A . 
F 4 HOH   165 565 5    HOH   HOH A . 
F 4 HOH   166 566 73   HOH   HOH A . 
F 4 HOH   167 567 1094 HOH   HOH A . 
F 4 HOH   168 568 107  HOH   HOH A . 
F 4 HOH   169 569 1284 HOH   HOH A . 
F 4 HOH   170 570 163  HOH   HOH A . 
F 4 HOH   171 571 1119 HOH   HOH A . 
F 4 HOH   172 572 509  HOH   HOH A . 
F 4 HOH   173 573 1134 HOH   HOH A . 
F 4 HOH   174 574 21   HOH   HOH A . 
F 4 HOH   175 575 361  HOH   HOH A . 
F 4 HOH   176 576 801  HOH   HOH A . 
F 4 HOH   177 577 556  HOH   HOH A . 
F 4 HOH   178 578 408  HOH   HOH A . 
F 4 HOH   179 579 756  HOH   HOH A . 
F 4 HOH   180 580 280  HOH   HOH A . 
F 4 HOH   181 581 1314 HOH   HOH A . 
F 4 HOH   182 582 342  HOH   HOH A . 
F 4 HOH   183 583 224  HOH   HOH A . 
F 4 HOH   184 584 319  HOH   HOH A . 
F 4 HOH   185 585 126  HOH   HOH A . 
F 4 HOH   186 586 370  HOH   HOH A . 
F 4 HOH   187 587 1276 HOH   HOH A . 
F 4 HOH   188 588 63   HOH   HOH A . 
F 4 HOH   189 589 250  HOH   HOH A . 
F 4 HOH   190 590 1287 HOH   HOH A . 
F 4 HOH   191 591 1307 HOH   HOH A . 
F 4 HOH   192 592 267  HOH   HOH A . 
F 4 HOH   193 593 1306 HOH   HOH A . 
F 4 HOH   194 594 202  HOH   HOH A . 
F 4 HOH   195 595 711  HOH   HOH A . 
F 4 HOH   196 596 521  HOH   HOH A . 
F 4 HOH   197 597 919  HOH   HOH A . 
F 4 HOH   198 598 695  HOH   HOH A . 
F 4 HOH   199 599 674  HOH   HOH A . 
F 4 HOH   200 600 135  HOH   HOH A . 
F 4 HOH   201 601 16   HOH   HOH A . 
F 4 HOH   202 602 318  HOH   HOH A . 
F 4 HOH   203 603 309  HOH   HOH A . 
F 4 HOH   204 604 331  HOH   HOH A . 
F 4 HOH   205 605 1299 HOH   HOH A . 
F 4 HOH   206 606 263  HOH   HOH A . 
F 4 HOH   207 607 941  HOH   HOH A . 
F 4 HOH   208 608 315  HOH   HOH A . 
F 4 HOH   209 609 805  HOH   HOH A . 
F 4 HOH   210 610 208  HOH   HOH A . 
F 4 HOH   211 611 152  HOH   HOH A . 
F 4 HOH   212 612 1071 HOH   HOH A . 
F 4 HOH   213 613 180  HOH   HOH A . 
F 4 HOH   214 614 18   HOH   HOH A . 
F 4 HOH   215 615 350  HOH   HOH A . 
F 4 HOH   216 616 356  HOH   HOH A . 
F 4 HOH   217 617 363  HOH   HOH A . 
F 4 HOH   218 618 313  HOH   HOH A . 
F 4 HOH   219 619 9    HOH   HOH A . 
F 4 HOH   220 620 326  HOH   HOH A . 
F 4 HOH   221 621 17   HOH   HOH A . 
F 4 HOH   222 622 371  HOH   HOH A . 
F 4 HOH   223 623 185  HOH   HOH A . 
F 4 HOH   224 624 429  HOH   HOH A . 
F 4 HOH   225 625 772  HOH   HOH A . 
F 4 HOH   226 626 1074 HOH   HOH A . 
F 4 HOH   227 627 376  HOH   HOH A . 
F 4 HOH   228 628 1292 HOH   HOH A . 
F 4 HOH   229 629 346  HOH   HOH A . 
F 4 HOH   230 630 1078 HOH   HOH A . 
G 4 HOH   1   201 64   HOH   HOH B . 
G 4 HOH   2   202 358  HOH   HOH B . 
G 4 HOH   3   203 531  HOH   HOH B . 
G 4 HOH   4   204 900  HOH   HOH B . 
G 4 HOH   5   205 654  HOH   HOH B . 
G 4 HOH   6   206 758  HOH   HOH B . 
G 4 HOH   7   207 398  HOH   HOH B . 
G 4 HOH   8   208 549  HOH   HOH B . 
G 4 HOH   9   209 1249 HOH   HOH B . 
G 4 HOH   10  210 364  HOH   HOH B . 
G 4 HOH   11  211 240  HOH   HOH B . 
G 4 HOH   12  212 444  HOH   HOH B . 
G 4 HOH   13  213 743  HOH   HOH B . 
G 4 HOH   14  214 282  HOH   HOH B . 
G 4 HOH   15  215 50   HOH   HOH B . 
G 4 HOH   16  216 120  HOH   HOH B . 
G 4 HOH   17  217 353  HOH   HOH B . 
G 4 HOH   18  218 343  HOH   HOH B . 
G 4 HOH   19  219 264  HOH   HOH B . 
G 4 HOH   20  220 452  HOH   HOH B . 
G 4 HOH   21  221 1140 HOH   HOH B . 
G 4 HOH   22  222 232  HOH   HOH B . 
G 4 HOH   23  223 54   HOH   HOH B . 
G 4 HOH   24  224 205  HOH   HOH B . 
G 4 HOH   25  225 131  HOH   HOH B . 
G 4 HOH   26  226 332  HOH   HOH B . 
G 4 HOH   27  227 252  HOH   HOH B . 
G 4 HOH   28  228 75   HOH   HOH B . 
G 4 HOH   29  229 82   HOH   HOH B . 
G 4 HOH   30  230 166  HOH   HOH B . 
G 4 HOH   31  231 276  HOH   HOH B . 
G 4 HOH   32  232 128  HOH   HOH B . 
G 4 HOH   33  233 1278 HOH   HOH B . 
G 4 HOH   34  234 127  HOH   HOH B . 
G 4 HOH   35  235 231  HOH   HOH B . 
G 4 HOH   36  236 300  HOH   HOH B . 
G 4 HOH   37  237 723  HOH   HOH B . 
G 4 HOH   38  238 60   HOH   HOH B . 
G 4 HOH   39  239 272  HOH   HOH B . 
G 4 HOH   40  240 110  HOH   HOH B . 
G 4 HOH   41  241 1    HOH   HOH B . 
G 4 HOH   42  242 181  HOH   HOH B . 
G 4 HOH   43  243 9    HOH   HOH B . 
G 4 HOH   44  244 72   HOH   HOH B . 
G 4 HOH   45  245 14   HOH   HOH B . 
G 4 HOH   46  246 271  HOH   HOH B . 
G 4 HOH   47  247 129  HOH   HOH B . 
G 4 HOH   48  248 325  HOH   HOH B . 
G 4 HOH   49  249 143  HOH   HOH B . 
G 4 HOH   50  250 52   HOH   HOH B . 
G 4 HOH   51  251 30   HOH   HOH B . 
G 4 HOH   52  252 41   HOH   HOH B . 
G 4 HOH   53  253 133  HOH   HOH B . 
G 4 HOH   54  254 1312 HOH   HOH B . 
G 4 HOH   55  255 69   HOH   HOH B . 
G 4 HOH   56  256 62   HOH   HOH B . 
G 4 HOH   57  257 10   HOH   HOH B . 
G 4 HOH   58  258 172  HOH   HOH B . 
G 4 HOH   59  259 47   HOH   HOH B . 
G 4 HOH   60  260 144  HOH   HOH B . 
G 4 HOH   61  261 150  HOH   HOH B . 
G 4 HOH   62  262 391  HOH   HOH B . 
G 4 HOH   63  263 20   HOH   HOH B . 
G 4 HOH   64  264 242  HOH   HOH B . 
G 4 HOH   65  265 31   HOH   HOH B . 
G 4 HOH   66  266 103  HOH   HOH B . 
G 4 HOH   67  267 61   HOH   HOH B . 
G 4 HOH   68  268 341  HOH   HOH B . 
G 4 HOH   69  269 117  HOH   HOH B . 
G 4 HOH   70  270 221  HOH   HOH B . 
G 4 HOH   71  271 11   HOH   HOH B . 
G 4 HOH   72  272 84   HOH   HOH B . 
G 4 HOH   73  273 59   HOH   HOH B . 
G 4 HOH   74  274 77   HOH   HOH B . 
G 4 HOH   75  275 416  HOH   HOH B . 
G 4 HOH   76  276 235  HOH   HOH B . 
G 4 HOH   77  277 175  HOH   HOH B . 
G 4 HOH   78  278 302  HOH   HOH B . 
G 4 HOH   79  279 220  HOH   HOH B . 
G 4 HOH   80  280 106  HOH   HOH B . 
G 4 HOH   81  281 347  HOH   HOH B . 
G 4 HOH   82  282 43   HOH   HOH B . 
G 4 HOH   83  283 1277 HOH   HOH B . 
G 4 HOH   84  284 114  HOH   HOH B . 
G 4 HOH   85  285 243  HOH   HOH B . 
G 4 HOH   86  286 216  HOH   HOH B . 
G 4 HOH   87  287 147  HOH   HOH B . 
G 4 HOH   88  288 287  HOH   HOH B . 
G 4 HOH   89  289 22   HOH   HOH B . 
G 4 HOH   90  290 1305 HOH   HOH B . 
G 4 HOH   91  291 88   HOH   HOH B . 
G 4 HOH   92  292 89   HOH   HOH B . 
G 4 HOH   93  293 387  HOH   HOH B . 
G 4 HOH   94  294 1126 HOH   HOH B . 
G 4 HOH   95  295 215  HOH   HOH B . 
G 4 HOH   96  296 137  HOH   HOH B . 
G 4 HOH   97  297 99   HOH   HOH B . 
G 4 HOH   98  298 13   HOH   HOH B . 
G 4 HOH   99  299 316  HOH   HOH B . 
G 4 HOH   100 300 635  HOH   HOH B . 
G 4 HOH   101 301 160  HOH   HOH B . 
G 4 HOH   102 302 112  HOH   HOH B . 
G 4 HOH   103 303 1066 HOH   HOH B . 
G 4 HOH   104 304 1106 HOH   HOH B . 
G 4 HOH   105 305 142  HOH   HOH B . 
G 4 HOH   106 306 311  HOH   HOH B . 
G 4 HOH   107 307 32   HOH   HOH B . 
G 4 HOH   108 308 101  HOH   HOH B . 
G 4 HOH   109 309 170  HOH   HOH B . 
G 4 HOH   110 310 91   HOH   HOH B . 
G 4 HOH   111 311 37   HOH   HOH B . 
G 4 HOH   112 312 182  HOH   HOH B . 
G 4 HOH   113 313 38   HOH   HOH B . 
G 4 HOH   114 314 297  HOH   HOH B . 
G 4 HOH   115 315 299  HOH   HOH B . 
G 4 HOH   116 316 23   HOH   HOH B . 
G 4 HOH   117 317 48   HOH   HOH B . 
G 4 HOH   118 318 141  HOH   HOH B . 
G 4 HOH   119 319 118  HOH   HOH B . 
G 4 HOH   120 320 44   HOH   HOH B . 
G 4 HOH   121 321 28   HOH   HOH B . 
G 4 HOH   122 322 1291 HOH   HOH B . 
G 4 HOH   123 323 177  HOH   HOH B . 
G 4 HOH   124 324 704  HOH   HOH B . 
G 4 HOH   125 325 334  HOH   HOH B . 
G 4 HOH   126 326 100  HOH   HOH B . 
G 4 HOH   127 327 1294 HOH   HOH B . 
G 4 HOH   128 328 161  HOH   HOH B . 
G 4 HOH   129 329 29   HOH   HOH B . 
G 4 HOH   130 330 1274 HOH   HOH B . 
G 4 HOH   131 331 197  HOH   HOH B . 
G 4 HOH   132 332 717  HOH   HOH B . 
G 4 HOH   133 333 98   HOH   HOH B . 
G 4 HOH   134 334 207  HOH   HOH B . 
G 4 HOH   135 335 339  HOH   HOH B . 
G 4 HOH   136 336 1285 HOH   HOH B . 
G 4 HOH   137 337 65   HOH   HOH B . 
G 4 HOH   138 338 234  HOH   HOH B . 
G 4 HOH   139 339 55   HOH   HOH B . 
G 4 HOH   140 340 445  HOH   HOH B . 
G 4 HOH   141 341 1293 HOH   HOH B . 
G 4 HOH   142 342 619  HOH   HOH B . 
G 4 HOH   143 343 960  HOH   HOH B . 
G 4 HOH   144 344 90   HOH   HOH B . 
G 4 HOH   145 345 362  HOH   HOH B . 
G 4 HOH   146 346 1304 HOH   HOH B . 
G 4 HOH   147 347 463  HOH   HOH B . 
G 4 HOH   148 348 178  HOH   HOH B . 
G 4 HOH   149 349 191  HOH   HOH B . 
G 4 HOH   150 350 87   HOH   HOH B . 
G 4 HOH   151 351 1046 HOH   HOH B . 
G 4 HOH   152 352 335  HOH   HOH B . 
G 4 HOH   153 353 541  HOH   HOH B . 
G 4 HOH   154 354 623  HOH   HOH B . 
G 4 HOH   155 355 203  HOH   HOH B . 
G 4 HOH   156 356 304  HOH   HOH B . 
G 4 HOH   157 357 1280 HOH   HOH B . 
G 4 HOH   158 358 1077 HOH   HOH B . 
G 4 HOH   159 359 290  HOH   HOH B . 
G 4 HOH   160 360 389  HOH   HOH B . 
G 4 HOH   161 361 479  HOH   HOH B . 
G 4 HOH   162 362 283  HOH   HOH B . 
G 4 HOH   163 363 718  HOH   HOH B . 
G 4 HOH   164 364 1072 HOH   HOH B . 
G 4 HOH   165 365 898  HOH   HOH B . 
G 4 HOH   166 366 340  HOH   HOH B . 
G 4 HOH   167 367 615  HOH   HOH B . 
G 4 HOH   168 368 291  HOH   HOH B . 
G 4 HOH   169 369 1316 HOH   HOH B . 
G 4 HOH   170 370 373  HOH   HOH B . 
G 4 HOH   171 371 1303 HOH   HOH B . 
G 4 HOH   172 372 310  HOH   HOH B . 
G 4 HOH   173 373 667  HOH   HOH B . 
G 4 HOH   174 374 149  HOH   HOH B . 
G 4 HOH   175 375 190  HOH   HOH B . 
G 4 HOH   176 376 431  HOH   HOH B . 
G 4 HOH   177 377 418  HOH   HOH B . 
G 4 HOH   178 378 1163 HOH   HOH B . 
G 4 HOH   179 379 183  HOH   HOH B . 
G 4 HOH   180 380 1311 HOH   HOH B . 
G 4 HOH   181 381 1173 HOH   HOH B . 
G 4 HOH   182 382 1000 HOH   HOH B . 
G 4 HOH   183 383 176  HOH   HOH B . 
G 4 HOH   184 384 424  HOH   HOH B . 
G 4 HOH   185 385 491  HOH   HOH B . 
G 4 HOH   186 386 265  HOH   HOH B . 
G 4 HOH   187 387 248  HOH   HOH B . 
G 4 HOH   188 388 1298 HOH   HOH B . 
G 4 HOH   189 389 470  HOH   HOH B . 
G 4 HOH   190 390 981  HOH   HOH B . 
G 4 HOH   191 391 184  HOH   HOH B . 
G 4 HOH   192 392 360  HOH   HOH B . 
G 4 HOH   193 393 355  HOH   HOH B . 
G 4 HOH   194 394 410  HOH   HOH B . 
G 4 HOH   195 395 792  HOH   HOH B . 
G 4 HOH   196 396 566  HOH   HOH B . 
G 4 HOH   197 397 274  HOH   HOH B . 
G 4 HOH   198 398 157  HOH   HOH B . 
G 4 HOH   199 399 314  HOH   HOH B . 
G 4 HOH   200 400 321  HOH   HOH B . 
G 4 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HE2 
_cell.length_a           88.676 
_cell.length_b           88.676 
_cell.length_c           39.642 
_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                         7HE2 
_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          7HE2 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.72 
_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                     7HE2 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.340 
_reflns.d_resolution_high            0.980 
_reflns.number_obs                   175598 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.500 
_reflns.pdbx_Rmerge_I_obs            0.043 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.500 
_reflns.B_iso_Wilson_estimate        11.300 
_reflns.pdbx_redundancy              6.200 
_reflns.pdbx_Rrim_I_all              0.046 
_reflns.pdbx_Rpim_I_all              0.018 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1088651 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 0.980 1.000  ? 27398 8043 ? 1.261 ? ? ? 3.400 ? 0.800  ? ? ? ? ? ? 93.300 1.490 0.769 0.445 
1 2 5.370 44.340 ? 8015  1166 ? 0.032 ? ? ? 6.900 ? 60.100 ? ? ? ? ? ? 99.800 0.034 0.013 0.999 
# 
_refine.entry_id                                 7HE2 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9800 
_refine.ls_d_res_low                             44.3400 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4000 
_refine.ls_number_reflns_obs                     175431 
_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                          0.1465 
_refine.ls_R_factor_R_work                       0.1458 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1602 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  8467 
_refine.ls_number_reflns_R_work                  166964 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.5290 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1100 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                59.790 
_refine.B_iso_min                                8.240 
_refine.pdbx_overall_phase_error                 17.8000 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9800 
_refine_hist.d_res_low                        44.3400 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.number_atoms_solvent             431 
_refine_hist.number_atoms_total               3027 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           17.27 
_refine_hist.pdbx_B_iso_mean_solvent          28.83 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
0.9800 0.9900  30 91.0000  5097 . 0.4203 0.4055 . 262 0.0000 5359 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 96.0000  5194 . 0.3478 0.3487 . 272 0.0000 5466 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 98.0000  5538 . 0.3048 0.2792 . 270 0.0000 5808 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 100.0000 5547 . 0.2582 0.2678 . 248 0.0000 5795 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5561 . 0.2500 0.2430 . 305 0.0000 5866 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5528 . 0.2067 0.2021 . 306 0.0000 5834 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5540 . 0.1941 0.2128 . 303 0.0000 5843 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5570 . 0.1897 0.2337 . 252 0.0000 5822 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5616 . 0.1596 0.1877 . 294 0.0000 5910 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5574 . 0.1504 0.1546 . 300 0.0000 5874 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5551 . 0.1483 0.1712 . 252 0.0000 5803 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5605 . 0.1339 0.1516 . 252 0.0000 5857 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5604 . 0.1349 0.1747 . 292 0.0000 5896 . 'X-RAY DIFFRACTION' 
1.1800 1.2100  30 100.0000 5527 . 0.1252 0.1570 . 310 0.0000 5837 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5632 . 0.1292 0.1683 . 256 0.0000 5888 . 'X-RAY DIFFRACTION' 
1.2400 1.2600  30 100.0000 5614 . 0.1375 0.1529 . 269 0.0000 5883 . 'X-RAY DIFFRACTION' 
1.2600 1.3000  30 100.0000 5513 . 0.1273 0.1407 . 296 0.0000 5809 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5572 . 0.1304 0.1420 . 300 0.0000 5872 . 'X-RAY DIFFRACTION' 
1.3300 1.3700  30 100.0000 5589 . 0.1296 0.1471 . 298 0.0000 5887 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5646 . 0.1229 0.1502 . 248 0.0000 5894 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5567 . 0.1242 0.1296 . 304 0.0000 5871 . 'X-RAY DIFFRACTION' 
1.4600 1.5200  30 100.0000 5582 . 0.1187 0.1389 . 264 0.0000 5846 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 5633 . 0.1176 0.1332 . 300 0.0000 5933 . 'X-RAY DIFFRACTION' 
1.5900 1.6800  30 100.0000 5572 . 0.1181 0.1259 . 280 0.0000 5852 . 'X-RAY DIFFRACTION' 
1.6800 1.7800  30 100.0000 5648 . 0.1286 0.1455 . 264 0.0000 5912 . 'X-RAY DIFFRACTION' 
1.7800 1.9200  30 100.0000 5575 . 0.1334 0.1359 . 305 0.0000 5880 . 'X-RAY DIFFRACTION' 
1.9200 2.1100  30 100.0000 5666 . 0.1391 0.1507 . 282 0.0000 5948 . 'X-RAY DIFFRACTION' 
2.1100 2.4200  30 100.0000 5592 . 0.1408 0.1414 . 308 0.0000 5900 . 'X-RAY DIFFRACTION' 
2.4200 3.0500  30 100.0000 5708 . 0.1518 0.1743 . 294 0.0000 6002 . 'X-RAY DIFFRACTION' 
3.0500 44.3400 30 100.0000 5803 . 0.1503 0.1705 . 281 0.0000 6084 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HE2 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003656' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HE2 
_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 2 ? 
E N N 3 ? 
F N N 4 ? 
G 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 7HE2 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HE2 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 7HE2 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HE2 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HE2 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HE2 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N 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 ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HE2 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    138 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    404 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.60 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86 ? ? 54.71 -130.97 
2 1 HIS A 86 ? ? 54.71 -134.30 
3 1 HIS B 86 ? ? 57.45 -128.87 
# 
_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 628 ? 5.90 . 
2 1 O ? A HOH 629 ? 5.98 . 
3 1 O ? A HOH 630 ? 7.34 . 
4 1 O ? B HOH 401 ? 6.22 . 
# 
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 
A1A9E N2   N Y N 1   
A1A9E C3   C N N 2   
A1A9E C6   C Y N 3   
A1A9E C9   C Y N 4   
A1A9E C12  C N N 5   
A1A9E C1   C N N 6   
A1A9E C10  C Y N 7   
A1A9E C11  C Y N 8   
A1A9E C2   C N R 9   
A1A9E C4   C N R 10  
A1A9E C5   C N N 11  
A1A9E C7   C Y N 12  
A1A9E C8   C Y N 13  
A1A9E N1   N N N 14  
A1A9E N3   N Y N 15  
A1A9E N4   N Y N 16  
A1A9E O1   O N N 17  
A1A9E O2   O N N 18  
A1A9E H7   H N N 19  
A1A9E H6   H N N 20  
A1A9E H16  H N N 21  
A1A9E H15  H N N 22  
A1A9E H4   H N N 23  
A1A9E H5   H N N 24  
A1A9E H3   H N N 25  
A1A9E H12  H N N 26  
A1A9E H13  H N N 27  
A1A9E H1   H N N 28  
A1A9E H2   H N N 29  
A1A9E H8   H N N 30  
A1A9E H9   H N N 31  
A1A9E H11  H N N 32  
A1A9E H14  H N N 33  
A1A9E H10  H N N 34  
ALA   N    N N N 35  
ALA   CA   C N S 36  
ALA   C    C N N 37  
ALA   O    O N N 38  
ALA   CB   C N N 39  
ALA   OXT  O N N 40  
ALA   H    H N N 41  
ALA   H2   H N N 42  
ALA   HA   H N N 43  
ALA   HB1  H N N 44  
ALA   HB2  H N N 45  
ALA   HB3  H N N 46  
ALA   HXT  H N N 47  
ARG   N    N N N 48  
ARG   CA   C N S 49  
ARG   C    C N N 50  
ARG   O    O N N 51  
ARG   CB   C N N 52  
ARG   CG   C N N 53  
ARG   CD   C N N 54  
ARG   NE   N N N 55  
ARG   CZ   C N N 56  
ARG   NH1  N N N 57  
ARG   NH2  N N N 58  
ARG   OXT  O N N 59  
ARG   H    H N N 60  
ARG   H2   H N N 61  
ARG   HA   H N N 62  
ARG   HB2  H N N 63  
ARG   HB3  H N N 64  
ARG   HG2  H N N 65  
ARG   HG3  H N N 66  
ARG   HD2  H N N 67  
ARG   HD3  H N N 68  
ARG   HE   H N N 69  
ARG   HH11 H N N 70  
ARG   HH12 H N N 71  
ARG   HH21 H N N 72  
ARG   HH22 H N N 73  
ARG   HXT  H N N 74  
ASN   N    N N N 75  
ASN   CA   C N S 76  
ASN   C    C N N 77  
ASN   O    O N N 78  
ASN   CB   C N N 79  
ASN   CG   C N N 80  
ASN   OD1  O N N 81  
ASN   ND2  N N N 82  
ASN   OXT  O N N 83  
ASN   H    H N N 84  
ASN   H2   H N N 85  
ASN   HA   H N N 86  
ASN   HB2  H N N 87  
ASN   HB3  H N N 88  
ASN   HD21 H N N 89  
ASN   HD22 H N N 90  
ASN   HXT  H N N 91  
ASP   N    N N N 92  
ASP   CA   C N S 93  
ASP   C    C N N 94  
ASP   O    O N N 95  
ASP   CB   C N N 96  
ASP   CG   C N N 97  
ASP   OD1  O N N 98  
ASP   OD2  O N N 99  
ASP   OXT  O N N 100 
ASP   H    H N N 101 
ASP   H2   H N N 102 
ASP   HA   H N N 103 
ASP   HB2  H N N 104 
ASP   HB3  H N N 105 
ASP   HD2  H N N 106 
ASP   HXT  H N N 107 
CYS   N    N N N 108 
CYS   CA   C N R 109 
CYS   C    C N N 110 
CYS   O    O N N 111 
CYS   CB   C N N 112 
CYS   SG   S N N 113 
CYS   OXT  O N N 114 
CYS   H    H N N 115 
CYS   H2   H N N 116 
CYS   HA   H N N 117 
CYS   HB2  H N N 118 
CYS   HB3  H N N 119 
CYS   HG   H N N 120 
CYS   HXT  H N N 121 
DMS   S    S N N 122 
DMS   O    O N N 123 
DMS   C1   C N N 124 
DMS   C2   C N N 125 
DMS   H11  H N N 126 
DMS   H12  H N N 127 
DMS   H13  H N N 128 
DMS   H21  H N N 129 
DMS   H22  H N N 130 
DMS   H23  H N N 131 
GLN   N    N N N 132 
GLN   CA   C N S 133 
GLN   C    C N N 134 
GLN   O    O N N 135 
GLN   CB   C N N 136 
GLN   CG   C N N 137 
GLN   CD   C N N 138 
GLN   OE1  O N N 139 
GLN   NE2  N N N 140 
GLN   OXT  O N N 141 
GLN   H    H N N 142 
GLN   H2   H N N 143 
GLN   HA   H N N 144 
GLN   HB2  H N N 145 
GLN   HB3  H N N 146 
GLN   HG2  H N N 147 
GLN   HG3  H N N 148 
GLN   HE21 H N N 149 
GLN   HE22 H N N 150 
GLN   HXT  H N N 151 
GLU   N    N N N 152 
GLU   CA   C N S 153 
GLU   C    C N N 154 
GLU   O    O N N 155 
GLU   CB   C N N 156 
GLU   CG   C N N 157 
GLU   CD   C N N 158 
GLU   OE1  O N N 159 
GLU   OE2  O N N 160 
GLU   OXT  O N N 161 
GLU   H    H N N 162 
GLU   H2   H N N 163 
GLU   HA   H N N 164 
GLU   HB2  H N N 165 
GLU   HB3  H N N 166 
GLU   HG2  H N N 167 
GLU   HG3  H N N 168 
GLU   HE2  H N N 169 
GLU   HXT  H N N 170 
GLY   N    N N N 171 
GLY   CA   C N N 172 
GLY   C    C N N 173 
GLY   O    O N N 174 
GLY   OXT  O N N 175 
GLY   H    H N N 176 
GLY   H2   H N N 177 
GLY   HA2  H N N 178 
GLY   HA3  H N N 179 
GLY   HXT  H N N 180 
HIS   N    N N N 181 
HIS   CA   C N S 182 
HIS   C    C N N 183 
HIS   O    O N N 184 
HIS   CB   C N N 185 
HIS   CG   C Y N 186 
HIS   ND1  N Y N 187 
HIS   CD2  C Y N 188 
HIS   CE1  C Y N 189 
HIS   NE2  N Y N 190 
HIS   OXT  O N N 191 
HIS   H    H N N 192 
HIS   H2   H N N 193 
HIS   HA   H N N 194 
HIS   HB2  H N N 195 
HIS   HB3  H N N 196 
HIS   HD1  H N N 197 
HIS   HD2  H N N 198 
HIS   HE1  H N N 199 
HIS   HE2  H N N 200 
HIS   HXT  H N N 201 
HOH   O    O N N 202 
HOH   H1   H N N 203 
HOH   H2   H N N 204 
ILE   N    N N N 205 
ILE   CA   C N S 206 
ILE   C    C N N 207 
ILE   O    O N N 208 
ILE   CB   C N S 209 
ILE   CG1  C N N 210 
ILE   CG2  C N N 211 
ILE   CD1  C N N 212 
ILE   OXT  O N N 213 
ILE   H    H N N 214 
ILE   H2   H N N 215 
ILE   HA   H N N 216 
ILE   HB   H N N 217 
ILE   HG12 H N N 218 
ILE   HG13 H N N 219 
ILE   HG21 H N N 220 
ILE   HG22 H N N 221 
ILE   HG23 H N N 222 
ILE   HD11 H N N 223 
ILE   HD12 H N N 224 
ILE   HD13 H N N 225 
ILE   HXT  H N N 226 
LEU   N    N N N 227 
LEU   CA   C N S 228 
LEU   C    C N N 229 
LEU   O    O N N 230 
LEU   CB   C N N 231 
LEU   CG   C N N 232 
LEU   CD1  C N N 233 
LEU   CD2  C N N 234 
LEU   OXT  O N N 235 
LEU   H    H N N 236 
LEU   H2   H N N 237 
LEU   HA   H N N 238 
LEU   HB2  H N N 239 
LEU   HB3  H N N 240 
LEU   HG   H N N 241 
LEU   HD11 H N N 242 
LEU   HD12 H N N 243 
LEU   HD13 H N N 244 
LEU   HD21 H N N 245 
LEU   HD22 H N N 246 
LEU   HD23 H N N 247 
LEU   HXT  H N N 248 
LYS   N    N N N 249 
LYS   CA   C N S 250 
LYS   C    C N N 251 
LYS   O    O N N 252 
LYS   CB   C N N 253 
LYS   CG   C N N 254 
LYS   CD   C N N 255 
LYS   CE   C N N 256 
LYS   NZ   N N N 257 
LYS   OXT  O N N 258 
LYS   H    H N N 259 
LYS   H2   H N N 260 
LYS   HA   H N N 261 
LYS   HB2  H N N 262 
LYS   HB3  H N N 263 
LYS   HG2  H N N 264 
LYS   HG3  H N N 265 
LYS   HD2  H N N 266 
LYS   HD3  H N N 267 
LYS   HE2  H N N 268 
LYS   HE3  H N N 269 
LYS   HZ1  H N N 270 
LYS   HZ2  H N N 271 
LYS   HZ3  H N N 272 
LYS   HXT  H N N 273 
MET   N    N N N 274 
MET   CA   C N S 275 
MET   C    C N N 276 
MET   O    O N N 277 
MET   CB   C N N 278 
MET   CG   C N N 279 
MET   SD   S N N 280 
MET   CE   C N N 281 
MET   OXT  O N N 282 
MET   H    H N N 283 
MET   H2   H N N 284 
MET   HA   H N N 285 
MET   HB2  H N N 286 
MET   HB3  H N N 287 
MET   HG2  H N N 288 
MET   HG3  H N N 289 
MET   HE1  H N N 290 
MET   HE2  H N N 291 
MET   HE3  H N N 292 
MET   HXT  H N N 293 
PHE   N    N N N 294 
PHE   CA   C N S 295 
PHE   C    C N N 296 
PHE   O    O N N 297 
PHE   CB   C N N 298 
PHE   CG   C Y N 299 
PHE   CD1  C Y N 300 
PHE   CD2  C Y N 301 
PHE   CE1  C Y N 302 
PHE   CE2  C Y N 303 
PHE   CZ   C Y N 304 
PHE   OXT  O N N 305 
PHE   H    H N N 306 
PHE   H2   H N N 307 
PHE   HA   H N N 308 
PHE   HB2  H N N 309 
PHE   HB3  H N N 310 
PHE   HD1  H N N 311 
PHE   HD2  H N N 312 
PHE   HE1  H N N 313 
PHE   HE2  H N N 314 
PHE   HZ   H N N 315 
PHE   HXT  H N N 316 
PRO   N    N N N 317 
PRO   CA   C N S 318 
PRO   C    C N N 319 
PRO   O    O N N 320 
PRO   CB   C N N 321 
PRO   CG   C N N 322 
PRO   CD   C N N 323 
PRO   OXT  O N N 324 
PRO   H    H N N 325 
PRO   HA   H N N 326 
PRO   HB2  H N N 327 
PRO   HB3  H N N 328 
PRO   HG2  H N N 329 
PRO   HG3  H N N 330 
PRO   HD2  H N N 331 
PRO   HD3  H N N 332 
PRO   HXT  H N N 333 
SER   N    N N N 334 
SER   CA   C N S 335 
SER   C    C N N 336 
SER   O    O N N 337 
SER   CB   C N N 338 
SER   OG   O N N 339 
SER   OXT  O N N 340 
SER   H    H N N 341 
SER   H2   H N N 342 
SER   HA   H N N 343 
SER   HB2  H N N 344 
SER   HB3  H N N 345 
SER   HG   H N N 346 
SER   HXT  H N N 347 
THR   N    N N N 348 
THR   CA   C N S 349 
THR   C    C N N 350 
THR   O    O N N 351 
THR   CB   C N R 352 
THR   OG1  O N N 353 
THR   CG2  C N N 354 
THR   OXT  O N N 355 
THR   H    H N N 356 
THR   H2   H N N 357 
THR   HA   H N N 358 
THR   HB   H N N 359 
THR   HG1  H N N 360 
THR   HG21 H N N 361 
THR   HG22 H N N 362 
THR   HG23 H N N 363 
THR   HXT  H N N 364 
TYR   N    N N N 365 
TYR   CA   C N S 366 
TYR   C    C N N 367 
TYR   O    O N N 368 
TYR   CB   C N N 369 
TYR   CG   C Y N 370 
TYR   CD1  C Y N 371 
TYR   CD2  C Y N 372 
TYR   CE1  C Y N 373 
TYR   CE2  C Y N 374 
TYR   CZ   C Y N 375 
TYR   OH   O N N 376 
TYR   OXT  O N N 377 
TYR   H    H N N 378 
TYR   H2   H N N 379 
TYR   HA   H N N 380 
TYR   HB2  H N N 381 
TYR   HB3  H N N 382 
TYR   HD1  H N N 383 
TYR   HD2  H N N 384 
TYR   HE1  H N N 385 
TYR   HE2  H N N 386 
TYR   HH   H N N 387 
TYR   HXT  H N N 388 
VAL   N    N N N 389 
VAL   CA   C N S 390 
VAL   C    C N N 391 
VAL   O    O N N 392 
VAL   CB   C N N 393 
VAL   CG1  C N N 394 
VAL   CG2  C N N 395 
VAL   OXT  O N N 396 
VAL   H    H N N 397 
VAL   H2   H N N 398 
VAL   HA   H N N 399 
VAL   HB   H N N 400 
VAL   HG11 H N N 401 
VAL   HG12 H N N 402 
VAL   HG13 H N N 403 
VAL   HG21 H N N 404 
VAL   HG22 H N N 405 
VAL   HG23 H N N 406 
VAL   HXT  H N N 407 
# 
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 
A1A9E C1  O1   sing N N 1   
A1A9E C3  C2   sing N N 2   
A1A9E C3  C4   sing N N 3   
A1A9E C2  O1   sing N N 4   
A1A9E C2  C12  sing N N 5   
A1A9E C12 N1   sing N N 6   
A1A9E C4  C5   sing N N 7   
A1A9E C4  N1   sing N N 8   
A1A9E C5  O2   sing N N 9   
A1A9E N1  C6   sing N N 10  
A1A9E C6  N2   doub Y N 11  
A1A9E C6  C9   sing Y N 12  
A1A9E C10 C9   sing Y N 13  
A1A9E C10 C11  doub Y N 14  
A1A9E N2  C7   sing Y N 15  
A1A9E C9  C8   doub Y N 16  
A1A9E C11 N4   sing Y N 17  
A1A9E C7  N3   doub Y N 18  
A1A9E C8  N4   sing Y N 19  
A1A9E C8  N3   sing Y N 20  
A1A9E C3  H7   sing N N 21  
A1A9E C3  H6   sing N N 22  
A1A9E C12 H16  sing N N 23  
A1A9E C12 H15  sing N N 24  
A1A9E C1  H4   sing N N 25  
A1A9E C1  H5   sing N N 26  
A1A9E C1  H3   sing N N 27  
A1A9E C10 H12  sing N N 28  
A1A9E C11 H13  sing N N 29  
A1A9E C2  H1   sing N N 30  
A1A9E C4  H2   sing N N 31  
A1A9E C5  H8   sing N N 32  
A1A9E C5  H9   sing N N 33  
A1A9E C7  H11  sing N N 34  
A1A9E N4  H14  sing N N 35  
A1A9E O2  H10  sing N N 36  
ALA   N   CA   sing N N 37  
ALA   N   H    sing N N 38  
ALA   N   H2   sing N N 39  
ALA   CA  C    sing N N 40  
ALA   CA  CB   sing N N 41  
ALA   CA  HA   sing N N 42  
ALA   C   O    doub N N 43  
ALA   C   OXT  sing N N 44  
ALA   CB  HB1  sing N N 45  
ALA   CB  HB2  sing N N 46  
ALA   CB  HB3  sing N N 47  
ALA   OXT HXT  sing N N 48  
ARG   N   CA   sing N N 49  
ARG   N   H    sing N N 50  
ARG   N   H2   sing N N 51  
ARG   CA  C    sing N N 52  
ARG   CA  CB   sing N N 53  
ARG   CA  HA   sing N N 54  
ARG   C   O    doub N N 55  
ARG   C   OXT  sing N N 56  
ARG   CB  CG   sing N N 57  
ARG   CB  HB2  sing N N 58  
ARG   CB  HB3  sing N N 59  
ARG   CG  CD   sing N N 60  
ARG   CG  HG2  sing N N 61  
ARG   CG  HG3  sing N N 62  
ARG   CD  NE   sing N N 63  
ARG   CD  HD2  sing N N 64  
ARG   CD  HD3  sing N N 65  
ARG   NE  CZ   sing N N 66  
ARG   NE  HE   sing N N 67  
ARG   CZ  NH1  sing N N 68  
ARG   CZ  NH2  doub N N 69  
ARG   NH1 HH11 sing N N 70  
ARG   NH1 HH12 sing N N 71  
ARG   NH2 HH21 sing N N 72  
ARG   NH2 HH22 sing N N 73  
ARG   OXT HXT  sing N N 74  
ASN   N   CA   sing N N 75  
ASN   N   H    sing N N 76  
ASN   N   H2   sing N N 77  
ASN   CA  C    sing N N 78  
ASN   CA  CB   sing N N 79  
ASN   CA  HA   sing N N 80  
ASN   C   O    doub N N 81  
ASN   C   OXT  sing N N 82  
ASN   CB  CG   sing N N 83  
ASN   CB  HB2  sing N N 84  
ASN   CB  HB3  sing N N 85  
ASN   CG  OD1  doub N N 86  
ASN   CG  ND2  sing N N 87  
ASN   ND2 HD21 sing N N 88  
ASN   ND2 HD22 sing N N 89  
ASN   OXT HXT  sing N N 90  
ASP   N   CA   sing N N 91  
ASP   N   H    sing N N 92  
ASP   N   H2   sing N N 93  
ASP   CA  C    sing N N 94  
ASP   CA  CB   sing N N 95  
ASP   CA  HA   sing N N 96  
ASP   C   O    doub N N 97  
ASP   C   OXT  sing N N 98  
ASP   CB  CG   sing N N 99  
ASP   CB  HB2  sing N N 100 
ASP   CB  HB3  sing N N 101 
ASP   CG  OD1  doub N N 102 
ASP   CG  OD2  sing N N 103 
ASP   OD2 HD2  sing N N 104 
ASP   OXT HXT  sing N N 105 
CYS   N   CA   sing N N 106 
CYS   N   H    sing N N 107 
CYS   N   H2   sing N N 108 
CYS   CA  C    sing N N 109 
CYS   CA  CB   sing N N 110 
CYS   CA  HA   sing N N 111 
CYS   C   O    doub N N 112 
CYS   C   OXT  sing N N 113 
CYS   CB  SG   sing N N 114 
CYS   CB  HB2  sing N N 115 
CYS   CB  HB3  sing N N 116 
CYS   SG  HG   sing N N 117 
CYS   OXT HXT  sing N N 118 
DMS   S   O    doub N N 119 
DMS   S   C1   sing N N 120 
DMS   S   C2   sing N N 121 
DMS   C1  H11  sing N N 122 
DMS   C1  H12  sing N N 123 
DMS   C1  H13  sing N N 124 
DMS   C2  H21  sing N N 125 
DMS   C2  H22  sing N N 126 
DMS   C2  H23  sing N N 127 
GLN   N   CA   sing N N 128 
GLN   N   H    sing N N 129 
GLN   N   H2   sing N N 130 
GLN   CA  C    sing N N 131 
GLN   CA  CB   sing N N 132 
GLN   CA  HA   sing N N 133 
GLN   C   O    doub N N 134 
GLN   C   OXT  sing N N 135 
GLN   CB  CG   sing N N 136 
GLN   CB  HB2  sing N N 137 
GLN   CB  HB3  sing N N 138 
GLN   CG  CD   sing N N 139 
GLN   CG  HG2  sing N N 140 
GLN   CG  HG3  sing N N 141 
GLN   CD  OE1  doub N N 142 
GLN   CD  NE2  sing N N 143 
GLN   NE2 HE21 sing N N 144 
GLN   NE2 HE22 sing N N 145 
GLN   OXT HXT  sing N N 146 
GLU   N   CA   sing N N 147 
GLU   N   H    sing N N 148 
GLU   N   H2   sing N N 149 
GLU   CA  C    sing N N 150 
GLU   CA  CB   sing N N 151 
GLU   CA  HA   sing N N 152 
GLU   C   O    doub N N 153 
GLU   C   OXT  sing N N 154 
GLU   CB  CG   sing N N 155 
GLU   CB  HB2  sing N N 156 
GLU   CB  HB3  sing N N 157 
GLU   CG  CD   sing N N 158 
GLU   CG  HG2  sing N N 159 
GLU   CG  HG3  sing N N 160 
GLU   CD  OE1  doub N N 161 
GLU   CD  OE2  sing N N 162 
GLU   OE2 HE2  sing N N 163 
GLU   OXT HXT  sing N N 164 
GLY   N   CA   sing N N 165 
GLY   N   H    sing N N 166 
GLY   N   H2   sing N N 167 
GLY   CA  C    sing N N 168 
GLY   CA  HA2  sing N N 169 
GLY   CA  HA3  sing N N 170 
GLY   C   O    doub N N 171 
GLY   C   OXT  sing N N 172 
GLY   OXT HXT  sing N N 173 
HIS   N   CA   sing N N 174 
HIS   N   H    sing N N 175 
HIS   N   H2   sing N N 176 
HIS   CA  C    sing N N 177 
HIS   CA  CB   sing N N 178 
HIS   CA  HA   sing N N 179 
HIS   C   O    doub N N 180 
HIS   C   OXT  sing N N 181 
HIS   CB  CG   sing N N 182 
HIS   CB  HB2  sing N N 183 
HIS   CB  HB3  sing N N 184 
HIS   CG  ND1  sing Y N 185 
HIS   CG  CD2  doub Y N 186 
HIS   ND1 CE1  doub Y N 187 
HIS   ND1 HD1  sing N N 188 
HIS   CD2 NE2  sing Y N 189 
HIS   CD2 HD2  sing N N 190 
HIS   CE1 NE2  sing Y N 191 
HIS   CE1 HE1  sing N N 192 
HIS   NE2 HE2  sing N N 193 
HIS   OXT HXT  sing N N 194 
HOH   O   H1   sing N N 195 
HOH   O   H2   sing N N 196 
ILE   N   CA   sing N N 197 
ILE   N   H    sing N N 198 
ILE   N   H2   sing N N 199 
ILE   CA  C    sing N N 200 
ILE   CA  CB   sing N N 201 
ILE   CA  HA   sing N N 202 
ILE   C   O    doub N N 203 
ILE   C   OXT  sing N N 204 
ILE   CB  CG1  sing N N 205 
ILE   CB  CG2  sing N N 206 
ILE   CB  HB   sing N N 207 
ILE   CG1 CD1  sing N N 208 
ILE   CG1 HG12 sing N N 209 
ILE   CG1 HG13 sing N N 210 
ILE   CG2 HG21 sing N N 211 
ILE   CG2 HG22 sing N N 212 
ILE   CG2 HG23 sing N N 213 
ILE   CD1 HD11 sing N N 214 
ILE   CD1 HD12 sing N N 215 
ILE   CD1 HD13 sing N N 216 
ILE   OXT HXT  sing N N 217 
LEU   N   CA   sing N N 218 
LEU   N   H    sing N N 219 
LEU   N   H2   sing N N 220 
LEU   CA  C    sing N N 221 
LEU   CA  CB   sing N N 222 
LEU   CA  HA   sing N N 223 
LEU   C   O    doub N N 224 
LEU   C   OXT  sing N N 225 
LEU   CB  CG   sing N N 226 
LEU   CB  HB2  sing N N 227 
LEU   CB  HB3  sing N N 228 
LEU   CG  CD1  sing N N 229 
LEU   CG  CD2  sing N N 230 
LEU   CG  HG   sing N N 231 
LEU   CD1 HD11 sing N N 232 
LEU   CD1 HD12 sing N N 233 
LEU   CD1 HD13 sing N N 234 
LEU   CD2 HD21 sing N N 235 
LEU   CD2 HD22 sing N N 236 
LEU   CD2 HD23 sing N N 237 
LEU   OXT HXT  sing N N 238 
LYS   N   CA   sing N N 239 
LYS   N   H    sing N N 240 
LYS   N   H2   sing N N 241 
LYS   CA  C    sing N N 242 
LYS   CA  CB   sing N N 243 
LYS   CA  HA   sing N N 244 
LYS   C   O    doub N N 245 
LYS   C   OXT  sing N N 246 
LYS   CB  CG   sing N N 247 
LYS   CB  HB2  sing N N 248 
LYS   CB  HB3  sing N N 249 
LYS   CG  CD   sing N N 250 
LYS   CG  HG2  sing N N 251 
LYS   CG  HG3  sing N N 252 
LYS   CD  CE   sing N N 253 
LYS   CD  HD2  sing N N 254 
LYS   CD  HD3  sing N N 255 
LYS   CE  NZ   sing N N 256 
LYS   CE  HE2  sing N N 257 
LYS   CE  HE3  sing N N 258 
LYS   NZ  HZ1  sing N N 259 
LYS   NZ  HZ2  sing N N 260 
LYS   NZ  HZ3  sing N N 261 
LYS   OXT HXT  sing N N 262 
MET   N   CA   sing N N 263 
MET   N   H    sing N N 264 
MET   N   H2   sing N N 265 
MET   CA  C    sing N N 266 
MET   CA  CB   sing N N 267 
MET   CA  HA   sing N N 268 
MET   C   O    doub N N 269 
MET   C   OXT  sing N N 270 
MET   CB  CG   sing N N 271 
MET   CB  HB2  sing N N 272 
MET   CB  HB3  sing N N 273 
MET   CG  SD   sing N N 274 
MET   CG  HG2  sing N N 275 
MET   CG  HG3  sing N N 276 
MET   SD  CE   sing N N 277 
MET   CE  HE1  sing N N 278 
MET   CE  HE2  sing N N 279 
MET   CE  HE3  sing N N 280 
MET   OXT HXT  sing N N 281 
PHE   N   CA   sing N N 282 
PHE   N   H    sing N N 283 
PHE   N   H2   sing N N 284 
PHE   CA  C    sing N N 285 
PHE   CA  CB   sing N N 286 
PHE   CA  HA   sing N N 287 
PHE   C   O    doub N N 288 
PHE   C   OXT  sing N N 289 
PHE   CB  CG   sing N N 290 
PHE   CB  HB2  sing N N 291 
PHE   CB  HB3  sing N N 292 
PHE   CG  CD1  doub Y N 293 
PHE   CG  CD2  sing Y N 294 
PHE   CD1 CE1  sing Y N 295 
PHE   CD1 HD1  sing N N 296 
PHE   CD2 CE2  doub Y N 297 
PHE   CD2 HD2  sing N N 298 
PHE   CE1 CZ   doub Y N 299 
PHE   CE1 HE1  sing N N 300 
PHE   CE2 CZ   sing Y N 301 
PHE   CE2 HE2  sing N N 302 
PHE   CZ  HZ   sing N N 303 
PHE   OXT HXT  sing N N 304 
PRO   N   CA   sing N N 305 
PRO   N   CD   sing N N 306 
PRO   N   H    sing N N 307 
PRO   CA  C    sing N N 308 
PRO   CA  CB   sing N N 309 
PRO   CA  HA   sing N N 310 
PRO   C   O    doub N N 311 
PRO   C   OXT  sing N N 312 
PRO   CB  CG   sing N N 313 
PRO   CB  HB2  sing N N 314 
PRO   CB  HB3  sing N N 315 
PRO   CG  CD   sing N N 316 
PRO   CG  HG2  sing N N 317 
PRO   CG  HG3  sing N N 318 
PRO   CD  HD2  sing N N 319 
PRO   CD  HD3  sing N N 320 
PRO   OXT HXT  sing N N 321 
SER   N   CA   sing N N 322 
SER   N   H    sing N N 323 
SER   N   H2   sing N N 324 
SER   CA  C    sing N N 325 
SER   CA  CB   sing N N 326 
SER   CA  HA   sing N N 327 
SER   C   O    doub N N 328 
SER   C   OXT  sing N N 329 
SER   CB  OG   sing N N 330 
SER   CB  HB2  sing N N 331 
SER   CB  HB3  sing N N 332 
SER   OG  HG   sing N N 333 
SER   OXT HXT  sing N N 334 
THR   N   CA   sing N N 335 
THR   N   H    sing N N 336 
THR   N   H2   sing N N 337 
THR   CA  C    sing N N 338 
THR   CA  CB   sing N N 339 
THR   CA  HA   sing N N 340 
THR   C   O    doub N N 341 
THR   C   OXT  sing N N 342 
THR   CB  OG1  sing N N 343 
THR   CB  CG2  sing N N 344 
THR   CB  HB   sing N N 345 
THR   OG1 HG1  sing N N 346 
THR   CG2 HG21 sing N N 347 
THR   CG2 HG22 sing N N 348 
THR   CG2 HG23 sing N N 349 
THR   OXT HXT  sing N N 350 
TYR   N   CA   sing N N 351 
TYR   N   H    sing N N 352 
TYR   N   H2   sing N N 353 
TYR   CA  C    sing N N 354 
TYR   CA  CB   sing N N 355 
TYR   CA  HA   sing N N 356 
TYR   C   O    doub N N 357 
TYR   C   OXT  sing N N 358 
TYR   CB  CG   sing N N 359 
TYR   CB  HB2  sing N N 360 
TYR   CB  HB3  sing N N 361 
TYR   CG  CD1  doub Y N 362 
TYR   CG  CD2  sing Y N 363 
TYR   CD1 CE1  sing Y N 364 
TYR   CD1 HD1  sing N N 365 
TYR   CD2 CE2  doub Y N 366 
TYR   CD2 HD2  sing N N 367 
TYR   CE1 CZ   doub Y N 368 
TYR   CE1 HE1  sing N N 369 
TYR   CE2 CZ   sing Y N 370 
TYR   CE2 HE2  sing N N 371 
TYR   CZ  OH   sing N N 372 
TYR   OH  HH   sing N N 373 
TYR   OXT HXT  sing N N 374 
VAL   N   CA   sing N N 375 
VAL   N   H    sing N N 376 
VAL   N   H2   sing N N 377 
VAL   CA  C    sing N N 378 
VAL   CA  CB   sing N N 379 
VAL   CA  HA   sing N N 380 
VAL   C   O    doub N N 381 
VAL   C   OXT  sing N N 382 
VAL   CB  CG1  sing N N 383 
VAL   CB  CG2  sing N N 384 
VAL   CB  HB   sing N N 385 
VAL   CG1 HG11 sing N N 386 
VAL   CG1 HG12 sing N N 387 
VAL   CG1 HG13 sing N N 388 
VAL   CG2 HG21 sing N N 389 
VAL   CG2 HG22 sing N N 390 
VAL   CG2 HG23 sing N N 391 
VAL   OXT HXT  sing N N 392 
# 
_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                    7HE2 
_atom_sites.fract_transf_matrix[1][1]   0.011277 
_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]   0.011277 
_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]   0.025226 
_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 
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   ? 19.655 -16.199 22.279  0.48 49.00 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.613 -16.155 22.408  0.52 49.04 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.662 -15.143 22.432  0.48 48.55 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.635 -15.086 22.565  0.52 48.58 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.297 -13.781 22.165  0.48 47.11 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.268 -13.740 22.238  0.52 47.14 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.422 -13.514 22.588  0.48 47.52 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.378 -13.446 22.683  0.52 47.57 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 17.996 -15.199 23.823  0.48 49.18 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.026 -15.089 23.983  0.52 49.16 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 16.945 -14.107 23.960  0.48 49.35 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.995 -13.977 24.124  0.52 49.33 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.376 -16.570 24.060  0.48 49.34 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.403 -16.443 24.291  0.52 49.31 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.964 -15.271 21.774  0.48 58.24 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.913 -15.230 21.939  0.52 58.27 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.670 -15.055 24.505  0.48 58.99 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.729 -14.929 24.633  0.52 58.97 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.435 -14.261 24.772  0.48 59.19 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.497 -14.112 24.946  0.52 59.17 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.386 -13.245 24.007  0.48 59.19 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.451 -13.122 24.153  0.52 59.17 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.355 -14.138 23.191  0.48 59.19 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.393 -14.008 23.365  0.52 59.17 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.897 -16.559 24.904  0.48 59.18 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.965 -16.401 25.155  0.52 59.15 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.762 -16.767 23.335  0.48 59.18 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.755 -16.655 23.601  0.52 59.15 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.080 -17.236 24.088  0.48 59.18 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.101 -17.116 24.307  0.52 59.15 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.566 -12.927 21.449  1.00 44.93 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.007 -11.573 21.134  1.00 40.27 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 17.848 -10.611 21.372  1.00 36.38 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.750 -11.015 21.770  1.00 35.88 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.568 -11.467 19.708  1.00 39.24 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.556 -11.841 18.649  1.00 38.26 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.449 -11.304 18.612  1.00 37.81 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 18.933 -12.770 17.776  1.00 37.97 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.789 -13.115 21.130  0.48 53.90 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.821 -13.144 21.076  0.52 53.90 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.720 -11.332 21.739  1.00 48.30 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 19.845 -10.551 19.546  1.00 47.07 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.327 -12.063 19.623  1.00 47.07 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.398 -13.019 17.151  1.00 45.54 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.717 -13.122 17.835  1.00 45.54 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.092 -9.325  21.118  1.00 32.86 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.170 -8.265  21.506  1.00 29.67 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.296 -7.761  20.359  1.00 25.55 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.581 -6.770  20.532  1.00 26.20 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 17.930 -7.104  22.154  1.00 31.03 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 18.851 -6.525  21.248  1.00 31.67 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 18.793 -9.042  20.708  1.00 39.41 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.572 -8.617  22.178  1.00 35.58 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.294 -6.426  22.435  1.00 37.22 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.416 -7.438  22.928  1.00 37.22 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.260 -5.889  21.622  1.00 37.98 ?  5   SER   A HG   1 
ATOM   57   N N    A PHE   A 1 6   ? 16.387 -8.400  19.192  0.48 22.34 ?  6   PHE   A N    1 
ATOM   58   N N    B PHE   A 1 6   ? 16.281 -8.424  19.209  0.52 23.36 ?  6   PHE   A N    1 
ATOM   59   C CA   A PHE   A 1 6   ? 15.510 -8.093  18.072  0.48 19.40 ?  6   PHE   A CA   1 
ATOM   60   C CA   B PHE   A 1 6   ? 15.366 -7.993  18.157  0.52 21.22 ?  6   PHE   A CA   1 
ATOM   61   C C    A PHE   A 1 6   ? 14.086 -8.497  18.426  0.48 19.22 ?  6   PHE   A C    1 
ATOM   62   C C    B PHE   A 1 6   ? 13.925 -8.311  18.550  0.52 21.00 ?  6   PHE   A C    1 
ATOM   63   O O    A PHE   A 1 6   ? 13.835 -9.641  18.810  0.48 19.55 ?  6   PHE   A O    1 
ATOM   64   O O    B PHE   A 1 6   ? 13.651 -9.345  19.164  0.52 21.79 ?  6   PHE   A O    1 
ATOM   65   C CB   A PHE   A 1 6   ? 15.967 -8.873  16.839  0.48 17.64 ?  6   PHE   A CB   1 
ATOM   66   C CB   B PHE   A 1 6   ? 15.725 -8.656  16.831  0.52 19.93 ?  6   PHE   A CB   1 
ATOM   67   C CG   A PHE   A 1 6   ? 17.266 -8.382  16.249  0.48 16.70 ?  6   PHE   A CG   1 
ATOM   68   C CG   B PHE   A 1 6   ? 17.019 -8.163  16.248  0.52 19.40 ?  6   PHE   A CG   1 
ATOM   69   C CD1  A PHE   A 1 6   ? 17.309 -7.200  15.533  0.48 16.17 ?  6   PHE   A CD1  1 
ATOM   70   C CD1  B PHE   A 1 6   ? 17.056 -7.000  15.497  0.52 19.19 ?  6   PHE   A CD1  1 
ATOM   71   C CD2  A PHE   A 1 6   ? 18.436 -9.115  16.393  0.48 17.07 ?  6   PHE   A CD2  1 
ATOM   72   C CD2  B PHE   A 1 6   ? 18.198 -8.856  16.462  0.52 19.86 ?  6   PHE   A CD2  1 
ATOM   73   C CE1  A PHE   A 1 6   ? 18.495 -6.746  14.981  0.48 16.43 ?  6   PHE   A CE1  1 
ATOM   74   C CE1  B PHE   A 1 6   ? 18.246 -6.541  14.963  0.52 19.39 ?  6   PHE   A CE1  1 
ATOM   75   C CE2  A PHE   A 1 6   ? 19.624 -8.666  15.841  0.48 17.15 ?  6   PHE   A CE2  1 
ATOM   76   C CE2  B PHE   A 1 6   ? 19.388 -8.404  15.930  0.52 20.04 ?  6   PHE   A CE2  1 
ATOM   77   C CZ   A PHE   A 1 6   ? 19.653 -7.480  15.135  0.48 16.80 ?  6   PHE   A CZ   1 
ATOM   78   C CZ   B PHE   A 1 6   ? 19.413 -7.244  15.180  0.52 19.69 ?  6   PHE   A CZ   1 
ATOM   79   H H    A PHE   A 1 6   ? 16.950 -9.028  19.029  0.48 26.79 ?  6   PHE   A H    1 
ATOM   80   H H    B PHE   A 1 6   ? 16.762 -9.111  19.021  0.52 28.01 ?  6   PHE   A H    1 
ATOM   81   H HA   A PHE   A 1 6   ? 15.532 -7.147  17.880  0.48 23.25 ?  6   PHE   A HA   1 
ATOM   82   H HA   B PHE   A 1 6   ? 15.437 -7.036  18.049  0.52 25.44 ?  6   PHE   A HA   1 
ATOM   83   H HB2  A PHE   A 1 6   ? 16.085 -9.807  17.087  0.48 21.15 ?  6   PHE   A HB2  1 
ATOM   84   H HB2  B PHE   A 1 6   ? 15.801 -9.613  16.971  0.52 23.89 ?  6   PHE   A HB2  1 
ATOM   85   H HB3  A PHE   A 1 6   ? 15.284 -8.803  16.155  0.48 21.15 ?  6   PHE   A HB3  1 
ATOM   86   H HB3  B PHE   A 1 6   ? 15.016 -8.474  16.192  0.52 23.89 ?  6   PHE   A HB3  1 
ATOM   87   H HD1  A PHE   A 1 6   ? 16.531 -6.705  15.426  0.48 19.38 ?  6   PHE   A HD1  1 
ATOM   88   H HD1  B PHE   A 1 6   ? 16.268 -6.523  15.348  0.52 23.00 ?  6   PHE   A HD1  1 
ATOM   89   H HD2  A PHE   A 1 6   ? 18.424 -9.916  16.870  0.48 20.46 ?  6   PHE   A HD2  1 
ATOM   90   H HD2  B PHE   A 1 6   ? 18.184 -9.637  16.969  0.52 23.81 ?  6   PHE   A HD2  1 
ATOM   91   H HE1  A PHE   A 1 6   ? 18.510 -5.950  14.504  0.48 19.69 ?  6   PHE   A HE1  1 
ATOM   92   H HE1  B PHE   A 1 6   ? 18.259 -5.760  14.457  0.52 23.24 ?  6   PHE   A HE1  1 
ATOM   93   H HE2  A PHE   A 1 6   ? 20.406 -9.162  15.948  0.48 20.56 ?  6   PHE   A HE2  1 
ATOM   94   H HE2  B PHE   A 1 6   ? 20.174 -8.878  16.080  0.52 24.02 ?  6   PHE   A HE2  1 
ATOM   95   H HZ   A PHE   A 1 6   ? 20.450 -7.177  14.764  0.48 20.13 ?  6   PHE   A HZ   1 
ATOM   96   H HZ   B PHE   A 1 6   ? 20.213 -6.937  14.823  0.52 23.60 ?  6   PHE   A HZ   1 
ATOM   97   N N    A SER   A 1 7   ? 13.150 -7.562  18.285  0.48 19.12 ?  7   SER   A N    1 
ATOM   98   N N    B SER   A 1 7   ? 13.001 -7.409  18.202  0.52 20.27 ?  7   SER   A N    1 
ATOM   99   C CA   A SER   A 1 7   ? 11.785 -7.751  18.755  0.48 19.34 ?  7   SER   A CA   1 
ATOM   100  C CA   B SER   A 1 7   ? 11.625 -7.471  18.687  0.52 19.89 ?  7   SER   A CA   1 
ATOM   101  C C    A SER   A 1 7   ? 10.793 -7.437  17.643  0.48 17.89 ?  7   SER   A C    1 
ATOM   102  C C    B SER   A 1 7   ? 10.628 -7.320  17.544  0.52 17.99 ?  7   SER   A C    1 
ATOM   103  O O    A SER   A 1 7   ? 11.018 -6.545  16.821  0.48 18.14 ?  7   SER   A O    1 
ATOM   104  O O    B SER   A 1 7   ? 10.775 -6.443  16.689  0.52 17.92 ?  7   SER   A O    1 
ATOM   105  C CB   A SER   A 1 7   ? 11.499 -6.835  19.950  0.48 21.01 ?  7   SER   A CB   1 
ATOM   106  C CB   B SER   A 1 7   ? 11.368 -6.368  19.730  0.52 21.51 ?  7   SER   A CB   1 
ATOM   107  O OG   A SER   A 1 7   ? 10.167 -6.986  20.403  0.48 22.42 ?  7   SER   A OG   1 
ATOM   108  O OG   B SER   A 1 7   ? 10.022 -6.376  20.171  0.52 22.95 ?  7   SER   A OG   1 
ATOM   109  H H    A SER   A 1 7   ? 13.286 -6.802  17.910  0.48 22.92 ?  7   SER   A H    1 
ATOM   110  H H    B SER   A 1 7   ? 13.152 -6.739  17.684  0.52 24.31 ?  7   SER   A H    1 
ATOM   111  H HA   A SER   A 1 7   ? 11.657 -8.671  19.036  0.48 23.19 ?  7   SER   A HA   1 
ATOM   112  H HA   B SER   A 1 7   ? 11.467 -8.326  19.111  0.52 23.85 ?  7   SER   A HA   1 
ATOM   113  H HB2  A SER   A 1 7   ? 12.093 -7.070  20.677  0.48 25.19 ?  7   SER   A HB2  1 
ATOM   114  H HB2  B SER   A 1 7   ? 11.956 -6.509  20.490  0.52 25.79 ?  7   SER   A HB2  1 
ATOM   115  H HB3  A SER   A 1 7   ? 11.658 -5.913  19.680  0.48 25.19 ?  7   SER   A HB3  1 
ATOM   116  H HB3  B SER   A 1 7   ? 11.545 -5.504  19.332  0.52 25.79 ?  7   SER   A HB3  1 
ATOM   117  H HG   A SER   A 1 7   ? 10.019 -6.451  21.035  0.48 26.88 ?  7   SER   A HG   1 
ATOM   118  H HG   B SER   A 1 7   ? 9.902  -5.786  20.758  0.52 27.51 ?  7   SER   A HG   1 
ATOM   119  N N    A GLY   A 1 8   ? 9.682  -8.175  17.635  0.48 16.81 ?  8   GLY   A N    1 
ATOM   120  N N    B GLY   A 1 8   ? 9.601  -8.171  17.546  0.52 16.69 ?  8   GLY   A N    1 
ATOM   121  C CA   A GLY   A 1 8   ? 8.604  -7.919  16.703  0.48 15.85 ?  8   GLY   A CA   1 
ATOM   122  C CA   B GLY   A 1 8   ? 8.497  -8.022  16.617  0.52 15.89 ?  8   GLY   A CA   1 
ATOM   123  C C    A GLY   A 1 8   ? 8.835  -8.388  15.287  0.48 14.52 ?  8   GLY   A C    1 
ATOM   124  C C    B GLY   A 1 8   ? 8.744  -8.535  15.219  0.52 15.12 ?  8   GLY   A C    1 
ATOM   125  O O    A GLY   A 1 8   ? 8.102  -7.959  14.387  0.48 14.99 ?  8   GLY   A O    1 
ATOM   126  O O    B GLY   A 1 8   ? 7.991  -8.184  14.304  0.52 15.66 ?  8   GLY   A O    1 
ATOM   127  H H    A GLY   A 1 8   ? 9.532  -8.832  18.169  0.48 20.15 ?  8   GLY   A H    1 
ATOM   128  H H    B GLY   A 1 8   ? 9.528  -8.839  18.081  0.52 20.00 ?  8   GLY   A H    1 
ATOM   129  H HA2  A GLY   A 1 8   ? 7.799  -8.349  17.034  0.48 19.00 ?  8   GLY   A HA2  1 
ATOM   130  H HA2  B GLY   A 1 8   ? 7.728  -8.490  16.975  0.52 19.04 ?  8   GLY   A HA2  1 
ATOM   131  H HA3  A GLY   A 1 8   ? 8.441  -6.966  16.668  0.48 19.00 ?  8   GLY   A HA3  1 
ATOM   132  H HA3  B GLY   A 1 8   ? 8.270  -7.081  16.554  0.52 19.04 ?  8   GLY   A HA3  1 
ATOM   133  N N    A TYR   A 1 9   ? 9.828  -9.242  15.051  0.48 13.36 ?  9   TYR   A N    1 
ATOM   134  N N    B TYR   A 1 9   ? 9.766  -9.365  15.020  0.52 14.35 ?  9   TYR   A N    1 
ATOM   135  C CA   A TYR   A 1 9   ? 10.049 -9.779  13.720  0.48 12.54 ?  9   TYR   A CA   1 
ATOM   136  C CA   B TYR   A 1 9   ? 10.093 -9.876  13.698  0.52 13.45 ?  9   TYR   A CA   1 
ATOM   137  C C    A TYR   A 1 9   ? 9.147  -10.975 13.452  0.48 12.15 ?  9   TYR   A C    1 
ATOM   138  C C    B TYR   A 1 9   ? 9.295  -11.133 13.368  0.52 12.80 ?  9   TYR   A C    1 
ATOM   139  O O    A TYR   A 1 9   ? 8.793  -11.741 14.356  0.48 12.78 ?  9   TYR   A O    1 
ATOM   140  O O    B TYR   A 1 9   ? 9.117  -12.025 14.207  0.52 12.95 ?  9   TYR   A O    1 
ATOM   141  C CB   A TYR   A 1 9   ? 11.503 -10.227 13.541  0.48 12.51 ?  9   TYR   A CB   1 
ATOM   142  C CB   B TYR   A 1 9   ? 11.596 -10.157 13.579  0.52 13.52 ?  9   TYR   A CB   1 
ATOM   143  C CG   A TYR   A 1 9   ? 12.464 -9.081  13.385  0.48 12.48 ?  9   TYR   A CG   1 
ATOM   144  C CG   B TYR   A 1 9   ? 12.439 -8.907  13.390  0.52 13.61 ?  9   TYR   A CG   1 
ATOM   145  C CD1  A TYR   A 1 9   ? 12.841 -8.321  14.479  0.48 12.55 ?  9   TYR   A CD1  1 
ATOM   146  C CD1  B TYR   A 1 9   ? 12.644 -8.018  14.437  0.52 13.72 ?  9   TYR   A CD1  1 
ATOM   147  C CD2  A TYR   A 1 9   ? 12.975 -8.742  12.139  0.48 12.68 ?  9   TYR   A CD2  1 
ATOM   148  C CD2  B TYR   A 1 9   ? 13.015 -8.610  12.160  0.52 13.25 ?  9   TYR   A CD2  1 
ATOM   149  C CE1  A TYR   A 1 9   ? 13.706 -7.255  14.344  0.48 12.71 ?  9   TYR   A CE1  1 
ATOM   150  C CE1  B TYR   A 1 9   ? 13.405 -6.868  14.266  0.52 13.42 ?  9   TYR   A CE1  1 
ATOM   151  C CE2  A TYR   A 1 9   ? 13.841 -7.677  11.991  0.48 12.96 ?  9   TYR   A CE2  1 
ATOM   152  C CE2  B TYR   A 1 9   ? 13.774 -7.460  11.978  0.52 12.86 ?  9   TYR   A CE2  1 
ATOM   153  C CZ   A TYR   A 1 9   ? 14.204 -6.936  13.096  0.48 13.00 ?  9   TYR   A CZ   1 
ATOM   154  C CZ   B TYR   A 1 9   ? 13.967 -6.598  13.035  0.52 12.75 ?  9   TYR   A CZ   1 
ATOM   155  O OH   A TYR   A 1 9   ? 15.067 -5.876  12.954  0.48 13.86 ?  9   TYR   A OH   1 
ATOM   156  O OH   B TYR   A 1 9   ? 14.722 -5.460  12.851  0.52 12.76 ?  9   TYR   A OH   1 
ATOM   157  H H    A TYR   A 1 9   ? 10.383 -9.525  15.646  0.48 16.01 ?  9   TYR   A H    1 
ATOM   158  H H    B TYR   A 1 9   ? 10.285 -9.651  15.643  0.52 17.20 ?  9   TYR   A H    1 
ATOM   159  H HA   A TYR   A 1 9   ? 9.861  -9.087  13.061  0.48 15.03 ?  9   TYR   A HA   1 
ATOM   160  H HA   B TYR   A 1 9   ? 9.870  -9.205  13.038  0.52 16.12 ?  9   TYR   A HA   1 
ATOM   161  H HB2  A TYR   A 1 9   ? 11.774 -10.744 14.313  0.48 14.99 ?  9   TYR   A HB2  1 
ATOM   162  H HB2  B TYR   A 1 9   ? 11.902 -10.608 14.382  0.52 16.20 ?  9   TYR   A HB2  1 
ATOM   163  H HB3  A TYR   A 1 9   ? 11.556 -10.773 12.740  0.48 14.99 ?  9   TYR   A HB3  1 
ATOM   164  H HB3  B TYR   A 1 9   ? 11.737 -10.726 12.807  0.52 16.20 ?  9   TYR   A HB3  1 
ATOM   165  H HD1  A TYR   A 1 9   ? 12.500 -8.534  15.318  0.48 15.04 ?  9   TYR   A HD1  1 
ATOM   166  H HD1  B TYR   A 1 9   ? 12.266 -8.196  15.267  0.52 16.44 ?  9   TYR   A HD1  1 
ATOM   167  H HD2  A TYR   A 1 9   ? 12.729 -9.242  11.389  0.48 15.19 ?  9   TYR   A HD2  1 
ATOM   168  H HD2  B TYR   A 1 9   ? 12.889 -9.188  11.443  0.52 15.88 ?  9   TYR   A HD2  1 
ATOM   169  H HE1  A TYR   A 1 9   ? 13.950 -6.759  15.088  0.48 15.22 ?  9   TYR   A HE1  1 
ATOM   170  H HE1  B TYR   A 1 9   ? 13.535 -6.283  14.976  0.52 16.09 ?  9   TYR   A HE1  1 
ATOM   171  H HE2  A TYR   A 1 9   ? 14.181 -7.468  11.151  0.48 15.53 ?  9   TYR   A HE2  1 
ATOM   172  H HE2  B TYR   A 1 9   ? 14.158 -7.276  11.148  0.52 15.41 ?  9   TYR   A HE2  1 
ATOM   173  H HH   A TYR   A 1 9   ? 15.198 -5.523  13.703  0.48 16.61 ?  9   TYR   A HH   1 
ATOM   174  H HH   B TYR   A 1 9   ? 14.842 -5.068  13.586  0.52 15.29 ?  9   TYR   A HH   1 
ATOM   175  N N    A LEU   A 1 10  ? 8.782  -11.123 12.186  0.48 12.05 ?  10  LEU   A N    1 
ATOM   176  N N    B LEU   A 1 10  ? 8.825  -11.192 12.125  0.52 12.53 ?  10  LEU   A N    1 
ATOM   177  C CA   A LEU   A 1 10  ? 8.185  -12.342 11.676  0.48 12.19 ?  10  LEU   A CA   1 
ATOM   178  C CA   B LEU   A 1 10  ? 8.194  -12.383 11.582  0.52 12.38 ?  10  LEU   A CA   1 
ATOM   179  C C    A LEU   A 1 10  ? 9.317  -13.284 11.281  0.48 11.87 ?  10  LEU   A C    1 
ATOM   180  C C    B LEU   A 1 10  ? 9.283  -13.343 11.118  0.52 12.22 ?  10  LEU   A C    1 
ATOM   181  O O    A LEU   A 1 10  ? 10.329 -12.850 10.726  0.48 11.40 ?  10  LEU   A O    1 
ATOM   182  O O    B LEU   A 1 10  ? 10.166 -12.964 10.342  0.52 11.72 ?  10  LEU   A O    1 
ATOM   183  C CB   A LEU   A 1 10  ? 7.340  -12.003 10.448  0.48 13.14 ?  10  LEU   A CB   1 
ATOM   184  C CB   B LEU   A 1 10  ? 7.306  -11.991 10.398  0.52 12.96 ?  10  LEU   A CB   1 
ATOM   185  C CG   A LEU   A 1 10  ? 6.587  -13.156 9.787   0.48 14.21 ?  10  LEU   A CG   1 
ATOM   186  C CG   B LEU   A 1 10  ? 6.742  -13.130 9.541   0.52 13.82 ?  10  LEU   A CG   1 
ATOM   187  C CD1  A LEU   A 1 10  ? 5.474  -13.653 10.691  0.48 14.40 ?  10  LEU   A CD1  1 
ATOM   188  C CD1  B LEU   A 1 10  ? 5.730  -13.955 10.322  0.52 14.06 ?  10  LEU   A CD1  1 
ATOM   189  C CD2  A LEU   A 1 10  ? 6.039  -12.742 8.428   0.48 15.03 ?  10  LEU   A CD2  1 
ATOM   190  C CD2  B LEU   A 1 10  ? 6.124  -12.592 8.260   0.52 14.80 ?  10  LEU   A CD2  1 
ATOM   191  H H    A LEU   A 1 10  ? 8.881  -10.511 11.582  0.48 14.44 ?  10  LEU   A H    1 
ATOM   192  H H    B LEU   A 1 10  ? 8.872  -10.544 11.561  0.52 15.01 ?  10  LEU   A H    1 
ATOM   193  H HA   A LEU   A 1 10  ? 7.622  -12.754 12.358  0.48 14.61 ?  10  LEU   A HA   1 
ATOM   194  H HA   B LEU   A 1 10  ? 7.645  -12.815 12.259  0.52 14.84 ?  10  LEU   A HA   1 
ATOM   195  H HB2  A LEU   A 1 10  ? 6.680  -11.338 10.704  0.48 15.74 ?  10  LEU   A HB2  1 
ATOM   196  H HB2  B LEU   A 1 10  ? 6.548  -11.489 10.740  0.52 15.53 ?  10  LEU   A HB2  1 
ATOM   197  H HB3  A LEU   A 1 10  ? 7.929  -11.623 9.777   0.48 15.74 ?  10  LEU   A HB3  1 
ATOM   198  H HB3  B LEU   A 1 10  ? 7.824  -11.422 9.808   0.52 15.53 ?  10  LEU   A HB3  1 
ATOM   199  H HG   A LEU   A 1 10  ? 7.203  -13.889 9.645   0.48 17.03 ?  10  LEU   A HG   1 
ATOM   200  H HG   B LEU   A 1 10  ? 7.464  -13.723 9.287   0.52 16.56 ?  10  LEU   A HG   1 
ATOM   201  H HD11 A LEU   A 1 10  ? 4.987  -14.355 10.234  0.48 17.25 ?  10  LEU   A HD11 1 
ATOM   202  H HD11 B LEU   A 1 10  ? 5.395  -14.666 9.752   0.52 16.85 ?  10  LEU   A HD11 1 
ATOM   203  H HD12 A LEU   A 1 10  ? 5.863  -13.998 11.510  0.48 17.25 ?  10  LEU   A HD12 1 
ATOM   204  H HD12 B LEU   A 1 10  ? 6.166  -14.337 11.102  0.52 16.85 ?  10  LEU   A HD12 1 
ATOM   205  H HD13 A LEU   A 1 10  ? 4.878  -12.914 10.895  0.48 17.25 ?  10  LEU   A HD13 1 
ATOM   206  H HD13 B LEU   A 1 10  ? 4.999  -13.382 10.600  0.52 16.85 ?  10  LEU   A HD13 1 
ATOM   207  H HD21 A LEU   A 1 10  ? 5.569  -13.494 8.037   0.48 18.01 ?  10  LEU   A HD21 1 
ATOM   208  H HD21 B LEU   A 1 10  ? 5.777  -13.337 7.744   0.52 17.74 ?  10  LEU   A HD21 1 
ATOM   209  H HD22 A LEU   A 1 10  ? 5.434  -11.994 8.545   0.48 18.01 ?  10  LEU   A HD22 1 
ATOM   210  H HD22 B LEU   A 1 10  ? 5.407  -11.983 8.488   0.52 17.74 ?  10  LEU   A HD22 1 
ATOM   211  H HD23 A LEU   A 1 10  ? 6.780  -12.482 7.857   0.48 18.01 ?  10  LEU   A HD23 1 
ATOM   212  H HD23 B LEU   A 1 10  ? 6.809  -12.129 7.754   0.52 17.74 ?  10  LEU   A HD23 1 
ATOM   213  N N    A LYS   A 1 11  ? 9.147  -14.573 11.568  0.48 12.24 ?  11  LYS   A N    1 
ATOM   214  N N    B LYS   A 1 11  ? 9.220  -14.581 11.597  0.52 12.26 ?  11  LYS   A N    1 
ATOM   215  C CA   A LYS   A 1 11  ? 10.174 -15.569 11.280  0.48 12.89 ?  11  LYS   A CA   1 
ATOM   216  C CA   B LYS   A 1 11  ? 10.149 -15.608 11.156  0.52 12.87 ?  11  LYS   A CA   1 
ATOM   217  C C    A LYS   A 1 11  ? 9.863  -16.180 9.920   0.48 13.04 ?  11  LYS   A C    1 
ATOM   218  C C    B LYS   A 1 11  ? 9.750  -16.070 9.760   0.52 12.48 ?  11  LYS   A C    1 
ATOM   219  O O    A LYS   A 1 11  ? 8.852  -16.873 9.762   0.48 13.60 ?  11  LYS   A O    1 
ATOM   220  O O    B LYS   A 1 11  ? 8.589  -16.425 9.526   0.52 12.00 ?  11  LYS   A O    1 
ATOM   221  C CB   A LYS   A 1 11  ? 10.216 -16.627 12.384  0.48 12.96 ?  11  LYS   A CB   1 
ATOM   222  C CB   B LYS   A 1 11  ? 10.103 -16.775 12.144  0.52 13.50 ?  11  LYS   A CB   1 
ATOM   223  C CG   A LYS   A 1 11  ? 11.225 -17.756 12.173  0.48 13.35 ?  11  LYS   A CG   1 
ATOM   224  C CG   B LYS   A 1 11  ? 11.181 -17.824 11.994  0.52 14.09 ?  11  LYS   A CG   1 
ATOM   225  C CD   A LYS   A 1 11  ? 11.384 -18.590 13.447  0.48 13.66 ?  11  LYS   A CD   1 
ATOM   226  C CD   B LYS   A 1 11  ? 11.096 -18.790 13.168  0.52 14.84 ?  11  LYS   A CD   1 
ATOM   227  C CE   A LYS   A 1 11  ? 12.306 -19.792 13.250  0.48 14.14 ?  11  LYS   A CE   1 
ATOM   228  C CE   B LYS   A 1 11  ? 12.187 -19.844 13.134  0.52 15.32 ?  11  LYS   A CE   1 
ATOM   229  N NZ   A LYS   A 1 11  ? 13.701 -19.420 12.865  0.48 13.95 ?  11  LYS   A NZ   1 
ATOM   230  N NZ   B LYS   A 1 11  ? 13.547 -19.243 13.202  0.52 15.23 ?  11  LYS   A NZ   1 
ATOM   231  H H    A LYS   A 1 11  ? 8.428  -14.901 11.913  0.48 14.66 ?  11  LYS   A H    1 
ATOM   232  H H    B LYS   A 1 11  ? 8.642  -14.849 12.184  0.52 14.69 ?  11  LYS   A H    1 
ATOM   233  H HA   A LYS   A 1 11  ? 11.033 -15.137 11.231  0.48 15.44 ?  11  LYS   A HA   1 
ATOM   234  H HA   B LYS   A 1 11  ? 11.045 -15.248 11.129  0.52 15.42 ?  11  LYS   A HA   1 
ATOM   235  H HB2  A LYS   A 1 11  ? 10.441 -16.184 13.219  0.48 15.52 ?  11  LYS   A HB2  1 
ATOM   236  H HB2  B LYS   A 1 11  ? 10.175 -16.414 13.043  0.52 16.18 ?  11  LYS   A HB2  1 
ATOM   237  H HB3  A LYS   A 1 11  ? 9.336  -17.029 12.463  0.48 15.52 ?  11  LYS   A HB3  1 
ATOM   238  H HB3  B LYS   A 1 11  ? 9.248  -17.222 12.048  0.52 16.18 ?  11  LYS   A HB3  1 
ATOM   239  H HG2  A LYS   A 1 11  ? 10.911 -18.340 11.465  0.48 15.99 ?  11  LYS   A HG2  1 
ATOM   240  H HG2  B LYS   A 1 11  ? 11.044 -18.324 11.174  0.52 16.89 ?  11  LYS   A HG2  1 
ATOM   241  H HG3  A LYS   A 1 11  ? 12.088 -17.380 11.945  0.48 15.99 ?  11  LYS   A HG3  1 
ATOM   242  H HG3  B LYS   A 1 11  ? 12.054 -17.404 12.000  0.52 16.89 ?  11  LYS   A HG3  1 
ATOM   243  H HD2  A LYS   A 1 11  ? 11.761 -18.032 14.146  0.48 16.37 ?  11  LYS   A HD2  1 
ATOM   244  H HD2  B LYS   A 1 11  ? 11.183 -18.292 13.996  0.52 17.78 ?  11  LYS   A HD2  1 
ATOM   245  H HD3  A LYS   A 1 11  ? 10.514 -18.921 13.721  0.48 16.37 ?  11  LYS   A HD3  1 
ATOM   246  H HD3  B LYS   A 1 11  ? 10.238 -19.245 13.144  0.52 17.78 ?  11  LYS   A HD3  1 
ATOM   247  H HE2  A LYS   A 1 11  ? 12.352 -20.294 14.078  0.48 16.95 ?  11  LYS   A HE2  1 
ATOM   248  H HE2  B LYS   A 1 11  ? 12.081 -20.437 13.895  0.52 18.36 ?  11  LYS   A HE2  1 
ATOM   249  H HE3  A LYS   A 1 11  ? 11.945 -20.353 12.545  0.48 16.95 ?  11  LYS   A HE3  1 
ATOM   250  H HE3  B LYS   A 1 11  ? 12.119 -20.344 12.307  0.52 18.36 ?  11  LYS   A HE3  1 
ATOM   251  H HZ1  A LYS   A 1 11  ? 14.196 -20.155 12.762  0.48 16.72 ?  11  LYS   A HZ1  1 
ATOM   252  H HZ1  B LYS   A 1 11  ? 13.919 -19.418 13.993  0.52 18.25 ?  11  LYS   A HZ1  1 
ATOM   253  H HZ2  A LYS   A 1 11  ? 13.697 -18.967 12.099  0.48 16.72 ?  11  LYS   A HZ2  1 
ATOM   254  H HZ2  B LYS   A 1 11  ? 14.063 -19.581 12.563  0.52 18.25 ?  11  LYS   A HZ2  1 
ATOM   255  H HZ3  A LYS   A 1 11  ? 14.068 -18.914 13.499  0.48 16.72 ?  11  LYS   A HZ3  1 
ATOM   256  H HZ3  B LYS   A 1 11  ? 13.499 -18.361 13.095  0.52 18.25 ?  11  LYS   A HZ3  1 
ATOM   257  N N    A LEU   A 1 12  ? 10.719 -15.912 8.928   0.48 12.58 ?  12  LEU   A N    1 
ATOM   258  N N    B LEU   A 1 12  ? 10.702 -16.054 8.827   0.52 12.71 ?  12  LEU   A N    1 
ATOM   259  C CA   A LEU   A 1 12  ? 10.483 -16.472 7.602   0.48 12.50 ?  12  LEU   A CA   1 
ATOM   260  C CA   B LEU   A 1 12  ? 10.485 -16.611 7.496   0.52 13.50 ?  12  LEU   A CA   1 
ATOM   261  C C    A LEU   A 1 12  ? 11.028 -17.891 7.474   0.48 12.09 ?  12  LEU   A C    1 
ATOM   262  C C    B LEU   A 1 12  ? 11.070 -18.011 7.359   0.52 13.86 ?  12  LEU   A C    1 
ATOM   263  O O    A LEU   A 1 12  ? 10.369 -18.755 6.884   0.48 12.52 ?  12  LEU   A O    1 
ATOM   264  O O    B LEU   A 1 12  ? 10.416 -18.911 6.823   0.52 14.30 ?  12  LEU   A O    1 
ATOM   265  C CB   A LEU   A 1 12  ? 11.069 -15.569 6.514   0.48 13.49 ?  12  LEU   A CB   1 
ATOM   266  C CB   B LEU   A 1 12  ? 11.091 -15.700 6.424   0.52 13.99 ?  12  LEU   A CB   1 
ATOM   267  C CG   A LEU   A 1 12  ? 10.367 -14.230 6.282   0.48 14.26 ?  12  LEU   A CG   1 
ATOM   268  C CG   B LEU   A 1 12  ? 10.529 -14.282 6.325   0.52 14.37 ?  12  LEU   A CG   1 
ATOM   269  C CD1  A LEU   A 1 12  ? 11.099 -13.438 5.207   0.48 15.10 ?  12  LEU   A CD1  1 
ATOM   270  C CD1  B LEU   A 1 12  ? 11.218 -13.542 5.189   0.52 15.24 ?  12  LEU   A CD1  1 
ATOM   271  C CD2  A LEU   A 1 12  ? 8.907  -14.440 5.896   0.48 14.75 ?  12  LEU   A CD2  1 
ATOM   272  C CD2  B LEU   A 1 12  ? 9.016  -14.294 6.130   0.52 14.71 ?  12  LEU   A CD2  1 
ATOM   273  H H    A LEU   A 1 12  ? 11.418 -15.406 8.994   0.48 15.07 ?  12  LEU   A H    1 
ATOM   274  H H    B LEU   A 1 12  ? 11.487 -15.717 8.944   0.52 15.23 ?  12  LEU   A H    1 
ATOM   275  H HA   A LEU   A 1 12  ? 9.527  -16.515 7.459   0.48 14.98 ?  12  LEU   A HA   1 
ATOM   276  H HA   B LEU   A 1 12  ? 9.531  -16.671 7.333   0.52 16.17 ?  12  LEU   A HA   1 
ATOM   277  H HB2  A LEU   A 1 12  ? 11.990 -15.373 6.740   0.48 16.16 ?  12  LEU   A HB2  1 
ATOM   278  H HB2  B LEU   A 1 12  ? 12.041 -15.620 6.599   0.52 16.76 ?  12  LEU   A HB2  1 
ATOM   279  H HB3  A LEU   A 1 12  ? 11.041 -16.053 5.672   0.48 16.16 ?  12  LEU   A HB3  1 
ATOM   280  H HB3  B LEU   A 1 12  ? 10.957 -16.122 5.562   0.52 16.76 ?  12  LEU   A HB3  1 
ATOM   281  H HG   A LEU   A 1 12  ? 10.390 -13.710 7.101   0.48 17.09 ?  12  LEU   A HG   1 
ATOM   282  H HG   B LEU   A 1 12  ? 10.722 -13.810 7.149   0.52 17.21 ?  12  LEU   A HG   1 
ATOM   283  H HD11 A LEU   A 1 12  ? 10.646 -12.592 5.072   0.48 18.10 ?  12  LEU   A HD11 1 
ATOM   284  H HD11 B LEU   A 1 12  ? 10.856 -12.645 5.133   0.52 18.26 ?  12  LEU   A HD11 1 
ATOM   285  H HD12 A LEU   A 1 12  ? 12.012 -13.283 5.498   0.48 18.10 ?  12  LEU   A HD12 1 
ATOM   286  H HD12 B LEU   A 1 12  ? 12.171 -13.506 5.368   0.52 18.26 ?  12  LEU   A HD12 1 
ATOM   287  H HD13 A LEU   A 1 12  ? 11.098 -13.951 4.383   0.48 18.10 ?  12  LEU   A HD13 1 
ATOM   288  H HD13 B LEU   A 1 12  ? 11.055 -14.018 4.359   0.52 18.26 ?  12  LEU   A HD13 1 
ATOM   289  H HD21 A LEU   A 1 12  ? 8.544  -13.606 5.563   0.48 17.67 ?  12  LEU   A HD21 1 
ATOM   290  H HD21 B LEU   A 1 12  ? 8.716  -13.391 5.942   0.52 17.63 ?  12  LEU   A HD21 1 
ATOM   291  H HD22 A LEU   A 1 12  ? 8.861  -15.121 5.206   0.48 17.67 ?  12  LEU   A HD22 1 
ATOM   292  H HD22 B LEU   A 1 12  ? 8.798  -14.877 5.386   0.52 17.63 ?  12  LEU   A HD22 1 
ATOM   293  H HD23 A LEU   A 1 12  ? 8.413  -14.729 6.679   0.48 17.67 ?  12  LEU   A HD23 1 
ATOM   294  H HD23 B LEU   A 1 12  ? 8.595  -14.621 6.940   0.52 17.63 ?  12  LEU   A HD23 1 
ATOM   295  N N    A THR   A 1 13  ? 12.227 -18.144 7.995   0.48 11.82 ?  13  THR   A N    1 
ATOM   296  N N    B THR   A 1 13  ? 12.304 -18.196 7.818   0.52 14.38 ?  13  THR   A N    1 
ATOM   297  C CA   A THR   A 1 13  ? 12.888 -19.437 7.840   0.48 12.11 ?  13  THR   A CA   1 
ATOM   298  C CA   B THR   A 1 13  ? 12.971 -19.489 7.835   0.52 14.63 ?  13  THR   A CA   1 
ATOM   299  C C    A THR   A 1 13  ? 13.682 -19.736 9.105   0.48 12.00 ?  13  THR   A C    1 
ATOM   300  C C    B THR   A 1 13  ? 13.674 -19.627 9.182   0.52 15.22 ?  13  THR   A C    1 
ATOM   301  O O    A THR   A 1 13  ? 13.612 -19.005 10.098  0.48 11.88 ?  13  THR   A O    1 
ATOM   302  O O    B THR   A 1 13  ? 13.552 -18.768 10.061  0.52 15.67 ?  13  THR   A O    1 
ATOM   303  C CB   A THR   A 1 13  ? 13.845 -19.433 6.643   0.48 13.29 ?  13  THR   A CB   1 
ATOM   304  C CB   B THR   A 1 13  ? 13.956 -19.640 6.664   0.52 15.14 ?  13  THR   A CB   1 
ATOM   305  O OG1  A THR   A 1 13  ? 14.878 -18.482 6.894   0.48 13.59 ?  13  THR   A OG1  1 
ATOM   306  O OG1  B THR   A 1 13  ? 15.062 -18.754 6.853   0.52 15.14 ?  13  THR   A OG1  1 
ATOM   307  C CG2  A THR   A 1 13  ? 13.131 -19.095 5.339   0.48 14.19 ?  13  THR   A CG2  1 
ATOM   308  C CG2  B THR   A 1 13  ? 13.291 -19.338 5.327   0.52 15.68 ?  13  THR   A CG2  1 
ATOM   309  H H    A THR   A 1 13  ? 12.696 -17.563 8.436   0.48 14.16 ?  13  THR   A H    1 
ATOM   310  H H    B THR   A 1 13  ? 12.788 -17.560 8.137   0.52 17.23 ?  13  THR   A H    1 
ATOM   311  H HA   A THR   A 1 13  ? 12.225 -20.130 7.711   0.48 14.51 ?  13  THR   A HA   1 
ATOM   312  H HA   B THR   A 1 13  ? 12.304 -20.185 7.753   0.52 17.53 ?  13  THR   A HA   1 
ATOM   313  H HB   A THR   A 1 13  ? 14.249 -20.305 6.548   0.48 15.93 ?  13  THR   A HB   1 
ATOM   314  H HB   B THR   A 1 13  ? 14.281 -20.552 6.633   0.52 18.14 ?  13  THR   A HB   1 
ATOM   315  H HG1  A THR   A 1 13  ? 15.409 -18.445 6.241   0.48 16.29 ?  13  THR   A HG1  1 
ATOM   316  H HG1  B THR   A 1 13  ? 15.601 -18.830 6.206   0.52 18.14 ?  13  THR   A HG1  1 
ATOM   317  H HG21 A THR   A 1 13  ? 13.720 -19.266 4.586   0.48 17.00 ?  13  THR   A HG21 1 
ATOM   318  H HG21 B THR   A 1 13  ? 13.896 -19.556 4.599   0.52 18.80 ?  13  THR   A HG21 1 
ATOM   319  H HG22 A THR   A 1 13  ? 12.339 -19.650 5.245   0.48 17.00 ?  13  THR   A HG22 1 
ATOM   320  H HG22 B THR   A 1 13  ? 12.484 -19.868 5.232   0.52 18.80 ?  13  THR   A HG22 1 
ATOM   321  H HG23 A THR   A 1 13  ? 12.867 -18.165 5.330   0.48 17.00 ?  13  THR   A HG23 1 
ATOM   322  H HG23 B THR   A 1 13  ? 13.061 -18.398 5.275   0.52 18.80 ?  13  THR   A HG23 1 
ATOM   323  N N    A ASP   A 1 14  ? 14.487 -20.799 9.047   0.48 12.07 ?  14  ASP   A N    1 
ATOM   324  N N    B ASP   A 1 14  ? 14.440 -20.707 9.334   0.52 15.31 ?  14  ASP   A N    1 
ATOM   325  C CA   A ASP   A 1 14  ? 15.352 -21.116 10.174  0.48 12.12 ?  14  ASP   A CA   1 
ATOM   326  C CA   B ASP   A 1 14  ? 15.194 -20.920 10.565  0.52 16.30 ?  14  ASP   A CA   1 
ATOM   327  C C    A ASP   A 1 14  ? 16.213 -19.928 10.585  0.48 11.93 ?  14  ASP   A C    1 
ATOM   328  C C    B ASP   A 1 14  ? 16.052 -19.710 10.916  0.52 15.31 ?  14  ASP   A C    1 
ATOM   329  O O    A ASP   A 1 14  ? 16.494 -19.757 11.777  0.48 12.50 ?  14  ASP   A O    1 
ATOM   330  O O    B ASP   A 1 14  ? 16.203 -19.377 12.097  0.52 15.58 ?  14  ASP   A O    1 
ATOM   331  C CB   A ASP   A 1 14  ? 16.243 -22.315 9.851   0.48 13.48 ?  14  ASP   A CB   1 
ATOM   332  C CB   B ASP   A 1 14  ? 16.076 -22.161 10.427  0.52 18.92 ?  14  ASP   A CB   1 
ATOM   333  C CG   A ASP   A 1 14  ? 17.205 -22.631 10.980  0.48 16.02 ?  14  ASP   A CG   1 
ATOM   334  C CG   B ASP   A 1 14  ? 16.890 -22.446 11.678  0.52 21.58 ?  14  ASP   A CG   1 
ATOM   335  O OD1  A ASP   A 1 14  ? 16.745 -23.064 12.061  0.48 16.97 ?  14  ASP   A OD1  1 
ATOM   336  O OD1  B ASP   A 1 14  ? 16.292 -22.696 12.744  0.52 22.58 ?  14  ASP   A OD1  1 
ATOM   337  O OD2  A ASP   A 1 14  ? 18.421 -22.423 10.787  0.48 17.59 -1 14  ASP   A OD2  1 
ATOM   338  O OD2  B ASP   A 1 14  ? 18.134 -22.433 11.590  0.52 23.27 -1 14  ASP   A OD2  1 
ATOM   339  H H    A ASP   A 1 14  ? 14.553 -21.338 8.372   0.48 14.46 ?  14  ASP   A H    1 
ATOM   340  H H    B ASP   A 1 14  ? 14.539 -21.318 8.743   0.52 18.35 ?  14  ASP   A H    1 
ATOM   341  H HA   A ASP   A 1 14  ? 14.801 -21.360 10.928  0.48 14.52 ?  14  ASP   A HA   1 
ATOM   342  H HA   B ASP   A 1 14  ? 14.574 -21.070 11.296  0.52 19.53 ?  14  ASP   A HA   1 
ATOM   343  H HB2  A ASP   A 1 14  ? 15.679 -23.102 9.685   0.48 16.15 ?  14  ASP   A HB2  1 
ATOM   344  H HB2  B ASP   A 1 14  ? 15.510 -22.926 10.225  0.52 22.69 ?  14  ASP   A HB2  1 
ATOM   345  H HB3  A ASP   A 1 14  ? 16.773 -22.130 9.062   0.48 16.15 ?  14  ASP   A HB3  1 
ATOM   346  H HB3  B ASP   A 1 14  ? 16.713 -22.020 9.716   0.52 22.69 ?  14  ASP   A HB3  1 
ATOM   347  N N    A ASN   A 1 15  ? 16.628 -19.087 9.625   0.48 11.68 ?  15  ASN   A N    1 
ATOM   348  N N    B ASN   A 1 15  ? 16.610 -19.030 9.906   0.52 14.78 ?  15  ASN   A N    1 
ATOM   349  C CA   A ASN   A 1 15  ? 17.615 -18.050 9.905   0.48 12.53 ?  15  ASN   A CA   1 
ATOM   350  C CA   B ASN   A 1 15  ? 17.630 -18.012 10.130  0.52 14.43 ?  15  ASN   A CA   1 
ATOM   351  C C    A ASN   A 1 15  ? 17.239 -16.643 9.453   0.48 13.09 ?  15  ASN   A C    1 
ATOM   352  C C    B ASN   A 1 15  ? 17.303 -16.639 9.558   0.52 14.53 ?  15  ASN   A C    1 
ATOM   353  O O    A ASN   A 1 15  ? 17.999 -15.711 9.737   0.48 14.67 ?  15  ASN   A O    1 
ATOM   354  O O    B ASN   A 1 15  ? 18.109 -15.719 9.734   0.52 15.91 ?  15  ASN   A O    1 
ATOM   355  C CB   A ASN   A 1 15  ? 18.983 -18.418 9.297   0.48 12.46 ?  15  ASN   A CB   1 
ATOM   356  C CB   B ASN   A 1 15  ? 18.990 -18.476 9.576   0.52 14.05 ?  15  ASN   A CB   1 
ATOM   357  C CG   A ASN   A 1 15  ? 18.942 -18.529 7.784   0.48 12.72 ?  15  ASN   A CG   1 
ATOM   358  C CG   B ASN   A 1 15  ? 19.007 -18.566 8.059   0.52 14.12 ?  15  ASN   A CG   1 
ATOM   359  O OD1  A ASN   A 1 15  ? 18.132 -19.275 7.222   0.48 13.32 ?  15  ASN   A OD1  1 
ATOM   360  O OD1  B ASN   A 1 15  ? 18.387 -19.458 7.474   0.52 14.83 ?  15  ASN   A OD1  1 
ATOM   361  N ND2  A ASN   A 1 15  ? 19.813 -17.781 7.115   0.48 13.03 ?  15  ASN   A ND2  1 
ATOM   362  N ND2  B ASN   A 1 15  ? 19.728 -17.649 7.415   0.52 14.09 ?  15  ASN   A ND2  1 
ATOM   363  H H    A ASN   A 1 15  ? 16.343 -19.104 8.813   0.48 13.99 ?  15  ASN   A H    1 
ATOM   364  H H    B ASN   A 1 15  ? 16.404 -19.139 9.080   0.52 17.72 ?  15  ASN   A H    1 
ATOM   365  H HA   A ASN   A 1 15  ? 17.740 -18.020 10.864  0.48 15.01 ?  15  ASN   A HA   1 
ATOM   366  H HA   B ASN   A 1 15  ? 17.739 -17.900 11.086  0.52 17.30 ?  15  ASN   A HA   1 
ATOM   367  H HB2  A ASN   A 1 15  ? 19.624 -17.726 9.534   0.48 14.93 ?  15  ASN   A HB2  1 
ATOM   368  H HB2  B ASN   A 1 15  ? 19.673 -17.840 9.846   0.52 16.84 ?  15  ASN   A HB2  1 
ATOM   369  H HB3  A ASN   A 1 15  ? 19.273 -19.271 9.654   0.48 14.93 ?  15  ASN   A HB3  1 
ATOM   370  H HB3  B ASN   A 1 15  ? 19.195 -19.353 9.931   0.52 16.84 ?  15  ASN   A HB3  1 
ATOM   371  H HD21 A ASN   A 1 15  ? 19.827 -17.806 6.256   0.48 15.61 ?  15  ASN   A HD21 1 
ATOM   372  H HD21 B ASN   A 1 15  ? 19.766 -17.659 6.555   0.52 16.88 ?  15  ASN   A HD21 1 
ATOM   373  H HD22 A ASN   A 1 15  ? 20.362 -17.272 7.539   0.48 15.61 ?  15  ASN   A HD22 1 
ATOM   374  H HD22 B ASN   A 1 15  ? 20.151 -17.043 7.856   0.52 16.88 ?  15  ASN   A HD22 1 
ATOM   375  N N    A VAL   A 1 16  ? 16.112 -16.453 8.766   0.48 12.72 ?  16  VAL   A N    1 
ATOM   376  N N    B VAL   A 1 16  ? 16.170 -16.462 8.879   0.52 13.67 ?  16  VAL   A N    1 
ATOM   377  C CA   A VAL   A 1 16  ? 15.726 -15.155 8.216   0.48 12.58 ?  16  VAL   A CA   1 
ATOM   378  C CA   B VAL   A 1 16  ? 15.799 -15.174 8.301   0.52 13.31 ?  16  VAL   A CA   1 
ATOM   379  C C    A VAL   A 1 16  ? 14.466 -14.655 8.914   0.48 12.03 ?  16  VAL   A C    1 
ATOM   380  C C    B VAL   A 1 16  ? 14.508 -14.683 8.937   0.52 12.78 ?  16  VAL   A C    1 
ATOM   381  O O    A VAL   A 1 16  ? 13.473 -15.388 9.030   0.48 12.41 ?  16  VAL   A O    1 
ATOM   382  O O    B VAL   A 1 16  ? 13.498 -15.400 8.958   0.52 12.93 ?  16  VAL   A O    1 
ATOM   383  C CB   A VAL   A 1 16  ? 15.522 -15.223 6.692   0.48 13.46 ?  16  VAL   A CB   1 
ATOM   384  C CB   B VAL   A 1 16  ? 15.668 -15.217 6.769   0.52 14.02 ?  16  VAL   A CB   1 
ATOM   385  C CG1  A VAL   A 1 16  ? 15.079 -13.865 6.143   0.48 14.23 ?  16  VAL   A CG1  1 
ATOM   386  C CG1  B VAL   A 1 16  ? 15.339 -13.817 6.234   0.52 14.64 ?  16  VAL   A CG1  1 
ATOM   387  C CG2  A VAL   A 1 16  ? 16.791 -15.700 6.001   0.48 14.00 ?  16  VAL   A CG2  1 
ATOM   388  C CG2  B VAL   A 1 16  ? 16.942 -15.747 6.138   0.52 14.82 ?  16  VAL   A CG2  1 
ATOM   389  H H    A VAL   A 1 16  ? 15.545 -17.080 8.596   0.48 15.24 ?  16  VAL   A H    1 
ATOM   390  H H    B VAL   A 1 16  ? 15.590 -17.084 8.744   0.52 16.38 ?  16  VAL   A H    1 
ATOM   391  H HA   A VAL   A 1 16  ? 16.440 -14.520 8.391   0.48 15.08 ?  16  VAL   A HA   1 
ATOM   392  H HA   B VAL   A 1 16  ? 16.489 -14.528 8.515   0.52 15.94 ?  16  VAL   A HA   1 
ATOM   393  H HB   A VAL   A 1 16  ? 14.818 -15.863 6.503   0.48 16.13 ?  16  VAL   A HB   1 
ATOM   394  H HB   B VAL   A 1 16  ? 14.938 -15.810 6.531   0.52 16.79 ?  16  VAL   A HB   1 
ATOM   395  H HG11 A VAL   A 1 16  ? 15.133 -13.890 5.175   0.48 17.05 ?  16  VAL   A HG11 1 
ATOM   396  H HG11 B VAL   A 1 16  ? 15.455 -13.814 5.273   0.52 17.54 ?  16  VAL   A HG11 1 
ATOM   397  H HG12 A VAL   A 1 16  ? 14.165 -13.693 6.418   0.48 17.05 ?  16  VAL   A HG12 1 
ATOM   398  H HG12 B VAL   A 1 16  ? 14.419 -13.599 6.457   0.52 17.54 ?  16  VAL   A HG12 1 
ATOM   399  H HG13 A VAL   A 1 16  ? 15.667 -13.178 6.490   0.48 17.05 ?  16  VAL   A HG13 1 
ATOM   400  H HG13 B VAL   A 1 16  ? 15.939 -13.174 6.643   0.52 17.54 ?  16  VAL   A HG13 1 
ATOM   401  H HG21 A VAL   A 1 16  ? 16.667 -15.649 5.041   0.48 16.78 ?  16  VAL   A HG21 1 
ATOM   402  H HG21 B VAL   A 1 16  ? 16.875 -15.657 5.175   0.52 17.76 ?  16  VAL   A HG21 1 
ATOM   403  H HG22 A VAL   A 1 16  ? 17.530 -15.133 6.269   0.48 16.78 ?  16  VAL   A HG22 1 
ATOM   404  H HG22 B VAL   A 1 16  ? 17.694 -15.236 6.470   0.52 17.76 ?  16  VAL   A HG22 1 
ATOM   405  H HG23 A VAL   A 1 16  ? 16.968 -16.618 6.263   0.48 16.78 ?  16  VAL   A HG23 1 
ATOM   406  H HG23 B VAL   A 1 16  ? 17.045 -16.681 6.378   0.52 17.76 ?  16  VAL   A HG23 1 
ATOM   407  N N    A TYR   A 1 17  ? 14.506 -13.387 9.338   0.48 11.48 ?  17  TYR   A N    1 
ATOM   408  N N    B TYR   A 1 17  ? 14.547 -13.442 9.410   0.52 12.33 ?  17  TYR   A N    1 
ATOM   409  C CA   A TYR   A 1 17  ? 13.431 -12.705 10.047  0.48 10.95 ?  17  TYR   A CA   1 
ATOM   410  C CA   B TYR   A 1 17  ? 13.454 -12.758 10.074  0.52 12.31 ?  17  TYR   A CA   1 
ATOM   411  C C    A TYR   A 1 17  ? 13.171 -11.363 9.373   0.48 11.33 ?  17  TYR   A C    1 
ATOM   412  C C    B TYR   A 1 17  ? 13.193 -11.449 9.335   0.52 11.93 ?  17  TYR   A C    1 
ATOM   413  O O    A TYR   A 1 17  ? 14.096 -10.750 8.837   0.48 11.95 ?  17  TYR   A O    1 
ATOM   414  O O    B TYR   A 1 17  ? 14.064 -10.944 8.622   0.52 12.26 ?  17  TYR   A O    1 
ATOM   415  C CB   A TYR   A 1 17  ? 13.835 -12.467 11.511  0.48 11.28 ?  17  TYR   A CB   1 
ATOM   416  C CB   B TYR   A 1 17  ? 13.835 -12.493 11.540  0.52 13.92 ?  17  TYR   A CB   1 
ATOM   417  C CG   A TYR   A 1 17  ? 13.980 -13.738 12.319  0.48 11.46 ?  17  TYR   A CG   1 
ATOM   418  C CG   B TYR   A 1 17  ? 14.165 -13.757 12.319  0.52 15.44 ?  17  TYR   A CG   1 
ATOM   419  C CD1  A TYR   A 1 17  ? 15.126 -14.526 12.226  0.48 12.18 ?  17  TYR   A CD1  1 
ATOM   420  C CD1  B TYR   A 1 17  ? 15.409 -14.374 12.200  0.52 16.52 ?  17  TYR   A CD1  1 
ATOM   421  C CD2  A TYR   A 1 17  ? 12.971 -14.153 13.176  0.48 11.36 ?  17  TYR   A CD2  1 
ATOM   422  C CD2  B TYR   A 1 17  ? 13.233 -14.335 13.173  0.52 16.32 ?  17  TYR   A CD2  1 
ATOM   423  C CE1  A TYR   A 1 17  ? 15.263 -15.699 12.959  0.48 12.18 ?  17  TYR   A CE1  1 
ATOM   424  C CE1  B TYR   A 1 17  ? 15.710 -15.531 12.903  0.52 17.39 ?  17  TYR   A CE1  1 
ATOM   425  C CE2  A TYR   A 1 17  ? 13.092 -15.335 13.917  0.48 11.75 ?  17  TYR   A CE2  1 
ATOM   426  C CE2  B TYR   A 1 17  ? 13.528 -15.495 13.884  0.52 17.28 ?  17  TYR   A CE2  1 
ATOM   427  C CZ   A TYR   A 1 17  ? 14.246 -16.101 13.805  0.48 11.96 ?  17  TYR   A CZ   1 
ATOM   428  C CZ   B TYR   A 1 17  ? 14.766 -16.085 13.741  0.52 17.89 ?  17  TYR   A CZ   1 
ATOM   429  O OH   A TYR   A 1 17  ? 14.383 -17.268 14.534  0.48 11.92 ?  17  TYR   A OH   1 
ATOM   430  O OH   B TYR   A 1 17  ? 15.082 -17.229 14.437  0.52 19.11 ?  17  TYR   A OH   1 
ATOM   431  H H    A TYR   A 1 17  ? 15.191 -12.869 9.210   0.48 13.75 ?  17  TYR   A H    1 
ATOM   432  H H    B TYR   A 1 17  ? 15.250 -12.944 9.340   0.52 14.77 ?  17  TYR   A H    1 
ATOM   433  H HA   A TYR   A 1 17  ? 12.623 -13.235 10.017  0.48 13.11 ?  17  TYR   A HA   1 
ATOM   434  H HA   B TYR   A 1 17  ? 12.655 -13.305 10.045  0.52 14.74 ?  17  TYR   A HA   1 
ATOM   435  H HB2  A TYR   A 1 17  ? 14.685 -12.006 11.530  0.48 13.51 ?  17  TYR   A HB2  1 
ATOM   436  H HB2  B TYR   A 1 17  ? 14.613 -11.915 11.566  0.52 16.68 ?  17  TYR   A HB2  1 
ATOM   437  H HB3  A TYR   A 1 17  ? 13.155 -11.922 11.935  0.48 13.51 ?  17  TYR   A HB3  1 
ATOM   438  H HB3  B TYR   A 1 17  ? 13.090 -12.065 11.981  0.52 16.68 ?  17  TYR   A HB3  1 
ATOM   439  H HD1  A TYR   A 1 17  ? 15.810 -14.265 11.654  0.48 14.59 ?  17  TYR   A HD1  1 
ATOM   440  H HD1  B TYR   A 1 17  ? 16.047 -14.012 11.635  0.52 19.80 ?  17  TYR   A HD1  1 
ATOM   441  H HD2  A TYR   A 1 17  ? 12.192 -13.648 13.251  0.48 13.61 ?  17  TYR   A HD2  1 
ATOM   442  H HD2  B TYR   A 1 17  ? 12.397 -13.945 13.271  0.52 19.56 ?  17  TYR   A HD2  1 
ATOM   443  H HE1  A TYR   A 1 17  ? 16.033 -16.215 12.882  0.48 14.60 ?  17  TYR   A HE1  1 
ATOM   444  H HE1  B TYR   A 1 17  ? 16.548 -15.934 12.812  0.52 20.84 ?  17  TYR   A HE1  1 
ATOM   445  H HE2  A TYR   A 1 17  ? 12.406 -15.602 14.487  0.48 14.08 ?  17  TYR   A HE2  1 
ATOM   446  H HE2  B TYR   A 1 17  ? 12.897 -15.876 14.454  0.52 20.72 ?  17  TYR   A HE2  1 
ATOM   447  H HH   A TYR   A 1 17  ? 13.660 -17.457 14.915  0.48 14.28 ?  17  TYR   A HH   1 
ATOM   448  H HH   B TYR   A 1 17  ? 14.393 -17.662 14.624  0.52 22.91 ?  17  TYR   A HH   1 
ATOM   449  N N    A ILE   A 1 18  ? 11.923 -10.883 9.415   0.48 11.30 ?  18  ILE   A N    1 
ATOM   450  N N    B ILE   A 1 18  ? 11.995 -10.881 9.500   0.52 11.86 ?  18  ILE   A N    1 
ATOM   451  C CA   A ILE   A 1 18  ? 11.552 -9.662  8.695   0.48 11.39 ?  18  ILE   A CA   1 
ATOM   452  C CA   B ILE   A 1 18  ? 11.630 -9.680  8.750   0.52 11.98 ?  18  ILE   A CA   1 
ATOM   453  C C    A ILE   A 1 18  ? 10.596 -8.806  9.524   0.48 11.61 ?  18  ILE   A C    1 
ATOM   454  C C    B ILE   A 1 18  ? 10.648 -8.830  9.550   0.52 12.20 ?  18  ILE   A C    1 
ATOM   455  O O    A ILE   A 1 18  ? 9.733  -9.325  10.240  0.48 11.70 ?  18  ILE   A O    1 
ATOM   456  O O    B ILE   A 1 18  ? 9.850  -9.341  10.340  0.52 12.52 ?  18  ILE   A O    1 
ATOM   457  C CB   A ILE   A 1 18  ? 10.982 -10.010 7.301   0.48 11.87 ?  18  ILE   A CB   1 
ATOM   458  C CB   B ILE   A 1 18  ? 11.097 -10.054 7.345   0.52 12.12 ?  18  ILE   A CB   1 
ATOM   459  C CG1  A ILE   A 1 18  ? 10.955 -8.787  6.385   0.48 12.86 ?  18  ILE   A CG1  1 
ATOM   460  C CG1  B ILE   A 1 18  ? 11.106 -8.840  6.414   0.52 12.39 ?  18  ILE   A CG1  1 
ATOM   461  C CG2  A ILE   A 1 18  ? 9.615  -10.686 7.413   0.48 12.38 ?  18  ILE   A CG2  1 
ATOM   462  C CG2  B ILE   A 1 18  ? 9.723  -10.718 7.433   0.52 12.50 ?  18  ILE   A CG2  1 
ATOM   463  C CD1  A ILE   A 1 18  ? 10.663 -9.146  4.951   0.48 14.45 ?  18  ILE   A CD1  1 
ATOM   464  C CD1  B ILE   A 1 18  ? 10.884 -9.209  4.974   0.52 13.06 ?  18  ILE   A CD1  1 
ATOM   465  H H    A ILE   A 1 18  ? 11.275 -11.253 9.839   0.48 13.54 ?  18  ILE   A H    1 
ATOM   466  H H    B ILE   A 1 18  ? 11.390 -11.174 10.030  0.52 14.21 ?  18  ILE   A H    1 
ATOM   467  H HA   A ILE   A 1 18  ? 12.358 -9.138  8.554   0.48 13.64 ?  18  ILE   A HA   1 
ATOM   468  H HA   B ILE   A 1 18  ? 12.436 -9.153  8.619   0.52 14.35 ?  18  ILE   A HA   1 
ATOM   469  H HB   A ILE   A 1 18  ? 11.586 -10.649 6.899   0.48 14.22 ?  18  ILE   A HB   1 
ATOM   470  H HB   B ILE   A 1 18  ? 11.708 -10.705 6.967   0.52 14.52 ?  18  ILE   A HB   1 
ATOM   471  H HG12 A ILE   A 1 18  ? 10.268 -8.176  6.686   0.48 15.40 ?  18  ILE   A HG12 1 
ATOM   472  H HG12 B ILE   A 1 18  ? 10.403 -8.231  6.680   0.52 14.84 ?  18  ILE   A HG12 1 
ATOM   473  H HG13 A ILE   A 1 18  ? 11.823 -8.351  6.410   0.48 15.40 ?  18  ILE   A HG13 1 
ATOM   474  H HG13 B ILE   A 1 18  ? 11.969 -8.398  6.475   0.52 14.84 ?  18  ILE   A HG13 1 
ATOM   475  H HG21 A ILE   A 1 18  ? 9.369  -11.041 6.543   0.48 14.84 ?  18  ILE   A HG21 1 
ATOM   476  H HG21 B ILE   A 1 18  ? 9.499  -11.095 6.567   0.52 14.97 ?  18  ILE   A HG21 1 
ATOM   477  H HG22 A ILE   A 1 18  ? 9.675  -11.407 8.058   0.48 14.84 ?  18  ILE   A HG22 1 
ATOM   478  H HG22 B ILE   A 1 18  ? 9.755  -11.419 8.101   0.52 14.97 ?  18  ILE   A HG22 1 
ATOM   479  H HG23 A ILE   A 1 18  ? 8.959  -10.034 7.702   0.48 14.84 ?  18  ILE   A HG23 1 
ATOM   480  H HG23 B ILE   A 1 18  ? 9.064  -10.051 7.683   0.52 14.97 ?  18  ILE   A HG23 1 
ATOM   481  H HD11 A ILE   A 1 18  ? 10.783 -8.361  4.396   0.48 17.31 ?  18  ILE   A HD11 1 
ATOM   482  H HD11 B ILE   A 1 18  ? 10.960 -8.410  4.428   0.52 15.64 ?  18  ILE   A HD11 1 
ATOM   483  H HD12 A ILE   A 1 18  ? 11.274 -9.846  4.670   0.48 17.31 ?  18  ILE   A HD12 1 
ATOM   484  H HD12 B ILE   A 1 18  ? 11.548 -9.860  4.706   0.52 15.64 ?  18  ILE   A HD12 1 
ATOM   485  H HD13 A ILE   A 1 18  ? 9.748  -9.463  4.886   0.48 17.31 ?  18  ILE   A HD13 1 
ATOM   486  H HD13 B ILE   A 1 18  ? 9.993  -9.586  4.881   0.52 15.64 ?  18  ILE   A HD13 1 
ATOM   487  N N    A LYS   A 1 19  ? 10.739 -7.483  9.399   0.48 11.97 ?  19  LYS   A N    1 
ATOM   488  N N    B LYS   A 1 19  ? 10.709 -7.516  9.322   0.52 12.63 ?  19  LYS   A N    1 
ATOM   489  C CA   A LYS   A 1 19  ? 9.957  -6.529  10.177  0.48 12.37 ?  19  LYS   A CA   1 
ATOM   490  C CA   B LYS   A 1 19  ? 9.886  -6.553  10.043  0.52 13.08 ?  19  LYS   A CA   1 
ATOM   491  C C    A LYS   A 1 19  ? 9.769  -5.260  9.356   0.48 12.04 ?  19  LYS   A C    1 
ATOM   492  C C    B LYS   A 1 19  ? 9.704  -5.302  9.193   0.52 12.52 ?  19  LYS   A C    1 
ATOM   493  O O    A LYS   A 1 19  ? 10.715 -4.788  8.721   0.48 11.45 ?  19  LYS   A O    1 
ATOM   494  O O    B LYS   A 1 19  ? 10.551 -4.975  8.354   0.52 12.02 ?  19  LYS   A O    1 
ATOM   495  C CB   A LYS   A 1 19  ? 10.686 -6.208  11.491  0.48 13.05 ?  19  LYS   A CB   1 
ATOM   496  C CB   B LYS   A 1 19  ? 10.559 -6.163  11.364  0.52 13.71 ?  19  LYS   A CB   1 
ATOM   497  C CG   A LYS   A 1 19  ? 9.956  -5.287  12.453  0.48 13.75 ?  19  LYS   A CG   1 
ATOM   498  C CG   B LYS   A 1 19  ? 9.734  -5.280  12.290  0.52 14.81 ?  19  LYS   A CG   1 
ATOM   499  C CD   A LYS   A 1 19  ? 10.836 -5.010  13.664  0.48 14.33 ?  19  LYS   A CD   1 
ATOM   500  C CD   B LYS   A 1 19  ? 10.540 -4.911  13.527  0.52 15.71 ?  19  LYS   A CD   1 
ATOM   501  C CE   A LYS   A 1 19  ? 10.141 -4.150  14.698  0.48 14.64 ?  19  LYS   A CE   1 
ATOM   502  C CE   B LYS   A 1 19  ? 9.758  -4.018  14.474  0.52 16.42 ?  19  LYS   A CE   1 
ATOM   503  N NZ   A LYS   A 1 19  ? 11.018 -3.905  15.876  0.48 14.79 ?  19  LYS   A NZ   1 
ATOM   504  N NZ   B LYS   A 1 19  ? 10.584 -3.624  15.652  0.52 16.79 ?  19  LYS   A NZ   1 
ATOM   505  H H    A LYS   A 1 19  ? 11.303 -7.104  8.860   0.48 14.34 ?  19  LYS   A H    1 
ATOM   506  H H    B LYS   A 1 19  ? 11.240 -7.158  8.746   0.52 15.13 ?  19  LYS   A H    1 
ATOM   507  H HA   A LYS   A 1 19  ? 9.090  -6.898  10.384  0.48 14.82 ?  19  LYS   A HA   1 
ATOM   508  H HA   B LYS   A 1 19  ? 9.020  -6.949  10.229  0.52 15.68 ?  19  LYS   A HA   1 
ATOM   509  H HB2  A LYS   A 1 19  ? 10.845 -7.042  11.964  0.48 15.63 ?  19  LYS   A HB2  1 
ATOM   510  H HB2  B LYS   A 1 19  ? 10.772 -6.975  11.846  0.52 16.43 ?  19  LYS   A HB2  1 
ATOM   511  H HB3  A LYS   A 1 19  ? 11.538 -5.791  11.283  0.48 15.63 ?  19  LYS   A HB3  1 
ATOM   512  H HB3  B LYS   A 1 19  ? 11.377 -5.685  11.156  0.52 16.43 ?  19  LYS   A HB3  1 
ATOM   513  H HG2  A LYS   A 1 19  ? 9.759  -4.445  12.017  0.48 16.47 ?  19  LYS   A HG2  1 
ATOM   514  H HG2  B LYS   A 1 19  ? 9.488  -4.464  11.833  0.52 17.75 ?  19  LYS   A HG2  1 
ATOM   515  H HG3  A LYS   A 1 19  ? 9.139  -5.714  12.759  0.48 16.47 ?  19  LYS   A HG3  1 
ATOM   516  H HG3  B LYS   A 1 19  ? 8.941  -5.763  12.576  0.52 17.75 ?  19  LYS   A HG3  1 
ATOM   517  H HD2  A LYS   A 1 19  ? 11.075 -5.852  14.083  0.48 17.17 ?  19  LYS   A HD2  1 
ATOM   518  H HD2  B LYS   A 1 19  ? 10.782 -5.721  14.005  0.52 18.82 ?  19  LYS   A HD2  1 
ATOM   519  H HD3  A LYS   A 1 19  ? 11.637 -4.544  13.374  0.48 17.17 ?  19  LYS   A HD3  1 
ATOM   520  H HD3  B LYS   A 1 19  ? 11.342 -4.436  13.254  0.52 18.82 ?  19  LYS   A HD3  1 
ATOM   521  H HE2  A LYS   A 1 19  ? 9.914  -3.292  14.304  0.48 17.54 ?  19  LYS   A HE2  1 
ATOM   522  H HE2  B LYS   A 1 19  ? 9.489  -3.212  14.006  0.52 19.67 ?  19  LYS   A HE2  1 
ATOM   523  H HE3  A LYS   A 1 19  ? 9.338  -4.601  15.005  0.48 17.54 ?  19  LYS   A HE3  1 
ATOM   524  H HE3  B LYS   A 1 19  ? 8.978  -4.497  14.795  0.52 19.67 ?  19  LYS   A HE3  1 
ATOM   525  H HZ1  A LYS   A 1 19  ? 10.582 -3.425  16.486  0.48 17.73 ?  19  LYS   A HZ1  1 
ATOM   526  H HZ1  B LYS   A 1 19  ? 10.110 -3.101  16.195  0.52 20.12 ?  19  LYS   A HZ1  1 
ATOM   527  H HZ2  A LYS   A 1 19  ? 11.263 -4.680  16.238  0.48 17.73 ?  19  LYS   A HZ2  1 
ATOM   528  H HZ2  B LYS   A 1 19  ? 10.841 -4.348  16.100  0.52 20.12 ?  19  LYS   A HZ2  1 
ATOM   529  H HZ3  A LYS   A 1 19  ? 11.746 -3.460  15.625  0.48 17.73 ?  19  LYS   A HZ3  1 
ATOM   530  H HZ3  B LYS   A 1 19  ? 11.306 -3.179  15.382  0.52 20.12 ?  19  LYS   A HZ3  1 
ATOM   531  N N    A ASN   A 1 20  ? 8.550  -4.715  9.354   0.48 13.01 ?  20  ASN   A N    1 
ATOM   532  N N    B ASN   A 1 20  ? 8.597  -4.591  9.437   0.52 12.98 ?  20  ASN   A N    1 
ATOM   533  C CA   A ASN   A 1 20  ? 8.320  -3.383  8.790   0.48 13.87 ?  20  ASN   A CA   1 
ATOM   534  C CA   B ASN   A 1 20  ? 8.316  -3.299  8.802   0.52 13.09 ?  20  ASN   A CA   1 
ATOM   535  C C    A ASN   A 1 20  ? 8.903  -2.370  9.760   0.48 13.92 ?  20  ASN   A C    1 
ATOM   536  C C    B ASN   A 1 20  ? 8.881  -2.217  9.718   0.52 13.47 ?  20  ASN   A C    1 
ATOM   537  O O    A ASN   A 1 20  ? 8.342  -2.121  10.829  0.48 14.12 ?  20  ASN   A O    1 
ATOM   538  O O    B ASN   A 1 20  ? 8.230  -1.786  10.673  0.52 14.04 ?  20  ASN   A O    1 
ATOM   539  C CB   A ASN   A 1 20  ? 6.833  -3.131  8.559   0.48 14.91 ?  20  ASN   A CB   1 
ATOM   540  C CB   B ASN   A 1 20  ? 6.806  -3.144  8.617   0.52 13.12 ?  20  ASN   A CB   1 
ATOM   541  C CG   A ASN   A 1 20  ? 6.521  -1.680  8.181   0.48 16.11 ?  20  ASN   A CG   1 
ATOM   542  C CG   B ASN   A 1 20  ? 6.399  -1.865  7.870   0.52 12.96 ?  20  ASN   A CG   1 
ATOM   543  O OD1  A ASN   A 1 20  ? 5.514  -1.127  8.620   0.48 17.45 ?  20  ASN   A OD1  1 
ATOM   544  O OD1  B ASN   A 1 20  ? 5.219  -1.486  7.883   0.52 13.09 ?  20  ASN   A OD1  1 
ATOM   545  N ND2  A ASN   A 1 20  ? 7.378  -1.065  7.369   0.48 16.14 ?  20  ASN   A ND2  1 
ATOM   546  N ND2  B ASN   A 1 20  ? 7.351  -1.213  7.206   0.52 13.41 ?  20  ASN   A ND2  1 
ATOM   547  H H    A ASN   A 1 20  ? 7.853  -5.096  9.660   0.48 15.58 ?  20  ASN   A H    1 
ATOM   548  H H    B ASN   A 1 20  ? 7.985  -4.844  9.980   0.52 15.55 ?  20  ASN   A H    1 
ATOM   549  H HA   A ASN   A 1 20  ? 8.783  -3.301  7.945   0.48 16.62 ?  20  ASN   A HA   1 
ATOM   550  H HA   B ASN   A 1 20  ? 8.751  -3.260  7.931   0.52 15.69 ?  20  ASN   A HA   1 
ATOM   551  H HB2  A ASN   A 1 20  ? 6.523  -3.695  7.839   0.48 17.87 ?  20  ASN   A HB2  1 
ATOM   552  H HB2  B ASN   A 1 20  ? 6.462  -3.901  8.124   0.52 15.72 ?  20  ASN   A HB2  1 
ATOM   553  H HB3  A ASN   A 1 20  ? 6.346  -3.337  9.374   0.48 17.87 ?  20  ASN   A HB3  1 
ATOM   554  H HB3  B ASN   A 1 20  ? 6.391  -3.117  9.496   0.52 15.72 ?  20  ASN   A HB3  1 
ATOM   555  H HD21 A ASN   A 1 20  ? 7.238  -0.249  7.132   0.48 19.35 ?  20  ASN   A HD21 1 
ATOM   556  H HD21 B ASN   A 1 20  ? 7.153  -0.500  6.779   0.52 16.07 ?  20  ASN   A HD21 1 
ATOM   557  H HD22 A ASN   A 1 20  ? 8.074  -1.480  7.084   0.48 19.35 ?  20  ASN   A HD22 1 
ATOM   558  H HD22 B ASN   A 1 20  ? 8.159  -1.505  7.204   0.52 16.07 ?  20  ASN   A HD22 1 
ATOM   559  N N    A ALA   A 1 21  ? 10.054 -1.808  9.407   0.48 14.24 ?  21  ALA   A N    1 
ATOM   560  N N    B ALA   A 1 21  ? 10.111 -1.778  9.438   0.52 13.77 ?  21  ALA   A N    1 
ATOM   561  C CA   A ALA   A 1 21  ? 10.739 -0.904  10.313  0.48 14.24 ?  21  ALA   A CA   1 
ATOM   562  C CA   B ALA   A 1 21  ? 10.778 -0.809  10.301  0.52 13.88 ?  21  ALA   A CA   1 
ATOM   563  C C    A ALA   A 1 21  ? 11.717 -0.053  9.527   0.48 14.04 ?  21  ALA   A C    1 
ATOM   564  C C    B ALA   A 1 21  ? 11.926 -0.146  9.552   0.52 12.84 ?  21  ALA   A C    1 
ATOM   565  O O    A ALA   A 1 21  ? 12.192 -0.448  8.460   0.48 14.32 ?  21  ALA   A O    1 
ATOM   566  O O    B ALA   A 1 21  ? 12.445 -0.684  8.571   0.52 13.07 ?  21  ALA   A O    1 
ATOM   567  C CB   A ALA   A 1 21  ? 11.482 -1.677  11.407  0.48 14.79 ?  21  ALA   A CB   1 
ATOM   568  C CB   B ALA   A 1 21  ? 11.292 -1.461  11.591  0.52 15.58 ?  21  ALA   A CB   1 
ATOM   569  H H    A ALA   A 1 21  ? 10.458 -1.940  8.656   0.48 17.07 ?  21  ALA   A H    1 
ATOM   570  H H    B ALA   A 1 21  ? 10.576 -2.027  8.757   0.52 16.51 ?  21  ALA   A H    1 
ATOM   571  H HA   A ALA   A 1 21  ? 10.087 -0.320  10.732  0.48 17.07 ?  21  ALA   A HA   1 
ATOM   572  H HA   B ALA   A 1 21  ? 10.143 -0.122  10.548  0.52 16.63 ?  21  ALA   A HA   1 
ATOM   573  H HB1  A ALA   A 1 21  ? 11.904 -1.041  12.004  0.48 17.72 ?  21  ALA   A HB1  1 
ATOM   574  H HB1  B ALA   A 1 21  ? 11.726 -0.785  12.136  0.52 18.67 ?  21  ALA   A HB1  1 
ATOM   575  H HB2  A ALA   A 1 21  ? 10.840 -2.216  11.898  0.48 17.72 ?  21  ALA   A HB2  1 
ATOM   576  H HB2  B ALA   A 1 21  ? 10.541 -1.842  12.075  0.52 18.67 ?  21  ALA   A HB2  1 
ATOM   577  H HB3  A ALA   A 1 21  ? 12.147 -2.244  10.995  0.48 17.72 ?  21  ALA   A HB3  1 
ATOM   578  H HB3  B ALA   A 1 21  ? 11.926 -2.159  11.364  0.52 18.67 ?  21  ALA   A HB3  1 
ATOM   579  N N    A ASP   A 1 22  ? 11.981 1.133   10.066  0.48 14.06 ?  22  ASP   A N    1 
ATOM   580  N N    B ASP   A 1 22  ? 12.303 1.042   10.040  0.52 12.16 ?  22  ASP   A N    1 
ATOM   581  C CA   A ASP   A 1 22  ? 13.051 1.995   9.590   0.48 14.16 ?  22  ASP   A CA   1 
ATOM   582  C CA   B ASP   A 1 22  ? 13.474 1.777   9.566   0.52 11.95 ?  22  ASP   A CA   1 
ATOM   583  C C    A ASP   A 1 22  ? 14.371 1.467   10.139  0.48 13.11 ?  22  ASP   A C    1 
ATOM   584  C C    B ASP   A 1 22  ? 14.717 1.135   10.165  0.52 10.95 ?  22  ASP   A C    1 
ATOM   585  O O    A ASP   A 1 22  ? 14.581 1.457   11.355  0.48 13.08 ?  22  ASP   A O    1 
ATOM   586  O O    B ASP   A 1 22  ? 14.821 1.007   11.388  0.52 11.24 ?  22  ASP   A O    1 
ATOM   587  C CB   A ASP   A 1 22  ? 12.793 3.407   10.106  0.48 15.35 ?  22  ASP   A CB   1 
ATOM   588  C CB   B ASP   A 1 22  ? 13.362 3.225   10.051  0.52 13.13 ?  22  ASP   A CB   1 
ATOM   589  C CG   A ASP   A 1 22  ? 13.785 4.418   9.571   0.48 16.54 ?  22  ASP   A CG   1 
ATOM   590  C CG   B ASP   A 1 22  ? 14.396 4.159   9.440   0.52 14.27 ?  22  ASP   A CG   1 
ATOM   591  O OD1  A ASP   A 1 22  ? 14.907 4.030   9.189   0.48 16.65 ?  22  ASP   A OD1  1 
ATOM   592  O OD1  B ASP   A 1 22  ? 15.425 3.682   8.919   0.52 13.61 ?  22  ASP   A OD1  1 
ATOM   593  O OD2  A ASP   A 1 22  ? 13.438 5.613   9.535   0.48 17.77 -1 22  ASP   A OD2  1 
ATOM   594  O OD2  B ASP   A 1 22  ? 14.178 5.390   9.506   0.52 16.19 -1 22  ASP   A OD2  1 
ATOM   595  H H    A ASP   A 1 22  ? 11.533 1.468   10.720  0.48 16.85 ?  22  ASP   A H    1 
ATOM   596  H H    B ASP   A 1 22  ? 11.880 1.449   10.673  0.52 14.57 ?  22  ASP   A H    1 
ATOM   597  H HA   A ASP   A 1 22  ? 13.078 2.004   8.619   0.48 16.96 ?  22  ASP   A HA   1 
ATOM   598  H HA   B ASP   A 1 22  ? 13.524 1.743   8.600   0.52 14.32 ?  22  ASP   A HA   1 
ATOM   599  H HB2  A ASP   A 1 22  ? 11.903 3.689   9.837   0.48 18.39 ?  22  ASP   A HB2  1 
ATOM   600  H HB2  B ASP   A 1 22  ? 12.485 3.560   9.831   0.52 15.73 ?  22  ASP   A HB2  1 
ATOM   601  H HB3  A ASP   A 1 22  ? 12.851 3.401   11.078  0.48 18.39 ?  22  ASP   A HB3  1 
ATOM   602  H HB3  B ASP   A 1 22  ? 13.506 3.247   11.006  0.52 15.73 ?  22  ASP   A HB3  1 
ATOM   603  N N    A ILE   A 1 23  ? 15.262 1.031   9.245   0.48 12.98 ?  23  ILE   A N    1 
ATOM   604  N N    B ILE   A 1 23  ? 15.661 0.730   9.312   0.52 10.31 ?  23  ILE   A N    1 
ATOM   605  C CA   A ILE   A 1 23  ? 16.515 0.420   9.682   0.48 12.51 ?  23  ILE   A CA   1 
ATOM   606  C CA   B ILE   A 1 23  ? 16.884 0.099   9.805   0.52 10.66 ?  23  ILE   A CA   1 
ATOM   607  C C    A ILE   A 1 23  ? 17.309 1.368   10.568  0.48 12.10 ?  23  ILE   A C    1 
ATOM   608  C C    B ILE   A 1 23  ? 17.612 1.013   10.786  0.52 11.02 ?  23  ILE   A C    1 
ATOM   609  O O    A ILE   A 1 23  ? 18.047 0.927   11.458  0.48 12.43 ?  23  ILE   A O    1 
ATOM   610  O O    B ILE   A 1 23  ? 18.247 0.539   11.736  0.52 11.26 ?  23  ILE   A O    1 
ATOM   611  C CB   A ILE   A 1 23  ? 17.326 -0.071  8.466   0.48 12.52 ?  23  ILE   A CB   1 
ATOM   612  C CB   B ILE   A 1 23  ? 17.782 -0.359  8.633   0.52 10.01 ?  23  ILE   A CB   1 
ATOM   613  C CG1  A ILE   A 1 23  ? 18.468 -0.980  8.925   0.48 12.35 ?  23  ILE   A CG1  1 
ATOM   614  C CG1  B ILE   A 1 23  ? 18.841 -1.350  9.135   0.52 10.63 ?  23  ILE   A CG1  1 
ATOM   615  C CG2  A ILE   A 1 23  ? 17.843 1.109   7.647   0.48 12.60 ?  23  ILE   A CG2  1 
ATOM   616  C CG2  B ILE   A 1 23  ? 18.423 0.843   7.918   0.52 9.92  ?  23  ILE   A CG2  1 
ATOM   617  C CD1  A ILE   A 1 23  ? 19.148 -1.730  7.799   0.48 12.56 ?  23  ILE   A CD1  1 
ATOM   618  C CD1  B ILE   A 1 23  ? 19.702 -1.948  8.044   0.52 10.97 ?  23  ILE   A CD1  1 
ATOM   619  H H    A ILE   A 1 23  ? 15.158 1.075   8.399   0.48 15.56 ?  23  ILE   A H    1 
ATOM   620  H H    B ILE   A 1 23  ? 15.619 0.804   8.465   0.52 12.35 ?  23  ILE   A H    1 
ATOM   621  H HA   A ILE   A 1 23  ? 16.301 -0.358  10.221  0.48 14.99 ?  23  ILE   A HA   1 
ATOM   622  H HA   B ILE   A 1 23  ? 16.634 -0.702  10.291  0.52 12.77 ?  23  ILE   A HA   1 
ATOM   623  H HB   A ILE   A 1 23  ? 16.734 -0.591  7.905   0.48 15.00 ?  23  ILE   A HB   1 
ATOM   624  H HB   B ILE   A 1 23  ? 17.225 -0.826  7.987   0.52 11.99 ?  23  ILE   A HB   1 
ATOM   625  H HG12 A ILE   A 1 23  ? 19.141 -0.440  9.368   0.48 14.80 ?  23  ILE   A HG12 1 
ATOM   626  H HG12 B ILE   A 1 23  ? 19.430 -0.892  9.753   0.52 12.74 ?  23  ILE   A HG12 1 
ATOM   627  H HG13 A ILE   A 1 23  ? 18.114 -1.637  9.547   0.48 14.80 ?  23  ILE   A HG13 1 
ATOM   628  H HG13 B ILE   A 1 23  ? 18.394 -2.081  9.588   0.52 12.74 ?  23  ILE   A HG13 1 
ATOM   629  H HG21 A ILE   A 1 23  ? 18.203 0.777   6.810   0.48 15.10 ?  23  ILE   A HG21 1 
ATOM   630  H HG21 B ILE   A 1 23  ? 18.823 0.538   7.084   0.52 11.88 ?  23  ILE   A HG21 1 
ATOM   631  H HG22 A ILE   A 1 23  ? 17.106 1.717   7.470   0.48 15.10 ?  23  ILE   A HG22 1 
ATOM   632  H HG22 B ILE   A 1 23  ? 17.736 1.499   7.731   0.52 11.88 ?  23  ILE   A HG22 1 
ATOM   633  H HG23 A ILE   A 1 23  ? 18.535 1.567   8.147   0.48 15.10 ?  23  ILE   A HG23 1 
ATOM   634  H HG23 B ILE   A 1 23  ? 19.105 1.225   8.489   0.52 11.88 ?  23  ILE   A HG23 1 
ATOM   635  H HD11 A ILE   A 1 23  ? 19.830 -2.310  8.173   0.48 15.05 ?  23  ILE   A HD11 1 
ATOM   636  H HD11 B ILE   A 1 23  ? 20.290 -2.617  8.436   0.52 13.14 ?  23  ILE   A HD11 1 
ATOM   637  H HD12 A ILE   A 1 23  ? 18.483 -2.263  7.332   0.48 15.05 ?  23  ILE   A HD12 1 
ATOM   638  H HD12 B ILE   A 1 23  ? 19.130 -2.365  7.381   0.52 13.14 ?  23  ILE   A HD12 1 
ATOM   639  H HD13 A ILE   A 1 23  ? 19.548 -1.093  7.191   0.48 15.05 ?  23  ILE   A HD13 1 
ATOM   640  H HD13 B ILE   A 1 23  ? 20.230 -1.247  7.633   0.52 13.14 ?  23  ILE   A HD13 1 
ATOM   641  N N    A VAL   A 1 24  ? 17.165 2.678   10.357  0.48 12.66 ?  24  VAL   A N    1 
ATOM   642  N N    B VAL   A 1 24  ? 17.525 2.331   10.584  0.52 12.02 ?  24  VAL   A N    1 
ATOM   643  C CA   A VAL   A 1 24  ? 17.845 3.649   11.213  0.48 13.88 ?  24  VAL   A CA   1 
ATOM   644  C CA   B VAL   A 1 24  ? 18.184 3.278   11.485  0.52 12.94 ?  24  VAL   A CA   1 
ATOM   645  C C    A VAL   A 1 24  ? 17.312 3.566   12.636  0.48 14.51 ?  24  VAL   A C    1 
ATOM   646  C C    B VAL   A 1 24  ? 17.599 3.176   12.888  0.52 13.55 ?  24  VAL   A C    1 
ATOM   647  O O    A VAL   A 1 24  ? 18.077 3.503   13.605  0.48 14.69 ?  24  VAL   A O    1 
ATOM   648  O O    B VAL   A 1 24  ? 18.327 3.204   13.889  0.52 13.83 ?  24  VAL   A O    1 
ATOM   649  C CB   A VAL   A 1 24  ? 17.704 5.069   10.638  0.48 14.67 ?  24  VAL   A CB   1 
ATOM   650  C CB   B VAL   A 1 24  ? 18.069 4.706   10.919  0.52 14.17 ?  24  VAL   A CB   1 
ATOM   651  C CG1  A VAL   A 1 24  ? 18.251 6.103   11.623  0.48 15.06 ?  24  VAL   A CG1  1 
ATOM   652  C CG1  B VAL   A 1 24  ? 18.618 5.722   11.909  0.52 15.23 ?  24  VAL   A CG1  1 
ATOM   653  C CG2  A VAL   A 1 24  ? 18.411 5.166   9.298   0.48 14.98 ?  24  VAL   A CG2  1 
ATOM   654  C CG2  B VAL   A 1 24  ? 18.797 4.805   9.584   0.52 15.07 ?  24  VAL   A CG2  1 
ATOM   655  H H    A VAL   A 1 24  ? 16.683 3.030   9.738   0.48 15.17 ?  24  VAL   A H    1 
ATOM   656  H H    B VAL   A 1 24  ? 17.101 2.692   9.935   0.52 14.40 ?  24  VAL   A H    1 
ATOM   657  H HA   A VAL   A 1 24  ? 18.788 3.436   11.243  0.48 16.63 ?  24  VAL   A HA   1 
ATOM   658  H HA   B VAL   A 1 24  ? 19.129 3.056   11.535  0.52 15.50 ?  24  VAL   A HA   1 
ATOM   659  H HB   A VAL   A 1 24  ? 16.764 5.264   10.496  0.48 17.58 ?  24  VAL   A HB   1 
ATOM   660  H HB   B VAL   A 1 24  ? 17.134 4.908   10.762  0.52 16.98 ?  24  VAL   A HB   1 
ATOM   661  H HG11 A VAL   A 1 24  ? 18.405 6.935   11.153  0.48 18.04 ?  24  VAL   A HG11 1 
ATOM   662  H HG11 B VAL   A 1 24  ? 18.735 6.568   11.451  0.52 18.25 ?  24  VAL   A HG11 1 
ATOM   663  H HG12 A VAL   A 1 24  ? 17.606 6.238   12.334  0.48 18.04 ?  24  VAL   A HG12 1 
ATOM   664  H HG12 B VAL   A 1 24  ? 17.986 5.824   12.636  0.52 18.25 ?  24  VAL   A HG12 1 
ATOM   665  H HG13 A VAL   A 1 24  ? 19.087 5.772   11.991  0.48 18.04 ?  24  VAL   A HG13 1 
ATOM   666  H HG13 B VAL   A 1 24  ? 19.469 5.404   12.244  0.52 18.25 ?  24  VAL   A HG13 1 
ATOM   667  H HG21 A VAL   A 1 24  ? 18.221 6.030   8.903   0.48 17.95 ?  24  VAL   A HG21 1 
ATOM   668  H HG21 B VAL   A 1 24  ? 18.667 5.694   9.219   0.52 18.06 ?  24  VAL   A HG21 1 
ATOM   669  H HG22 A VAL   A 1 24  ? 19.366 5.070   9.440   0.48 17.95 ?  24  VAL   A HG22 1 
ATOM   670  H HG22 B VAL   A 1 24  ? 19.742 4.641   9.726   0.52 18.06 ?  24  VAL   A HG22 1 
ATOM   671  H HG23 A VAL   A 1 24  ? 18.089 4.458   8.719   0.48 17.95 ?  24  VAL   A HG23 1 
ATOM   672  H HG23 B VAL   A 1 24  ? 18.435 4.143   8.972   0.52 18.06 ?  24  VAL   A HG23 1 
ATOM   673  N N    A GLU   A 1 25  ? 15.987 3.579   12.784  0.48 15.07 ?  25  GLU   A N    1 
ATOM   674  N N    B GLU   A 1 25  ? 16.272 3.065   12.982  0.52 14.04 ?  25  GLU   A N    1 
ATOM   675  C CA   A GLU   A 1 25  ? 15.404 3.523   14.119  0.48 16.22 ?  25  GLU   A CA   1 
ATOM   676  C CA   B GLU   A 1 25  ? 15.616 2.945   14.280  0.52 15.09 ?  25  GLU   A CA   1 
ATOM   677  C C    A GLU   A 1 25  ? 15.645 2.172   14.779  0.48 15.03 ?  25  GLU   A C    1 
ATOM   678  C C    B GLU   A 1 25  ? 15.899 1.596   14.928  0.52 13.85 ?  25  GLU   A C    1 
ATOM   679  O O    A GLU   A 1 25  ? 15.848 2.108   15.997  0.48 15.30 ?  25  GLU   A O    1 
ATOM   680  O O    B GLU   A 1 25  ? 16.127 1.523   16.141  0.52 14.01 ?  25  GLU   A O    1 
ATOM   681  C CB   A GLU   A 1 25  ? 13.914 3.869   14.060  0.48 18.38 ?  25  GLU   A CB   1 
ATOM   682  C CB   B GLU   A 1 25  ? 14.115 3.186   14.123  0.52 16.59 ?  25  GLU   A CB   1 
ATOM   683  C CG   A GLU   A 1 25  ? 13.651 5.330   13.695  0.48 21.20 ?  25  GLU   A CG   1 
ATOM   684  C CG   B GLU   A 1 25  ? 13.788 4.581   13.631  0.52 19.15 ?  25  GLU   A CG   1 
ATOM   685  C CD   A GLU   A 1 25  ? 14.419 6.316   14.565  0.48 23.64 ?  25  GLU   A CD   1 
ATOM   686  C CD   B GLU   A 1 25  ? 14.315 5.646   14.566  0.52 21.61 ?  25  GLU   A CD   1 
ATOM   687  O OE1  A GLU   A 1 25  ? 14.445 6.136   15.801  0.48 24.39 ?  25  GLU   A OE1  1 
ATOM   688  O OE1  B GLU   A 1 25  ? 14.148 5.486   15.795  0.52 22.26 ?  25  GLU   A OE1  1 
ATOM   689  O OE2  A GLU   A 1 25  ? 15.011 7.265   14.008  0.48 24.96 -1 25  GLU   A OE2  1 
ATOM   690  O OE2  B GLU   A 1 25  ? 14.908 6.631   14.078  0.52 23.00 -1 25  GLU   A OE2  1 
ATOM   691  H H    A GLU   A 1 25  ? 15.417 3.624   12.142  0.48 18.06 ?  25  GLU   A H    1 
ATOM   692  H H    B GLU   A 1 25  ? 15.740 3.059   12.312  0.52 16.83 ?  25  GLU   A H    1 
ATOM   693  H HA   A GLU   A 1 25  ? 15.838 4.184   14.673  0.48 19.45 ?  25  GLU   A HA   1 
ATOM   694  H HA   B GLU   A 1 25  ? 15.972 3.622   14.872  0.52 18.08 ?  25  GLU   A HA   1 
ATOM   695  H HB2  A GLU   A 1 25  ? 13.482 3.317   13.386  0.48 22.04 ?  25  GLU   A HB2  1 
ATOM   696  H HB2  B GLU   A 1 25  ? 13.759 2.551   13.481  0.52 19.88 ?  25  GLU   A HB2  1 
ATOM   697  H HB3  A GLU   A 1 25  ? 13.510 3.703   14.926  0.48 22.04 ?  25  GLU   A HB3  1 
ATOM   698  H HB3  B GLU   A 1 25  ? 13.685 3.065   14.983  0.52 19.88 ?  25  GLU   A HB3  1 
ATOM   699  H HG2  A GLU   A 1 25  ? 13.923 5.480   12.778  0.48 25.42 ?  25  GLU   A HG2  1 
ATOM   700  H HG2  B GLU   A 1 25  ? 14.178 4.708   12.749  0.52 22.96 ?  25  GLU   A HG2  1 
ATOM   701  H HG3  A GLU   A 1 25  ? 12.706 5.519   13.800  0.48 25.42 ?  25  GLU   A HG3  1 
ATOM   702  H HG3  B GLU   A 1 25  ? 12.825 4.684   13.584  0.52 22.96 ?  25  GLU   A HG3  1 
ATOM   703  N N    A GLU   A 1 26  ? 15.656 1.092   13.996  0.48 14.67 ?  26  GLU   A N    1 
ATOM   704  N N    B GLU   A 1 26  ? 15.893 0.515   14.141  0.52 13.29 ?  26  GLU   A N    1 
ATOM   705  C CA   A GLU   A 1 26  ? 15.969 -0.219  14.555  0.48 14.85 ?  26  GLU   A CA   1 
ATOM   706  C CA   B GLU   A 1 26  ? 16.285 -0.784  14.680  0.52 13.42 ?  26  GLU   A CA   1 
ATOM   707  C C    A GLU   A 1 26  ? 17.399 -0.262  15.074  0.48 14.51 ?  26  GLU   A C    1 
ATOM   708  C C    B GLU   A 1 26  ? 17.703 -0.736  15.234  0.52 13.18 ?  26  GLU   A C    1 
ATOM   709  O O    A GLU   A 1 26  ? 17.657 -0.776  16.168  0.48 14.69 ?  26  GLU   A O    1 
ATOM   710  O O    B GLU   A 1 26  ? 17.972 -1.251  16.325  0.52 13.90 ?  26  GLU   A O    1 
ATOM   711  C CB   A GLU   A 1 26  ? 15.772 -1.293  13.488  0.48 15.40 ?  26  GLU   A CB   1 
ATOM   712  C CB   B GLU   A 1 26  ? 16.164 -1.865  13.600  0.52 14.38 ?  26  GLU   A CB   1 
ATOM   713  C CG   A GLU   A 1 26  ? 14.337 -1.700  13.288  0.48 16.98 ?  26  GLU   A CG   1 
ATOM   714  C CG   B GLU   A 1 26  ? 14.739 -2.219  13.224  0.52 15.20 ?  26  GLU   A CG   1 
ATOM   715  C CD   A GLU   A 1 26  ? 13.813 -2.543  14.430  0.48 18.49 ?  26  GLU   A CD   1 
ATOM   716  C CD   B GLU   A 1 26  ? 13.960 -2.806  14.385  0.52 15.91 ?  26  GLU   A CD   1 
ATOM   717  O OE1  A GLU   A 1 26  ? 14.374 -3.633  14.671  0.48 19.30 ?  26  GLU   A OE1  1 
ATOM   718  O OE1  B GLU   A 1 26  ? 14.347 -3.886  14.898  0.52 15.98 ?  26  GLU   A OE1  1 
ATOM   719  O OE2  A GLU   A 1 26  ? 12.852 -2.104  15.096  0.48 19.46 -1 26  GLU   A OE2  1 
ATOM   720  O OE2  B GLU   A 1 26  ? 12.960 -2.179  14.782  0.52 16.58 -1 26  GLU   A OE2  1 
ATOM   721  H H    A GLU   A 1 26  ? 15.493 1.096   13.152  0.48 17.58 ?  26  GLU   A H    1 
ATOM   722  H H    B GLU   A 1 26  ? 15.671 0.504   13.310  0.52 15.92 ?  26  GLU   A H    1 
ATOM   723  H HA   A GLU   A 1 26  ? 15.363 -0.407  15.291  0.48 17.80 ?  26  GLU   A HA   1 
ATOM   724  H HA   B GLU   A 1 26  ? 15.691 -1.026  15.406  0.52 16.07 ?  26  GLU   A HA   1 
ATOM   725  H HB2  A GLU   A 1 26  ? 16.101 -0.955  12.640  0.48 18.45 ?  26  GLU   A HB2  1 
ATOM   726  H HB2  B GLU   A 1 26  ? 16.608 -1.559  12.793  0.52 17.23 ?  26  GLU   A HB2  1 
ATOM   727  H HB3  A GLU   A 1 26  ? 16.270 -2.083  13.744  0.48 18.45 ?  26  GLU   A HB3  1 
ATOM   728  H HB3  B GLU   A 1 26  ? 16.590 -2.681  13.915  0.52 17.23 ?  26  GLU   A HB3  1 
ATOM   729  H HG2  A GLU   A 1 26  ? 13.787 -0.906  13.248  0.48 20.35 ?  26  GLU   A HG2  1 
ATOM   730  H HG2  B GLU   A 1 26  ? 14.283 -1.419  12.919  0.52 18.22 ?  26  GLU   A HG2  1 
ATOM   731  H HG3  A GLU   A 1 26  ? 14.265 -2.199  12.457  0.48 20.35 ?  26  GLU   A HG3  1 
ATOM   732  H HG3  B GLU   A 1 26  ? 14.748 -2.884  12.515  0.52 18.22 ?  26  GLU   A HG3  1 
ATOM   733  N N    A ALA   A 1 27  ? 18.343 0.274   14.300  0.48 14.25 ?  27  ALA   A N    1 
ATOM   734  N N    B ALA   A 1 27  ? 18.624 -0.102  14.504  0.52 12.91 ?  27  ALA   A N    1 
ATOM   735  C CA   A ALA   A 1 27  ? 19.741 0.239   14.710  0.48 14.63 ?  27  ALA   A CA   1 
ATOM   736  C CA   B ALA   A 1 27  ? 19.998 -0.010  14.982  0.52 13.25 ?  27  ALA   A CA   1 
ATOM   737  C C    A ALA   A 1 27  ? 19.945 0.995   16.017  0.48 15.84 ?  27  ALA   A C    1 
ATOM   738  C C    B ALA   A 1 27  ? 20.083 0.862   16.229  0.52 13.98 ?  27  ALA   A C    1 
ATOM   739  O O    A ALA   A 1 27  ? 20.620 0.508   16.929  0.48 15.90 ?  27  ALA   A O    1 
ATOM   740  O O    B ALA   A 1 27  ? 20.754 0.501   17.202  0.52 14.44 ?  27  ALA   A O    1 
ATOM   741  C CB   A ALA   A 1 27  ? 20.622 0.813   13.600  0.48 14.36 ?  27  ALA   A CB   1 
ATOM   742  C CB   B ALA   A 1 27  ? 20.908 0.521   13.872  0.52 13.61 ?  27  ALA   A CB   1 
ATOM   743  H H    A ALA   A 1 27  ? 18.192 0.661   13.550  0.48 17.07 ?  27  ALA   A H    1 
ATOM   744  H H    B ALA   A 1 27  ? 18.481 0.264   13.743  0.52 15.47 ?  27  ALA   A H    1 
ATOM   745  H HA   A ALA   A 1 27  ? 19.998 -0.681  14.858  0.48 17.53 ?  27  ALA   A HA   1 
ATOM   746  H HA   B ALA   A 1 27  ? 20.314 -0.898  15.218  0.52 15.88 ?  27  ALA   A HA   1 
ATOM   747  H HB1  A ALA   A 1 27  ? 21.545 0.782   13.888  0.48 17.21 ?  27  ALA   A HB1  1 
ATOM   748  H HB1  B ALA   A 1 27  ? 21.819 0.578   14.207  0.52 16.31 ?  27  ALA   A HB1  1 
ATOM   749  H HB2  A ALA   A 1 27  ? 20.503 0.277   12.800  0.48 17.21 ?  27  ALA   A HB2  1 
ATOM   750  H HB2  B ALA   A 1 27  ? 20.878 -0.091  13.116  0.52 16.31 ?  27  ALA   A HB2  1 
ATOM   751  H HB3  A ALA   A 1 27  ? 20.355 1.729   13.428  0.48 17.21 ?  27  ALA   A HB3  1 
ATOM   752  H HB3  B ALA   A 1 27  ? 20.601 1.397   13.600  0.52 16.31 ?  27  ALA   A HB3  1 
ATOM   753  N N    A LYS   A 1 28  ? 19.360 2.191   16.130  0.48 17.48 ?  28  LYS   A N    1 
ATOM   754  N N    B LYS   A 1 28  ? 19.399 2.011   16.222  0.52 15.64 ?  28  LYS   A N    1 
ATOM   755  C CA   A LYS   A 1 28  ? 19.533 2.971   17.351  0.48 19.58 ?  28  LYS   A CA   1 
ATOM   756  C CA   B LYS   A 1 28  ? 19.380 2.869   17.404  0.52 17.87 ?  28  LYS   A CA   1 
ATOM   757  C C    A LYS   A 1 28  ? 18.974 2.245   18.567  0.48 20.51 ?  28  LYS   A C    1 
ATOM   758  C C    B LYS   A 1 28  ? 18.882 2.119   18.632  0.52 19.20 ?  28  LYS   A C    1 
ATOM   759  O O    A LYS   A 1 28  ? 19.524 2.367   19.668  0.48 21.51 ?  28  LYS   A O    1 
ATOM   760  O O    B LYS   A 1 28  ? 19.359 2.363   19.746  0.52 20.57 ?  28  LYS   A O    1 
ATOM   761  C CB   A LYS   A 1 28  ? 18.896 4.354   17.195  0.48 20.70 ?  28  LYS   A CB   1 
ATOM   762  C CB   B LYS   A 1 28  ? 18.502 4.097   17.150  0.52 18.57 ?  28  LYS   A CB   1 
ATOM   763  C CG   A LYS   A 1 28  ? 19.651 5.260   16.232  0.48 22.01 ?  28  LYS   A CG   1 
ATOM   764  C CG   B LYS   A 1 28  ? 19.143 5.184   16.297  0.52 19.87 ?  28  LYS   A CG   1 
ATOM   765  C CD   A LYS   A 1 28  ? 19.154 6.696   16.284  0.48 23.64 ?  28  LYS   A CD   1 
ATOM   766  C CD   B LYS   A 1 28  ? 18.210 6.381   16.171  0.52 21.80 ?  28  LYS   A CD   1 
ATOM   767  C CE   A LYS   A 1 28  ? 17.826 6.858   15.568  0.48 24.83 ?  28  LYS   A CE   1 
ATOM   768  C CE   B LYS   A 1 28  ? 18.772 7.452   15.251  0.52 23.64 ?  28  LYS   A CE   1 
ATOM   769  N NZ   A LYS   A 1 28  ? 17.398 8.282   15.534  0.48 25.49 ?  28  LYS   A NZ   1 
ATOM   770  N NZ   B LYS   A 1 28  ? 17.784 8.541   14.997  0.52 24.98 ?  28  LYS   A NZ   1 
ATOM   771  H H    A LYS   A 1 28  ? 18.869 2.564   15.531  0.48 20.95 ?  28  LYS   A H    1 
ATOM   772  H H    B LYS   A 1 28  ? 18.944 2.304   15.555  0.52 18.74 ?  28  LYS   A H    1 
ATOM   773  H HA   A LYS   A 1 28  ? 20.479 3.104   17.506  0.48 23.47 ?  28  LYS   A HA   1 
ATOM   774  H HA   B LYS   A 1 28  ? 20.278 3.178   17.586  0.52 21.42 ?  28  LYS   A HA   1 
ATOM   775  H HB2  A LYS   A 1 28  ? 17.994 4.251   16.857  0.48 24.82 ?  28  LYS   A HB2  1 
ATOM   776  H HB2  B LYS   A 1 28  ? 17.694 3.814   16.693  0.52 22.27 ?  28  LYS   A HB2  1 
ATOM   777  H HB3  A LYS   A 1 28  ? 18.877 4.794   18.060  0.48 24.82 ?  28  LYS   A HB3  1 
ATOM   778  H HB3  B LYS   A 1 28  ? 18.273 4.497   18.001  0.52 22.27 ?  28  LYS   A HB3  1 
ATOM   779  H HG2  A LYS   A 1 28  ? 20.593 5.259   16.464  0.48 26.39 ?  28  LYS   A HG2  1 
ATOM   780  H HG2  B LYS   A 1 28  ? 19.966 5.481   16.715  0.52 23.82 ?  28  LYS   A HG2  1 
ATOM   781  H HG3  A LYS   A 1 28  ? 19.530 4.933   15.326  0.48 26.39 ?  28  LYS   A HG3  1 
ATOM   782  H HG3  B LYS   A 1 28  ? 19.319 4.840   15.407  0.52 23.82 ?  28  LYS   A HG3  1 
ATOM   783  H HD2  A LYS   A 1 28  ? 19.033 6.959   17.210  0.48 28.35 ?  28  LYS   A HD2  1 
ATOM   784  H HD2  B LYS   A 1 28  ? 17.360 6.088   15.807  0.52 26.13 ?  28  LYS   A HD2  1 
ATOM   785  H HD3  A LYS   A 1 28  ? 19.803 7.275   15.854  0.48 28.35 ?  28  LYS   A HD3  1 
ATOM   786  H HD3  B LYS   A 1 28  ? 18.078 6.777   17.048  0.52 26.13 ?  28  LYS   A HD3  1 
ATOM   787  H HE2  A LYS   A 1 28  ? 17.916 6.544   14.654  0.48 29.77 ?  28  LYS   A HE2  1 
ATOM   788  H HE2  B LYS   A 1 28  ? 19.558 7.847   15.661  0.52 28.35 ?  28  LYS   A HE2  1 
ATOM   789  H HE3  A LYS   A 1 28  ? 17.147 6.346   16.034  0.48 29.77 ?  28  LYS   A HE3  1 
ATOM   790  H HE3  B LYS   A 1 28  ? 19.005 7.051   14.399  0.52 28.35 ?  28  LYS   A HE3  1 
ATOM   791  H HZ1  A LYS   A 1 28  ? 16.620 8.356   15.110  0.48 30.56 ?  28  LYS   A HZ1  1 
ATOM   792  H HZ1  B LYS   A 1 28  ? 18.137 9.154   14.456  0.52 29.96 ?  28  LYS   A HZ1  1 
ATOM   793  H HZ2  A LYS   A 1 28  ? 17.308 8.593   16.363  0.48 30.56 ?  28  LYS   A HZ2  1 
ATOM   794  H HZ2  B LYS   A 1 28  ? 17.052 8.206   14.615  0.52 29.96 ?  28  LYS   A HZ2  1 
ATOM   795  H HZ3  A LYS   A 1 28  ? 18.007 8.773   15.107  0.48 30.56 ?  28  LYS   A HZ3  1 
ATOM   796  H HZ3  B LYS   A 1 28  ? 17.556 8.931   15.765  0.52 29.96 ?  28  LYS   A HZ3  1 
ATOM   797  N N    A LYS   A 1 29  ? 17.901 1.472   18.390  0.48 21.15 ?  29  LYS   A N    1 
ATOM   798  N N    B LYS   A 1 29  ? 17.933 1.200   18.452  0.52 19.81 ?  29  LYS   A N    1 
ATOM   799  C CA   A LYS   A 1 29  ? 17.290 0.770   19.514  0.48 22.87 ?  29  LYS   A CA   1 
ATOM   800  C CA   B LYS   A 1 29  ? 17.346 0.489   19.584  0.52 21.23 ?  29  LYS   A CA   1 
ATOM   801  C C    A LYS   A 1 29  ? 18.105 -0.456  19.917  0.48 22.69 ?  29  LYS   A C    1 
ATOM   802  C C    B LYS   A 1 29  ? 18.187 -0.718  19.984  0.52 20.53 ?  29  LYS   A C    1 
ATOM   803  O O    A LYS   A 1 29  ? 18.375 -0.669  21.104  0.48 23.45 ?  29  LYS   A O    1 
ATOM   804  O O    B LYS   A 1 29  ? 18.455 -0.934  21.172  0.52 21.15 ?  29  LYS   A O    1 
ATOM   805  C CB   A LYS   A 1 29  ? 15.858 0.365   19.150  0.48 25.07 ?  29  LYS   A CB   1 
ATOM   806  C CB   B LYS   A 1 29  ? 15.927 0.043   19.224  0.52 23.95 ?  29  LYS   A CB   1 
ATOM   807  C CG   A LYS   A 1 29  ? 15.099 -0.335  20.268  0.48 27.59 ?  29  LYS   A CG   1 
ATOM   808  C CG   B LYS   A 1 29  ? 15.137 -0.550  20.380  0.52 26.92 ?  29  LYS   A CG   1 
ATOM   809  C CD   A LYS   A 1 29  ? 14.747 0.631   21.385  0.48 30.07 ?  29  LYS   A CD   1 
ATOM   810  C CD   B LYS   A 1 29  ? 14.757 0.513   21.396  0.52 29.69 ?  29  LYS   A CD   1 
ATOM   811  C CE   A LYS   A 1 29  ? 13.872 -0.032  22.436  0.48 31.75 ?  29  LYS   A CE   1 
ATOM   812  C CE   B LYS   A 1 29  ? 13.835 -0.047  22.466  0.52 31.54 ?  29  LYS   A CE   1 
ATOM   813  N NZ   A LYS   A 1 29  ? 13.410 0.938   23.465  0.48 32.71 ?  29  LYS   A NZ   1 
ATOM   814  N NZ   B LYS   A 1 29  ? 13.402 1.003   23.427  0.52 32.60 ?  29  LYS   A NZ   1 
ATOM   815  H H    A LYS   A 1 29  ? 17.513 1.339   17.634  0.48 25.35 ?  29  LYS   A H    1 
ATOM   816  H H    B LYS   A 1 29  ? 17.614 0.971   17.686  0.52 23.75 ?  29  LYS   A H    1 
ATOM   817  H HA   A LYS   A 1 29  ? 17.244 1.368   20.276  0.48 27.42 ?  29  LYS   A HA   1 
ATOM   818  H HA   B LYS   A 1 29  ? 17.292 1.088   20.344  0.52 25.45 ?  29  LYS   A HA   1 
ATOM   819  H HB2  A LYS   A 1 29  ? 15.356 1.163   18.914  0.48 30.06 ?  29  LYS   A HB2  1 
ATOM   820  H HB2  B LYS   A 1 29  ? 15.434 0.810   18.896  0.52 28.71 ?  29  LYS   A HB2  1 
ATOM   821  H HB3  A LYS   A 1 29  ? 15.885 -0.238  18.391  0.48 30.06 ?  29  LYS   A HB3  1 
ATOM   822  H HB3  B LYS   A 1 29  ? 15.981 -0.632  18.530  0.52 28.71 ?  29  LYS   A HB3  1 
ATOM   823  H HG2  A LYS   A 1 29  ? 14.275 -0.701  19.912  0.48 33.08 ?  29  LYS   A HG2  1 
ATOM   824  H HG2  B LYS   A 1 29  ? 14.321 -0.948  20.038  0.52 32.28 ?  29  LYS   A HG2  1 
ATOM   825  H HG3  A LYS   A 1 29  ? 15.646 -1.046  20.639  0.48 33.08 ?  29  LYS   A HG3  1 
ATOM   826  H HG3  B LYS   A 1 29  ? 15.674 -1.222  20.829  0.52 32.28 ?  29  LYS   A HG3  1 
ATOM   827  H HD2  A LYS   A 1 29  ? 15.562 0.936   21.815  0.48 36.05 ?  29  LYS   A HD2  1 
ATOM   828  H HD2  B LYS   A 1 29  ? 15.560 0.845   21.829  0.52 35.60 ?  29  LYS   A HD2  1 
ATOM   829  H HD3  A LYS   A 1 29  ? 14.261 1.385   21.014  0.48 36.05 ?  29  LYS   A HD3  1 
ATOM   830  H HD3  B LYS   A 1 29  ? 14.296 1.238   20.944  0.52 35.60 ?  29  LYS   A HD3  1 
ATOM   831  H HE2  A LYS   A 1 29  ? 13.090 -0.413  22.005  0.48 38.08 ?  29  LYS   A HE2  1 
ATOM   832  H HE2  B LYS   A 1 29  ? 13.044 -0.417  22.043  0.52 37.83 ?  29  LYS   A HE2  1 
ATOM   833  H HE3  A LYS   A 1 29  ? 14.381 -0.728  22.881  0.48 38.08 ?  29  LYS   A HE3  1 
ATOM   834  H HE3  B LYS   A 1 29  ? 14.303 -0.738  22.961  0.52 37.83 ?  29  LYS   A HE3  1 
ATOM   835  H HZ1  A LYS   A 1 29  ? 12.901 0.524   24.066  0.48 39.22 ?  29  LYS   A HZ1  1 
ATOM   836  H HZ1  B LYS   A 1 29  ? 12.864 0.650   24.041  0.52 39.10 ?  29  LYS   A HZ1  1 
ATOM   837  H HZ2  A LYS   A 1 29  ? 14.111 1.299   23.879  0.48 39.22 ?  29  LYS   A HZ2  1 
ATOM   838  H HZ2  B LYS   A 1 29  ? 14.112 1.356   23.831  0.52 39.10 ?  29  LYS   A HZ2  1 
ATOM   839  H HZ3  A LYS   A 1 29  ? 12.936 1.586   23.081  0.48 39.22 ?  29  LYS   A HZ3  1 
ATOM   840  H HZ3  B LYS   A 1 29  ? 12.965 1.647   22.995  0.52 39.10 ?  29  LYS   A HZ3  1 
ATOM   841  N N    A VAL   A 1 30  ? 18.503 -1.271  18.943  0.48 21.91 ?  30  VAL   A N    1 
ATOM   842  N N    B VAL   A 1 30  ? 18.601 -1.520  19.008  0.52 19.37 ?  30  VAL   A N    1 
ATOM   843  C CA   A VAL   A 1 30  ? 19.132 -2.561  19.221  0.48 21.86 ?  30  VAL   A CA   1 
ATOM   844  C CA   B VAL   A 1 30  ? 19.288 -2.772  19.299  0.52 19.61 ?  30  VAL   A CA   1 
ATOM   845  C C    A VAL   A 1 30  ? 20.636 -2.427  19.446  0.48 21.37 ?  30  VAL   A C    1 
ATOM   846  C C    B VAL   A 1 30  ? 20.793 -2.582  19.472  0.52 18.98 ?  30  VAL   A C    1 
ATOM   847  O O    A VAL   A 1 30  ? 21.205 -3.133  20.282  0.48 21.60 ?  30  VAL   A O    1 
ATOM   848  O O    B VAL   A 1 30  ? 21.426 -3.330  20.226  0.52 19.30 ?  30  VAL   A O    1 
ATOM   849  C CB   A VAL   A 1 30  ? 18.807 -3.543  18.075  0.48 22.55 ?  30  VAL   A CB   1 
ATOM   850  C CB   B VAL   A 1 30  ? 18.985 -3.793  18.188  0.52 21.00 ?  30  VAL   A CB   1 
ATOM   851  C CG1  A VAL   A 1 30  ? 19.555 -4.857  18.255  0.48 23.00 ?  30  VAL   A CG1  1 
ATOM   852  C CG1  B VAL   A 1 30  ? 19.784 -5.072  18.393  0.52 21.63 ?  30  VAL   A CG1  1 
ATOM   853  C CG2  A VAL   A 1 30  ? 17.307 -3.790  17.998  0.48 22.94 ?  30  VAL   A CG2  1 
ATOM   854  C CG2  B VAL   A 1 30  ? 17.495 -4.090  18.132  0.52 21.76 ?  30  VAL   A CG2  1 
ATOM   855  H H    A VAL   A 1 30  ? 18.409 -1.103  18.105  0.48 26.27 ?  30  VAL   A H    1 
ATOM   856  H H    B VAL   A 1 30  ? 18.493 -1.366  18.166  0.52 23.22 ?  30  VAL   A H    1 
ATOM   857  H HA   A VAL   A 1 30  ? 18.745 -2.927  20.031  0.48 26.20 ?  30  VAL   A HA   1 
ATOM   858  H HA   B VAL   A 1 30  ? 18.931 -3.130  20.128  0.52 23.51 ?  30  VAL   A HA   1 
ATOM   859  H HB   A VAL   A 1 30  ? 19.087 -3.153  17.232  0.48 27.03 ?  30  VAL   A HB   1 
ATOM   860  H HB   B VAL   A 1 30  ? 19.248 -3.416  17.335  0.52 25.18 ?  30  VAL   A HB   1 
ATOM   861  H HG11 A VAL   A 1 30  ? 19.164 -5.525  17.668  0.48 27.58 ?  30  VAL   A HG11 1 
ATOM   862  H HG11 B VAL   A 1 30  ? 19.398 -5.774  17.845  0.52 25.94 ?  30  VAL   A HG11 1 
ATOM   863  H HG12 A VAL   A 1 30  ? 20.488 -4.726  18.027  0.48 27.58 ?  30  VAL   A HG12 1 
ATOM   864  H HG12 B VAL   A 1 30  ? 20.704 -4.918  18.131  0.52 25.94 ?  30  VAL   A HG12 1 
ATOM   865  H HG13 A VAL   A 1 30  ? 19.472 -5.143  19.178  0.48 27.58 ?  30  VAL   A HG13 1 
ATOM   866  H HG13 B VAL   A 1 30  ? 19.741 -5.323  19.328  0.52 25.94 ?  30  VAL   A HG13 1 
ATOM   867  H HG21 A VAL   A 1 30  ? 17.128 -4.442  17.300  0.48 27.50 ?  30  VAL   A HG21 1 
ATOM   868  H HG21 B VAL   A 1 30  ? 17.333 -4.768  17.458  0.52 26.09 ?  30  VAL   A HG21 1 
ATOM   869  H HG22 A VAL   A 1 30  ? 17.000 -4.132  18.853  0.48 27.50 ?  30  VAL   A HG22 1 
ATOM   870  H HG22 B VAL   A 1 30  ? 17.204 -4.410  19.000  0.52 26.09 ?  30  VAL   A HG22 1 
ATOM   871  H HG23 A VAL   A 1 30  ? 16.857 -2.956  17.794  0.48 27.50 ?  30  VAL   A HG23 1 
ATOM   872  H HG23 B VAL   A 1 30  ? 17.020 -3.276  17.903  0.52 26.09 ?  30  VAL   A HG23 1 
ATOM   873  N N    A LYS   A 1 31  ? 21.297 -1.527  18.726  0.48 20.80 ?  31  LYS   A N    1 
ATOM   874  N N    B LYS   A 1 31  ? 21.376 -1.594  18.801  0.52 18.45 ?  31  LYS   A N    1 
ATOM   875  C CA   A LYS   A 1 31  ? 22.753 -1.443  18.700  0.48 21.23 ?  31  LYS   A CA   1 
ATOM   876  C CA   B LYS   A 1 31  ? 22.823 -1.442  18.712  0.52 19.36 ?  31  LYS   A CA   1 
ATOM   877  C C    A LYS   A 1 31  ? 23.359 -2.810  18.363  0.48 19.03 ?  31  LYS   A C    1 
ATOM   878  C C    B LYS   A 1 31  ? 23.456 -2.780  18.320  0.52 17.90 ?  31  LYS   A C    1 
ATOM   879  O O    A LYS   A 1 31  ? 24.080 -3.397  19.175  0.48 19.19 ?  31  LYS   A O    1 
ATOM   880  O O    B LYS   A 1 31  ? 24.290 -3.321  19.054  0.52 18.27 ?  31  LYS   A O    1 
ATOM   881  C CB   A LYS   A 1 31  ? 23.315 -0.895  20.004  0.48 24.91 ?  31  LYS   A CB   1 
ATOM   882  C CB   B LYS   A 1 31  ? 23.422 -0.907  20.006  0.52 23.46 ?  31  LYS   A CB   1 
ATOM   883  C CG   A LYS   A 1 31  ? 22.596 0.357   20.501  0.48 28.93 ?  31  LYS   A CG   1 
ATOM   884  C CG   B LYS   A 1 31  ? 22.703 0.321   20.556  0.52 28.06 ?  31  LYS   A CG   1 
ATOM   885  C CD   A LYS   A 1 31  ? 23.568 1.458   20.903  0.48 32.11 ?  31  LYS   A CD   1 
ATOM   886  C CD   B LYS   A 1 31  ? 23.654 1.492   20.763  0.52 31.57 ?  31  LYS   A CD   1 
ATOM   887  C CE   A LYS   A 1 31  ? 22.900 2.498   21.797  0.48 34.17 ?  31  LYS   A CE   1 
ATOM   888  C CE   B LYS   A 1 31  ? 23.091 2.505   21.753  0.52 33.80 ?  31  LYS   A CE   1 
ATOM   889  N NZ   A LYS   A 1 31  ? 21.735 3.167   21.152  0.48 35.31 ?  31  LYS   A NZ   1 
ATOM   890  N NZ   B LYS   A 1 31  ? 21.745 3.016   21.368  0.52 34.98 ?  31  LYS   A NZ   1 
ATOM   891  H H    A LYS   A 1 31  ? 20.914 -0.934  18.235  0.48 24.94 ?  31  LYS   A H    1 
ATOM   892  H H    B LYS   A 1 31  ? 20.940 -0.984  18.379  0.52 22.12 ?  31  LYS   A H    1 
ATOM   893  H HA   A LYS   A 1 31  ? 23.005 -0.825  18.000  0.48 25.45 ?  31  LYS   A HA   1 
ATOM   894  H HA   B LYS   A 1 31  ? 23.019 -0.809  18.010  0.52 23.21 ?  31  LYS   A HA   1 
ATOM   895  H HB2  A LYS   A 1 31  ? 23.241 -1.574  20.690  0.48 29.86 ?  31  LYS   A HB2  1 
ATOM   896  H HB2  B LYS   A 1 31  ? 23.387 -1.600  20.681  0.52 28.12 ?  31  LYS   A HB2  1 
ATOM   897  H HB3  A LYS   A 1 31  ? 24.250 -0.665  19.869  0.48 29.86 ?  31  LYS   A HB3  1 
ATOM   898  H HB3  B LYS   A 1 31  ? 24.346 -0.659  19.837  0.52 28.12 ?  31  LYS   A HB3  1 
ATOM   899  H HG2  A LYS   A 1 31  ? 22.028 0.701   19.794  0.48 34.69 ?  31  LYS   A HG2  1 
ATOM   900  H HG2  B LYS   A 1 31  ? 22.024 0.600   19.925  0.52 33.65 ?  31  LYS   A HG2  1 
ATOM   901  H HG3  A LYS   A 1 31  ? 22.061 0.128   21.277  0.48 34.69 ?  31  LYS   A HG3  1 
ATOM   902  H HG3  B LYS   A 1 31  ? 22.291 0.102   21.406  0.52 33.65 ?  31  LYS   A HG3  1 
ATOM   903  H HD2  A LYS   A 1 31  ? 24.309 1.070   21.392  0.48 38.51 ?  31  LYS   A HD2  1 
ATOM   904  H HD2  B LYS   A 1 31  ? 24.497 1.165   21.112  0.52 37.87 ?  31  LYS   A HD2  1 
ATOM   905  H HD3  A LYS   A 1 31  ? 23.891 1.907   20.104  0.48 38.51 ?  31  LYS   A HD3  1 
ATOM   906  H HD3  B LYS   A 1 31  ? 23.794 1.942   19.914  0.52 37.87 ?  31  LYS   A HD3  1 
ATOM   907  H HE2  A LYS   A 1 31  ? 22.584 2.063   22.604  0.48 40.98 ?  31  LYS   A HE2  1 
ATOM   908  H HE2  B LYS   A 1 31  ? 23.012 2.083   22.622  0.52 40.53 ?  31  LYS   A HE2  1 
ATOM   909  H HE3  A LYS   A 1 31  ? 23.548 3.184   22.023  0.48 40.98 ?  31  LYS   A HE3  1 
ATOM   910  H HE3  B LYS   A 1 31  ? 23.694 3.263   21.806  0.52 40.53 ?  31  LYS   A HE3  1 
ATOM   911  H HZ1  A LYS   A 1 31  ? 21.379 3.764   21.709  0.48 42.35 ?  31  LYS   A HZ1  1 
ATOM   912  H HZ1  B LYS   A 1 31  ? 21.463 3.610   21.969  0.52 41.95 ?  31  LYS   A HZ1  1 
ATOM   913  H HZ2  A LYS   A 1 31  ? 21.995 3.583   20.410  0.48 42.35 ?  31  LYS   A HZ2  1 
ATOM   914  H HZ2  B LYS   A 1 31  ? 21.785 3.408   20.571  0.52 41.95 ?  31  LYS   A HZ2  1 
ATOM   915  H HZ3  A LYS   A 1 31  ? 21.115 2.563   20.943  0.48 42.35 ?  31  LYS   A HZ3  1 
ATOM   916  H HZ3  B LYS   A 1 31  ? 21.163 2.343   21.332  0.52 41.95 ?  31  LYS   A HZ3  1 
ATOM   917  N N    . PRO   A 1 32  ? 23.072 -3.338  17.177  1.00 16.80 ?  32  PRO   A N    1 
ATOM   918  C CA   . PRO   A 1 32  ? 23.550 -4.671  16.816  1.00 16.56 ?  32  PRO   A CA   1 
ATOM   919  C C    . PRO   A 1 32  ? 25.048 -4.677  16.586  1.00 16.35 ?  32  PRO   A C    1 
ATOM   920  O O    . PRO   A 1 32  ? 25.681 -3.641  16.371  1.00 16.26 ?  32  PRO   A O    1 
ATOM   921  C CB   . PRO   A 1 32  ? 22.804 -4.951  15.507  1.00 16.87 ?  32  PRO   A CB   1 
ATOM   922  C CG   . PRO   A 1 32  ? 22.631 -3.583  14.900  1.00 15.82 ?  32  PRO   A CG   1 
ATOM   923  C CD   . PRO   A 1 32  ? 22.336 -2.697  16.075  1.00 15.78 ?  32  PRO   A CD   1 
ATOM   924  H HA   . PRO   A 1 32  ? 23.310 -5.326  17.489  1.00 19.85 ?  32  PRO   A HA   1 
ATOM   925  H HB2  . PRO   A 1 32  ? 23.336 -5.527  14.935  1.00 20.22 ?  32  PRO   A HB2  1 
ATOM   926  H HB3  . PRO   A 1 32  ? 21.941 -5.360  15.699  1.00 20.22 ?  32  PRO   A HB3  1 
ATOM   927  H HG2  . PRO   A 1 32  ? 23.450 -3.325  14.454  1.00 18.96 ?  32  PRO   A HG2  1 
ATOM   928  H HG3  . PRO   A 1 32  ? 21.886 -3.600  14.276  1.00 18.96 ?  32  PRO   A HG3  1 
ATOM   929  H HD2  . PRO   A 1 32  ? 22.680 -1.806  15.900  1.00 18.92 ?  32  PRO   A HD2  1 
ATOM   930  H HD3  . PRO   A 1 32  ? 21.389 -2.689  16.256  1.00 18.92 ?  32  PRO   A HD3  1 
ATOM   931  N N    A THR   A 1 33  ? 25.615 -5.883  16.628  0.48 16.47 ?  33  THR   A N    1 
ATOM   932  N N    B THR   A 1 33  ? 25.614 -5.883  16.616  0.52 16.52 ?  33  THR   A N    1 
ATOM   933  C CA   A THR   A 1 33  ? 27.023 -6.044  16.290  0.48 16.65 ?  33  THR   A CA   1 
ATOM   934  C CA   B THR   A 1 33  ? 27.027 -6.036  16.292  0.52 16.65 ?  33  THR   A CA   1 
ATOM   935  C C    A THR   A 1 33  ? 27.298 -5.563  14.870  0.48 15.08 ?  33  THR   A C    1 
ATOM   936  C C    B THR   A 1 33  ? 27.311 -5.583  14.865  0.52 15.04 ?  33  THR   A C    1 
ATOM   937  O O    A THR   A 1 33  ? 28.308 -4.895  14.615  0.48 15.24 ?  33  THR   A O    1 
ATOM   938  O O    B THR   A 1 33  ? 28.345 -4.957  14.598  0.52 15.14 ?  33  THR   A O    1 
ATOM   939  C CB   A THR   A 1 33  ? 27.420 -7.511  16.458  0.48 18.14 ?  33  THR   A CB   1 
ATOM   940  C CB   B THR   A 1 33  ? 27.444 -7.492  16.501  0.52 18.12 ?  33  THR   A CB   1 
ATOM   941  O OG1  A THR   A 1 33  ? 27.113 -7.936  17.791  0.48 19.26 ?  33  THR   A OG1  1 
ATOM   942  O OG1  B THR   A 1 33  ? 27.211 -7.860  17.866  0.52 19.38 ?  33  THR   A OG1  1 
ATOM   943  C CG2  A THR   A 1 33  ? 28.907 -7.709  16.192  0.48 18.60 ?  33  THR   A CG2  1 
ATOM   944  C CG2  B THR   A 1 33  ? 28.915 -7.690  16.169  0.52 18.65 ?  33  THR   A CG2  1 
ATOM   945  H H    A THR   A 1 33  ? 25.210 -6.611  16.840  0.48 19.74 ?  33  THR   A H    1 
ATOM   946  H H    B THR   A 1 33  ? 25.207 -6.615  16.811  0.52 19.80 ?  33  THR   A H    1 
ATOM   947  H HA   A THR   A 1 33  ? 27.559 -5.514  16.896  0.48 19.95 ?  33  THR   A HA   1 
ATOM   948  H HA   B THR   A 1 33  ? 27.550 -5.486  16.891  0.52 19.96 ?  33  THR   A HA   1 
ATOM   949  H HB   A THR   A 1 33  ? 26.924 -8.056  15.826  0.48 21.74 ?  33  THR   A HB   1 
ATOM   950  H HB   B THR   A 1 33  ? 26.920 -8.068  15.919  0.52 21.72 ?  33  THR   A HB   1 
ATOM   951  H HG1  A THR   A 1 33  ? 27.539 -7.468  18.346  0.48 23.09 ?  33  THR   A HG1  1 
ATOM   952  H HG1  B THR   A 1 33  ? 27.665 -7.370  18.376  0.52 23.23 ?  33  THR   A HG1  1 
ATOM   953  H HG21 A THR   A 1 33  ? 29.171 -8.608  16.444  0.48 22.29 ?  33  THR   A HG21 1 
ATOM   954  H HG21 B THR   A 1 33  ? 29.210 -8.558  16.484  0.52 22.35 ?  33  THR   A HG21 1 
ATOM   955  H HG22 A THR   A 1 33  ? 29.099 -7.578  15.250  0.48 22.29 ?  33  THR   A HG22 1 
ATOM   956  H HG22 B THR   A 1 33  ? 29.051 -7.640  15.210  0.52 22.35 ?  33  THR   A HG22 1 
ATOM   957  H HG23 A THR   A 1 33  ? 29.423 -7.072  16.711  0.48 22.29 ?  33  THR   A HG23 1 
ATOM   958  H HG23 B THR   A 1 33  ? 29.445 -7.002  16.601  0.52 22.35 ?  33  THR   A HG23 1 
ATOM   959  N N    . VAL   A 1 34  ? 26.399 -5.875  13.937  1.00 13.92 ?  34  VAL   A N    1 
ATOM   960  C CA   . VAL   A 1 34  ? 26.565 -5.527  12.528  1.00 12.38 ?  34  VAL   A CA   1 
ATOM   961  C C    . VAL   A 1 34  ? 25.256 -4.965  11.984  1.00 12.12 ?  34  VAL   A C    1 
ATOM   962  O O    . VAL   A 1 34  ? 24.219 -5.641  12.028  1.00 12.68 ?  34  VAL   A O    1 
ATOM   963  C CB   . VAL   A 1 34  ? 26.993 -6.737  11.676  1.00 13.01 ?  34  VAL   A CB   1 
ATOM   964  C CG1  . VAL   A 1 34  ? 27.162 -6.319  10.223  1.00 13.50 ?  34  VAL   A CG1  1 
ATOM   965  C CG2  . VAL   A 1 34  ? 28.269 -7.380  12.212  1.00 14.68 ?  34  VAL   A CG2  1 
ATOM   966  H H    A VAL   A 1 34  ? 25.668 -6.297  14.101  0.48 16.68 ?  34  VAL   A H    1 
ATOM   967  H H    B VAL   A 1 34  ? 25.660 -6.283  14.104  0.52 16.68 ?  34  VAL   A H    1 
ATOM   968  H HA   . VAL   A 1 34  ? 27.240 -4.837  12.439  1.00 14.83 ?  34  VAL   A HA   1 
ATOM   969  H HB   . VAL   A 1 34  ? 26.288 -7.399  11.705  1.00 15.59 ?  34  VAL   A HB   1 
ATOM   970  H HG11 . VAL   A 1 34  ? 27.644 -7.015  9.748   1.00 16.18 ?  34  VAL   A HG11 1 
ATOM   971  H HG12 . VAL   A 1 34  ? 26.290 -6.189  9.817   1.00 16.18 ?  34  VAL   A HG12 1 
ATOM   972  H HG13 . VAL   A 1 34  ? 27.670 -5.489  10.186  1.00 16.18 ?  34  VAL   A HG13 1 
ATOM   973  H HG21 . VAL   A 1 34  ? 28.530 -8.104  11.618  1.00 17.59 ?  34  VAL   A HG21 1 
ATOM   974  H HG22 . VAL   A 1 34  ? 28.972 -6.713  12.245  1.00 17.59 ?  34  VAL   A HG22 1 
ATOM   975  H HG23 . VAL   A 1 34  ? 28.098 -7.728  13.099  1.00 17.59 ?  34  VAL   A HG23 1 
ATOM   976  N N    . VAL   A 1 35  ? 25.310 -3.746  11.441  1.00 11.33 ?  35  VAL   A N    1 
ATOM   977  C CA   . VAL   A 1 35  ? 24.269 -3.224  10.564  1.00 11.24 ?  35  VAL   A CA   1 
ATOM   978  C C    . VAL   A 1 35  ? 24.812 -3.214  9.141   1.00 10.41 ?  35  VAL   A C    1 
ATOM   979  O O    . VAL   A 1 35  ? 25.955 -2.797  8.907   1.00 10.80 ?  35  VAL   A O    1 
ATOM   980  C CB   . VAL   A 1 35  ? 23.752 -1.838  11.001  1.00 11.60 ?  35  VAL   A CB   1 
ATOM   981  C CG1  . VAL   A 1 35  ? 24.820 -0.742  10.867  1.00 12.12 ?  35  VAL   A CG1  1 
ATOM   982  C CG2  . VAL   A 1 35  ? 22.503 -1.470  10.203  1.00 12.09 ?  35  VAL   A CG2  1 
ATOM   983  H H    . VAL   A 1 35  ? 25.942 -3.186  11.576  1.00 13.58 ?  35  VAL   A H    1 
ATOM   984  H HA   . VAL   A 1 35  ? 23.505 -3.829  10.588  1.00 13.47 ?  35  VAL   A HA   1 
ATOM   985  H HB   . VAL   A 1 35  ? 23.486 -1.876  11.932  1.00 13.89 ?  35  VAL   A HB   1 
ATOM   986  H HG11 . VAL   A 1 35  ? 24.478 0.087   11.250  1.00 14.52 ?  35  VAL   A HG11 1 
ATOM   987  H HG12 . VAL   A 1 35  ? 25.614 -1.020  11.342  1.00 14.52 ?  35  VAL   A HG12 1 
ATOM   988  H HG13 . VAL   A 1 35  ? 25.023 -0.605  9.927   1.00 14.52 ?  35  VAL   A HG13 1 
ATOM   989  H HG21 . VAL   A 1 35  ? 22.152 -0.622  10.523  1.00 14.48 ?  35  VAL   A HG21 1 
ATOM   990  H HG22 . VAL   A 1 35  ? 22.732 -1.394  9.262   1.00 14.48 ?  35  VAL   A HG22 1 
ATOM   991  H HG23 . VAL   A 1 35  ? 21.832 -2.165  10.321  1.00 14.48 ?  35  VAL   A HG23 1 
ATOM   992  N N    . VAL   A 1 36  ? 23.997 -3.677  8.196   1.00 10.04 ?  36  VAL   A N    1 
ATOM   993  C CA   . VAL   A 1 36  ? 24.362 -3.679  6.785   1.00 9.63  ?  36  VAL   A CA   1 
ATOM   994  C C    . VAL   A 1 36  ? 23.894 -2.380  6.147   1.00 9.72  ?  36  VAL   A C    1 
ATOM   995  O O    . VAL   A 1 36  ? 22.736 -1.969  6.312   1.00 10.46 ?  36  VAL   A O    1 
ATOM   996  C CB   . VAL   A 1 36  ? 23.746 -4.883  6.059   1.00 9.74  ?  36  VAL   A CB   1 
ATOM   997  C CG1  . VAL   A 1 36  ? 24.003 -4.788  4.570   1.00 10.01 ?  36  VAL   A CG1  1 
ATOM   998  C CG2  . VAL   A 1 36  ? 24.279 -6.184  6.627   1.00 10.62 ?  36  VAL   A CG2  1 
ATOM   999  H H    . VAL   A 1 36  ? 23.209 -4.007  8.349   1.00 12.02 ?  36  VAL   A H    1 
ATOM   1000 H HA   . VAL   A 1 36  ? 25.326 -3.743  6.705   1.00 11.53 ?  36  VAL   A HA   1 
ATOM   1001 H HB   . VAL   A 1 36  ? 22.782 -4.870  6.192   1.00 11.66 ?  36  VAL   A HB   1 
ATOM   1002 H HG11 . VAL   A 1 36  ? 23.868 -5.658  4.172   1.00 11.99 ?  36  VAL   A HG11 1 
ATOM   1003 H HG12 . VAL   A 1 36  ? 23.388 -4.145  4.180   1.00 11.99 ?  36  VAL   A HG12 1 
ATOM   1004 H HG13 . VAL   A 1 36  ? 24.919 -4.497  4.432   1.00 11.99 ?  36  VAL   A HG13 1 
ATOM   1005 H HG21 . VAL   A 1 36  ? 23.888 -6.927  6.141   1.00 12.72 ?  36  VAL   A HG21 1 
ATOM   1006 H HG22 . VAL   A 1 36  ? 25.244 -6.196  6.530   1.00 12.72 ?  36  VAL   A HG22 1 
ATOM   1007 H HG23 . VAL   A 1 36  ? 24.040 -6.243  7.566   1.00 12.72 ?  36  VAL   A HG23 1 
ATOM   1008 N N    . ASN   A 1 37  ? 24.798 -1.742  5.405   1.00 9.10  ?  37  ASN   A N    1 
ATOM   1009 C CA   . ASN   A 1 37  ? 24.455 -0.621  4.548   1.00 8.90  ?  37  ASN   A CA   1 
ATOM   1010 C C    . ASN   A 1 37  ? 24.303 -1.083  3.109   1.00 8.98  ?  37  ASN   A C    1 
ATOM   1011 O O    . ASN   A 1 37  ? 25.090 -1.900  2.616   1.00 9.54  ?  37  ASN   A O    1 
ATOM   1012 C CB   . ASN   A 1 37  ? 25.527 0.470   4.618   1.00 8.93  ?  37  ASN   A CB   1 
ATOM   1013 C CG   . ASN   A 1 37  ? 25.185 1.669   3.764   1.00 8.91  ?  37  ASN   A CG   1 
ATOM   1014 O OD1  . ASN   A 1 37  ? 24.010 1.998   3.588   1.00 10.01 ?  37  ASN   A OD1  1 
ATOM   1015 N ND2  . ASN   A 1 37  ? 26.211 2.329   3.235   1.00 9.36  ?  37  ASN   A ND2  1 
ATOM   1016 H H    . ASN   A 1 37  ? 25.639 -1.948  5.384   1.00 10.89 ?  37  ASN   A H    1 
ATOM   1017 H HA   . ASN   A 1 37  ? 23.620 -0.237  4.845   1.00 10.66 ?  37  ASN   A HA   1 
ATOM   1018 H HB2  . ASN   A 1 37  ? 25.618 0.774   5.538   1.00 10.69 ?  37  ASN   A HB2  1 
ATOM   1019 H HB3  . ASN   A 1 37  ? 26.376 0.110   4.309   1.00 10.69 ?  37  ASN   A HB3  1 
ATOM   1020 H HD21 . ASN   A 1 37  ? 26.065 3.013   2.736   1.00 11.20 ?  37  ASN   A HD21 1 
ATOM   1021 H HD22 . ASN   A 1 37  ? 27.013 2.072   3.380   1.00 11.20 ?  37  ASN   A HD22 1 
ATOM   1022 N N    A ALA   A 1 38  ? 23.277 -0.548  2.443   0.48 9.29  ?  38  ALA   A N    1 
ATOM   1023 N N    B ALA   A 1 38  ? 23.281 -0.550  2.438   0.52 9.43  ?  38  ALA   A N    1 
ATOM   1024 C CA   A ALA   A 1 38  ? 23.066 -0.712  1.007   0.48 9.35  ?  38  ALA   A CA   1 
ATOM   1025 C CA   B ALA   A 1 38  ? 23.077 -0.743  1.003   0.52 9.64  ?  38  ALA   A CA   1 
ATOM   1026 C C    A ALA   A 1 38  ? 23.946 0.307   0.282   0.48 9.56  ?  38  ALA   A C    1 
ATOM   1027 C C    B ALA   A 1 38  ? 23.936 0.281   0.258   0.52 9.66  ?  38  ALA   A C    1 
ATOM   1028 O O    A ALA   A 1 38  ? 23.513 1.397   -0.104  0.48 9.88  ?  38  ALA   A O    1 
ATOM   1029 O O    B ALA   A 1 38  ? 23.477 1.346   -0.169  0.52 10.00 ?  38  ALA   A O    1 
ATOM   1030 C CB   A ALA   A 1 38  ? 21.589 -0.533  0.671   0.48 10.34 ?  38  ALA   A CB   1 
ATOM   1031 C CB   B ALA   A 1 38  ? 21.598 -0.621  0.657   0.52 10.84 ?  38  ALA   A CB   1 
ATOM   1032 H H    A ALA   A 1 38  ? 22.675 -0.064  2.822   0.48 11.12 ?  38  ALA   A H    1 
ATOM   1033 H H    B ALA   A 1 38  ? 22.681 -0.057  2.809   0.52 11.29 ?  38  ALA   A H    1 
ATOM   1034 H HA   A ALA   A 1 38  ? 23.339 -1.606  0.741   0.48 11.19 ?  38  ALA   A HA   1 
ATOM   1035 H HA   B ALA   A 1 38  ? 23.379 -1.633  0.757   0.52 11.55 ?  38  ALA   A HA   1 
ATOM   1036 H HB1  A ALA   A 1 38  ? 21.466 -0.669  -0.282  0.48 12.38 ?  38  ALA   A HB1  1 
ATOM   1037 H HB1  B ALA   A 1 38  ? 21.491 -0.744  -0.299  0.52 12.98 ?  38  ALA   A HB1  1 
ATOM   1038 H HB2  A ALA   A 1 38  ? 21.070 -1.187  1.167   0.48 12.38 ?  38  ALA   A HB2  1 
ATOM   1039 H HB2  B ALA   A 1 38  ? 21.103 -1.306  1.136   0.52 12.98 ?  38  ALA   A HB2  1 
ATOM   1040 H HB3  A ALA   A 1 38  ? 21.317 0.363   0.917   0.48 12.38 ?  38  ALA   A HB3  1 
ATOM   1041 H HB3  B ALA   A 1 38  ? 21.286 0.258   0.917   0.52 12.98 ?  38  ALA   A HB3  1 
ATOM   1042 N N    . ALA   A 1 39  ? 25.214 -0.056  0.113   1.00 9.29  ?  39  ALA   A N    1 
ATOM   1043 C CA   . ALA   A 1 39  ? 26.232 0.846   -0.396  1.00 9.19  ?  39  ALA   A CA   1 
ATOM   1044 C C    . ALA   A 1 39  ? 26.335 0.802   -1.917  1.00 9.19  ?  39  ALA   A C    1 
ATOM   1045 O O    . ALA   A 1 39  ? 25.834 -0.111  -2.579  1.00 9.50  ?  39  ALA   A O    1 
ATOM   1046 C CB   . ALA   A 1 39  ? 27.577 0.488   0.235   1.00 10.04 ?  39  ALA   A CB   1 
ATOM   1047 H H    A ALA   A 1 39  ? 25.510 -0.845  0.294   0.48 11.12 ?  39  ALA   A H    1 
ATOM   1048 H H    B ALA   A 1 39  ? 25.519 -0.838  0.308   0.52 11.12 ?  39  ALA   A H    1 
ATOM   1049 H HA   . ALA   A 1 39  ? 26.002 1.752   -0.137  1.00 11.00 ?  39  ALA   A HA   1 
ATOM   1050 H HB1  . ALA   A 1 39  ? 28.252 1.093   -0.103  1.00 12.02 ?  39  ALA   A HB1  1 
ATOM   1051 H HB2  . ALA   A 1 39  ? 27.503 0.581   1.201   1.00 12.02 ?  39  ALA   A HB2  1 
ATOM   1052 H HB3  . ALA   A 1 39  ? 27.799 -0.426  0.008   1.00 12.02 ?  39  ALA   A HB3  1 
ATOM   1053 N N    . ASN   A 1 40  ? 27.031 1.806   -2.466  1.00 9.49  ?  40  ASN   A N    1 
ATOM   1054 C CA   . ASN   A 1 40  ? 27.557 1.760   -3.823  1.00 10.08 ?  40  ASN   A CA   1 
ATOM   1055 C C    . ASN   A 1 40  ? 29.082 1.640   -3.772  1.00 9.48  ?  40  ASN   A C    1 
ATOM   1056 O O    . ASN   A 1 40  ? 29.696 1.736   -2.705  1.00 9.62  ?  40  ASN   A O    1 
ATOM   1057 C CB   . ASN   A 1 40  ? 27.081 2.958   -4.666  1.00 10.59 ?  40  ASN   A CB   1 
ATOM   1058 C CG   . ASN   A 1 40  ? 27.448 4.296   -4.061  1.00 11.41 ?  40  ASN   A CG   1 
ATOM   1059 O OD1  . ASN   A 1 40  ? 28.619 4.557   -3.765  1.00 12.57 ?  40  ASN   A OD1  1 
ATOM   1060 N ND2  . ASN   A 1 40  ? 26.449 5.163   -3.896  1.00 12.34 ?  40  ASN   A ND2  1 
ATOM   1061 H H    . ASN   A 1 40  ? 27.216 2.536   -2.057  1.00 11.37 ?  40  ASN   A H    1 
ATOM   1062 H HA   . ASN   A 1 40  ? 27.223 0.958   -4.255  1.00 12.07 ?  40  ASN   A HA   1 
ATOM   1063 H HB2  . ASN   A 1 40  ? 27.486 2.901   -5.549  1.00 12.69 ?  40  ASN   A HB2  1 
ATOM   1064 H HB3  . ASN   A 1 40  ? 26.117 2.917   -4.747  1.00 12.69 ?  40  ASN   A HB3  1 
ATOM   1065 H HD21 . ASN   A 1 40  ? 26.607 5.943   -3.567  1.00 14.79 ?  40  ASN   A HD21 1 
ATOM   1066 H HD22 . ASN   A 1 40  ? 25.650 4.946   -4.123  1.00 14.79 ?  40  ASN   A HD22 1 
ATOM   1067 N N    . VAL   A 1 41  ? 29.690 1.394   -4.937  1.00 10.11 ?  41  VAL   A N    1 
ATOM   1068 C CA   . VAL   A 1 41  ? 31.123 1.086   -4.970  1.00 10.82 ?  41  VAL   A CA   1 
ATOM   1069 C C    . VAL   A 1 41  ? 31.990 2.234   -4.485  1.00 10.88 ?  41  VAL   A C    1 
ATOM   1070 O O    . VAL   A 1 41  ? 33.139 2.004   -4.084  1.00 11.13 ?  41  VAL   A O    1 
ATOM   1071 C CB   . VAL   A 1 41  ? 31.611 0.617   -6.359  1.00 11.62 ?  41  VAL   A CB   1 
ATOM   1072 C CG1  . VAL   A 1 41  ? 30.926 -0.679  -6.752  1.00 11.91 ?  41  VAL   A CG1  1 
ATOM   1073 C CG2  . VAL   A 1 41  ? 31.416 1.702   -7.420  1.00 12.80 ?  41  VAL   A CG2  1 
ATOM   1074 H H    . VAL   A 1 41  ? 29.302 1.387   -5.704  1.00 12.11 ?  41  VAL   A H    1 
ATOM   1075 H HA   . VAL   A 1 41  ? 31.278 0.344   -4.360  1.00 12.96 ?  41  VAL   A HA   1 
ATOM   1076 H HB   . VAL   A 1 41  ? 32.563 0.430   -6.303  1.00 13.92 ?  41  VAL   A HB   1 
ATOM   1077 H HG11 . VAL   A 1 41  ? 31.287 -0.988  -7.596  1.00 14.26 ?  41  VAL   A HG11 1 
ATOM   1078 H HG12 . VAL   A 1 41  ? 31.086 -1.346  -6.061  1.00 14.26 ?  41  VAL   A HG12 1 
ATOM   1079 H HG13 . VAL   A 1 41  ? 29.973 -0.519  -6.837  1.00 14.26 ?  41  VAL   A HG13 1 
ATOM   1080 H HG21 . VAL   A 1 41  ? 31.652 1.338   -8.288  1.00 15.34 ?  41  VAL   A HG21 1 
ATOM   1081 H HG22 . VAL   A 1 41  ? 30.487 1.977   -7.418  1.00 15.34 ?  41  VAL   A HG22 1 
ATOM   1082 H HG23 . VAL   A 1 41  ? 31.987 2.454   -7.208  1.00 15.34 ?  41  VAL   A HG23 1 
ATOM   1083 N N    . TYR   A 1 42  ? 31.486 3.472   -4.546  1.00 10.69 ?  42  TYR   A N    1 
ATOM   1084 C CA   . TYR   A 1 42  ? 32.231 4.654   -4.131  1.00 10.39 ?  42  TYR   A CA   1 
ATOM   1085 C C    . TYR   A 1 42  ? 31.970 5.026   -2.680  1.00 10.38 ?  42  TYR   A C    1 
ATOM   1086 O O    . TYR   A 1 42  ? 32.531 6.017   -2.194  1.00 10.96 ?  42  TYR   A O    1 
ATOM   1087 C CB   . TYR   A 1 42  ? 31.902 5.847   -5.052  1.00 11.39 ?  42  TYR   A CB   1 
ATOM   1088 C CG   . TYR   A 1 42  ? 32.104 5.542   -6.522  1.00 12.52 ?  42  TYR   A CG   1 
ATOM   1089 C CD1  . TYR   A 1 42  ? 33.372 5.345   -7.045  1.00 13.16 ?  42  TYR   A CD1  1 
ATOM   1090 C CD2  . TYR   A 1 42  ? 31.022 5.419   -7.378  1.00 14.05 ?  42  TYR   A CD2  1 
ATOM   1091 C CE1  . TYR   A 1 42  ? 33.557 5.043   -8.386  1.00 13.45 ?  42  TYR   A CE1  1 
ATOM   1092 C CE2  . TYR   A 1 42  ? 31.200 5.125   -8.720  1.00 14.67 ?  42  TYR   A CE2  1 
ATOM   1093 C CZ   . TYR   A 1 42  ? 32.471 4.938   -9.220  1.00 14.52 ?  42  TYR   A CZ   1 
ATOM   1094 O OH   . TYR   A 1 42  ? 32.649 4.639   -10.553 1.00 16.15 ?  42  TYR   A OH   1 
ATOM   1095 H H    . TYR   A 1 42  ? 30.691 3.650   -4.839  1.00 12.80 ?  42  TYR   A H    1 
ATOM   1096 H HA   . TYR   A 1 42  ? 33.172 4.472   -4.223  1.00 12.45 ?  42  TYR   A HA   1 
ATOM   1097 H HB2  . TYR   A 1 42  ? 30.973 6.104   -4.924  1.00 13.64 ?  42  TYR   A HB2  1 
ATOM   1098 H HB3  . TYR   A 1 42  ? 32.481 6.593   -4.818  1.00 13.64 ?  42  TYR   A HB3  1 
ATOM   1099 H HD1  . TYR   A 1 42  ? 34.115 5.412   -6.484  1.00 15.77 ?  42  TYR   A HD1  1 
ATOM   1100 H HD2  . TYR   A 1 42  ? 30.164 5.547   -7.046  1.00 16.83 ?  42  TYR   A HD2  1 
ATOM   1101 H HE1  . TYR   A 1 42  ? 34.417 4.917   -8.723  1.00 16.12 ?  42  TYR   A HE1  1 
ATOM   1102 H HE2  . TYR   A 1 42  ? 30.464 5.052   -9.284  1.00 17.58 ?  42  TYR   A HE2  1 
ATOM   1103 H HH   . TYR   A 1 42  ? 33.468 4.545   -10.721 1.00 19.35 ?  42  TYR   A HH   1 
ATOM   1104 N N    . LEU   A 1 43  ? 31.119 4.263   -1.991  1.00 10.05 ?  43  LEU   A N    1 
ATOM   1105 C CA   . LEU   A 1 43  ? 30.681 4.593   -0.639  1.00 9.89  ?  43  LEU   A CA   1 
ATOM   1106 C C    . LEU   A 1 43  ? 30.207 6.042   -0.544  1.00 9.73  ?  43  LEU   A C    1 
ATOM   1107 O O    . LEU   A 1 43  ? 30.476 6.737   0.435   1.00 10.66 ?  43  LEU   A O    1 
ATOM   1108 C CB   . LEU   A 1 43  ? 31.742 4.283   0.415   1.00 10.14 ?  43  LEU   A CB   1 
ATOM   1109 C CG   . LEU   A 1 43  ? 32.236 2.828   0.486   1.00 10.28 ?  43  LEU   A CG   1 
ATOM   1110 C CD1  . LEU   A 1 43  ? 33.286 2.712   1.580   1.00 11.41 ?  43  LEU   A CD1  1 
ATOM   1111 C CD2  . LEU   A 1 43  ? 31.100 1.840   0.717   1.00 10.69 ?  43  LEU   A CD2  1 
ATOM   1112 H H    . LEU   A 1 43  ? 30.776 3.528   -2.290  1.00 12.04 ?  43  LEU   A H    1 
ATOM   1113 H HA   . LEU   A 1 43  ? 29.911 4.035   -0.434  1.00 11.85 ?  43  LEU   A HA   1 
ATOM   1114 H HB2  . LEU   A 1 43  ? 32.512 4.847   0.244   1.00 12.14 ?  43  LEU   A HB2  1 
ATOM   1115 H HB3  . LEU   A 1 43  ? 31.372 4.502   1.286   1.00 12.14 ?  43  LEU   A HB3  1 
ATOM   1116 H HG   . LEU   A 1 43  ? 32.668 2.606   -0.353  1.00 12.31 ?  43  LEU   A HG   1 
ATOM   1117 H HD11 . LEU   A 1 43  ? 33.600 1.796   1.621   1.00 13.67 ?  43  LEU   A HD11 1 
ATOM   1118 H HD12 . LEU   A 1 43  ? 34.028 3.307   1.375   1.00 13.67 ?  43  LEU   A HD12 1 
ATOM   1119 H HD13 . LEU   A 1 43  ? 32.888 2.965   2.428   1.00 13.67 ?  43  LEU   A HD13 1 
ATOM   1120 H HD21 . LEU   A 1 43  ? 31.481 0.957   0.844   1.00 12.80 ?  43  LEU   A HD21 1 
ATOM   1121 H HD22 . LEU   A 1 43  ? 30.611 2.110   1.507   1.00 12.80 ?  43  LEU   A HD22 1 
ATOM   1122 H HD23 . LEU   A 1 43  ? 30.523 1.847   -0.058  1.00 12.80 ?  43  LEU   A HD23 1 
ATOM   1123 N N    . LYS   A 1 44  ? 29.473 6.484   -1.568  1.00 9.97  ?  44  LYS   A N    1 
ATOM   1124 C CA   . LYS   A 1 44  ? 28.823 7.794   -1.559  1.00 10.56 ?  44  LYS   A CA   1 
ATOM   1125 C C    . LYS   A 1 44  ? 27.404 7.592   -1.040  1.00 9.93  ?  44  LYS   A C    1 
ATOM   1126 O O    . LYS   A 1 44  ? 26.539 7.065   -1.743  1.00 10.78 ?  44  LYS   A O    1 
ATOM   1127 C CB   . LYS   A 1 44  ? 28.850 8.423   -2.947  1.00 12.61 ?  44  LYS   A CB   1 
ATOM   1128 C CG   . LYS   A 1 44  ? 30.229 8.882   -3.386  1.00 16.02 ?  44  LYS   A CG   1 
ATOM   1129 C CD   . LYS   A 1 44  ? 30.913 9.765   -2.343  1.00 21.60 ?  44  LYS   A CD   1 
ATOM   1130 C CE   . LYS   A 1 44  ? 32.218 10.330  -2.870  1.00 24.79 ?  44  LYS   A CE   1 
ATOM   1131 N NZ   . LYS   A 1 44  ? 33.087 10.853  -1.780  1.00 26.66 ?  44  LYS   A NZ   1 
ATOM   1132 H H    . LYS   A 1 44  ? 29.332 6.034   -2.290  1.00 11.95 ?  44  LYS   A H    1 
ATOM   1133 H HA   . LYS   A 1 44  ? 29.277 8.376   -0.933  1.00 12.65 ?  44  LYS   A HA   1 
ATOM   1134 H HB2  . LYS   A 1 44  ? 28.542 7.771   -3.596  1.00 15.11 ?  44  LYS   A HB2  1 
ATOM   1135 H HB3  . LYS   A 1 44  ? 28.270 9.198   -2.957  1.00 15.11 ?  44  LYS   A HB3  1 
ATOM   1136 H HG2  . LYS   A 1 44  ? 30.791 8.105   -3.539  1.00 19.21 ?  44  LYS   A HG2  1 
ATOM   1137 H HG3  . LYS   A 1 44  ? 30.148 9.398   -4.205  1.00 19.21 ?  44  LYS   A HG3  1 
ATOM   1138 H HD2  . LYS   A 1 44  ? 30.321 10.495  -2.107  1.00 25.89 ?  44  LYS   A HD2  1 
ATOM   1139 H HD3  . LYS   A 1 44  ? 31.116 9.228   -1.557  1.00 25.89 ?  44  LYS   A HD3  1 
ATOM   1140 H HE2  . LYS   A 1 44  ? 32.703 9.628   -3.332  1.00 29.72 ?  44  LYS   A HE2  1 
ATOM   1141 H HE3  . LYS   A 1 44  ? 32.022 11.057  -3.479  1.00 29.72 ?  44  LYS   A HE3  1 
ATOM   1142 H HZ1  . LYS   A 1 44  ? 33.840 11.178  -2.123  1.00 31.96 ?  44  LYS   A HZ1  1 
ATOM   1143 H HZ2  . LYS   A 1 44  ? 32.663 11.504  -1.342  1.00 31.96 ?  44  LYS   A HZ2  1 
ATOM   1144 H HZ3  . LYS   A 1 44  ? 33.284 10.202  -1.208  1.00 31.96 ?  44  LYS   A HZ3  1 
ATOM   1145 N N    A HIS   A 1 45  ? 27.172 8.001   0.203   0.48 9.39  ?  45  HIS   A N    1 
ATOM   1146 N N    B HIS   A 1 45  ? 27.172 7.974   0.212   0.52 9.98  ?  45  HIS   A N    1 
ATOM   1147 C CA   A HIS   A 1 45  ? 25.950 7.649   0.923   0.48 9.20  ?  45  HIS   A CA   1 
ATOM   1148 C CA   B HIS   A 1 45  ? 25.923 7.651   0.900   0.52 10.31 ?  45  HIS   A CA   1 
ATOM   1149 C C    A HIS   A 1 45  ? 24.914 8.768   0.792   0.48 10.00 ?  45  HIS   A C    1 
ATOM   1150 C C    B HIS   A 1 45  ? 24.926 8.778   0.664   0.52 11.32 ?  45  HIS   A C    1 
ATOM   1151 O O    A HIS   A 1 45  ? 24.529 9.425   1.759   0.48 10.08 ?  45  HIS   A O    1 
ATOM   1152 O O    B HIS   A 1 45  ? 24.782 9.690   1.478   0.52 12.53 ?  45  HIS   A O    1 
ATOM   1153 C CB   A HIS   A 1 45  ? 26.285 7.355   2.378   0.48 9.16  ?  45  HIS   A CB   1 
ATOM   1154 C CB   B HIS   A 1 45  ? 26.192 7.430   2.379   0.52 10.41 ?  45  HIS   A CB   1 
ATOM   1155 C CG   A HIS   A 1 45  ? 27.401 6.374   2.551   0.48 8.66  ?  45  HIS   A CG   1 
ATOM   1156 C CG   B HIS   A 1 45  ? 27.321 6.486   2.646   0.52 9.65  ?  45  HIS   A CG   1 
ATOM   1157 N ND1  A HIS   A 1 45  ? 27.355 5.093   2.041   0.48 9.01  ?  45  HIS   A ND1  1 
ATOM   1158 N ND1  B HIS   A 1 45  ? 27.340 5.193   2.168   0.52 10.17 ?  45  HIS   A ND1  1 
ATOM   1159 C CD2  A HIS   A 1 45  ? 28.596 6.494   3.176   0.48 9.52  ?  45  HIS   A CD2  1 
ATOM   1160 C CD2  B HIS   A 1 45  ? 28.476 6.657   3.331   0.52 9.27  ?  45  HIS   A CD2  1 
ATOM   1161 C CE1  A HIS   A 1 45  ? 28.479 4.468   2.350   0.48 9.31  ?  45  HIS   A CE1  1 
ATOM   1162 C CE1  B HIS   A 1 45  ? 28.460 4.608   2.554   0.52 9.33  ?  45  HIS   A CE1  1 
ATOM   1163 N NE2  A HIS   A 1 45  ? 29.247 5.294   3.039   0.48 9.82  ?  45  HIS   A NE2  1 
ATOM   1164 N NE2  B HIS   A 1 45  ? 29.166 5.474   3.261   0.52 8.78  ?  45  HIS   A NE2  1 
ATOM   1165 H H    A HIS   A 1 45  ? 27.713 8.494   0.658   0.48 11.24 ?  45  HIS   A H    1 
ATOM   1166 H H    B HIS   A 1 45  ? 27.724 8.433   0.689   0.52 11.96 ?  45  HIS   A H    1 
ATOM   1167 H HA   A HIS   A 1 45  ? 25.571 6.849   0.530   0.48 11.01 ?  45  HIS   A HA   1 
ATOM   1168 H HA   B HIS   A 1 45  ? 25.549 6.841   0.524   0.52 12.35 ?  45  HIS   A HA   1 
ATOM   1169 H HB2  A HIS   A 1 45  ? 26.543 8.182   2.813   0.48 10.97 ?  45  HIS   A HB2  1 
ATOM   1170 H HB2  B HIS   A 1 45  ? 26.408 8.280   2.789   0.52 12.46 ?  45  HIS   A HB2  1 
ATOM   1171 H HB3  A HIS   A 1 45  ? 25.496 6.988   2.810   0.48 10.97 ?  45  HIS   A HB3  1 
ATOM   1172 H HB3  B HIS   A 1 45  ? 25.390 7.062   2.787   0.52 12.46 ?  45  HIS   A HB3  1 
ATOM   1173 H HD2  A HIS   A 1 45  ? 28.920 7.249   3.614   0.48 11.40 ?  45  HIS   A HD2  1 
ATOM   1174 H HD2  B HIS   A 1 45  ? 28.750 7.433   3.762   0.52 11.10 ?  45  HIS   A HD2  1 
ATOM   1175 H HE1  A HIS   A 1 45  ? 28.689 3.585   2.134   0.48 11.15 ?  45  HIS   A HE1  1 
ATOM   1176 H HE1  B HIS   A 1 45  ? 28.703 3.730   2.368   0.52 11.17 ?  45  HIS   A HE1  1 
ATOM   1177 H HE2  A HIS   A 1 45  ? 30.029 5.107   3.352   0.48 11.76 ?  45  HIS   A HE2  1 
ATOM   1178 H HE2  B HIS   A 1 45  ? 29.930 5.319   3.617   0.52 10.51 ?  45  HIS   A HE2  1 
ATOM   1179 N N    A GLY   A 1 46  ? 24.446 8.960   -0.440  0.48 10.83 ?  46  GLY   A N    1 
ATOM   1180 N N    B GLY   A 1 46  ? 24.215 8.700   -0.459  0.52 10.96 ?  46  GLY   A N    1 
ATOM   1181 C CA   A GLY   A 1 46  ? 23.626 10.116  -0.761  0.48 11.27 ?  46  GLY   A CA   1 
ATOM   1182 C CA   B GLY   A 1 46  ? 23.394 9.807   -0.913  0.52 11.29 ?  46  GLY   A CA   1 
ATOM   1183 C C    A GLY   A 1 46  ? 22.143 9.974   -0.476  0.48 11.65 ?  46  GLY   A C    1 
ATOM   1184 C C    B GLY   A 1 46  ? 21.919 9.717   -0.580  0.52 11.76 ?  46  GLY   A C    1 
ATOM   1185 O O    A GLY   A 1 46  ? 21.492 10.943  -0.071  0.48 13.06 ?  46  GLY   A O    1 
ATOM   1186 O O    B GLY   A 1 46  ? 21.276 10.746  -0.348  0.52 13.12 ?  46  GLY   A O    1 
ATOM   1187 H H    A GLY   A 1 46  ? 24.593 8.439   -1.108  0.48 12.97 ?  46  GLY   A H    1 
ATOM   1188 H H    B GLY   A 1 46  ? 24.191 8.010   -0.973  0.52 13.13 ?  46  GLY   A H    1 
ATOM   1189 H HA2  A GLY   A 1 46  ? 23.955 10.881  -0.258  0.48 13.50 ?  46  GLY   A HA2  1 
ATOM   1190 H HA2  B GLY   A 1 46  ? 23.726 10.628  -0.522  0.52 13.52 ?  46  GLY   A HA2  1 
ATOM   1191 H HA3  A GLY   A 1 46  ? 23.731 10.321  -1.705  0.48 13.50 ?  46  GLY   A HA3  1 
ATOM   1192 H HA3  B GLY   A 1 46  ? 23.470 9.880   -1.875  0.52 13.52 ?  46  GLY   A HA3  1 
ATOM   1193 N N    A GLY   A 1 47  ? 21.591 8.783   -0.694  0.48 10.90 ?  47  GLY   A N    1 
ATOM   1194 N N    B GLY   A 1 47  ? 21.358 8.512   -0.575  0.52 11.70 ?  47  GLY   A N    1 
ATOM   1195 C CA   A GLY   A 1 47  ? 20.161 8.571   -0.625  0.48 11.20 ?  47  GLY   A CA   1 
ATOM   1196 C CA   B GLY   A 1 47  ? 19.934 8.369   -0.342  0.52 11.68 ?  47  GLY   A CA   1 
ATOM   1197 C C    A GLY   A 1 47  ? 19.841 7.130   -0.287  0.48 10.63 ?  47  GLY   A C    1 
ATOM   1198 C C    B GLY   A 1 47  ? 19.604 6.979   0.149   0.52 10.59 ?  47  GLY   A C    1 
ATOM   1199 O O    A GLY   A 1 47  ? 20.732 6.304   -0.080  0.48 10.58 ?  47  GLY   A O    1 
ATOM   1200 O O    B GLY   A 1 47  ? 20.487 6.142   0.348   0.52 10.31 ?  47  GLY   A O    1 
ATOM   1201 H H    A GLY   A 1 47  ? 22.040 8.080   -0.878  0.48 13.06 ?  47  GLY   A H    1 
ATOM   1202 H H    B GLY   A 1 47  ? 21.774 7.764   -0.705  0.52 14.01 ?  47  GLY   A H    1 
ATOM   1203 H HA2  A GLY   A 1 47  ? 19.775 9.151   0.054   0.48 13.41 ?  47  GLY   A HA2  1 
ATOM   1204 H HA2  B GLY   A 1 47  ? 19.644 9.007   0.326   0.52 13.99 ?  47  GLY   A HA2  1 
ATOM   1205 H HA3  A GLY   A 1 47  ? 19.760 8.789   -1.482  0.48 13.41 ?  47  GLY   A HA3  1 
ATOM   1206 H HA3  B GLY   A 1 47  ? 19.446 8.531   -1.164  0.52 13.99 ?  47  GLY   A HA3  1 
ATOM   1207 N N    A GLY   A 1 48  ? 18.549 6.827   -0.243  0.48 10.60 ?  48  GLY   A N    1 
ATOM   1208 N N    B GLY   A 1 48  ? 18.306 6.744   0.348   0.52 10.40 ?  48  GLY   A N    1 
ATOM   1209 C CA   A GLY   A 1 48  ? 18.123 5.498   0.141   0.48 10.18 ?  48  GLY   A CA   1 
ATOM   1210 C CA   B GLY   A 1 48  ? 17.858 5.439   0.798   0.52 9.62  ?  48  GLY   A CA   1 
ATOM   1211 C C    A GLY   A 1 48  ? 18.575 5.150   1.547   0.48 9.63  ?  48  GLY   A C    1 
ATOM   1212 C C    B GLY   A 1 48  ? 18.472 5.064   2.132   0.52 9.67  ?  48  GLY   A C    1 
ATOM   1213 O O    A GLY   A 1 48  ? 18.735 6.015   2.418   0.48 9.90  ?  48  GLY   A O    1 
ATOM   1214 O O    B GLY   A 1 48  ? 18.676 5.905   3.017   0.52 9.86  ?  48  GLY   A O    1 
ATOM   1215 H H    A GLY   A 1 48  ? 17.916 7.370   -0.428  0.48 12.70 ?  48  GLY   A H    1 
ATOM   1216 H H    B GLY   A 1 48  ? 17.667 7.318   0.235   0.52 12.46 ?  48  GLY   A H    1 
ATOM   1217 H HA2  A GLY   A 1 48  ? 17.158 5.444   0.102   0.48 12.20 ?  48  GLY   A HA2  1 
ATOM   1218 H HA2  B GLY   A 1 48  ? 16.885 5.433   0.883   0.52 11.52 ?  48  GLY   A HA2  1 
ATOM   1219 H HA3  A GLY   A 1 48  ? 18.499 4.844   -0.469  0.48 12.20 ?  48  GLY   A HA3  1 
ATOM   1220 H HA3  B GLY   A 1 48  ? 18.106 4.765   0.146   0.52 11.52 ?  48  GLY   A HA3  1 
ATOM   1221 N N    A VAL   A 1 49  ? 18.790 3.851   1.770   0.48 9.75  ?  49  VAL   A N    1 
ATOM   1222 N N    B VAL   A 1 49  ? 18.763 3.771   2.280   0.52 8.42  ?  49  VAL   A N    1 
ATOM   1223 C CA   A VAL   A 1 49  ? 19.281 3.377   3.062   0.48 10.11 ?  49  VAL   A CA   1 
ATOM   1224 C CA   B VAL   A 1 49  ? 19.364 3.262   3.510   0.52 8.59  ?  49  VAL   A CA   1 
ATOM   1225 C C    A VAL   A 1 49  ? 20.591 4.067   3.417   0.48 9.43  ?  49  VAL   A C    1 
ATOM   1226 C C    B VAL   A 1 49  ? 20.662 3.996   3.817   0.52 8.77  ?  49  VAL   A C    1 
ATOM   1227 O O    A VAL   A 1 49  ? 20.801 4.486   4.558   0.48 9.63  ?  49  VAL   A O    1 
ATOM   1228 O O    B VAL   A 1 49  ? 20.914 4.391   4.960   0.52 9.20  ?  49  VAL   A O    1 
ATOM   1229 C CB   A VAL   A 1 49  ? 19.455 1.847   3.037   0.48 10.30 ?  49  VAL   A CB   1 
ATOM   1230 C CB   B VAL   A 1 49  ? 19.600 1.745   3.391   0.52 9.36  ?  49  VAL   A CB   1 
ATOM   1231 C CG1  A VAL   A 1 49  ? 20.213 1.379   4.272   0.48 10.70 ?  49  VAL   A CG1  1 
ATOM   1232 C CG1  B VAL   A 1 49  ? 20.510 1.260   4.510   0.52 9.75  ?  49  VAL   A CG1  1 
ATOM   1233 C CG2  A VAL   A 1 49  ? 18.107 1.153   2.936   0.48 10.67 ?  49  VAL   A CG2  1 
ATOM   1234 C CG2  B VAL   A 1 49  ? 18.283 0.993   3.398   0.52 10.44 ?  49  VAL   A CG2  1 
ATOM   1235 H H    A VAL   A 1 49  ? 18.660 3.226   1.196   0.48 11.67 ?  49  VAL   A H    1 
ATOM   1236 H H    B VAL   A 1 49  ? 18.619 3.169   1.684   0.52 10.08 ?  49  VAL   A H    1 
ATOM   1237 H HA   A VAL   A 1 49  ? 18.630 3.589   3.751   0.48 12.11 ?  49  VAL   A HA   1 
ATOM   1238 H HA   B VAL   A 1 49  ? 18.757 3.409   4.250   0.52 10.28 ?  49  VAL   A HA   1 
ATOM   1239 H HB   A VAL   A 1 49  ? 19.981 1.601   2.260   0.48 12.34 ?  49  VAL   A HB   1 
ATOM   1240 H HB   B VAL   A 1 49  ? 20.045 1.558   2.548   0.52 11.20 ?  49  VAL   A HB   1 
ATOM   1241 H HG11 A VAL   A 1 49  ? 20.059 0.428   4.394   0.48 12.81 ?  49  VAL   A HG11 1 
ATOM   1242 H HG11 B VAL   A 1 49  ? 20.401 0.302   4.607   0.52 11.68 ?  49  VAL   A HG11 1 
ATOM   1243 H HG12 A VAL   A 1 49  ? 21.160 1.546   4.154   0.48 12.81 ?  49  VAL   A HG12 1 
ATOM   1244 H HG12 B VAL   A 1 49  ? 21.429 1.468   4.286   0.52 11.68 ?  49  VAL   A HG12 1 
ATOM   1245 H HG13 A VAL   A 1 49  ? 19.883 1.863   5.048   0.48 12.81 ?  49  VAL   A HG13 1 
ATOM   1246 H HG13 B VAL   A 1 49  ? 20.256 1.705   5.334   0.52 11.68 ?  49  VAL   A HG13 1 
ATOM   1247 H HG21 A VAL   A 1 49  ? 18.248 0.192   2.919   0.48 12.78 ?  49  VAL   A HG21 1 
ATOM   1248 H HG21 B VAL   A 1 49  ? 18.460 0.044   3.305   0.52 12.50 ?  49  VAL   A HG21 1 
ATOM   1249 H HG22 A VAL   A 1 49  ? 17.571 1.394   3.708   0.48 12.78 ?  49  VAL   A HG22 1 
ATOM   1250 H HG22 B VAL   A 1 49  ? 17.828 1.165   4.237   0.52 12.50 ?  49  VAL   A HG22 1 
ATOM   1251 H HG23 A VAL   A 1 49  ? 17.668 1.439   2.123   0.48 12.78 ?  49  VAL   A HG23 1 
ATOM   1252 H HG23 B VAL   A 1 49  ? 17.741 1.303   2.656   0.52 12.50 ?  49  VAL   A HG23 1 
ATOM   1253 N N    A ALA   A 1 50  ? 21.506 4.153   2.451   0.48 9.47  ?  50  ALA   A N    1 
ATOM   1254 N N    B ALA   A 1 50  ? 21.530 4.134   2.811   0.52 8.85  ?  50  ALA   A N    1 
ATOM   1255 C CA   A ALA   A 1 50  ? 22.830 4.709   2.715   0.48 9.60  ?  50  ALA   A CA   1 
ATOM   1256 C CA   B ALA   A 1 50  ? 22.854 4.701   3.050   0.52 8.43  ?  50  ALA   A CA   1 
ATOM   1257 C C    A ALA   A 1 50  ? 22.742 6.166   3.144   0.48 9.08  ?  50  ALA   A C    1 
ATOM   1258 C C    B ALA   A 1 50  ? 22.756 6.148   3.508   0.52 8.44  ?  50  ALA   A C    1 
ATOM   1259 O O    A ALA   A 1 50  ? 23.394 6.583   4.106   0.48 8.96  ?  50  ALA   A O    1 
ATOM   1260 O O    B ALA   A 1 50  ? 23.401 6.548   4.482   0.52 8.70  ?  50  ALA   A O    1 
ATOM   1261 C CB   A ALA   A 1 50  ? 23.696 4.580   1.464   0.48 9.76  ?  50  ALA   A CB   1 
ATOM   1262 C CB   B ALA   A 1 50  ? 23.709 4.582   1.787   0.52 8.52  ?  50  ALA   A CB   1 
ATOM   1263 H H    A ALA   A 1 50  ? 21.385 3.889   1.648   0.48 11.34 ?  50  ALA   A H    1 
ATOM   1264 H H    B ALA   A 1 50  ? 21.376 3.913   1.993   0.52 10.59 ?  50  ALA   A H    1 
ATOM   1265 H HA   A ALA   A 1 50  ? 23.251 4.214   3.434   0.48 11.50 ?  50  ALA   A HA   1 
ATOM   1266 H HA   B ALA   A 1 50  ? 23.291 4.206   3.753   0.52 10.10 ?  50  ALA   A HA   1 
ATOM   1267 H HB1  A ALA   A 1 50  ? 24.569 4.956   1.647   0.48 11.69 ?  50  ALA   A HB1  1 
ATOM   1268 H HB1  B ALA   A 1 50  ? 24.583 4.964   1.958   0.52 10.20 ?  50  ALA   A HB1  1 
ATOM   1269 H HB2  A ALA   A 1 50  ? 23.775 3.642   1.236   0.48 11.69 ?  50  ALA   A HB2  1 
ATOM   1270 H HB2  B ALA   A 1 50  ? 23.798 3.643   1.555   0.52 10.20 ?  50  ALA   A HB2  1 
ATOM   1271 H HB3  A ALA   A 1 50  ? 23.270 5.064   0.739   0.48 11.69 ?  50  ALA   A HB3  1 
ATOM   1272 H HB3  B ALA   A 1 50  ? 23.275 5.060   1.062   0.52 10.20 ?  50  ALA   A HB3  1 
ATOM   1273 N N    A GLY   A 1 51  ? 21.958 6.966   2.425   0.48 9.34  ?  51  GLY   A N    1 
ATOM   1274 N N    B GLY   A 1 51  ? 21.943 6.950   2.818   0.52 9.23  ?  51  GLY   A N    1 
ATOM   1275 C CA   A GLY   A 1 51  ? 21.813 8.361   2.802   0.48 8.96  ?  51  GLY   A CA   1 
ATOM   1276 C CA   B GLY   A 1 51  ? 21.754 8.326   3.244   0.52 9.66  ?  51  GLY   A CA   1 
ATOM   1277 C C    A GLY   A 1 51  ? 21.217 8.532   4.185   0.48 8.43  ?  51  GLY   A C    1 
ATOM   1278 C C    B GLY   A 1 51  ? 21.168 8.416   4.639   0.52 9.83  ?  51  GLY   A C    1 
ATOM   1279 O O    A GLY   A 1 51  ? 21.615 9.425   4.937   0.48 8.65  ?  51  GLY   A O    1 
ATOM   1280 O O    B GLY   A 1 51  ? 21.551 9.281   5.432   0.52 10.25 ?  51  GLY   A O    1 
ATOM   1281 H H    A GLY   A 1 51  ? 21.513 6.731   1.730   0.48 11.18 ?  51  GLY   A H    1 
ATOM   1282 H H    B GLY   A 1 51  ? 21.496 6.722   2.113   0.52 11.06 ?  51  GLY   A H    1 
ATOM   1283 H HA2  A GLY   A 1 51  ? 22.679 8.791   2.801   0.48 10.73 ?  51  GLY   A HA2  1 
ATOM   1284 H HA2  B GLY   A 1 51  ? 22.607 8.786   3.234   0.52 11.57 ?  51  GLY   A HA2  1 
ATOM   1285 H HA3  A GLY   A 1 51  ? 21.242 8.815   2.163   0.48 10.73 ?  51  GLY   A HA3  1 
ATOM   1286 H HA3  B GLY   A 1 51  ? 21.154 8.776   2.623   0.52 11.57 ?  51  GLY   A HA3  1 
ATOM   1287 N N    A ALA   A 1 52  ? 20.246 7.684   4.535   0.48 8.62  ?  52  ALA   A N    1 
ATOM   1288 N N    B ALA   A 1 52  ? 20.231 7.517   4.955   0.52 9.95  ?  52  ALA   A N    1 
ATOM   1289 C CA   A ALA   A 1 52  ? 19.600 7.796   5.839   0.48 8.91  ?  52  ALA   A CA   1 
ATOM   1290 C CA   B ALA   A 1 52  ? 19.609 7.514   6.275   0.52 9.94  ?  52  ALA   A CA   1 
ATOM   1291 C C    A ALA   A 1 52  ? 20.535 7.364   6.967   0.48 9.19  ?  52  ALA   A C    1 
ATOM   1292 C C    B ALA   A 1 52  ? 20.608 7.113   7.356   0.52 9.41  ?  52  ALA   A C    1 
ATOM   1293 O O    A ALA   A 1 52  ? 20.618 8.036   8.000   0.48 9.94  ?  52  ALA   A O    1 
ATOM   1294 O O    B ALA   A 1 52  ? 20.696 7.763   8.406   0.52 9.93  ?  52  ALA   A O    1 
ATOM   1295 C CB   A ALA   A 1 52  ? 18.302 6.985   5.856   0.48 9.46  ?  52  ALA   A CB   1 
ATOM   1296 C CB   B ALA   A 1 52  ? 18.397 6.580   6.276   0.52 10.90 ?  52  ALA   A CB   1 
ATOM   1297 H H    A ALA   A 1 52  ? 19.953 7.041   4.042   0.48 10.32 ?  52  ALA   A H    1 
ATOM   1298 H H    B ALA   A 1 52  ? 19.950 6.894   4.421   0.52 11.91 ?  52  ALA   A H    1 
ATOM   1299 H HA   A ALA   A 1 52  ? 19.360 8.722   5.985   0.48 10.67 ?  52  ALA   A HA   1 
ATOM   1300 H HA   B ALA   A 1 52  ? 19.298 8.404   6.470   0.52 11.91 ?  52  ALA   A HA   1 
ATOM   1301 H HB1  A ALA   A 1 52  ? 17.883 7.071   6.728   0.48 11.33 ?  52  ALA   A HB1  1 
ATOM   1302 H HB1  B ALA   A 1 52  ? 17.990 6.594   7.157   0.52 13.06 ?  52  ALA   A HB1  1 
ATOM   1303 H HB2  A ALA   A 1 52  ? 17.703 7.325   5.170   0.48 11.33 ?  52  ALA   A HB2  1 
ATOM   1304 H HB2  B ALA   A 1 52  ? 17.756 6.890   5.613   0.52 13.06 ?  52  ALA   A HB2  1 
ATOM   1305 H HB3  A ALA   A 1 52  ? 18.505 6.052   5.680   0.48 11.33 ?  52  ALA   A HB3  1 
ATOM   1306 H HB3  B ALA   A 1 52  ? 18.684 5.679   6.058   0.52 13.06 ?  52  ALA   A HB3  1 
ATOM   1307 N N    A LEU   A 1 53  ? 21.239 6.243   6.797   0.48 9.41  ?  53  LEU   A N    1 
ATOM   1308 N N    B LEU   A 1 53  ? 21.354 6.027   7.132   0.52 9.24  ?  53  LEU   A N    1 
ATOM   1309 C CA   A LEU   A 1 53  ? 22.184 5.808   7.823   0.48 9.74  ?  53  LEU   A CA   1 
ATOM   1310 C CA   B LEU   A 1 53  ? 22.381 5.638   8.095   0.52 8.99  ?  53  LEU   A CA   1 
ATOM   1311 C C    A LEU   A 1 53  ? 23.265 6.858   8.040   0.48 9.67  ?  53  LEU   A C    1 
ATOM   1312 C C    B LEU   A 1 53  ? 23.401 6.752   8.273   0.52 9.61  ?  53  LEU   A C    1 
ATOM   1313 O O    A LEU   A 1 53  ? 23.593 7.206   9.179   0.48 10.18 ?  53  LEU   A O    1 
ATOM   1314 O O    B LEU   A 1 53  ? 23.758 7.116   9.400   0.52 10.78 ?  53  LEU   A O    1 
ATOM   1315 C CB   A LEU   A 1 53  ? 22.812 4.467   7.435   0.48 10.70 ?  53  LEU   A CB   1 
ATOM   1316 C CB   B LEU   A 1 53  ? 23.085 4.357   7.639   0.52 8.73  ?  53  LEU   A CB   1 
ATOM   1317 C CG   A LEU   A 1 53  ? 21.941 3.208   7.532   0.48 10.74 ?  53  LEU   A CG   1 
ATOM   1318 C CG   B LEU   A 1 53  ? 22.311 3.045   7.756   0.52 9.56  ?  53  LEU   A CG   1 
ATOM   1319 C CD1  A LEU   A 1 53  ? 22.667 2.020   6.919   0.48 10.90 ?  53  LEU   A CD1  1 
ATOM   1320 C CD1  B LEU   A 1 53  ? 23.076 1.937   7.039   0.52 10.02 ?  53  LEU   A CD1  1 
ATOM   1321 C CD2  A LEU   A 1 53  ? 21.569 2.905   8.974   0.48 11.30 ?  53  LEU   A CD2  1 
ATOM   1322 C CD2  B LEU   A 1 53  ? 22.073 2.664   9.206   0.52 10.30 ?  53  LEU   A CD2  1 
ATOM   1323 H H    A LEU   A 1 53  ? 21.183 5.729   6.116   0.48 11.27 ?  53  LEU   A H    1 
ATOM   1324 H H    B LEU   A 1 53  ? 21.284 5.503   6.445   0.52 11.07 ?  53  LEU   A H    1 
ATOM   1325 H HA   A LEU   A 1 53  ? 21.710 5.694   8.663   0.48 11.67 ?  53  LEU   A HA   1 
ATOM   1326 H HA   B LEU   A 1 53  ? 21.963 5.464   8.953   0.52 10.76 ?  53  LEU   A HA   1 
ATOM   1327 H HB2  A LEU   A 1 53  ? 23.107 4.537   6.516   0.48 12.82 ?  53  LEU   A HB2  1 
ATOM   1328 H HB2  B LEU   A 1 53  ? 23.327 4.462   6.707   0.52 10.46 ?  53  LEU   A HB2  1 
ATOM   1329 H HB3  A LEU   A 1 53  ? 23.578 4.323   8.008   0.48 12.82 ?  53  LEU   A HB3  1 
ATOM   1330 H HB3  B LEU   A 1 53  ? 23.893 4.256   8.168   0.52 10.46 ?  53  LEU   A HB3  1 
ATOM   1331 H HG   A LEU   A 1 53  ? 21.120 3.346   7.030   0.48 12.87 ?  53  LEU   A HG   1 
ATOM   1332 H HG   B LEU   A 1 53  ? 21.452 3.139   7.320   0.52 11.45 ?  53  LEU   A HG   1 
ATOM   1333 H HD11 A LEU   A 1 53  ? 22.104 1.234   6.989   0.48 13.05 ?  53  LEU   A HD11 1 
ATOM   1334 H HD11 B LEU   A 1 53  ? 22.581 1.105   7.122   0.52 12.00 ?  53  LEU   A HD11 1 
ATOM   1335 H HD12 A LEU   A 1 53  ? 22.856 2.211   5.987   0.48 13.05 ?  53  LEU   A HD12 1 
ATOM   1336 H HD12 B LEU   A 1 53  ? 23.173 2.172   6.103   0.52 12.00 ?  53  LEU   A HD12 1 
ATOM   1337 H HD13 A LEU   A 1 53  ? 23.497 1.877   7.402   0.48 13.05 ?  53  LEU   A HD13 1 
ATOM   1338 H HD13 B LEU   A 1 53  ? 23.951 1.841   7.448   0.52 12.00 ?  53  LEU   A HD13 1 
ATOM   1339 H HD21 A LEU   A 1 53  ? 21.014 2.111   8.996   0.48 13.53 ?  53  LEU   A HD21 1 
ATOM   1340 H HD21 B LEU   A 1 53  ? 21.580 1.831   9.238   0.52 12.34 ?  53  LEU   A HD21 1 
ATOM   1341 H HD22 A LEU   A 1 53  ? 22.383 2.754   9.481   0.48 13.53 ?  53  LEU   A HD22 1 
ATOM   1342 H HD22 B LEU   A 1 53  ? 22.929 2.561   9.650   0.52 12.34 ?  53  LEU   A HD22 1 
ATOM   1343 H HD23 A LEU   A 1 53  ? 21.085 3.659   9.341   0.48 13.53 ?  53  LEU   A HD23 1 
ATOM   1344 H HD23 B LEU   A 1 53  ? 21.562 3.369   9.635   0.52 12.34 ?  53  LEU   A HD23 1 
ATOM   1345 N N    A ASN   A 1 54  ? 23.817 7.394   6.952   0.48 9.24  ?  54  ASN   A N    1 
ATOM   1346 N N    B ASN   A 1 54  ? 23.890 7.303   7.163   0.52 9.64  ?  54  ASN   A N    1 
ATOM   1347 C CA   A ASN   A 1 54  ? 24.880 8.380   7.097   0.48 9.52  ?  54  ASN   A CA   1 
ATOM   1348 C CA   B ASN   A 1 54  ? 24.929 8.318   7.263   0.52 9.92  ?  54  ASN   A CA   1 
ATOM   1349 C C    A ASN   A 1 54  ? 24.376 9.631   7.806   0.48 10.27 ?  54  ASN   A C    1 
ATOM   1350 C C    B ASN   A 1 54  ? 24.425 9.548   8.009   0.52 10.28 ?  54  ASN   A C    1 
ATOM   1351 O O    A ASN   A 1 54  ? 25.104 10.241  8.600   0.48 10.55 ?  54  ASN   A O    1 
ATOM   1352 O O    B ASN   A 1 54  ? 25.087 10.054  8.927   0.52 9.42  ?  54  ASN   A O    1 
ATOM   1353 C CB   A ASN   A 1 54  ? 25.469 8.728   5.736   0.48 9.72  ?  54  ASN   A CB   1 
ATOM   1354 C CB   B ASN   A 1 54  ? 25.436 8.704   5.880   0.52 9.98  ?  54  ASN   A CB   1 
ATOM   1355 C CG   A ASN   A 1 54  ? 26.490 9.829   5.833   0.48 10.27 ?  54  ASN   A CG   1 
ATOM   1356 C CG   B ASN   A 1 54  ? 26.453 9.806   5.959   0.52 9.91  ?  54  ASN   A CG   1 
ATOM   1357 O OD1  A ASN   A 1 54  ? 27.481 9.698   6.554   0.48 10.52 ?  54  ASN   A OD1  1 
ATOM   1358 O OD1  B ASN   A 1 54  ? 27.484 9.642   6.615   0.52 9.71  ?  54  ASN   A OD1  1 
ATOM   1359 N ND2  A ASN   A 1 54  ? 26.259 10.927  5.128   0.48 11.11 ?  54  ASN   A ND2  1 
ATOM   1360 N ND2  B ASN   A 1 54  ? 26.163 10.951  5.344   0.52 10.67 ?  54  ASN   A ND2  1 
ATOM   1361 H H    A ASN   A 1 54  ? 23.593 7.216   6.144   0.48 11.06 ?  54  ASN   A H    1 
ATOM   1362 H H    B ASN   A 1 54  ? 23.642 7.103   6.359   0.52 11.54 ?  54  ASN   A H    1 
ATOM   1363 H HA   A ASN   A 1 54  ? 25.582 8.006   7.645   0.48 11.40 ?  54  ASN   A HA   1 
ATOM   1364 H HA   B ASN   A 1 54  ? 25.672 7.948   7.757   0.52 11.88 ?  54  ASN   A HA   1 
ATOM   1365 H HB2  A ASN   A 1 54  ? 25.903 7.934   5.376   0.48 11.64 ?  54  ASN   A HB2  1 
ATOM   1366 H HB2  B ASN   A 1 54  ? 25.855 7.929   5.463   0.52 11.96 ?  54  ASN   A HB2  1 
ATOM   1367 H HB3  A ASN   A 1 54  ? 24.759 9.017   5.146   0.48 11.64 ?  54  ASN   A HB3  1 
ATOM   1368 H HB3  B ASN   A 1 54  ? 24.692 9.008   5.335   0.52 11.96 ?  54  ASN   A HB3  1 
ATOM   1369 H HD21 A ASN   A 1 54  ? 26.817 11.577  5.161   0.48 13.30 ?  54  ASN   A HD21 1 
ATOM   1370 H HD21 B ASN   A 1 54  ? 26.718 11.608  5.371   0.52 12.79 ?  54  ASN   A HD21 1 
ATOM   1371 H HD22 A ASN   A 1 54  ? 25.554 10.982  4.641   0.48 13.30 ?  54  ASN   A HD22 1 
ATOM   1372 H HD22 B ASN   A 1 54  ? 25.426 11.030  4.905   0.52 12.79 ?  54  ASN   A HD22 1 
ATOM   1373 N N    A LYS   A 1 55  ? 23.127 10.022  7.541   0.48 10.40 ?  55  LYS   A N    1 
ATOM   1374 N N    B LYS   A 1 55  ? 23.246 10.045  7.623   0.52 11.11 ?  55  LYS   A N    1 
ATOM   1375 C CA   A LYS   A 1 55  ? 22.548 11.173  8.225   0.48 10.86 ?  55  LYS   A CA   1 
ATOM   1376 C CA   B LYS   A 1 55  ? 22.685 11.215  8.286   0.52 12.69 ?  55  LYS   A CA   1 
ATOM   1377 C C    A LYS   A 1 55  ? 22.521 10.949  9.732   0.48 11.26 ?  55  LYS   A C    1 
ATOM   1378 C C    B LYS   A 1 55  ? 22.533 10.963  9.779   0.52 12.31 ?  55  LYS   A C    1 
ATOM   1379 O O    A LYS   A 1 55  ? 22.855 11.851  10.510  0.48 11.67 ?  55  LYS   A O    1 
ATOM   1380 O O    B LYS   A 1 55  ? 22.789 11.856  10.596  0.52 12.87 ?  55  LYS   A O    1 
ATOM   1381 C CB   A LYS   A 1 55  ? 21.143 11.428  7.674   0.48 11.25 ?  55  LYS   A CB   1 
ATOM   1382 C CB   B LYS   A 1 55  ? 21.348 11.583  7.635   0.52 15.18 ?  55  LYS   A CB   1 
ATOM   1383 C CG   A LYS   A 1 55  ? 20.403 12.599  8.294   0.48 11.43 ?  55  LYS   A CG   1 
ATOM   1384 C CG   B LYS   A 1 55  ? 20.811 12.965  7.983   0.52 18.09 ?  55  LYS   A CG   1 
ATOM   1385 C CD   A LYS   A 1 55  ? 19.138 12.928  7.487   0.48 11.79 ?  55  LYS   A CD   1 
ATOM   1386 C CD   B LYS   A 1 55  ? 19.857 13.464  6.896   0.52 20.81 ?  55  LYS   A CD   1 
ATOM   1387 C CE   A LYS   A 1 55  ? 18.282 13.994  8.156   0.48 12.81 ?  55  LYS   A CE   1 
ATOM   1388 C CE   B LYS   A 1 55  ? 18.493 13.829  7.453   0.52 22.35 ?  55  LYS   A CE   1 
ATOM   1389 N NZ   A LYS   A 1 55  ? 16.994 14.179  7.425   0.48 13.08 ?  55  LYS   A NZ   1 
ATOM   1390 N NZ   B LYS   A 1 55  ? 17.390 13.267  6.626   0.52 22.76 ?  55  LYS   A NZ   1 
ATOM   1391 H H    A LYS   A 1 55  ? 22.593 9.639   6.982   0.48 12.45 ?  55  LYS   A H    1 
ATOM   1392 H H    B LYS   A 1 55  ? 22.755 9.723   6.991   0.52 13.31 ?  55  LYS   A H    1 
ATOM   1393 H HA   A LYS   A 1 55  ? 23.082 11.960  8.043   0.48 13.01 ?  55  LYS   A HA   1 
ATOM   1394 H HA   B LYS   A 1 55  ? 23.288 11.963  8.168   0.52 15.20 ?  55  LYS   A HA   1 
ATOM   1395 H HB2  A LYS   A 1 55  ? 21.203 11.598  6.721   0.48 13.48 ?  55  LYS   A HB2  1 
ATOM   1396 H HB2  B LYS   A 1 55  ? 21.459 11.549  6.672   0.52 18.20 ?  55  LYS   A HB2  1 
ATOM   1397 H HB3  A LYS   A 1 55  ? 20.599 10.634  7.824   0.48 13.48 ?  55  LYS   A HB3  1 
ATOM   1398 H HB3  B LYS   A 1 55  ? 20.677 10.938  7.907   0.52 18.20 ?  55  LYS   A HB3  1 
ATOM   1399 H HG2  A LYS   A 1 55  ? 20.136 12.369  9.199   0.48 13.69 ?  55  LYS   A HG2  1 
ATOM   1400 H HG2  B LYS   A 1 55  ? 20.335 12.924  8.828   0.52 21.68 ?  55  LYS   A HG2  1 
ATOM   1401 H HG3  A LYS   A 1 55  ? 20.978 13.377  8.296   0.48 13.69 ?  55  LYS   A HG3  1 
ATOM   1402 H HG3  B LYS   A 1 55  ? 21.546 13.592  8.045   0.52 21.68 ?  55  LYS   A HG3  1 
ATOM   1403 H HD2  A LYS   A 1 55  ? 19.400 13.256  6.612   0.48 14.13 ?  55  LYS   A HD2  1 
ATOM   1404 H HD2  B LYS   A 1 55  ? 20.237 14.256  6.478   0.52 24.94 ?  55  LYS   A HD2  1 
ATOM   1405 H HD3  A LYS   A 1 55  ? 18.604 12.124  7.395   0.48 14.13 ?  55  LYS   A HD3  1 
ATOM   1406 H HD3  B LYS   A 1 55  ? 19.735 12.768  6.229   0.52 24.94 ?  55  LYS   A HD3  1 
ATOM   1407 H HE2  A LYS   A 1 55  ? 18.082 13.721  9.065   0.48 15.35 ?  55  LYS   A HE2  1 
ATOM   1408 H HE2  B LYS   A 1 55  ? 18.397 13.479  8.351   0.52 26.80 ?  55  LYS   A HE2  1 
ATOM   1409 H HE3  A LYS   A 1 55  ? 18.760 14.837  8.154   0.48 15.35 ?  55  LYS   A HE3  1 
ATOM   1410 H HE3  B LYS   A 1 55  ? 18.405 14.795  7.461   0.52 26.80 ?  55  LYS   A HE3  1 
ATOM   1411 H HZ1  A LYS   A 1 55  ? 16.440 14.682  7.909   0.48 15.67 ?  55  LYS   A HZ1  1 
ATOM   1412 H HZ1  B LYS   A 1 55  ? 16.814 13.910  6.411   0.52 27.29 ?  55  LYS   A HZ1  1 
ATOM   1413 H HZ2  A LYS   A 1 55  ? 17.141 14.583  6.646   0.48 15.67 ?  55  LYS   A HZ2  1 
ATOM   1414 H HZ2  B LYS   A 1 55  ? 17.718 12.911  5.877   0.52 27.29 ?  55  LYS   A HZ2  1 
ATOM   1415 H HZ3  A LYS   A 1 55  ? 16.610 13.390  7.276   0.48 15.67 ?  55  LYS   A HZ3  1 
ATOM   1416 H HZ3  B LYS   A 1 55  ? 16.963 12.634  7.080   0.52 27.29 ?  55  LYS   A HZ3  1 
ATOM   1417 N N    . ALA   A 1 56  ? 22.140 9.743   10.158  1.00 12.21 ?  56  ALA   A N    1 
ATOM   1418 C CA   . ALA   A 1 56  ? 22.034 9.414   11.574  1.00 12.50 ?  56  ALA   A CA   1 
ATOM   1419 C C    . ALA   A 1 56  ? 23.382 9.413   12.288  1.00 12.60 ?  56  ALA   A C    1 
ATOM   1420 O O    . ALA   A 1 56  ? 23.414 9.566   13.511  1.00 13.82 ?  56  ALA   A O    1 
ATOM   1421 C CB   . ALA   A 1 56  ? 21.320 8.068   11.751  1.00 13.62 ?  56  ALA   A CB   1 
ATOM   1422 H H    A ALA   A 1 56  ? 21.935 9.094   9.633   0.48 14.63 ?  56  ALA   A H    1 
ATOM   1423 H H    B ALA   A 1 56  ? 21.926 9.107   9.620   0.52 14.63 ?  56  ALA   A H    1 
ATOM   1424 H HA   . ALA   A 1 56  ? 21.481 10.082  12.000  1.00 14.97 ?  56  ALA   A HA   1 
ATOM   1425 H HB1  . ALA   A 1 56  ? 21.257 7.865   12.699  1.00 16.31 ?  56  ALA   A HB1  1 
ATOM   1426 H HB2  . ALA   A 1 56  ? 20.428 8.128   11.370  1.00 16.31 ?  56  ALA   A HB2  1 
ATOM   1427 H HB3  . ALA   A 1 56  ? 21.825 7.374   11.298  1.00 16.31 ?  56  ALA   A HB3  1 
ATOM   1428 N N    . THR   A 1 57  ? 24.490 9.246   11.561  1.00 11.33 ?  57  THR   A N    1 
ATOM   1429 C CA   . THR   A 1 57  ? 25.835 9.369   12.125  1.00 11.42 ?  57  THR   A CA   1 
ATOM   1430 C C    . THR   A 1 57  ? 26.384 10.788  12.041  1.00 11.81 ?  57  THR   A C    1 
ATOM   1431 O O    . THR   A 1 57  ? 27.572 11.001  12.316  1.00 12.35 ?  57  THR   A O    1 
ATOM   1432 C CB   . THR   A 1 57  ? 26.838 8.416   11.449  1.00 11.17 ?  57  THR   A CB   1 
ATOM   1433 O OG1  . THR   A 1 57  ? 27.206 8.911   10.148  1.00 10.76 ?  57  THR   A OG1  1 
ATOM   1434 C CG2  . THR   A 1 57  ? 26.291 7.009   11.346  1.00 11.49 ?  57  THR   A CG2  1 
ATOM   1435 H H    . THR   A 1 57  ? 24.486 9.045   10.724  1.00 13.57 ?  57  THR   A H    1 
ATOM   1436 H HA   . THR   A 1 57  ? 25.790 9.122   13.068  1.00 13.67 ?  57  THR   A HA   1 
ATOM   1437 H HB   . THR   A 1 57  ? 27.633 8.367   12.003  1.00 13.38 ?  57  THR   A HB   1 
ATOM   1438 H HG1  . THR   A 1 57  ? 26.519 8.968   9.667   1.00 12.89 ?  57  THR   A HG1  1 
ATOM   1439 H HG21 . THR   A 1 57  ? 27.012 6.363   11.380  1.00 13.76 ?  57  THR   A HG21 1 
ATOM   1440 H HG22 . THR   A 1 57  ? 25.676 6.830   12.079  1.00 13.76 ?  57  THR   A HG22 1 
ATOM   1441 H HG23 . THR   A 1 57  ? 25.810 6.899   10.509  1.00 13.76 ?  57  THR   A HG23 1 
ATOM   1442 N N    . ASN   A 1 58  ? 25.564 11.759  11.652  1.00 12.29 ?  58  ASN   A N    1 
ATOM   1443 C CA   . ASN   A 1 58  ? 26.026 13.138  11.556  1.00 12.90 ?  58  ASN   A CA   1 
ATOM   1444 C C    . ASN   A 1 58  ? 27.161 13.271  10.538  1.00 11.98 ?  58  ASN   A C    1 
ATOM   1445 O O    . ASN   A 1 58  ? 28.062 14.101  10.695  1.00 12.55 ?  58  ASN   A O    1 
ATOM   1446 C CB   . ASN   A 1 58  ? 26.423 13.667  12.948  1.00 15.33 ?  58  ASN   A CB   1 
ATOM   1447 C CG   . ASN   A 1 58  ? 26.811 15.131  12.951  1.00 18.80 ?  58  ASN   A CG   1 
ATOM   1448 O OD1  . ASN   A 1 58  ? 26.180 15.948  12.291  1.00 20.19 ?  58  ASN   A OD1  1 
ATOM   1449 N ND2  . ASN   A 1 58  ? 27.851 15.472  13.711  1.00 19.88 ?  58  ASN   A ND2  1 
ATOM   1450 H H    . ASN   A 1 58  ? 24.739 11.638  11.433  1.00 14.72 ?  58  ASN   A H    1 
ATOM   1451 H HA   . ASN   A 1 58  ? 25.285 13.676  11.241  1.00 15.45 ?  58  ASN   A HA   1 
ATOM   1452 H HB2  . ASN   A 1 58  ? 25.665 13.550  13.554  1.00 18.37 ?  58  ASN   A HB2  1 
ATOM   1453 H HB3  . ASN   A 1 58  ? 27.179 13.162  13.277  1.00 18.37 ?  58  ASN   A HB3  1 
ATOM   1454 H HD21 . ASN   A 1 58  ? 28.097 16.295  13.751  1.00 23.83 ?  58  ASN   A HD21 1 
ATOM   1455 H HD22 . ASN   A 1 58  ? 28.260 14.874  14.165  1.00 23.83 ?  58  ASN   A HD22 1 
ATOM   1456 N N    . ASN   A 1 59  ? 27.127 12.454  9.480   1.00 11.09 ?  59  ASN   A N    1 
ATOM   1457 C CA   . ASN   A 1 59  ? 28.095 12.437  8.377   1.00 10.98 ?  59  ASN   A CA   1 
ATOM   1458 C C    . ASN   A 1 59  ? 29.419 11.760  8.745   1.00 10.48 ?  59  ASN   A C    1 
ATOM   1459 O O    . ASN   A 1 59  ? 30.325 11.717  7.906   1.00 10.49 ?  59  ASN   A O    1 
ATOM   1460 C CB   . ASN   A 1 59  ? 28.376 13.828  7.781   1.00 11.28 ?  59  ASN   A CB   1 
ATOM   1461 C CG   . ASN   A 1 59  ? 28.723 13.779  6.306   1.00 11.16 ?  59  ASN   A CG   1 
ATOM   1462 O OD1  . ASN   A 1 59  ? 28.018 13.164  5.507   1.00 11.51 ?  59  ASN   A OD1  1 
ATOM   1463 N ND2  . ASN   A 1 59  ? 29.808 14.453  5.930   1.00 11.91 ?  59  ASN   A ND2  1 
ATOM   1464 H H    . ASN   A 1 59  ? 26.506 11.869  9.370   1.00 13.28 ?  59  ASN   A H    1 
ATOM   1465 H HA   . ASN   A 1 59  ? 27.705 11.913  7.664   1.00 13.15 ?  59  ASN   A HA   1 
ATOM   1466 H HB2  . ASN   A 1 59  ? 27.590 14.385  7.877   1.00 13.52 ?  59  ASN   A HB2  1 
ATOM   1467 H HB3  . ASN   A 1 59  ? 29.127 14.230  8.247   1.00 13.52 ?  59  ASN   A HB3  1 
ATOM   1468 H HD21 . ASN   A 1 59  ? 30.050 14.462  5.103   1.00 14.27 ?  59  ASN   A HD21 1 
ATOM   1469 H HD22 . ASN   A 1 59  ? 30.280 14.881  6.513   1.00 14.27 ?  59  ASN   A HD22 1 
ATOM   1470 N N    . ALA   A 1 60  ? 29.564 11.218  9.953   1.00 10.48 ?  60  ALA   A N    1 
ATOM   1471 C CA   . ALA   A 1 60  ? 30.802 10.525  10.288  1.00 10.31 ?  60  ALA   A CA   1 
ATOM   1472 C C    . ALA   A 1 60  ? 31.018 9.296   9.413   1.00 10.27 ?  60  ALA   A C    1 
ATOM   1473 O O    . ALA   A 1 60  ? 32.162 8.973   9.077   1.00 10.88 ?  60  ALA   A O    1 
ATOM   1474 C CB   . ALA   A 1 60  ? 30.818 10.155  11.767  1.00 11.58 ?  60  ALA   A CB   1 
ATOM   1475 H H    . ALA   A 1 60  ? 28.975 11.235  10.578  1.00 12.55 ?  60  ALA   A H    1 
ATOM   1476 H HA   . ALA   A 1 60  ? 31.544 11.127  10.127  1.00 12.35 ?  60  ALA   A HA   1 
ATOM   1477 H HB1  . ALA   A 1 60  ? 31.650 9.695   11.967  1.00 13.88 ?  60  ALA   A HB1  1 
ATOM   1478 H HB2  . ALA   A 1 60  ? 30.752 10.965  12.295  1.00 13.88 ?  60  ALA   A HB2  1 
ATOM   1479 H HB3  . ALA   A 1 60  ? 30.066 9.573   11.956  1.00 13.88 ?  60  ALA   A HB3  1 
ATOM   1480 N N    . MET   A 1 61  ? 29.942 8.597   9.040   1.00 9.93  ?  61  MET   A N    1 
ATOM   1481 C CA   . MET   A 1 61  ? 30.072 7.466   8.127   1.00 9.96  ?  61  MET   A CA   1 
ATOM   1482 C C    . MET   A 1 61  ? 30.685 7.902   6.800   1.00 9.79  ?  61  MET   A C    1 
ATOM   1483 O O    . MET   A 1 61  ? 31.576 7.226   6.269   1.00 9.91  ?  61  MET   A O    1 
ATOM   1484 C CB   . MET   A 1 61  ? 28.709 6.792   7.925   1.00 9.90  ?  61  MET   A CB   1 
ATOM   1485 C CG   . MET   A 1 61  ? 28.710 5.643   6.940   1.00 10.07 ?  61  MET   A CG   1 
ATOM   1486 S SD   . MET   A 1 61  ? 27.091 4.890   6.750   1.00 11.30 ?  61  MET   A SD   1 
ATOM   1487 C CE   . MET   A 1 61  ? 26.986 3.966   8.282   1.00 12.71 ?  61  MET   A CE   1 
ATOM   1488 H H    . MET   A 1 61  ? 29.135 8.757   9.295   1.00 11.89 ?  61  MET   A H    1 
ATOM   1489 H HA   . MET   A 1 61  ? 30.658 6.810   8.533   1.00 11.93 ?  61  MET   A HA   1 
ATOM   1490 H HB2  . MET   A 1 61  ? 28.408 6.444   8.778   1.00 11.85 ?  61  MET   A HB2  1 
ATOM   1491 H HB3  . MET   A 1 61  ? 28.079 7.455   7.602   1.00 11.85 ?  61  MET   A HB3  1 
ATOM   1492 H HG2  . MET   A 1 61  ? 28.980 5.968   6.064   1.00 12.06 ?  61  MET   A HG2  1 
ATOM   1493 H HG3  . MET   A 1 61  ? 29.325 4.959   7.242   1.00 12.06 ?  61  MET   A HG3  1 
ATOM   1494 H HE1  . MET   A 1 61  ? 26.152 3.467   8.298   1.00 15.23 ?  61  MET   A HE1  1 
ATOM   1495 H HE2  . MET   A 1 61  ? 27.736 3.349   8.330   1.00 15.23 ?  61  MET   A HE2  1 
ATOM   1496 H HE3  . MET   A 1 61  ? 27.017 4.581   9.029   1.00 15.23 ?  61  MET   A HE3  1 
ATOM   1497 N N    . GLN   A 1 62  ? 30.235 9.035   6.253   1.00 9.79  ?  62  GLN   A N    1 
ATOM   1498 C CA   . GLN   A 1 62  ? 30.787 9.514   4.989   1.00 9.81  ?  62  GLN   A CA   1 
ATOM   1499 C C    . GLN   A 1 62  ? 32.260 9.888   5.123   1.00 10.00 ?  62  GLN   A C    1 
ATOM   1500 O O    . GLN   A 1 62  ? 33.061 9.579   4.234   1.00 10.20 ?  62  GLN   A O    1 
ATOM   1501 C CB   . GLN   A 1 62  ? 29.985 10.704  4.467   1.00 10.15 ?  62  GLN   A CB   1 
ATOM   1502 C CG   . GLN   A 1 62  ? 30.344 11.076  3.035   1.00 10.13 ?  62  GLN   A CG   1 
ATOM   1503 C CD   . GLN   A 1 62  ? 30.003 9.949   2.082   1.00 10.52 ?  62  GLN   A CD   1 
ATOM   1504 O OE1  . GLN   A 1 62  ? 28.824 9.649   1.876   1.00 10.98 ?  62  GLN   A OE1  1 
ATOM   1505 N NE2  . GLN   A 1 62  ? 31.019 9.285   1.535   1.00 10.74 ?  62  GLN   A NE2  1 
ATOM   1506 H H    . GLN   A 1 62  ? 29.620 9.528   6.586   1.00 11.72 ?  62  GLN   A H    1 
ATOM   1507 H HA   . GLN   A 1 62  ? 30.725 8.800   4.334   1.00 11.74 ?  62  GLN   A HA   1 
ATOM   1508 H HB2  . GLN   A 1 62  ? 29.043 10.491  4.494   1.00 12.16 ?  62  GLN   A HB2  1 
ATOM   1509 H HB3  . GLN   A 1 62  ? 30.169 11.478  5.025   1.00 12.16 ?  62  GLN   A HB3  1 
ATOM   1510 H HG2  . GLN   A 1 62  ? 29.835 11.856  2.769   1.00 12.13 ?  62  GLN   A HG2  1 
ATOM   1511 H HG3  . GLN   A 1 62  ? 31.293 11.250  2.970   1.00 12.13 ?  62  GLN   A HG3  1 
ATOM   1512 H HE21 . GLN   A 1 62  ? 31.827 9.514   1.714   1.00 12.86 ?  62  GLN   A HE21 1 
ATOM   1513 H HE22 . GLN   A 1 62  ? 30.867 8.631   0.995   1.00 12.86 ?  62  GLN   A HE22 1 
ATOM   1514 N N    . VAL   A 1 63  ? 32.631 10.573  6.209   1.00 10.34 ?  63  VAL   A N    1 
ATOM   1515 C CA   . VAL   A 1 63  ? 34.026 10.964  6.408   1.00 11.30 ?  63  VAL   A CA   1 
ATOM   1516 C C    . VAL   A 1 63  ? 34.925 9.730   6.456   1.00 10.59 ?  63  VAL   A C    1 
ATOM   1517 O O    . VAL   A 1 63  ? 35.975 9.669   5.800   1.00 11.10 ?  63  VAL   A O    1 
ATOM   1518 C CB   . VAL   A 1 63  ? 34.152 11.834  7.672   1.00 12.61 ?  63  VAL   A CB   1 
ATOM   1519 C CG1  . VAL   A 1 63  ? 35.601 12.091  8.006   1.00 14.45 ?  63  VAL   A CG1  1 
ATOM   1520 C CG2  . VAL   A 1 63  ? 33.409 13.155  7.479   1.00 13.40 ?  63  VAL   A CG2  1 
ATOM   1521 H H    . VAL   A 1 63  ? 32.096 10.816  6.839   1.00 12.38 ?  63  VAL   A H    1 
ATOM   1522 H HA   . VAL   A 1 63  ? 34.305 11.500  5.653   1.00 13.54 ?  63  VAL   A HA   1 
ATOM   1523 H HB   . VAL   A 1 63  ? 33.750 11.369  8.422   1.00 15.11 ?  63  VAL   A HB   1 
ATOM   1524 H HG11 . VAL   A 1 63  ? 35.653 12.825  8.638   1.00 17.31 ?  63  VAL   A HG11 1 
ATOM   1525 H HG12 . VAL   A 1 63  ? 35.987 11.292  8.394   1.00 17.31 ?  63  VAL   A HG12 1 
ATOM   1526 H HG13 . VAL   A 1 63  ? 36.075 12.327  7.190   1.00 17.31 ?  63  VAL   A HG13 1 
ATOM   1527 H HG21 . VAL   A 1 63  ? 33.510 13.695  8.282   1.00 16.06 ?  63  VAL   A HG21 1 
ATOM   1528 H HG22 . VAL   A 1 63  ? 33.790 13.625  6.719   1.00 16.06 ?  63  VAL   A HG22 1 
ATOM   1529 H HG23 . VAL   A 1 63  ? 32.471 12.973  7.320   1.00 16.06 ?  63  VAL   A HG23 1 
ATOM   1530 N N    . GLU   A 1 64  ? 34.512 8.720   7.226   1.00 10.51 ?  64  GLU   A N    1 
ATOM   1531 C CA   . GLU   A 1 64  ? 35.275 7.480   7.310   1.00 10.31 ?  64  GLU   A CA   1 
ATOM   1532 C C    . GLU   A 1 64  ? 35.348 6.794   5.952   1.00 9.91  ?  64  GLU   A C    1 
ATOM   1533 O O    . GLU   A 1 64  ? 36.397 6.257   5.563   1.00 10.44 ?  64  GLU   A O    1 
ATOM   1534 C CB   . GLU   A 1 64  ? 34.597 6.572   8.333   1.00 10.92 ?  64  GLU   A CB   1 
ATOM   1535 C CG   . GLU   A 1 64  ? 35.248 5.217   8.476   1.00 11.33 ?  64  GLU   A CG   1 
ATOM   1536 C CD   . GLU   A 1 64  ? 34.370 4.213   9.191   1.00 11.88 ?  64  GLU   A CD   1 
ATOM   1537 O OE1  . GLU   A 1 64  ? 33.129 4.300   9.054   1.00 12.69 ?  64  GLU   A OE1  1 
ATOM   1538 O OE2  . GLU   A 1 64  ? 34.913 3.321   9.882   1.00 12.29 -1 64  GLU   A OE2  1 
ATOM   1539 H H    . GLU   A 1 64  ? 33.793 8.726   7.698   1.00 12.59 ?  64  GLU   A H    1 
ATOM   1540 H HA   . GLU   A 1 64  ? 36.179 7.678   7.612   1.00 12.35 ?  64  GLU   A HA   1 
ATOM   1541 H HB2  . GLU   A 1 64  ? 34.627 7.013   9.201   1.00 13.08 ?  64  GLU   A HB2  1 
ATOM   1542 H HB3  . GLU   A 1 64  ? 33.676 6.445   8.063   1.00 13.08 ?  64  GLU   A HB3  1 
ATOM   1543 H HG2  . GLU   A 1 64  ? 35.452 4.860   7.594   1.00 13.58 ?  64  GLU   A HG2  1 
ATOM   1544 H HG3  . GLU   A 1 64  ? 36.069 5.318   8.982   1.00 13.58 ?  64  GLU   A HG3  1 
ATOM   1545 N N    . SER   A 1 65  ? 34.223 6.789   5.230   1.00 9.96  ?  65  SER   A N    1 
ATOM   1546 C CA   . SER   A 1 65  ? 34.160 6.137   3.927   1.00 9.77  ?  65  SER   A CA   1 
ATOM   1547 C C    . SER   A 1 65  ? 35.075 6.814   2.916   1.00 10.22 ?  65  SER   A C    1 
ATOM   1548 O O    . SER   A 1 65  ? 35.708 6.141   2.096   1.00 10.68 ?  65  SER   A O    1 
ATOM   1549 C CB   . SER   A 1 65  ? 32.723 6.163   3.407   1.00 9.98  ?  65  SER   A CB   1 
ATOM   1550 O OG   . SER   A 1 65  ? 31.865 5.340   4.197   1.00 10.34 ?  65  SER   A OG   1 
ATOM   1551 H H    . SER   A 1 65  ? 33.489 7.160   5.475   1.00 11.93 ?  65  SER   A H    1 
ATOM   1552 H HA   . SER   A 1 65  ? 34.437 5.212   4.018   1.00 11.70 ?  65  SER   A HA   1 
ATOM   1553 H HB2  . SER   A 1 65  ? 32.394 7.075   3.432   1.00 11.95 ?  65  SER   A HB2  1 
ATOM   1554 H HB3  . SER   A 1 65  ? 32.714 5.833   2.495   1.00 11.95 ?  65  SER   A HB3  1 
ATOM   1555 H HG   . SER   A 1 65  ? 31.869 5.620   4.997   1.00 12.39 ?  65  SER   A HG   1 
ATOM   1556 N N    . ASP   A 1 66  ? 35.148 8.148   2.943   1.00 10.10 ?  66  ASP   A N    1 
ATOM   1557 C CA   . ASP   A 1 66  ? 36.004 8.854   1.995   1.00 11.20 ?  66  ASP   A CA   1 
ATOM   1558 C C    . ASP   A 1 66  ? 37.468 8.492   2.215   1.00 10.80 ?  66  ASP   A C    1 
ATOM   1559 O O    . ASP   A 1 66  ? 38.229 8.325   1.256   1.00 11.63 ?  66  ASP   A O    1 
ATOM   1560 C CB   . ASP   A 1 66  ? 35.790 10.359  2.119   1.00 12.32 ?  66  ASP   A CB   1 
ATOM   1561 C CG   . ASP   A 1 66  ? 34.449 10.826  1.543   1.00 14.18 ?  66  ASP   A CG   1 
ATOM   1562 O OD1  . ASP   A 1 66  ? 33.724 10.044  0.888   1.00 14.41 ?  66  ASP   A OD1  1 
ATOM   1563 O OD2  . ASP   A 1 66  ? 34.141 12.017  1.734   1.00 17.13 -1 66  ASP   A OD2  1 
ATOM   1564 H H    . ASP   A 1 66  ? 34.714 8.655   3.492   1.00 12.10 ?  66  ASP   A H    1 
ATOM   1565 H HA   . ASP   A 1 66  ? 35.758 8.590   1.097   1.00 13.42 ?  66  ASP   A HA   1 
ATOM   1566 H HB2  . ASP   A 1 66  ? 35.811 10.606  3.058   1.00 14.76 ?  66  ASP   A HB2  1 
ATOM   1567 H HB3  . ASP   A 1 66  ? 36.503 10.817  1.644   1.00 14.76 ?  66  ASP   A HB3  1 
ATOM   1568 N N    . ASP   A 1 67  ? 37.882 8.358   3.474   1.00 10.99 ?  67  ASP   A N    1 
ATOM   1569 C CA   . ASP   A 1 67  ? 39.235 7.902   3.757   1.00 11.80 ?  67  ASP   A CA   1 
ATOM   1570 C C    . ASP   A 1 67  ? 39.448 6.470   3.274   1.00 11.75 ?  67  ASP   A C    1 
ATOM   1571 O O    . ASP   A 1 67  ? 40.506 6.148   2.722   1.00 12.45 ?  67  ASP   A O    1 
ATOM   1572 C CB   . ASP   A 1 67  ? 39.525 8.034   5.250   1.00 12.85 ?  67  ASP   A CB   1 
ATOM   1573 C CG   . ASP   A 1 67  ? 40.825 7.368   5.651   1.00 13.97 ?  67  ASP   A CG   1 
ATOM   1574 O OD1  . ASP   A 1 67  ? 41.899 8.000   5.502   1.00 16.69 ?  67  ASP   A OD1  1 
ATOM   1575 O OD2  . ASP   A 1 67  ? 40.772 6.206   6.114   1.00 13.78 -1 67  ASP   A OD2  1 
ATOM   1576 H H    . ASP   A 1 67  ? 37.407 8.521   4.168   1.00 13.16 ?  67  ASP   A H    1 
ATOM   1577 H HA   . ASP   A 1 67  ? 39.863 8.463   3.282   1.00 14.14 ?  67  ASP   A HA   1 
ATOM   1578 H HB2  . ASP   A 1 67  ? 39.586 8.971   5.473   1.00 15.40 ?  67  ASP   A HB2  1 
ATOM   1579 H HB3  . ASP   A 1 67  ? 38.803 7.615   5.748   1.00 15.40 ?  67  ASP   A HB3  1 
ATOM   1580 N N    A TYR   A 1 68  ? 38.451 5.602   3.457   0.48 11.30 ?  68  TYR   A N    1 
ATOM   1581 N N    B TYR   A 1 68  ? 38.454 5.589   3.480   0.52 11.30 ?  68  TYR   A N    1 
ATOM   1582 C CA   A TYR   A 1 68  ? 38.588 4.224   2.995   0.48 11.22 ?  68  TYR   A CA   1 
ATOM   1583 C CA   B TYR   A 1 68  ? 38.561 4.214   2.986   0.52 11.34 ?  68  TYR   A CA   1 
ATOM   1584 C C    A TYR   A 1 68  ? 38.795 4.161   1.483   0.48 10.96 ?  68  TYR   A C    1 
ATOM   1585 C C    B TYR   A 1 68  ? 38.820 4.191   1.484   0.52 11.12 ?  68  TYR   A C    1 
ATOM   1586 O O    A TYR   A 1 68  ? 39.642 3.401   0.995   0.48 11.10 ?  68  TYR   A O    1 
ATOM   1587 O O    B TYR   A 1 68  ? 39.716 3.485   1.003   0.52 11.45 ?  68  TYR   A O    1 
ATOM   1588 C CB   A TYR   A 1 68  ? 37.364 3.398   3.413   0.48 11.55 ?  68  TYR   A CB   1 
ATOM   1589 C CB   B TYR   A 1 68  ? 37.295 3.394   3.315   0.52 11.72 ?  68  TYR   A CB   1 
ATOM   1590 C CG   A TYR   A 1 68  ? 37.420 1.999   2.857   0.48 12.23 ?  68  TYR   A CG   1 
ATOM   1591 C CG   B TYR   A 1 68  ? 37.305 2.034   2.620   0.52 12.23 ?  68  TYR   A CG   1 
ATOM   1592 C CD1  A TYR   A 1 68  ? 36.926 1.720   1.589   0.48 13.11 ?  68  TYR   A CD1  1 
ATOM   1593 C CD1  B TYR   A 1 68  ? 36.847 1.895   1.310   0.52 12.67 ?  68  TYR   A CD1  1 
ATOM   1594 C CD2  A TYR   A 1 68  ? 38.011 0.968   3.571   0.48 13.29 ?  68  TYR   A CD2  1 
ATOM   1595 C CD2  B TYR   A 1 68  ? 37.820 0.906   3.250   0.52 12.47 ?  68  TYR   A CD2  1 
ATOM   1596 C CE1  A TYR   A 1 68  ? 37.010 0.461   1.050   0.48 14.32 ?  68  TYR   A CE1  1 
ATOM   1597 C CE1  B TYR   A 1 68  ? 36.898 0.682   0.654   0.52 12.25 ?  68  TYR   A CE1  1 
ATOM   1598 C CE2  A TYR   A 1 68  ? 38.091 -0.311  3.040   0.48 13.95 ?  68  TYR   A CE2  1 
ATOM   1599 C CE2  B TYR   A 1 68  ? 37.863 -0.326  2.601   0.52 11.56 ?  68  TYR   A CE2  1 
ATOM   1600 C CZ   A TYR   A 1 68  ? 37.593 -0.550  1.779   0.48 14.69 ?  68  TYR   A CZ   1 
ATOM   1601 C CZ   B TYR   A 1 68  ? 37.410 -0.420  1.306   0.52 11.44 ?  68  TYR   A CZ   1 
ATOM   1602 O OH   A TYR   A 1 68  ? 37.679 -1.805  1.234   0.48 16.32 ?  68  TYR   A OH   1 
ATOM   1603 O OH   B TYR   A 1 68  ? 37.477 -1.630  0.668   0.52 11.91 ?  68  TYR   A OH   1 
ATOM   1604 H H    A TYR   A 1 68  ? 37.698 5.780   3.833   0.48 13.54 ?  68  TYR   A H    1 
ATOM   1605 H H    B TYR   A 1 68  ? 37.717 5.761   3.892   0.52 13.54 ?  68  TYR   A H    1 
ATOM   1606 H HA   A TYR   A 1 68  ? 39.365 3.829   3.413   0.48 13.44 ?  68  TYR   A HA   1 
ATOM   1607 H HA   B TYR   A 1 68  ? 39.310 3.781   3.420   0.52 13.59 ?  68  TYR   A HA   1 
ATOM   1608 H HB2  A TYR   A 1 68  ? 37.340 3.335   4.380   0.48 13.83 ?  68  TYR   A HB2  1 
ATOM   1609 H HB2  B TYR   A 1 68  ? 37.252 3.239   4.272   0.52 14.04 ?  68  TYR   A HB2  1 
ATOM   1610 H HB3  A TYR   A 1 68  ? 36.561 3.823   3.080   0.48 13.83 ?  68  TYR   A HB3  1 
ATOM   1611 H HB3  B TYR   A 1 68  ? 36.509 3.878   3.018   0.52 14.04 ?  68  TYR   A HB3  1 
ATOM   1612 H HD1  A TYR   A 1 68  ? 36.540 2.405   1.090   0.48 15.71 ?  68  TYR   A HD1  1 
ATOM   1613 H HD1  B TYR   A 1 68  ? 36.506 2.636   0.863   0.52 15.18 ?  68  TYR   A HD1  1 
ATOM   1614 H HD2  A TYR   A 1 68  ? 38.364 1.134   4.413   0.48 15.93 ?  68  TYR   A HD2  1 
ATOM   1615 H HD2  B TYR   A 1 68  ? 38.144 0.974   4.116   0.52 14.94 ?  68  TYR   A HD2  1 
ATOM   1616 H HE1  A TYR   A 1 68  ? 36.667 0.293   0.198   0.48 17.16 ?  68  TYR   A HE1  1 
ATOM   1617 H HE1  B TYR   A 1 68  ? 36.581 0.602   -0.221  0.52 14.68 ?  68  TYR   A HE1  1 
ATOM   1618 H HE2  A TYR   A 1 68  ? 38.494 -0.997  3.518   0.48 16.72 ?  68  TYR   A HE2  1 
ATOM   1619 H HE2  B TYR   A 1 68  ? 38.218 -1.073  3.025   0.52 13.85 ?  68  TYR   A HE2  1 
ATOM   1620 H HH   A TYR   A 1 68  ? 38.046 -2.330  1.770   0.48 19.56 ?  68  TYR   A HH   1 
ATOM   1621 H HH   B TYR   A 1 68  ? 37.206 -1.560  -0.123  0.52 14.27 ?  68  TYR   A HH   1 
ATOM   1622 N N    . ILE   A 1 69  ? 38.015 4.936   0.722   1.00 10.80 ?  69  ILE   A N    1 
ATOM   1623 C CA   . ILE   A 1 69  ? 38.148 4.938   -0.733  1.00 10.77 ?  69  ILE   A CA   1 
ATOM   1624 C C    . ILE   A 1 69  ? 39.483 5.542   -1.156  1.00 10.78 ?  69  ILE   A C    1 
ATOM   1625 O O    . ILE   A 1 69  ? 40.128 5.058   -2.094  1.00 11.36 ?  69  ILE   A O    1 
ATOM   1626 C CB   . ILE   A 1 69  ? 36.953 5.659   -1.391  1.00 11.73 ?  69  ILE   A CB   1 
ATOM   1627 C CG1  . ILE   A 1 69  ? 35.637 4.925   -1.112  1.00 12.20 ?  69  ILE   A CG1  1 
ATOM   1628 C CG2  . ILE   A 1 69  ? 37.190 5.849   -2.891  1.00 13.50 ?  69  ILE   A CG2  1 
ATOM   1629 C CD1  . ILE   A 1 69  ? 35.462 3.627   -1.855  1.00 12.73 ?  69  ILE   A CD1  1 
ATOM   1630 H H    A ILE   A 1 69  ? 37.407 5.463   1.024   0.48 12.93 ?  69  ILE   A H    1 
ATOM   1631 H H    B ILE   A 1 69  ? 37.393 5.448   1.022   0.52 12.93 ?  69  ILE   A H    1 
ATOM   1632 H HA   . ILE   A 1 69  ? 38.143 4.019   -1.039  1.00 12.90 ?  69  ILE   A HA   1 
ATOM   1633 H HB   . ILE   A 1 69  ? 36.890 6.537   -0.991  1.00 14.05 ?  69  ILE   A HB   1 
ATOM   1634 H HG12 . ILE   A 1 69  ? 35.592 4.727   -0.161  1.00 14.61 ?  69  ILE   A HG12 1 
ATOM   1635 H HG13 . ILE   A 1 69  ? 34.905 5.509   -1.356  1.00 14.61 ?  69  ILE   A HG13 1 
ATOM   1636 H HG21 . ILE   A 1 69  ? 36.346 6.071   -3.317  1.00 16.18 ?  69  ILE   A HG21 1 
ATOM   1637 H HG22 . ILE   A 1 69  ? 37.821 6.580   -3.024  1.00 16.18 ?  69  ILE   A HG22 1 
ATOM   1638 H HG23 . ILE   A 1 69  ? 37.546 5.033   -3.268  1.00 16.18 ?  69  ILE   A HG23 1 
ATOM   1639 H HD11 . ILE   A 1 69  ? 34.644 3.204   -1.552  1.00 15.25 ?  69  ILE   A HD11 1 
ATOM   1640 H HD12 . ILE   A 1 69  ? 35.403 3.815   -2.805  1.00 15.25 ?  69  ILE   A HD12 1 
ATOM   1641 H HD13 . ILE   A 1 69  ? 36.219 3.053   -1.675  1.00 15.25 ?  69  ILE   A HD13 1 
ATOM   1642 N N    . ALA   A 1 70  ? 39.907 6.624   -0.500  1.00 11.17 ?  70  ALA   A N    1 
ATOM   1643 C CA   . ALA   A 1 70  ? 41.185 7.228   -0.857  1.00 11.90 ?  70  ALA   A CA   1 
ATOM   1644 C C    . ALA   A 1 70  ? 42.329 6.236   -0.699  1.00 12.59 ?  70  ALA   A C    1 
ATOM   1645 O O    . ALA   A 1 70  ? 43.289 6.264   -1.474  1.00 14.30 ?  70  ALA   A O    1 
ATOM   1646 C CB   . ALA   A 1 70  ? 41.433 8.473   -0.007  1.00 12.71 ?  70  ALA   A CB   1 
ATOM   1647 H H    . ALA   A 1 70  ? 39.487 7.011   0.146   1.00 13.38 ?  70  ALA   A H    1 
ATOM   1648 H HA   . ALA   A 1 70  ? 41.149 7.510   -1.784  1.00 14.26 ?  70  ALA   A HA   1 
ATOM   1649 H HB1  . ALA   A 1 70  ? 42.290 8.865   -0.262  1.00 15.23 ?  70  ALA   A HB1  1 
ATOM   1650 H HB2  . ALA   A 1 70  ? 40.724 9.116   -0.160  1.00 15.23 ?  70  ALA   A HB2  1 
ATOM   1651 H HB3  . ALA   A 1 70  ? 41.458 8.223   0.930   1.00 15.23 ?  70  ALA   A HB3  1 
ATOM   1652 N N    . THR   A 1 71  ? 42.236 5.341   0.281   1.00 11.88 ?  71  THR   A N    1 
ATOM   1653 C CA   . THR   A 1 71  ? 43.294 4.369   0.521   1.00 13.26 ?  71  THR   A CA   1 
ATOM   1654 C C    . THR   A 1 71  ? 43.169 3.146   -0.379  1.00 13.45 ?  71  THR   A C    1 
ATOM   1655 O O    . THR   A 1 71  ? 44.177 2.649   -0.897  1.00 15.28 ?  71  THR   A O    1 
ATOM   1656 C CB   . THR   A 1 71  ? 43.239 3.926   1.978   1.00 14.65 ?  71  THR   A CB   1 
ATOM   1657 O OG1  . THR   A 1 71  ? 43.498 5.055   2.819   1.00 16.08 ?  71  THR   A OG1  1 
ATOM   1658 C CG2  . THR   A 1 71  ? 44.242 2.811   2.259   1.00 15.96 ?  71  THR   A CG2  1 
ATOM   1659 H H    . THR   A 1 71  ? 41.567 5.274   0.812   1.00 14.23 ?  71  THR   A H    1 
ATOM   1660 H HA   . THR   A 1 71  ? 44.155 4.780   0.352   1.00 15.89 ?  71  THR   A HA   1 
ATOM   1661 H HB   . THR   A 1 71  ? 42.353 3.582   2.168   1.00 17.56 ?  71  THR   A HB   1 
ATOM   1662 H HG1  . THR   A 1 71  ? 43.471 4.815   3.625   1.00 19.27 ?  71  THR   A HG1  1 
ATOM   1663 H HG21 . THR   A 1 71  ? 44.390 2.733   3.216   1.00 19.12 ?  71  THR   A HG21 1 
ATOM   1664 H HG22 . THR   A 1 71  ? 43.912 1.963   1.924   1.00 19.12 ?  71  THR   A HG22 1 
ATOM   1665 H HG23 . THR   A 1 71  ? 45.093 3.010   1.831   1.00 19.12 ?  71  THR   A HG23 1 
ATOM   1666 N N    . ASN   A 1 72  ? 41.945 2.646   -0.566  1.00 12.36 ?  72  ASN   A N    1 
ATOM   1667 C CA   . ASN   A 1 72  ? 41.717 1.321   -1.127  1.00 12.49 ?  72  ASN   A CA   1 
ATOM   1668 C C    . ASN   A 1 72  ? 41.083 1.313   -2.504  1.00 12.85 ?  72  ASN   A C    1 
ATOM   1669 O O    . ASN   A 1 72  ? 41.093 0.259   -3.155  1.00 13.88 ?  72  ASN   A O    1 
ATOM   1670 C CB   . ASN   A 1 72  ? 40.835 0.495   -0.181  1.00 13.08 ?  72  ASN   A CB   1 
ATOM   1671 C CG   . ASN   A 1 72  ? 41.460 0.335   1.176   1.00 14.13 ?  72  ASN   A CG   1 
ATOM   1672 O OD1  . ASN   A 1 72  ? 41.014 0.939   2.154   1.00 16.10 ?  72  ASN   A OD1  1 
ATOM   1673 N ND2  . ASN   A 1 72  ? 42.513 -0.456  1.244   1.00 14.86 ?  72  ASN   A ND2  1 
ATOM   1674 H H    . ASN   A 1 72  ? 41.218 3.069   -0.378  1.00 14.81 ?  72  ASN   A H    1 
ATOM   1675 H HA   . ASN   A 1 72  ? 42.567 0.868   -1.204  1.00 14.97 ?  72  ASN   A HA   1 
ATOM   1676 H HB2  . ASN   A 1 72  ? 39.981 0.939   -0.072  1.00 15.67 ?  72  ASN   A HB2  1 
ATOM   1677 H HB3  . ASN   A 1 72  ? 40.706 -0.390  -0.559  1.00 15.67 ?  72  ASN   A HB3  1 
ATOM   1678 H HD21 . ASN   A 1 72  ? 42.915 -0.576  1.995   1.00 17.81 ?  72  ASN   A HD21 1 
ATOM   1679 H HD22 . ASN   A 1 72  ? 42.800 -0.854  0.537   1.00 17.81 ?  72  ASN   A HD22 1 
ATOM   1680 N N    . GLY   A 1 73  ? 40.531 2.430   -2.964  1.00 12.36 ?  73  GLY   A N    1 
ATOM   1681 C CA   . GLY   A 1 73  ? 39.786 2.445   -4.196  1.00 12.14 ?  73  GLY   A CA   1 
ATOM   1682 C C    . GLY   A 1 73  ? 38.395 1.866   -4.021  1.00 11.57 ?  73  GLY   A C    1 
ATOM   1683 O O    . GLY   A 1 73  ? 38.016 1.395   -2.942  1.00 12.19 ?  73  GLY   A O    1 
ATOM   1684 H H    . GLY   A 1 73  ? 40.581 3.203   -2.578  1.00 14.81 ?  73  GLY   A H    1 
ATOM   1685 H HA2  . GLY   A 1 73  ? 39.709 3.358   -4.518  1.00 14.55 ?  73  GLY   A HA2  1 
ATOM   1686 H HA3  . GLY   A 1 73  ? 40.255 1.922   -4.867  1.00 14.55 ?  73  GLY   A HA3  1 
ATOM   1687 N N    . PRO   A 1 74  ? 37.611 1.897   -5.096  1.00 12.08 ?  74  PRO   A N    1 
ATOM   1688 C CA   . PRO   A 1 74  ? 36.213 1.466   -5.013  1.00 12.36 ?  74  PRO   A CA   1 
ATOM   1689 C C    . PRO   A 1 74  ? 36.065 -0.016  -4.702  1.00 11.30 ?  74  PRO   A C    1 
ATOM   1690 O O    . PRO   A 1 74  ? 36.931 -0.845  -4.997  1.00 12.14 ?  74  PRO   A O    1 
ATOM   1691 C CB   . PRO   A 1 74  ? 35.666 1.772   -6.414  1.00 14.05 ?  74  PRO   A CB   1 
ATOM   1692 C CG   . PRO   A 1 74  ? 36.620 2.743   -7.019  1.00 16.51 ?  74  PRO   A CG   1 
ATOM   1693 C CD   . PRO   A 1 74  ? 37.956 2.418   -6.428  1.00 14.23 ?  74  PRO   A CD   1 
ATOM   1694 H HA   . PRO   A 1 74  ? 35.731 1.993   -4.353  1.00 14.81 ?  74  PRO   A HA   1 
ATOM   1695 H HB2  . PRO   A 1 74  ? 35.631 0.954   -6.932  1.00 16.84 ?  74  PRO   A HB2  1 
ATOM   1696 H HB3  . PRO   A 1 74  ? 34.781 2.166   -6.337  1.00 16.84 ?  74  PRO   A HB3  1 
ATOM   1697 H HG2  . PRO   A 1 74  ? 36.638 2.626   -7.980  1.00 19.78 ?  74  PRO   A HG2  1 
ATOM   1698 H HG3  . PRO   A 1 74  ? 36.358 3.646   -6.786  1.00 19.78 ?  74  PRO   A HG3  1 
ATOM   1699 H HD2  . PRO   A 1 74  ? 38.404 1.734   -6.951  1.00 17.05 ?  74  PRO   A HD2  1 
ATOM   1700 H HD3  . PRO   A 1 74  ? 38.495 3.223   -6.362  1.00 17.05 ?  74  PRO   A HD3  1 
ATOM   1701 N N    . LEU   A 1 75  ? 34.916 -0.341  -4.115  1.00 10.90 ?  75  LEU   A N    1 
ATOM   1702 C CA   . LEU   A 1 75  ? 34.514 -1.731  -3.971  1.00 10.67 ?  75  LEU   A CA   1 
ATOM   1703 C C    . LEU   A 1 75  ? 34.119 -2.302  -5.331  1.00 11.22 ?  75  LEU   A C    1 
ATOM   1704 O O    . LEU   A 1 75  ? 33.982 -1.586  -6.326  1.00 12.69 ?  75  LEU   A O    1 
ATOM   1705 C CB   . LEU   A 1 75  ? 33.329 -1.851  -3.012  1.00 10.64 ?  75  LEU   A CB   1 
ATOM   1706 C CG   . LEU   A 1 75  ? 33.547 -1.420  -1.565  1.00 11.87 ?  75  LEU   A CG   1 
ATOM   1707 C CD1  . LEU   A 1 75  ? 32.263 -1.599  -0.752  1.00 13.57 ?  75  LEU   A CD1  1 
ATOM   1708 C CD2  . LEU   A 1 75  ? 34.693 -2.151  -0.920  1.00 15.18 ?  75  LEU   A CD2  1 
ATOM   1709 H H    . LEU   A 1 75  ? 34.353 0.228   -3.795  1.00 13.06 ?  75  LEU   A H    1 
ATOM   1710 H HA   . LEU   A 1 75  ? 35.255 -2.246  -3.622  1.00 12.79 ?  75  LEU   A HA   1 
ATOM   1711 H HB2  . LEU   A 1 75  ? 32.600 -1.320  -3.361  1.00 12.75 ?  75  LEU   A HB2  1 
ATOM   1712 H HB3  . LEU   A 1 75  ? 33.060 -2.786  -2.989  1.00 12.75 ?  75  LEU   A HB3  1 
ATOM   1713 H HG   . LEU   A 1 75  ? 33.771 -0.473  -1.556  1.00 14.22 ?  75  LEU   A HG   1 
ATOM   1714 H HD11 . LEU   A 1 75  ? 32.428 -1.313  0.162   1.00 16.26 ?  75  LEU   A HD11 1 
ATOM   1715 H HD12 . LEU   A 1 75  ? 31.567 -1.054  -1.148  1.00 16.26 ?  75  LEU   A HD12 1 
ATOM   1716 H HD13 . LEU   A 1 75  ? 32.011 -2.531  -0.769  1.00 16.26 ?  75  LEU   A HD13 1 
ATOM   1717 H HD21 . LEU   A 1 75  ? 34.755 -1.888  0.013   1.00 18.19 ?  75  LEU   A HD21 1 
ATOM   1718 H HD22 . LEU   A 1 75  ? 34.537 -3.105  -0.985  1.00 18.19 ?  75  LEU   A HD22 1 
ATOM   1719 H HD23 . LEU   A 1 75  ? 35.519 -1.921  -1.380  1.00 18.19 ?  75  LEU   A HD23 1 
ATOM   1720 N N    . LYS   A 1 76  ? 33.937 -3.619  -5.357  1.00 11.76 ?  76  LYS   A N    1 
ATOM   1721 C CA   . LYS   A 1 76  ? 33.326 -4.319  -6.479  1.00 12.47 ?  76  LYS   A CA   1 
ATOM   1722 C C    . LYS   A 1 76  ? 31.817 -4.403  -6.274  1.00 10.98 ?  76  LYS   A C    1 
ATOM   1723 O O    . LYS   A 1 76  ? 31.342 -4.535  -5.148  1.00 10.72 ?  76  LYS   A O    1 
ATOM   1724 C CB   . LYS   A 1 76  ? 33.868 -5.758  -6.560  1.00 14.43 ?  76  LYS   A CB   1 
ATOM   1725 C CG   . LYS   A 1 76  ? 35.374 -5.861  -6.752  1.00 16.25 ?  76  LYS   A CG   1 
ATOM   1726 C CD   . LYS   A 1 76  ? 35.895 -7.272  -6.571  1.00 17.70 ?  76  LYS   A CD   1 
ATOM   1727 C CE   . LYS   A 1 76  ? 37.394 -7.326  -6.759  1.00 20.71 ?  76  LYS   A CE   1 
ATOM   1728 N NZ   . LYS   A 1 76  ? 37.943 -8.679  -6.523  1.00 21.85 ?  76  LYS   A NZ   1 
ATOM   1729 H H    . LYS   A 1 76  ? 34.170 -4.143  -4.716  1.00 14.09 ?  76  LYS   A H    1 
ATOM   1730 H HA   . LYS   A 1 76  ? 33.518 -3.856  -7.313  1.00 14.94 ?  76  LYS   A HA   1 
ATOM   1731 H HB2  . LYS   A 1 76  ? 33.644 -6.214  -5.735  1.00 17.29 ?  76  LYS   A HB2  1 
ATOM   1732 H HB3  . LYS   A 1 76  ? 33.445 -6.204  -7.308  1.00 17.29 ?  76  LYS   A HB3  1 
ATOM   1733 H HG2  . LYS   A 1 76  ? 35.600 -5.570  -7.649  1.00 19.48 ?  76  LYS   A HG2  1 
ATOM   1734 H HG3  . LYS   A 1 76  ? 35.818 -5.294  -6.099  1.00 19.48 ?  76  LYS   A HG3  1 
ATOM   1735 H HD2  . LYS   A 1 76  ? 35.686 -7.581  -5.675  1.00 21.22 ?  76  LYS   A HD2  1 
ATOM   1736 H HD3  . LYS   A 1 76  ? 35.482 -7.854  -7.231  1.00 21.22 ?  76  LYS   A HD3  1 
ATOM   1737 H HE2  . LYS   A 1 76  ? 37.607 -7.066  -7.669  1.00 24.83 ?  76  LYS   A HE2  1 
ATOM   1738 H HE3  . LYS   A 1 76  ? 37.812 -6.715  -6.131  1.00 24.83 ?  76  LYS   A HE3  1 
ATOM   1739 H HZ1  . LYS   A 1 76  ? 38.822 -8.677  -6.641  1.00 26.20 ?  76  LYS   A HZ1  1 
ATOM   1740 H HZ2  . LYS   A 1 76  ? 37.761 -8.941  -5.691  1.00 26.20 ?  76  LYS   A HZ2  1 
ATOM   1741 H HZ3  . LYS   A 1 76  ? 37.574 -9.260  -7.092  1.00 26.20 ?  76  LYS   A HZ3  1 
ATOM   1742 N N    . VAL   A 1 77  ? 31.061 -4.356  -7.375  1.00 11.15 ?  77  VAL   A N    1 
ATOM   1743 C CA   . VAL   A 1 77  ? 29.655 -4.743  -7.290  1.00 11.26 ?  77  VAL   A CA   1 
ATOM   1744 C C    . VAL   A 1 77  ? 29.593 -6.200  -6.858  1.00 10.97 ?  77  VAL   A C    1 
ATOM   1745 O O    . VAL   A 1 77  ? 30.256 -7.062  -7.446  1.00 11.16 ?  77  VAL   A O    1 
ATOM   1746 C CB   . VAL   A 1 77  ? 28.925 -4.512  -8.622  1.00 12.38 ?  77  VAL   A CB   1 
ATOM   1747 C CG1  . VAL   A 1 77  ? 27.461 -4.943  -8.508  1.00 13.19 ?  77  VAL   A CG1  1 
ATOM   1748 C CG2  . VAL   A 1 77  ? 29.009 -3.049  -9.033  1.00 13.92 ?  77  VAL   A CG2  1 
ATOM   1749 H H    . VAL   A 1 77  ? 31.335 -4.110  -8.152  1.00 13.35 ?  77  VAL   A H    1 
ATOM   1750 H HA   . VAL   A 1 77  ? 29.222 -4.206  -6.609  1.00 13.48 ?  77  VAL   A HA   1 
ATOM   1751 H HB   . VAL   A 1 77  ? 29.352 -5.042  -9.314  1.00 14.83 ?  77  VAL   A HB   1 
ATOM   1752 H HG11 . VAL   A 1 77  ? 26.985 -4.634  -9.292  1.00 15.80 ?  77  VAL   A HG11 1 
ATOM   1753 H HG12 . VAL   A 1 77  ? 27.421 -5.908  -8.451  1.00 15.80 ?  77  VAL   A HG12 1 
ATOM   1754 H HG13 . VAL   A 1 77  ? 27.081 -4.544  -7.710  1.00 15.80 ?  77  VAL   A HG13 1 
ATOM   1755 H HG21 . VAL   A 1 77  ? 28.504 -2.920  -9.850  1.00 16.68 ?  77  VAL   A HG21 1 
ATOM   1756 H HG22 . VAL   A 1 77  ? 28.636 -2.500  -8.323  1.00 16.68 ?  77  VAL   A HG22 1 
ATOM   1757 H HG23 . VAL   A 1 77  ? 29.939 -2.808  -9.178  1.00 16.68 ?  77  VAL   A HG23 1 
ATOM   1758 N N    . GLY   A 1 78  ? 28.808 -6.478  -5.814  1.00 10.71 ?  78  GLY   A N    1 
ATOM   1759 C CA   . GLY   A 1 78  ? 28.787 -7.770  -5.161  1.00 10.81 ?  78  GLY   A CA   1 
ATOM   1760 C C    . GLY   A 1 78  ? 29.716 -7.876  -3.973  1.00 10.18 ?  78  GLY   A C    1 
ATOM   1761 O O    . GLY   A 1 78  ? 29.665 -8.887  -3.258  1.00 11.13 ?  78  GLY   A O    1 
ATOM   1762 H H    . GLY   A 1 78  ? 28.256 -5.910  -5.470  1.00 12.82 ?  78  GLY   A H    1 
ATOM   1763 H HA2  . GLY   A 1 78  ? 27.885 -7.960  -4.863  1.00 12.95 ?  78  GLY   A HA2  1 
ATOM   1764 H HA3  . GLY   A 1 78  ? 29.040 -8.452  -5.807  1.00 12.95 ?  78  GLY   A HA3  1 
ATOM   1765 N N    . GLY   A 1 79  ? 30.563 -6.869  -3.748  1.00 10.32 ?  79  GLY   A N    1 
ATOM   1766 C CA   . GLY   A 1 79  ? 31.541 -6.889  -2.686  1.00 10.22 ?  79  GLY   A CA   1 
ATOM   1767 C C    . GLY   A 1 79  ? 31.100 -6.113  -1.460  1.00 9.67  ?  79  GLY   A C    1 
ATOM   1768 O O    . GLY   A 1 79  ? 29.975 -5.617  -1.363  1.00 10.54 ?  79  GLY   A O    1 
ATOM   1769 H H    . GLY   A 1 79  ? 30.589 -6.145  -4.220  1.00 12.35 ?  79  GLY   A H    1 
ATOM   1770 H HA2  . GLY   A 1 79  ? 31.712 -7.810  -2.427  1.00 12.24 ?  79  GLY   A HA2  1 
ATOM   1771 H HA3  . GLY   A 1 79  ? 32.373 -6.506  -3.007  1.00 12.24 ?  79  GLY   A HA3  1 
ATOM   1772 N N    . SER   A 1 80  ? 32.018 -6.017  -0.502  1.00 10.33 ?  80  SER   A N    1 
ATOM   1773 C CA   . SER   A 1 80  ? 31.718 -5.393  0.776   1.00 10.00 ?  80  SER   A CA   1 
ATOM   1774 C C    . SER   A 1 80  ? 32.997 -4.948  1.463   1.00 9.82  ?  80  SER   A C    1 
ATOM   1775 O O    . SER   A 1 80  ? 34.104 -5.375  1.115   1.00 11.09 ?  80  SER   A O    1 
ATOM   1776 C CB   . SER   A 1 80  ? 30.974 -6.351  1.709   1.00 10.86 ?  80  SER   A CB   1 
ATOM   1777 O OG   . SER   A 1 80  ? 31.807 -7.412  2.147   1.00 12.41 ?  80  SER   A OG   1 
ATOM   1778 H H    . SER   A 1 80  ? 32.827 -6.305  -0.568  1.00 12.37 ?  80  SER   A H    1 
ATOM   1779 H HA   . SER   A 1 80  ? 31.166 -4.613  0.618   1.00 11.98 ?  80  SER   A HA   1 
ATOM   1780 H HB2  . SER   A 1 80  ? 30.664 -5.855  2.485   1.00 13.01 ?  80  SER   A HB2  1 
ATOM   1781 H HB3  . SER   A 1 80  ? 30.213 -6.721  1.233   1.00 13.01 ?  80  SER   A HB3  1 
ATOM   1782 H HG   . SER   A 1 80  ? 32.078 -7.850  1.481   1.00 14.87 ?  80  SER   A HG   1 
ATOM   1783 N N    . CYS   A 1 81  ? 32.820 -4.116  2.488   1.00 9.66  ?  81  CYS   A N    1 
ATOM   1784 C CA   . CYS   A 1 81  ? 33.879 -3.843  3.446   1.00 9.87  ?  81  CYS   A CA   1 
ATOM   1785 C C    . CYS   A 1 81  ? 33.249 -3.617  4.812   1.00 9.65  ?  81  CYS   A C    1 
ATOM   1786 O O    . CYS   A 1 81  ? 32.086 -3.211  4.913   1.00 10.76 ?  81  CYS   A O    1 
ATOM   1787 C CB   . CYS   A 1 81  ? 34.746 -2.645  3.033   1.00 10.78 ?  81  CYS   A CB   1 
ATOM   1788 S SG   . CYS   A 1 81  ? 33.857 -1.070  3.069   1.00 10.74 ?  81  CYS   A SG   1 
ATOM   1789 H H    . CYS   A 1 81  ? 32.089 -3.696  2.651   1.00 11.56 ?  81  CYS   A H    1 
ATOM   1790 H HA   . CYS   A 1 81  ? 34.461 -4.620  3.505   1.00 11.82 ?  81  CYS   A HA   1 
ATOM   1791 H HB2  . CYS   A 1 81  ? 35.500 -2.579  3.644   1.00 12.91 ?  81  CYS   A HB2  1 
ATOM   1792 H HB3  . CYS   A 1 81  ? 35.073 -2.791  2.129   1.00 12.91 ?  81  CYS   A HB3  1 
ATOM   1793 H HG   . CYS   A 1 81  ? 34.600 -0.191  2.732   1.00 12.86 ?  81  CYS   A HG   1 
ATOM   1794 N N    . VAL   A 1 82  ? 34.030 -3.878  5.857   1.00 10.09 ?  82  VAL   A N    1 
ATOM   1795 C CA   . VAL   A 1 82  ? 33.615 -3.642  7.234   1.00 10.15 ?  82  VAL   A CA   1 
ATOM   1796 C C    . VAL   A 1 82  ? 34.224 -2.331  7.709   1.00 10.54 ?  82  VAL   A C    1 
ATOM   1797 O O    . VAL   A 1 82  ? 35.450 -2.155  7.683   1.00 11.49 ?  82  VAL   A O    1 
ATOM   1798 C CB   . VAL   A 1 82  ? 34.041 -4.787  8.165   1.00 11.87 ?  82  VAL   A CB   1 
ATOM   1799 C CG1  . VAL   A 1 82  ? 33.596 -4.488  9.586   1.00 13.75 ?  82  VAL   A CG1  1 
ATOM   1800 C CG2  . VAL   A 1 82  ? 33.490 -6.118  7.683   1.00 12.45 ?  82  VAL   A CG2  1 
ATOM   1801 H H    . VAL   A 1 82  ? 34.828 -4.209  5.790   1.00 12.09 ?  82  VAL   A H    1 
ATOM   1802 H HA   . VAL   A 1 82  ? 32.650 -3.557  7.264   1.00 12.16 ?  82  VAL   A HA   1 
ATOM   1803 H HB   . VAL   A 1 82  ? 35.008 -4.840  8.164   1.00 14.22 ?  82  VAL   A HB   1 
ATOM   1804 H HG11 . VAL   A 1 82  ? 33.671 -5.298  10.112  1.00 16.47 ?  82  VAL   A HG11 1 
ATOM   1805 H HG12 . VAL   A 1 82  ? 34.160 -3.795  9.961   1.00 16.47 ?  82  VAL   A HG12 1 
ATOM   1806 H HG13 . VAL   A 1 82  ? 32.671 -4.190  9.571   1.00 16.47 ?  82  VAL   A HG13 1 
ATOM   1807 H HG21 . VAL   A 1 82  ? 33.745 -6.805  8.316   1.00 14.91 ?  82  VAL   A HG21 1 
ATOM   1808 H HG22 . VAL   A 1 82  ? 32.527 -6.055  7.624   1.00 14.91 ?  82  VAL   A HG22 1 
ATOM   1809 H HG23 . VAL   A 1 82  ? 33.867 -6.313  6.810   1.00 14.91 ?  82  VAL   A HG23 1 
ATOM   1810 N N    . LEU   A 1 83  ? 33.368 -1.414  8.148   1.00 9.98  ?  83  LEU   A N    1 
ATOM   1811 C CA   . LEU   A 1 83  ? 33.790 -0.149  8.729   1.00 10.54 ?  83  LEU   A CA   1 
ATOM   1812 C C    . LEU   A 1 83  ? 33.087 0.022   10.072  1.00 10.40 ?  83  LEU   A C    1 
ATOM   1813 O O    . LEU   A 1 83  ? 32.382 -0.877  10.545  1.00 11.09 ?  83  LEU   A O    1 
ATOM   1814 C CB   . LEU   A 1 83  ? 33.532 1.011   7.753   1.00 10.62 ?  83  LEU   A CB   1 
ATOM   1815 C CG   . LEU   A 1 83  ? 34.431 1.015   6.511   1.00 11.30 ?  83  LEU   A CG   1 
ATOM   1816 C CD1  . LEU   A 1 83  ? 33.989 2.063   5.500   1.00 12.20 ?  83  LEU   A CD1  1 
ATOM   1817 C CD2  . LEU   A 1 83  ? 35.897 1.251   6.897   1.00 12.16 ?  83  LEU   A CD2  1 
ATOM   1818 H H    . LEU   A 1 83  ? 32.515 -1.503  8.108   1.00 11.96 ?  83  LEU   A H    1 
ATOM   1819 H HA   . LEU   A 1 83  ? 34.746 -0.181  8.898   1.00 12.62 ?  83  LEU   A HA   1 
ATOM   1820 H HB2  . LEU   A 1 83  ? 32.615 0.963   7.445   1.00 12.73 ?  83  LEU   A HB2  1 
ATOM   1821 H HB3  . LEU   A 1 83  ? 33.676 1.850   8.218   1.00 12.73 ?  83  LEU   A HB3  1 
ATOM   1822 H HG   . LEU   A 1 83  ? 34.380 0.145   6.087   1.00 13.53 ?  83  LEU   A HG   1 
ATOM   1823 H HD11 . LEU   A 1 83  ? 34.582 2.018   4.730   1.00 14.62 ?  83  LEU   A HD11 1 
ATOM   1824 H HD12 . LEU   A 1 83  ? 33.082 1.865   5.229   1.00 14.62 ?  83  LEU   A HD12 1 
ATOM   1825 H HD13 . LEU   A 1 83  ? 34.039 2.934   5.910   1.00 14.62 ?  83  LEU   A HD13 1 
ATOM   1826 H HD21 . LEU   A 1 83  ? 36.414 1.413   6.090   1.00 14.57 ?  83  LEU   A HD21 1 
ATOM   1827 H HD22 . LEU   A 1 83  ? 35.950 2.025   7.480   1.00 14.57 ?  83  LEU   A HD22 1 
ATOM   1828 H HD23 . LEU   A 1 83  ? 36.239 0.468   7.354   1.00 14.57 ?  83  LEU   A HD23 1 
ATOM   1829 N N    . SER   A 1 84  ? 33.295 1.171   10.708  1.00 10.99 ?  84  SER   A N    1 
ATOM   1830 C CA   . SER   A 1 84  ? 32.655 1.419   11.991  1.00 11.43 ?  84  SER   A CA   1 
ATOM   1831 C C    . SER   A 1 84  ? 31.135 1.506   11.854  1.00 11.18 ?  84  SER   A C    1 
ATOM   1832 O O    . SER   A 1 84  ? 30.602 1.969   10.847  1.00 11.28 ?  84  SER   A O    1 
ATOM   1833 C CB   . SER   A 1 84  ? 33.162 2.731   12.580  1.00 12.42 ?  84  SER   A CB   1 
ATOM   1834 O OG   . SER   A 1 84  ? 32.547 2.984   13.827  1.00 13.26 ?  84  SER   A OG   1 
ATOM   1835 H H    . SER   A 1 84  ? 33.792 1.820   10.415  1.00 13.17 ?  84  SER   A H    1 
ATOM   1836 H HA   . SER   A 1 84  ? 32.876 0.705   12.599  1.00 13.69 ?  84  SER   A HA   1 
ATOM   1837 H HB2  . SER   A 1 84  ? 34.122 2.674   12.714  1.00 14.88 ?  84  SER   A HB2  1 
ATOM   1838 H HB3  . SER   A 1 84  ? 32.959 3.459   11.967  1.00 14.88 ?  84  SER   A HB3  1 
ATOM   1839 H HG   . SER   A 1 84  ? 32.819 3.715   14.145  1.00 15.89 ?  84  SER   A HG   1 
ATOM   1840 N N    . GLY   A 1 85  ? 30.437 1.083   12.906  1.00 12.06 ?  85  GLY   A N    1 
ATOM   1841 C CA   . GLY   A 1 85  ? 29.017 1.332   13.022  1.00 12.83 ?  85  GLY   A CA   1 
ATOM   1842 C C    . GLY   A 1 85  ? 28.677 2.638   13.695  1.00 12.62 ?  85  GLY   A C    1 
ATOM   1843 O O    . GLY   A 1 85  ? 27.493 2.958   13.842  1.00 13.40 ?  85  GLY   A O    1 
ATOM   1844 H H    . GLY   A 1 85  ? 30.777 0.648   13.565  1.00 14.44 ?  85  GLY   A H    1 
ATOM   1845 H HA2  . GLY   A 1 85  ? 28.628 1.335   12.130  1.00 15.37 ?  85  GLY   A HA2  1 
ATOM   1846 H HA3  . GLY   A 1 85  ? 28.613 0.619   13.526  1.00 15.37 ?  85  GLY   A HA3  1 
ATOM   1847 N N    . HIS   A 1 86  ? 29.683 3.399   14.118  1.00 12.47 ?  86  HIS   A N    1 
ATOM   1848 C CA   . HIS   A 1 86  ? 29.488 4.726   14.711  1.00 12.89 ?  86  HIS   A CA   1 
ATOM   1849 C C    . HIS   A 1 86  ? 28.519 4.605   15.882  1.00 14.31 ?  86  HIS   A C    1 
ATOM   1850 O O    . HIS   A 1 86  ? 28.693 3.710   16.723  1.00 14.98 ?  86  HIS   A O    1 
ATOM   1851 C CB   . HIS   A 1 86  ? 29.099 5.724   13.631  1.00 12.97 ?  86  HIS   A CB   1 
ATOM   1852 C CG   . HIS   A 1 86  ? 30.127 5.827   12.566  1.00 12.52 ?  86  HIS   A CG   1 
ATOM   1853 N ND1  . HIS   A 1 86  ? 31.218 6.661   12.674  1.00 13.61 ?  86  HIS   A ND1  1 
ATOM   1854 C CD2  . HIS   A 1 86  ? 30.283 5.139   11.413  1.00 12.16 ?  86  HIS   A CD2  1 
ATOM   1855 C CE1  . HIS   A 1 86  ? 31.983 6.504   11.609  1.00 13.04 ?  86  HIS   A CE1  1 
ATOM   1856 N NE2  . HIS   A 1 86  ? 31.448 5.576   10.836  1.00 12.37 ?  86  HIS   A NE2  1 
ATOM   1857 H H    . HIS   A 1 86  ? 30.505 3.160   14.089  1.00 14.94 ?  86  HIS   A H    1 
ATOM   1858 H HA   . HIS   A 1 86  ? 30.338 5.022   15.075  1.00 15.44 ?  86  HIS   A HA   1 
ATOM   1859 H HB2  . HIS   A 1 86  ? 28.266 5.449   13.221  1.00 15.54 ?  86  HIS   A HB2  1 
ATOM   1860 H HB3  . HIS   A 1 86  ? 28.997 6.608   14.029  1.00 15.54 ?  86  HIS   A HB3  1 
ATOM   1861 H HD2  . HIS   A 1 86  ? 29.714 4.479   11.078  1.00 14.57 ?  86  HIS   A HD2  1 
ATOM   1862 H HE1  . HIS   A 1 86  ? 32.773 6.962   11.423  1.00 15.63 ?  86  HIS   A HE1  1 
ATOM   1863 H HE2  . HIS   A 1 86  ? 31.765 5.302   10.077  1.00 14.83 ?  86  HIS   A HE2  1 
ATOM   1864 N N    A ASN   A 1 87  ? 27.493 5.451   15.955  0.48 15.04 ?  87  ASN   A N    1 
ATOM   1865 N N    B ASN   A 1 87  ? 27.536 5.480   16.001  0.52 14.51 ?  87  ASN   A N    1 
ATOM   1866 C CA   A ASN   A 1 87  ? 26.483 5.461   17.002  0.48 15.89 ?  87  ASN   A CA   1 
ATOM   1867 C CA   B ASN   A 1 87  ? 26.628 5.462   17.135  0.52 15.00 ?  87  ASN   A CA   1 
ATOM   1868 C C    A ASN   A 1 87  ? 25.317 4.525   16.710  0.48 16.81 ?  87  ASN   A C    1 
ATOM   1869 C C    B ASN   A 1 87  ? 25.527 4.422   16.993  0.52 14.62 ?  87  ASN   A C    1 
ATOM   1870 O O    A ASN   A 1 87  ? 24.309 4.571   17.423  0.48 17.88 ?  87  ASN   A O    1 
ATOM   1871 O O    B ASN   A 1 87  ? 24.745 4.244   17.932  0.52 14.33 ?  87  ASN   A O    1 
ATOM   1872 C CB   A ASN   A 1 87  ? 25.937 6.884   17.165  0.48 16.37 ?  87  ASN   A CB   1 
ATOM   1873 C CB   B ASN   A 1 87  ? 26.006 6.851   17.315  0.52 16.11 ?  87  ASN   A CB   1 
ATOM   1874 C CG   A ASN   A 1 87  ? 25.331 7.427   15.877  0.48 16.85 ?  87  ASN   A CG   1 
ATOM   1875 C CG   B ASN   A 1 87  ? 25.573 7.471   15.997  0.52 16.76 ?  87  ASN   A CG   1 
ATOM   1876 O OD1  A ASN   A 1 87  ? 25.888 7.253   14.794  0.48 16.51 ?  87  ASN   A OD1  1 
ATOM   1877 O OD1  B ASN   A 1 87  ? 26.313 7.451   15.014  0.52 16.80 ?  87  ASN   A OD1  1 
ATOM   1878 N ND2  A ASN   A 1 87  ? 24.182 8.081   15.990  0.48 17.73 ?  87  ASN   A ND2  1 
ATOM   1879 N ND2  B ASN   A 1 87  ? 24.370 8.018   15.968  0.52 17.52 ?  87  ASN   A ND2  1 
ATOM   1880 H H    A ASN   A 1 87  ? 27.354 6.063   15.371  0.48 18.02 ?  87  ASN   A H    1 
ATOM   1881 H H    B ASN   A 1 87  ? 27.372 6.096   15.426  0.52 17.39 ?  87  ASN   A H    1 
ATOM   1882 H HA   A ASN   A 1 87  ? 26.885 5.194   17.844  0.48 19.05 ?  87  ASN   A HA   1 
ATOM   1883 H HA   B ASN   A 1 87  ? 27.130 5.254   17.940  0.52 17.97 ?  87  ASN   A HA   1 
ATOM   1884 H HB2  A ASN   A 1 87  ? 25.243 6.883   17.846  0.48 19.62 ?  87  ASN   A HB2  1 
ATOM   1885 H HB2  B ASN   A 1 87  ? 25.222 6.773   17.884  0.52 19.30 ?  87  ASN   A HB2  1 
ATOM   1886 H HB3  A ASN   A 1 87  ? 26.659 7.474   17.430  0.48 19.62 ?  87  ASN   A HB3  1 
ATOM   1887 H HB3  B ASN   A 1 87  ? 26.659 7.436   17.729  0.52 19.30 ?  87  ASN   A HB3  1 
ATOM   1888 H HD21 A ASN   A 1 87  ? 23.802 8.404   15.290  0.48 21.25 ?  87  ASN   A HD21 1 
ATOM   1889 H HD21 B ASN   A 1 87  ? 24.084 8.381   15.245  0.52 21.00 ?  87  ASN   A HD21 1 
ATOM   1890 H HD22 A ASN   A 1 87  ? 23.819 8.182   16.763  0.48 21.25 ?  87  ASN   A HD22 1 
ATOM   1891 H HD22 B ASN   A 1 87  ? 23.880 8.015   16.674  0.52 21.00 ?  87  ASN   A HD22 1 
ATOM   1892 N N    A LEU   A 1 88  ? 25.420 3.690   15.674  0.48 16.47 ?  88  LEU   A N    1 
ATOM   1893 N N    B LEU   A 1 88  ? 25.464 3.719   15.863  0.52 14.36 ?  88  LEU   A N    1 
ATOM   1894 C CA   A LEU   A 1 88  ? 24.315 2.834   15.264  0.48 16.08 ?  88  LEU   A CA   1 
ATOM   1895 C CA   B LEU   A 1 88  ? 24.324 2.873   15.528  0.52 14.40 ?  88  LEU   A CA   1 
ATOM   1896 C C    A LEU   A 1 88  ? 24.539 1.357   15.544  0.48 15.24 ?  88  LEU   A C    1 
ATOM   1897 C C    B LEU   A 1 88  ? 24.555 1.392   15.797  0.52 14.12 ?  88  LEU   A C    1 
ATOM   1898 O O    A LEU   A 1 88  ? 23.560 0.608   15.644  0.48 15.66 ?  88  LEU   A O    1 
ATOM   1899 O O    B LEU   A 1 88  ? 23.604 0.679   16.145  0.52 14.79 ?  88  LEU   A O    1 
ATOM   1900 C CB   A LEU   A 1 88  ? 24.061 2.985   13.759  0.48 16.66 ?  88  LEU   A CB   1 
ATOM   1901 C CB   B LEU   A 1 88  ? 23.966 3.063   14.050  0.52 14.77 ?  88  LEU   A CB   1 
ATOM   1902 C CG   A LEU   A 1 88  ? 23.715 4.382   13.248  0.48 17.74 ?  88  LEU   A CG   1 
ATOM   1903 C CG   B LEU   A 1 88  ? 23.673 4.502   13.621  0.52 15.86 ?  88  LEU   A CG   1 
ATOM   1904 C CD1  A LEU   A 1 88  ? 23.530 4.353   11.743  0.48 18.05 ?  88  LEU   A CD1  1 
ATOM   1905 C CD1  B LEU   A 1 88  ? 23.416 4.561   12.123  0.52 16.06 ?  88  LEU   A CD1  1 
ATOM   1906 C CD2  A LEU   A 1 88  ? 22.469 4.915   13.934  0.48 18.61 ?  88  LEU   A CD2  1 
ATOM   1907 C CD2  B LEU   A 1 88  ? 22.491 5.067   14.394  0.52 17.05 ?  88  LEU   A CD2  1 
ATOM   1908 H H    A LEU   A 1 88  ? 26.127 3.609   15.192  0.48 19.74 ?  88  LEU   A H    1 
ATOM   1909 H H    B LEU   A 1 88  ? 26.080 3.722   15.263  0.52 17.21 ?  88  LEU   A H    1 
ATOM   1910 H HA   A LEU   A 1 88  ? 23.513 3.113   15.733  0.48 19.28 ?  88  LEU   A HA   1 
ATOM   1911 H HA   B LEU   A 1 88  ? 23.561 3.152   16.053  0.52 17.26 ?  88  LEU   A HA   1 
ATOM   1912 H HB2  A LEU   A 1 88  ? 24.859 2.698   13.291  0.48 19.97 ?  88  LEU   A HB2  1 
ATOM   1913 H HB2  B LEU   A 1 88  ? 24.704 2.748   13.507  0.52 17.70 ?  88  LEU   A HB2  1 
ATOM   1914 H HB3  A LEU   A 1 88  ? 23.323 2.402   13.524  0.48 19.97 ?  88  LEU   A HB3  1 
ATOM   1915 H HB3  B LEU   A 1 88  ? 23.172 2.541   13.854  0.52 17.70 ?  88  LEU   A HB3  1 
ATOM   1916 H HG   A LEU   A 1 88  ? 24.449 4.981   13.448  0.48 21.26 ?  88  LEU   A HG   1 
ATOM   1917 H HG   B LEU   A 1 88  ? 24.448 5.055   13.807  0.52 19.00 ?  88  LEU   A HG   1 
ATOM   1918 H HD11 A LEU   A 1 88  ? 23.327 5.249   11.433  0.48 21.64 ?  88  LEU   A HD11 1 
ATOM   1919 H HD11 B LEU   A 1 88  ? 23.233 5.479   11.867  0.52 19.25 ?  88  LEU   A HD11 1 
ATOM   1920 H HD12 A LEU   A 1 88  ? 24.348 4.036   11.330  0.48 21.64 ?  88  LEU   A HD12 1 
ATOM   1921 H HD12 B LEU   A 1 88  ? 24.201 4.237   11.653  0.52 19.25 ?  88  LEU   A HD12 1 
ATOM   1922 H HD13 A LEU   A 1 88  ? 22.797 3.754   11.528  0.48 21.64 ?  88  LEU   A HD13 1 
ATOM   1923 H HD13 B LEU   A 1 88  ? 22.651 4.002   11.911  0.52 19.25 ?  88  LEU   A HD13 1 
ATOM   1924 H HD21 A LEU   A 1 88  ? 22.212 5.750   13.514  0.48 22.31 ?  88  LEU   A HD21 1 
ATOM   1925 H HD21 B LEU   A 1 88  ? 22.252 5.930   14.020  0.52 20.44 ?  88  LEU   A HD21 1 
ATOM   1926 H HD22 A LEU   A 1 88  ? 21.756 4.264   13.845  0.48 22.31 ?  88  LEU   A HD22 1 
ATOM   1927 H HD22 B LEU   A 1 88  ? 21.744 4.454   14.317  0.52 20.44 ?  88  LEU   A HD22 1 
ATOM   1928 H HD23 A LEU   A 1 88  ? 22.665 5.064   14.873  0.48 22.31 ?  88  LEU   A HD23 1 
ATOM   1929 H HD23 B LEU   A 1 88  ? 22.744 5.167   15.324  0.52 20.44 ?  88  LEU   A HD23 1 
ATOM   1930 N N    . ALA   A 1 89  ? 25.789 0.922   15.648  1.00 14.24 ?  89  ALA   A N    1 
ATOM   1931 C CA   . ALA   A 1 89  ? 26.120 -0.491  15.749  1.00 13.97 ?  89  ALA   A CA   1 
ATOM   1932 C C    . ALA   A 1 89  ? 27.612 -0.568  16.023  1.00 14.42 ?  89  ALA   A C    1 
ATOM   1933 O O    . ALA   A 1 89  ? 28.327 0.424   15.890  1.00 15.22 ?  89  ALA   A O    1 
ATOM   1934 C CB   . ALA   A 1 89  ? 25.803 -1.200  14.434  1.00 13.91 ?  89  ALA   A CB   1 
ATOM   1935 H H    A ALA   A 1 89  ? 26.479 1.440   15.639  0.48 17.06 ?  89  ALA   A H    1 
ATOM   1936 H H    B ALA   A 1 89  ? 26.474 1.424   15.489  0.52 17.06 ?  89  ALA   A H    1 
ATOM   1937 H HA   . ALA   A 1 89  ? 25.628 -0.902  16.476  1.00 16.74 ?  89  ALA   A HA   1 
ATOM   1938 H HB1  . ALA   A 1 89  ? 26.065 -2.132  14.510  1.00 16.67 ?  89  ALA   A HB1  1 
ATOM   1939 H HB2  . ALA   A 1 89  ? 24.852 -1.136  14.261  1.00 16.67 ?  89  ALA   A HB2  1 
ATOM   1940 H HB3  . ALA   A 1 89  ? 26.302 -0.776  13.719  1.00 16.67 ?  89  ALA   A HB3  1 
ATOM   1941 N N    . LYS   A 1 90  ? 28.092 -1.755  16.392  1.00 15.09 ?  90  LYS   A N    1 
ATOM   1942 C CA   . LYS   A 1 90  ? 29.537 -1.911  16.524  1.00 15.83 ?  90  LYS   A CA   1 
ATOM   1943 C C    . LYS   A 1 90  ? 30.221 -1.715  15.173  1.00 14.67 ?  90  LYS   A C    1 
ATOM   1944 O O    . LYS   A 1 90  ? 31.146 -0.899  15.036  1.00 15.64 ?  90  LYS   A O    1 
ATOM   1945 C CB   . LYS   A 1 90  ? 29.873 -3.274  17.129  1.00 18.16 ?  90  LYS   A CB   1 
ATOM   1946 C CG   . LYS   A 1 90  ? 31.347 -3.422  17.478  1.00 22.76 ?  90  LYS   A CG   1 
ATOM   1947 C CD   . LYS   A 1 90  ? 31.587 -4.606  18.400  1.00 27.43 ?  90  LYS   A CD   1 
ATOM   1948 C CE   . LYS   A 1 90  ? 33.017 -4.630  18.921  1.00 31.01 ?  90  LYS   A CE   1 
ATOM   1949 N NZ   . LYS   A 1 90  ? 34.004 -4.977  17.865  1.00 32.98 ?  90  LYS   A NZ   1 
ATOM   1950 H H    . LYS   A 1 90  ? 27.624 -2.455  16.557  1.00 18.09 ?  90  LYS   A H    1 
ATOM   1951 H HA   . LYS   A 1 90  ? 29.871 -1.231  17.129  1.00 18.97 ?  90  LYS   A HA   1 
ATOM   1952 H HB2  . LYS   A 1 90  ? 29.360 -3.395  17.946  1.00 21.76 ?  90  LYS   A HB2  1 
ATOM   1953 H HB3  . LYS   A 1 90  ? 29.646 -3.970  16.493  1.00 21.76 ?  90  LYS   A HB3  1 
ATOM   1954 H HG2  . LYS   A 1 90  ? 31.855 -3.563  16.664  1.00 27.29 ?  90  LYS   A HG2  1 
ATOM   1955 H HG3  . LYS   A 1 90  ? 31.651 -2.619  17.929  1.00 27.29 ?  90  LYS   A HG3  1 
ATOM   1956 H HD2  . LYS   A 1 90  ? 30.987 -4.547  19.161  1.00 32.89 ?  90  LYS   A HD2  1 
ATOM   1957 H HD3  . LYS   A 1 90  ? 31.427 -5.430  17.911  1.00 32.89 ?  90  LYS   A HD3  1 
ATOM   1958 H HE2  . LYS   A 1 90  ? 33.243 -3.752  19.266  1.00 37.19 ?  90  LYS   A HE2  1 
ATOM   1959 H HE3  . LYS   A 1 90  ? 33.086 -5.292  19.627  1.00 37.19 ?  90  LYS   A HE3  1 
ATOM   1960 H HZ1  . LYS   A 1 90  ? 34.825 -4.998  18.211  1.00 39.56 ?  90  LYS   A HZ1  1 
ATOM   1961 H HZ2  . LYS   A 1 90  ? 33.815 -5.777  17.523  1.00 39.56 ?  90  LYS   A HZ2  1 
ATOM   1962 H HZ3  . LYS   A 1 90  ? 33.980 -4.371  17.214  1.00 39.56 ?  90  LYS   A HZ3  1 
ATOM   1963 N N    . HIS   A 1 91  ? 29.747 -2.435  14.157  1.00 12.63 ?  91  HIS   A N    1 
ATOM   1964 C CA   . HIS   A 1 91  ? 30.307 -2.412  12.821  1.00 11.98 ?  91  HIS   A CA   1 
ATOM   1965 C C    . HIS   A 1 91  ? 29.208 -2.129  11.814  1.00 11.00 ?  91  HIS   A C    1 
ATOM   1966 O O    . HIS   A 1 91  ? 28.042 -2.482  12.024  1.00 11.72 ?  91  HIS   A O    1 
ATOM   1967 C CB   . HIS   A 1 91  ? 30.892 -3.781  12.443  1.00 14.22 ?  91  HIS   A CB   1 
ATOM   1968 C CG   . HIS   A 1 91  ? 31.868 -4.327  13.437  1.00 18.46 ?  91  HIS   A CG   1 
ATOM   1969 N ND1  . HIS   A 1 91  ? 33.138 -3.816  13.594  1.00 20.70 ?  91  HIS   A ND1  1 
ATOM   1970 C CD2  . HIS   A 1 91  ? 31.765 -5.353  14.315  1.00 20.16 ?  91  HIS   A CD2  1 
ATOM   1971 C CE1  . HIS   A 1 91  ? 33.773 -4.497  14.532  1.00 21.29 ?  91  HIS   A CE1  1 
ATOM   1972 N NE2  . HIS   A 1 91  ? 32.962 -5.437  14.985  1.00 21.58 ?  91  HIS   A NE2  1 
ATOM   1973 H H    . HIS   A 1 91  ? 29.080 -2.977  14.235  1.00 15.13 ?  91  HIS   A H    1 
ATOM   1974 H HA   . HIS   A 1 91  ? 30.998 -1.739  12.751  1.00 14.35 ?  91  HIS   A HA   1 
ATOM   1975 H HB2  . HIS   A 1 91  ? 30.168 -4.422  12.363  1.00 17.04 ?  91  HIS   A HB2  1 
ATOM   1976 H HB3  . HIS   A 1 91  ? 31.353 -3.701  11.592  1.00 17.04 ?  91  HIS   A HB3  1 
ATOM   1977 H HD1  . HIS   A 1 91  ? 33.466 -3.152  13.153  1.00 24.82 ?  91  HIS   A HD1  1 
ATOM   1978 H HD2  . HIS   A 1 91  ? 31.027 -5.900  14.444  1.00 24.17 ?  91  HIS   A HD2  1 
ATOM   1979 H HE1  . HIS   A 1 91  ? 34.645 -4.338  14.822  1.00 25.52 ?  91  HIS   A HE1  1 
ATOM   1980 N N    . CYS   A 1 92  ? 29.598 -1.532  10.694  1.00 10.98 ?  92  CYS   A N    1 
ATOM   1981 C CA   . CYS   A 1 92  ? 28.746 -1.452  9.515   1.00 10.45 ?  92  CYS   A CA   1 
ATOM   1982 C C    . CYS   A 1 92  ? 29.389 -2.262  8.396   1.00 9.98  ?  92  CYS   A C    1 
ATOM   1983 O O    . CYS   A 1 92  ? 30.539 -1.999  8.014   1.00 10.42 ?  92  CYS   A O    1 
ATOM   1984 C CB   . CYS   A 1 92  ? 28.534 -0.008  9.060   1.00 10.74 ?  92  CYS   A CB   1 
ATOM   1985 S SG   . CYS   A 1 92  ? 27.507 0.118   7.561   1.00 10.42 ?  92  CYS   A SG   1 
ATOM   1986 H H    . CYS   A 1 92  ? 30.368 -1.160  10.586  1.00 13.15 ?  92  CYS   A H    1 
ATOM   1987 H HA   . CYS   A 1 92  ? 27.879 -1.839  9.719   1.00 12.52 ?  92  CYS   A HA   1 
ATOM   1988 H HB2  . CYS   A 1 92  ? 28.087 0.486   9.767   1.00 12.87 ?  92  CYS   A HB2  1 
ATOM   1989 H HB3  . CYS   A 1 92  ? 29.394 0.393   8.867   1.00 12.87 ?  92  CYS   A HB3  1 
ATOM   1990 H HG   . CYS   A 1 92  ? 27.378 1.272   7.274   1.00 12.48 ?  92  CYS   A HG   1 
ATOM   1991 N N    . LEU   A 1 93  ? 28.647 -3.240  7.880   1.00 9.76  ?  93  LEU   A N    1 
ATOM   1992 C CA   . LEU   A 1 93  ? 29.042 -3.989  6.692   1.00 9.39  ?  93  LEU   A CA   1 
ATOM   1993 C C    . LEU   A 1 93  ? 28.434 -3.293  5.478   1.00 9.03  ?  93  LEU   A C    1 
ATOM   1994 O O    . LEU   A 1 93  ? 27.217 -3.347  5.266   1.00 9.44  ?  93  LEU   A O    1 
ATOM   1995 C CB   . LEU   A 1 93  ? 28.551 -5.432  6.796   1.00 10.11 ?  93  LEU   A CB   1 
ATOM   1996 C CG   . LEU   A 1 93  ? 28.934 -6.322  5.614   1.00 10.29 ?  93  LEU   A CG   1 
ATOM   1997 C CD1  . LEU   A 1 93  ? 30.434 -6.583  5.591   1.00 11.32 ?  93  LEU   A CD1  1 
ATOM   1998 C CD2  . LEU   A 1 93  ? 28.157 -7.643  5.632   1.00 10.78 ?  93  LEU   A CD2  1 
ATOM   1999 H H    . LEU   A 1 93  ? 27.892 -3.490  8.215   1.00 11.68 ?  93  LEU   A H    1 
ATOM   2000 H HA   . LEU   A 1 93  ? 30.004 -3.982  6.612   1.00 11.25 ?  93  LEU   A HA   1 
ATOM   2001 H HB2  . LEU   A 1 93  ? 28.925 -5.826  7.600   1.00 12.11 ?  93  LEU   A HB2  1 
ATOM   2002 H HB3  . LEU   A 1 93  ? 27.583 -5.427  6.856   1.00 12.11 ?  93  LEU   A HB3  1 
ATOM   2003 H HG   . LEU   A 1 93  ? 28.715 -5.865  4.792   1.00 12.33 ?  93  LEU   A HG   1 
ATOM   2004 H HD11 . LEU   A 1 93  ? 30.646 -7.195  4.867   1.00 13.56 ?  93  LEU   A HD11 1 
ATOM   2005 H HD12 . LEU   A 1 93  ? 30.908 -5.744  5.457   1.00 13.56 ?  93  LEU   A HD12 1 
ATOM   2006 H HD13 . LEU   A 1 93  ? 30.707 -6.977  6.440   1.00 13.56 ?  93  LEU   A HD13 1 
ATOM   2007 H HD21 . LEU   A 1 93  ? 28.435 -8.180  4.867   1.00 12.92 ?  93  LEU   A HD21 1 
ATOM   2008 H HD22 . LEU   A 1 93  ? 28.355 -8.117  6.453   1.00 12.92 ?  93  LEU   A HD22 1 
ATOM   2009 H HD23 . LEU   A 1 93  ? 27.212 -7.452  5.572   1.00 12.92 ?  93  LEU   A HD23 1 
ATOM   2010 N N    . HIS   A 1 94  ? 29.272 -2.601  4.710   1.00 8.89  ?  94  HIS   A N    1 
ATOM   2011 C CA   . HIS   A 1 94  ? 28.836 -1.917  3.496   1.00 8.83  ?  94  HIS   A CA   1 
ATOM   2012 C C    . HIS   A 1 94  ? 28.830 -2.942  2.378   1.00 8.84  ?  94  HIS   A C    1 
ATOM   2013 O O    . HIS   A 1 94  ? 29.887 -3.458  2.018   1.00 10.24 ?  94  HIS   A O    1 
ATOM   2014 C CB   . HIS   A 1 94  ? 29.784 -0.768  3.156   1.00 8.88  ?  94  HIS   A CB   1 
ATOM   2015 C CG   . HIS   A 1 94  ? 29.789 0.317   4.177   1.00 8.98  ?  94  HIS   A CG   1 
ATOM   2016 N ND1  . HIS   A 1 94  ? 28.914 1.382   4.138   1.00 9.13  ?  94  HIS   A ND1  1 
ATOM   2017 C CD2  . HIS   A 1 94  ? 30.542 0.474   5.291   1.00 9.43  ?  94  HIS   A CD2  1 
ATOM   2018 C CE1  . HIS   A 1 94  ? 29.136 2.151   5.187   1.00 9.45  ?  94  HIS   A CE1  1 
ATOM   2019 N NE2  . HIS   A 1 94  ? 30.117 1.624   5.901   1.00 9.46  ?  94  HIS   A NE2  1 
ATOM   2020 H H    . HIS   A 1 94  ? 30.115 -2.512  4.867   1.00 10.64 ?  94  HIS   A H    1 
ATOM   2021 H HA   . HIS   A 1 94  ? 27.933 -1.575  3.612   1.00 10.57 ?  94  HIS   A HA   1 
ATOM   2022 H HB2  . HIS   A 1 94  ? 30.679 -1.116  3.081   1.00 10.63 ?  94  HIS   A HB2  1 
ATOM   2023 H HB3  . HIS   A 1 94  ? 29.503 -0.377  2.311   1.00 10.63 ?  94  HIS   A HB3  1 
ATOM   2024 H HD2  . HIS   A 1 94  ? 31.219 -0.093  5.583   1.00 11.29 ?  94  HIS   A HD2  1 
ATOM   2025 H HE1  . HIS   A 1 94  ? 28.677 2.934   5.390   1.00 11.32 ?  94  HIS   A HE1  1 
ATOM   2026 H HE2  . HIS   A 1 94  ? 30.443 1.957   6.623   1.00 11.33 ?  94  HIS   A HE2  1 
ATOM   2027 N N    . VAL   A 1 95  ? 27.652 -3.256  1.836   1.00 8.24  ?  95  VAL   A N    1 
ATOM   2028 C CA   . VAL   A 1 95  ? 27.495 -4.289  0.814   1.00 8.47  ?  95  VAL   A CA   1 
ATOM   2029 C C    . VAL   A 1 95  ? 26.932 -3.643  -0.442  1.00 8.29  ?  95  VAL   A C    1 
ATOM   2030 O O    . VAL   A 1 95  ? 25.935 -2.912  -0.370  1.00 9.03  ?  95  VAL   A O    1 
ATOM   2031 C CB   . VAL   A 1 95  ? 26.563 -5.421  1.281   1.00 9.40  ?  95  VAL   A CB   1 
ATOM   2032 C CG1  . VAL   A 1 95  ? 26.407 -6.458  0.185   1.00 9.95  ?  95  VAL   A CG1  1 
ATOM   2033 C CG2  . VAL   A 1 95  ? 27.081 -6.058  2.559   1.00 9.75  ?  95  VAL   A CG2  1 
ATOM   2034 H H    . VAL   A 1 95  ? 26.912 -2.880  2.051   1.00 9.86  ?  95  VAL   A H    1 
ATOM   2035 H HA   . VAL   A 1 95  ? 28.358 -4.672  0.596   1.00 10.14 ?  95  VAL   A HA   1 
ATOM   2036 H HB   . VAL   A 1 95  ? 25.687 -5.057  1.464   1.00 11.26 ?  95  VAL   A HB   1 
ATOM   2037 H HG11 . VAL   A 1 95  ? 26.013 -7.263  0.566   1.00 11.91 ?  95  VAL   A HG11 1 
ATOM   2038 H HG12 . VAL   A 1 95  ? 25.831 -6.110  -0.509  1.00 11.91 ?  95  VAL   A HG12 1 
ATOM   2039 H HG13 . VAL   A 1 95  ? 27.282 -6.669  -0.180  1.00 11.91 ?  95  VAL   A HG13 1 
ATOM   2040 H HG21 . VAL   A 1 95  ? 26.513 -6.805  2.795   1.00 11.68 ?  95  VAL   A HG21 1 
ATOM   2041 H HG22 . VAL   A 1 95  ? 27.990 -6.360  2.416   1.00 11.68 ?  95  VAL   A HG22 1 
ATOM   2042 H HG23 . VAL   A 1 95  ? 27.062 -5.391  3.266   1.00 11.68 ?  95  VAL   A HG23 1 
ATOM   2043 N N    A VAL   A 1 96  ? 27.557 -3.922  -1.583  0.48 8.96  ?  96  VAL   A N    1 
ATOM   2044 N N    B VAL   A 1 96  ? 27.531 -3.944  -1.592  0.52 8.34  ?  96  VAL   A N    1 
ATOM   2045 C CA   A VAL   A 1 96  ? 27.168 -3.340  -2.863  0.48 9.83  ?  96  VAL   A CA   1 
ATOM   2046 C CA   B VAL   A 1 96  ? 27.104 -3.376  -2.868  0.52 8.64  ?  96  VAL   A CA   1 
ATOM   2047 C C    A VAL   A 1 96  ? 26.376 -4.382  -3.644  0.48 10.01 ?  96  VAL   A C    1 
ATOM   2048 C C    B VAL   A 1 96  ? 26.263 -4.409  -3.611  0.52 9.06  ?  96  VAL   A C    1 
ATOM   2049 O O    A VAL   A 1 96  ? 26.948 -5.292  -4.249  0.48 10.89 ?  96  VAL   A O    1 
ATOM   2050 O O    B VAL   A 1 96  ? 26.791 -5.360  -4.192  0.52 10.11 ?  96  VAL   A O    1 
ATOM   2051 C CB   A VAL   A 1 96  ? 28.380 -2.857  -3.662  0.48 10.56 ?  96  VAL   A CB   1 
ATOM   2052 C CB   B VAL   A 1 96  ? 28.285 -2.901  -3.717  0.52 8.68  ?  96  VAL   A CB   1 
ATOM   2053 C CG1  A VAL   A 1 96  ? 27.915 -2.179  -4.945  0.48 11.16 ?  96  VAL   A CG1  1 
ATOM   2054 C CG1  B VAL   A 1 96  ? 27.764 -2.263  -4.998  0.52 8.72  ?  96  VAL   A CG1  1 
ATOM   2055 C CG2  A VAL   A 1 96  ? 29.240 -1.924  -2.828  0.48 10.93 ?  96  VAL   A CG2  1 
ATOM   2056 C CG2  B VAL   A 1 96  ? 29.148 -1.921  -2.941  0.52 9.27  ?  96  VAL   A CG2  1 
ATOM   2057 H H    A VAL   A 1 96  ? 28.233 -4.453  -1.643  0.48 10.72 ?  96  VAL   A H    1 
ATOM   2058 H H    B VAL   A 1 96  ? 28.200 -4.482  -1.665  0.52 9.98  ?  96  VAL   A H    1 
ATOM   2059 H HA   A VAL   A 1 96  ? 26.593 -2.576  -2.704  0.48 11.77 ?  96  VAL   A HA   1 
ATOM   2060 H HA   B VAL   A 1 96  ? 26.542 -2.607  -2.699  0.52 10.34 ?  96  VAL   A HA   1 
ATOM   2061 H HB   A VAL   A 1 96  ? 28.923 -3.619  -3.910  0.48 12.65 ?  96  VAL   A HB   1 
ATOM   2062 H HB   B VAL   A 1 96  ? 28.836 -3.657  -3.963  0.52 10.39 ?  96  VAL   A HB   1 
ATOM   2063 H HG11 A VAL   A 1 96  ? 28.674 -1.739  -5.362  0.48 13.37 ?  96  VAL   A HG11 1 
ATOM   2064 H HG11 B VAL   A 1 96  ? 28.494 -1.789  -5.434  0.52 10.45 ?  96  VAL   A HG11 1 
ATOM   2065 H HG12 A VAL   A 1 96  ? 27.553 -2.849  -5.546  0.48 13.37 ?  96  VAL   A HG12 1 
ATOM   2066 H HG12 B VAL   A 1 96  ? 27.428 -2.956  -5.586  0.52 10.45 ?  96  VAL   A HG12 1 
ATOM   2067 H HG13 A VAL   A 1 96  ? 27.235 -1.523  -4.728  0.48 13.37 ?  96  VAL   A HG13 1 
ATOM   2068 H HG13 B VAL   A 1 96  ? 27.056 -1.639  -4.778  0.52 10.45 ?  96  VAL   A HG13 1 
ATOM   2069 H HG21 A VAL   A 1 96  ? 29.947 -1.562  -3.385  0.48 13.09 ?  96  VAL   A HG21 1 
ATOM   2070 H HG21 B VAL   A 1 96  ? 29.848 -1.583  -3.520  0.52 11.10 ?  96  VAL   A HG21 1 
ATOM   2071 H HG22 A VAL   A 1 96  ? 28.686 -1.203  -2.488  0.48 13.09 ?  96  VAL   A HG22 1 
ATOM   2072 H HG22 B VAL   A 1 96  ? 28.592 -1.185  -2.632  0.52 11.10 ?  96  VAL   A HG22 1 
ATOM   2073 H HG23 A VAL   A 1 96  ? 29.623 -2.423  -2.090  0.48 13.09 ?  96  VAL   A HG23 1 
ATOM   2074 H HG23 B VAL   A 1 96  ? 29.538 -2.379  -2.181  0.52 11.10 ?  96  VAL   A HG23 1 
ATOM   2075 N N    A GLY   A 1 97  ? 25.054 -4.243  -3.659  0.48 10.13 ?  97  GLY   A N    1 
ATOM   2076 N N    B GLY   A 1 97  ? 24.946 -4.221  -3.611  0.52 9.57  ?  97  GLY   A N    1 
ATOM   2077 C CA   A GLY   A 1 97  ? 24.240 -5.001  -4.575  0.48 10.47 ?  97  GLY   A CA   1 
ATOM   2078 C CA   B GLY   A 1 97  ? 24.082 -4.935  -4.519  0.52 10.57 ?  97  GLY   A CA   1 
ATOM   2079 C C    A GLY   A 1 97  ? 24.241 -4.330  -5.931  0.48 10.33 ?  97  GLY   A C    1 
ATOM   2080 C C    B GLY   A 1 97  ? 24.083 -4.258  -5.875  0.52 11.29 ?  97  GLY   A C    1 
ATOM   2081 O O    A GLY   A 1 97  ? 24.552 -3.142  -6.055  0.48 10.69 ?  97  GLY   A O    1 
ATOM   2082 O O    B GLY   A 1 97  ? 24.370 -3.063  -5.991  0.52 11.62 ?  97  GLY   A O    1 
ATOM   2083 H H    A GLY   A 1 97  ? 24.612 -3.706  -3.150  0.48 12.13 ?  97  GLY   A H    1 
ATOM   2084 H H    B GLY   A 1 97  ? 24.530 -3.676  -3.088  0.52 11.46 ?  97  GLY   A H    1 
ATOM   2085 H HA2  A GLY   A 1 97  ? 24.600 -5.896  -4.665  0.48 12.54 ?  97  GLY   A HA2  1 
ATOM   2086 H HA2  B GLY   A 1 97  ? 24.393 -5.846  -4.613  0.52 12.66 ?  97  GLY   A HA2  1 
ATOM   2087 H HA3  A GLY   A 1 97  ? 23.331 -5.056  -4.241  0.48 12.54 ?  97  GLY   A HA3  1 
ATOM   2088 H HA3  B GLY   A 1 97  ? 23.172 -4.946  -4.176  0.52 12.66 ?  97  GLY   A HA3  1 
ATOM   2089 N N    A PRO   A 1 98  ? 23.899 -5.072  -6.980  0.48 10.68 ?  98  PRO   A N    1 
ATOM   2090 N N    B PRO   A 1 98  ? 23.755 -4.999  -6.929  0.52 11.41 ?  98  PRO   A N    1 
ATOM   2091 C CA   A PRO   A 1 98  ? 23.819 -4.454  -8.308  0.48 11.81 ?  98  PRO   A CA   1 
ATOM   2092 C CA   B PRO   A 1 98  ? 23.661 -4.376  -8.257  0.52 12.17 ?  98  PRO   A CA   1 
ATOM   2093 C C    A PRO   A 1 98  ? 22.692 -3.438  -8.385  0.48 12.19 ?  98  PRO   A C    1 
ATOM   2094 C C    B PRO   A 1 98  ? 22.563 -3.317  -8.305  0.52 11.82 ?  98  PRO   A C    1 
ATOM   2095 O O    A PRO   A 1 98  ? 21.585 -3.668  -7.892  0.48 11.85 ?  98  PRO   A O    1 
ATOM   2096 O O    B PRO   A 1 98  ? 21.491 -3.487  -7.721  0.52 11.07 ?  98  PRO   A O    1 
ATOM   2097 C CB   A PRO   A 1 98  ? 23.543 -5.641  -9.237  0.48 12.28 ?  98  PRO   A CB   1 
ATOM   2098 C CB   B PRO   A 1 98  ? 23.347 -5.561  -9.181  0.52 12.81 ?  98  PRO   A CB   1 
ATOM   2099 C CG   A PRO   A 1 98  ? 22.895 -6.659  -8.358  0.48 12.16 ?  98  PRO   A CG   1 
ATOM   2100 C CG   B PRO   A 1 98  ? 22.743 -6.610  -8.279  0.52 12.58 ?  98  PRO   A CG   1 
ATOM   2101 C CD   A PRO   A 1 98  ? 23.567 -6.506  -7.020  0.48 11.47 ?  98  PRO   A CD   1 
ATOM   2102 C CD   B PRO   A 1 98  ? 23.448 -6.441  -6.963  0.52 11.96 ?  98  PRO   A CD   1 
ATOM   2103 H HA   A PRO   A 1 98  ? 24.658 -4.028  -8.543  0.48 14.14 ?  98  PRO   A HA   1 
ATOM   2104 H HA   B PRO   A 1 98  ? 24.507 -3.981  -8.509  0.52 14.59 ?  98  PRO   A HA   1 
ATOM   2105 H HB2  A PRO   A 1 98  ? 22.938 -5.361  -9.947  0.48 14.71 ?  98  PRO   A HB2  1 
ATOM   2106 H HB2  B PRO   A 1 98  ? 22.715 -5.290  -9.863  0.52 15.35 ?  98  PRO   A HB2  1 
ATOM   2107 H HB3  A PRO   A 1 98  ? 24.374 -5.967  -9.599  0.48 14.71 ?  98  PRO   A HB3  1 
ATOM   2108 H HB3  B PRO   A 1 98  ? 24.169 -5.888  -9.581  0.52 15.35 ?  98  PRO   A HB3  1 
ATOM   2109 H HG2  A PRO   A 1 98  ? 21.945 -6.475  -8.289  0.48 14.57 ?  98  PRO   A HG2  1 
ATOM   2110 H HG2  B PRO   A 1 98  ? 21.791 -6.450  -8.182  0.52 15.08 ?  98  PRO   A HG2  1 
ATOM   2111 H HG3  A PRO   A 1 98  ? 23.050 -7.542  -8.721  0.48 14.57 ?  98  PRO   A HG3  1 
ATOM   2112 H HG3  B PRO   A 1 98  ? 22.908 -7.494  -8.645  0.52 15.08 ?  98  PRO   A HG3  1 
ATOM   2113 H HD2  A PRO   A 1 98  ? 22.955 -6.734  -6.304  0.48 13.74 ?  98  PRO   A HD2  1 
ATOM   2114 H HD2  B PRO   A 1 98  ? 22.858 -6.686  -6.230  0.52 14.33 ?  98  PRO   A HD2  1 
ATOM   2115 H HD3  A PRO   A 1 98  ? 24.379 -7.034  -6.983  0.48 13.74 ?  98  PRO   A HD3  1 
ATOM   2116 H HD3  B PRO   A 1 98  ? 24.268 -6.958  -6.946  0.52 14.33 ?  98  PRO   A HD3  1 
ATOM   2117 N N    A ASN   A 1 99  ? 22.987 -2.305  -9.016  0.48 13.28 ?  99  ASN   A N    1 
ATOM   2118 N N    B ASN   A 1 99  ? 22.845 -2.206  -9.007  0.52 12.11 ?  99  ASN   A N    1 
ATOM   2119 C CA   A ASN   A 1 99  ? 21.988 -1.284  -9.305  0.48 14.93 ?  99  ASN   A CA   1 
ATOM   2120 C CA   B ASN   A 1 99  ? 21.896 -1.102  -9.212  0.52 12.62 ?  99  ASN   A CA   1 
ATOM   2121 C C    A ASN   A 1 99  ? 21.415 -1.564  -10.691 0.48 16.04 ?  99  ASN   A C    1 
ATOM   2122 C C    B ASN   A 1 99  ? 21.427 -1.145  -10.666 0.52 12.82 ?  99  ASN   A C    1 
ATOM   2123 O O    A ASN   A 1 99  ? 22.135 -1.507  -11.697 0.48 16.17 ?  99  ASN   A O    1 
ATOM   2124 O O    B ASN   A 1 99  ? 22.139 -0.709  -11.579 0.52 12.85 ?  99  ASN   A O    1 
ATOM   2125 C CB   A ASN   A 1 99  ? 22.623 0.107   -9.235  0.48 15.99 ?  99  ASN   A CB   1 
ATOM   2126 C CB   B ASN   A 1 99  ? 22.522 0.253   -8.865  0.52 12.42 ?  99  ASN   A CB   1 
ATOM   2127 C CG   A ASN   A 1 99  ? 21.591 1.230   -9.189  0.48 17.19 ?  99  ASN   A CG   1 
ATOM   2128 C CG   B ASN   A 1 99  ? 21.522 1.424   -8.970  0.52 12.99 ?  99  ASN   A CG   1 
ATOM   2129 O OD1  A ASN   A 1 99  ? 20.554 1.167   -9.855  0.48 18.07 ?  99  ASN   A OD1  1 
ATOM   2130 O OD1  B ASN   A 1 99  ? 20.637 1.438   -9.831  0.52 14.04 ?  99  ASN   A OD1  1 
ATOM   2131 N ND2  A ASN   A 1 99  ? 21.880 2.270   -8.395  0.48 17.95 ?  99  ASN   A ND2  1 
ATOM   2132 N ND2  B ASN   A 1 99  ? 21.678 2.412   -8.088  0.52 13.75 ?  99  ASN   A ND2  1 
ATOM   2133 H H    A ASN   A 1 99  ? 23.773 -2.093  -9.285  0.48 15.91 ?  99  ASN   A H    1 
ATOM   2134 H H    B ASN   A 1 99  ? 23.606 -2.065  -9.376  0.52 14.51 ?  99  ASN   A H    1 
ATOM   2135 H HA   A ASN   A 1 99  ? 21.267 -1.320  -8.648  0.48 17.90 ?  99  ASN   A HA   1 
ATOM   2136 H HA   B ASN   A 1 99  ? 21.127 -1.229  -8.630  0.52 15.12 ?  99  ASN   A HA   1 
ATOM   2137 H HB2  A ASN   A 1 99  ? 23.173 0.174   -8.433  0.48 19.16 ?  99  ASN   A HB2  1 
ATOM   2138 H HB2  B ASN   A 1 99  ? 22.861 0.229   -7.953  0.52 14.88 ?  99  ASN   A HB2  1 
ATOM   2139 H HB3  A ASN   A 1 99  ? 23.170 0.251   -10.020 0.48 19.16 ?  99  ASN   A HB3  1 
ATOM   2140 H HB3  B ASN   A 1 99  ? 23.251 0.426   -9.481  0.52 14.88 ?  99  ASN   A HB3  1 
ATOM   2141 H HD21 A ASN   A 1 99  ? 21.336 2.933   -8.322  0.48 21.51 ?  99  ASN   A HD21 1 
ATOM   2142 H HD21 B ASN   A 1 99  ? 21.148 3.089   -8.100  0.52 16.48 ?  99  ASN   A HD21 1 
ATOM   2143 H HD22 A ASN   A 1 99  ? 22.619 2.280   -7.940  0.48 21.51 ?  99  ASN   A HD22 1 
ATOM   2144 H HD22 B ASN   A 1 99  ? 22.309 2.372   -7.501  0.52 16.48 ?  99  ASN   A HD22 1 
ATOM   2145 N N    A VAL   A 1 100 ? 20.123 -1.896  -10.737 0.48 17.82 ?  100 VAL   A N    1 
ATOM   2146 N N    B VAL   A 1 100 ? 20.213 -1.669  -10.864 0.52 13.82 ?  100 VAL   A N    1 
ATOM   2147 C CA   A VAL   A 1 100 ? 19.481 -2.184  -12.013 0.48 19.32 ?  100 VAL   A CA   1 
ATOM   2148 C CA   B VAL   A 1 100 ? 19.667 -1.834  -12.207 0.52 15.37 ?  100 VAL   A CA   1 
ATOM   2149 C C    A VAL   A 1 100 ? 19.394 -0.926  -12.861 0.48 20.47 ?  100 VAL   A C    1 
ATOM   2150 C C    B VAL   A 1 100 ? 19.408 -0.485  -12.869 0.52 14.02 ?  100 VAL   A C    1 
ATOM   2151 O O    A VAL   A 1 100 ? 19.494 -0.992  -14.092 0.48 21.09 ?  100 VAL   A O    1 
ATOM   2152 O O    B VAL   A 1 100 ? 19.437 -0.376  -14.100 0.52 14.69 ?  100 VAL   A O    1 
ATOM   2153 C CB   A VAL   A 1 100 ? 18.102 -2.834  -11.788 0.48 19.81 ?  100 VAL   A CB   1 
ATOM   2154 C CB   B VAL   A 1 100 ? 18.413 -2.733  -12.164 0.52 18.43 ?  100 VAL   A CB   1 
ATOM   2155 C CG1  A VAL   A 1 100 ? 17.348 -2.967  -13.104 0.48 19.70 ?  100 VAL   A CG1  1 
ATOM   2156 C CG1  B VAL   A 1 100 ? 17.940 -3.080  -13.568 0.52 19.92 ?  100 VAL   A CG1  1 
ATOM   2157 C CG2  A VAL   A 1 100 ? 18.273 -4.191  -11.134 0.48 20.50 ?  100 VAL   A CG2  1 
ATOM   2158 C CG2  B VAL   A 1 100 ? 18.699 -4.008  -11.380 0.52 19.18 ?  100 VAL   A CG2  1 
ATOM   2159 H H    A VAL   A 1 100 ? 19.604 -1.948  -10.053 0.48 21.36 ?  100 VAL   A H    1 
ATOM   2160 H H    B VAL   A 1 100 ? 19.694 -1.945  -10.231 0.52 16.56 ?  100 VAL   A H    1 
ATOM   2161 H HA   A VAL   A 1 100 ? 20.031 -2.814  -12.497 0.48 23.17 ?  100 VAL   A HA   1 
ATOM   2162 H HA   B VAL   A 1 100 ? 20.324 -2.296  -12.743 0.52 18.43 ?  100 VAL   A HA   1 
ATOM   2163 H HB   A VAL   A 1 100 ? 17.579 -2.272  -11.197 0.48 23.75 ?  100 VAL   A HB   1 
ATOM   2164 H HB   B VAL   A 1 100 ? 17.693 -2.265  -11.714 0.52 22.09 ?  100 VAL   A HB   1 
ATOM   2165 H HG11 A VAL   A 1 100 ? 16.601 -3.574  -12.976 0.48 23.62 ?  100 VAL   A HG11 1 
ATOM   2166 H HG11 B VAL   A 1 100 ? 17.194 -3.701  -13.508 0.52 23.89 ?  100 VAL   A HG11 1 
ATOM   2167 H HG12 A VAL   A 1 100 ? 17.020 -2.096  -13.377 0.48 23.62 ?  100 VAL   A HG12 1 
ATOM   2168 H HG12 B VAL   A 1 100 ? 17.658 -2.270  -14.016 0.52 23.89 ?  100 VAL   A HG12 1 
ATOM   2169 H HG13 A VAL   A 1 100 ? 17.947 -3.323  -13.779 0.48 23.62 ?  100 VAL   A HG13 1 
ATOM   2170 H HG13 B VAL   A 1 100 ? 18.671 -3.494  -14.054 0.52 23.89 ?  100 VAL   A HG13 1 
ATOM   2171 H HG21 A VAL   A 1 100 ? 17.402 -4.595  -11.017 0.48 24.58 ?  100 VAL   A HG21 1 
ATOM   2172 H HG21 B VAL   A 1 100 ? 17.979 -4.643  -11.530 0.52 23.00 ?  100 VAL   A HG21 1 
ATOM   2173 H HG22 A VAL   A 1 100 ? 18.825 -4.749  -11.706 0.48 24.58 ?  100 VAL   A HG22 1 
ATOM   2174 H HG22 B VAL   A 1 100 ? 19.539 -4.384  -11.685 0.52 23.00 ?  100 VAL   A HG22 1 
ATOM   2175 H HG23 A VAL   A 1 100 ? 18.705 -4.073  -10.273 0.48 24.58 ?  100 VAL   A HG23 1 
ATOM   2176 H HG23 B VAL   A 1 100 ? 18.755 -3.794  -10.435 0.52 23.00 ?  100 VAL   A HG23 1 
ATOM   2177 N N    A ASN   A 1 101 ? 19.211 0.234   -12.225 0.48 21.70 ?  101 ASN   A N    1 
ATOM   2178 N N    B ASN   A 1 101 ? 19.159 0.566   -12.084 0.52 13.88 ?  101 ASN   A N    1 
ATOM   2179 C CA   A ASN   A 1 101 ? 19.173 1.508   -12.933 0.48 22.80 ?  101 ASN   A CA   1 
ATOM   2180 C CA   B ASN   A 1 101 ? 18.988 1.884   -12.689 0.52 14.17 ?  101 ASN   A CA   1 
ATOM   2181 C C    A ASN   A 1 101 ? 20.534 1.918   -13.484 0.48 23.83 ?  101 ASN   A C    1 
ATOM   2182 C C    B ASN   A 1 101 ? 20.298 2.444   -13.226 0.52 15.12 ?  101 ASN   A C    1 
ATOM   2183 O O    A ASN   A 1 101 ? 20.618 2.925   -14.195 0.48 24.76 ?  101 ASN   A O    1 
ATOM   2184 O O    B ASN   A 1 101 ? 20.273 3.379   -14.036 0.52 16.29 ?  101 ASN   A O    1 
ATOM   2185 C CB   A ASN   A 1 101 ? 18.591 2.585   -12.012 0.48 22.79 ?  101 ASN   A CB   1 
ATOM   2186 C CB   B ASN   A 1 101 ? 18.322 2.839   -11.701 0.52 14.32 ?  101 ASN   A CB   1 
ATOM   2187 C CG   A ASN   A 1 101 ? 17.226 2.197   -11.464 0.48 22.71 ?  101 ASN   A CG   1 
ATOM   2188 C CG   B ASN   A 1 101 ? 16.900 2.431   -11.388 0.52 14.63 ?  101 ASN   A CG   1 
ATOM   2189 O OD1  A ASN   A 1 101 ? 16.407 1.614   -12.175 0.48 22.82 ?  101 ASN   A OD1  1 
ATOM   2190 O OD1  B ASN   A 1 101 ? 16.188 1.924   -12.259 0.52 15.36 ?  101 ASN   A OD1  1 
ATOM   2191 N ND2  A ASN   A 1 101 ? 16.982 2.501   -10.192 0.48 22.72 ?  101 ASN   A ND2  1 
ATOM   2192 N ND2  B ASN   A 1 101 ? 16.479 2.631   -10.144 0.52 14.53 ?  101 ASN   A ND2  1 
ATOM   2193 H H    A ASN   A 1 101 ? 19.099 0.307   -11.377 0.48 26.01 ?  101 ASN   A H    1 
ATOM   2194 H H    B ASN   A 1 101 ? 19.075 0.541   -11.228 0.52 16.64 ?  101 ASN   A H    1 
ATOM   2195 H HA   A ASN   A 1 101 ? 18.575 1.427   -13.687 0.48 27.34 ?  101 ASN   A HA   1 
ATOM   2196 H HA   B ASN   A 1 101 ? 18.390 1.795   -13.444 0.52 16.97 ?  101 ASN   A HA   1 
ATOM   2197 H HB2  A ASN   A 1 101 ? 19.184 2.726   -11.258 0.48 27.32 ?  101 ASN   A HB2  1 
ATOM   2198 H HB2  B ASN   A 1 101 ? 18.822 2.845   -10.871 0.52 17.16 ?  101 ASN   A HB2  1 
ATOM   2199 H HB3  A ASN   A 1 101 ? 18.487 3.415   -12.511 0.48 27.32 ?  101 ASN   A HB3  1 
ATOM   2200 H HB3  B ASN   A 1 101 ? 18.301 3.730   -12.085 0.52 17.16 ?  101 ASN   A HB3  1 
ATOM   2201 H HD21 A ASN   A 1 101 ? 16.222 2.301   -9.838  0.48 27.24 ?  101 ASN   A HD21 1 
ATOM   2202 H HD21 B ASN   A 1 101 ? 15.675 2.414   -9.917  0.52 17.41 ?  101 ASN   A HD21 1 
ATOM   2203 H HD22 A ASN   A 1 101 ? 17.580 2.901   -9.722  0.48 27.24 ?  101 ASN   A HD22 1 
ATOM   2204 H HD22 B ASN   A 1 101 ? 17.004 2.986   -9.563  0.52 17.41 ?  101 ASN   A HD22 1 
ATOM   2205 N N    A LYS   A 1 102 ? 21.592 1.166   -13.181 0.48 24.12 ?  102 LYS   A N    1 
ATOM   2206 N N    B LYS   A 1 102 ? 21.434 1.885   -12.799 0.52 16.51 ?  102 LYS   A N    1 
ATOM   2207 C CA   A LYS   A 1 102 ? 22.894 1.338   -13.807 0.48 24.10 ?  102 LYS   A CA   1 
ATOM   2208 C CA   B LYS   A 1 102 ? 22.740 2.170   -13.376 0.52 18.38 ?  102 LYS   A CA   1 
ATOM   2209 C C    A LYS   A 1 102 ? 23.205 0.229   -14.804 0.48 23.47 ?  102 LYS   A C    1 
ATOM   2210 C C    B LYS   A 1 102 ? 23.134 1.168   -14.454 0.52 18.72 ?  102 LYS   A C    1 
ATOM   2211 O O    A LYS   A 1 102 ? 24.309 0.202   -15.356 0.48 23.49 ?  102 LYS   A O    1 
ATOM   2212 O O    B LYS   A 1 102 ? 24.201 1.317   -15.060 0.52 19.16 ?  102 LYS   A O    1 
ATOM   2213 C CB   A LYS   A 1 102 ? 24.002 1.380   -12.746 0.48 24.79 ?  102 LYS   A CB   1 
ATOM   2214 C CB   B LYS   A 1 102 ? 23.813 2.168   -12.279 0.52 20.21 ?  102 LYS   A CB   1 
ATOM   2215 C CG   A LYS   A 1 102 ? 23.943 2.563   -11.790 0.48 25.34 ?  102 LYS   A CG   1 
ATOM   2216 C CG   B LYS   A 1 102 ? 23.659 3.250   -11.223 0.52 21.96 ?  102 LYS   A CG   1 
ATOM   2217 C CD   A LYS   A 1 102 ? 25.101 2.509   -10.798 0.48 25.96 ?  102 LYS   A CD   1 
ATOM   2218 C CD   B LYS   A 1 102 ? 24.649 3.029   -10.085 0.52 23.58 ?  102 LYS   A CD   1 
ATOM   2219 C CE   A LYS   A 1 102 ? 25.049 3.653   -9.796  0.48 26.51 ?  102 LYS   A CE   1 
ATOM   2220 C CE   B LYS   A 1 102 ? 24.732 4.227   -9.156  0.52 24.52 ?  102 LYS   A CE   1 
ATOM   2221 N NZ   A LYS   A 1 102 ? 26.140 3.547   -8.782  0.48 26.76 ?  102 LYS   A NZ   1 
ATOM   2222 N NZ   B LYS   A 1 102 ? 25.690 3.992   -8.037  0.52 24.96 ?  102 LYS   A NZ   1 
ATOM   2223 H H    A LYS   A 1 102 ? 21.573 0.531   -12.604 0.48 28.92 ?  102 LYS   A H    1 
ATOM   2224 H H    B LYS   A 1 102 ? 21.469 1.316   -12.150 0.52 19.79 ?  102 LYS   A H    1 
ATOM   2225 H HA   A LYS   A 1 102 ? 22.905 2.189   -14.276 0.48 28.90 ?  102 LYS   A HA   1 
ATOM   2226 H HA   B LYS   A 1 102 ? 22.725 3.046   -13.779 0.52 22.03 ?  102 LYS   A HA   1 
ATOM   2227 H HB2  A LYS   A 1 102 ? 23.949 0.573   -12.212 0.48 29.72 ?  102 LYS   A HB2  1 
ATOM   2228 H HB2  B LYS   A 1 102 ? 23.791 1.313   -11.821 0.52 24.23 ?  102 LYS   A HB2  1 
ATOM   2229 H HB3  A LYS   A 1 102 ? 24.860 1.416   -13.198 0.48 29.72 ?  102 LYS   A HB3  1 
ATOM   2230 H HB3  B LYS   A 1 102 ? 24.681 2.291   -12.694 0.52 24.23 ?  102 LYS   A HB3  1 
ATOM   2231 H HG2  A LYS   A 1 102 ? 24.010 3.390   -12.294 0.48 30.38 ?  102 LYS   A HG2  1 
ATOM   2232 H HG2  B LYS   A 1 102 ? 23.837 4.118   -11.619 0.52 26.33 ?  102 LYS   A HG2  1 
ATOM   2233 H HG3  A LYS   A 1 102 ? 23.112 2.536   -11.292 0.48 30.38 ?  102 LYS   A HG3  1 
ATOM   2234 H HG3  B LYS   A 1 102 ? 22.759 3.222   -10.858 0.52 26.33 ?  102 LYS   A HG3  1 
ATOM   2235 H HD2  A LYS   A 1 102 ? 25.060 1.674   -10.306 0.48 31.13 ?  102 LYS   A HD2  1 
ATOM   2236 H HD2  B LYS   A 1 102 ? 24.366 2.262   -9.561  0.52 28.28 ?  102 LYS   A HD2  1 
ATOM   2237 H HD3  A LYS   A 1 102 ? 25.940 2.570   -11.283 0.48 31.13 ?  102 LYS   A HD3  1 
ATOM   2238 H HD3  B LYS   A 1 102 ? 25.529 2.869   -10.457 0.52 28.28 ?  102 LYS   A HD3  1 
ATOM   2239 H HE2  A LYS   A 1 102 ? 25.153 4.496   -10.266 0.48 31.78 ?  102 LYS   A HE2  1 
ATOM   2240 H HE2  B LYS   A 1 102 ? 25.036 4.998   -9.658  0.52 29.40 ?  102 LYS   A HE2  1 
ATOM   2241 H HE3  A LYS   A 1 102 ? 24.198 3.633   -9.330  0.48 31.78 ?  102 LYS   A HE3  1 
ATOM   2242 H HE3  B LYS   A 1 102 ? 23.857 4.398   -8.775  0.52 29.40 ?  102 LYS   A HE3  1 
ATOM   2243 H HZ1  A LYS   A 1 102 ? 26.089 4.225   -8.208  0.48 32.09 ?  102 LYS   A HZ1  1 
ATOM   2244 H HZ1  B LYS   A 1 102 ? 25.722 4.706   -7.509  0.52 29.93 ?  102 LYS   A HZ1  1 
ATOM   2245 H HZ2  A LYS   A 1 102 ? 26.064 2.782   -8.333  0.48 32.09 ?  102 LYS   A HZ2  1 
ATOM   2246 H HZ2  B LYS   A 1 102 ? 25.430 3.288   -7.557  0.52 29.93 ?  102 LYS   A HZ2  1 
ATOM   2247 H HZ3  A LYS   A 1 102 ? 26.933 3.568   -9.185  0.48 32.09 ?  102 LYS   A HZ3  1 
ATOM   2248 H HZ3  B LYS   A 1 102 ? 26.504 3.835   -8.361  0.52 29.93 ?  102 LYS   A HZ3  1 
ATOM   2249 N N    A GLY   A 1 103 ? 22.273 -0.695  -15.030 0.48 23.39 ?  103 GLY   A N    1 
ATOM   2250 N N    B GLY   A 1 103 ? 22.310 0.152   -14.702 0.52 19.49 ?  103 GLY   A N    1 
ATOM   2251 C CA   A GLY   A 1 103 ? 22.495 -1.785  -15.960 0.48 22.91 ?  103 GLY   A CA   1 
ATOM   2252 C CA   B GLY   A 1 103 ? 22.662 -0.879  -15.656 0.52 20.77 ?  103 GLY   A CA   1 
ATOM   2253 C C    A GLY   A 1 103 ? 23.314 -2.938  -15.420 0.48 22.32 ?  103 GLY   A C    1 
ATOM   2254 C C    B GLY   A 1 103 ? 23.561 -1.964  -15.121 0.52 21.64 ?  103 GLY   A C    1 
ATOM   2255 O O    A GLY   A 1 103 ? 23.801 -3.757  -16.205 0.48 23.43 ?  103 GLY   A O    1 
ATOM   2256 O O    B GLY   A 1 103 ? 24.214 -2.653  -15.913 0.52 22.42 ?  103 GLY   A O    1 
ATOM   2257 H H    A GLY   A 1 103 ? 21.501 -0.702  -14.656 0.48 28.04 ?  103 GLY   A H    1 
ATOM   2258 H H    B GLY   A 1 103 ? 21.546 0.036   -14.326 0.52 23.36 ?  103 GLY   A H    1 
ATOM   2259 H HA2  A GLY   A 1 103 ? 21.634 -2.139  -16.232 0.48 27.47 ?  103 GLY   A HA2  1 
ATOM   2260 H HA2  B GLY   A 1 103 ? 21.857 -1.300  -15.989 0.52 24.90 ?  103 GLY   A HA2  1 
ATOM   2261 H HA3  A GLY   A 1 103 ? 22.934 -1.430  -16.753 0.48 27.47 ?  103 GLY   A HA3  1 
ATOM   2262 H HA3  B GLY   A 1 103 ? 23.131 -0.475  -16.394 0.52 24.90 ?  103 GLY   A HA3  1 
ATOM   2263 N N    A GLU   A 1 104 ? 23.465 -3.043  -14.104 0.48 20.48 ?  104 GLU   A N    1 
ATOM   2264 N N    B GLU   A 1 104 ? 23.615 -2.147  -13.805 0.52 21.53 ?  104 GLU   A N    1 
ATOM   2265 C CA   A GLU   A 1 104 ? 24.361 -4.032  -13.520 0.48 18.87 ?  104 GLU   A CA   1 
ATOM   2266 C CA   B GLU   A 1 104 ? 24.485 -3.152  -13.215 0.52 21.76 ?  104 GLU   A CA   1 
ATOM   2267 C C    A GLU   A 1 104 ? 23.685 -5.399  -13.399 0.48 19.25 ?  104 GLU   A C    1 
ATOM   2268 C C    B GLU   A 1 104 ? 23.795 -4.511  -13.204 0.52 22.89 ?  104 GLU   A C    1 
ATOM   2269 O O    A GLU   A 1 104 ? 22.467 -5.509  -13.230 0.48 19.19 ?  104 GLU   A O    1 
ATOM   2270 O O    B GLU   A 1 104 ? 22.564 -4.608  -13.179 0.52 23.27 ?  104 GLU   A O    1 
ATOM   2271 C CB   A GLU   A 1 104 ? 24.877 -3.541  -12.164 0.48 17.55 ?  104 GLU   A CB   1 
ATOM   2272 C CB   B GLU   A 1 104 ? 24.915 -2.723  -11.809 0.52 21.37 ?  104 GLU   A CB   1 
ATOM   2273 C CG   A GLU   A 1 104 ? 25.768 -2.304  -12.303 0.48 16.54 ?  104 GLU   A CG   1 
ATOM   2274 C CG   B GLU   A 1 104 ? 25.799 -1.477  -11.833 0.52 21.32 ?  104 GLU   A CG   1 
ATOM   2275 C CD   A GLU   A 1 104 ? 26.129 -1.625  -10.996 0.48 16.03 ?  104 GLU   A CD   1 
ATOM   2276 C CD   B GLU   A 1 104 ? 26.121 -0.933  -10.459 0.52 21.24 ?  104 GLU   A CD   1 
ATOM   2277 O OE1  A GLU   A 1 104 ? 25.558 -1.976  -9.944  0.48 15.13 ?  104 GLU   A OE1  1 
ATOM   2278 O OE1  B GLU   A 1 104 ? 25.513 -1.401  -9.476  0.52 20.27 ?  104 GLU   A OE1  1 
ATOM   2279 O OE2  A GLU   A 1 104 ? 26.989 -0.716  -11.043 0.48 16.11 -1 104 GLU   A OE2  1 
ATOM   2280 O OE2  B GLU   A 1 104 ? 26.988 -0.035  -10.369 0.52 22.36 -1 104 GLU   A OE2  1 
ATOM   2281 H H    A GLU   A 1 104 ? 23.056 -2.548  -13.532 0.48 24.56 ?  104 GLU   A H    1 
ATOM   2282 H H    B GLU   A 1 104 ? 23.150 -1.710  -13.226 0.52 25.81 ?  104 GLU   A H    1 
ATOM   2283 H HA   A GLU   A 1 104 ? 25.129 -4.127  -14.109 0.48 22.61 ?  104 GLU   A HA   1 
ATOM   2284 H HA   B GLU   A 1 104 ? 25.280 -3.241  -13.749 0.52 26.09 ?  104 GLU   A HA   1 
ATOM   2285 H HB2  A GLU   A 1 104 ? 24.123 -3.310  -11.605 0.48 21.04 ?  104 GLU   A HB2  1 
ATOM   2286 H HB2  B GLU   A 1 104 ? 24.126 -2.524  -11.281 0.52 25.62 ?  104 GLU   A HB2  1 
ATOM   2287 H HB3  A GLU   A 1 104 ? 25.400 -4.247  -11.757 0.48 21.04 ?  104 GLU   A HB3  1 
ATOM   2288 H HB3  B GLU   A 1 104 ? 25.420 -3.441  -11.390 0.52 25.62 ?  104 GLU   A HB3  1 
ATOM   2289 H HG2  A GLU   A 1 104 ? 26.591 -2.564  -12.744 0.48 19.83 ?  104 GLU   A HG2  1 
ATOM   2290 H HG2  B GLU   A 1 104 ? 26.643 -1.698  -12.250 0.52 25.57 ?  104 GLU   A HG2  1 
ATOM   2291 H HG3  A GLU   A 1 104 ? 25.302 -1.645  -12.839 0.48 19.83 ?  104 GLU   A HG3  1 
ATOM   2292 H HG3  B GLU   A 1 104 ? 25.347 -0.784  -12.339 0.52 25.57 ?  104 GLU   A HG3  1 
ATOM   2293 N N    A ASP   A 1 105 ? 24.504 -6.445  -13.479 0.48 20.20 ?  105 ASP   A N    1 
ATOM   2294 N N    B ASP   A 1 105 ? 24.611 -5.565  -13.237 0.52 23.50 ?  105 ASP   A N    1 
ATOM   2295 C CA   A ASP   A 1 105 ? 24.010 -7.814  -13.594 0.48 21.65 ?  105 ASP   A CA   1 
ATOM   2296 C CA   B ASP   A 1 105 ? 24.136 -6.919  -13.502 0.52 24.05 ?  105 ASP   A CA   1 
ATOM   2297 C C    A ASP   A 1 105 ? 23.305 -8.245  -12.311 0.48 20.14 ?  105 ASP   A C    1 
ATOM   2298 C C    B ASP   A 1 105 ? 23.423 -7.491  -12.281 0.52 23.71 ?  105 ASP   A C    1 
ATOM   2299 O O    A ASP   A 1 105 ? 23.935 -8.351  -11.253 0.48 18.19 ?  105 ASP   A O    1 
ATOM   2300 O O    B ASP   A 1 105 ? 24.033 -7.667  -11.222 0.52 23.51 ?  105 ASP   A O    1 
ATOM   2301 C CB   A ASP   A 1 105 ? 25.188 -8.742  -13.882 0.48 24.48 ?  105 ASP   A CB   1 
ATOM   2302 C CB   B ASP   A 1 105 ? 25.322 -7.800  -13.889 0.52 25.37 ?  105 ASP   A CB   1 
ATOM   2303 C CG   A ASP   A 1 105 ? 24.758 -10.173 -14.150 0.48 26.82 ?  105 ASP   A CG   1 
ATOM   2304 C CG   B ASP   A 1 105 ? 24.919 -9.227  -14.162 0.52 26.25 ?  105 ASP   A CG   1 
ATOM   2305 O OD1  A ASP   A 1 105 ? 23.541 -10.414 -14.276 0.48 27.40 ?  105 ASP   A OD1  1 
ATOM   2306 O OD1  B ASP   A 1 105 ? 23.709 -9.480  -14.343 0.52 26.13 ?  105 ASP   A OD1  1 
ATOM   2307 O OD2  A ASP   A 1 105 ? 25.639 -11.058 -14.231 0.48 28.06 -1 105 ASP   A OD2  1 
ATOM   2308 O OD2  B ASP   A 1 105 ? 25.818 -10.092 -14.210 0.52 27.13 -1 105 ASP   A OD2  1 
ATOM   2309 H H    A ASP   A 1 105 ? 25.362 -6.376  -13.476 0.48 24.21 ?  105 ASP   A H    1 
ATOM   2310 H H    B ASP   A 1 105 ? 25.466 -5.528  -13.113 0.52 28.18 ?  105 ASP   A H    1 
ATOM   2311 H HA   A ASP   A 1 105 ? 23.379 -7.866  -14.329 0.48 25.95 ?  105 ASP   A HA   1 
ATOM   2312 H HA   B ASP   A 1 105 ? 23.515 -6.912  -14.244 0.52 28.83 ?  105 ASP   A HA   1 
ATOM   2313 H HB2  A ASP   A 1 105 ? 25.667 -8.405  -14.659 0.48 29.35 ?  105 ASP   A HB2  1 
ATOM   2314 H HB2  B ASP   A 1 105 ? 25.714 -7.475  -14.712 0.52 30.42 ?  105 ASP   A HB2  1 
ATOM   2315 H HB3  A ASP   A 1 105 ? 25.776 -8.744  -13.111 0.48 29.35 ?  105 ASP   A HB3  1 
ATOM   2316 H HB3  B ASP   A 1 105 ? 25.984 -7.786  -13.177 0.52 30.42 ?  105 ASP   A HB3  1 
ATOM   2317 N N    A ILE   A 1 106 ? 22.000 -8.515  -12.409 0.48 20.39 ?  106 ILE   A N    1 
ATOM   2318 N N    B ILE   A 1 106 ? 22.140 -7.823  -12.447 0.52 23.99 ?  106 ILE   A N    1 
ATOM   2319 C CA   A ILE   A 1 106 ? 21.240 -8.953  -11.245 0.48 20.62 ?  106 ILE   A CA   1 
ATOM   2320 C CA   B ILE   A 1 106 ? 21.333 -8.355  -11.351 0.52 24.02 ?  106 ILE   A CA   1 
ATOM   2321 C C    A ILE   A 1 106 ? 21.791 -10.253 -10.688 0.48 20.46 ?  106 ILE   A C    1 
ATOM   2322 C C    B ILE   A 1 106 ? 21.824 -9.717  -10.859 0.52 23.08 ?  106 ILE   A C    1 
ATOM   2323 O O    A ILE   A 1 106 ? 21.607 -10.544 -9.501  0.48 19.95 ?  106 ILE   A O    1 
ATOM   2324 O O    B ILE   A 1 106 ? 21.543 -10.088 -9.714  0.52 22.31 ?  106 ILE   A O    1 
ATOM   2325 C CB   A ILE   A 1 106 ? 19.733 -9.045  -11.575 0.48 21.61 ?  106 ILE   A CB   1 
ATOM   2326 C CB   B ILE   A 1 106 ? 19.843 -8.365  -11.761 0.52 25.04 ?  106 ILE   A CB   1 
ATOM   2327 C CG1  A ILE   A 1 106 ? 18.902 -9.054  -10.290 0.48 22.43 ?  106 ILE   A CG1  1 
ATOM   2328 C CG1  B ILE   A 1 106 ? 18.952 -8.905  -10.637 0.52 25.63 ?  106 ILE   A CG1  1 
ATOM   2329 C CG2  A ILE   A 1 106 ? 19.437 -10.282 -12.408 0.48 21.65 ?  106 ILE   A CG2  1 
ATOM   2330 C CG2  B ILE   A 1 106 ? 19.640 -9.180  -13.026 0.52 25.29 ?  106 ILE   A CG2  1 
ATOM   2331 C CD1  A ILE   A 1 106 ? 19.064 -7.800  -9.450  0.48 22.88 ?  106 ILE   A CD1  1 
ATOM   2332 C CD1  B ILE   A 1 106 ? 19.011 -8.095  -9.364  0.52 25.82 ?  106 ILE   A CD1  1 
ATOM   2333 H H    A ILE   A 1 106 ? 21.545 -8.443  -13.129 0.48 24.45 ?  106 ILE   A H    1 
ATOM   2334 H H    B ILE   A 1 106 ? 21.716 -7.746  -13.189 0.52 28.77 ?  106 ILE   A H    1 
ATOM   2335 H HA   A ILE   A 1 106 ? 21.354 -8.289  -10.551 0.48 24.72 ?  106 ILE   A HA   1 
ATOM   2336 H HA   B ILE   A 1 106 ? 21.417 -7.752  -10.606 0.52 28.81 ?  106 ILE   A HA   1 
ATOM   2337 H HB   A ILE   A 1 106 ? 19.490 -8.261  -12.091 0.48 25.91 ?  106 ILE   A HB   1 
ATOM   2338 H HB   B ILE   A 1 106 ? 19.577 -7.451  -11.944 0.52 30.03 ?  106 ILE   A HB   1 
ATOM   2339 H HG12 A ILE   A 1 106 ? 17.965 -9.132  -10.526 0.48 26.89 ?  106 ILE   A HG12 1 
ATOM   2340 H HG12 B ILE   A 1 106 ? 18.030 -8.894  -10.944 0.52 30.73 ?  106 ILE   A HG12 1 
ATOM   2341 H HG13 A ILE   A 1 106 ? 19.171 -9.810  -9.747  0.48 26.89 ?  106 ILE   A HG13 1 
ATOM   2342 H HG13 B ILE   A 1 106 ? 19.211 -9.814  -10.427 0.52 30.73 ?  106 ILE   A HG13 1 
ATOM   2343 H HG21 A ILE   A 1 106 ? 18.555 -10.189 -12.799 0.48 25.95 ?  106 ILE   A HG21 1 
ATOM   2344 H HG21 B ILE   A 1 106 ? 18.690 -9.317  -13.159 0.52 30.32 ?  106 ILE   A HG21 1 
ATOM   2345 H HG22 A ILE   A 1 106 ? 20.105 -10.354 -13.107 0.48 25.95 ?  106 ILE   A HG22 1 
ATOM   2346 H HG22 B ILE   A 1 106 ? 20.012 -8.695  -13.778 0.52 30.32 ?  106 ILE   A HG22 1 
ATOM   2347 H HG23 A ILE   A 1 106 ? 19.468 -11.063 -11.836 0.48 25.95 ?  106 ILE   A HG23 1 
ATOM   2348 H HG23 B ILE   A 1 106 ? 20.086 -10.035 -12.927 0.52 30.32 ?  106 ILE   A HG23 1 
ATOM   2349 H HD11 A ILE   A 1 106 ? 18.308 -7.726  -8.850  0.48 27.43 ?  106 ILE   A HD11 1 
ATOM   2350 H HD11 B ILE   A 1 106 ? 18.332 -8.418  -8.752  0.52 30.96 ?  106 ILE   A HD11 1 
ATOM   2351 H HD12 A ILE   A 1 106 ? 19.887 -7.863  -8.939  0.48 27.43 ?  106 ILE   A HD12 1 
ATOM   2352 H HD12 B ILE   A 1 106 ? 19.889 -8.195  -8.966  0.52 30.96 ?  106 ILE   A HD12 1 
ATOM   2353 H HD13 A ILE   A 1 106 ? 19.096 -7.028  -10.038 0.48 27.43 ?  106 ILE   A HD13 1 
ATOM   2354 H HD13 B ILE   A 1 106 ? 18.847 -7.162  -9.575  0.52 30.96 ?  106 ILE   A HD13 1 
ATOM   2355 N N    A GLN   A 1 107 ? 22.486 -11.040 -11.514 0.48 21.42 ?  107 GLN   A N    1 
ATOM   2356 N N    B GLN   A 1 107 ? 22.563 -10.471 -11.685 0.52 23.59 ?  107 GLN   A N    1 
ATOM   2357 C CA   A GLN   A 1 107 ? 23.169 -12.215 -10.998 0.48 23.41 ?  107 GLN   A CA   1 
ATOM   2358 C CA   B GLN   A 1 107 ? 23.044 -11.794 -11.274 0.52 24.38 ?  107 GLN   A CA   1 
ATOM   2359 C C    A GLN   A 1 107 ? 24.173 -11.847 -9.920  0.48 22.15 ?  107 GLN   A C    1 
ATOM   2360 C C    B GLN   A 1 107 ? 23.964 -11.725 -10.057 0.52 22.57 ?  107 GLN   A C    1 
ATOM   2361 O O    A GLN   A 1 107 ? 24.535 -12.710 -9.112  0.48 22.95 ?  107 GLN   A O    1 
ATOM   2362 O O    B GLN   A 1 107 ? 24.082 -12.701 -9.309  0.52 23.52 ?  107 GLN   A O    1 
ATOM   2363 C CB   A GLN   A 1 107 ? 23.868 -12.978 -12.130 0.48 26.84 ?  107 GLN   A CB   1 
ATOM   2364 C CB   B GLN   A 1 107 ? 23.781 -12.467 -12.437 0.52 27.85 ?  107 GLN   A CB   1 
ATOM   2365 C CG   A GLN   A 1 107 ? 22.965 -13.300 -13.313 0.48 30.22 ?  107 GLN   A CG   1 
ATOM   2366 C CG   B GLN   A 1 107 ? 22.907 -12.782 -13.638 0.52 31.25 ?  107 GLN   A CG   1 
ATOM   2367 C CD   A GLN   A 1 107 ? 21.698 -14.028 -12.908 0.48 33.02 ?  107 GLN   A CD   1 
ATOM   2368 C CD   B GLN   A 1 107 ? 21.775 -13.728 -13.298 0.52 34.12 ?  107 GLN   A CD   1 
ATOM   2369 O OE1  A GLN   A 1 107 ? 21.744 -15.059 -12.236 0.48 34.09 ?  107 GLN   A OE1  1 
ATOM   2370 O OE1  B GLN   A 1 107 ? 22.000 -14.824 -12.785 0.52 35.22 ?  107 GLN   A OE1  1 
ATOM   2371 N NE2  A GLN   A 1 107 ? 20.554 -13.488 -13.311 0.48 33.98 ?  107 GLN   A NE2  1 
ATOM   2372 N NE2  B GLN   A 1 107 ? 20.548 -13.306 -13.572 0.52 35.11 ?  107 GLN   A NE2  1 
ATOM   2373 H H    A GLN   A 1 107 ? 22.583 -10.915 -12.356 0.48 25.68 ?  107 GLN   A H    1 
ATOM   2374 H H    B GLN   A 1 107 ? 22.789 -10.246 -12.482 0.52 28.28 ?  107 GLN   A H    1 
ATOM   2375 H HA   A GLN   A 1 107 ? 22.522 -12.813 -10.598 0.48 28.07 ?  107 GLN   A HA   1 
ATOM   2376 H HA   B GLN   A 1 107 ? 22.291 -12.350 -11.036 0.52 29.24 ?  107 GLN   A HA   1 
ATOM   2377 H HB2  A GLN   A 1 107 ? 24.609 -12.444 -12.459 0.48 32.19 ?  107 GLN   A HB2  1 
ATOM   2378 H HB2  B GLN   A 1 107 ? 24.494 -11.883 -12.741 0.52 33.40 ?  107 GLN   A HB2  1 
ATOM   2379 H HB3  A GLN   A 1 107 ? 24.205 -13.821 -11.781 0.48 32.19 ?  107 GLN   A HB3  1 
ATOM   2380 H HB3  B GLN   A 1 107 ? 24.159 -13.306 -12.125 0.52 33.40 ?  107 GLN   A HB3  1 
ATOM   2381 H HG2  A GLN   A 1 107 ? 22.706 -12.474 -13.749 0.48 36.24 ?  107 GLN   A HG2  1 
ATOM   2382 H HG2  B GLN   A 1 107 ? 22.521 -11.959 -13.972 0.52 37.48 ?  107 GLN   A HG2  1 
ATOM   2383 H HG3  A GLN   A 1 107 ? 23.451 -13.862 -13.936 0.48 36.24 ?  107 GLN   A HG3  1 
ATOM   2384 H HG3  B GLN   A 1 107 ? 23.452 -13.199 -14.326 0.52 37.48 ?  107 GLN   A HG3  1 
ATOM   2385 H HE21 A GLN   A 1 107 ? 20.560 -12.765 -13.777 0.48 40.76 ?  107 GLN   A HE21 1 
ATOM   2386 H HE21 B GLN   A 1 107 ? 20.431 -12.534 -13.929 0.52 42.10 ?  107 GLN   A HE21 1 
ATOM   2387 H HE22 A GLN   A 1 107 ? 19.809 -13.863 -13.107 0.48 40.76 ?  107 GLN   A HE22 1 
ATOM   2388 H HE22 B GLN   A 1 107 ? 19.873 -13.807 -13.395 0.52 42.10 ?  107 GLN   A HE22 1 
ATOM   2389 N N    . LEU   A 1 108 ? 24.629 -10.589 -9.862  1.00 19.53 ?  108 LEU   A N    1 
ATOM   2390 C CA   . LEU   A 1 108 ? 25.553 -10.289 -8.775  1.00 16.22 ?  108 LEU   A CA   1 
ATOM   2391 C C    . LEU   A 1 108 ? 24.863 -10.165 -7.423  1.00 13.80 ?  108 LEU   A C    1 
ATOM   2392 O O    . LEU   A 1 108 ? 25.552 -10.023 -6.409  1.00 13.90 ?  108 LEU   A O    1 
ATOM   2393 C CB   . LEU   A 1 108 ? 26.339 -9.013  -9.094  1.00 15.80 ?  108 LEU   A CB   1 
ATOM   2394 C CG   . LEU   A 1 108 ? 27.317 -9.190  -10.255 1.00 17.24 ?  108 LEU   A CG   1 
ATOM   2395 C CD1  . LEU   A 1 108 ? 27.795 -7.846  -10.771 1.00 17.89 ?  108 LEU   A CD1  1 
ATOM   2396 C CD2  . LEU   A 1 108 ? 28.502 -10.046 -9.829  1.00 19.49 ?  108 LEU   A CD2  1 
ATOM   2397 H H    A LEU   A 1 108 ? 24.448 -9.951  -10.404 0.48 23.41 ?  108 LEU   A H    1 
ATOM   2398 H H    B LEU   A 1 108 ? 24.554 -9.921  -10.395 0.52 23.41 ?  108 LEU   A H    1 
ATOM   2399 H HA   . LEU   A 1 108 ? 26.193 -11.012 -8.699  1.00 19.44 ?  108 LEU   A HA   1 
ATOM   2400 H HB2  . LEU   A 1 108 ? 25.715 -8.312  -9.338  1.00 18.94 ?  108 LEU   A HB2  1 
ATOM   2401 H HB3  . LEU   A 1 108 ? 26.847 -8.750  -8.313  1.00 18.94 ?  108 LEU   A HB3  1 
ATOM   2402 H HG   . LEU   A 1 108 ? 26.868 -9.651  -10.982 1.00 20.67 ?  108 LEU   A HG   1 
ATOM   2403 H HD11 . LEU   A 1 108 ? 28.396 -7.991  -11.520 1.00 21.45 ?  108 LEU   A HD11 1 
ATOM   2404 H HD12 . LEU   A 1 108 ? 27.028 -7.329  -11.059 1.00 21.45 ?  108 LEU   A HD12 1 
ATOM   2405 H HD13 . LEU   A 1 108 ? 28.261 -7.382  -10.059 1.00 21.45 ?  108 LEU   A HD13 1 
ATOM   2406 H HD21 . LEU   A 1 108 ? 29.173 -10.027 -10.528 1.00 23.36 ?  108 LEU   A HD21 1 
ATOM   2407 H HD22 . LEU   A 1 108 ? 28.869 -9.687  -9.006  1.00 23.36 ?  108 LEU   A HD22 1 
ATOM   2408 H HD23 . LEU   A 1 108 ? 28.200 -10.958 -9.685  1.00 23.36 ?  108 LEU   A HD23 1 
ATOM   2409 N N    . LEU   A 1 109 ? 23.533 -10.232 -7.372  1.00 12.77 ?  109 LEU   A N    1 
ATOM   2410 C CA   . LEU   A 1 109 ? 22.847 -10.107 -6.093  1.00 11.86 ?  109 LEU   A CA   1 
ATOM   2411 C C    . LEU   A 1 109 ? 23.196 -11.259 -5.154  1.00 11.29 ?  109 LEU   A C    1 
ATOM   2412 O O    . LEU   A 1 109 ? 23.332 -11.058 -3.944  1.00 11.85 ?  109 LEU   A O    1 
ATOM   2413 C CB   . LEU   A 1 109 ? 21.343 -10.018 -6.335  1.00 12.46 ?  109 LEU   A CB   1 
ATOM   2414 C CG   . LEU   A 1 109 ? 20.450 -9.744  -5.129  1.00 12.46 ?  109 LEU   A CG   1 
ATOM   2415 C CD1  . LEU   A 1 109 ? 20.873 -8.470  -4.426  1.00 12.58 ?  109 LEU   A CD1  1 
ATOM   2416 C CD2  . LEU   A 1 109 ? 18.997 -9.639  -5.586  1.00 13.65 ?  109 LEU   A CD2  1 
ATOM   2417 H H    . LEU   A 1 109 ? 23.010 -10.349 -8.046  1.00 15.30 ?  109 LEU   A H    1 
ATOM   2418 H HA   . LEU   A 1 109 ? 23.130 -9.282  -5.665  1.00 14.21 ?  109 LEU   A HA   1 
ATOM   2419 H HB2  . LEU   A 1 109 ? 21.182 -9.299  -6.966  1.00 14.93 ?  109 LEU   A HB2  1 
ATOM   2420 H HB3  . LEU   A 1 109 ? 21.047 -10.854 -6.718  1.00 14.93 ?  109 LEU   A HB3  1 
ATOM   2421 H HG   . LEU   A 1 109 ? 20.514 -10.479 -4.497  1.00 14.92 ?  109 LEU   A HG   1 
ATOM   2422 H HD11 . LEU   A 1 109 ? 20.206 -8.238  -3.759  1.00 15.07 ?  109 LEU   A HD11 1 
ATOM   2423 H HD12 . LEU   A 1 109 ? 21.730 -8.612  -4.002  1.00 15.07 ?  109 LEU   A HD12 1 
ATOM   2424 H HD13 . LEU   A 1 109 ? 20.939 -7.757  -5.083  1.00 15.07 ?  109 LEU   A HD13 1 
ATOM   2425 H HD21 . LEU   A 1 109 ? 18.458 -9.279  -4.860  1.00 16.36 ?  109 LEU   A HD21 1 
ATOM   2426 H HD22 . LEU   A 1 109 ? 18.947 -9.049  -6.353  1.00 16.36 ?  109 LEU   A HD22 1 
ATOM   2427 H HD23 . LEU   A 1 109 ? 18.672 -10.522 -5.827  1.00 16.36 ?  109 LEU   A HD23 1 
ATOM   2428 N N    . LYS   A 1 110 ? 23.342 -12.478 -5.684  1.00 11.01 ?  110 LYS   A N    1 
ATOM   2429 C CA   . LYS   A 1 110 ? 23.713 -13.598 -4.822  1.00 11.43 ?  110 LYS   A CA   1 
ATOM   2430 C C    . LYS   A 1 110 ? 25.095 -13.374 -4.208  1.00 10.76 ?  110 LYS   A C    1 
ATOM   2431 O O    . LYS   A 1 110 ? 25.287 -13.567 -3.005  1.00 10.91 ?  110 LYS   A O    1 
ATOM   2432 C CB   . LYS   A 1 110 ? 23.639 -14.924 -5.586  1.00 12.04 ?  110 LYS   A CB   1 
ATOM   2433 C CG   . LYS   A 1 110 ? 23.850 -16.139 -4.683  1.00 11.99 ?  110 LYS   A CG   1 
ATOM   2434 C CD   . LYS   A 1 110 ? 23.595 -17.454 -5.393  1.00 12.57 ?  110 LYS   A CD   1 
ATOM   2435 C CE   . LYS   A 1 110 ? 23.723 -18.635 -4.443  1.00 13.53 ?  110 LYS   A CE   1 
ATOM   2436 N NZ   . LYS   A 1 110 ? 22.527 -18.771 -3.571  1.00 14.06 ?  110 LYS   A NZ   1 
ATOM   2437 H H    . LYS   A 1 110 ? 23.230 -12.673 -6.514  1.00 13.19 ?  110 LYS   A H    1 
ATOM   2438 H HA   . LYS   A 1 110 ? 23.072 -13.649 -4.095  1.00 13.70 ?  110 LYS   A HA   1 
ATOM   2439 H HB2  . LYS   A 1 110 ? 22.765 -15.001 -6.000  1.00 14.42 ?  110 LYS   A HB2  1 
ATOM   2440 H HB3  . LYS   A 1 110 ? 24.330 -14.930 -6.268  1.00 14.42 ?  110 LYS   A HB3  1 
ATOM   2441 H HG2  . LYS   A 1 110 ? 24.766 -16.143 -4.367  1.00 14.36 ?  110 LYS   A HG2  1 
ATOM   2442 H HG3  . LYS   A 1 110 ? 23.239 -16.083 -3.933  1.00 14.36 ?  110 LYS   A HG3  1 
ATOM   2443 H HD2  . LYS   A 1 110 ? 22.697 -17.451 -5.758  1.00 15.06 ?  110 LYS   A HD2  1 
ATOM   2444 H HD3  . LYS   A 1 110 ? 24.246 -17.562 -6.105  1.00 15.06 ?  110 LYS   A HD3  1 
ATOM   2445 H HE2  . LYS   A 1 110 ? 23.821 -19.451 -4.957  1.00 16.21 ?  110 LYS   A HE2  1 
ATOM   2446 H HE3  . LYS   A 1 110 ? 24.499 -18.503 -3.872  1.00 16.21 ?  110 LYS   A HE3  1 
ATOM   2447 H HZ1  . LYS   A 1 110 ? 22.619 -19.464 -3.026  1.00 16.85 ?  110 LYS   A HZ1  1 
ATOM   2448 H HZ2  . LYS   A 1 110 ? 22.414 -18.031 -3.087  1.00 16.85 ?  110 LYS   A HZ2  1 
ATOM   2449 H HZ3  . LYS   A 1 110 ? 21.797 -18.894 -4.074  1.00 16.85 ?  110 LYS   A HZ3  1 
ATOM   2450 N N    . SER   A 1 111 ? 26.063 -12.936 -5.021  1.00 10.90 ?  111 SER   A N    1 
ATOM   2451 C CA   . SER   A 1 111 ? 27.390 -12.624 -4.494  1.00 10.96 ?  111 SER   A CA   1 
ATOM   2452 C C    . SER   A 1 111 ? 27.310 -11.585 -3.383  1.00 10.71 ?  111 SER   A C    1 
ATOM   2453 O O    . SER   A 1 111 ? 27.999 -11.691 -2.362  1.00 11.29 ?  111 SER   A O    1 
ATOM   2454 C CB   . SER   A 1 111 ? 28.291 -12.126 -5.625  1.00 12.01 ?  111 SER   A CB   1 
ATOM   2455 O OG   . SER   A 1 111 ? 28.418 -13.123 -6.626  1.00 13.85 ?  111 SER   A OG   1 
ATOM   2456 H H    . SER   A 1 111 ? 25.973 -12.809 -5.867  1.00 13.05 ?  111 SER   A H    1 
ATOM   2457 H HA   . SER   A 1 111 ? 27.782 -13.432 -4.128  1.00 13.13 ?  111 SER   A HA   1 
ATOM   2458 H HB2  . SER   A 1 111 ? 27.894 -11.337 -6.022  1.00 14.39 ?  111 SER   A HB2  1 
ATOM   2459 H HB3  . SER   A 1 111 ? 29.164 -11.917 -5.263  1.00 14.39 ?  111 SER   A HB3  1 
ATOM   2460 H HG   . SER   A 1 111 ? 28.929 -12.842 -7.243  1.00 16.60 ?  111 SER   A HG   1 
ATOM   2461 N N    . ALA   A 1 112 ? 26.468 -10.567 -3.566  1.00 10.70 ?  112 ALA   A N    1 
ATOM   2462 C CA   . ALA   A 1 112 ? 26.309 -9.536  -2.542  1.00 10.66 ?  112 ALA   A CA   1 
ATOM   2463 C C    . ALA   A 1 112 ? 25.829 -10.139 -1.222  1.00 10.70 ?  112 ALA   A C    1 
ATOM   2464 O O    . ALA   A 1 112 ? 26.380 -9.856  -0.153  1.00 10.81 ?  112 ALA   A O    1 
ATOM   2465 C CB   . ALA   A 1 112 ? 25.351 -8.452  -3.038  1.00 11.20 ?  112 ALA   A CB   1 
ATOM   2466 H H    . ALA   A 1 112 ? 25.984 -10.448 -4.264  1.00 12.82 ?  112 ALA   A H    1 
ATOM   2467 H HA   . ALA   A 1 112 ? 27.168 -9.116  -2.381  1.00 12.77 ?  112 ALA   A HA   1 
ATOM   2468 H HB1  . ALA   A 1 112 ? 25.261 -7.768  -2.349  1.00 13.41 ?  112 ALA   A HB1  1 
ATOM   2469 H HB2  . ALA   A 1 112 ? 25.709 -8.054  -3.846  1.00 13.41 ?  112 ALA   A HB2  1 
ATOM   2470 H HB3  . ALA   A 1 112 ? 24.485 -8.848  -3.218  1.00 13.41 ?  112 ALA   A HB3  1 
ATOM   2471 N N    . TYR   A 1 113 ? 24.803 -10.990 -1.275  1.00 10.63 ?  113 TYR   A N    1 
ATOM   2472 C CA   . TYR   A 1 113 ? 24.295 -11.599 -0.047  1.00 10.50 ?  113 TYR   A CA   1 
ATOM   2473 C C    . TYR   A 1 113 ? 25.299 -12.552 0.599   1.00 10.28 ?  113 TYR   A C    1 
ATOM   2474 O O    . TYR   A 1 113 ? 25.260 -12.737 1.819   1.00 10.72 ?  113 TYR   A O    1 
ATOM   2475 C CB   . TYR   A 1 113 ? 22.981 -12.333 -0.311  1.00 10.72 ?  113 TYR   A CB   1 
ATOM   2476 C CG   . TYR   A 1 113 ? 21.755 -11.443 -0.253  1.00 10.54 ?  113 TYR   A CG   1 
ATOM   2477 C CD1  . TYR   A 1 113 ? 21.371 -10.843 0.938   1.00 10.29 ?  113 TYR   A CD1  1 
ATOM   2478 C CD2  . TYR   A 1 113 ? 20.970 -11.228 -1.381  1.00 10.71 ?  113 TYR   A CD2  1 
ATOM   2479 C CE1  . TYR   A 1 113 ? 20.247 -10.043 1.003   1.00 10.39 ?  113 TYR   A CE1  1 
ATOM   2480 C CE2  . TYR   A 1 113 ? 19.832 -10.431 -1.322  1.00 10.75 ?  113 TYR   A CE2  1 
ATOM   2481 C CZ   . TYR   A 1 113 ? 19.481 -9.842  -0.127  1.00 10.34 ?  113 TYR   A CZ   1 
ATOM   2482 O OH   . TYR   A 1 113 ? 18.347 -9.052  -0.027  1.00 11.31 ?  113 TYR   A OH   1 
ATOM   2483 H H    . TYR   A 1 113 ? 24.388 -11.220 -1.993  1.00 12.74 ?  113 TYR   A H    1 
ATOM   2484 H HA   . TYR   A 1 113 ? 24.113 -10.892 0.591   1.00 12.57 ?  113 TYR   A HA   1 
ATOM   2485 H HB2  . TYR   A 1 113 ? 23.018 -12.730 -1.195  1.00 12.85 ?  113 TYR   A HB2  1 
ATOM   2486 H HB3  . TYR   A 1 113 ? 22.877 -13.029 0.356   1.00 12.85 ?  113 TYR   A HB3  1 
ATOM   2487 H HD1  . TYR   A 1 113 ? 21.885 -10.978 1.701   1.00 12.32 ?  113 TYR   A HD1  1 
ATOM   2488 H HD2  . TYR   A 1 113 ? 21.207 -11.634 -2.186  1.00 12.83 ?  113 TYR   A HD2  1 
ATOM   2489 H HE1  . TYR   A 1 113 ? 20.005 -9.647  1.808   1.00 12.44 ?  113 TYR   A HE1  1 
ATOM   2490 H HE2  . TYR   A 1 113 ? 19.311 -10.293 -2.080  1.00 12.87 ?  113 TYR   A HE2  1 
ATOM   2491 H HH   . TYR   A 1 113 ? 17.934 -9.057  -0.767  1.00 13.55 ?  113 TYR   A HH   1 
ATOM   2492 N N    . GLU   A 1 114 ? 26.204 -13.160 -0.184  1.00 10.45 ?  114 GLU   A N    1 
ATOM   2493 C CA   . GLU   A 1 114 ? 27.195 -14.064 0.405   1.00 10.53 ?  114 GLU   A CA   1 
ATOM   2494 C C    . GLU   A 1 114 ? 28.048 -13.360 1.451   1.00 10.47 ?  114 GLU   A C    1 
ATOM   2495 O O    . GLU   A 1 114 ? 28.522 -13.994 2.401   1.00 10.63 ?  114 GLU   A O    1 
ATOM   2496 C CB   . GLU   A 1 114 ? 28.069 -14.698 -0.685  1.00 10.73 ?  114 GLU   A CB   1 
ATOM   2497 C CG   . GLU   A 1 114 ? 27.304 -15.759 -1.470  1.00 10.98 ?  114 GLU   A CG   1 
ATOM   2498 C CD   . GLU   A 1 114 ? 28.010 -16.285 -2.720  1.00 11.07 ?  114 GLU   A CD   1 
ATOM   2499 O OE1  . GLU   A 1 114 ? 28.971 -15.653 -3.213  1.00 11.12 ?  114 GLU   A OE1  1 
ATOM   2500 O OE2  . GLU   A 1 114 ? 27.564 -17.349 -3.217  1.00 12.06 -1 114 GLU   A OE2  1 
ATOM   2501 H H    . GLU   A 1 114 ? 26.264 -13.061 -1.043  1.00 12.51 ?  114 GLU   A H    1 
ATOM   2502 H HA   . GLU   A 1 114 ? 26.720 -14.780 0.847   1.00 12.61 ?  114 GLU   A HA   1 
ATOM   2503 H HB2  . GLU   A 1 114 ? 28.356 -14.013 -1.310  1.00 12.85 ?  114 GLU   A HB2  1 
ATOM   2504 H HB3  . GLU   A 1 114 ? 28.837 -15.121 -0.274  1.00 12.85 ?  114 GLU   A HB3  1 
ATOM   2505 H HG2  . GLU   A 1 114 ? 27.146 -16.520 -0.885  1.00 13.15 ?  114 GLU   A HG2  1 
ATOM   2506 H HG3  . GLU   A 1 114 ? 26.452 -15.387 -1.748  1.00 13.15 ?  114 GLU   A HG3  1 
ATOM   2507 N N    . ASN   A 1 115 ? 28.231 -12.043 1.321   1.00 10.40 ?  115 ASN   A N    1 
ATOM   2508 C CA   . ASN   A 1 115 ? 28.998 -11.313 2.326   1.00 10.52 ?  115 ASN   A CA   1 
ATOM   2509 C C    . ASN   A 1 115 ? 28.383 -11.448 3.713   1.00 10.31 ?  115 ASN   A C    1 
ATOM   2510 O O    . ASN   A 1 115 ? 29.097 -11.383 4.722   1.00 10.72 ?  115 ASN   A O    1 
ATOM   2511 C CB   . ASN   A 1 115 ? 29.108 -9.835  1.948   1.00 10.44 ?  115 ASN   A CB   1 
ATOM   2512 C CG   . ASN   A 1 115 ? 29.899 -9.617  0.679   1.00 11.30 ?  115 ASN   A CG   1 
ATOM   2513 O OD1  . ASN   A 1 115 ? 31.117 -9.729  0.683   1.00 14.43 ?  115 ASN   A OD1  1 
ATOM   2514 N ND2  . ASN   A 1 115 ? 29.216 -9.307  -0.407  1.00 10.89 ?  115 ASN   A ND2  1 
ATOM   2515 H H    . ASN   A 1 115 ? 27.923 -11.556 0.681   1.00 12.45 ?  115 ASN   A H    1 
ATOM   2516 H HA   . ASN   A 1 115 ? 29.894 -11.681 2.364   1.00 12.60 ?  115 ASN   A HA   1 
ATOM   2517 H HB2  . ASN   A 1 115 ? 28.218 -9.477  1.822   1.00 12.51 ?  115 ASN   A HB2  1 
ATOM   2518 H HB3  . ASN   A 1 115 ? 29.559 -9.363  2.667   1.00 12.51 ?  115 ASN   A HB3  1 
ATOM   2519 H HD21 . ASN   A 1 115 ? 29.631 -9.170  -1.149  1.00 13.04 ?  115 ASN   A HD21 1 
ATOM   2520 H HD22 . ASN   A 1 115 ? 28.360 -9.248  -0.376  1.00 13.04 ?  115 ASN   A HD22 1 
ATOM   2521 N N    . PHE   A 1 116 ? 27.058 -11.617 3.790   1.00 10.50 ?  116 PHE   A N    1 
ATOM   2522 C CA   . PHE   A 1 116 ? 26.413 -11.721 5.094   1.00 10.49 ?  116 PHE   A CA   1 
ATOM   2523 C C    . PHE   A 1 116 ? 26.895 -12.953 5.861   1.00 10.47 ?  116 PHE   A C    1 
ATOM   2524 O O    . PHE   A 1 116 ? 26.818 -12.980 7.092   1.00 11.04 ?  116 PHE   A O    1 
ATOM   2525 C CB   . PHE   A 1 116 ? 24.884 -11.848 4.962   1.00 10.76 ?  116 PHE   A CB   1 
ATOM   2526 C CG   . PHE   A 1 116 ? 24.130 -10.600 4.500   1.00 10.01 ?  116 PHE   A CG   1 
ATOM   2527 C CD1  . PHE   A 1 116 ? 24.704 -9.580  3.753   1.00 10.56 ?  116 PHE   A CD1  1 
ATOM   2528 C CD2  . PHE   A 1 116 ? 22.776 -10.496 4.821   1.00 10.97 ?  116 PHE   A CD2  1 
ATOM   2529 C CE1  . PHE   A 1 116 ? 23.933 -8.497  3.331   1.00 10.65 ?  116 PHE   A CE1  1 
ATOM   2530 C CE2  . PHE   A 1 116 ? 22.011 -9.426  4.409   1.00 10.85 ?  116 PHE   A CE2  1 
ATOM   2531 C CZ   . PHE   A 1 116 ? 22.581 -8.422  3.669   1.00 10.30 ?  116 PHE   A CZ   1 
ATOM   2532 H H    . PHE   A 1 116 ? 26.522 -11.668 3.117   1.00 12.58 ?  116 PHE   A H    1 
ATOM   2533 H HA   . PHE   A 1 116 ? 26.606 -10.932 5.623   1.00 12.56 ?  116 PHE   A HA   1 
ATOM   2534 H HB2  . PHE   A 1 116 ? 24.691 -12.553 4.322   1.00 12.89 ?  116 PHE   A HB2  1 
ATOM   2535 H HB3  . PHE   A 1 116 ? 24.522 -12.101 5.829   1.00 12.89 ?  116 PHE   A HB3  1 
ATOM   2536 H HD1  . PHE   A 1 116 ? 25.598 -9.639  3.517   1.00 12.65 ?  116 PHE   A HD1  1 
ATOM   2537 H HD2  . PHE   A 1 116 ? 22.372 -11.181 5.314   1.00 13.14 ?  116 PHE   A HD2  1 
ATOM   2538 H HE1  . PHE   A 1 116 ? 24.330 -7.817  2.836   1.00 12.75 ?  116 PHE   A HE1  1 
ATOM   2539 H HE2  . PHE   A 1 116 ? 21.109 -9.382  4.644   1.00 12.99 ?  116 PHE   A HE2  1 
ATOM   2540 H HZ   . PHE   A 1 116 ? 22.077 -7.689  3.403   1.00 12.34 ?  116 PHE   A HZ   1 
ATOM   2541 N N    . ASN   A 1 117 ? 27.333 -14.002 5.154   1.00 10.88 ?  117 ASN   A N    1 
ATOM   2542 C CA   . ASN   A 1 117 ? 27.701 -15.253 5.816   1.00 11.26 ?  117 ASN   A CA   1 
ATOM   2543 C C    . ASN   A 1 117 ? 28.968 -15.144 6.646   1.00 11.62 ?  117 ASN   A C    1 
ATOM   2544 O O    . ASN   A 1 117 ? 29.273 -16.072 7.407   1.00 12.87 ?  117 ASN   A O    1 
ATOM   2545 C CB   . ASN   A 1 117 ? 27.807 -16.371 4.784   1.00 11.25 ?  117 ASN   A CB   1 
ATOM   2546 C CG   . ASN   A 1 117 ? 26.451 -16.749 4.253   1.00 11.05 ?  117 ASN   A CG   1 
ATOM   2547 O OD1  . ASN   A 1 117 ? 25.479 -16.779 5.013   1.00 12.21 ?  117 ASN   A OD1  1 
ATOM   2548 N ND2  . ASN   A 1 117 ? 26.357 -17.012 2.962   1.00 11.35 ?  117 ASN   A ND2  1 
ATOM   2549 H H    . ASN   A 1 117 ? 27.404 -14.013 4.297   1.00 13.03 ?  117 ASN   A H    1 
ATOM   2550 H HA   . ASN   A 1 117 ? 26.981 -15.493 6.418   1.00 13.48 ?  117 ASN   A HA   1 
ATOM   2551 H HB2  . ASN   A 1 117 ? 28.352 -16.072 4.034   1.00 13.47 ?  117 ASN   A HB2  1 
ATOM   2552 H HB3  . ASN   A 1 117 ? 28.205 -17.152 5.195   1.00 13.47 ?  117 ASN   A HB3  1 
ATOM   2553 H HD21 . ASN   A 1 117 ? 25.599 -17.231 2.624   1.00 13.59 ?  117 ASN   A HD21 1 
ATOM   2554 H HD22 . ASN   A 1 117 ? 27.057 -16.975 2.462   1.00 13.59 ?  117 ASN   A HD22 1 
ATOM   2555 N N    . GLN   A 1 118 ? 29.694 -14.032 6.532   1.00 11.42 ?  118 GLN   A N    1 
ATOM   2556 C CA   . GLN   A 1 118 ? 30.878 -13.803 7.347   1.00 11.67 ?  118 GLN   A CA   1 
ATOM   2557 C C    . GLN   A 1 118 ? 30.545 -13.240 8.726   1.00 11.70 ?  118 GLN   A C    1 
ATOM   2558 O O    . GLN   A 1 118 ? 31.464 -12.959 9.504   1.00 13.28 ?  118 GLN   A O    1 
ATOM   2559 C CB   . GLN   A 1 118 ? 31.865 -12.896 6.605   1.00 11.91 ?  118 GLN   A CB   1 
ATOM   2560 C CG   . GLN   A 1 118 ? 32.345 -13.475 5.282   1.00 12.09 ?  118 GLN   A CG   1 
ATOM   2561 C CD   . GLN   A 1 118 ? 33.157 -14.740 5.457   1.00 12.32 ?  118 GLN   A CD   1 
ATOM   2562 O OE1  . GLN   A 1 118 ? 34.021 -14.814 6.339   1.00 13.14 ?  118 GLN   A OE1  1 
ATOM   2563 N NE2  . GLN   A 1 118 ? 32.905 -15.738 4.608   1.00 12.18 ?  118 GLN   A NE2  1 
ATOM   2564 H H    . GLN   A 1 118 ? 29.511 -13.382 5.985   1.00 13.68 ?  118 GLN   A H    1 
ATOM   2565 H HA   . GLN   A 1 118 ? 31.309 -14.658 7.480   1.00 13.99 ?  118 GLN   A HA   1 
ATOM   2566 H HB2  . GLN   A 1 118 ? 31.434 -12.048 6.423   1.00 14.27 ?  118 GLN   A HB2  1 
ATOM   2567 H HB3  . GLN   A 1 118 ? 32.640 -12.760 7.173   1.00 14.27 ?  118 GLN   A HB3  1 
ATOM   2568 H HG2  . GLN   A 1 118 ? 31.578 -13.686 4.726   1.00 14.48 ?  118 GLN   A HG2  1 
ATOM   2569 H HG3  . GLN   A 1 118 ? 32.906 -12.821 4.834   1.00 14.48 ?  118 GLN   A HG3  1 
ATOM   2570 H HE21 . GLN   A 1 118 ? 32.294 -15.647 4.002   1.00 14.59 ?  118 GLN   A HE21 1 
ATOM   2571 H HE22 . GLN   A 1 118 ? 33.339 -16.479 4.661   1.00 14.59 ?  118 GLN   A HE22 1 
ATOM   2572 N N    . HIS   A 1 119 ? 29.260 -13.095 9.057   1.00 11.37 ?  119 HIS   A N    1 
ATOM   2573 C CA   . HIS   A 1 119 ? 28.824 -12.504 10.319  1.00 11.95 ?  119 HIS   A CA   1 
ATOM   2574 C C    . HIS   A 1 119 ? 27.685 -13.331 10.890  1.00 12.89 ?  119 HIS   A C    1 
ATOM   2575 O O    . HIS   A 1 119 ? 26.728 -13.635 10.178  1.00 13.03 ?  119 HIS   A O    1 
ATOM   2576 C CB   . HIS   A 1 119 ? 28.371 -11.067 10.076  1.00 12.84 ?  119 HIS   A CB   1 
ATOM   2577 C CG   . HIS   A 1 119 ? 29.445 -10.249 9.456   1.00 13.70 ?  119 HIS   A CG   1 
ATOM   2578 N ND1  . HIS   A 1 119 ? 30.425 -9.647  10.205  1.00 15.73 ?  119 HIS   A ND1  1 
ATOM   2579 C CD2  . HIS   A 1 119 ? 29.771 -10.043 8.160   1.00 14.34 ?  119 HIS   A CD2  1 
ATOM   2580 C CE1  . HIS   A 1 119 ? 31.285 -9.053  9.397   1.00 15.79 ?  119 HIS   A CE1  1 
ATOM   2581 N NE2  . HIS   A 1 119 ? 30.921 -9.290  8.150   1.00 15.61 ?  119 HIS   A NE2  1 
ATOM   2582 H H    . HIS   A 1 119 ? 28.603 -13.346 8.555   1.00 13.62 ?  119 HIS   A H    1 
ATOM   2583 H HA   . HIS   A 1 119 ? 29.557 -12.508 10.953  1.00 14.31 ?  119 HIS   A HA   1 
ATOM   2584 H HB2  . HIS   A 1 119 ? 27.603 -11.078 9.481   1.00 15.39 ?  119 HIS   A HB2  1 
ATOM   2585 H HB3  . HIS   A 1 119 ? 28.130 -10.669 10.926  1.00 15.39 ?  119 HIS   A HB3  1 
ATOM   2586 H HD1  . HIS   A 1 119 ? 30.457 -9.643  11.065  1.00 18.86 ?  119 HIS   A HD1  1 
ATOM   2587 H HD2  . HIS   A 1 119 ? 29.302 -10.351 7.415   1.00 17.19 ?  119 HIS   A HD2  1 
ATOM   2588 H HE1  . HIS   A 1 119 ? 32.019 -8.554  9.662   1.00 18.93 ?  119 HIS   A HE1  1 
ATOM   2589 N N    A GLU   A 1 120 ? 27.789 -13.682 12.174  0.48 13.71 ?  120 GLU   A N    1 
ATOM   2590 N N    B GLU   A 1 120 ? 27.784 -13.686 12.172  0.52 13.45 ?  120 GLU   A N    1 
ATOM   2591 C CA   A GLU   A 1 120 ? 26.834 -14.617 12.768  0.48 15.62 ?  120 GLU   A CA   1 
ATOM   2592 C CA   B GLU   A 1 120 ? 26.826 -14.630 12.747  0.52 15.25 ?  120 GLU   A CA   1 
ATOM   2593 C C    A GLU   A 1 120 ? 25.425 -14.035 12.829  0.48 14.43 ?  120 GLU   A C    1 
ATOM   2594 C C    B GLU   A 1 120 ? 25.421 -14.045 12.869  0.52 14.04 ?  120 GLU   A C    1 
ATOM   2595 O O    A GLU   A 1 120 ? 24.440 -14.766 12.652  0.48 14.54 ?  120 GLU   A O    1 
ATOM   2596 O O    B GLU   A 1 120 ? 24.436 -14.793 12.789  0.52 13.69 ?  120 GLU   A O    1 
ATOM   2597 C CB   A GLU   A 1 120 ? 27.304 -15.030 14.165  0.48 19.57 ?  120 GLU   A CB   1 
ATOM   2598 C CB   B GLU   A 1 120 ? 27.313 -15.119 14.112  0.52 19.22 ?  120 GLU   A CB   1 
ATOM   2599 C CG   A GLU   A 1 120 ? 28.483 -15.988 14.171  0.48 24.51 ?  120 GLU   A CG   1 
ATOM   2600 C CG   B GLU   A 1 120 ? 28.490 -16.080 14.050  0.52 24.48 ?  120 GLU   A CG   1 
ATOM   2601 C CD   A GLU   A 1 120 ? 28.664 -16.674 15.510  0.48 28.50 ?  120 GLU   A CD   1 
ATOM   2602 C CD   B GLU   A 1 120 ? 28.785 -16.733 15.386  0.52 28.70 ?  120 GLU   A CD   1 
ATOM   2603 O OE1  A GLU   A 1 120 ? 28.260 -16.089 16.539  0.48 29.98 ?  120 GLU   A OE1  1 
ATOM   2604 O OE1  B GLU   A 1 120 ? 28.201 -16.302 16.404  0.52 30.43 ?  120 GLU   A OE1  1 
ATOM   2605 O OE2  A GLU   A 1 120 ? 29.200 -17.802 15.533  0.48 30.02 -1 120 GLU   A OE2  1 
ATOM   2606 O OE2  B GLU   A 1 120 ? 29.601 -17.679 15.416  0.52 30.17 -1 120 GLU   A OE2  1 
ATOM   2607 H H    A GLU   A 1 120 ? 28.398 -13.404 12.712  0.48 16.43 ?  120 GLU   A H    1 
ATOM   2608 H H    B GLU   A 1 120 ? 28.389 -13.411 12.716  0.52 16.12 ?  120 GLU   A H    1 
ATOM   2609 H HA   A GLU   A 1 120 ? 26.798 -15.419 12.225  0.48 18.72 ?  120 GLU   A HA   1 
ATOM   2610 H HA   B GLU   A 1 120 ? 26.770 -15.405 12.167  0.52 18.27 ?  120 GLU   A HA   1 
ATOM   2611 H HB2  A GLU   A 1 120 ? 27.570 -14.238 14.656  0.48 23.46 ?  120 GLU   A HB2  1 
ATOM   2612 H HB2  B GLU   A 1 120 ? 27.584 -14.355 14.640  0.52 23.04 ?  120 GLU   A HB2  1 
ATOM   2613 H HB3  A GLU   A 1 120 ? 26.571 -15.470 14.626  0.48 23.46 ?  120 GLU   A HB3  1 
ATOM   2614 H HB3  B GLU   A 1 120 ? 26.581 -15.580 14.556  0.52 23.04 ?  120 GLU   A HB3  1 
ATOM   2615 H HG2  A GLU   A 1 120 ? 28.343 -16.672 13.499  0.48 29.39 ?  120 GLU   A HG2  1 
ATOM   2616 H HG2  B GLU   A 1 120 ? 28.296 -16.780 13.407  0.52 29.35 ?  120 GLU   A HG2  1 
ATOM   2617 H HG3  A GLU   A 1 120 ? 29.296 -15.495 13.982  0.48 29.39 ?  120 GLU   A HG3  1 
ATOM   2618 H HG3  B GLU   A 1 120 ? 29.284 -15.593 13.788  0.52 29.35 ?  120 GLU   A HG3  1 
ATOM   2619 N N    . VAL   A 1 121 ? 25.306 -12.735 13.099  1.00 13.76 ?  121 VAL   A N    1 
ATOM   2620 C CA   . VAL   A 1 121 ? 24.017 -12.058 13.233  1.00 13.56 ?  121 VAL   A CA   1 
ATOM   2621 C C    . VAL   A 1 121 ? 24.129 -10.676 12.593  1.00 12.73 ?  121 VAL   A C    1 
ATOM   2622 O O    . VAL   A 1 121 ? 25.108 -9.958  12.827  1.00 13.43 ?  121 VAL   A O    1 
ATOM   2623 C CB   . VAL   A 1 121 ? 23.599 -11.899 14.714  1.00 16.57 ?  121 VAL   A CB   1 
ATOM   2624 C CG1  . VAL   A 1 121 ? 22.239 -11.213 14.820  1.00 17.12 ?  121 VAL   A CG1  1 
ATOM   2625 C CG2  . VAL   A 1 121 ? 23.565 -13.229 15.442  1.00 18.24 ?  121 VAL   A CG2  1 
ATOM   2626 H H    A VAL   A 1 121 ? 25.981 -12.210 13.206  0.48 16.48 ?  121 VAL   A H    1 
ATOM   2627 H H    B VAL   A 1 121 ? 25.981 -12.208 13.192  0.52 16.48 ?  121 VAL   A H    1 
ATOM   2628 H HA   . VAL   A 1 121 ? 23.335 -12.567 12.770  1.00 16.25 ?  121 VAL   A HA   1 
ATOM   2629 H HB   . VAL   A 1 121 ? 24.247 -11.337 15.164  1.00 19.86 ?  121 VAL   A HB   1 
ATOM   2630 H HG11 . VAL   A 1 121 ? 21.919 -11.281 15.733  1.00 20.52 ?  121 VAL   A HG11 1 
ATOM   2631 H HG12 . VAL   A 1 121 ? 22.334 -10.277 14.575  1.00 20.52 ?  121 VAL   A HG12 1 
ATOM   2632 H HG13 . VAL   A 1 121 ? 21.615 -11.650 14.219  1.00 20.52 ?  121 VAL   A HG13 1 
ATOM   2633 H HG21 . VAL   A 1 121 ? 23.249 -13.083 16.354  1.00 21.86 ?  121 VAL   A HG21 1 
ATOM   2634 H HG22 . VAL   A 1 121 ? 22.955 -13.829 14.982  1.00 21.86 ?  121 VAL   A HG22 1 
ATOM   2635 H HG23 . VAL   A 1 121 ? 24.453 -13.608 15.461  1.00 21.86 ?  121 VAL   A HG23 1 
ATOM   2636 N N    . LEU   A 1 122 ? 23.116 -10.282 11.811  1.00 12.15 ?  122 LEU   A N    1 
ATOM   2637 C CA   . LEU   A 1 122 ? 23.117 -8.971  11.161  1.00 12.10 ?  122 LEU   A CA   1 
ATOM   2638 C C    . LEU   A 1 122 ? 21.724 -8.369  11.122  1.00 11.60 ?  122 LEU   A C    1 
ATOM   2639 O O    . LEU   A 1 122 ? 20.731 -9.084  10.982  1.00 12.71 ?  122 LEU   A O    1 
ATOM   2640 C CB   . LEU   A 1 122 ? 23.546 -9.041  9.692   1.00 13.77 ?  122 LEU   A CB   1 
ATOM   2641 C CG   . LEU   A 1 122 ? 24.741 -9.901  9.311   1.00 13.63 ?  122 LEU   A CG   1 
ATOM   2642 C CD1  . LEU   A 1 122 ? 24.340 -11.351 9.094   1.00 14.45 ?  122 LEU   A CD1  1 
ATOM   2643 C CD2  . LEU   A 1 122 ? 25.403 -9.331  8.062   1.00 12.66 ?  122 LEU   A CD2  1 
ATOM   2644 H H    . LEU   A 1 122 ? 22.418 -10.759 11.645  1.00 14.55 ?  122 LEU   A H    1 
ATOM   2645 H HA   . LEU   A 1 122 ? 23.706 -8.368  11.638  1.00 14.50 ?  122 LEU   A HA   1 
ATOM   2646 H HB2  . LEU   A 1 122 ? 22.798 -9.367  9.179   1.00 16.50 ?  122 LEU   A HB2  1 
ATOM   2647 H HB3  . LEU   A 1 122 ? 23.756 -8.136  9.408   1.00 16.50 ?  122 LEU   A HB3  1 
ATOM   2648 H HG   . LEU   A 1 122 ? 25.398 -9.872  10.026  1.00 16.34 ?  122 LEU   A HG   1 
ATOM   2649 H HD11 . LEU   A 1 122 ? 25.107 -11.844 8.762   1.00 17.32 ?  122 LEU   A HD11 1 
ATOM   2650 H HD12 . LEU   A 1 122 ? 24.050 -11.726 9.941   1.00 17.32 ?  122 LEU   A HD12 1 
ATOM   2651 H HD13 . LEU   A 1 122 ? 23.619 -11.385 8.450   1.00 17.32 ?  122 LEU   A HD13 1 
ATOM   2652 H HD21 . LEU   A 1 122 ? 26.144 -9.906  7.801   1.00 15.17 ?  122 LEU   A HD21 1 
ATOM   2653 H HD22 . LEU   A 1 122 ? 24.753 -9.289  7.345   1.00 15.17 ?  122 LEU   A HD22 1 
ATOM   2654 H HD23 . LEU   A 1 122 ? 25.740 -8.439  8.255   1.00 15.17 ?  122 LEU   A HD23 1 
ATOM   2655 N N    A LEU   A 1 123 ? 21.662 -7.036  11.150  0.48 11.69 ?  123 LEU   A N    1 
ATOM   2656 N N    B LEU   A 1 123 ? 21.681 -7.058  11.342  0.52 11.09 ?  123 LEU   A N    1 
ATOM   2657 C CA   A LEU   A 1 123 ? 20.478 -6.270  10.761  0.48 11.17 ?  123 LEU   A CA   1 
ATOM   2658 C CA   B LEU   A 1 123 ? 20.539 -6.221  11.011  0.52 10.61 ?  123 LEU   A CA   1 
ATOM   2659 C C    A LEU   A 1 123 ? 20.709 -5.731  9.352   0.48 10.44 ?  123 LEU   A C    1 
ATOM   2660 C C    B LEU   A 1 123 ? 20.796 -5.667  9.618   0.52 10.06 ?  123 LEU   A C    1 
ATOM   2661 O O    A LEU   A 1 123 ? 21.805 -5.249  9.050   0.48 10.44 ?  123 LEU   A O    1 
ATOM   2662 O O    B LEU   A 1 123 ? 21.789 -4.964  9.407   0.52 10.12 ?  123 LEU   A O    1 
ATOM   2663 C CB   A LEU   A 1 123 ? 20.281 -5.098  11.730  0.48 11.70 ?  123 LEU   A CB   1 
ATOM   2664 C CB   B LEU   A 1 123 ? 20.462 -5.068  12.010  0.52 10.96 ?  123 LEU   A CB   1 
ATOM   2665 C CG   A LEU   A 1 123 ? 19.251 -4.020  11.374  0.48 12.29 ?  123 LEU   A CG   1 
ATOM   2666 C CG   B LEU   A 1 123 ? 19.445 -3.987  11.661  0.52 11.39 ?  123 LEU   A CG   1 
ATOM   2667 C CD1  A LEU   A 1 123 ? 17.845 -4.592  11.343  0.48 12.39 ?  123 LEU   A CD1  1 
ATOM   2668 C CD1  B LEU   A 1 123 ? 18.039 -4.556  11.671  0.52 11.98 ?  123 LEU   A CD1  1 
ATOM   2669 C CD2  A LEU   A 1 123 ? 19.332 -2.847  12.354  0.48 12.59 ?  123 LEU   A CD2  1 
ATOM   2670 C CD2  B LEU   A 1 123 ? 19.568 -2.820  12.621  0.52 11.83 ?  123 LEU   A CD2  1 
ATOM   2671 H H    A LEU   A 1 123 ? 22.321 -6.534  11.393  0.48 14.00 ?  123 LEU   A H    1 
ATOM   2672 H H    B LEU   A 1 123 ? 22.334 -6.613  11.690  0.52 13.29 ?  123 LEU   A H    1 
ATOM   2673 H HA   A LEU   A 1 123 ? 19.689 -6.831  10.770  0.48 13.38 ?  123 LEU   A HA   1 
ATOM   2674 H HA   B LEU   A 1 123 ? 19.715 -6.729  11.024  0.52 12.71 ?  123 LEU   A HA   1 
ATOM   2675 H HB2  A LEU   A 1 123 ? 20.007 -5.464  12.590  0.48 14.01 ?  123 LEU   A HB2  1 
ATOM   2676 H HB2  B LEU   A 1 123 ? 20.215 -5.425  12.880  0.52 13.13 ?  123 LEU   A HB2  1 
ATOM   2677 H HB3  A LEU   A 1 123 ? 21.129 -4.648  11.838  0.48 14.01 ?  123 LEU   A HB3  1 
ATOM   2678 H HB3  B LEU   A 1 123 ? 21.330 -4.644  12.069  0.52 13.13 ?  123 LEU   A HB3  1 
ATOM   2679 H HG   A LEU   A 1 123 ? 19.447 -3.669  10.493  0.48 14.73 ?  123 LEU   A HG   1 
ATOM   2680 H HG   B LEU   A 1 123 ? 19.625 -3.650  10.768  0.52 13.64 ?  123 LEU   A HG   1 
ATOM   2681 H HD11 A LEU   A 1 123 ? 17.212 -3.874  11.185  0.48 14.85 ?  123 LEU   A HD11 1 
ATOM   2682 H HD11 B LEU   A 1 123 ? 17.404 -3.839  11.530  0.52 14.35 ?  123 LEU   A HD11 1 
ATOM   2683 H HD12 A LEU   A 1 123 ? 17.788 -5.246  10.632  0.48 14.85 ?  123 LEU   A HD12 1 
ATOM   2684 H HD12 B LEU   A 1 123 ? 17.957 -5.214  10.961  0.52 14.35 ?  123 LEU   A HD12 1 
ATOM   2685 H HD13 A LEU   A 1 123 ? 17.657 -5.014  12.198  0.48 14.85 ?  123 LEU   A HD13 1 
ATOM   2686 H HD13 B LEU   A 1 123 ? 17.875 -4.979  12.530  0.52 14.35 ?  123 LEU   A HD13 1 
ATOM   2687 H HD21 A LEU   A 1 123 ? 18.673 -2.179  12.108  0.48 15.08 ?  123 LEU   A HD21 1 
ATOM   2688 H HD21 B LEU   A 1 123 ? 18.915 -2.146  12.379  0.52 14.18 ?  123 LEU   A HD21 1 
ATOM   2689 H HD22 A LEU   A 1 123 ? 19.151 -3.172  13.253  0.48 15.08 ?  123 LEU   A HD22 1 
ATOM   2690 H HD22 B LEU   A 1 123 ? 19.400 -3.139  13.521  0.52 14.18 ?  123 LEU   A HD22 1 
ATOM   2691 H HD23 A LEU   A 1 123 ? 20.223 -2.464  12.317  0.48 15.08 ?  123 LEU   A HD23 1 
ATOM   2692 H HD23 B LEU   A 1 123 ? 20.463 -2.456  12.558  0.52 14.18 ?  123 LEU   A HD23 1 
ATOM   2693 N N    A ALA   A 1 124 ? 19.700 -5.804  8.480   0.48 10.28 ?  124 ALA   A N    1 
ATOM   2694 N N    B ALA   A 1 124 ? 19.922 -5.974  8.672   0.52 10.08 ?  124 ALA   A N    1 
ATOM   2695 C CA   A ALA   A 1 124 ? 19.988 -5.541  7.073   0.48 9.61  ?  124 ALA   A CA   1 
ATOM   2696 C CA   B ALA   A 1 124 ? 20.211 -5.698  7.276   0.52 10.61 ?  124 ALA   A CA   1 
ATOM   2697 C C    A ALA   A 1 124 ? 18.737 -5.075  6.337   0.48 9.67  ?  124 ALA   A C    1 
ATOM   2698 C C    B ALA   A 1 124 ? 18.987 -5.173  6.546   0.52 10.35 ?  124 ALA   A C    1 
ATOM   2699 O O    A ALA   A 1 124 ? 17.612 -5.417  6.722   0.48 10.03 ?  124 ALA   A O    1 
ATOM   2700 O O    B ALA   A 1 124 ? 17.847 -5.460  6.933   0.52 10.96 ?  124 ALA   A O    1 
ATOM   2701 C CB   A ALA   A 1 124 ? 20.557 -6.785  6.386   0.48 9.45  ?  124 ALA   A CB   1 
ATOM   2702 C CB   B ALA   A 1 124 ? 20.699 -6.967  6.565   0.52 11.69 ?  124 ALA   A CB   1 
ATOM   2703 H H    A ALA   A 1 124 ? 18.884 -5.994  8.680   0.48 12.31 ?  124 ALA   A H    1 
ATOM   2704 H H    B ALA   A 1 124 ? 19.162 -6.337  8.814   0.52 12.07 ?  124 ALA   A H    1 
ATOM   2705 H HA   A ALA   A 1 124 ? 20.634 -4.832  7.028   0.48 11.51 ?  124 ALA   A HA   1 
ATOM   2706 H HA   B ALA   A 1 124 ? 20.921 -5.035  7.234   0.52 12.71 ?  124 ALA   A HA   1 
ATOM   2707 H HB1  A ALA   A 1 124 ? 20.723 -6.574  5.456   0.48 11.31 ?  124 ALA   A HB1  1 
ATOM   2708 H HB1  B ALA   A 1 124 ? 20.887 -6.759  5.636   0.52 14.00 ?  124 ALA   A HB1  1 
ATOM   2709 H HB2  A ALA   A 1 124 ? 21.383 -7.025  6.829   0.48 11.31 ?  124 ALA   A HB2  1 
ATOM   2710 H HB2  B ALA   A 1 124 ? 21.508 -7.289  6.999   0.52 14.00 ?  124 ALA   A HB2  1 
ATOM   2711 H HB3  A ALA   A 1 124 ? 19.915 -7.507  6.457   0.48 11.31 ?  124 ALA   A HB3  1 
ATOM   2712 H HB3  B ALA   A 1 124 ? 20.007 -7.645  6.618   0.52 14.00 ?  124 ALA   A HB3  1 
ATOM   2713 N N    A PRO   A 1 125 ? 18.913 -4.336  5.237   0.48 9.77  ?  125 PRO   A N    1 
ATOM   2714 N N    B PRO   A 1 125 ? 19.194 -4.424  5.467   0.52 9.51  ?  125 PRO   A N    1 
ATOM   2715 C CA   A PRO   A 1 125 ? 17.837 -4.098  4.275   0.48 10.35 ?  125 PRO   A CA   1 
ATOM   2716 C CA   B PRO   A 1 125 ? 18.107 -4.051  4.567   0.52 9.66  ?  125 PRO   A CA   1 
ATOM   2717 C C    A PRO   A 1 125 ? 17.895 -5.133  3.155   0.48 10.34 ?  125 PRO   A C    1 
ATOM   2718 C C    B PRO   A 1 125 ? 17.991 -5.099  3.467   0.52 9.69  ?  125 PRO   A C    1 
ATOM   2719 O O    A PRO   A 1 125 ? 18.869 -5.877  3.008   0.48 10.77 ?  125 PRO   A O    1 
ATOM   2720 O O    B PRO   A 1 125 ? 18.835 -5.987  3.330   0.52 10.01 ?  125 PRO   A O    1 
ATOM   2721 C CB   A PRO   A 1 125 ? 18.220 -2.725  3.709   0.48 10.55 ?  125 PRO   A CB   1 
ATOM   2722 C CB   B PRO   A 1 125 ? 18.631 -2.738  3.979   0.52 9.53  ?  125 PRO   A CB   1 
ATOM   2723 C CG   A PRO   A 1 125 ? 19.716 -2.800  3.642   0.48 10.58 ?  125 PRO   A CG   1 
ATOM   2724 C CG   B PRO   A 1 125 ? 20.113 -3.007  3.818   0.52 9.26  ?  125 PRO   A CG   1 
ATOM   2725 C CD   A PRO   A 1 125 ? 20.145 -3.619  4.851   0.48 10.23 ?  125 PRO   A CD   1 
ATOM   2726 C CD   B PRO   A 1 125 ? 20.489 -3.904  4.989   0.52 8.95  ?  125 PRO   A CD   1 
ATOM   2727 H HA   A PRO   A 1 125 ? 16.961 -4.068  4.699   0.48 12.39 ?  125 PRO   A HA   1 
ATOM   2728 H HA   B PRO   A 1 125 ? 17.264 -3.926  5.037   0.52 11.57 ?  125 PRO   A HA   1 
ATOM   2729 H HB2  A PRO   A 1 125 ? 17.838 -2.608  2.822   0.48 12.63 ?  125 PRO   A HB2  1 
ATOM   2730 H HB2  B PRO   A 1 125 ? 18.210 -2.567  3.126   0.52 11.41 ?  125 PRO   A HB2  1 
ATOM   2731 H HB3  A PRO   A 1 125 ? 17.933 -2.019  4.308   0.48 12.63 ?  125 PRO   A HB3  1 
ATOM   2732 H HB3  B PRO   A 1 125 ? 18.476 -2.010  4.603   0.52 11.41 ?  125 PRO   A HB3  1 
ATOM   2733 H HG2  A PRO   A 1 125 ? 19.981 -3.241  2.819   0.48 12.67 ?  125 PRO   A HG2  1 
ATOM   2734 H HG2  B PRO   A 1 125 ? 20.272 -3.465  2.977   0.52 11.09 ?  125 PRO   A HG2  1 
ATOM   2735 H HG3  A PRO   A 1 125 ? 20.087 -1.906  3.684   0.48 12.67 ?  125 PRO   A HG3  1 
ATOM   2736 H HG3  B PRO   A 1 125 ? 20.604 -2.174  3.854   0.52 11.09 ?  125 PRO   A HG3  1 
ATOM   2737 H HD2  A PRO   A 1 125 ? 20.843 -4.245  4.605   0.48 12.25 ?  125 PRO   A HD2  1 
ATOM   2738 H HD2  B PRO   A 1 125 ? 21.058 -4.630  4.690   0.52 10.72 ?  125 PRO   A HD2  1 
ATOM   2739 H HD3  A PRO   A 1 125 ? 20.428 -3.033  5.571   0.48 12.25 ?  125 PRO   A HD3  1 
ATOM   2740 H HD3  B PRO   A 1 125 ? 20.920 -3.382  5.685   0.52 10.72 ?  125 PRO   A HD3  1 
ATOM   2741 N N    A LEU   A 1 126 ? 16.840 -5.142  2.339   0.48 10.95 ?  126 LEU   A N    1 
ATOM   2742 N N    B LEU   A 1 126 ? 16.939 -4.959  2.665   0.52 10.10 ?  126 LEU   A N    1 
ATOM   2743 C CA   A LEU   A 1 126 ? 16.838 -5.952  1.126   0.48 11.36 ?  126 LEU   A CA   1 
ATOM   2744 C CA   B LEU   A 1 126 ? 16.762 -5.807  1.493   0.52 10.53 ?  126 LEU   A CA   1 
ATOM   2745 C C    A LEU   A 1 126 ? 17.759 -5.331  0.082   0.48 10.87 ?  126 LEU   A C    1 
ATOM   2746 C C    B LEU   A 1 126 ? 17.649 -5.290  0.365   0.52 10.33 ?  126 LEU   A C    1 
ATOM   2747 O O    A LEU   A 1 126 ? 17.507 -4.225  -0.407  0.48 11.15 ?  126 LEU   A O    1 
ATOM   2748 O O    B LEU   A 1 126 ? 17.479 -4.157  -0.095  0.52 11.84 ?  126 LEU   A O    1 
ATOM   2749 C CB   A LEU   A 1 126 ? 15.427 -6.061  0.567   0.48 12.22 ?  126 LEU   A CB   1 
ATOM   2750 C CB   B LEU   A 1 126 ? 15.297 -5.804  1.069   0.52 11.66 ?  126 LEU   A CB   1 
ATOM   2751 C CG   A LEU   A 1 126 ? 14.502 -7.036  1.287   0.48 12.82 ?  126 LEU   A CG   1 
ATOM   2752 C CG   B LEU   A 1 126 ? 14.878 -6.846  0.030   0.52 12.33 ?  126 LEU   A CG   1 
ATOM   2753 C CD1  A LEU   A 1 126 ? 13.107 -6.899  0.719   0.48 13.74 ?  126 LEU   A CD1  1 
ATOM   2754 C CD1  B LEU   A 1 126 ? 15.015 -8.263  0.566   0.52 12.72 ?  126 LEU   A CD1  1 
ATOM   2755 C CD2  A LEU   A 1 126 ? 14.997 -8.470  1.147   0.48 12.42 ?  126 LEU   A CD2  1 
ATOM   2756 C CD2  B LEU   A 1 126 ? 13.445 -6.582  -0.418  0.52 12.42 ?  126 LEU   A CD2  1 
ATOM   2757 H H    A LEU   A 1 126 ? 16.119 -4.689  2.466   0.48 13.12 ?  126 LEU   A H    1 
ATOM   2758 H H    B LEU   A 1 126 ? 16.317 -4.370  2.774   0.52 12.10 ?  126 LEU   A H    1 
ATOM   2759 H HA   A LEU   A 1 126 ? 17.166 -6.841  1.333   0.48 13.61 ?  126 LEU   A HA   1 
ATOM   2760 H HA   B LEU   A 1 126 ? 17.028 -6.710  1.709   0.52 12.62 ?  126 LEU   A HA   1 
ATOM   2761 H HB2  A LEU   A 1 126 ? 15.014 -5.186  0.608   0.48 14.64 ?  126 LEU   A HB2  1 
ATOM   2762 H HB2  B LEU   A 1 126 ? 14.756 -5.954  1.857   0.52 13.97 ?  126 LEU   A HB2  1 
ATOM   2763 H HB3  A LEU   A 1 126 ? 15.487 -6.350  -0.356  0.48 14.64 ?  126 LEU   A HB3  1 
ATOM   2764 H HB3  B LEU   A 1 126 ? 15.091 -4.931  0.699   0.52 13.97 ?  126 LEU   A HB3  1 
ATOM   2765 H HG   A LEU   A 1 126 ? 14.467 -6.813  2.231   0.48 15.36 ?  126 LEU   A HG   1 
ATOM   2766 H HG   B LEU   A 1 126 ? 15.450 -6.761  -0.752  0.52 14.77 ?  126 LEU   A HG   1 
ATOM   2767 H HD11 A LEU   A 1 126 ? 12.519 -7.523  1.171   0.48 16.46 ?  126 LEU   A HD11 1 
ATOM   2768 H HD11 B LEU   A 1 126 ? 14.644 -8.882  -0.082  0.52 15.24 ?  126 LEU   A HD11 1 
ATOM   2769 H HD12 A LEU   A 1 126 ? 12.798 -5.991  0.854   0.48 16.46 ?  126 LEU   A HD12 1 
ATOM   2770 H HD12 B LEU   A 1 126 ? 15.954 -8.456  0.708   0.52 15.24 ?  126 LEU   A HD12 1 
ATOM   2771 H HD13 A LEU   A 1 126 ? 13.135 -7.101  -0.231  0.48 16.46 ?  126 LEU   A HD13 1 
ATOM   2772 H HD13 B LEU   A 1 126 ? 14.531 -8.330  1.403   0.52 15.24 ?  126 LEU   A HD13 1 
ATOM   2773 H HD21 A LEU   A 1 126 ? 14.306 -9.076  1.455   0.48 14.88 ?  126 LEU   A HD21 1 
ATOM   2774 H HD21 B LEU   A 1 126 ? 13.189 -7.249  -1.075  0.52 14.88 ?  126 LEU   A HD21 1 
ATOM   2775 H HD22 A LEU   A 1 126 ? 15.197 -8.644  0.213   0.48 14.88 ?  126 LEU   A HD22 1 
ATOM   2776 H HD22 B LEU   A 1 126 ? 12.858 -6.636  0.353   0.52 14.88 ?  126 LEU   A HD22 1 
ATOM   2777 H HD23 A LEU   A 1 126 ? 15.799 -8.582  1.681   0.48 14.88 ?  126 LEU   A HD23 1 
ATOM   2778 H HD23 B LEU   A 1 126 ? 13.391 -5.695  -0.811  0.52 14.88 ?  126 LEU   A HD23 1 
ATOM   2779 N N    A LEU   A 1 127 ? 18.811 -6.051  -0.281  0.48 10.56 ?  127 LEU   A N    1 
ATOM   2780 N N    B LEU   A 1 127 ? 18.598 -6.109  -0.079  0.52 10.74 ?  127 LEU   A N    1 
ATOM   2781 C CA   A LEU   A 1 127 ? 19.791 -5.515  -1.213  0.48 10.12 ?  127 LEU   A CA   1 
ATOM   2782 C CA   B LEU   A 1 127 ? 19.592 -5.639  -1.035  0.52 10.77 ?  127 LEU   A CA   1 
ATOM   2783 C C    A LEU   A 1 127 ? 19.179 -5.333  -2.595  0.48 10.24 ?  127 LEU   A C    1 
ATOM   2784 C C    B LEU   A 1 127 ? 18.981 -5.388  -2.409  0.52 10.19 ?  127 LEU   A C    1 
ATOM   2785 O O    A LEU   A 1 127 ? 18.358 -6.139  -3.050  0.48 10.44 ?  127 LEU   A O    1 
ATOM   2786 O O    B LEU   A 1 127 ? 18.091 -6.115  -2.865  0.52 10.46 ?  127 LEU   A O    1 
ATOM   2787 C CB   A LEU   A 1 127 ? 20.990 -6.452  -1.314  0.48 10.21 ?  127 LEU   A CB   1 
ATOM   2788 C CB   B LEU   A 1 127 ? 20.745 -6.637  -1.150  0.52 11.55 ?  127 LEU   A CB   1 
ATOM   2789 C CG   A LEU   A 1 127 ? 21.750 -6.770  -0.026  0.48 11.04 ?  127 LEU   A CG   1 
ATOM   2790 C CG   B LEU   A 1 127 ? 21.620 -6.795  0.100   0.52 12.56 ?  127 LEU   A CG   1 
ATOM   2791 C CD1  A LEU   A 1 127 ? 22.786 -7.855  -0.292  0.48 11.55 ?  127 LEU   A CD1  1 
ATOM   2792 C CD1  B LEU   A 1 127 ? 22.846 -7.650  -0.196  0.52 13.24 ?  127 LEU   A CD1  1 
ATOM   2793 C CD2  A LEU   A 1 127 ? 22.419 -5.532  0.530   0.48 11.45 ?  127 LEU   A CD2  1 
ATOM   2794 C CD2  B LEU   A 1 127 ? 22.041 -5.450  0.664   0.52 12.81 ?  127 LEU   A CD2  1 
ATOM   2795 H H    A LEU   A 1 127 ? 18.981 -6.845  -0.001  0.48 12.65 ?  127 LEU   A H    1 
ATOM   2796 H H    B LEU   A 1 127 ? 18.699 -6.930  0.165   0.52 12.87 ?  127 LEU   A H    1 
ATOM   2797 H HA   A LEU   A 1 127 ? 20.105 -4.651  -0.894  0.48 12.13 ?  127 LEU   A HA   1 
ATOM   2798 H HA   B LEU   A 1 127 ? 19.956 -4.798  -0.719  0.52 12.91 ?  127 LEU   A HA   1 
ATOM   2799 H HB2  A LEU   A 1 127 ? 20.684 -7.295  -1.674  0.48 12.23 ?  127 LEU   A HB2  1 
ATOM   2800 H HB2  B LEU   A 1 127 ? 20.377 -7.512  -1.358  0.52 13.84 ?  127 LEU   A HB2  1 
ATOM   2801 H HB3  A LEU   A 1 127 ? 21.632 -6.055  -1.923  0.48 12.23 ?  127 LEU   A HB3  1 
ATOM   2802 H HB3  B LEU   A 1 127 ? 21.327 -6.355  -1.874  0.52 13.84 ?  127 LEU   A HB3  1 
ATOM   2803 H HG   A LEU   A 1 127 ? 21.129 -7.106  0.643   0.48 13.23 ?  127 LEU   A HG   1 
ATOM   2804 H HG   B LEU   A 1 127 ? 21.107 -7.252  0.785   0.52 15.04 ?  127 LEU   A HG   1 
ATOM   2805 H HD11 A LEU   A 1 127 ? 23.242 -8.072  0.539   0.48 13.83 ?  127 LEU   A HD11 1 
ATOM   2806 H HD11 B LEU   A 1 127 ? 23.375 -7.737  0.615   0.52 15.87 ?  127 LEU   A HD11 1 
ATOM   2807 H HD12 A LEU   A 1 127 ? 22.339 -8.644  -0.637  0.48 13.83 ?  127 LEU   A HD12 1 
ATOM   2808 H HD12 B LEU   A 1 127 ? 22.557 -8.525  -0.495  0.52 15.87 ?  127 LEU   A HD12 1 
ATOM   2809 H HD13 A LEU   A 1 127 ? 23.427 -7.528  -0.943  0.48 13.83 ?  127 LEU   A HD13 1 
ATOM   2810 H HD13 B LEU   A 1 127 ? 23.373 -7.219  -0.887  0.52 15.87 ?  127 LEU   A HD13 1 
ATOM   2811 H HD21 A LEU   A 1 127 ? 22.922 -5.773  1.325   0.48 13.72 ?  127 LEU   A HD21 1 
ATOM   2812 H HD21 B LEU   A 1 127 ? 22.757 -5.585  1.306   0.52 15.35 ?  127 LEU   A HD21 1 
ATOM   2813 H HD22 A LEU   A 1 127 ? 23.016 -5.170  -0.142  0.48 13.72 ?  127 LEU   A HD22 1 
ATOM   2814 H HD22 B LEU   A 1 127 ? 22.351 -4.887  -0.062  0.52 15.35 ?  127 LEU   A HD22 1 
ATOM   2815 H HD23 A LEU   A 1 127 ? 21.737 -4.881  0.755   0.48 13.72 ?  127 LEU   A HD23 1 
ATOM   2816 H HD23 B LEU   A 1 127 ? 21.280 -5.038  1.101   0.52 15.35 ?  127 LEU   A HD23 1 
ATOM   2817 N N    A SER   A 1 128 ? 19.603 -4.264  -3.266  0.48 10.41 ?  128 SER   A N    1 
ATOM   2818 N N    B SER   A 1 128 ? 19.481 -4.341  -3.065  0.52 10.19 ?  128 SER   A N    1 
ATOM   2819 C CA   A SER   A 1 128 ? 19.212 -3.893  -4.620  0.48 10.93 ?  128 SER   A CA   1 
ATOM   2820 C CA   B SER   A 1 128 ? 19.071 -3.934  -4.406  0.52 10.76 ?  128 SER   A CA   1 
ATOM   2821 C C    A SER   A 1 128 ? 17.759 -3.441  -4.721  0.48 10.73 ?  128 SER   A C    1 
ATOM   2822 C C    B SER   A 1 128 ? 17.600 -3.516  -4.483  0.52 11.22 ?  128 SER   A C    1 
ATOM   2823 O O    A SER   A 1 128 ? 17.308 -3.112  -5.824  0.48 10.70 ?  128 SER   A O    1 
ATOM   2824 O O    B SER   A 1 128 ? 17.038 -3.431  -5.577  0.52 12.82 ?  128 SER   A O    1 
ATOM   2825 C CB   A SER   A 1 128 ? 19.540 -4.974  -5.663  0.48 10.86 ?  128 SER   A CB   1 
ATOM   2826 C CB   B SER   A 1 128 ? 19.433 -4.977  -5.471  0.52 10.91 ?  128 SER   A CB   1 
ATOM   2827 O OG   A SER   A 1 128 ? 20.940 -5.219  -5.711  0.48 11.27 ?  128 SER   A OG   1 
ATOM   2828 O OG   B SER   A 1 128 ? 20.845 -5.095  -5.588  0.52 11.15 ?  128 SER   A OG   1 
ATOM   2829 H H    A SER   A 1 128 ? 20.167 -3.702  -2.927  0.48 12.47 ?  128 SER   A H    1 
ATOM   2830 H H    B SER   A 1 128 ? 20.098 -3.832  -2.742  0.52 12.20 ?  128 SER   A H    1 
ATOM   2831 H HA   A SER   A 1 128 ? 19.745 -3.126  -4.859  0.48 13.09 ?  128 SER   A HA   1 
ATOM   2832 H HA   B SER   A 1 128 ? 19.594 -3.150  -4.621  0.52 12.89 ?  128 SER   A HA   1 
ATOM   2833 H HB2  A SER   A 1 128 ? 19.084 -5.797  -5.429  0.48 13.01 ?  128 SER   A HB2  1 
ATOM   2834 H HB2  B SER   A 1 128 ? 19.062 -5.836  -5.219  0.52 13.07 ?  128 SER   A HB2  1 
ATOM   2835 H HB3  A SER   A 1 128 ? 19.249 -4.668  -6.536  0.48 13.01 ?  128 SER   A HB3  1 
ATOM   2836 H HB3  B SER   A 1 128 ? 19.068 -4.695  -6.328  0.52 13.07 ?  128 SER   A HB3  1 
ATOM   2837 H HG   A SER   A 1 128 ? 21.349 -4.512  -5.905  0.48 13.50 ?  128 SER   A HG   1 
ATOM   2838 H HG   B SER   A 1 128 ? 21.178 -4.353  -5.806  0.52 13.36 ?  128 SER   A HG   1 
ATOM   2839 N N    A ALA   A 1 129 ? 17.024 -3.380  -3.612  0.48 11.05 ?  129 ALA   A N    1 
ATOM   2840 N N    B ALA   A 1 129 ? 16.975 -3.231  -3.341  0.52 11.12 ?  129 ALA   A N    1 
ATOM   2841 C CA   A ALA   A 1 129 ? 15.653 -2.888  -3.624  0.48 11.86 ?  129 ALA   A CA   1 
ATOM   2842 C CA   B ALA   A 1 129 ? 15.608 -2.733  -3.311  0.52 10.86 ?  129 ALA   A CA   1 
ATOM   2843 C C    A ALA   A 1 129 ? 15.643 -1.359  -3.596  0.48 11.57 ?  129 ALA   A C    1 
ATOM   2844 C C    B ALA   A 1 129 ? 15.588 -1.216  -3.500  0.52 10.41 ?  129 ALA   A C    1 
ATOM   2845 O O    A ALA   A 1 129 ? 16.681 -0.699  -3.693  0.48 11.91 ?  129 ALA   A O    1 
ATOM   2846 O O    B ALA   A 1 129 ? 16.625 -0.551  -3.570  0.52 10.78 ?  129 ALA   A O    1 
ATOM   2847 C CB   A ALA   A 1 129 ? 14.858 -3.506  -2.475  0.48 12.46 ?  129 ALA   A CB   1 
ATOM   2848 C CB   B ALA   A 1 129 ? 14.927 -3.129  -2.003  0.52 11.52 ?  129 ALA   A CB   1 
ATOM   2849 H H    A ALA   A 1 129 ? 17.303 -3.627  -2.831  0.48 13.23 ?  129 ALA   A H    1 
ATOM   2850 H H    B ALA   A 1 129 ? 17.326 -3.323  -2.564  0.52 13.31 ?  129 ALA   A H    1 
ATOM   2851 H HA   A ALA   A 1 129 ? 15.239 -3.161  -4.450  0.48 14.21 ?  129 ALA   A HA   1 
ATOM   2852 H HA   B ALA   A 1 129 ? 15.113 -3.134  -4.040  0.52 13.01 ?  129 ALA   A HA   1 
ATOM   2853 H HB1  A ALA   A 1 129 ? 13.950 -3.173  -2.509  0.48 14.93 ?  129 ALA   A HB1  1 
ATOM   2854 H HB1  B ALA   A 1 129 ? 14.019 -2.793  -2.006  0.52 13.80 ?  129 ALA   A HB1  1 
ATOM   2855 H HB2  A ALA   A 1 129 ? 14.865 -4.470  -2.569  0.48 14.93 ?  129 ALA   A HB2  1 
ATOM   2856 H HB2  B ALA   A 1 129 ? 14.921 -4.099  -1.935  0.52 13.80 ?  129 ALA   A HB2  1 
ATOM   2857 H HB3  A ALA   A 1 129 ? 15.273 -3.254  -1.631  0.48 14.93 ?  129 ALA   A HB3  1 
ATOM   2858 H HB3  B ALA   A 1 129 ? 15.422 -2.750  -1.261  0.52 13.80 ?  129 ALA   A HB3  1 
ATOM   2859 N N    A GLY   A 1 130 ? 14.451 -0.783  -3.480  0.48 11.59 ?  130 GLY   A N    1 
ATOM   2860 N N    B GLY   A 1 130 ? 14.383 -0.659  -3.585  0.52 10.78 ?  130 GLY   A N    1 
ATOM   2861 C CA   A GLY   A 1 130 ? 14.331 0.662   -3.420  0.48 11.34 ?  130 GLY   A CA   1 
ATOM   2862 C CA   B GLY   A 1 130 ? 14.258 0.783   -3.726  0.52 11.08 ?  130 GLY   A CA   1 
ATOM   2863 C C    A GLY   A 1 130 ? 14.901 1.316   -4.661  0.48 11.08 ?  130 GLY   A C    1 
ATOM   2864 C C    B GLY   A 1 130 ? 14.904 1.268   -5.009  0.52 11.59 ?  130 GLY   A C    1 
ATOM   2865 O O    A GLY   A 1 130 ? 14.682 0.865   -5.790  0.48 11.28 ?  130 GLY   A O    1 
ATOM   2866 O O    B GLY   A 1 130 ? 14.683 0.712   -6.091  0.52 11.40 ?  130 GLY   A O    1 
ATOM   2867 H H    A GLY   A 1 130 ? 13.712 -1.214  -3.441  0.48 13.89 ?  130 GLY   A H    1 
ATOM   2868 H H    B GLY   A 1 130 ? 13.638 -1.088  -3.563  0.52 12.91 ?  130 GLY   A H    1 
ATOM   2869 H HA2  A GLY   A 1 130 ? 13.395 0.899   -3.333  0.48 13.59 ?  130 GLY   A HA2  1 
ATOM   2870 H HA2  B GLY   A 1 130 ? 13.319 1.027   -3.736  0.52 13.27 ?  130 GLY   A HA2  1 
ATOM   2871 H HA3  A GLY   A 1 130 ? 14.811 0.997   -2.649  0.48 13.59 ?  130 GLY   A HA3  1 
ATOM   2872 H HA3  B GLY   A 1 130 ? 14.686 1.220   -2.975  0.52 13.27 ?  130 GLY   A HA3  1 
ATOM   2873 N N    A ILE   A 1 131 ? 15.647 2.405   -4.449  0.48 10.97 ?  131 ILE   A N    1 
ATOM   2874 N N    B ILE   A 1 131 ? 15.722 2.319   -4.893  0.52 12.68 ?  131 ILE   A N    1 
ATOM   2875 C CA   A ILE   A 1 131 ? 16.207 3.174   -5.558  0.48 10.41 ?  131 ILE   A CA   1 
ATOM   2876 C CA   B ILE   A 1 131 ? 16.289 2.956   -6.079  0.52 14.11 ?  131 ILE   A CA   1 
ATOM   2877 C C    A ILE   A 1 131 ? 17.279 2.421   -6.335  0.48 10.20 ?  131 ILE   A C    1 
ATOM   2878 C C    B ILE   A 1 131 ? 17.348 2.105   -6.770  0.52 13.28 ?  131 ILE   A C    1 
ATOM   2879 O O    A ILE   A 1 131 ? 17.754 2.927   -7.359  0.48 9.88  ?  131 ILE   A O    1 
ATOM   2880 O O    B ILE   A 1 131 ? 17.775 2.454   -7.876  0.52 13.99 ?  131 ILE   A O    1 
ATOM   2881 C CB   A ILE   A 1 131 ? 16.739 4.548   -5.090  0.48 11.73 ?  131 ILE   A CB   1 
ATOM   2882 C CB   B ILE   A 1 131 ? 16.745 4.409   -5.808  0.52 16.30 ?  131 ILE   A CB   1 
ATOM   2883 C CG1  A ILE   A 1 131 ? 17.974 4.388   -4.196  0.48 12.68 ?  131 ILE   A CG1  1 
ATOM   2884 C CG1  B ILE   A 1 131 ? 18.001 4.449   -4.938  0.52 17.98 ?  131 ILE   A CG1  1 
ATOM   2885 C CG2  A ILE   A 1 131 ? 15.648 5.331   -4.368  0.48 11.94 ?  131 ILE   A CG2  1 
ATOM   2886 C CG2  B ILE   A 1 131 ? 15.612 5.216   -5.162  0.52 16.36 ?  131 ILE   A CG2  1 
ATOM   2887 C CD1  A ILE   A 1 131 ? 18.607 5.704   -3.778  0.48 13.54 ?  131 ILE   A CD1  1 
ATOM   2888 C CD1  B ILE   A 1 131 ? 18.561 5.849   -4.756  0.52 18.92 ?  131 ILE   A CD1  1 
ATOM   2889 H H    A ILE   A 1 131 ? 15.818 2.724   -3.670  0.48 13.15 ?  131 ILE   A H    1 
ATOM   2890 H H    B ILE   A 1 131 ? 15.955 2.677   -4.144  0.52 15.20 ?  131 ILE   A H    1 
ATOM   2891 H HA   A ILE   A 1 131 ? 15.481 3.365   -6.176  0.48 12.47 ?  131 ILE   A HA   1 
ATOM   2892 H HA   B ILE   A 1 131 ? 15.573 3.028   -6.718  0.52 16.91 ?  131 ILE   A HA   1 
ATOM   2893 H HB   A ILE   A 1 131 ? 16.995 5.056   -5.874  0.48 14.05 ?  131 ILE   A HB   1 
ATOM   2894 H HB   B ILE   A 1 131 ? 16.953 4.821   -6.658  0.52 19.54 ?  131 ILE   A HB   1 
ATOM   2895 H HG12 A ILE   A 1 131 ? 17.719 3.912   -3.392  0.48 15.19 ?  131 ILE   A HG12 1 
ATOM   2896 H HG12 B ILE   A 1 131 ? 17.789 4.096   -4.061  0.52 21.55 ?  131 ILE   A HG12 1 
ATOM   2897 H HG13 A ILE   A 1 131 ? 18.648 3.883   -4.678  0.48 15.19 ?  131 ILE   A HG13 1 
ATOM   2898 H HG13 B ILE   A 1 131 ? 18.692 3.910   -5.354  0.52 21.55 ?  131 ILE   A HG13 1 
ATOM   2899 H HG21 A ILE   A 1 131 ? 15.947 6.245   -4.231  0.48 14.31 ?  131 ILE   A HG21 1 
ATOM   2900 H HG21 B ILE   A 1 131 ? 15.831 6.160   -5.197  0.52 19.61 ?  131 ILE   A HG21 1 
ATOM   2901 H HG22 A ILE   A 1 131 ? 14.844 5.328   -4.910  0.48 14.31 ?  131 ILE   A HG22 1 
ATOM   2902 H HG22 B ILE   A 1 131 ? 14.790 5.052   -5.651  0.52 19.61 ?  131 ILE   A HG22 1 
ATOM   2903 H HG23 A ILE   A 1 131 ? 15.470 4.911   -3.511  0.48 14.31 ?  131 ILE   A HG23 1 
ATOM   2904 H HG23 B ILE   A 1 131 ? 15.506 4.933   -4.240  0.52 19.61 ?  131 ILE   A HG23 1 
ATOM   2905 H HD11 A ILE   A 1 131 ? 19.445 5.520   -3.324  0.48 16.23 ?  131 ILE   A HD11 1 
ATOM   2906 H HD11 B ILE   A 1 131 ? 19.355 5.799   -4.204  0.52 22.69 ?  131 ILE   A HD11 1 
ATOM   2907 H HD12 A ILE   A 1 131 ? 18.773 6.240   -4.570  0.48 16.23 ?  131 ILE   A HD12 1 
ATOM   2908 H HD12 B ILE   A 1 131 ? 18.784 6.212   -5.628  0.52 22.69 ?  131 ILE   A HD12 1 
ATOM   2909 H HD13 A ILE   A 1 131 ? 18.003 6.172   -3.182  0.48 16.23 ?  131 ILE   A HD13 1 
ATOM   2910 H HD13 B ILE   A 1 131 ? 17.894 6.407   -4.329  0.52 22.69 ?  131 ILE   A HD13 1 
ATOM   2911 N N    A PHE   A 1 132 ? 17.693 1.237   -5.875  0.48 10.37 ?  132 PHE   A N    1 
ATOM   2912 N N    B PHE   A 1 132 ? 17.771 0.987   -6.172  0.52 12.55 ?  132 PHE   A N    1 
ATOM   2913 C CA   A PHE   A 1 132 ? 18.569 0.398   -6.685  0.48 10.56 ?  132 PHE   A CA   1 
ATOM   2914 C CA   B PHE   A 1 132 ? 18.656 0.080   -6.897  0.52 12.61 ?  132 PHE   A CA   1 
ATOM   2915 C C    A PHE   A 1 132 ? 17.819 -0.322  -7.803  0.48 11.15 ?  132 PHE   A C    1 
ATOM   2916 C C    B PHE   A 1 132 ? 17.914 -0.704  -7.980  0.52 13.46 ?  132 PHE   A C    1 
ATOM   2917 O O    A PHE   A 1 132 ? 18.457 -0.883  -8.699  0.48 12.18 ?  132 PHE   A O    1 
ATOM   2918 O O    B PHE   A 1 132 ? 18.557 -1.330  -8.830  0.52 14.48 ?  132 PHE   A O    1 
ATOM   2919 C CB   A PHE   A 1 132 ? 19.336 -0.606  -5.812  0.48 10.39 ?  132 PHE   A CB   1 
ATOM   2920 C CB   B PHE   A 1 132 ? 19.356 -0.887  -5.942  0.52 12.35 ?  132 PHE   A CB   1 
ATOM   2921 C CG   A PHE   A 1 132 ? 20.607 -0.060  -5.192  0.48 10.82 ?  132 PHE   A CG   1 
ATOM   2922 C CG   B PHE   A 1 132 ? 20.520 -0.291  -5.191  0.52 12.36 ?  132 PHE   A CG   1 
ATOM   2923 C CD1  A PHE   A 1 132 ? 20.573 1.032   -4.338  0.48 12.03 ?  132 PHE   A CD1  1 
ATOM   2924 C CD1  B PHE   A 1 132 ? 20.335 0.742   -4.286  0.52 13.06 ?  132 PHE   A CD1  1 
ATOM   2925 C CD2  A PHE   A 1 132 ? 21.833 -0.672  -5.435  0.48 11.53 ?  132 PHE   A CD2  1 
ATOM   2926 C CD2  B PHE   A 1 132 ? 21.797 -0.808  -5.354  0.52 12.55 ?  132 PHE   A CD2  1 
ATOM   2927 C CE1  A PHE   A 1 132 ? 21.740 1.517   -3.757  0.48 12.95 ?  132 PHE   A CE1  1 
ATOM   2928 C CE1  B PHE   A 1 132 ? 21.408 1.267   -3.582  0.52 13.11 ?  132 PHE   A CE1  1 
ATOM   2929 C CE2  A PHE   A 1 132 ? 23.001 -0.192  -4.853  0.48 12.22 ?  132 PHE   A CE2  1 
ATOM   2930 C CE2  B PHE   A 1 132 ? 22.873 -0.290  -4.652  0.52 12.22 ?  132 PHE   A CE2  1 
ATOM   2931 C CZ   A PHE   A 1 132 ? 22.950 0.903   -4.014  0.48 12.78 ?  132 PHE   A CZ   1 
ATOM   2932 C CZ   B PHE   A 1 132 ? 22.677 0.750   -3.765  0.52 12.37 ?  132 PHE   A CZ   1 
ATOM   2933 H H    A PHE   A 1 132 ? 17.484 0.916   -5.107  0.48 12.43 ?  132 PHE   A H    1 
ATOM   2934 H H    B PHE   A 1 132 ? 17.568 0.741   -5.367  0.52 15.04 ?  132 PHE   A H    1 
ATOM   2935 H HA   A PHE   A 1 132 ? 19.221 0.974   -7.109  0.48 12.65 ?  132 PHE   A HA   1 
ATOM   2936 H HA   B PHE   A 1 132 ? 19.346 0.615   -7.319  0.52 15.11 ?  132 PHE   A HA   1 
ATOM   2937 H HB2  A PHE   A 1 132 ? 18.759 -0.890  -5.086  0.48 12.44 ?  132 PHE   A HB2  1 
ATOM   2938 H HB2  B PHE   A 1 132 ? 18.713 -1.191  -5.286  0.52 14.80 ?  132 PHE   A HB2  1 
ATOM   2939 H HB3  A PHE   A 1 132 ? 19.578 -1.365  -6.358  0.48 12.44 ?  132 PHE   A HB3  1 
ATOM   2940 H HB3  B PHE   A 1 132 ? 19.689 -1.640  -6.453  0.52 14.80 ?  132 PHE   A HB3  1 
ATOM   2941 H HD1  A PHE   A 1 132 ? 19.764 1.450   -4.158  0.48 14.41 ?  132 PHE   A HD1  1 
ATOM   2942 H HD1  B PHE   A 1 132 ? 19.485 1.097   -4.158  0.52 15.64 ?  132 PHE   A HD1  1 
ATOM   2943 H HD2  A PHE   A 1 132 ? 21.874 -1.411  -5.999  0.48 13.81 ?  132 PHE   A HD2  1 
ATOM   2944 H HD2  B PHE   A 1 132 ? 21.933 -1.511  -5.951  0.52 15.03 ?  132 PHE   A HD2  1 
ATOM   2945 H HE1  A PHE   A 1 132 ? 21.705 2.255   -3.191  0.48 15.51 ?  132 PHE   A HE1  1 
ATOM   2946 H HE1  B PHE   A 1 132 ? 21.275 1.971   -2.986  0.52 15.71 ?  132 PHE   A HE1  1 
ATOM   2947 H HE2  A PHE   A 1 132 ? 23.815 -0.608  -5.032  0.48 14.64 ?  132 PHE   A HE2  1 
ATOM   2948 H HE2  B PHE   A 1 132 ? 23.722 -0.642  -4.784  0.52 14.64 ?  132 PHE   A HE2  1 
ATOM   2949 H HZ   A PHE   A 1 132 ? 23.731 1.230   -3.626  0.48 15.31 ?  132 PHE   A HZ   1 
ATOM   2950 H HZ   B PHE   A 1 132 ? 23.397 1.105   -3.298  0.52 14.83 ?  132 PHE   A HZ   1 
ATOM   2951 N N    A GLY   A 1 133 ? 16.487 -0.316  -7.783  0.48 11.41 ?  133 GLY   A N    1 
ATOM   2952 N N    B GLY   A 1 133 ? 16.583 -0.723  -7.947  0.52 14.07 ?  133 GLY   A N    1 
ATOM   2953 C CA   A GLY   A 1 133 ? 15.714 -0.649  -8.958  0.48 11.84 ?  133 GLY   A CA   1 
ATOM   2954 C CA   B GLY   A 1 133 ? 15.792 -1.112  -9.097  0.52 15.12 ?  133 GLY   A CA   1 
ATOM   2955 C C    A GLY   A 1 133 ? 15.364 -2.105  -9.175  0.48 12.34 ?  133 GLY   A C    1 
ATOM   2956 C C    B GLY   A 1 133 ? 15.529 -2.594  -9.280  0.52 15.87 ?  133 GLY   A C    1 
ATOM   2957 O O    A GLY   A 1 133 ? 14.687 -2.404  -10.167 0.48 12.87 ?  133 GLY   A O    1 
ATOM   2958 O O    B GLY   A 1 133 ? 14.925 -2.969  -10.294 0.52 17.49 ?  133 GLY   A O    1 
ATOM   2959 H H    A GLY   A 1 133 ? 16.006 -0.095  -7.102  0.48 13.67 ?  133 GLY   A H    1 
ATOM   2960 H H    B GLY   A 1 133 ? 16.118 -0.521  -7.254  0.52 16.85 ?  133 GLY   A H    1 
ATOM   2961 H HA2  A GLY   A 1 133 ? 14.875 -0.175  -8.915  0.48 14.18 ?  133 GLY   A HA2  1 
ATOM   2962 H HA2  B GLY   A 1 133 ? 14.933 -0.665  -9.044  0.52 18.12 ?  133 GLY   A HA2  1 
ATOM   2963 H HA3  A GLY   A 1 133 ? 16.191 -0.348  -9.748  0.48 14.18 ?  133 GLY   A HA3  1 
ATOM   2964 H HA3  B GLY   A 1 133 ? 16.238 -0.796  -9.899  0.52 18.12 ?  133 GLY   A HA3  1 
ATOM   2965 N N    A ALA   A 1 134 ? 15.789 -3.021  -8.305  0.48 12.19 ?  134 ALA   A N    1 
ATOM   2966 N N    B ALA   A 1 134 ? 15.949 -3.449  -8.353  0.52 15.73 ?  134 ALA   A N    1 
ATOM   2967 C CA   A ALA   A 1 134 ? 15.459 -4.425  -8.507  0.48 12.26 ?  134 ALA   A CA   1 
ATOM   2968 C CA   B ALA   A 1 134 ? 15.695 -4.871  -8.526  0.52 15.78 ?  134 ALA   A CA   1 
ATOM   2969 C C    A ALA   A 1 134 ? 14.106 -4.762  -7.876  0.48 12.09 ?  134 ALA   A C    1 
ATOM   2970 C C    B ALA   A 1 134 ? 14.306 -5.248  -8.014  0.52 15.74 ?  134 ALA   A C    1 
ATOM   2971 O O    A ALA   A 1 134 ? 13.542 -3.990  -7.097  0.48 13.01 ?  134 ALA   A O    1 
ATOM   2972 O O    B ALA   A 1 134 ? 13.659 -4.501  -7.275  0.52 16.47 ?  134 ALA   A O    1 
ATOM   2973 C CB   A ALA   A 1 134 ? 16.552 -5.335  -7.947  0.48 13.33 ?  134 ALA   A CB   1 
ATOM   2974 C CB   B ALA   A 1 134 ? 16.746 -5.705  -7.799  0.52 16.02 ?  134 ALA   A CB   1 
ATOM   2975 H H    A ALA   A 1 134 ? 16.270 -2.857  -7.601  0.48 14.60 ?  134 ALA   A H    1 
ATOM   2976 H H    B ALA   A 1 134 ? 16.381 -3.236  -7.637  0.52 18.85 ?  134 ALA   A H    1 
ATOM   2977 H HA   A ALA   A 1 134 ? 15.398 -4.592  -9.461  0.48 14.68 ?  134 ALA   A HA   1 
ATOM   2978 H HA   B ALA   A 1 134 ? 15.747 -5.084  -9.473  0.52 18.92 ?  134 ALA   A HA   1 
ATOM   2979 H HB1  A ALA   A 1 134 ? 16.313 -6.256  -8.126  0.48 15.98 ?  134 ALA   A HB1  1 
ATOM   2980 H HB1  B ALA   A 1 134 ? 16.555 -6.644  -7.946  0.52 19.20 ?  134 ALA   A HB1  1 
ATOM   2981 H HB2  A ALA   A 1 134 ? 17.393 -5.120  -8.382  0.48 15.98 ?  134 ALA   A HB2  1 
ATOM   2982 H HB2  B ALA   A 1 134 ? 17.622 -5.486  -8.153  0.52 19.20 ?  134 ALA   A HB2  1 
ATOM   2983 H HB3  A ALA   A 1 134 ? 16.626 -5.188  -6.993  0.48 15.98 ?  134 ALA   A HB3  1 
ATOM   2984 H HB3  B ALA   A 1 134 ? 16.708 -5.501  -6.853  0.52 19.20 ?  134 ALA   A HB3  1 
ATOM   2985 N N    A ASP   A 1 135 ? 13.582 -5.934  -8.236  0.48 11.91 ?  135 ASP   A N    1 
ATOM   2986 N N    B ASP   A 1 135 ? 13.853 -6.428  -8.426  0.52 15.47 ?  135 ASP   A N    1 
ATOM   2987 C CA   A ASP   A 1 135 ? 12.331 -6.431  -7.660  0.48 13.03 ?  135 ASP   A CA   1 
ATOM   2988 C CA   B ASP   A 1 135 ? 12.593 -6.987  -7.949  0.52 15.72 ?  135 ASP   A CA   1 
ATOM   2989 C C    A ASP   A 1 135 ? 12.578 -6.898  -6.229  0.48 12.60 ?  135 ASP   A C    1 
ATOM   2990 C C    B ASP   A 1 135 ? 12.747 -7.368  -6.482  0.52 14.80 ?  135 ASP   A C    1 
ATOM   2991 O O    A ASP   A 1 135 ? 13.328 -7.862  -6.024  0.48 12.39 ?  135 ASP   A O    1 
ATOM   2992 O O    B ASP   A 1 135 ? 13.548 -8.256  -6.166  0.52 15.09 ?  135 ASP   A O    1 
ATOM   2993 C CB   A ASP   A 1 135 ? 11.811 -7.593  -8.507  0.48 15.63 ?  135 ASP   A CB   1 
ATOM   2994 C CB   B ASP   A 1 135 ? 12.280 -8.232  -8.773  0.52 17.48 ?  135 ASP   A CB   1 
ATOM   2995 C CG   A ASP   A 1 135 ? 10.462 -8.131  -8.028  0.48 17.77 ?  135 ASP   A CG   1 
ATOM   2996 C CG   B ASP   A 1 135 ? 10.946 -8.865  -8.410  0.52 19.12 ?  135 ASP   A CG   1 
ATOM   2997 O OD1  A ASP   A 1 135 ? 9.992  -7.726  -6.944  0.48 18.32 ?  135 ASP   A OD1  1 
ATOM   2998 O OD1  B ASP   A 1 135 ? 10.396 -8.568  -7.329  0.52 19.37 ?  135 ASP   A OD1  1 
ATOM   2999 O OD2  A ASP   A 1 135 ? 9.860  -8.951  -8.758  0.48 19.46 -1 135 ASP   A OD2  1 
ATOM   3000 O OD2  B ASP   A 1 135 ? 10.460 -9.683  -9.215  0.52 20.55 -1 135 ASP   A OD2  1 
ATOM   3001 H H    A ASP   A 1 135 ? 13.927 -6.454  -8.825  0.48 14.27 ?  135 ASP   A H    1 
ATOM   3002 H H    B ASP   A 1 135 ? 14.267 -6.931  -8.987  0.52 18.54 ?  135 ASP   A H    1 
ATOM   3003 H HA   A ASP   A 1 135 ? 11.667 -5.721  -7.671  0.48 15.61 ?  135 ASP   A HA   1 
ATOM   3004 H HA   B ASP   A 1 135 ? 11.878 -6.344  -8.061  0.52 18.84 ?  135 ASP   A HA   1 
ATOM   3005 H HB2  A ASP   A 1 135 ? 11.665 -7.285  -9.408  0.48 18.73 ?  135 ASP   A HB2  1 
ATOM   3006 H HB2  B ASP   A 1 135 ? 12.264 -7.994  -9.715  0.52 20.95 ?  135 ASP   A HB2  1 
ATOM   3007 H HB3  A ASP   A 1 135 ? 12.477 -8.301  -8.496  0.48 18.73 ?  135 ASP   A HB3  1 
ATOM   3008 H HB3  B ASP   A 1 135 ? 12.966 -8.900  -8.615  0.52 20.95 ?  135 ASP   A HB3  1 
ATOM   3009 N N    A PRO   A 1 136 ? 11.981 -6.259  -5.218  0.48 12.35 ?  136 PRO   A N    1 
ATOM   3010 N N    B PRO   A 1 136 ? 12.013 -6.741  -5.559  0.52 14.22 ?  136 PRO   A N    1 
ATOM   3011 C CA   A PRO   A 1 136 ? 12.252 -6.673  -3.829  0.48 12.47 ?  136 PRO   A CA   1 
ATOM   3012 C CA   B PRO   A 1 136 ? 12.207 -7.063  -4.135  0.52 13.83 ?  136 PRO   A CA   1 
ATOM   3013 C C    A PRO   A 1 136 ? 11.801 -8.089  -3.510  0.48 12.22 ?  136 PRO   A C    1 
ATOM   3014 C C    B PRO   A 1 136 ? 11.804 -8.481  -3.762  0.52 13.26 ?  136 PRO   A C    1 
ATOM   3015 O O    A PRO   A 1 136 ? 12.377 -8.731  -2.621  0.48 12.03 ?  136 PRO   A O    1 
ATOM   3016 O O    B PRO   A 1 136 ? 12.414 -9.064  -2.856  0.52 13.22 ?  136 PRO   A O    1 
ATOM   3017 C CB   A PRO   A 1 136 ? 11.501 -5.622  -2.998  0.48 12.90 ?  136 PRO   A CB   1 
ATOM   3018 C CB   B PRO   A 1 136 ? 11.354 -6.008  -3.416  0.52 14.36 ?  136 PRO   A CB   1 
ATOM   3019 C CG   A PRO   A 1 136 ? 10.445 -5.096  -3.920  0.48 13.61 ?  136 PRO   A CG   1 
ATOM   3020 C CG   B PRO   A 1 136 ? 10.343 -5.572  -4.439  0.52 14.85 ?  136 PRO   A CG   1 
ATOM   3021 C CD   A PRO   A 1 136 ? 11.062 -5.110  -5.281  0.48 13.30 ?  136 PRO   A CD   1 
ATOM   3022 C CD   B PRO   A 1 136 ? 11.031 -5.661  -5.762  0.52 14.72 ?  136 PRO   A CD   1 
ATOM   3023 H HA   A PRO   A 1 136 ? 13.202 -6.589  -3.639  0.48 14.94 ?  136 PRO   A HA   1 
ATOM   3024 H HA   B PRO   A 1 136 ? 13.137 -6.934  -3.888  0.52 16.57 ?  136 PRO   A HA   1 
ATOM   3025 H HB2  A PRO   A 1 136 ? 11.099 -6.038  -2.222  0.48 15.45 ?  136 PRO   A HB2  1 
ATOM   3026 H HB2  B PRO   A 1 136 ? 10.916 -6.409  -2.648  0.52 17.21 ?  136 PRO   A HB2  1 
ATOM   3027 H HB3  A PRO   A 1 136 ? 12.106 -4.907  -2.732  0.48 15.45 ?  136 PRO   A HB3  1 
ATOM   3028 H HB3  B PRO   A 1 136 ? 11.914 -5.265  -3.144  0.52 17.21 ?  136 PRO   A HB3  1 
ATOM   3029 H HG2  A PRO   A 1 136 ? 9.671  -5.679  -3.893  0.48 16.30 ?  136 PRO   A HG2  1 
ATOM   3030 H HG2  B PRO   A 1 136 ? 9.579  -6.167  -4.415  0.52 17.79 ?  136 PRO   A HG2  1 
ATOM   3031 H HG3  A PRO   A 1 136 ? 10.204 -4.193  -3.663  0.48 16.30 ?  136 PRO   A HG3  1 
ATOM   3032 H HG3  B PRO   A 1 136 ? 10.074 -4.659  -4.260  0.52 17.79 ?  136 PRO   A HG3  1 
ATOM   3033 H HD2  A PRO   A 1 136 ? 10.383 -5.257  -5.959  0.48 15.94 ?  136 PRO   A HD2  1 
ATOM   3034 H HD2  B PRO   A 1 136 ? 10.404 -5.912  -6.459  0.52 17.63 ?  136 PRO   A HD2  1 
ATOM   3035 H HD3  A PRO   A 1 136 ? 11.551 -4.284  -5.445  0.48 15.94 ?  136 PRO   A HD3  1 
ATOM   3036 H HD3  B PRO   A 1 136 ? 11.484 -4.829  -5.976  0.52 17.63 ?  136 PRO   A HD3  1 
ATOM   3037 N N    A ILE   A 1 137 ? 10.772 -8.593  -4.193  0.48 12.63 ?  137 ILE   A N    1 
ATOM   3038 N N    B ILE   A 1 137 ? 10.787 -9.051  -4.416  0.52 13.61 ?  137 ILE   A N    1 
ATOM   3039 C CA   A ILE   A 1 137 ? 10.386 -9.987  -3.999  0.48 13.13 ?  137 ILE   A CA   1 
ATOM   3040 C CA   B ILE   A 1 137 ? 10.433 -10.446 -4.162  0.52 14.36 ?  137 ILE   A CA   1 
ATOM   3041 C C    A ILE   A 1 137 ? 11.526 -10.905 -4.419  0.48 13.00 ?  137 ILE   A C    1 
ATOM   3042 C C    B ILE   A 1 137 ? 11.613 -11.352 -4.483  0.52 14.29 ?  137 ILE   A C    1 
ATOM   3043 O O    A ILE   A 1 137 ? 11.819 -11.906 -3.753  0.48 13.36 ?  137 ILE   A O    1 
ATOM   3044 O O    B ILE   A 1 137 ? 11.941 -12.270 -3.720  0.52 14.43 ?  137 ILE   A O    1 
ATOM   3045 C CB   A ILE   A 1 137 ? 9.079  -10.298 -4.752  0.48 14.09 ?  137 ILE   A CB   1 
ATOM   3046 C CB   B ILE   A 1 137 ? 9.174  -10.842 -4.960  0.52 15.09 ?  137 ILE   A CB   1 
ATOM   3047 C CG1  A ILE   A 1 137 ? 7.923  -9.480  -4.175  0.48 15.21 ?  137 ILE   A CG1  1 
ATOM   3048 C CG1  B ILE   A 1 137 ? 7.957  -10.033 -4.503  0.52 15.49 ?  137 ILE   A CG1  1 
ATOM   3049 C CG2  A ILE   A 1 137 ? 8.760  -11.788 -4.686  0.48 14.77 ?  137 ILE   A CG2  1 
ATOM   3050 C CG2  B ILE   A 1 137 ? 8.902  -12.344 -4.829  0.52 15.42 ?  137 ILE   A CG2  1 
ATOM   3051 C CD1  A ILE   A 1 137 ? 6.608  -9.731  -4.863  0.48 16.21 ?  137 ILE   A CD1  1 
ATOM   3052 C CD1  B ILE   A 1 137 ? 6.723  -10.238 -5.370  0.52 16.20 ?  137 ILE   A CD1  1 
ATOM   3053 H H    A ILE   A 1 137 ? 10.291 -8.150  -4.760  0.48 15.13 ?  137 ILE   A H    1 
ATOM   3054 H H    B ILE   A 1 137 ? 10.296 -8.661  -5.002  0.52 16.31 ?  137 ILE   A H    1 
ATOM   3055 H HA   A ILE   A 1 137 ? 10.224 -10.126 -3.056  0.48 15.73 ?  137 ILE   A HA   1 
ATOM   3056 H HA   B ILE   A 1 137 ? 10.231 -10.556 -3.223  0.52 17.21 ?  137 ILE   A HA   1 
ATOM   3057 H HB   A ILE   A 1 137 ? 9.189  -10.044 -5.680  0.48 16.89 ?  137 ILE   A HB   1 
ATOM   3058 H HB   B ILE   A 1 137 ? 9.330  -10.649 -5.895  0.52 18.08 ?  137 ILE   A HB   1 
ATOM   3059 H HG12 A ILE   A 1 137 ? 7.812  -9.700  -3.236  0.48 18.23 ?  137 ILE   A HG12 1 
ATOM   3060 H HG12 B ILE   A 1 137 ? 7.729  -10.294 -3.597  0.52 18.57 ?  137 ILE   A HG12 1 
ATOM   3061 H HG13 A ILE   A 1 137 ? 8.125  -8.531  -4.265  0.48 18.23 ?  137 ILE   A HG13 1 
ATOM   3062 H HG13 B ILE   A 1 137 ? 8.183  -9.091  -4.527  0.52 18.57 ?  137 ILE   A HG13 1 
ATOM   3063 H HG21 A ILE   A 1 137 ? 8.010  -11.977 -5.266  0.48 17.70 ?  137 ILE   A HG21 1 
ATOM   3064 H HG21 B ILE   A 1 137 ? 8.034  -12.549 -5.211  0.52 18.49 ?  137 ILE   A HG21 1 
ATOM   3065 H HG22 A ILE   A 1 137 ? 9.525  -12.296 -4.986  0.48 17.70 ?  137 ILE   A HG22 1 
ATOM   3066 H HG22 B ILE   A 1 137 ? 9.588  -12.834 -5.308  0.52 18.49 ?  137 ILE   A HG22 1 
ATOM   3067 H HG23 A ILE   A 1 137 ? 8.543  -12.019 -3.771  0.48 17.70 ?  137 ILE   A HG23 1 
ATOM   3068 H HG23 B ILE   A 1 137 ? 8.913  -12.585 -3.891  0.52 18.49 ?  137 ILE   A HG23 1 
ATOM   3069 H HD11 A ILE   A 1 137 ? 5.926  -9.274  -4.360  0.48 19.43 ?  137 ILE   A HD11 1 
ATOM   3070 H HD11 B ILE   A 1 137 ? 6.059  -9.573  -5.136  0.52 19.41 ?  137 ILE   A HD11 1 
ATOM   3071 H HD12 A ILE   A 1 137 ? 6.649  -9.387  -5.771  0.48 19.43 ?  137 ILE   A HD12 1 
ATOM   3072 H HD12 B ILE   A 1 137 ? 6.973  -10.142 -6.303  0.52 19.41 ?  137 ILE   A HD12 1 
ATOM   3073 H HD13 A ILE   A 1 137 ? 6.412  -10.681 -4.875  0.48 19.43 ?  137 ILE   A HD13 1 
ATOM   3074 H HD13 B ILE   A 1 137 ? 6.367  -11.127 -5.215  0.52 19.41 ?  137 ILE   A HD13 1 
ATOM   3075 N N    A HIS   A 1 138 ? 12.182 -10.579 -5.536  0.48 12.61 ?  138 HIS   A N    1 
ATOM   3076 N N    B HIS   A 1 138 ? 12.272 -11.105 -5.617  0.52 13.76 ?  138 HIS   A N    1 
ATOM   3077 C CA   A HIS   A 1 138 ? 13.351 -11.346 -5.957  0.48 12.23 ?  138 HIS   A CA   1 
ATOM   3078 C CA   B HIS   A 1 138 ? 13.441 -11.895 -5.983  0.52 13.81 ?  138 HIS   A CA   1 
ATOM   3079 C C    A HIS   A 1 138 ? 14.487 -11.227 -4.944  0.48 12.05 ?  138 HIS   A C    1 
ATOM   3080 C C    B HIS   A 1 138 ? 14.566 -11.702 -4.979  0.52 12.91 ?  138 HIS   A C    1 
ATOM   3081 O O    A HIS   A 1 138 ? 15.148 -12.222 -4.621  0.48 12.36 ?  138 HIS   A O    1 
ATOM   3082 O O    B HIS   A 1 138 ? 15.237 -12.666 -4.591  0.52 13.09 ?  138 HIS   A O    1 
ATOM   3083 C CB   A HIS   A 1 138 ? 13.792 -10.889 -7.348  0.48 12.07 ?  138 HIS   A CB   1 
ATOM   3084 C CB   B HIS   A 1 138 ? 13.911 -11.500 -7.382  0.52 15.05 ?  138 HIS   A CB   1 
ATOM   3085 C CG   A HIS   A 1 138 ? 15.068 -11.520 -7.813  0.48 12.86 ?  138 HIS   A CG   1 
ATOM   3086 C CG   B HIS   A 1 138 ? 15.183 -12.167 -7.805  0.52 16.38 ?  138 HIS   A CG   1 
ATOM   3087 N ND1  A HIS   A 1 138 ? 15.184 -12.870 -8.072  0.48 14.01 ?  138 HIS   A ND1  1 
ATOM   3088 N ND1  B HIS   A 1 138 ? 15.279 -13.527 -8.012  0.52 17.05 ?  138 HIS   A ND1  1 
ATOM   3089 C CD2  A HIS   A 1 138 ? 16.288 -10.986 -8.057  0.48 13.06 ?  138 HIS   A CD2  1 
ATOM   3090 C CD2  B HIS   A 1 138 ? 16.412 -11.661 -8.064  0.52 17.13 ?  138 HIS   A CD2  1 
ATOM   3091 C CE1  A HIS   A 1 138 ? 16.418 -13.138 -8.460  0.48 14.01 ?  138 HIS   A CE1  1 
ATOM   3092 C CE1  B HIS   A 1 138 ? 16.511 -13.830 -8.380  0.52 17.56 ?  138 HIS   A CE1  1 
ATOM   3093 N NE2  A HIS   A 1 138 ? 17.108 -12.012 -8.460  0.48 13.39 ?  138 HIS   A NE2  1 
ATOM   3094 N NE2  B HIS   A 1 138 ? 17.219 -12.716 -8.418  0.52 17.33 ?  138 HIS   A NE2  1 
ATOM   3095 H H    A HIS   A 1 138 ? 11.964 -9.930  -6.066  0.48 15.11 ?  138 HIS   A H    1 
ATOM   3096 H H    B HIS   A 1 138 ? 12.070 -10.487 -6.180  0.52 16.49 ?  138 HIS   A H    1 
ATOM   3097 H HA   A HIS   A 1 138 ? 13.102 -12.276 -6.020  0.48 14.65 ?  138 HIS   A HA   1 
ATOM   3098 H HA   B HIS   A 1 138 ? 13.201 -12.835 -5.999  0.52 16.55 ?  138 HIS   A HA   1 
ATOM   3099 H HB2  A HIS   A 1 138 ? 13.097 -11.115 -7.990  0.48 14.46 ?  138 HIS   A HB2  1 
ATOM   3100 H HB2  B HIS   A 1 138 ? 13.226 -11.740 -8.023  0.52 18.04 ?  138 HIS   A HB2  1 
ATOM   3101 H HB3  A HIS   A 1 138 ? 13.922 -9.925  -7.340  0.48 14.46 ?  138 HIS   A HB3  1 
ATOM   3102 H HB3  B HIS   A 1 138 ? 14.063 -10.543 -7.402  0.52 18.04 ?  138 HIS   A HB3  1 
ATOM   3103 H HD1  B HIS   A 1 138 ? 14.636 -14.090 -7.917  0.52 20.44 ?  138 HIS   A HD1  1 
ATOM   3104 H HD2  A HIS   A 1 138 ? 16.525 -10.091 -7.973  0.48 15.65 ?  138 HIS   A HD2  1 
ATOM   3105 H HD2  B HIS   A 1 138 ? 16.666 -10.771 -8.013  0.52 20.53 ?  138 HIS   A HD2  1 
ATOM   3106 H HE1  A HIS   A 1 138 ? 16.738 -13.979 -8.690  0.48 16.78 ?  138 HIS   A HE1  1 
ATOM   3107 H HE1  B HIS   A 1 138 ? 16.822 -14.684 -8.577  0.52 21.05 ?  138 HIS   A HE1  1 
ATOM   3108 H HE2  A HIS   A 1 138 ? 17.935 -11.937 -8.675  0.48 16.04 ?  138 HIS   A HE2  1 
ATOM   3109 N N    A SER   A 1 139 ? 14.721 -10.020 -4.421  0.48 11.40 ?  139 SER   A N    1 
ATOM   3110 N N    B SER   A 1 139 ? 14.796 -10.461 -4.549  0.52 12.11 ?  139 SER   A N    1 
ATOM   3111 C CA   A SER   A 1 139 ? 15.796 -9.829  -3.450  0.48 11.42 ?  139 SER   A CA   1 
ATOM   3112 C CA   B SER   A 1 139 ? 15.866 -10.221 -3.590  0.52 11.37 ?  139 SER   A CA   1 
ATOM   3113 C C    A SER   A 1 139 ? 15.614 -10.723 -2.223  0.48 11.75 ?  139 SER   A C    1 
ATOM   3114 C C    B SER   A 1 139 ? 15.606 -10.949 -2.281  0.52 11.41 ?  139 SER   A C    1 
ATOM   3115 O O    A SER   A 1 139 ? 16.589 -11.269 -1.690  0.48 11.73 ?  139 SER   A O    1 
ATOM   3116 O O    B SER   A 1 139 ? 16.522 -11.557 -1.714  0.52 10.97 ?  139 SER   A O    1 
ATOM   3117 C CB   A SER   A 1 139 ? 15.886 -8.351  -3.057  0.48 10.98 ?  139 SER   A CB   1 
ATOM   3118 C CB   B SER   A 1 139 ? 16.046 -8.728  -3.336  0.52 10.38 ?  139 SER   A CB   1 
ATOM   3119 O OG   A SER   A 1 139 ? 16.934 -8.157  -2.119  0.48 11.18 ?  139 SER   A OG   1 
ATOM   3120 O OG   B SER   A 1 139 ? 17.111 -8.531  -2.420  0.52 10.06 ?  139 SER   A OG   1 
ATOM   3121 H H    A SER   A 1 139 ? 14.284 -9.301  -4.612  0.48 13.66 ?  139 SER   A H    1 
ATOM   3122 H H    B SER   A 1 139 ? 14.360 -9.766  -4.789  0.52 14.50 ?  139 SER   A H    1 
ATOM   3123 H HA   A SER   A 1 139 ? 16.639 -10.064 -3.861  0.48 13.68 ?  139 SER   A HA   1 
ATOM   3124 H HA   B SER   A 1 139 ? 16.697 -10.564 -3.957  0.52 13.62 ?  139 SER   A HA   1 
ATOM   3125 H HB2  A SER   A 1 139 ? 16.054 -7.812  -3.857  0.48 13.15 ?  139 SER   A HB2  1 
ATOM   3126 H HB2  B SER   A 1 139 ? 16.274 -8.292  -4.168  0.52 12.43 ?  139 SER   A HB2  1 
ATOM   3127 H HB3  A SER   A 1 139 ? 15.048 -8.066  -2.655  0.48 13.15 ?  139 SER   A HB3  1 
ATOM   3128 H HB3  B SER   A 1 139 ? 15.227 -8.368  -2.971  0.52 12.43 ?  139 SER   A HB3  1 
ATOM   3129 H HG   A SER   A 1 139 ? 17.680 -8.245  -2.493  0.48 13.39 ?  139 SER   A HG   1 
ATOM   3130 H HG   B SER   A 1 139 ? 17.208 -7.717  -2.256  0.52 12.05 ?  139 SER   A HG   1 
ATOM   3131 N N    . LEU   A 1 140 ? 14.372 -10.891 -1.770  1.00 11.94 ?  140 LEU   A N    1 
ATOM   3132 C CA   . LEU   A 1 140 ? 14.091 -11.665 -0.565  1.00 12.06 ?  140 LEU   A CA   1 
ATOM   3133 C C    . LEU   A 1 140 ? 14.336 -13.151 -0.813  1.00 12.14 ?  140 LEU   A C    1 
ATOM   3134 O O    . LEU   A 1 140 ? 14.878 -13.856 0.050   1.00 12.94 ?  140 LEU   A O    1 
ATOM   3135 C CB   . LEU   A 1 140 ? 12.657 -11.408 -0.097  1.00 12.15 ?  140 LEU   A CB   1 
ATOM   3136 C CG   . LEU   A 1 140 ? 12.204 -12.183 1.140   1.00 12.98 ?  140 LEU   A CG   1 
ATOM   3137 C CD1  . LEU   A 1 140 ? 13.133 -11.958 2.324   1.00 13.38 ?  140 LEU   A CD1  1 
ATOM   3138 C CD2  . LEU   A 1 140 ? 10.757 -11.825 1.493   1.00 14.05 ?  140 LEU   A CD2  1 
ATOM   3139 H H    A LEU   A 1 140 ? 13.671 -10.571 -2.150  0.48 14.30 ?  140 LEU   A H    1 
ATOM   3140 H H    B LEU   A 1 140 ? 13.716 -10.434 -2.084  0.52 14.30 ?  140 LEU   A H    1 
ATOM   3141 H HA   . LEU   A 1 140 ? 14.689 -11.380 0.140   1.00 14.45 ?  140 LEU   A HA   1 
ATOM   3142 H HB2  . LEU   A 1 140 ? 12.567 -10.466 0.105   1.00 14.56 ?  140 LEU   A HB2  1 
ATOM   3143 H HB3  . LEU   A 1 140 ? 12.053 -11.641 -0.821  1.00 14.56 ?  140 LEU   A HB3  1 
ATOM   3144 H HG   . LEU   A 1 140 ? 12.216 -13.131 0.931   1.00 15.55 ?  140 LEU   A HG   1 
ATOM   3145 H HD11 . LEU   A 1 140 ? 12.750 -12.383 3.108   1.00 16.03 ?  140 LEU   A HD11 1 
ATOM   3146 H HD12 . LEU   A 1 140 ? 13.995 -12.357 2.123   1.00 16.03 ?  140 LEU   A HD12 1 
ATOM   3147 H HD13 . LEU   A 1 140 ? 13.229 -11.009 2.472   1.00 16.03 ?  140 LEU   A HD13 1 
ATOM   3148 H HD21 . LEU   A 1 140 ? 10.489 -12.329 2.276   1.00 16.84 ?  140 LEU   A HD21 1 
ATOM   3149 H HD22 . LEU   A 1 140 ? 10.703 -10.875 1.673   1.00 16.84 ?  140 LEU   A HD22 1 
ATOM   3150 H HD23 . LEU   A 1 140 ? 10.183 -12.052 0.742   1.00 16.84 ?  140 LEU   A HD23 1 
ATOM   3151 N N    . ARG   A 1 141 ? 13.950 -13.641 -1.994  1.00 13.08 ?  141 ARG   A N    1 
ATOM   3152 C CA   . ARG   A 1 141 ? 14.191 -15.035 -2.347  1.00 14.64 ?  141 ARG   A CA   1 
ATOM   3153 C C    . ARG   A 1 141 ? 15.687 -15.341 -2.351  1.00 14.06 ?  141 ARG   A C    1 
ATOM   3154 O O    . ARG   A 1 141 ? 16.133 -16.343 -1.780  1.00 14.25 ?  141 ARG   A O    1 
ATOM   3155 C CB   . ARG   A 1 141 ? 13.582 -15.303 -3.724  1.00 16.13 ?  141 ARG   A CB   1 
ATOM   3156 C CG   . ARG   A 1 141 ? 13.611 -16.742 -4.182  1.00 18.06 ?  141 ARG   A CG   1 
ATOM   3157 C CD   . ARG   A 1 141 ? 12.594 -17.553 -3.438  1.00 19.52 ?  141 ARG   A CD   1 
ATOM   3158 N NE   . ARG   A 1 141 ? 13.191 -18.305 -2.346  1.00 20.19 ?  141 ARG   A NE   1 
ATOM   3159 C CZ   . ARG   A 1 141 ? 12.495 -18.845 -1.354  1.00 20.71 ?  141 ARG   A CZ   1 
ATOM   3160 N NH1  . ARG   A 1 141 ? 11.207 -18.593 -1.200  1.00 20.36 ?  141 ARG   A NH1  1 
ATOM   3161 N NH2  . ARG   A 1 141 ? 13.108 -19.648 -0.491  1.00 21.66 ?  141 ARG   A NH2  1 
ATOM   3162 H H    . ARG   A 1 141 ? 13.554 -13.185 -2.603  1.00 15.67 ?  141 ARG   A H    1 
ATOM   3163 H HA   . ARG   A 1 141 ? 13.762 -15.615 -1.701  1.00 17.54 ?  141 ARG   A HA   1 
ATOM   3164 H HB2  . ARG   A 1 141 ? 12.657 -15.013 -3.713  1.00 19.34 ?  141 ARG   A HB2  1 
ATOM   3165 H HB3  . ARG   A 1 141 ? 14.073 -14.783 -4.380  1.00 19.34 ?  141 ARG   A HB3  1 
ATOM   3166 H HG2  . ARG   A 1 141 ? 13.408 -16.783 -5.130  1.00 21.65 ?  141 ARG   A HG2  1 
ATOM   3167 H HG3  . ARG   A 1 141 ? 14.491 -17.120 -4.012  1.00 21.65 ?  141 ARG   A HG3  1 
ATOM   3168 H HD2  . ARG   A 1 141 ? 11.925 -16.959 -3.061  1.00 23.40 ?  141 ARG   A HD2  1 
ATOM   3169 H HD3  . ARG   A 1 141 ? 12.174 -18.177 -4.051  1.00 23.40 ?  141 ARG   A HD3  1 
ATOM   3170 H HE   . ARG   A 1 141 ? 14.024 -18.505 -2.407  1.00 24.20 ?  141 ARG   A HE   1 
ATOM   3171 H HH11 . ARG   A 1 141 ? 10.793 -18.089 -1.759  1.00 24.41 ?  141 ARG   A HH11 1 
ATOM   3172 H HH12 . ARG   A 1 141 ? 10.776 -18.952 -0.548  1.00 24.41 ?  141 ARG   A HH12 1 
ATOM   3173 H HH21 . ARG   A 1 141 ? 13.951 -19.811 -0.578  1.00 25.97 ?  141 ARG   A HH21 1 
ATOM   3174 H HH22 . ARG   A 1 141 ? 12.673 -19.990 0.166   1.00 25.97 ?  141 ARG   A HH22 1 
ATOM   3175 N N    . VAL   A 1 142 ? 16.482 -14.486 -3.004  1.00 13.46 ?  142 VAL   A N    1 
ATOM   3176 C CA   . VAL   A 1 142 ? 17.931 -14.688 -3.022  1.00 13.47 ?  142 VAL   A CA   1 
ATOM   3177 C C    . VAL   A 1 142 ? 18.491 -14.653 -1.605  1.00 12.42 ?  142 VAL   A C    1 
ATOM   3178 O O    . VAL   A 1 142 ? 19.346 -15.467 -1.242  1.00 12.76 ?  142 VAL   A O    1 
ATOM   3179 C CB   . VAL   A 1 142 ? 18.630 -13.681 -3.957  1.00 13.89 ?  142 VAL   A CB   1 
ATOM   3180 C CG1  . VAL   A 1 142 ? 20.139 -13.877 -3.895  1.00 13.53 ?  142 VAL   A CG1  1 
ATOM   3181 C CG2  . VAL   A 1 142 ? 18.141 -13.850 -5.389  1.00 14.99 ?  142 VAL   A CG2  1 
ATOM   3182 H H    . VAL   A 1 142 ? 16.212 -13.789 -3.433  1.00 16.13 ?  142 VAL   A H    1 
ATOM   3183 H HA   . VAL   A 1 142 ? 18.105 -15.570 -3.377  1.00 16.15 ?  142 VAL   A HA   1 
ATOM   3184 H HB   . VAL   A 1 142 ? 18.430 -12.775 -3.668  1.00 16.64 ?  142 VAL   A HB   1 
ATOM   3185 H HG11 . VAL   A 1 142 ? 20.548 -13.405 -4.635  1.00 16.22 ?  142 VAL   A HG11 1 
ATOM   3186 H HG12 . VAL   A 1 142 ? 20.471 -13.524 -3.053  1.00 16.22 ?  142 VAL   A HG12 1 
ATOM   3187 H HG13 . VAL   A 1 142 ? 20.334 -14.825 -3.957  1.00 16.22 ?  142 VAL   A HG13 1 
ATOM   3188 H HG21 . VAL   A 1 142 ? 18.550 -13.163 -5.941  1.00 17.97 ?  142 VAL   A HG21 1 
ATOM   3189 H HG22 . VAL   A 1 142 ? 18.405 -14.727 -5.706  1.00 17.97 ?  142 VAL   A HG22 1 
ATOM   3190 H HG23 . VAL   A 1 142 ? 17.180 -13.763 -5.407  1.00 17.97 ?  142 VAL   A HG23 1 
ATOM   3191 N N    . CYS   A 1 143 ? 18.020 -13.715 -0.780  1.00 11.94 ?  143 CYS   A N    1 
ATOM   3192 C CA   . CYS   A 1 143 ? 18.481 -13.653 0.603   1.00 11.69 ?  143 CYS   A CA   1 
ATOM   3193 C C    . CYS   A 1 143 ? 18.271 -14.987 1.312   1.00 11.96 ?  143 CYS   A C    1 
ATOM   3194 O O    . CYS   A 1 143 ? 19.202 -15.564 1.883   1.00 12.15 ?  143 CYS   A O    1 
ATOM   3195 C CB   . CYS   A 1 143 ? 17.730 -12.546 1.338   1.00 12.03 ?  143 CYS   A CB   1 
ATOM   3196 S SG   . CYS   A 1 143 ? 18.218 -12.355 3.056   1.00 12.20 ?  143 CYS   A SG   1 
ATOM   3197 H H    . CYS   A 1 143 ? 17.449 -13.116 -0.995  1.00 14.30 ?  143 CYS   A H    1 
ATOM   3198 H HA   . CYS   A 1 143 ? 19.426 -13.449 0.620   1.00 14.00 ?  143 CYS   A HA   1 
ATOM   3199 H HB2  . CYS   A 1 143 ? 17.892 -11.704 0.885   1.00 14.41 ?  143 CYS   A HB2  1 
ATOM   3200 H HB3  . CYS   A 1 143 ? 16.783 -12.747 1.320   1.00 14.41 ?  143 CYS   A HB3  1 
ATOM   3201 H HG   . CYS   A 1 143 ? 17.640 -11.415 3.523   1.00 14.61 ?  143 CYS   A HG   1 
ATOM   3202 N N    . VAL   A 1 144 ? 17.044 -15.492 1.284   1.00 12.85 ?  144 VAL   A N    1 
ATOM   3203 C CA   . VAL   A 1 144 ? 16.719 -16.714 2.011   1.00 14.76 ?  144 VAL   A CA   1 
ATOM   3204 C C    . VAL   A 1 144 ? 17.521 -17.895 1.484   1.00 14.61 ?  144 VAL   A C    1 
ATOM   3205 O O    . VAL   A 1 144 ? 17.886 -18.803 2.244   1.00 15.19 ?  144 VAL   A O    1 
ATOM   3206 C CB   . VAL   A 1 144 ? 15.199 -16.953 1.926   1.00 18.16 ?  144 VAL   A CB   1 
ATOM   3207 C CG1  . VAL   A 1 144 ? 14.835 -18.387 2.262   1.00 20.46 ?  144 VAL   A CG1  1 
ATOM   3208 C CG2  . VAL   A 1 144 ? 14.475 -15.940 2.816   1.00 17.84 ?  144 VAL   A CG2  1 
ATOM   3209 H H    . VAL   A 1 144 ? 16.383 -15.150 0.854   1.00 15.40 ?  144 VAL   A H    1 
ATOM   3210 H HA   . VAL   A 1 144 ? 16.945 -16.599 2.943   1.00 17.69 ?  144 VAL   A HA   1 
ATOM   3211 H HB   . VAL   A 1 144 ? 14.911 -16.788 1.011   1.00 21.77 ?  144 VAL   A HB   1 
ATOM   3212 H HG11 . VAL   A 1 144 ? 13.882 -18.434 2.451   1.00 24.52 ?  144 VAL   A HG11 1 
ATOM   3213 H HG12 . VAL   A 1 144 ? 15.043 -18.956 1.502   1.00 24.52 ?  144 VAL   A HG12 1 
ATOM   3214 H HG13 . VAL   A 1 144 ? 15.339 -18.668 3.038   1.00 24.52 ?  144 VAL   A HG13 1 
ATOM   3215 H HG21 . VAL   A 1 144 ? 13.524 -16.133 2.815   1.00 21.39 ?  144 VAL   A HG21 1 
ATOM   3216 H HG22 . VAL   A 1 144 ? 14.823 -16.004 3.718   1.00 21.39 ?  144 VAL   A HG22 1 
ATOM   3217 H HG23 . VAL   A 1 144 ? 14.627 -15.044 2.467   1.00 21.39 ?  144 VAL   A HG23 1 
ATOM   3218 N N    . ASP   A 1 145 ? 17.776 -17.926 0.179   1.00 14.68 ?  145 ASP   A N    1 
ATOM   3219 C CA   . ASP   A 1 145 ? 18.481 -19.034 -0.456  1.00 15.64 ?  145 ASP   A CA   1 
ATOM   3220 C C    . ASP   A 1 145 ? 20.000 -18.878 -0.435  1.00 15.19 ?  145 ASP   A C    1 
ATOM   3221 O O    . ASP   A 1 145 ? 20.699 -19.758 -0.946  1.00 16.82 ?  145 ASP   A O    1 
ATOM   3222 C CB   . ASP   A 1 145 ? 18.022 -19.174 -1.911  1.00 17.32 ?  145 ASP   A CB   1 
ATOM   3223 C CG   . ASP   A 1 145 ? 16.573 -19.608 -2.029  1.00 19.42 ?  145 ASP   A CG   1 
ATOM   3224 O OD1  . ASP   A 1 145 ? 16.022 -20.154 -1.051  1.00 20.01 ?  145 ASP   A OD1  1 
ATOM   3225 O OD2  . ASP   A 1 145 ? 15.980 -19.400 -3.106  1.00 20.44 -1 145 ASP   A OD2  1 
ATOM   3226 H H    . ASP   A 1 145 ? 17.530 -17.313 -0.372  1.00 17.60 ?  145 ASP   A H    1 
ATOM   3227 H HA   . ASP   A 1 145 ? 18.253 -19.858 0.004   1.00 18.75 ?  145 ASP   A HA   1 
ATOM   3228 H HB2  . ASP   A 1 145 ? 18.116 -18.319 -2.359  1.00 20.75 ?  145 ASP   A HB2  1 
ATOM   3229 H HB3  . ASP   A 1 145 ? 18.560 -19.845 -2.353  1.00 20.75 ?  145 ASP   A HB3  1 
ATOM   3230 N N    . THR   A 1 146 ? 20.527 -17.788 0.113   1.00 13.16 ?  146 THR   A N    1 
ATOM   3231 C CA   . THR   A 1 146 ? 21.970 -17.541 0.132   1.00 12.43 ?  146 THR   A CA   1 
ATOM   3232 C C    . THR   A 1 146 ? 22.526 -17.356 1.532   1.00 12.28 ?  146 THR   A C    1 
ATOM   3233 O O    . THR   A 1 146 ? 23.596 -17.888 1.847   1.00 13.16 ?  146 THR   A O    1 
ATOM   3234 C CB   . THR   A 1 146 ? 22.294 -16.292 -0.706  1.00 11.95 ?  146 THR   A CB   1 
ATOM   3235 O OG1  . THR   A 1 146 ? 21.770 -16.451 -2.027  1.00 12.71 ?  146 THR   A OG1  1 
ATOM   3236 C CG2  . THR   A 1 146 ? 23.795 -16.063 -0.797  1.00 12.09 ?  146 THR   A CG2  1 
ATOM   3237 H H    . THR   A 1 146 ? 20.068 -17.167 0.489   1.00 15.77 ?  146 THR   A H    1 
ATOM   3238 H HA   . THR   A 1 146 ? 22.427 -18.297 -0.268  1.00 14.90 ?  146 THR   A HA   1 
ATOM   3239 H HB   . THR   A 1 146 ? 21.902 -15.511 -0.289  1.00 14.32 ?  146 THR   A HB   1 
ATOM   3240 H HG1  . THR   A 1 146 ? 20.936 -16.524 -1.993  1.00 15.23 ?  146 THR   A HG1  1 
ATOM   3241 H HG21 . THR   A 1 146 ? 23.984 -15.393 -1.471  1.00 14.48 ?  146 THR   A HG21 1 
ATOM   3242 H HG22 . THR   A 1 146 ? 24.141 -15.763 0.055   1.00 14.48 ?  146 THR   A HG22 1 
ATOM   3243 H HG23 . THR   A 1 146 ? 24.238 -16.892 -1.047  1.00 14.48 ?  146 THR   A HG23 1 
ATOM   3244 N N    . VAL   A 1 147 ? 21.845 -16.580 2.365   1.00 12.07 ?  147 VAL   A N    1 
ATOM   3245 C CA   . VAL   A 1 147 ? 22.327 -16.287 3.705   1.00 12.51 ?  147 VAL   A CA   1 
ATOM   3246 C C    . VAL   A 1 147 ? 22.010 -17.460 4.617   1.00 12.42 ?  147 VAL   A C    1 
ATOM   3247 O O    . VAL   A 1 147 ? 20.866 -17.937 4.671   1.00 13.32 ?  147 VAL   A O    1 
ATOM   3248 C CB   . VAL   A 1 147 ? 21.705 -14.985 4.230   1.00 12.01 ?  147 VAL   A CB   1 
ATOM   3249 C CG1  . VAL   A 1 147 ? 22.240 -14.680 5.608   1.00 13.23 ?  147 VAL   A CG1  1 
ATOM   3250 C CG2  . VAL   A 1 147 ? 21.970 -13.830 3.276   1.00 12.17 ?  147 VAL   A CG2  1 
ATOM   3251 H H    . VAL   A 1 147 ? 21.091 -16.208 2.175   1.00 14.46 ?  147 VAL   A H    1 
ATOM   3252 H HA   . VAL   A 1 147 ? 23.290 -16.174 3.675   1.00 14.98 ?  147 VAL   A HA   1 
ATOM   3253 H HB   . VAL   A 1 147 ? 20.745 -15.103 4.301   1.00 14.39 ?  147 VAL   A HB   1 
ATOM   3254 H HG11 . VAL   A 1 147 ? 21.987 -13.779 5.851   1.00 15.85 ?  147 VAL   A HG11 1 
ATOM   3255 H HG12 . VAL   A 1 147 ? 21.857 -15.312 6.243   1.00 15.85 ?  147 VAL   A HG12 1 
ATOM   3256 H HG13 . VAL   A 1 147 ? 23.204 -14.766 5.598   1.00 15.85 ?  147 VAL   A HG13 1 
ATOM   3257 H HG21 . VAL   A 1 147 ? 21.631 -13.012 3.672   1.00 14.58 ?  147 VAL   A HG21 1 
ATOM   3258 H HG22 . VAL   A 1 147 ? 22.925 -13.757 3.129   1.00 14.58 ?  147 VAL   A HG22 1 
ATOM   3259 H HG23 . VAL   A 1 147 ? 21.517 -14.004 2.437   1.00 14.58 ?  147 VAL   A HG23 1 
ATOM   3260 N N    . ARG   A 1 148 ? 23.035 -17.935 5.325   1.00 12.75 ?  148 ARG   A N    1 
ATOM   3261 C CA   . ARG   A 1 148 ? 22.905 -19.018 6.287   1.00 12.80 ?  148 ARG   A CA   1 
ATOM   3262 C C    . ARG   A 1 148 ? 23.038 -18.552 7.725   1.00 13.24 ?  148 ARG   A C    1 
ATOM   3263 O O    . ARG   A 1 148 ? 22.635 -19.284 8.638   1.00 14.77 ?  148 ARG   A O    1 
ATOM   3264 C CB   . ARG   A 1 148 ? 23.943 -20.115 6.000   1.00 13.42 ?  148 ARG   A CB   1 
ATOM   3265 C CG   . ARG   A 1 148 ? 23.762 -20.767 4.639   1.00 14.63 ?  148 ARG   A CG   1 
ATOM   3266 C CD   . ARG   A 1 148 ? 24.848 -21.792 4.332   1.00 15.10 ?  148 ARG   A CD   1 
ATOM   3267 N NE   . ARG   A 1 148 ? 26.185 -21.204 4.356   1.00 15.04 ?  148 ARG   A NE   1 
ATOM   3268 C CZ   . ARG   A 1 148 ? 26.696 -20.457 3.383   1.00 14.51 ?  148 ARG   A CZ   1 
ATOM   3269 N NH1  . ARG   A 1 148 ? 26.026 -20.220 2.266   1.00 14.75 ?  148 ARG   A NH1  1 
ATOM   3270 N NH2  . ARG   A 1 148 ? 27.914 -19.935 3.532   1.00 14.96 ?  148 ARG   A NH2  1 
ATOM   3271 H H    . ARG   A 1 148 ? 23.842 -17.636 5.247   1.00 15.27 ?  148 ARG   A H    1 
ATOM   3272 H HA   . ARG   A 1 148 ? 22.030 -19.414 6.185   1.00 15.34 ?  148 ARG   A HA   1 
ATOM   3273 H HB2  . ARG   A 1 148 ? 24.832 -19.732 6.029   1.00 16.07 ?  148 ARG   A HB2  1 
ATOM   3274 H HB3  . ARG   A 1 148 ? 23.859 -20.811 6.671   1.00 16.07 ?  148 ARG   A HB3  1 
ATOM   3275 H HG2  . ARG   A 1 148 ? 22.904 -21.219 4.616   1.00 17.53 ?  148 ARG   A HG2  1 
ATOM   3276 H HG3  . ARG   A 1 148 ? 23.792 -20.079 3.954   1.00 17.53 ?  148 ARG   A HG3  1 
ATOM   3277 H HD2  . ARG   A 1 148 ? 24.819 -22.494 4.998   1.00 18.10 ?  148 ARG   A HD2  1 
ATOM   3278 H HD3  . ARG   A 1 148 ? 24.697 -22.160 3.447   1.00 18.10 ?  148 ARG   A HD3  1 
ATOM   3279 H HE   . ARG   A 1 148 ? 26.668 -21.336 5.051   1.00 18.02 ?  148 ARG   A HE   1 
ATOM   3280 H HH11 . ARG   A 1 148 ? 25.241 -20.552 2.151   1.00 17.68 ?  148 ARG   A HH11 1 
ATOM   3281 H HH12 . ARG   A 1 148 ? 26.380 -19.737 1.645   1.00 17.68 ?  148 ARG   A HH12 1 
ATOM   3282 H HH21 . ARG   A 1 148 ? 28.352 -20.067 4.255   1.00 17.92 ?  148 ARG   A HH21 1 
ATOM   3283 H HH22 . ARG   A 1 148 ? 28.251 -19.443 2.907   1.00 17.92 ?  148 ARG   A HH22 1 
ATOM   3284 N N    . THR   A 1 149 ? 23.597 -17.366 7.943   1.00 12.90 ?  149 THR   A N    1 
ATOM   3285 C CA   . THR   A 1 149 ? 23.682 -16.781 9.266   1.00 13.06 ?  149 THR   A CA   1 
ATOM   3286 C C    . THR   A 1 149 ? 22.362 -16.082 9.591   1.00 12.80 ?  149 THR   A C    1 
ATOM   3287 O O    . THR   A 1 149 ? 21.420 -16.072 8.793   1.00 13.16 ?  149 THR   A O    1 
ATOM   3288 C CB   . THR   A 1 149 ? 24.883 -15.849 9.325   1.00 13.28 ?  149 THR   A CB   1 
ATOM   3289 O OG1  . THR   A 1 149 ? 24.756 -14.906 8.259   1.00 13.40 ?  149 THR   A OG1  1 
ATOM   3290 C CG2  . THR   A 1 149 ? 26.188 -16.645 9.176   1.00 13.72 ?  149 THR   A CG2  1 
ATOM   3291 H H    . THR   A 1 149 ? 23.944 -16.871 7.326   1.00 15.45 ?  149 THR   A H    1 
ATOM   3292 H HA   . THR   A 1 149 ? 23.813 -17.491 9.914   1.00 15.65 ?  149 THR   A HA   1 
ATOM   3293 H HB   . THR   A 1 149 ? 24.886 -15.390 10.181  1.00 15.91 ?  149 THR   A HB   1 
ATOM   3294 H HG1  . THR   A 1 149 ? 25.402 -14.366 8.278   1.00 16.06 ?  149 THR   A HG1  1 
ATOM   3295 H HG21 . THR   A 1 149 ? 26.950 -16.047 9.238   1.00 16.44 ?  149 THR   A HG21 1 
ATOM   3296 H HG22 . THR   A 1 149 ? 26.257 -17.314 9.876   1.00 16.44 ?  149 THR   A HG22 1 
ATOM   3297 H HG23 . THR   A 1 149 ? 26.212 -17.092 8.313   1.00 16.44 ?  149 THR   A HG23 1 
ATOM   3298 N N    . ASN   A 1 150 ? 22.247 -15.559 10.803  1.00 12.76 ?  150 ASN   A N    1 
ATOM   3299 C CA   . ASN   A 1 150 ? 20.971 -15.045 11.299  1.00 13.59 ?  150 ASN   A CA   1 
ATOM   3300 C C    . ASN   A 1 150 ? 20.800 -13.596 10.858  1.00 12.83 ?  150 ASN   A C    1 
ATOM   3301 O O    . ASN   A 1 150 ? 21.544 -12.710 11.300  1.00 14.34 ?  150 ASN   A O    1 
ATOM   3302 C CB   . ASN   A 1 150 ? 20.920 -15.172 12.816  1.00 16.06 ?  150 ASN   A CB   1 
ATOM   3303 C CG   . ASN   A 1 150 ? 20.796 -16.604 13.263  1.00 20.11 ?  150 ASN   A CG   1 
ATOM   3304 O OD1  . ASN   A 1 150 ? 20.207 -17.424 12.561  1.00 21.66 ?  150 ASN   A OD1  1 
ATOM   3305 N ND2  . ASN   A 1 150 ? 21.360 -16.921 14.424  1.00 22.63 ?  150 ASN   A ND2  1 
ATOM   3306 H H    . ASN   A 1 150 ? 22.893 -15.491 11.362  1.00 15.29 ?  150 ASN   A H    1 
ATOM   3307 H HA   . ASN   A 1 150 ? 20.243 -15.574 10.926  1.00 16.29 ?  150 ASN   A HA   1 
ATOM   3308 H HB2  . ASN   A 1 150 ? 21.735 -14.810 13.194  1.00 19.25 ?  150 ASN   A HB2  1 
ATOM   3309 H HB3  . ASN   A 1 150 ? 20.149 -14.689 13.152  1.00 19.25 ?  150 ASN   A HB3  1 
ATOM   3310 H HD21 . ASN   A 1 150 ? 21.317 -17.730 14.726  1.00 27.13 ?  150 ASN   A HD21 1 
ATOM   3311 H HD22 . ASN   A 1 150 ? 21.764 -16.319 14.888  1.00 27.13 ?  150 ASN   A HD22 1 
ATOM   3312 N N    . VAL   A 1 151 ? 19.821 -13.352 9.991   1.00 12.20 ?  151 VAL   A N    1 
ATOM   3313 C CA   . VAL   A 1 151 ? 19.613 -12.033 9.411   1.00 12.23 ?  151 VAL   A CA   1 
ATOM   3314 C C    . VAL   A 1 151 ? 18.229 -11.519 9.779   1.00 12.32 ?  151 VAL   A C    1 
ATOM   3315 O O    . VAL   A 1 151 ? 17.221 -12.225 9.621   1.00 13.49 ?  151 VAL   A O    1 
ATOM   3316 C CB   . VAL   A 1 151 ? 19.895 -12.003 7.894   1.00 13.35 ?  151 VAL   A CB   1 
ATOM   3317 C CG1  . VAL   A 1 151 ? 19.063 -13.018 7.143   1.00 14.78 ?  151 VAL   A CG1  1 
ATOM   3318 C CG2  . VAL   A 1 151 ? 19.692 -10.597 7.332   1.00 13.98 ?  151 VAL   A CG2  1 
ATOM   3319 H H    . VAL   A 1 151 ? 19.258 -13.947 9.720   1.00 14.61 ?  151 VAL   A H    1 
ATOM   3320 H HA   . VAL   A 1 151 ? 20.256 -11.430 9.817   1.00 14.66 ?  151 VAL   A HA   1 
ATOM   3321 H HB   . VAL   A 1 151 ? 20.828 -12.233 7.752   1.00 15.99 ?  151 VAL   A HB   1 
ATOM   3322 H HG11 . VAL   A 1 151 ? 19.245 -12.940 6.193   1.00 17.72 ?  151 VAL   A HG11 1 
ATOM   3323 H HG12 . VAL   A 1 151 ? 19.301 -13.911 7.449   1.00 17.72 ?  151 VAL   A HG12 1 
ATOM   3324 H HG13 . VAL   A 1 151 ? 18.124 -12.851 7.315   1.00 17.72 ?  151 VAL   A HG13 1 
ATOM   3325 H HG21 . VAL   A 1 151 ? 20.010 -10.575 6.416   1.00 16.75 ?  151 VAL   A HG21 1 
ATOM   3326 H HG22 . VAL   A 1 151 ? 18.745 -10.381 7.355   1.00 16.75 ?  151 VAL   A HG22 1 
ATOM   3327 H HG23 . VAL   A 1 151 ? 20.189 -9.965  7.871   1.00 16.75 ?  151 VAL   A HG23 1 
ATOM   3328 N N    . TYR   A 1 152 ? 18.213 -10.277 10.279  1.00 12.15 ?  152 TYR   A N    1 
ATOM   3329 C CA   . TYR   A 1 152 ? 17.017 -9.539  10.659  1.00 11.63 ?  152 TYR   A CA   1 
ATOM   3330 C C    . TYR   A 1 152 ? 16.840 -8.431  9.634   1.00 10.97 ?  152 TYR   A C    1 
ATOM   3331 O O    . TYR   A 1 152 ? 17.609 -7.463  9.610   1.00 11.42 ?  152 TYR   A O    1 
ATOM   3332 C CB   . TYR   A 1 152 ? 17.174 -8.999  12.079  1.00 12.02 ?  152 TYR   A CB   1 
ATOM   3333 C CG   . TYR   A 1 152 ? 17.134 -10.129 13.067  1.00 13.10 ?  152 TYR   A CG   1 
ATOM   3334 C CD1  . TYR   A 1 152 ? 18.265 -10.885 13.337  1.00 14.54 ?  152 TYR   A CD1  1 
ATOM   3335 C CD2  . TYR   A 1 152 ? 15.949 -10.483 13.695  1.00 13.16 ?  152 TYR   A CD2  1 
ATOM   3336 C CE1  . TYR   A 1 152 ? 18.229 -11.950 14.211  1.00 15.62 ?  152 TYR   A CE1  1 
ATOM   3337 C CE2  . TYR   A 1 152 ? 15.895 -11.558 14.580  1.00 14.54 ?  152 TYR   A CE2  1 
ATOM   3338 C CZ   . TYR   A 1 152 ? 17.044 -12.281 14.837  1.00 15.51 ?  152 TYR   A CZ   1 
ATOM   3339 O OH   . TYR   A 1 152 ? 17.006 -13.352 15.709  1.00 17.67 ?  152 TYR   A OH   1 
ATOM   3340 H H    . TYR   A 1 152 ? 18.936 -9.812  10.402  1.00 14.56 ?  152 TYR   A H    1 
ATOM   3341 H HA   . TYR   A 1 152 ? 16.249 -10.124 10.626  1.00 13.93 ?  152 TYR   A HA   1 
ATOM   3342 H HB2  . TYR   A 1 152 ? 18.027 -8.554  12.169  1.00 14.40 ?  152 TYR   A HB2  1 
ATOM   3343 H HB3  . TYR   A 1 152 ? 16.447 -8.391  12.281  1.00 14.40 ?  152 TYR   A HB3  1 
ATOM   3344 H HD1  . TYR   A 1 152 ? 19.062 -10.668 12.914  1.00 17.43 ?  152 TYR   A HD1  1 
ATOM   3345 H HD2  . TYR   A 1 152 ? 15.167 -10.000 13.520  1.00 15.77 ?  152 TYR   A HD2  1 
ATOM   3346 H HE1  . TYR   A 1 152 ? 19.000 -12.438 14.384  1.00 18.72 ?  152 TYR   A HE1  1 
ATOM   3347 H HE2  . TYR   A 1 152 ? 15.095 -11.780 15.001  1.00 17.43 ?  152 TYR   A HE2  1 
ATOM   3348 H HH   . TYR   A 1 152 ? 16.227 -13.438 16.020  1.00 21.18 ?  152 TYR   A HH   1 
ATOM   3349 N N    . LEU   A 1 153 ? 15.850 -8.601  8.763   1.00 11.09 ?  153 LEU   A N    1 
ATOM   3350 C CA   . LEU   A 1 153 ? 15.594 -7.676  7.669   1.00 11.06 ?  153 LEU   A CA   1 
ATOM   3351 C C    . LEU   A 1 153 ? 14.597 -6.611  8.095   1.00 11.65 ?  153 LEU   A C    1 
ATOM   3352 O O    . LEU   A 1 153 ? 13.479 -6.930  8.523   1.00 12.29 ?  153 LEU   A O    1 
ATOM   3353 C CB   . LEU   A 1 153 ? 15.029 -8.415  6.456   1.00 11.46 ?  153 LEU   A CB   1 
ATOM   3354 C CG   . LEU   A 1 153 ? 15.940 -9.434  5.772   1.00 11.75 ?  153 LEU   A CG   1 
ATOM   3355 C CD1  . LEU   A 1 153 ? 15.145 -10.288 4.788   1.00 12.26 ?  153 LEU   A CD1  1 
ATOM   3356 C CD2  . LEU   A 1 153 ? 17.092 -8.746  5.062   1.00 12.19 ?  153 LEU   A CD2  1 
ATOM   3357 H H    . LEU   A 1 153 ? 15.292 -9.258  8.798   1.00 13.29 ?  153 LEU   A H    1 
ATOM   3358 H HA   . LEU   A 1 153 ? 16.421 -7.249  7.419   1.00 13.25 ?  153 LEU   A HA   1 
ATOM   3359 H HB2  . LEU   A 1 153 ? 14.233 -8.886  6.739   1.00 13.73 ?  153 LEU   A HB2  1 
ATOM   3360 H HB3  . LEU   A 1 153 ? 14.793 -7.751  5.790   1.00 13.73 ?  153 LEU   A HB3  1 
ATOM   3361 H HG   . LEU   A 1 153 ? 16.314 -10.021 6.450   1.00 14.07 ?  153 LEU   A HG   1 
ATOM   3362 H HD11 . LEU   A 1 153 ? 15.693 -11.032 4.501   1.00 14.69 ?  153 LEU   A HD11 1 
ATOM   3363 H HD12 . LEU   A 1 153 ? 14.347 -10.618 5.233   1.00 14.69 ?  153 LEU   A HD12 1 
ATOM   3364 H HD13 . LEU   A 1 153 ? 14.895 -9.741  4.028   1.00 14.69 ?  153 LEU   A HD13 1 
ATOM   3365 H HD21 . LEU   A 1 153 ? 17.645 -9.426  4.646   1.00 14.60 ?  153 LEU   A HD21 1 
ATOM   3366 H HD22 . LEU   A 1 153 ? 16.732 -8.152  4.391   1.00 14.60 ?  153 LEU   A HD22 1 
ATOM   3367 H HD23 . LEU   A 1 153 ? 17.609 -8.249  5.712   1.00 14.60 ?  153 LEU   A HD23 1 
ATOM   3368 N N    A ALA   A 1 154 ? 14.932 -5.351  7.814   0.48 11.48 ?  154 ALA   A N    1 
ATOM   3369 N N    B ALA   A 1 154 ? 15.062 -5.365  8.113   0.52 10.96 ?  154 ALA   A N    1 
ATOM   3370 C CA   A ALA   A 1 154 ? 14.029 -4.219  8.001   0.48 11.21 ?  154 ALA   A CA   1 
ATOM   3371 C CA   B ALA   A 1 154 ? 14.237 -4.208  8.421   0.52 10.51 ?  154 ALA   A CA   1 
ATOM   3372 C C    A ALA   A 1 154 ? 13.544 -3.732  6.638   0.48 11.00 ?  154 ALA   A C    1 
ATOM   3373 C C    B ALA   A 1 154 ? 13.823 -3.584  7.098   0.52 10.42 ?  154 ALA   A C    1 
ATOM   3374 O O    A ALA   A 1 154 ? 14.354 -3.343  5.786   0.48 11.81 ?  154 ALA   A O    1 
ATOM   3375 O O    B ALA   A 1 154 ? 14.682 -3.164  6.315   0.52 10.28 ?  154 ALA   A O    1 
ATOM   3376 C CB   A ALA   A 1 154 ? 14.733 -3.080  8.738   0.48 11.43 ?  154 ALA   A CB   1 
ATOM   3377 C CB   B ALA   A 1 154 ? 15.017 -3.194  9.258   0.52 10.49 ?  154 ALA   A CB   1 
ATOM   3378 H H    A ALA   A 1 154 ? 15.697 -5.122  7.497   0.48 13.75 ?  154 ALA   A H    1 
ATOM   3379 H H    B ALA   A 1 154 ? 15.887 -5.159  7.950   0.52 13.12 ?  154 ALA   A H    1 
ATOM   3380 H HA   A ALA   A 1 154 ? 13.261 -4.497  8.527   0.48 13.43 ?  154 ALA   A HA   1 
ATOM   3381 H HA   B ALA   A 1 154 ? 13.449 -4.477  8.914   0.52 12.59 ?  154 ALA   A HA   1 
ATOM   3382 H HB1  A ALA   A 1 154 ? 14.111 -2.342  8.847   0.48 13.69 ?  154 ALA   A HB1  1 
ATOM   3383 H HB1  B ALA   A 1 154 ? 14.448 -2.431  9.449   0.52 12.56 ?  154 ALA   A HB1  1 
ATOM   3384 H HB2  A ALA   A 1 154 ? 15.027 -3.396  9.605   0.48 13.69 ?  154 ALA   A HB2  1 
ATOM   3385 H HB2  B ALA   A 1 154 ? 15.299 -3.610  10.089  0.52 12.56 ?  154 ALA   A HB2  1 
ATOM   3386 H HB3  A ALA   A 1 154 ? 15.497 -2.790  8.213   0.48 13.69 ?  154 ALA   A HB3  1 
ATOM   3387 H HB3  B ALA   A 1 154 ? 15.799 -2.901  8.758   0.52 12.56 ?  154 ALA   A HB3  1 
ATOM   3388 N N    A VAL   A 1 155 ? 12.226 -3.748  6.441   0.48 10.72 ?  155 VAL   A N    1 
ATOM   3389 N N    B VAL   A 1 155 ? 12.519 -3.536  6.849   0.52 10.70 ?  155 VAL   A N    1 
ATOM   3390 C CA   A VAL   A 1 155 ? 11.582 -3.260  5.223   0.48 11.38 ?  155 VAL   A CA   1 
ATOM   3391 C CA   B VAL   A 1 155 ? 11.965 -3.010  5.608   0.52 11.19 ?  155 VAL   A CA   1 
ATOM   3392 C C    A VAL   A 1 155 ? 10.871 -1.960  5.566   0.48 12.05 ?  155 VAL   A C    1 
ATOM   3393 C C    B VAL   A 1 155 ? 11.167 -1.755  5.946   0.52 11.19 ?  155 VAL   A C    1 
ATOM   3394 O O    A VAL   A 1 155 ? 9.911  -1.963  6.344   0.48 11.99 ?  155 VAL   A O    1 
ATOM   3395 O O    B VAL   A 1 155 ? 10.136 -1.818  6.625   0.52 11.43 ?  155 VAL   A O    1 
ATOM   3396 C CB   A VAL   A 1 155 ? 10.588 -4.289  4.663   0.48 11.73 ?  155 VAL   A CB   1 
ATOM   3397 C CB   B VAL   A 1 155 ? 11.113 -4.053  4.874   0.52 11.11 ?  155 VAL   A CB   1 
ATOM   3398 C CG1  A VAL   A 1 155 ? 9.879  -3.733  3.437   0.48 12.06 ?  155 VAL   A CG1  1 
ATOM   3399 C CG1  B VAL   A 1 155 ? 10.455 -3.435  3.654   0.52 11.35 ?  155 VAL   A CG1  1 
ATOM   3400 C CG2  A VAL   A 1 155 ? 11.300 -5.591  4.328   0.48 11.96 ?  155 VAL   A CG2  1 
ATOM   3401 C CG2  B VAL   A 1 155 ? 11.977 -5.254  4.476   0.52 11.28 ?  155 VAL   A CG2  1 
ATOM   3402 H H    A VAL   A 1 155 ? 11.658 -4.047  7.025   0.48 12.83 ?  155 VAL   A H    1 
ATOM   3403 H H    B VAL   A 1 155 ? 11.924 -3.812  7.406   0.52 12.81 ?  155 VAL   A H    1 
ATOM   3404 H HA   A VAL   A 1 155 ? 12.250 -3.080  4.550   0.48 13.63 ?  155 VAL   A HA   1 
ATOM   3405 H HA   B VAL   A 1 155 ? 12.695 -2.752  5.026   0.52 13.40 ?  155 VAL   A HA   1 
ATOM   3406 H HB   A VAL   A 1 155 ? 9.914  -4.484  5.337   0.48 14.06 ?  155 VAL   A HB   1 
ATOM   3407 H HB   B VAL   A 1 155 ? 10.414 -4.363  5.474   0.52 13.31 ?  155 VAL   A HB   1 
ATOM   3408 H HG11 A VAL   A 1 155 ? 9.395  -4.450  3.001   0.48 14.45 ?  155 VAL   A HG11 1 
ATOM   3409 H HG11 B VAL   A 1 155 ? 10.094 -4.144  3.105   0.52 13.60 ?  155 VAL   A HG11 1 
ATOM   3410 H HG12 A VAL   A 1 155 ? 9.259  -3.040  3.715   0.48 14.45 ?  155 VAL   A HG12 1 
ATOM   3411 H HG12 B VAL   A 1 155 ? 9.744  -2.841  3.942   0.52 13.60 ?  155 VAL   A HG12 1 
ATOM   3412 H HG13 A VAL   A 1 155 ? 10.541 -3.365  2.832   0.48 14.45 ?  155 VAL   A HG13 1 
ATOM   3413 H HG13 B VAL   A 1 155 ? 11.123 -2.937  3.158   0.52 13.60 ?  155 VAL   A HG13 1 
ATOM   3414 H HG21 A VAL   A 1 155 ? 10.681 -6.182  3.873   0.48 14.33 ?  155 VAL   A HG21 1 
ATOM   3415 H HG21 B VAL   A 1 155 ? 11.426 -5.892  3.998   0.52 13.51 ?  155 VAL   A HG21 1 
ATOM   3416 H HG22 A VAL   A 1 155 ? 12.056 -5.395  3.751   0.48 14.33 ?  155 VAL   A HG22 1 
ATOM   3417 H HG22 B VAL   A 1 155 ? 12.701 -4.947  3.907   0.52 13.51 ?  155 VAL   A HG22 1 
ATOM   3418 H HG23 A VAL   A 1 155 ? 11.611 -6.003  5.150   0.48 14.33 ?  155 VAL   A HG23 1 
ATOM   3419 H HG23 B VAL   A 1 155 ? 12.340 -5.665  5.278   0.52 13.51 ?  155 VAL   A HG23 1 
ATOM   3420 N N    A PHE   A 1 156 ? 11.311 -0.852  4.963   0.48 13.44 ?  156 PHE   A N    1 
ATOM   3421 N N    B PHE   A 1 156 ? 11.647 -0.615  5.447   0.52 10.97 ?  156 PHE   A N    1 
ATOM   3422 C CA   A PHE   A 1 156 ? 10.799 0.458   5.368   0.48 15.00 ?  156 PHE   A CA   1 
ATOM   3423 C CA   B PHE   A 1 156 ? 11.108 0.700   5.792   0.52 12.00 ?  156 PHE   A CA   1 
ATOM   3424 C C    A PHE   A 1 156 ? 9.350  0.663   4.933   0.48 14.88 ?  156 PHE   A C    1 
ATOM   3425 C C    B PHE   A 1 156 ? 9.695  0.889   5.244   0.52 11.73 ?  156 PHE   A C    1 
ATOM   3426 O O    A PHE   A 1 156 ? 8.541  1.201   5.696   0.48 14.78 ?  156 PHE   A O    1 
ATOM   3427 O O    B PHE   A 1 156 ? 8.798  1.362   5.950   0.52 12.95 ?  156 PHE   A O    1 
ATOM   3428 C CB   A PHE   A 1 156 ? 11.696 1.574   4.823   0.48 16.83 ?  156 PHE   A CB   1 
ATOM   3429 C CB   B PHE   A 1 156 ? 12.084 1.722   5.197   0.52 13.42 ?  156 PHE   A CB   1 
ATOM   3430 C CG   A PHE   A 1 156 ? 11.205 2.967   5.152   0.48 18.42 ?  156 PHE   A CG   1 
ATOM   3431 C CG   B PHE   A 1 156 ? 11.649 3.165   5.250   0.52 14.53 ?  156 PHE   A CG   1 
ATOM   3432 C CD1  A PHE   A 1 156 ? 11.200 3.420   6.463   0.48 19.11 ?  156 PHE   A CD1  1 
ATOM   3433 C CD1  B PHE   A 1 156 ? 11.726 3.885   6.429   0.52 15.76 ?  156 PHE   A CD1  1 
ATOM   3434 C CD2  A PHE   A 1 156 ? 10.742 3.816   4.154   0.48 19.41 ?  156 PHE   A CD2  1 
ATOM   3435 C CD2  B PHE   A 1 156 ? 11.280 3.832   4.087   0.52 15.58 ?  156 PHE   A CD2  1 
ATOM   3436 C CE1  A PHE   A 1 156 ? 10.748 4.695   6.774   0.48 19.70 ?  156 PHE   A CE1  1 
ATOM   3437 C CE1  B PHE   A 1 156 ? 11.373 5.219   6.465   0.52 16.29 ?  156 PHE   A CE1  1 
ATOM   3438 C CE2  A PHE   A 1 156 ? 10.290 5.093   4.458   0.48 20.04 ?  156 PHE   A CE2  1 
ATOM   3439 C CE2  B PHE   A 1 156 ? 10.924 5.170   4.117   0.52 15.73 ?  156 PHE   A CE2  1 
ATOM   3440 C CZ   A PHE   A 1 156 ? 10.296 5.533   5.770   0.48 20.09 ?  156 PHE   A CZ   1 
ATOM   3441 C CZ   B PHE   A 1 156 ? 10.976 5.861   5.308   0.52 15.64 ?  156 PHE   A CZ   1 
ATOM   3442 H H    A PHE   A 1 156 ? 11.890 -0.839  4.330   0.48 16.11 ?  156 PHE   A H    1 
ATOM   3443 H H    B PHE   A 1 156 ? 12.301 -0.579  4.888   0.52 13.14 ?  156 PHE   A H    1 
ATOM   3444 H HA   A PHE   A 1 156 ? 10.827 0.507   6.335   0.48 17.98 ?  156 PHE   A HA   1 
ATOM   3445 H HA   B PHE   A 1 156 ? 11.107 0.814   6.763   0.52 14.38 ?  156 PHE   A HA   1 
ATOM   3446 H HB2  A PHE   A 1 156 ? 12.584 1.474   5.205   0.48 20.17 ?  156 PHE   A HB2  1 
ATOM   3447 H HB2  B PHE   A 1 156 ? 12.910 1.663   5.698   0.52 16.08 ?  156 PHE   A HB2  1 
ATOM   3448 H HB3  A PHE   A 1 156 ? 11.743 1.494   3.859   0.48 20.17 ?  156 PHE   A HB3  1 
ATOM   3449 H HB3  B PHE   A 1 156 ? 12.246 1.500   4.269   0.52 16.08 ?  156 PHE   A HB3  1 
ATOM   3450 H HD1  A PHE   A 1 156 ? 11.504 2.862   7.143   0.48 22.91 ?  156 PHE   A HD1  1 
ATOM   3451 H HD1  B PHE   A 1 156 ? 11.993 3.457   7.212   0.52 18.88 ?  156 PHE   A HD1  1 
ATOM   3452 H HD2  A PHE   A 1 156 ? 10.739 3.525   3.271   0.48 23.26 ?  156 PHE   A HD2  1 
ATOM   3453 H HD2  B PHE   A 1 156 ? 11.245 3.360   3.285   0.52 18.68 ?  156 PHE   A HD2  1 
ATOM   3454 H HE1  A PHE   A 1 156 ? 10.752 4.988   7.658   0.48 23.61 ?  156 PHE   A HE1  1 
ATOM   3455 H HE1  B PHE   A 1 156 ? 11.405 5.688   7.266   0.52 19.53 ?  156 PHE   A HE1  1 
ATOM   3456 H HE2  A PHE   A 1 156 ? 9.986  5.653   3.781   0.48 24.02 ?  156 PHE   A HE2  1 
ATOM   3457 H HE2  B PHE   A 1 156 ? 10.654 5.597   3.335   0.52 18.85 ?  156 PHE   A HE2  1 
ATOM   3458 H HZ   A PHE   A 1 156 ? 9.991  6.389   5.979   0.48 24.09 ?  156 PHE   A HZ   1 
ATOM   3459 H HZ   B PHE   A 1 156 ? 10.733 6.758   5.332   0.52 18.74 ?  156 PHE   A HZ   1 
ATOM   3460 N N    A ASP   A 1 157 ? 9.003  0.256   3.718   0.48 15.50 ?  157 ASP   A N    1 
ATOM   3461 N N    B ASP   A 1 157 ? 9.482  0.533   3.984   0.52 10.66 ?  157 ASP   A N    1 
ATOM   3462 C CA   A ASP   A 1 157 ? 7.683  0.539   3.164   0.48 16.68 ?  157 ASP   A CA   1 
ATOM   3463 C CA   B ASP   A 1 157 ? 8.242  0.842   3.281   0.52 10.79 ?  157 ASP   A CA   1 
ATOM   3464 C C    A ASP   A 1 157 ? 6.684  -0.501  3.656   0.48 17.18 ?  157 ASP   A C    1 
ATOM   3465 C C    B ASP   A 1 157 ? 7.158  -0.162  3.673   0.52 11.23 ?  157 ASP   A C    1 
ATOM   3466 O O    A ASP   A 1 157 ? 6.803  -1.686  3.323   0.48 17.01 ?  157 ASP   A O    1 
ATOM   3467 O O    B ASP   A 1 157 ? 7.328  -1.374  3.484   0.52 11.97 ?  157 ASP   A O    1 
ATOM   3468 C CB   A ASP   A 1 157 ? 7.761  0.511   1.642   0.48 18.02 ?  157 ASP   A CB   1 
ATOM   3469 C CB   B ASP   A 1 157 ? 8.522  0.815   1.780   0.52 11.14 ?  157 ASP   A CB   1 
ATOM   3470 C CG   A ASP   A 1 157 ? 6.525  1.071   0.979   0.48 19.43 ?  157 ASP   A CG   1 
ATOM   3471 C CG   B ASP   A 1 157 ? 7.338  1.254   0.940   0.52 11.77 ?  157 ASP   A CG   1 
ATOM   3472 O OD1  A ASP   A 1 157 ? 6.465  2.302   0.800   0.48 20.84 ?  157 ASP   A OD1  1 
ATOM   3473 O OD1  B ASP   A 1 157 ? 6.354  0.495   0.862   0.52 12.73 ?  157 ASP   A OD1  1 
ATOM   3474 O OD2  A ASP   A 1 157 ? 5.614  0.284   0.634   0.48 19.62 -1 157 ASP   A OD2  1 
ATOM   3475 O OD2  B ASP   A 1 157 ? 7.402  2.347   0.335   0.52 12.59 -1 157 ASP   A OD2  1 
ATOM   3476 H H    A ASP   A 1 157 ? 9.513  -0.190  3.197   0.48 18.58 ?  157 ASP   A H    1 
ATOM   3477 H H    B ASP   A 1 157 ? 10.054 0.101   3.522   0.52 12.77 ?  157 ASP   A H    1 
ATOM   3478 H HA   A ASP   A 1 157 ? 7.387  1.418   3.455   0.48 19.99 ?  157 ASP   A HA   1 
ATOM   3479 H HA   B ASP   A 1 157 ? 7.948  1.735   3.535   0.52 12.92 ?  157 ASP   A HA   1 
ATOM   3480 H HB2  A ASP   A 1 157 ? 8.521  1.036   1.364   0.48 21.60 ?  157 ASP   A HB2  1 
ATOM   3481 H HB2  B ASP   A 1 157 ? 9.266  1.405   1.596   0.52 13.35 ?  157 ASP   A HB2  1 
ATOM   3482 H HB3  A ASP   A 1 157 ? 7.862  -0.402  1.353   0.48 21.60 ?  157 ASP   A HB3  1 
ATOM   3483 H HB3  B ASP   A 1 157 ? 8.752  -0.094  1.531   0.52 13.35 ?  157 ASP   A HB3  1 
ATOM   3484 N N    A LYS   A 1 158 ? 5.691  -0.057  4.435   0.48 18.51 ?  158 LYS   A N    1 
ATOM   3485 N N    B LYS   A 1 158 ? 6.043  0.350   4.213   0.52 11.22 ?  158 LYS   A N    1 
ATOM   3486 C CA   A LYS   A 1 158 ? 4.720  -0.993  4.998   0.48 19.95 ?  158 LYS   A CA   1 
ATOM   3487 C CA   B LYS   A 1 158 ? 4.993  -0.518  4.746   0.52 11.92 ?  158 LYS   A CA   1 
ATOM   3488 C C    A LYS   A 1 158 ? 3.950  -1.714  3.899   0.48 19.78 ?  158 LYS   A C    1 
ATOM   3489 C C    B LYS   A 1 158 ? 4.336  -1.337  3.643   0.52 11.66 ?  158 LYS   A C    1 
ATOM   3490 O O    A LYS   A 1 158 ? 3.715  -2.925  3.986   0.48 19.92 ?  158 LYS   A O    1 
ATOM   3491 O O    B LYS   A 1 158 ? 4.117  -2.544  3.798   0.52 12.25 ?  158 LYS   A O    1 
ATOM   3492 C CB   A LYS   A 1 158 ? 3.770  -0.265  5.955   0.48 21.87 ?  158 LYS   A CB   1 
ATOM   3493 C CB   B LYS   A 1 158 ? 3.935  0.302   5.491   0.52 13.53 ?  158 LYS   A CB   1 
ATOM   3494 C CG   A LYS   A 1 158 ? 2.522  -1.060  6.361   0.48 23.76 ?  158 LYS   A CG   1 
ATOM   3495 C CG   B LYS   A 1 158 ? 2.696  -0.514  5.863   0.52 15.50 ?  158 LYS   A CG   1 
ATOM   3496 C CD   A LYS   A 1 158 ? 2.857  -2.328  7.149   0.48 25.25 ?  158 LYS   A CD   1 
ATOM   3497 C CD   B LYS   A 1 158 ? 1.612  0.332   6.496   0.52 17.57 ?  158 LYS   A CD   1 
ATOM   3498 C CE   A LYS   A 1 158 ? 1.590  -3.019  7.654   0.48 26.13 ?  158 LYS   A CE   1 
ATOM   3499 C CE   B LYS   A 1 158 ? 0.453  -0.529  6.983   0.52 18.47 ?  158 LYS   A CE   1 
ATOM   3500 N NZ   A LYS   A 1 158 ? 1.865  -4.331  8.313   0.48 26.47 ?  158 LYS   A NZ   1 
ATOM   3501 N NZ   B LYS   A 1 158 ? -0.188 -1.317  5.894   0.52 19.09 ?  158 LYS   A NZ   1 
ATOM   3502 H H    A LYS   A 1 158 ? 5.555  0.767   4.647   0.48 22.19 ?  158 LYS   A H    1 
ATOM   3503 H H    B LYS   A 1 158 ? 5.871  1.194   4.274   0.52 13.45 ?  158 LYS   A H    1 
ATOM   3504 H HA   A LYS   A 1 158 ? 5.190  -1.662  5.516   0.48 23.91 ?  158 LYS   A HA   1 
ATOM   3505 H HA   B LYS   A 1 158 ? 5.390  -1.132  5.385   0.52 14.28 ?  158 LYS   A HA   1 
ATOM   3506 H HB2  A LYS   A 1 158 ? 4.252  -0.050  6.773   0.48 26.23 ?  158 LYS   A HB2  1 
ATOM   3507 H HB2  B LYS   A 1 158 ? 4.323  0.648   6.315   0.52 16.21 ?  158 LYS   A HB2  1 
ATOM   3508 H HB3  A LYS   A 1 158 ? 3.467  0.555   5.536   0.48 26.23 ?  158 LYS   A HB3  1 
ATOM   3509 H HB3  B LYS   A 1 158 ? 3.653  1.040   4.929   0.52 16.21 ?  158 LYS   A HB3  1 
ATOM   3510 H HG2  A LYS   A 1 158 ? 1.967  -0.503  6.927   0.48 28.48 ?  158 LYS   A HG2  1 
ATOM   3511 H HG2  B LYS   A 1 158 ? 2.318  -0.913  5.065   0.52 18.57 ?  158 LYS   A HG2  1 
ATOM   3512 H HG3  A LYS   A 1 158 ? 2.021  -1.317  5.570   0.48 28.48 ?  158 LYS   A HG3  1 
ATOM   3513 H HG3  B LYS   A 1 158 ? 2.955  -1.205  6.491   0.52 18.57 ?  158 LYS   A HG3  1 
ATOM   3514 H HD2  A LYS   A 1 158 ? 3.334  -2.948  6.576   0.48 30.28 ?  158 LYS   A HD2  1 
ATOM   3515 H HD2  B LYS   A 1 158 ? 1.982  0.810   7.254   0.52 21.06 ?  158 LYS   A HD2  1 
ATOM   3516 H HD3  A LYS   A 1 158 ? 3.399  -2.094  7.918   0.48 30.28 ?  158 LYS   A HD3  1 
ATOM   3517 H HD3  B LYS   A 1 158 ? 1.273  0.960   5.836   0.52 21.06 ?  158 LYS   A HD3  1 
ATOM   3518 H HE2  A LYS   A 1 158 ? 1.153  -2.446  8.304   0.48 31.33 ?  158 LYS   A HE2  1 
ATOM   3519 H HE2  B LYS   A 1 158 ? 0.785  -1.153  7.645   0.52 22.14 ?  158 LYS   A HE2  1 
ATOM   3520 H HE3  A LYS   A 1 158 ? 0.995  -3.180  6.905   0.48 31.33 ?  158 LYS   A HE3  1 
ATOM   3521 H HE3  B LYS   A 1 158 ? -0.221 0.046   7.375   0.52 22.14 ?  158 LYS   A HE3  1 
ATOM   3522 H HZ1  A LYS   A 1 158 ? 1.103  -4.700  8.592   0.48 31.74 ?  158 LYS   A HZ1  1 
ATOM   3523 H HZ1  B LYS   A 1 158 ? -0.865 -1.792  6.222   0.52 22.88 ?  158 LYS   A HZ1  1 
ATOM   3524 H HZ2  A LYS   A 1 158 ? 2.259  -4.885  7.738   0.48 31.74 ?  158 LYS   A HZ2  1 
ATOM   3525 H HZ2  B LYS   A 1 158 ? -0.498 -0.768  5.265   0.52 22.88 ?  158 LYS   A HZ2  1 
ATOM   3526 H HZ3  A LYS   A 1 158 ? 2.401  -4.214  9.014   0.48 31.74 ?  158 LYS   A HZ3  1 
ATOM   3527 H HZ3  B LYS   A 1 158 ? 0.405  -1.870  5.529   0.52 22.88 ?  158 LYS   A HZ3  1 
ATOM   3528 N N    A ASN   A 1 159 ? 3.538  -0.989  2.859   0.48 19.63 ?  159 ASN   A N    1 
ATOM   3529 N N    B ASN   A 1 159 ? 3.976  -0.693  2.531   0.52 12.01 ?  159 ASN   A N    1 
ATOM   3530 C CA   A ASN   A 1 159 ? 2.843  -1.638  1.753   0.48 18.84 ?  159 ASN   A CA   1 
ATOM   3531 C CA   B ASN   A 1 159 ? 3.348  -1.437  1.445   0.52 12.72 ?  159 ASN   A CA   1 
ATOM   3532 C C    A ASN   A 1 159 ? 3.729  -2.684  1.087   0.48 18.07 ?  159 ASN   A C    1 
ATOM   3533 C C    B ASN   A 1 159 ? 4.282  -2.516  0.910   0.52 13.43 ?  159 ASN   A C    1 
ATOM   3534 O O    A ASN   A 1 159 ? 3.254  -3.763  0.713   0.48 17.68 ?  159 ASN   A O    1 
ATOM   3535 O O    B ASN   A 1 159 ? 3.833  -3.614  0.557   0.52 13.95 ?  159 ASN   A O    1 
ATOM   3536 C CB   A ASN   A 1 159 ? 2.361  -0.595  0.745   0.48 19.17 ?  159 ASN   A CB   1 
ATOM   3537 C CB   B ASN   A 1 159 ? 2.911  -0.488  0.330   0.52 13.82 ?  159 ASN   A CB   1 
ATOM   3538 C CG   A ASN   A 1 159 ? 1.122  0.138   1.215   0.48 19.68 ?  159 ASN   A CG   1 
ATOM   3539 C CG   B ASN   A 1 159 ? 1.704  0.346   0.715   0.52 15.18 ?  159 ASN   A CG   1 
ATOM   3540 O OD1  A ASN   A 1 159 ? 0.288  -0.426  1.921   0.48 20.30 ?  159 ASN   A OD1  1 
ATOM   3541 O OD1  B ASN   A 1 159 ? 0.879  -0.070  1.529   0.52 16.66 ?  159 ASN   A OD1  1 
ATOM   3542 N ND2  A ASN   A 1 159 ? 0.995  1.399   0.824   0.48 19.44 ?  159 ASN   A ND2  1 
ATOM   3543 N ND2  B ASN   A 1 159 ? 1.595  1.536   0.134   0.52 15.73 ?  159 ASN   A ND2  1 
ATOM   3544 H H    A ASN   A 1 159 ? 3.641  -0.140  2.781   0.48 23.53 ?  159 ASN   A H    1 
ATOM   3545 H H    B ASN   A 1 159 ? 4.077  0.149   2.394   0.52 14.39 ?  159 ASN   A H    1 
ATOM   3546 H HA   A ASN   A 1 159 ? 2.061  -2.094  2.102   0.48 22.59 ?  159 ASN   A HA   1 
ATOM   3547 H HA   B ASN   A 1 159 ? 2.556  -1.878  1.786   0.52 15.24 ?  159 ASN   A HA   1 
ATOM   3548 H HB2  A ASN   A 1 159 ? 3.060  0.060   0.608   0.48 22.98 ?  159 ASN   A HB2  1 
ATOM   3549 H HB2  B ASN   A 1 159 ? 3.642  0.117   0.125   0.52 16.56 ?  159 ASN   A HB2  1 
ATOM   3550 H HB3  A ASN   A 1 159 ? 2.147  -1.039  -0.088  0.48 22.98 ?  159 ASN   A HB3  1 
ATOM   3551 H HB3  B ASN   A 1 159 ? 2.680  -1.009  -0.454  0.52 16.56 ?  159 ASN   A HB3  1 
ATOM   3552 H HD21 A ASN   A 1 159 ? 0.307  1.856   1.067   0.48 23.30 ?  159 ASN   A HD21 1 
ATOM   3553 H HD21 B ASN   A 1 159 ? 0.929  2.044   0.319   0.52 18.85 ?  159 ASN   A HD21 1 
ATOM   3554 H HD22 A ASN   A 1 159 ? 1.598  1.757   0.330   0.48 23.30 ?  159 ASN   A HD22 1 
ATOM   3555 H HD22 B ASN   A 1 159 ? 2.191  1.793   -0.431  0.52 18.85 ?  159 ASN   A HD22 1 
ATOM   3556 N N    A LEU   A 1 160 ? 5.024  -2.396  0.946   0.48 17.69 ?  160 LEU   A N    1 
ATOM   3557 N N    B LEU   A 1 160 ? 5.584  -2.220  0.841   0.52 12.67 ?  160 LEU   A N    1 
ATOM   3558 C CA   A LEU   A 1 160 ? 5.926  -3.404  0.404   0.48 17.28 ?  160 LEU   A CA   1 
ATOM   3559 C CA   B LEU   A 1 160 ? 6.555  -3.218  0.401   0.52 12.84 ?  160 LEU   A CA   1 
ATOM   3560 C C    A LEU   A 1 160 ? 6.085  -4.572  1.370   0.48 16.91 ?  160 LEU   A C    1 
ATOM   3561 C C    B LEU   A 1 160 ? 6.614  -4.387  1.376   0.52 12.88 ?  160 LEU   A C    1 
ATOM   3562 O O    A LEU   A 1 160 ? 6.114  -5.733  0.946   0.48 16.83 ?  160 LEU   A O    1 
ATOM   3563 O O    B LEU   A 1 160 ? 6.613  -5.552  0.966   0.52 13.28 ?  160 LEU   A O    1 
ATOM   3564 C CB   A LEU   A 1 160 ? 7.284  -2.787  0.072   0.48 17.13 ?  160 LEU   A CB   1 
ATOM   3565 C CB   B LEU   A 1 160 ? 7.935  -2.576  0.236   0.52 13.06 ?  160 LEU   A CB   1 
ATOM   3566 C CG   A LEU   A 1 160 ? 8.346  -3.803  -0.353  0.48 17.62 ?  160 LEU   A CG   1 
ATOM   3567 C CG   B LEU   A 1 160 ? 9.069  -3.541  -0.130  0.52 14.27 ?  160 LEU   A CG   1 
ATOM   3568 C CD1  A LEU   A 1 160 ? 7.876  -4.604  -1.551  0.48 17.94 ?  160 LEU   A CD1  1 
ATOM   3569 C CD1  B LEU   A 1 160 ? 8.743  -4.282  -1.423  0.52 14.86 ?  160 LEU   A CD1  1 
ATOM   3570 C CD2  A LEU   A 1 160 ? 9.662  -3.115  -0.653  0.48 17.86 ?  160 LEU   A CD2  1 
ATOM   3571 C CD2  B LEU   A 1 160 ? 10.398 -2.807  -0.235  0.52 14.64 ?  160 LEU   A CD2  1 
ATOM   3572 H H    A LEU   A 1 160 ? 5.393  -1.646  1.163   0.48 21.21 ?  160 LEU   A H    1 
ATOM   3573 H H    B LEU   A 1 160 ? 5.926  -1.452  1.040   0.52 15.18 ?  160 LEU   A H    1 
ATOM   3574 H HA   A LEU   A 1 160 ? 5.545  -3.746  -0.414  0.48 20.71 ?  160 LEU   A HA   1 
ATOM   3575 H HA   B LEU   A 1 160 ? 6.279  -3.559  -0.463  0.52 15.38 ?  160 LEU   A HA   1 
ATOM   3576 H HB2  A LEU   A 1 160 ? 7.176  -2.137  -0.646  0.48 20.53 ?  160 LEU   A HB2  1 
ATOM   3577 H HB2  B LEU   A 1 160 ? 7.884  -1.905  -0.464  0.52 15.65 ?  160 LEU   A HB2  1 
ATOM   3578 H HB3  A LEU   A 1 160 ? 7.617  -2.348  0.867   0.48 20.53 ?  160 LEU   A HB3  1 
ATOM   3579 H HB3  B LEU   A 1 160 ? 8.175  -2.153  1.074   0.52 15.65 ?  160 LEU   A HB3  1 
ATOM   3580 H HG   A LEU   A 1 160 ? 8.503  -4.419  0.381   0.48 21.12 ?  160 LEU   A HG   1 
ATOM   3581 H HG   B LEU   A 1 160 ? 9.155  -4.201  0.575   0.52 17.10 ?  160 LEU   A HG   1 
ATOM   3582 H HD11 A LEU   A 1 160 ? 8.608  -5.158  -1.861  0.48 21.50 ?  160 LEU   A HD11 1 
ATOM   3583 H HD11 B LEU   A 1 160 ? 9.521  -4.788  -1.698  0.52 17.80 ?  160 LEU   A HD11 1 
ATOM   3584 H HD12 A LEU   A 1 160 ? 7.129  -5.164  -1.286  0.48 21.50 ?  160 LEU   A HD12 1 
ATOM   3585 H HD12 B LEU   A 1 160 ? 7.996  -4.881  -1.266  0.52 17.80 ?  160 LEU   A HD12 1 
ATOM   3586 H HD13 A LEU   A 1 160 ? 7.602  -3.993  -2.251  0.48 21.50 ?  160 LEU   A HD13 1 
ATOM   3587 H HD13 B LEU   A 1 160 ? 8.510  -3.634  -2.107  0.52 17.80 ?  160 LEU   A HD13 1 
ATOM   3588 H HD21 A LEU   A 1 160 ? 10.314 -3.785  -0.911  0.48 21.41 ?  160 LEU   A HD21 1 
ATOM   3589 H HD21 B LEU   A 1 160 ? 11.103 -3.454  -0.390  0.52 17.55 ?  160 LEU   A HD21 1 
ATOM   3590 H HD22 A LEU   A 1 160 ? 9.530  -2.483  -1.375  0.48 21.41 ?  160 LEU   A HD22 1 
ATOM   3591 H HD22 B LEU   A 1 160 ? 10.354 -2.179  -0.972  0.52 17.55 ?  160 LEU   A HD22 1 
ATOM   3592 H HD23 A LEU   A 1 160 ? 9.965  -2.650  0.144   0.48 21.41 ?  160 LEU   A HD23 1 
ATOM   3593 H HD23 B LEU   A 1 160 ? 10.560 -2.333  0.596   0.52 17.55 ?  160 LEU   A HD23 1 
ATOM   3594 N N    A TYR   A 1 161 ? 6.189  -4.282  2.669   0.48 16.77 ?  161 TYR   A N    1 
ATOM   3595 N N    B TYR   A 1 161 ? 6.660  -4.093  2.677   0.52 12.46 ?  161 TYR   A N    1 
ATOM   3596 C CA   A TYR   A 1 161 ? 6.344  -5.342  3.661   0.48 16.83 ?  161 TYR   A CA   1 
ATOM   3597 C CA   B TYR   A 1 161 ? 6.672  -5.160  3.670   0.52 12.72 ?  161 TYR   A CA   1 
ATOM   3598 C C    A TYR   A 1 161 ? 5.191  -6.334  3.589   0.48 17.82 ?  161 TYR   A C    1 
ATOM   3599 C C    B TYR   A 1 161 ? 5.465  -6.074  3.500   0.52 13.25 ?  161 TYR   A C    1 
ATOM   3600 O O    A TYR   A 1 161 ? 5.403  -7.553  3.578   0.48 17.43 ?  161 TYR   A O    1 
ATOM   3601 O O    B TYR   A 1 161 ? 5.600  -7.304  3.458   0.52 13.45 ?  161 TYR   A O    1 
ATOM   3602 C CB   A TYR   A 1 161 ? 6.459  -4.729  5.060   0.48 16.77 ?  161 TYR   A CB   1 
ATOM   3603 C CB   B TYR   A 1 161 ? 6.703  -4.572  5.081   0.52 12.97 ?  161 TYR   A CB   1 
ATOM   3604 C CG   A TYR   A 1 161 ? 6.424  -5.742  6.184   0.48 16.44 ?  161 TYR   A CG   1 
ATOM   3605 C CG   B TYR   A 1 161 ? 6.583  -5.655  6.115   0.52 13.05 ?  161 TYR   A CG   1 
ATOM   3606 C CD1  A TYR   A 1 161 ? 7.586  -6.359  6.629   0.48 16.19 ?  161 TYR   A CD1  1 
ATOM   3607 C CD1  B TYR   A 1 161 ? 7.683  -6.414  6.464   0.52 13.29 ?  161 TYR   A CD1  1 
ATOM   3608 C CD2  A TYR   A 1 161 ? 5.228  -6.072  6.811   0.48 16.33 ?  161 TYR   A CD2  1 
ATOM   3609 C CD2  B TYR   A 1 161 ? 5.362  -5.952  6.717   0.52 13.14 ?  161 TYR   A CD2  1 
ATOM   3610 C CE1  A TYR   A 1 161 ? 7.555  -7.283  7.660   0.48 15.97 ?  161 TYR   A CE1  1 
ATOM   3611 C CE1  B TYR   A 1 161 ? 7.588  -7.422  7.392   0.52 12.99 ?  161 TYR   A CE1  1 
ATOM   3612 C CE2  A TYR   A 1 161 ? 5.187  -6.993  7.836   0.48 16.16 ?  161 TYR   A CE2  1 
ATOM   3613 C CE2  B TYR   A 1 161 ? 5.254  -6.970  7.650   0.52 12.59 ?  161 TYR   A CE2  1 
ATOM   3614 C CZ   A TYR   A 1 161 ? 6.352  -7.595  8.258   0.48 16.34 ?  161 TYR   A CZ   1 
ATOM   3615 C CZ   B TYR   A 1 161 ? 6.377  -7.701  7.983   0.52 12.63 ?  161 TYR   A CZ   1 
ATOM   3616 O OH   A TYR   A 1 161 ? 6.320  -8.513  9.282   0.48 17.22 ?  161 TYR   A OH   1 
ATOM   3617 O OH   B TYR   A 1 161 ? 6.330  -8.721  8.904   0.52 12.64 ?  161 TYR   A OH   1 
ATOM   3618 H H    A TYR   A 1 161 ? 6.170  -3.484  2.999   0.48 20.10 ?  161 TYR   A H    1 
ATOM   3619 H H    B TYR   A 1 161 ? 6.670  -3.292  3.003   0.52 14.93 ?  161 TYR   A H    1 
ATOM   3620 H HA   A TYR   A 1 161 ? 7.164  -5.822  3.481   0.48 20.17 ?  161 TYR   A HA   1 
ATOM   3621 H HA   B TYR   A 1 161 ? 7.468  -5.690  3.548   0.52 15.24 ?  161 TYR   A HA   1 
ATOM   3622 H HB2  A TYR   A 1 161 ? 7.302  -4.248  5.124   0.48 20.10 ?  161 TYR   A HB2  1 
ATOM   3623 H HB2  B TYR   A 1 161 ? 7.549  -4.110  5.219   0.52 15.54 ?  161 TYR   A HB2  1 
ATOM   3624 H HB3  A TYR   A 1 161 ? 5.723  -4.113  5.197   0.48 20.10 ?  161 TYR   A HB3  1 
ATOM   3625 H HB3  B TYR   A 1 161 ? 5.964  -3.955  5.196   0.52 15.54 ?  161 TYR   A HB3  1 
ATOM   3626 H HD1  A TYR   A 1 161 ? 8.402  -6.153  6.229   0.48 19.40 ?  161 TYR   A HD1  1 
ATOM   3627 H HD1  B TYR   A 1 161 ? 8.508  -6.238  6.068   0.52 15.92 ?  161 TYR   A HD1  1 
ATOM   3628 H HD2  A TYR   A 1 161 ? 4.441  -5.670  6.532   0.48 19.57 ?  161 TYR   A HD2  1 
ATOM   3629 H HD2  B TYR   A 1 161 ? 4.610  -5.458  6.494   0.52 15.74 ?  161 TYR   A HD2  1 
ATOM   3630 H HE1  A TYR   A 1 161 ? 8.343  -7.694  7.947   0.48 19.14 ?  161 TYR   A HE1  1 
ATOM   3631 H HE1  B TYR   A 1 161 ? 8.345  -7.924  7.615   0.52 15.56 ?  161 TYR   A HE1  1 
ATOM   3632 H HE2  A TYR   A 1 161 ? 4.379  -7.204  8.244   0.48 19.36 ?  161 TYR   A HE2  1 
ATOM   3633 H HE2  B TYR   A 1 161 ? 4.439  -7.155  8.051   0.52 15.09 ?  161 TYR   A HE2  1 
ATOM   3634 H HH   A TYR   A 1 161 ? 5.528  -8.610  9.553   0.48 20.64 ?  161 TYR   A HH   1 
ATOM   3635 H HH   B TYR   A 1 161 ? 5.533  -8.837  9.162   0.52 15.15 ?  161 TYR   A HH   1 
ATOM   3636 N N    A ASP   A 1 162 ? 3.955  -5.831  3.539   0.48 18.72 ?  162 ASP   A N    1 
ATOM   3637 N N    B ASP   A 1 162 ? 4.270  -5.483  3.402   0.52 13.54 ?  162 ASP   A N    1 
ATOM   3638 C CA   A ASP   A 1 162 ? 2.808  -6.732  3.483   0.48 19.13 ?  162 ASP   A CA   1 
ATOM   3639 C CA   B ASP   A 1 162 ? 3.052  -6.279  3.265   0.52 14.24 ?  162 ASP   A CA   1 
ATOM   3640 C C    A ASP   A 1 162 ? 2.847  -7.590  2.224   0.48 18.85 ?  162 ASP   A C    1 
ATOM   3641 C C    B ASP   A 1 162 ? 3.094  -7.137  2.006   0.52 14.26 ?  162 ASP   A C    1 
ATOM   3642 O O    A ASP   A 1 162 ? 2.462  -8.765  2.251   0.48 18.70 ?  162 ASP   A O    1 
ATOM   3643 O O    B ASP   A 1 162 ? 2.705  -8.312  2.027   0.52 14.54 ?  162 ASP   A O    1 
ATOM   3644 C CB   A ASP   A 1 162 ? 1.501  -5.940  3.556   0.48 19.78 ?  162 ASP   A CB   1 
ATOM   3645 C CB   B ASP   A 1 162 ? 1.824  -5.361  3.232   0.52 15.37 ?  162 ASP   A CB   1 
ATOM   3646 C CG   A ASP   A 1 162 ? 1.249  -5.345  4.925   0.48 20.41 ?  162 ASP   A CG   1 
ATOM   3647 C CG   B ASP   A 1 162 ? 1.557  -4.668  4.567   0.52 16.31 ?  162 ASP   A CG   1 
ATOM   3648 O OD1  A ASP   A 1 162 ? 1.832  -5.841  5.911   0.48 20.48 ?  162 ASP   A OD1  1 
ATOM   3649 O OD1  B ASP   A 1 162 ? 2.070  -5.136  5.607   0.52 16.61 ?  162 ASP   A OD1  1 
ATOM   3650 O OD2  A ASP   A 1 162 ? 0.455  -4.385  5.012   0.48 21.02 -1 162 ASP   A OD2  1 
ATOM   3651 O OD2  B ASP   A 1 162 ? 0.815  -3.656  4.576   0.52 16.73 -1 162 ASP   A OD2  1 
ATOM   3652 H H    A ASP   A 1 162 ? 3.758  -4.990  3.537   0.48 22.44 ?  162 ASP   A H    1 
ATOM   3653 H H    B ASP   A 1 162 ? 4.135  -4.628  3.402   0.52 16.23 ?  162 ASP   A H    1 
ATOM   3654 H HA   A ASP   A 1 162 ? 2.839  -7.324  4.251   0.48 22.93 ?  162 ASP   A HA   1 
ATOM   3655 H HA   B ASP   A 1 162 ? 2.966  -6.867  4.026   0.52 17.06 ?  162 ASP   A HA   1 
ATOM   3656 H HB2  A ASP   A 1 162 ? 1.535  -5.207  2.930   0.48 23.71 ?  162 ASP   A HB2  1 
ATOM   3657 H HB2  B ASP   A 1 162 ? 1.957  -4.677  2.554   0.52 18.43 ?  162 ASP   A HB2  1 
ATOM   3658 H HB3  A ASP   A 1 162 ? 0.762  -6.531  3.346   0.48 23.71 ?  162 ASP   A HB3  1 
ATOM   3659 H HB3  B ASP   A 1 162 ? 1.040  -5.891  3.012   0.52 18.43 ?  162 ASP   A HB3  1 
ATOM   3660 N N    A LYS   A 1 163 ? 3.319  -7.029  1.110   0.48 19.19 ?  163 LYS   A N    1 
ATOM   3661 N N    B LYS   A 1 163 ? 3.561  -6.558  0.897   0.52 14.46 ?  163 LYS   A N    1 
ATOM   3662 C CA   A LYS   A 1 163 ? 3.410  -7.816  -0.115  0.48 19.49 ?  163 LYS   A CA   1 
ATOM   3663 C CA   B LYS   A 1 163 ? 3.672  -7.309  -0.350  0.52 15.32 ?  163 LYS   A CA   1 
ATOM   3664 C C    A LYS   A 1 163 ? 4.537  -8.840  -0.031  0.48 18.37 ?  163 LYS   A C    1 
ATOM   3665 C C    B LYS   A 1 163 ? 4.644  -8.474  -0.209  0.52 14.38 ?  163 LYS   A C    1 
ATOM   3666 O O    A LYS   A 1 163 ? 4.390  -9.973  -0.507  0.48 18.56 ?  163 LYS   A O    1 
ATOM   3667 O O    B LYS   A 1 163 ? 4.379  -9.576  -0.704  0.52 13.83 ?  163 LYS   A O    1 
ATOM   3668 C CB   A LYS   A 1 163 ? 3.599  -6.899  -1.321  0.48 21.46 ?  163 LYS   A CB   1 
ATOM   3669 C CB   B LYS   A 1 163 ? 4.124  -6.364  -1.468  0.52 17.16 ?  163 LYS   A CB   1 
ATOM   3670 C CG   A LYS   A 1 163 ? 3.576  -7.638  -2.647  0.48 23.56 ?  163 LYS   A CG   1 
ATOM   3671 C CG   B LYS   A 1 163 ? 4.332  -7.017  -2.831  0.52 19.99 ?  163 LYS   A CG   1 
ATOM   3672 C CD   A LYS   A 1 163 ? 3.991  -6.737  -3.789  0.48 25.52 ?  163 LYS   A CD   1 
ATOM   3673 C CD   B LYS   A 1 163 ? 4.933  -6.021  -3.825  0.52 22.63 ?  163 LYS   A CD   1 
ATOM   3674 C CE   A LYS   A 1 163 ? 3.898  -7.461  -5.119  0.48 26.93 ?  163 LYS   A CE   1 
ATOM   3675 C CE   B LYS   A 1 163 ? 4.996  -6.591  -5.237  0.52 24.60 ?  163 LYS   A CE   1 
ATOM   3676 N NZ   A LYS   A 1 163 ? 4.583  -6.713  -6.206  0.48 27.81 ?  163 LYS   A NZ   1 
ATOM   3677 N NZ   B LYS   A 1 163 ? 5.686  -5.670  -6.188  0.52 25.85 ?  163 LYS   A NZ   1 
ATOM   3678 H H    A LYS   A 1 163 ? 3.585  -6.215  1.046   0.48 23.01 ?  163 LYS   A H    1 
ATOM   3679 H H    B LYS   A 1 163 ? 3.816  -5.736  0.839   0.52 17.33 ?  163 LYS   A H    1 
ATOM   3680 H HA   A LYS   A 1 163 ? 2.578  -8.299  -0.233  0.48 23.36 ?  163 LYS   A HA   1 
ATOM   3681 H HA   B LYS   A 1 163 ? 2.803  -7.660  -0.594  0.52 18.36 ?  163 LYS   A HA   1 
ATOM   3682 H HB2  A LYS   A 1 163 ? 2.881  -6.246  -1.331  0.48 25.73 ?  163 LYS   A HB2  1 
ATOM   3683 H HB2  B LYS   A 1 163 ? 3.452  -5.669  -1.584  0.52 20.57 ?  163 LYS   A HB2  1 
ATOM   3684 H HB3  A LYS   A 1 163 ? 4.453  -6.451  -1.241  0.48 25.73 ?  163 LYS   A HB3  1 
ATOM   3685 H HB3  B LYS   A 1 163 ? 4.966  -5.953  -1.213  0.52 20.57 ?  163 LYS   A HB3  1 
ATOM   3686 H HG2  A LYS   A 1 163 ? 4.194  -8.386  -2.611  0.48 28.24 ?  163 LYS   A HG2  1 
ATOM   3687 H HG2  B LYS   A 1 163 ? 4.947  -7.761  -2.749  0.52 23.97 ?  163 LYS   A HG2  1 
ATOM   3688 H HG3  A LYS   A 1 163 ? 2.676  -7.957  -2.818  0.48 28.24 ?  163 LYS   A HG3  1 
ATOM   3689 H HG3  B LYS   A 1 163 ? 3.480  -7.316  -3.183  0.52 23.97 ?  163 LYS   A HG3  1 
ATOM   3690 H HD2  A LYS   A 1 163 ? 3.401  -5.968  -3.818  0.48 30.60 ?  163 LYS   A HD2  1 
ATOM   3691 H HD2  B LYS   A 1 163 ? 4.387  -5.219  -3.849  0.52 27.13 ?  163 LYS   A HD2  1 
ATOM   3692 H HD3  A LYS   A 1 163 ? 4.909  -6.454  -3.654  0.48 30.60 ?  163 LYS   A HD3  1 
ATOM   3693 H HD3  B LYS   A 1 163 ? 5.838  -5.799  -3.551  0.52 27.13 ?  163 LYS   A HD3  1 
ATOM   3694 H HE2  A LYS   A 1 163 ? 4.294  -8.342  -5.047  0.48 32.29 ?  163 LYS   A HE2  1 
ATOM   3695 H HE2  B LYS   A 1 163 ? 5.485  -7.427  -5.223  0.52 29.49 ?  163 LYS   A HE2  1 
ATOM   3696 H HE3  A LYS   A 1 163 ? 2.967  -7.545  -5.359  0.48 32.29 ?  163 LYS   A HE3  1 
ATOM   3697 H HE3  B LYS   A 1 163 ? 4.093  -6.737  -5.564  0.52 29.49 ?  163 LYS   A HE3  1 
ATOM   3698 H HZ1  A LYS   A 1 163 ? 4.515  -7.161  -6.971  0.48 33.35 ?  163 LYS   A HZ1  1 
ATOM   3699 H HZ1  B LYS   A 1 163 ? 5.706  -6.030  -7.003  0.52 30.99 ?  163 LYS   A HZ1  1 
ATOM   3700 H HZ2  A LYS   A 1 163 ? 4.207  -5.912  -6.303  0.48 33.35 ?  163 LYS   A HZ2  1 
ATOM   3701 H HZ2  B LYS   A 1 163 ? 5.255  -4.892  -6.228  0.52 30.99 ?  163 LYS   A HZ2  1 
ATOM   3702 H HZ3  A LYS   A 1 163 ? 5.444  -6.606  -6.008  0.48 33.35 ?  163 LYS   A HZ3  1 
ATOM   3703 H HZ3  B LYS   A 1 163 ? 6.522  -5.523  -5.919  0.52 30.99 ?  163 LYS   A HZ3  1 
ATOM   3704 N N    A LEU   A 1 164 ? 5.670  -8.462  0.564   0.48 16.78 ?  164 LEU   A N    1 
ATOM   3705 N N    B LEU   A 1 164 ? 5.775  -8.249  0.460   0.52 14.40 ?  164 LEU   A N    1 
ATOM   3706 C CA   A LEU   A 1 164 ? 6.763  -9.413  0.740   0.48 15.67 ?  164 LEU   A CA   1 
ATOM   3707 C CA   B LEU   A 1 164 ? 6.779  -9.299  0.601   0.52 14.77 ?  164 LEU   A CA   1 
ATOM   3708 C C    A LEU   A 1 164 ? 6.327  -10.590 1.600   0.48 15.53 ?  164 LEU   A C    1 
ATOM   3709 C C    B LEU   A 1 164 ? 6.244  -10.458 1.432   0.52 14.79 ?  164 LEU   A C    1 
ATOM   3710 O O    A LEU   A 1 164 ? 6.637  -11.748 1.291   0.48 14.82 ?  164 LEU   A O    1 
ATOM   3711 O O    B LEU   A 1 164 ? 6.414  -11.629 1.071   0.52 15.06 ?  164 LEU   A O    1 
ATOM   3712 C CB   A LEU   A 1 164 ? 7.958  -8.711  1.380   0.48 14.80 ?  164 LEU   A CB   1 
ATOM   3713 C CB   B LEU   A 1 164 ? 8.037  -8.720  1.246   0.52 15.31 ?  164 LEU   A CB   1 
ATOM   3714 C CG   A LEU   A 1 164 ? 8.778  -7.783  0.485   0.48 14.59 ?  164 LEU   A CG   1 
ATOM   3715 C CG   B LEU   A 1 164 ? 8.895  -7.807  0.364   0.52 15.89 ?  164 LEU   A CG   1 
ATOM   3716 C CD1  A LEU   A 1 164 ? 9.631  -6.882  1.353   0.48 14.26 ?  164 LEU   A CD1  1 
ATOM   3717 C CD1  B LEU   A 1 164 ? 10.021 -7.173  1.169   0.52 16.24 ?  164 LEU   A CD1  1 
ATOM   3718 C CD2  A LEU   A 1 164 ? 9.645  -8.583  -0.478  0.48 14.44 ?  164 LEU   A CD2  1 
ATOM   3719 C CD2  B LEU   A 1 164 ? 9.453  -8.576  -0.825  0.52 15.93 ?  164 LEU   A CD2  1 
ATOM   3720 H H    A LEU   A 1 164 ? 5.827  -7.672  0.873   0.48 20.11 ?  164 LEU   A H    1 
ATOM   3721 H H    B LEU   A 1 164 ? 5.982  -7.499  0.835   0.52 17.26 ?  164 LEU   A H    1 
ATOM   3722 H HA   A LEU   A 1 164 ? 7.039  -9.752  -0.124  0.48 18.78 ?  164 LEU   A HA   1 
ATOM   3723 H HA   B LEU   A 1 164 ? 7.014  -9.631  -0.280  0.52 17.70 ?  164 LEU   A HA   1 
ATOM   3724 H HB2  A LEU   A 1 164 ? 7.636  -8.174  2.120   0.48 17.73 ?  164 LEU   A HB2  1 
ATOM   3725 H HB2  B LEU   A 1 164 ? 7.770  -8.199  2.021   0.52 18.35 ?  164 LEU   A HB2  1 
ATOM   3726 H HB3  A LEU   A 1 164 ? 8.567  -9.385  1.714   0.48 17.73 ?  164 LEU   A HB3  1 
ATOM   3727 H HB3  B LEU   A 1 164 ? 8.599  -9.455  1.531   0.52 18.35 ?  164 LEU   A HB3  1 
ATOM   3728 H HG   A LEU   A 1 164 ? 8.180  -7.222  -0.035  0.48 17.48 ?  164 LEU   A HG   1 
ATOM   3729 H HG   B LEU   A 1 164 ? 8.342  -7.089  0.020   0.52 19.04 ?  164 LEU   A HG   1 
ATOM   3730 H HD11 A LEU   A 1 164 ? 10.128 -6.272  0.787   0.48 17.08 ?  164 LEU   A HD11 1 
ATOM   3731 H HD11 B LEU   A 1 164 ? 10.533 -6.583  0.591   0.52 19.46 ?  164 LEU   A HD11 1 
ATOM   3732 H HD12 A LEU   A 1 164 ? 9.050  -6.381  1.949   0.48 17.08 ?  164 LEU   A HD12 1 
ATOM   3733 H HD12 B LEU   A 1 164 ? 9.641  -6.665  1.903   0.52 19.46 ?  164 LEU   A HD12 1 
ATOM   3734 H HD13 A LEU   A 1 164 ? 10.241 -7.429  1.871   0.48 17.08 ?  164 LEU   A HD13 1 
ATOM   3735 H HD13 B LEU   A 1 164 ? 10.597 -7.874  1.516   0.52 19.46 ?  164 LEU   A HD13 1 
ATOM   3736 H HD21 A LEU   A 1 164 ? 10.169 -7.969  -1.019  0.48 17.31 ?  164 LEU   A HD21 1 
ATOM   3737 H HD21 B LEU   A 1 164 ? 10.142 -8.041  -1.252  0.52 19.10 ?  164 LEU   A HD21 1 
ATOM   3738 H HD22 A LEU   A 1 164 ? 10.238 -9.157  0.034   0.48 17.31 ?  164 LEU   A HD22 1 
ATOM   3739 H HD22 B LEU   A 1 164 ? 9.832  -9.411  -0.510  0.52 19.10 ?  164 LEU   A HD22 1 
ATOM   3740 H HD23 A LEU   A 1 164 ? 9.073  -9.119  -1.047  0.48 17.31 ?  164 LEU   A HD23 1 
ATOM   3741 H HD23 B LEU   A 1 164 ? 8.735  -8.753  -1.451  0.52 19.10 ?  164 LEU   A HD23 1 
ATOM   3742 N N    A VAL   A 1 165 ? 5.604  -10.317 2.685   0.48 15.52 ?  165 VAL   A N    1 
ATOM   3743 N N    B VAL   A 1 165 ? 5.598  -10.151 2.555   0.52 14.22 ?  165 VAL   A N    1 
ATOM   3744 C CA   A VAL   A 1 165 ? 5.157  -11.393 3.563   0.48 15.94 ?  165 VAL   A CA   1 
ATOM   3745 C CA   B VAL   A 1 165 ? 5.067  -11.201 3.420   0.52 14.47 ?  165 VAL   A CA   1 
ATOM   3746 C C    A VAL   A 1 165 ? 4.111  -12.249 2.863   0.48 16.25 ?  165 VAL   A C    1 
ATOM   3747 C C    B VAL   A 1 165 ? 4.012  -12.012 2.682   0.52 14.14 ?  165 VAL   A C    1 
ATOM   3748 O O    A VAL   A 1 165 ? 4.208  -13.482 2.834   0.48 15.93 ?  165 VAL   A O    1 
ATOM   3749 O O    B VAL   A 1 165 ? 4.033  -13.249 2.688   0.52 14.17 ?  165 VAL   A O    1 
ATOM   3750 C CB   A VAL   A 1 165 ? 4.630  -10.823 4.890   0.48 16.25 ?  165 VAL   A CB   1 
ATOM   3751 C CB   B VAL   A 1 165 ? 4.516  -10.592 4.721   0.52 15.39 ?  165 VAL   A CB   1 
ATOM   3752 C CG1  A VAL   A 1 165 ? 3.878  -11.901 5.662   0.48 16.17 ?  165 VAL   A CG1  1 
ATOM   3753 C CG1  B VAL   A 1 165 ? 3.726  -11.628 5.507   0.52 15.55 ?  165 VAL   A CG1  1 
ATOM   3754 C CG2  A VAL   A 1 165 ? 5.776  -10.258 5.716   0.48 16.67 ?  165 VAL   A CG2  1 
ATOM   3755 C CG2  B VAL   A 1 165 ? 5.655  -10.020 5.553   0.52 15.78 ?  165 VAL   A CG2  1 
ATOM   3756 H H    A VAL   A 1 165 ? 5.363  -9.524  2.929   0.48 18.60 ?  165 VAL   A H    1 
ATOM   3757 H H    B VAL   A 1 165 ? 5.459  -9.351  2.834   0.52 17.04 ?  165 VAL   A H    1 
ATOM   3758 H HA   A VAL   A 1 165 ? 5.919  -11.956 3.771   0.48 19.10 ?  165 VAL   A HA   1 
ATOM   3759 H HA   B VAL   A 1 165 ? 5.790  -11.802 3.657   0.52 17.34 ?  165 VAL   A HA   1 
ATOM   3760 H HB   A VAL   A 1 165 ? 4.013  -10.096 4.703   0.48 19.48 ?  165 VAL   A HB   1 
ATOM   3761 H HB   B VAL   A 1 165 ? 3.918  -9.860  4.498   0.52 18.44 ?  165 VAL   A HB   1 
ATOM   3762 H HG11 A VAL   A 1 165 ? 3.812  -11.633 6.590   0.48 19.38 ?  165 VAL   A HG11 1 
ATOM   3763 H HG11 B VAL   A 1 165 ? 3.633  -11.322 6.423   0.52 18.63 ?  165 VAL   A HG11 1 
ATOM   3764 H HG12 A VAL   A 1 165 ? 2.990  -11.998 5.283   0.48 19.38 ?  165 VAL   A HG12 1 
ATOM   3765 H HG12 B VAL   A 1 165 ? 2.851  -11.732 5.104   0.52 18.63 ?  165 VAL   A HG12 1 
ATOM   3766 H HG13 A VAL   A 1 165 ? 4.366  -12.735 5.592   0.48 19.38 ?  165 VAL   A HG13 1 
ATOM   3767 H HG13 B VAL   A 1 165 ? 4.207  -12.470 5.488   0.52 18.63 ?  165 VAL   A HG13 1 
ATOM   3768 H HG21 A VAL   A 1 165 ? 5.423  -9.900  6.546   0.48 19.98 ?  165 VAL   A HG21 1 
ATOM   3769 H HG21 B VAL   A 1 165 ? 5.299  -9.698  6.394   0.52 18.91 ?  165 VAL   A HG21 1 
ATOM   3770 H HG22 A VAL   A 1 165 ? 6.409  -10.968 5.904   0.48 19.98 ?  165 VAL   A HG22 1 
ATOM   3771 H HG22 B VAL   A 1 165 ? 6.309  -10.718 5.714   0.52 18.91 ?  165 VAL   A HG22 1 
ATOM   3772 H HG23 A VAL   A 1 165 ? 6.212  -9.552  5.211   0.48 19.98 ?  165 VAL   A HG23 1 
ATOM   3773 H HG23 B VAL   A 1 165 ? 6.068  -9.288  5.066   0.52 18.91 ?  165 VAL   A HG23 1 
ATOM   3774 N N    A SER   A 1 166 ? 3.092  -11.608 2.290   0.48 16.81 ?  166 SER   A N    1 
ATOM   3775 N N    B SER   A 1 166 ? 3.076  -11.326 2.026   0.52 14.41 ?  166 SER   A N    1 
ATOM   3776 C CA   A SER   A 1 166 ? 1.987  -12.358 1.710   0.48 17.66 ?  166 SER   A CA   1 
ATOM   3777 C CA   B SER   A 1 166 ? 1.966  -12.018 1.387   0.52 15.42 ?  166 SER   A CA   1 
ATOM   3778 C C    A SER   A 1 166 ? 2.410  -13.179 0.503   0.48 18.01 ?  166 SER   A C    1 
ATOM   3779 C C    B SER   A 1 166 ? 2.407  -12.871 0.207   0.52 14.78 ?  166 SER   A C    1 
ATOM   3780 O O    A SER   A 1 166 ? 1.751  -14.174 0.187   0.48 18.45 ?  166 SER   A O    1 
ATOM   3781 O O    B SER   A 1 166 ? 1.654  -13.758 -0.208  0.52 15.74 ?  166 SER   A O    1 
ATOM   3782 C CB   A SER   A 1 166 ? 0.854  -11.414 1.315   0.48 18.49 ?  166 SER   A CB   1 
ATOM   3783 C CB   B SER   A 1 166 ? 0.908  -11.014 0.931   0.52 17.44 ?  166 SER   A CB   1 
ATOM   3784 O OG   A SER   A 1 166 ? 0.277  -10.817 2.464   0.48 19.77 ?  166 SER   A OG   1 
ATOM   3785 O OG   B SER   A 1 166 ? 0.190  -10.495 2.037   0.52 19.60 ?  166 SER   A OG   1 
ATOM   3786 H H    A SER   A 1 166 ? 3.021  -10.753 2.225   0.48 20.15 ?  166 SER   A H    1 
ATOM   3787 H H    B SER   A 1 166 ? 3.067  -10.471 1.932   0.52 17.27 ?  166 SER   A H    1 
ATOM   3788 H HA   A SER   A 1 166 ? 1.643  -12.967 2.383   0.48 21.17 ?  166 SER   A HA   1 
ATOM   3789 H HA   B SER   A 1 166 ? 1.555  -12.608 2.030   0.52 18.48 ?  166 SER   A HA   1 
ATOM   3790 H HB2  A SER   A 1 166 ? 1.207  -10.724 0.732   0.48 22.16 ?  166 SER   A HB2  1 
ATOM   3791 H HB2  B SER   A 1 166 ? 1.342  -10.278 0.474   0.52 20.90 ?  166 SER   A HB2  1 
ATOM   3792 H HB3  A SER   A 1 166 ? 0.170  -11.921 0.848   0.48 22.16 ?  166 SER   A HB3  1 
ATOM   3793 H HB3  B SER   A 1 166 ? 0.290  -11.459 0.326   0.52 20.90 ?  166 SER   A HB3  1 
ATOM   3794 H HG   A SER   A 1 166 ? 0.855  -10.358 2.868   0.48 23.70 ?  166 SER   A HG   1 
ATOM   3795 H HG   B SER   A 1 166 ? -0.397 -9.960  1.772   0.52 23.50 ?  166 SER   A HG   1 
ATOM   3796 N N    A SER   A 1 167 ? 3.487  -12.797 -0.179  0.48 18.34 ?  167 SER   A N    1 
ATOM   3797 N N    B SER   A 1 167 ? 3.600  -12.631 -0.341  0.52 14.50 ?  167 SER   A N    1 
ATOM   3798 C CA   A SER   A 1 167 ? 3.928  -13.526 -1.358  0.48 18.93 ?  167 SER   A CA   1 
ATOM   3799 C CA   B SER   A 1 167 ? 4.080  -13.368 -1.502  0.52 15.07 ?  167 SER   A CA   1 
ATOM   3800 C C    A SER   A 1 167 ? 5.083  -14.480 -1.083  0.48 19.21 ?  167 SER   A C    1 
ATOM   3801 C C    B SER   A 1 167 ? 5.194  -14.352 -1.175  0.52 16.17 ?  167 SER   A C    1 
ATOM   3802 O O    A SER   A 1 167 ? 5.576  -15.116 -2.020  0.48 19.90 ?  167 SER   A O    1 
ATOM   3803 O O    B SER   A 1 167 ? 5.660  -15.056 -2.077  0.52 17.24 ?  167 SER   A O    1 
ATOM   3804 C CB   A SER   A 1 167 ? 4.307  -12.553 -2.481  0.48 19.44 ?  167 SER   A CB   1 
ATOM   3805 C CB   B SER   A 1 167 ? 4.553  -12.399 -2.594  0.52 15.07 ?  167 SER   A CB   1 
ATOM   3806 O OG   A SER   A 1 167 ? 5.346  -11.680 -2.079  0.48 20.02 ?  167 SER   A OG   1 
ATOM   3807 O OG   B SER   A 1 167 ? 5.647  -11.620 -2.142  0.52 15.07 ?  167 SER   A OG   1 
ATOM   3808 H H    A SER   A 1 167 ? 3.972  -12.110 0.021   0.48 21.99 ?  167 SER   A H    1 
ATOM   3809 H H    B SER   A 1 167 ? 4.155  -12.039 -0.053  0.52 17.37 ?  167 SER   A H    1 
ATOM   3810 H HA   A SER   A 1 167 ? 3.187  -14.056 -1.679  0.48 22.69 ?  167 SER   A HA   1 
ATOM   3811 H HA   B SER   A 1 167 ? 3.348  -13.880 -1.871  0.52 18.06 ?  167 SER   A HA   1 
ATOM   3812 H HB2  A SER   A 1 167 ? 4.606  -13.064 -3.250  0.48 23.30 ?  167 SER   A HB2  1 
ATOM   3813 H HB2  B SER   A 1 167 ? 4.830  -12.908 -3.373  0.52 18.06 ?  167 SER   A HB2  1 
ATOM   3814 H HB3  A SER   A 1 167 ? 3.525  -12.029 -2.719  0.48 23.30 ?  167 SER   A HB3  1 
ATOM   3815 H HB3  B SER   A 1 167 ? 3.815  -11.811 -2.835  0.52 18.06 ?  167 SER   A HB3  1 
ATOM   3816 H HG   A SER   A 1 167 ? 5.105  -11.236 -1.408  0.48 24.00 ?  167 SER   A HG   1 
ATOM   3817 H HG   B SER   A 1 167 ? 5.412  -11.161 -1.477  0.52 18.06 ?  167 SER   A HG   1 
ATOM   3818 N N    A PHE   A 1 168 ? 5.518  -14.614 0.168   0.48 19.37 ?  168 PHE   A N    1 
ATOM   3819 N N    B PHE   A 1 168 ? 5.635  -14.428 0.077   0.52 16.38 ?  168 PHE   A N    1 
ATOM   3820 C CA   A PHE   A 1 168 ? 6.685  -15.438 0.454   0.48 19.82 ?  168 PHE   A CA   1 
ATOM   3821 C CA   B PHE   A 1 168 ? 6.795  -15.249 0.395   0.52 17.31 ?  168 PHE   A CA   1 
ATOM   3822 C C    A PHE   A 1 168 ? 6.335  -16.917 0.359   0.48 21.42 ?  168 PHE   A C    1 
ATOM   3823 C C    B PHE   A 1 168 ? 6.450  -16.729 0.299   0.52 18.33 ?  168 PHE   A C    1 
ATOM   3824 O O    A PHE   A 1 168 ? 5.358  -17.377 0.959   0.48 21.49 ?  168 PHE   A O    1 
ATOM   3825 O O    B PHE   A 1 168 ? 5.399  -17.175 0.771   0.52 19.01 ?  168 PHE   A O    1 
ATOM   3826 C CB   A PHE   A 1 168 ? 7.241  -15.137 1.842   0.48 19.04 ?  168 PHE   A CB   1 
ATOM   3827 C CB   B PHE   A 1 168 ? 7.316  -14.934 1.796   0.52 17.58 ?  168 PHE   A CB   1 
ATOM   3828 C CG   A PHE   A 1 168 ? 8.476  -15.928 2.168   0.48 18.09 ?  168 PHE   A CG   1 
ATOM   3829 C CG   B PHE   A 1 168 ? 8.554  -15.704 2.157   0.52 17.38 ?  168 PHE   A CG   1 
ATOM   3830 C CD1  A PHE   A 1 168 ? 9.680  -15.626 1.556   0.48 17.96 ?  168 PHE   A CD1  1 
ATOM   3831 C CD1  B PHE   A 1 168 ? 9.779  -15.354 1.616   0.52 17.66 ?  168 PHE   A CD1  1 
ATOM   3832 C CD2  A PHE   A 1 168 ? 8.434  -16.986 3.063   0.48 17.80 ?  168 PHE   A CD2  1 
ATOM   3833 C CD2  B PHE   A 1 168 ? 8.498  -16.785 3.024   0.52 17.30 ?  168 PHE   A CD2  1 
ATOM   3834 C CE1  A PHE   A 1 168 ? 10.819 -16.355 1.836   0.48 17.71 ?  168 PHE   A CE1  1 
ATOM   3835 C CE1  B PHE   A 1 168 ? 10.921 -16.061 1.937   0.52 17.77 ?  168 PHE   A CE1  1 
ATOM   3836 C CE2  A PHE   A 1 168 ? 9.574  -17.718 3.349   0.48 17.84 ?  168 PHE   A CE2  1 
ATOM   3837 C CE2  B PHE   A 1 168 ? 9.644  -17.495 3.350   0.52 17.48 ?  168 PHE   A CE2  1 
ATOM   3838 C CZ   A PHE   A 1 168 ? 10.767 -17.399 2.735   0.48 17.82 ?  168 PHE   A CZ   1 
ATOM   3839 C CZ   B PHE   A 1 168 ? 10.854 -17.131 2.804   0.52 17.76 ?  168 PHE   A CZ   1 
ATOM   3840 H H    A PHE   A 1 168 ? 5.161  -14.245 0.858   0.48 23.22 ?  168 PHE   A H    1 
ATOM   3841 H H    B PHE   A 1 168 ? 5.288  -14.018 0.748   0.52 19.64 ?  168 PHE   A H    1 
ATOM   3842 H HA   A PHE   A 1 168 ? 7.378  -15.250 -0.198  0.48 23.76 ?  168 PHE   A HA   1 
ATOM   3843 H HA   B PHE   A 1 168 ? 7.508  -15.056 -0.240  0.52 20.75 ?  168 PHE   A HA   1 
ATOM   3844 H HB2  A PHE   A 1 168 ? 7.469  -14.195 1.892   0.48 22.82 ?  168 PHE   A HB2  1 
ATOM   3845 H HB2  B PHE   A 1 168 ? 7.527  -13.988 1.848   0.52 21.07 ?  168 PHE   A HB2  1 
ATOM   3846 H HB3  A PHE   A 1 168 ? 6.567  -15.350 2.505   0.48 22.82 ?  168 PHE   A HB3  1 
ATOM   3847 H HB3  B PHE   A 1 168 ? 6.629  -15.155 2.441   0.52 21.07 ?  168 PHE   A HB3  1 
ATOM   3848 H HD1  A PHE   A 1 168 ? 9.723  -14.923 0.948   0.48 21.53 ?  168 PHE   A HD1  1 
ATOM   3849 H HD1  B PHE   A 1 168 ? 9.836  -14.632 1.030   0.52 21.17 ?  168 PHE   A HD1  1 
ATOM   3850 H HD2  A PHE   A 1 168 ? 7.631  -17.205 3.480   0.48 21.33 ?  168 PHE   A HD2  1 
ATOM   3851 H HD2  B PHE   A 1 168 ? 7.681  -17.033 3.394   0.52 20.73 ?  168 PHE   A HD2  1 
ATOM   3852 H HE1  A PHE   A 1 168 ? 11.624 -16.140 1.420   0.48 21.23 ?  168 PHE   A HE1  1 
ATOM   3853 H HE1  B PHE   A 1 168 ? 11.742 -15.814 1.569   0.52 21.30 ?  168 PHE   A HE1  1 
ATOM   3854 H HE2  A PHE   A 1 168 ? 9.534  -18.424 3.953   0.48 21.38 ?  168 PHE   A HE2  1 
ATOM   3855 H HE2  B PHE   A 1 168 ? 9.592  -18.217 3.934   0.52 20.95 ?  168 PHE   A HE2  1 
ATOM   3856 H HZ   A PHE   A 1 168 ? 11.534 -17.891 2.923   0.48 21.36 ?  168 PHE   A HZ   1 
ATOM   3857 H HZ   B PHE   A 1 168 ? 11.625 -17.606 3.020   0.52 21.29 ?  168 PHE   A HZ   1 
ATOM   3858 N N    A LEU   A 1 169 ? 7.147  -17.663 -0.385  0.48 23.26 ?  169 LEU   A N    1 
ATOM   3859 N N    B LEU   A 1 169 ? 7.355  -17.493 -0.309  0.52 19.34 ?  169 LEU   A N    1 
ATOM   3860 C CA   A LEU   A 1 169 ? 6.946  -19.099 -0.519  0.48 25.65 ?  169 LEU   A CA   1 
ATOM   3861 C CA   B LEU   A 1 169 ? 7.156  -18.924 -0.486  0.52 22.03 ?  169 LEU   A CA   1 
ATOM   3862 C C    A LEU   A 1 169 ? 7.843  -19.859 0.449   0.48 26.45 ?  169 LEU   A C    1 
ATOM   3863 C C    B LEU   A 1 169 ? 7.912  -19.708 0.581   0.52 22.55 ?  169 LEU   A C    1 
ATOM   3864 O O    A LEU   A 1 169 ? 7.396  -20.268 1.521   0.48 26.51 ?  169 LEU   A O    1 
ATOM   3865 O O    B LEU   A 1 169 ? 7.299  -20.267 1.494   0.52 22.79 ?  169 LEU   A O    1 
ATOM   3866 C CB   A LEU   A 1 169 ? 7.219  -19.549 -1.957  0.48 26.97 ?  169 LEU   A CB   1 
ATOM   3867 C CB   B LEU   A 1 169 ? 7.604  -19.355 -1.886  0.52 23.99 ?  169 LEU   A CB   1 
ATOM   3868 C CG   A LEU   A 1 169 ? 6.936  -21.019 -2.279  0.48 28.05 ?  169 LEU   A CG   1 
ATOM   3869 C CG   B LEU   A 1 169 ? 7.354  -20.813 -2.282  0.52 25.79 ?  169 LEU   A CG   1 
ATOM   3870 C CD1  A LEU   A 1 169 ? 5.519  -21.399 -1.882  0.48 28.49 ?  169 LEU   A CD1  1 
ATOM   3871 C CD1  B LEU   A 1 169 ? 5.943  -21.236 -1.917  0.52 26.41 ?  169 LEU   A CD1  1 
ATOM   3872 C CD2  A LEU   A 1 169 ? 7.166  -21.295 -3.759  0.48 28.40 ?  169 LEU   A CD2  1 
ATOM   3873 C CD2  B LEU   A 1 169 ? 7.596  -21.011 -3.774  0.52 26.49 ?  169 LEU   A CD2  1 
ATOM   3874 O OXT  A LEU   A 1 169 ? 9.029  -20.077 0.187   0.48 26.95 -1 169 LEU   A OXT  1 
ATOM   3875 O OXT  B LEU   A 1 169 ? 9.143  -19.793 0.563   0.52 22.75 -1 169 LEU   A OXT  1 
ATOM   3876 H H    A LEU   A 1 169 ? 7.819  -17.358 -0.827  0.48 27.89 ?  169 LEU   A H    1 
ATOM   3877 H H    B LEU   A 1 169 ? 8.103  -17.200 -0.631  0.52 23.19 ?  169 LEU   A H    1 
ATOM   3878 H HA   A LEU   A 1 169 ? 6.026  -19.309 -0.303  0.48 30.75 ?  169 LEU   A HA   1 
ATOM   3879 H HA   B LEU   A 1 169 ? 6.213  -19.118 -0.393  0.52 26.41 ?  169 LEU   A HA   1 
ATOM   3880 H HB2  A LEU   A 1 169 ? 6.668  -19.016 -2.549  0.48 32.34 ?  169 LEU   A HB2  1 
ATOM   3881 H HB2  B LEU   A 1 169 ? 7.140  -18.803 -2.534  0.52 28.76 ?  169 LEU   A HB2  1 
ATOM   3882 H HB3  A LEU   A 1 169 ? 8.154  -19.388 -2.153  0.48 32.34 ?  169 LEU   A HB3  1 
ATOM   3883 H HB3  B LEU   A 1 169 ? 8.558  -19.201 -1.960  0.52 28.76 ?  169 LEU   A HB3  1 
ATOM   3884 H HG   A LEU   A 1 169 ? 7.548  -21.578 -1.775  0.48 33.64 ?  169 LEU   A HG   1 
ATOM   3885 H HG   B LEU   A 1 169 ? 7.974  -21.385 -1.803  0.52 30.93 ?  169 LEU   A HG   1 
ATOM   3886 H HD11 A LEU   A 1 169 ? 5.311  -22.271 -2.251  0.48 34.17 ?  169 LEU   A HD11 1 
ATOM   3887 H HD11 B LEU   A 1 169 ? 5.750  -22.087 -2.339  0.52 31.67 ?  169 LEU   A HD11 1 
ATOM   3888 H HD12 A LEU   A 1 169 ? 5.459  -21.426 -0.914  0.48 34.17 ?  169 LEU   A HD12 1 
ATOM   3889 H HD12 B LEU   A 1 169 ? 5.880  -21.322 -0.953  0.52 31.67 ?  169 LEU   A HD12 1 
ATOM   3890 H HD13 A LEU   A 1 169 ? 4.905  -20.736 -2.235  0.48 34.17 ?  169 LEU   A HD13 1 
ATOM   3891 H HD13 B LEU   A 1 169 ? 5.322  -20.561 -2.232  0.52 31.67 ?  169 LEU   A HD13 1 
ATOM   3892 H HD21 A LEU   A 1 169 ? 6.985  -22.231 -3.939  0.48 34.06 ?  169 LEU   A HD21 1 
ATOM   3893 H HD21 B LEU   A 1 169 ? 7.439  -21.941 -4.001  0.52 31.77 ?  169 LEU   A HD21 1 
ATOM   3894 H HD22 A LEU   A 1 169 ? 6.568  -20.737 -4.281  0.48 34.06 ?  169 LEU   A HD22 1 
ATOM   3895 H HD22 B LEU   A 1 169 ? 6.986  -20.443 -4.271  0.52 31.77 ?  169 LEU   A HD22 1 
ATOM   3896 H HD23 A LEU   A 1 169 ? 8.088  -21.088 -3.979  0.48 34.06 ?  169 LEU   A HD23 1 
ATOM   3897 H HD23 B LEU   A 1 169 ? 8.513  -20.771 -3.981  0.52 31.77 ?  169 LEU   A HD23 1 
ATOM   3898 N N    A SER   B 1 1   ? 50.736 -9.145  -23.682 0.48 29.50 ?  1   SER   B N    1 
ATOM   3899 N N    B SER   B 1 1   ? 50.761 -9.276  -23.791 0.52 27.98 ?  1   SER   B N    1 
ATOM   3900 C CA   A SER   B 1 1   ? 51.257 -10.232 -22.829 0.48 29.27 ?  1   SER   B CA   1 
ATOM   3901 C CA   B SER   B 1 1   ? 51.204 -10.295 -22.816 0.52 28.03 ?  1   SER   B CA   1 
ATOM   3902 C C    A SER   B 1 1   ? 50.182 -11.278 -22.581 0.48 28.15 ?  1   SER   B C    1 
ATOM   3903 C C    B SER   B 1 1   ? 50.092 -11.302 -22.541 0.52 27.27 ?  1   SER   B C    1 
ATOM   3904 O O    A SER   B 1 1   ? 48.998 -11.066 -22.865 0.48 28.10 ?  1   SER   B O    1 
ATOM   3905 O O    B SER   B 1 1   ? 48.929 -11.097 -22.909 0.52 26.87 ?  1   SER   B O    1 
ATOM   3906 C CB   A SER   B 1 1   ? 51.757 -9.679  -21.498 0.48 29.80 ?  1   SER   B CB   1 
ATOM   3907 C CB   B SER   B 1 1   ? 51.643 -9.640  -21.510 0.52 28.51 ?  1   SER   B CB   1 
ATOM   3908 O OG   A SER   B 1 1   ? 50.673 -9.345  -20.654 0.48 30.85 ?  1   SER   B OG   1 
ATOM   3909 O OG   B SER   B 1 1   ? 50.536 -9.455  -20.647 0.52 29.59 ?  1   SER   B OG   1 
ATOM   3910 H H1   A SER   B 1 1   ? 50.470 -9.489  -24.456 0.48 35.38 ?  1   SER   B H1   1 
ATOM   3911 H H1   B SER   B 1 1   ? 51.458 -8.773  -24.019 0.52 33.55 ?  1   SER   B H1   1 
ATOM   3912 H H2   A SER   B 1 1   ? 50.055 -8.756  -23.271 0.48 35.38 ?  1   SER   B H2   1 
ATOM   3913 H H2   B SER   B 1 1   ? 50.438 -9.684  -24.510 0.52 33.55 ?  1   SER   B H2   1 
ATOM   3914 H H3   A SER   B 1 1   ? 51.385 -8.555  -23.821 0.48 35.38 ?  1   SER   B H3   1 
ATOM   3915 H H3   B SER   B 1 1   ? 50.134 -8.772  -23.420 0.52 33.55 ?  1   SER   B H3   1 
ATOM   3916 H HA   A SER   B 1 1   ? 51.997 -10.653 -23.285 0.48 35.10 ?  1   SER   B HA   1 
ATOM   3917 H HA   B SER   B 1 1   ? 51.961 -10.763 -23.193 0.52 33.61 ?  1   SER   B HA   1 
ATOM   3918 H HB2  A SER   B 1 1   ? 52.304 -10.354 -21.069 0.48 35.74 ?  1   SER   B HB2  1 
ATOM   3919 H HB2  B SER   B 1 1   ? 52.292 -10.217 -21.080 0.52 34.18 ?  1   SER   B HB2  1 
ATOM   3920 H HB3  A SER   B 1 1   ? 52.283 -8.881  -21.665 0.48 35.74 ?  1   SER   B HB3  1 
ATOM   3921 H HB3  B SER   B 1 1   ? 52.042 -8.777  -21.703 0.52 34.18 ?  1   SER   B HB3  1 
ATOM   3922 H HG   A SER   B 1 1   ? 50.924 -8.788  -20.078 0.48 36.99 ?  1   SER   B HG   1 
ATOM   3923 H HG   B SER   B 1 1   ? 50.737 -8.903  -20.046 0.52 35.48 ?  1   SER   B HG   1 
ATOM   3924 N N    A MET   B 1 2   ? 50.612 -12.406 -22.031 0.48 26.96 ?  2   MET   B N    1 
ATOM   3925 N N    B MET   B 1 2   ? 50.467 -12.384 -21.870 0.52 26.88 ?  2   MET   B N    1 
ATOM   3926 C CA   A MET   B 1 2   ? 49.773 -13.581 -21.860 0.48 26.20 ?  2   MET   B CA   1 
ATOM   3927 C CA   B MET   B 1 2   ? 49.634 -13.575 -21.735 0.52 26.78 ?  2   MET   B CA   1 
ATOM   3928 C C    A MET   B 1 2   ? 49.539 -13.785 -20.371 0.48 22.94 ?  2   MET   B C    1 
ATOM   3929 C C    B MET   B 1 2   ? 49.371 -13.836 -20.257 0.52 24.64 ?  2   MET   B C    1 
ATOM   3930 O O    A MET   B 1 2   ? 50.490 -14.000 -19.613 0.48 22.23 ?  2   MET   B O    1 
ATOM   3931 O O    B MET   B 1 2   ? 50.228 -14.381 -19.554 0.52 25.32 ?  2   MET   B O    1 
ATOM   3932 C CB   A MET   B 1 2   ? 50.467 -14.791 -22.478 0.48 29.26 ?  2   MET   B CB   1 
ATOM   3933 C CB   B MET   B 1 2   ? 50.357 -14.746 -22.375 0.52 29.38 ?  2   MET   B CB   1 
ATOM   3934 C CG   A MET   B 1 2   ? 49.593 -16.022 -22.634 0.48 32.03 ?  2   MET   B CG   1 
ATOM   3935 C CG   B MET   B 1 2   ? 49.482 -15.922 -22.774 0.52 31.66 ?  2   MET   B CG   1 
ATOM   3936 S SD   A MET   B 1 2   ? 50.411 -17.286 -23.624 0.48 34.66 ?  2   MET   B SD   1 
ATOM   3937 S SD   B MET   B 1 2   ? 50.375 -17.058 -23.845 0.52 33.83 ?  2   MET   B SD   1 
ATOM   3938 C CE   A MET   B 1 2   ? 50.960 -16.283 -25.003 0.48 34.94 ?  2   MET   B CE   1 
ATOM   3939 C CE   B MET   B 1 2   ? 51.309 -15.897 -24.829 0.52 34.11 ?  2   MET   B CE   1 
ATOM   3940 H H    A MET   B 1 2   ? 51.413 -12.518 -21.733 0.48 32.33 ?  2   MET   B H    1 
ATOM   3941 H H    B MET   B 1 2   ? 51.233 -12.460 -21.486 0.52 32.23 ?  2   MET   B H    1 
ATOM   3942 H HA   A MET   B 1 2   ? 48.926 -13.457 -22.314 0.48 31.41 ?  2   MET   B HA   1 
ATOM   3943 H HA   B MET   B 1 2   ? 48.797 -13.444 -22.209 0.52 32.11 ?  2   MET   B HA   1 
ATOM   3944 H HB2  A MET   B 1 2   ? 50.779 -14.515 -23.352 0.48 35.09 ?  2   MET   B HB2  1 
ATOM   3945 H HB2  B MET   B 1 2   ? 50.784 -14.375 -23.155 0.52 35.23 ?  2   MET   B HB2  1 
ATOM   3946 H HB3  A MET   B 1 2   ? 51.222 -15.046 -21.930 0.48 35.09 ?  2   MET   B HB3  1 
ATOM   3947 H HB3  B MET   B 1 2   ? 51.031 -15.094 -21.772 0.52 35.23 ?  2   MET   B HB3  1 
ATOM   3948 H HG2  A MET   B 1 2   ? 49.409 -16.392 -21.755 0.48 38.42 ?  2   MET   B HG2  1 
ATOM   3949 H HG2  B MET   B 1 2   ? 49.209 -16.403 -21.975 0.52 37.97 ?  2   MET   B HG2  1 
ATOM   3950 H HG3  A MET   B 1 2   ? 48.766 -15.781 -23.079 0.48 38.42 ?  2   MET   B HG3  1 
ATOM   3951 H HG3  B MET   B 1 2   ? 48.705 -15.612 -23.256 0.52 37.97 ?  2   MET   B HG3  1 
ATOM   3952 H HE1  A MET   B 1 2   ? 51.106 -16.854 -25.763 0.48 41.90 ?  2   MET   B HE1  1 
ATOM   3953 H HE1  B MET   B 1 2   ? 51.621 -16.356 -25.603 0.52 40.90 ?  2   MET   B HE1  1 
ATOM   3954 H HE2  A MET   B 1 2   ? 50.270 -15.627 -25.203 0.48 41.90 ?  2   MET   B HE2  1 
ATOM   3955 H HE2  B MET   B 1 2   ? 50.727 -15.159 -25.088 0.52 40.90 ?  2   MET   B HE2  1 
ATOM   3956 H HE3  A MET   B 1 2   ? 51.785 -15.825 -24.763 0.48 41.90 ?  2   MET   B HE3  1 
ATOM   3957 H HE3  B MET   B 1 2   ? 52.064 -15.561 -24.309 0.52 40.90 ?  2   MET   B HE3  1 
ATOM   3958 N N    A VAL   B 1 3   ? 48.277 -13.683 -19.956 0.48 20.79 ?  3   VAL   B N    1 
ATOM   3959 N N    B VAL   B 1 3   ? 48.185 -13.457 -19.790 0.52 22.14 ?  3   VAL   B N    1 
ATOM   3960 C CA   A VAL   B 1 3   ? 47.872 -13.919 -18.578 0.48 19.31 ?  3   VAL   B CA   1 
ATOM   3961 C CA   B VAL   B 1 3   ? 47.758 -13.727 -18.424 0.52 20.28 ?  3   VAL   B CA   1 
ATOM   3962 C C    A VAL   B 1 3   ? 46.637 -14.808 -18.596 0.48 17.44 ?  3   VAL   B C    1 
ATOM   3963 C C    B VAL   B 1 3   ? 46.507 -14.592 -18.464 0.52 18.08 ?  3   VAL   B C    1 
ATOM   3964 O O    A VAL   B 1 3   ? 45.940 -14.924 -19.607 0.48 17.17 ?  3   VAL   B O    1 
ATOM   3965 O O    B VAL   B 1 3   ? 45.683 -14.491 -19.378 0.52 18.10 ?  3   VAL   B O    1 
ATOM   3966 C CB   A VAL   B 1 3   ? 47.595 -12.602 -17.815 0.48 20.25 ?  3   VAL   B CB   1 
ATOM   3967 C CB   B VAL   B 1 3   ? 47.516 -12.440 -17.601 0.52 20.81 ?  3   VAL   B CB   1 
ATOM   3968 C CG1  A VAL   B 1 3   ? 48.859 -11.746 -17.741 0.48 20.60 ?  3   VAL   B CG1  1 
ATOM   3969 C CG1  B VAL   B 1 3   ? 48.788 -11.606 -17.520 0.52 21.00 ?  3   VAL   B CG1  1 
ATOM   3970 C CG2  A VAL   B 1 3   ? 46.463 -11.833 -18.476 0.48 20.76 ?  3   VAL   B CG2  1 
ATOM   3971 C CG2  B VAL   B 1 3   ? 46.370 -11.630 -18.190 0.52 21.03 ?  3   VAL   B CG2  1 
ATOM   3972 H H    A VAL   B 1 3   ? 47.622 -13.468 -20.471 0.48 24.92 ?  3   VAL   B H    1 
ATOM   3973 H H    B VAL   B 1 3   ? 47.598 -13.043 -20.266 0.52 26.54 ?  3   VAL   B H    1 
ATOM   3974 H HA   A VAL   B 1 3   ? 48.578 -14.393 -18.113 0.48 23.15 ?  3   VAL   B HA   1 
ATOM   3975 H HA   B VAL   B 1 3   ? 48.450 -14.233 -17.978 0.52 24.32 ?  3   VAL   B HA   1 
ATOM   3976 H HB   A VAL   B 1 3   ? 47.326 -12.815 -16.907 0.48 24.28 ?  3   VAL   B HB   1 
ATOM   3977 H HB   B VAL   B 1 3   ? 47.270 -12.691 -16.698 0.52 24.95 ?  3   VAL   B HB   1 
ATOM   3978 H HG11 A VAL   B 1 3   ? 48.662 -10.936 -17.245 0.48 24.69 ?  3   VAL   B HG11 1 
ATOM   3979 H HG11 B VAL   B 1 3   ? 48.613 -10.818 -16.981 0.52 25.18 ?  3   VAL   B HG11 1 
ATOM   3980 H HG12 A VAL   B 1 3   ? 49.555 -12.249 -17.290 0.48 24.69 ?  3   VAL   B HG12 1 
ATOM   3981 H HG12 B VAL   B 1 3   ? 49.488 -12.138 -17.112 0.52 25.18 ?  3   VAL   B HG12 1 
ATOM   3982 H HG13 A VAL   B 1 3   ? 49.142 -11.523 -18.642 0.48 24.69 ?  3   VAL   B HG13 1 
ATOM   3983 H HG13 B VAL   B 1 3   ? 49.050 -11.343 -18.416 0.52 25.18 ?  3   VAL   B HG13 1 
ATOM   3984 H HG21 A VAL   B 1 3   ? 46.406 -10.953 -18.074 0.48 24.89 ?  3   VAL   B HG21 1 
ATOM   3985 H HG21 B VAL   B 1 3   ? 46.349 -10.760 -17.763 0.52 25.21 ?  3   VAL   B HG21 1 
ATOM   3986 H HG22 A VAL   B 1 3   ? 46.647 -11.752 -19.424 0.48 24.89 ?  3   VAL   B HG22 1 
ATOM   3987 H HG22 B VAL   B 1 3   ? 46.512 -11.529 -19.143 0.52 25.21 ?  3   VAL   B HG22 1 
ATOM   3988 H HG23 A VAL   B 1 3   ? 45.632 -12.313 -18.339 0.48 24.89 ?  3   VAL   B HG23 1 
ATOM   3989 H HG23 B VAL   B 1 3   ? 45.536 -12.098 -18.027 0.52 25.21 ?  3   VAL   B HG23 1 
ATOM   3990 N N    . ASN   B 1 4   ? 46.376 -15.453 -17.458 1.00 16.32 ?  4   ASN   B N    1 
ATOM   3991 C CA   . ASN   B 1 4   ? 45.242 -16.373 -17.345 1.00 15.46 ?  4   ASN   B CA   1 
ATOM   3992 C C    . ASN   B 1 4   ? 45.191 -17.339 -18.530 1.00 15.89 ?  4   ASN   B C    1 
ATOM   3993 O O    . ASN   B 1 4   ? 44.128 -17.612 -19.088 1.00 16.81 ?  4   ASN   B O    1 
ATOM   3994 C CB   . ASN   B 1 4   ? 43.913 -15.627 -17.182 1.00 14.44 ?  4   ASN   B CB   1 
ATOM   3995 C CG   . ASN   B 1 4   ? 43.870 -14.800 -15.920 1.00 13.61 ?  4   ASN   B CG   1 
ATOM   3996 O OD1  . ASN   B 1 4   ? 44.159 -15.300 -14.836 1.00 13.66 ?  4   ASN   B OD1  1 
ATOM   3997 N ND2  . ASN   B 1 4   ? 43.535 -13.522 -16.054 1.00 14.51 ?  4   ASN   B ND2  1 
ATOM   3998 H H    A ASN   B 1 4   ? 46.840 -15.375 -16.739 0.48 19.57 ?  4   ASN   B H    1 
ATOM   3999 H H    B ASN   B 1 4   ? 46.944 -15.527 -16.817 0.52 19.57 ?  4   ASN   B H    1 
ATOM   4000 H HA   . ASN   B 1 4   ? 45.372 -16.904 -16.540 1.00 18.53 ?  4   ASN   B HA   1 
ATOM   4001 H HB2  . ASN   B 1 4   ? 43.783 -15.035 -17.933 1.00 17.31 ?  4   ASN   B HB2  1 
ATOM   4002 H HB3  . ASN   B 1 4   ? 43.191 -16.278 -17.139 1.00 17.31 ?  4   ASN   B HB3  1 
ATOM   4003 H HD21 . ASN   B 1 4   ? 43.502 -13.010 -15.361 1.00 17.39 ?  4   ASN   B HD21 1 
ATOM   4004 H HD22 . ASN   B 1 4   ? 43.348 -13.207 -16.830 1.00 17.39 ?  4   ASN   B HD22 1 
ATOM   4005 N N    . SER   B 1 5   ? 46.355 -17.862 -18.918 1.00 17.34 ?  5   SER   B N    1 
ATOM   4006 C CA   . SER   B 1 5   ? 46.453 -18.780 -20.052 1.00 19.77 ?  5   SER   B CA   1 
ATOM   4007 C C    . SER   B 1 5   ? 46.461 -20.200 -19.501 1.00 20.59 ?  5   SER   B C    1 
ATOM   4008 O O    . SER   B 1 5   ? 47.494 -20.860 -19.406 1.00 22.54 ?  5   SER   B O    1 
ATOM   4009 C CB   . SER   B 1 5   ? 47.692 -18.481 -20.889 1.00 21.54 ?  5   SER   B CB   1 
ATOM   4010 O OG   . SER   B 1 5   ? 48.876 -18.674 -20.135 1.00 23.88 ?  5   SER   B OG   1 
ATOM   4011 H H    . SER   B 1 5   ? 47.111 -17.698 -18.535 1.00 20.78 ?  5   SER   B H    1 
ATOM   4012 H HA   . SER   B 1 5   ? 45.673 -18.676 -20.614 1.00 23.70 ?  5   SER   B HA   1 
ATOM   4013 H HB2  . SER   B 1 5   ? 47.700 -19.069 -21.661 1.00 25.83 ?  5   SER   B HB2  1 
ATOM   4014 H HB3  . SER   B 1 5   ? 47.641 -17.558 -21.180 1.00 25.83 ?  5   SER   B HB3  1 
ATOM   4015 H HG   . SER   B 1 5   ? 48.944 -19.479 -19.910 1.00 28.63 ?  5   SER   B HG   1 
ATOM   4016 N N    . PHE   B 1 6   ? 45.275 -20.663 -19.119 1.00 20.24 ?  6   PHE   B N    1 
ATOM   4017 C CA   . PHE   B 1 6   ? 45.110 -22.008 -18.588 1.00 19.79 ?  6   PHE   B CA   1 
ATOM   4018 C C    . PHE   B 1 6   ? 45.059 -23.001 -19.739 1.00 22.76 ?  6   PHE   B C    1 
ATOM   4019 O O    . PHE   B 1 6   ? 44.368 -22.770 -20.735 1.00 24.76 ?  6   PHE   B O    1 
ATOM   4020 C CB   . PHE   B 1 6   ? 43.821 -22.085 -17.772 1.00 17.62 ?  6   PHE   B CB   1 
ATOM   4021 C CG   . PHE   B 1 6   ? 43.824 -21.208 -16.549 1.00 15.85 ?  6   PHE   B CG   1 
ATOM   4022 C CD1  . PHE   B 1 6   ? 44.325 -21.676 -15.350 1.00 14.75 ?  6   PHE   B CD1  1 
ATOM   4023 C CD2  . PHE   B 1 6   ? 43.326 -19.914 -16.601 1.00 15.71 ?  6   PHE   B CD2  1 
ATOM   4024 C CE1  . PHE   B 1 6   ? 44.319 -20.875 -14.217 1.00 14.63 ?  6   PHE   B CE1  1 
ATOM   4025 C CE2  . PHE   B 1 6   ? 43.335 -19.101 -15.477 1.00 15.64 ?  6   PHE   B CE2  1 
ATOM   4026 C CZ   . PHE   B 1 6   ? 43.830 -19.581 -14.285 1.00 14.91 ?  6   PHE   B CZ   1 
ATOM   4027 H H    . PHE   B 1 6   ? 44.541 -20.214 -19.165 1.00 24.26 ?  6   PHE   B H    1 
ATOM   4028 H HA   . PHE   B 1 6   ? 45.857 -22.233 -18.014 1.00 23.73 ?  6   PHE   B HA   1 
ATOM   4029 H HB2  . PHE   B 1 6   ? 43.077 -21.812 -18.331 1.00 21.12 ?  6   PHE   B HB2  1 
ATOM   4030 H HB3  . PHE   B 1 6   ? 43.689 -23.001 -17.477 1.00 21.12 ?  6   PHE   B HB3  1 
ATOM   4031 H HD1  . PHE   B 1 6   ? 44.661 -22.542 -15.295 1.00 17.68 ?  6   PHE   B HD1  1 
ATOM   4032 H HD2  . PHE   B 1 6   ? 42.988 -19.587 -17.401 1.00 18.83 ?  6   PHE   B HD2  1 
ATOM   4033 H HE1  . PHE   B 1 6   ? 44.667 -21.196 -13.414 1.00 17.53 ?  6   PHE   B HE1  1 
ATOM   4034 H HE2  . PHE   B 1 6   ? 42.993 -18.238 -15.525 1.00 18.75 ?  6   PHE   B HE2  1 
ATOM   4035 H HZ   . PHE   B 1 6   ? 43.832 -19.042 -13.527 1.00 17.87 ?  6   PHE   B HZ   1 
ATOM   4036 N N    A SER   B 1 7   ? 45.783 -24.112 -19.605 0.48 23.09 ?  7   SER   B N    1 
ATOM   4037 N N    B SER   B 1 7   ? 45.801 -24.100 -19.603 0.52 23.17 ?  7   SER   B N    1 
ATOM   4038 C CA   A SER   B 1 7   ? 45.840 -25.113 -20.660 0.48 24.22 ?  7   SER   B CA   1 
ATOM   4039 C CA   B SER   B 1 7   ? 45.916 -25.102 -20.652 0.52 24.46 ?  7   SER   B CA   1 
ATOM   4040 C C    A SER   B 1 7   ? 45.815 -26.511 -20.056 0.48 23.50 ?  7   SER   B C    1 
ATOM   4041 C C    B SER   B 1 7   ? 45.884 -26.492 -20.035 0.52 23.77 ?  7   SER   B C    1 
ATOM   4042 O O    A SER   B 1 7   ? 46.391 -26.752 -18.991 0.48 24.06 ?  7   SER   B O    1 
ATOM   4043 O O    B SER   B 1 7   ? 46.482 -26.731 -18.982 0.52 24.40 ?  7   SER   B O    1 
ATOM   4044 C CB   A SER   B 1 7   ? 47.097 -24.931 -21.525 0.48 25.89 ?  7   SER   B CB   1 
ATOM   4045 C CB   B SER   B 1 7   ? 47.220 -24.918 -21.444 0.52 26.23 ?  7   SER   B CB   1 
ATOM   4046 O OG   A SER   B 1 7   ? 47.028 -25.722 -22.698 0.48 27.39 ?  7   SER   B OG   1 
ATOM   4047 O OG   B SER   B 1 7   ? 47.337 -25.889 -22.469 0.52 27.75 ?  7   SER   B OG   1 
ATOM   4048 H H    A SER   B 1 7   ? 46.254 -24.304 -18.911 0.48 27.68 ?  7   SER   B H    1 
ATOM   4049 H H    B SER   B 1 7   ? 46.258 -24.285 -18.898 0.52 27.78 ?  7   SER   B H    1 
ATOM   4050 H HA   A SER   B 1 7   ? 45.065 -25.021 -21.235 0.48 29.04 ?  7   SER   B HA   1 
ATOM   4051 H HA   B SER   B 1 7   ? 45.170 -25.021 -21.265 0.52 29.33 ?  7   SER   B HA   1 
ATOM   4052 H HB2  A SER   B 1 7   ? 47.171 -23.997 -21.783 0.48 31.05 ?  7   SER   B HB2  1 
ATOM   4053 H HB2  B SER   B 1 7   ? 47.225 -24.030 -21.841 0.52 31.46 ?  7   SER   B HB2  1 
ATOM   4054 H HB3  A SER   B 1 7   ? 47.876 -25.192 -21.010 0.48 31.05 ?  7   SER   B HB3  1 
ATOM   4055 H HB3  B SER   B 1 7   ? 47.973 -25.013 -20.841 0.52 31.46 ?  7   SER   B HB3  1 
ATOM   4056 H HG   A SER   B 1 7   ? 47.724 -25.615 -23.158 0.48 32.84 ?  7   SER   B HG   1 
ATOM   4057 H HG   B SER   B 1 7   ? 48.046 -25.768 -22.900 0.52 33.28 ?  7   SER   B HG   1 
ATOM   4058 N N    A GLY   B 1 8   ? 45.137 -27.427 -20.744 0.48 22.96 ?  8   GLY   B N    1 
ATOM   4059 N N    B GLY   B 1 8   ? 45.176 -27.405 -20.695 0.52 23.21 ?  8   GLY   B N    1 
ATOM   4060 C CA   A GLY   B 1 8   ? 45.099 -28.818 -20.344 0.48 22.36 ?  8   GLY   B CA   1 
ATOM   4061 C CA   B GLY   B 1 8   ? 45.156 -28.788 -20.271 0.52 22.57 ?  8   GLY   B CA   1 
ATOM   4062 C C    A GLY   B 1 8   ? 44.118 -29.153 -19.246 0.48 21.34 ?  8   GLY   B C    1 
ATOM   4063 C C    B GLY   B 1 8   ? 44.185 -29.106 -19.160 0.52 21.47 ?  8   GLY   B C    1 
ATOM   4064 O O    A GLY   B 1 8   ? 44.206 -30.247 -18.674 0.48 21.86 ?  8   GLY   B O    1 
ATOM   4065 O O    B GLY   B 1 8   ? 44.344 -30.135 -18.494 0.52 22.04 ?  8   GLY   B O    1 
ATOM   4066 H H    A GLY   B 1 8   ? 44.689 -27.258 -21.456 0.48 27.52 ?  8   GLY   B H    1 
ATOM   4067 H H    B GLY   B 1 8   ? 44.699 -27.241 -21.390 0.52 27.83 ?  8   GLY   B H    1 
ATOM   4068 H HA2  A GLY   B 1 8   ? 44.873 -29.358 -21.117 0.48 26.81 ?  8   GLY   B HA2  1 
ATOM   4069 H HA2  B GLY   B 1 8   ? 44.934 -29.347 -21.032 0.52 27.06 ?  8   GLY   B HA2  1 
ATOM   4070 H HA3  A GLY   B 1 8   ? 45.977 -29.084 -20.038 0.48 26.81 ?  8   GLY   B HA3  1 
ATOM   4071 H HA3  B GLY   B 1 8   ? 46.039 -29.038 -19.961 0.52 27.06 ?  8   GLY   B HA3  1 
ATOM   4072 N N    . TYR   B 1 9   ? 43.181 -28.263 -18.937 1.00 20.22 ?  9   TYR   B N    1 
ATOM   4073 C CA   . TYR   B 1 9   ? 42.200 -28.522 -17.897 1.00 18.28 ?  9   TYR   B CA   1 
ATOM   4074 C C    . TYR   B 1 9   ? 41.018 -29.306 -18.443 1.00 17.81 ?  9   TYR   B C    1 
ATOM   4075 O O    . TYR   B 1 9   ? 40.628 -29.167 -19.604 1.00 19.55 ?  9   TYR   B O    1 
ATOM   4076 C CB   . TYR   B 1 9   ? 41.694 -27.226 -17.270 1.00 18.00 ?  9   TYR   B CB   1 
ATOM   4077 C CG   . TYR   B 1 9   ? 42.698 -26.610 -16.334 1.00 17.47 ?  9   TYR   B CG   1 
ATOM   4078 C CD1  . TYR   B 1 9   ? 43.815 -25.953 -16.827 1.00 18.43 ?  9   TYR   B CD1  1 
ATOM   4079 C CD2  . TYR   B 1 9   ? 42.544 -26.698 -14.961 1.00 16.74 ?  9   TYR   B CD2  1 
ATOM   4080 C CE1  . TYR   B 1 9   ? 44.750 -25.396 -15.980 1.00 18.16 ?  9   TYR   B CE1  1 
ATOM   4081 C CE2  . TYR   B 1 9   ? 43.475 -26.146 -14.103 1.00 17.23 ?  9   TYR   B CE2  1 
ATOM   4082 C CZ   . TYR   B 1 9   ? 44.579 -25.494 -14.621 1.00 18.23 ?  9   TYR   B CZ   1 
ATOM   4083 O OH   . TYR   B 1 9   ? 45.519 -24.947 -13.784 1.00 18.96 ?  9   TYR   B OH   1 
ATOM   4084 H H    A TYR   B 1 9   ? 43.083 -27.501 -19.326 0.48 24.24 ?  9   TYR   B H    1 
ATOM   4085 H H    B TYR   B 1 9   ? 43.039 -27.537 -19.380 0.52 24.24 ?  9   TYR   B H    1 
ATOM   4086 H HA   . TYR   B 1 9   ? 42.609 -29.052 -17.197 1.00 21.91 ?  9   TYR   B HA   1 
ATOM   4087 H HB2  . TYR   B 1 9   ? 41.498 -26.583 -17.970 1.00 21.58 ?  9   TYR   B HB2  1 
ATOM   4088 H HB3  . TYR   B 1 9   ? 40.896 -27.423 -16.762 1.00 21.58 ?  9   TYR   B HB3  1 
ATOM   4089 H HD1  . TYR   B 1 9   ? 43.938 -25.889 -17.745 1.00 22.09 ?  9   TYR   B HD1  1 
ATOM   4090 H HD2  . TYR   B 1 9   ? 41.799 -27.144 -14.609 1.00 20.06 ?  9   TYR   B HD2  1 
ATOM   4091 H HE1  . TYR   B 1 9   ? 45.491 -24.963 -16.324 1.00 21.77 ?  9   TYR   B HE1  1 
ATOM   4092 H HE2  . TYR   B 1 9   ? 43.353 -26.217 -13.181 1.00 20.65 ?  9   TYR   B HE2  1 
ATOM   4093 H HH   . TYR   B 1 9   ? 46.121 -24.585 -14.230 1.00 22.73 ?  9   TYR   B HH   1 
ATOM   4094 N N    . LEU   B 1 10  ? 40.455 -30.139 -17.580 1.00 16.04 ?  10  LEU   B N    1 
ATOM   4095 C CA   . LEU   B 1 10  ? 39.252 -30.898 -17.876 1.00 15.67 ?  10  LEU   B CA   1 
ATOM   4096 C C    . LEU   B 1 10  ? 38.053 -30.140 -17.320 1.00 15.00 ?  10  LEU   B C    1 
ATOM   4097 O O    . LEU   B 1 10  ? 38.054 -29.735 -16.155 1.00 14.77 ?  10  LEU   B O    1 
ATOM   4098 C CB   . LEU   B 1 10  ? 39.353 -32.279 -17.228 1.00 16.37 ?  10  LEU   B CB   1 
ATOM   4099 C CG   . LEU   B 1 10  ? 38.201 -33.223 -17.547 1.00 18.06 ?  10  LEU   B CG   1 
ATOM   4100 C CD1  . LEU   B 1 10  ? 38.293 -33.715 -18.984 1.00 19.55 ?  10  LEU   B CD1  1 
ATOM   4101 C CD2  . LEU   B 1 10  ? 38.169 -34.394 -16.581 1.00 19.33 ?  10  LEU   B CD2  1 
ATOM   4102 H H    . LEU   B 1 10  ? 40.761 -30.288 -16.786 1.00 19.22 ?  10  LEU   B H    1 
ATOM   4103 H HA   . LEU   B 1 10  ? 39.150 -31.008 -18.832 1.00 18.78 ?  10  LEU   B HA   1 
ATOM   4104 H HB2  . LEU   B 1 10  ? 40.173 -32.709 -17.527 1.00 19.63 ?  10  LEU   B HB2  1 
ATOM   4105 H HB3  . LEU   B 1 10  ? 39.381 -32.173 -16.262 1.00 19.63 ?  10  LEU   B HB3  1 
ATOM   4106 H HG   . LEU   B 1 10  ? 37.365 -32.746 -17.452 1.00 21.65 ?  10  LEU   B HG   1 
ATOM   4107 H HD11 . LEU   B 1 10  ? 37.579 -34.350 -19.148 1.00 23.44 ?  10  LEU   B HD11 1 
ATOM   4108 H HD12 . LEU   B 1 10  ? 38.200 -32.954 -19.581 1.00 23.44 ?  10  LEU   B HD12 1 
ATOM   4109 H HD13 . LEU   B 1 10  ? 39.153 -34.139 -19.120 1.00 23.44 ?  10  LEU   B HD13 1 
ATOM   4110 H HD21 . LEU   B 1 10  ? 37.428 -34.975 -16.815 1.00 23.17 ?  10  LEU   B HD21 1 
ATOM   4111 H HD22 . LEU   B 1 10  ? 39.005 -34.879 -16.644 1.00 23.17 ?  10  LEU   B HD22 1 
ATOM   4112 H HD23 . LEU   B 1 10  ? 38.050 -34.053 -15.680 1.00 23.17 ?  10  LEU   B HD23 1 
ATOM   4113 N N    . LYS   B 1 11  ? 37.039 -29.948 -18.152 1.00 16.28 ?  11  LYS   B N    1 
ATOM   4114 C CA   . LYS   B 1 11  ? 35.841 -29.230 -17.740 1.00 17.98 ?  11  LYS   B CA   1 
ATOM   4115 C C    . LYS   B 1 11  ? 34.945 -30.153 -16.918 1.00 17.46 ?  11  LYS   B C    1 
ATOM   4116 O O    . LYS   B 1 11  ? 34.553 -31.226 -17.389 1.00 19.22 ?  11  LYS   B O    1 
ATOM   4117 C CB   . LYS   B 1 11  ? 35.109 -28.734 -18.986 1.00 21.61 ?  11  LYS   B CB   1 
ATOM   4118 C CG   . LYS   B 1 11  ? 33.904 -27.859 -18.713 1.00 25.43 ?  11  LYS   B CG   1 
ATOM   4119 C CD   . LYS   B 1 11  ? 33.126 -27.594 -19.996 1.00 28.82 ?  11  LYS   B CD   1 
ATOM   4120 C CE   . LYS   B 1 11  ? 32.129 -26.462 -19.822 1.00 31.26 ?  11  LYS   B CE   1 
ATOM   4121 N NZ   . LYS   B 1 11  ? 32.812 -25.153 -19.644 1.00 32.67 ?  11  LYS   B NZ   1 
ATOM   4122 H H    . LYS   B 1 11  ? 37.014 -30.239 -18.963 1.00 19.52 ?  11  LYS   B H    1 
ATOM   4123 H HA   . LYS   B 1 11  ? 36.087 -28.470 -17.195 1.00 21.56 ?  11  LYS   B HA   1 
ATOM   4124 H HB2  . LYS   B 1 11  ? 35.732 -28.215 -19.520 1.00 25.90 ?  11  LYS   B HB2  1 
ATOM   4125 H HB3  . LYS   B 1 11  ? 34.806 -29.501 -19.495 1.00 25.90 ?  11  LYS   B HB3  1 
ATOM   4126 H HG2  . LYS   B 1 11  ? 33.314 -28.307 -18.089 1.00 30.49 ?  11  LYS   B HG2  1 
ATOM   4127 H HG3  . LYS   B 1 11  ? 34.198 -27.010 -18.353 1.00 30.49 ?  11  LYS   B HG3  1 
ATOM   4128 H HD2  . LYS   B 1 11  ? 33.747 -27.348 -20.701 1.00 34.56 ?  11  LYS   B HD2  1 
ATOM   4129 H HD3  . LYS   B 1 11  ? 32.638 -28.395 -20.246 1.00 34.56 ?  11  LYS   B HD3  1 
ATOM   4130 H HE2  . LYS   B 1 11  ? 31.565 -26.407 -20.610 1.00 37.49 ?  11  LYS   B HE2  1 
ATOM   4131 H HE3  . LYS   B 1 11  ? 31.588 -26.635 -19.036 1.00 37.49 ?  11  LYS   B HE3  1 
ATOM   4132 H HZ1  . LYS   B 1 11  ? 32.209 -24.501 -19.585 1.00 39.18 ?  11  LYS   B HZ1  1 
ATOM   4133 H HZ2  . LYS   B 1 11  ? 33.302 -25.163 -18.902 1.00 39.18 ?  11  LYS   B HZ2  1 
ATOM   4134 H HZ3  . LYS   B 1 11  ? 33.344 -24.991 -20.340 1.00 39.18 ?  11  LYS   B HZ3  1 
ATOM   4135 N N    . LEU   B 1 12  ? 34.610 -29.738 -15.695 1.00 15.99 ?  12  LEU   B N    1 
ATOM   4136 C CA   . LEU   B 1 12  ? 33.651 -30.457 -14.861 1.00 15.71 ?  12  LEU   B CA   1 
ATOM   4137 C C    . LEU   B 1 12  ? 32.255 -29.860 -14.948 1.00 15.80 ?  12  LEU   B C    1 
ATOM   4138 O O    . LEU   B 1 12  ? 31.271 -30.583 -15.121 1.00 16.37 ?  12  LEU   B O    1 
ATOM   4139 C CB   . LEU   B 1 12  ? 34.106 -30.475 -13.398 1.00 15.33 ?  12  LEU   B CB   1 
ATOM   4140 C CG   . LEU   B 1 12  ? 35.442 -31.156 -13.122 1.00 15.42 ?  12  LEU   B CG   1 
ATOM   4141 C CD1  . LEU   B 1 12  ? 35.748 -31.122 -11.634 1.00 15.91 ?  12  LEU   B CD1  1 
ATOM   4142 C CD2  . LEU   B 1 12  ? 35.439 -32.583 -13.647 1.00 16.14 ?  12  LEU   B CD2  1 
ATOM   4143 H H    . LEU   B 1 12  ? 34.929 -29.032 -15.327 1.00 19.17 ?  12  LEU   B H    1 
ATOM   4144 H HA   . LEU   B 1 12  ? 33.587 -31.370 -15.171 1.00 18.83 ?  12  LEU   B HA   1 
ATOM   4145 H HB2  . LEU   B 1 12  ? 34.176 -29.561 -13.089 1.00 18.38 ?  12  LEU   B HB2  1 
ATOM   4146 H HB3  . LEU   B 1 12  ? 33.431 -30.941 -12.878 1.00 18.38 ?  12  LEU   B HB3  1 
ATOM   4147 H HG   . LEU   B 1 12  ? 36.144 -30.671 -13.582 1.00 18.47 ?  12  LEU   B HG   1 
ATOM   4148 H HD11 . LEU   B 1 12  ? 36.601 -31.561 -11.478 1.00 19.07 ?  12  LEU   B HD11 1 
ATOM   4149 H HD12 . LEU   B 1 12  ? 35.788 -30.204 -11.338 1.00 19.07 ?  12  LEU   B HD12 1 
ATOM   4150 H HD13 . LEU   B 1 12  ? 35.046 -31.597 -11.157 1.00 19.07 ?  12  LEU   B HD13 1 
ATOM   4151 H HD21 . LEU   B 1 12  ? 36.222 -33.043 -13.316 1.00 19.35 ?  12  LEU   B HD21 1 
ATOM   4152 H HD22 . LEU   B 1 12  ? 34.634 -33.028 -13.337 1.00 19.35 ?  12  LEU   B HD22 1 
ATOM   4153 H HD23 . LEU   B 1 12  ? 35.449 -32.561 -14.618 1.00 19.35 ?  12  LEU   B HD23 1 
ATOM   4154 N N    . THR   B 1 13  ? 32.157 -28.543 -14.815 1.00 15.72 ?  13  THR   B N    1 
ATOM   4155 C CA   . THR   B 1 13  ? 30.930 -27.796 -15.028 1.00 15.61 ?  13  THR   B CA   1 
ATOM   4156 C C    . THR   B 1 13  ? 31.261 -26.590 -15.899 1.00 17.27 ?  13  THR   B C    1 
ATOM   4157 O O    . THR   B 1 13  ? 32.410 -26.381 -16.305 1.00 18.20 ?  13  THR   B O    1 
ATOM   4158 C CB   . THR   B 1 13  ? 30.322 -27.324 -13.704 1.00 15.28 ?  13  THR   B CB   1 
ATOM   4159 O OG1  . THR   B 1 13  ? 31.157 -26.296 -13.152 1.00 15.36 ?  13  THR   B OG1  1 
ATOM   4160 C CG2  . THR   B 1 13  ? 30.197 -28.473 -12.714 1.00 15.95 ?  13  THR   B CG2  1 
ATOM   4161 H H    . THR   B 1 13  ? 32.817 -28.035 -14.591 1.00 18.85 ?  13  THR   B H    1 
ATOM   4162 H HA   . THR   B 1 13  ? 30.280 -28.349 -15.488 1.00 18.71 ?  13  THR   B HA   1 
ATOM   4163 H HB   . THR   B 1 13  ? 29.435 -26.957 -13.867 1.00 18.32 ?  13  THR   B HB   1 
ATOM   4164 H HG1  . THR   B 1 13  ? 30.830 -25.534 -13.317 1.00 18.41 ?  13  THR   B HG1  1 
ATOM   4165 H HG21 . THR   B 1 13  ? 29.683 -28.193 -11.940 1.00 19.12 ?  13  THR   B HG21 1 
ATOM   4166 H HG22 . THR   B 1 13  ? 29.746 -29.223 -13.134 1.00 19.12 ?  13  THR   B HG22 1 
ATOM   4167 H HG23 . THR   B 1 13  ? 31.076 -28.759 -12.422 1.00 19.12 ?  13  THR   B HG23 1 
ATOM   4168 N N    A ASP   B 1 14  ? 30.240 -25.773 -16.165 0.48 18.26 ?  14  ASP   B N    1 
ATOM   4169 N N    B ASP   B 1 14  ? 30.244 -25.769 -16.173 0.52 18.30 ?  14  ASP   B N    1 
ATOM   4170 C CA   A ASP   B 1 14  ? 30.436 -24.601 -17.009 0.48 19.64 ?  14  ASP   B CA   1 
ATOM   4171 C CA   B ASP   B 1 14  ? 30.449 -24.602 -17.025 0.52 19.77 ?  14  ASP   B CA   1 
ATOM   4172 C C    A ASP   B 1 14  ? 31.535 -23.690 -16.476 0.48 17.98 ?  14  ASP   B C    1 
ATOM   4173 C C    B ASP   B 1 14  ? 31.467 -23.622 -16.459 0.52 18.20 ?  14  ASP   B C    1 
ATOM   4174 O O    A ASP   B 1 14  ? 32.196 -22.999 -17.260 0.48 18.78 ?  14  ASP   B O    1 
ATOM   4175 O O    B ASP   B 1 14  ? 31.970 -22.778 -17.209 0.52 19.23 ?  14  ASP   B O    1 
ATOM   4176 C CB   A ASP   B 1 14  ? 29.121 -23.830 -17.154 0.48 22.65 ?  14  ASP   B CB   1 
ATOM   4177 C CB   B ASP   B 1 14  ? 29.130 -23.865 -17.261 0.52 22.86 ?  14  ASP   B CB   1 
ATOM   4178 C CG   A ASP   B 1 14  ? 28.145 -24.502 -18.101 0.48 25.58 ?  14  ASP   B CG   1 
ATOM   4179 C CG   B ASP   B 1 14  ? 28.267 -24.541 -18.308 0.52 25.91 ?  14  ASP   B CG   1 
ATOM   4180 O OD1  A ASP   B 1 14  ? 28.477 -25.566 -18.671 0.48 26.46 ?  14  ASP   B OD1  1 
ATOM   4181 O OD1  B ASP   B 1 14  ? 28.828 -25.230 -19.187 0.52 26.95 ?  14  ASP   B OD1  1 
ATOM   4182 O OD2  A ASP   B 1 14  ? 27.035 -23.957 -18.271 0.48 26.93 -1 14  ASP   B OD2  1 
ATOM   4183 O OD2  B ASP   B 1 14  ? 27.031 -24.384 -18.256 0.52 27.21 -1 14  ASP   B OD2  1 
ATOM   4184 H H    A ASP   B 1 14  ? 29.440 -25.868 -15.865 0.48 21.89 ?  14  ASP   B H    1 
ATOM   4185 H H    B ASP   B 1 14  ? 29.441 -25.864 -15.882 0.52 21.94 ?  14  ASP   B H    1 
ATOM   4186 H HA   A ASP   B 1 14  ? 30.709 -24.884 -17.890 0.48 23.54 ?  14  ASP   B HA   1 
ATOM   4187 H HA   B ASP   B 1 14  ? 30.777 -24.899 -17.886 0.52 23.70 ?  14  ASP   B HA   1 
ATOM   4188 H HB2  A ASP   B 1 14  ? 28.679 -23.778 -16.294 0.48 27.15 ?  14  ASP   B HB2  1 
ATOM   4189 H HB2  B ASP   B 1 14  ? 28.634 -23.827 -16.426 0.52 27.41 ?  14  ASP   B HB2  1 
ATOM   4190 H HB3  A ASP   B 1 14  ? 29.303 -22.938 -17.490 0.48 27.15 ?  14  ASP   B HB3  1 
ATOM   4191 H HB3  B ASP   B 1 14  ? 29.323 -22.961 -17.567 0.52 27.41 ?  14  ASP   B HB3  1 
ATOM   4192 N N    . ASN   B 1 15  ? 31.762 -23.688 -15.159 1.00 15.83 ?  15  ASN   B N    1 
ATOM   4193 C CA   . ASN   B 1 15  ? 32.717 -22.764 -14.553 1.00 13.84 ?  15  ASN   B CA   1 
ATOM   4194 C C    . ASN   B 1 15  ? 33.814 -23.413 -13.718 1.00 13.10 ?  15  ASN   B C    1 
ATOM   4195 O O    . ASN   B 1 15  ? 34.645 -22.681 -13.173 1.00 13.29 ?  15  ASN   B O    1 
ATOM   4196 C CB   . ASN   B 1 15  ? 31.999 -21.712 -13.692 1.00 14.36 ?  15  ASN   B CB   1 
ATOM   4197 C CG   . ASN   B 1 15  ? 31.365 -22.314 -12.455 1.00 13.94 ?  15  ASN   B CG   1 
ATOM   4198 O OD1  . ASN   B 1 15  ? 30.428 -23.112 -12.547 1.00 15.26 ?  15  ASN   B OD1  1 
ATOM   4199 N ND2  . ASN   B 1 15  ? 31.874 -21.953 -11.292 1.00 13.27 ?  15  ASN   B ND2  1 
ATOM   4200 H H    A ASN   B 1 15  ? 31.386 -24.223 -14.598 0.48 18.97 ?  15  ASN   B H    1 
ATOM   4201 H H    B ASN   B 1 15  ? 31.405 -24.242 -14.604 0.52 18.97 ?  15  ASN   B H    1 
ATOM   4202 H HA   . ASN   B 1 15  ? 33.167 -22.283 -15.254 1.00 16.59 ?  15  ASN   B HA   1 
ATOM   4203 H HB2  . ASN   B 1 15  ? 32.640 -21.042 -13.406 1.00 17.21 ?  15  ASN   B HB2  1 
ATOM   4204 H HB3  . ASN   B 1 15  ? 31.297 -21.297 -14.218 1.00 17.21 ?  15  ASN   B HB3  1 
ATOM   4205 H HD21 . ASN   B 1 15  ? 31.543 -22.268 -10.561 1.00 15.90 ?  15  ASN   B HD21 1 
ATOM   4206 H HD22 . ASN   B 1 15  ? 32.528 -21.395 -11.260 1.00 15.90 ?  15  ASN   B HD22 1 
ATOM   4207 N N    . VAL   B 1 16  ? 33.845 -24.739 -13.592 1.00 12.72 ?  16  VAL   B N    1 
ATOM   4208 C CA   . VAL   B 1 16  ? 34.837 -25.432 -12.775 1.00 12.44 ?  16  VAL   B CA   1 
ATOM   4209 C C    . VAL   B 1 16  ? 35.634 -26.373 -13.664 1.00 12.64 ?  16  VAL   B C    1 
ATOM   4210 O O    . VAL   B 1 16  ? 35.058 -27.253 -14.323 1.00 13.65 ?  16  VAL   B O    1 
ATOM   4211 C CB   . VAL   B 1 16  ? 34.197 -26.197 -11.602 1.00 13.11 ?  16  VAL   B CB   1 
ATOM   4212 C CG1  . VAL   B 1 16  ? 35.265 -26.927 -10.783 1.00 13.27 ?  16  VAL   B CG1  1 
ATOM   4213 C CG2  . VAL   B 1 16  ? 33.383 -25.247 -10.719 1.00 13.67 ?  16  VAL   B CG2  1 
ATOM   4214 H H    . VAL   B 1 16  ? 33.291 -25.276 -13.977 1.00 15.24 ?  16  VAL   B H    1 
ATOM   4215 H HA   . VAL   B 1 16  ? 35.453 -24.781 -12.396 1.00 14.91 ?  16  VAL   B HA   1 
ATOM   4216 H HB   . VAL   B 1 16  ? 33.590 -26.864 -11.955 1.00 15.71 ?  16  VAL   B HB   1 
ATOM   4217 H HG11 . VAL   B 1 16  ? 34.870 -27.232 -9.950  1.00 15.90 ?  16  VAL   B HG11 1 
ATOM   4218 H HG12 . VAL   B 1 16  ? 35.592 -27.685 -11.289 1.00 15.90 ?  16  VAL   B HG12 1 
ATOM   4219 H HG13 . VAL   B 1 16  ? 35.992 -26.312 -10.594 1.00 15.90 ?  16  VAL   B HG13 1 
ATOM   4220 H HG21 . VAL   B 1 16  ? 33.031 -25.737 -9.960  1.00 16.38 ?  16  VAL   B HG21 1 
ATOM   4221 H HG22 . VAL   B 1 16  ? 33.957 -24.527 -10.411 1.00 16.38 ?  16  VAL   B HG22 1 
ATOM   4222 H HG23 . VAL   B 1 16  ? 32.650 -24.880 -11.242 1.00 16.38 ?  16  VAL   B HG23 1 
ATOM   4223 N N    . TYR   B 1 17  ? 36.959 -26.211 -13.631 1.00 12.74 ?  17  TYR   B N    1 
ATOM   4224 C CA   . TYR   B 1 17  ? 37.908 -26.962 -14.439 1.00 13.09 ?  17  TYR   B CA   1 
ATOM   4225 C C    . TYR   B 1 17  ? 38.950 -27.570 -13.512 1.00 12.31 ?  17  TYR   B C    1 
ATOM   4226 O O    . TYR   B 1 17  ? 39.211 -27.035 -12.430 1.00 12.60 ?  17  TYR   B O    1 
ATOM   4227 C CB   . TYR   B 1 17  ? 38.620 -26.019 -15.425 1.00 15.34 ?  17  TYR   B CB   1 
ATOM   4228 C CG   . TYR   B 1 17  ? 37.688 -25.243 -16.325 1.00 18.02 ?  17  TYR   B CG   1 
ATOM   4229 C CD1  . TYR   B 1 17  ? 37.083 -24.066 -15.895 1.00 19.23 ?  17  TYR   B CD1  1 
ATOM   4230 C CD2  . TYR   B 1 17  ? 37.413 -25.688 -17.609 1.00 19.85 ?  17  TYR   B CD2  1 
ATOM   4231 C CE1  . TYR   B 1 17  ? 36.228 -23.356 -16.724 1.00 20.56 ?  17  TYR   B CE1  1 
ATOM   4232 C CE2  . TYR   B 1 17  ? 36.563 -24.985 -18.445 1.00 21.17 ?  17  TYR   B CE2  1 
ATOM   4233 C CZ   . TYR   B 1 17  ? 35.974 -23.823 -17.996 1.00 21.83 ?  17  TYR   B CZ   1 
ATOM   4234 O OH   . TYR   B 1 17  ? 35.128 -23.122 -18.824 1.00 23.70 ?  17  TYR   B OH   1 
ATOM   4235 H H    . TYR   B 1 17  ? 37.353 -25.636 -13.116 1.00 15.27 ?  17  TYR   B H    1 
ATOM   4236 H HA   . TYR   B 1 17  ? 37.455 -27.666 -14.929 1.00 15.69 ?  17  TYR   B HA   1 
ATOM   4237 H HB2  . TYR   B 1 17  ? 39.152 -25.382 -14.924 1.00 18.39 ?  17  TYR   B HB2  1 
ATOM   4238 H HB3  . TYR   B 1 17  ? 39.194 -26.550 -15.995 1.00 18.39 ?  17  TYR   B HB3  1 
ATOM   4239 H HD1  . TYR   B 1 17  ? 37.254 -23.747 -15.039 1.00 23.05 ?  17  TYR   B HD1  1 
ATOM   4240 H HD2  . TYR   B 1 17  ? 37.804 -26.470 -17.919 1.00 23.80 ?  17  TYR   B HD2  1 
ATOM   4241 H HE1  . TYR   B 1 17  ? 35.828 -22.567 -16.426 1.00 24.65 ?  17  TYR   B HE1  1 
ATOM   4242 H HE2  . TYR   B 1 17  ? 36.383 -25.296 -19.305 1.00 25.38 ?  17  TYR   B HE2  1 
ATOM   4243 H HH   . TYR   B 1 17  ? 35.053 -23.509 -19.565 1.00 28.42 ?  17  TYR   B HH   1 
ATOM   4244 N N    . ILE   B 1 18  ? 39.575 -28.668 -13.939 1.00 12.18 ?  18  ILE   B N    1 
ATOM   4245 C CA   . ILE   B 1 18  ? 40.505 -29.386 -13.073 1.00 11.78 ?  18  ILE   B CA   1 
ATOM   4246 C C    . ILE   B 1 18  ? 41.673 -29.933 -13.886 1.00 12.28 ?  18  ILE   B C    1 
ATOM   4247 O O    . ILE   B 1 18  ? 41.518 -30.336 -15.044 1.00 13.70 ?  18  ILE   B O    1 
ATOM   4248 C CB   . ILE   B 1 18  ? 39.749 -30.485 -12.285 1.00 12.63 ?  18  ILE   B CB   1 
ATOM   4249 C CG1  . ILE   B 1 18  ? 40.599 -31.032 -11.138 1.00 13.30 ?  18  ILE   B CG1  1 
ATOM   4250 C CG2  . ILE   B 1 18  ? 39.252 -31.595 -13.219 1.00 13.12 ?  18  ILE   B CG2  1 
ATOM   4251 C CD1  . ILE   B 1 18  ? 39.779 -31.832 -10.135 1.00 14.87 ?  18  ILE   B CD1  1 
ATOM   4252 H H    . ILE   B 1 18  ? 39.480 -29.011 -14.720 1.00 14.59 ?  18  ILE   B H    1 
ATOM   4253 H HA   . ILE   B 1 18  ? 40.865 -28.763 -12.421 1.00 14.11 ?  18  ILE   B HA   1 
ATOM   4254 H HB   . ILE   B 1 18  ? 38.966 -30.076 -11.888 1.00 15.14 ?  18  ILE   B HB   1 
ATOM   4255 H HG12 . ILE   B 1 18  ? 41.285 -31.614 -11.496 1.00 15.93 ?  18  ILE   B HG12 1 
ATOM   4256 H HG13 . ILE   B 1 18  ? 41.006 -30.289 -10.663 1.00 15.93 ?  18  ILE   B HG13 1 
ATOM   4257 H HG21 . ILE   B 1 18  ? 38.661 -32.182 -12.721 1.00 15.72 ?  18  ILE   B HG21 1 
ATOM   4258 H HG22 . ILE   B 1 18  ? 38.772 -31.188 -13.956 1.00 15.72 ?  18  ILE   B HG22 1 
ATOM   4259 H HG23 . ILE   B 1 18  ? 40.013 -32.093 -13.550 1.00 15.72 ?  18  ILE   B HG23 1 
ATOM   4260 H HD11 . ILE   B 1 18  ? 40.355 -32.109 -9.405  1.00 17.82 ?  18  ILE   B HD11 1 
ATOM   4261 H HD12 . ILE   B 1 18  ? 39.061 -31.275 -9.797  1.00 17.82 ?  18  ILE   B HD12 1 
ATOM   4262 H HD13 . ILE   B 1 18  ? 39.411 -32.613 -10.580 1.00 17.82 ?  18  ILE   B HD13 1 
ATOM   4263 N N    . LYS   B 1 19  ? 42.852 -29.959 -13.258 1.00 12.71 ?  19  LYS   B N    1 
ATOM   4264 C CA   . LYS   B 1 19  ? 44.065 -30.442 -13.905 1.00 13.29 ?  19  LYS   B CA   1 
ATOM   4265 C C    . LYS   B 1 19  ? 44.952 -31.129 -12.878 1.00 13.22 ?  19  LYS   B C    1 
ATOM   4266 O O    . LYS   B 1 19  ? 45.032 -30.696 -11.728 1.00 12.93 ?  19  LYS   B O    1 
ATOM   4267 C CB   . LYS   B 1 19  ? 44.850 -29.283 -14.531 1.00 14.48 ?  19  LYS   B CB   1 
ATOM   4268 C CG   . LYS   B 1 19  ? 46.081 -29.692 -15.328 1.00 16.23 ?  19  LYS   B CG   1 
ATOM   4269 C CD   . LYS   B 1 19  ? 46.801 -28.458 -15.867 1.00 18.11 ?  19  LYS   B CD   1 
ATOM   4270 C CE   . LYS   B 1 19  ? 47.962 -28.829 -16.773 1.00 20.14 ?  19  LYS   B CE   1 
ATOM   4271 N NZ   . LYS   B 1 19  ? 48.694 -27.624 -17.254 1.00 21.32 ?  19  LYS   B NZ   1 
ATOM   4272 H H    . LYS   B 1 19  ? 42.966 -29.704 -12.441 1.00 15.23 ?  19  LYS   B H    1 
ATOM   4273 H HA   . LYS   B 1 19  ? 43.832 -31.079 -14.597 1.00 15.93 ?  19  LYS   B HA   1 
ATOM   4274 H HB2  . LYS   B 1 19  ? 44.258 -28.804 -15.128 1.00 17.35 ?  19  LYS   B HB2  1 
ATOM   4275 H HB3  . LYS   B 1 19  ? 45.139 -28.691 -13.815 1.00 17.35 ?  19  LYS   B HB3  1 
ATOM   4276 H HG2  . LYS   B 1 19  ? 46.689 -30.179 -14.751 1.00 19.45 ?  19  LYS   B HG2  1 
ATOM   4277 H HG3  . LYS   B 1 19  ? 45.805 -30.243 -16.075 1.00 19.45 ?  19  LYS   B HG3  1 
ATOM   4278 H HD2  . LYS   B 1 19  ? 46.174 -27.921 -16.376 1.00 21.71 ?  19  LYS   B HD2  1 
ATOM   4279 H HD3  . LYS   B 1 19  ? 47.150 -27.943 -15.120 1.00 21.71 ?  19  LYS   B HD3  1 
ATOM   4280 H HE2  . LYS   B 1 19  ? 48.582 -29.389 -16.281 1.00 24.15 ?  19  LYS   B HE2  1 
ATOM   4281 H HE3  . LYS   B 1 19  ? 47.619 -29.307 -17.545 1.00 24.15 ?  19  LYS   B HE3  1 
ATOM   4282 H HZ1  . LYS   B 1 19  ? 49.338 -27.866 -17.819 1.00 25.56 ?  19  LYS   B HZ1  1 
ATOM   4283 H HZ2  . LYS   B 1 19  ? 48.134 -27.074 -17.672 1.00 25.56 ?  19  LYS   B HZ2  1 
ATOM   4284 H HZ3  . LYS   B 1 19  ? 49.060 -27.196 -16.565 1.00 25.56 ?  19  LYS   B HZ3  1 
ATOM   4285 N N    . ASN   B 1 20  ? 45.636 -32.183 -13.310 1.00 14.43 ?  20  ASN   B N    1 
ATOM   4286 C CA   . ASN   B 1 20  ? 46.670 -32.812 -12.495 1.00 15.30 ?  20  ASN   B CA   1 
ATOM   4287 C C    . ASN   B 1 20  ? 47.935 -31.982 -12.680 1.00 15.56 ?  20  ASN   B C    1 
ATOM   4288 O O    . ASN   B 1 20  ? 48.584 -32.049 -13.729 1.00 17.46 ?  20  ASN   B O    1 
ATOM   4289 C CB   . ASN   B 1 20  ? 46.862 -34.257 -12.946 1.00 16.38 ?  20  ASN   B CB   1 
ATOM   4290 C CG   . ASN   B 1 20  ? 47.992 -34.969 -12.228 1.00 17.96 ?  20  ASN   B CG   1 
ATOM   4291 O OD1  . ASN   B 1 20  ? 48.647 -35.838 -12.811 1.00 20.31 ?  20  ASN   B OD1  1 
ATOM   4292 N ND2  . ASN   B 1 20  ? 48.218 -34.633 -10.967 1.00 17.87 ?  20  ASN   B ND2  1 
ATOM   4293 H H    . ASN   B 1 20  ? 45.519 -32.553 -14.075 1.00 17.29 ?  20  ASN   B H    1 
ATOM   4294 H HA   . ASN   B 1 20  ? 46.399 -32.801 -11.562 1.00 18.33 ?  20  ASN   B HA   1 
ATOM   4295 H HB2  . ASN   B 1 20  ? 46.048 -34.752 -12.777 1.00 19.64 ?  20  ASN   B HB2  1 
ATOM   4296 H HB3  . ASN   B 1 20  ? 47.061 -34.260 -13.897 1.00 19.64 ?  20  ASN   B HB3  1 
ATOM   4297 H HD21 . ASN   B 1 20  ? 48.856 -35.005 -10.528 1.00 21.43 ?  20  ASN   B HD21 1 
ATOM   4298 H HD22 . ASN   B 1 20  ? 47.737 -34.026 -10.583 1.00 21.43 ?  20  ASN   B HD22 1 
ATOM   4299 N N    . ALA   B 1 21  ? 48.283 -31.180 -11.671 1.00 14.92 ?  21  ALA   B N    1 
ATOM   4300 C CA   . ALA   B 1 21  ? 49.398 -30.256 -11.810 1.00 15.97 ?  21  ALA   B CA   1 
ATOM   4301 C C    . ALA   B 1 21  ? 49.843 -29.759 -10.444 1.00 15.27 ?  21  ALA   B C    1 
ATOM   4302 O O    . ALA   B 1 21  ? 49.091 -29.785 -9.467  1.00 15.56 ?  21  ALA   B O    1 
ATOM   4303 C CB   . ALA   B 1 21  ? 49.024 -29.079 -12.710 1.00 17.60 ?  21  ALA   B CB   1 
ATOM   4304 H H    . ALA   B 1 21  ? 47.890 -31.156 -10.900 1.00 17.88 ?  21  ALA   B H    1 
ATOM   4305 H HA   . ALA   B 1 21  ? 50.143 -30.726 -12.215 1.00 19.15 ?  21  ALA   B HA   1 
ATOM   4306 H HB1  . ALA   B 1 21  ? 49.808 -28.529 -12.839 1.00 21.09 ?  21  ALA   B HB1  1 
ATOM   4307 H HB2  . ALA   B 1 21  ? 48.714 -29.425 -13.561 1.00 21.09 ?  21  ALA   B HB2  1 
ATOM   4308 H HB3  . ALA   B 1 21  ? 48.318 -28.569 -12.284 1.00 21.09 ?  21  ALA   B HB3  1 
ATOM   4309 N N    . ASP   B 1 22  ? 51.099 -29.311 -10.413 1.00 14.53 ?  22  ASP   B N    1 
ATOM   4310 C CA   . ASP   B 1 22  ? 51.704 -28.606 -9.290  1.00 14.10 ?  22  ASP   B CA   1 
ATOM   4311 C C    . ASP   B 1 22  ? 51.288 -27.137 -9.382  1.00 13.09 ?  22  ASP   B C    1 
ATOM   4312 O O    . ASP   B 1 22  ? 51.598 -26.466 -10.369 1.00 13.39 ?  22  ASP   B O    1 
ATOM   4313 C CB   . ASP   B 1 22  ? 53.222 -28.784 -9.441  1.00 15.20 ?  22  ASP   B CB   1 
ATOM   4314 C CG   . ASP   B 1 22  ? 54.047 -28.020 -8.413  1.00 16.95 ?  22  ASP   B CG   1 
ATOM   4315 O OD1  . ASP   B 1 22  ? 53.675 -26.904 -8.018  1.00 17.41 ?  22  ASP   B OD1  1 
ATOM   4316 O OD2  . ASP   B 1 22  ? 55.124 -28.526 -8.024  1.00 19.23 -1 22  ASP   B OD2  1 
ATOM   4317 H H    . ASP   B 1 22  ? 51.643 -29.407 -11.073 1.00 17.42 ?  22  ASP   B H    1 
ATOM   4318 H HA   . ASP   B 1 22  ? 51.413 -28.988 -8.444  1.00 16.90 ?  22  ASP   B HA   1 
ATOM   4319 H HB2  . ASP   B 1 22  ? 53.441 -29.723 -9.359  1.00 18.22 ?  22  ASP   B HB2  1 
ATOM   4320 H HB3  . ASP   B 1 22  ? 53.487 -28.459 -10.317 1.00 18.22 ?  22  ASP   B HB3  1 
ATOM   4321 N N    . ILE   B 1 23  ? 50.565 -26.645 -8.371  1.00 12.51 ?  23  ILE   B N    1 
ATOM   4322 C CA   . ILE   B 1 23  ? 49.975 -25.305 -8.448  1.00 11.81 ?  23  ILE   B CA   1 
ATOM   4323 C C    . ILE   B 1 23  ? 51.030 -24.214 -8.580  1.00 11.49 ?  23  ILE   B C    1 
ATOM   4324 O O    . ILE   B 1 23  ? 50.761 -23.167 -9.182  1.00 11.36 ?  23  ILE   B O    1 
ATOM   4325 C CB   . ILE   B 1 23  ? 49.024 -25.060 -7.259  1.00 12.33 ?  23  ILE   B CB   1 
ATOM   4326 C CG1  . ILE   B 1 23  ? 48.187 -23.796 -7.474  1.00 13.31 ?  23  ILE   B CG1  1 
ATOM   4327 C CG2  . ILE   B 1 23  ? 49.787 -25.017 -5.949  1.00 13.46 ?  23  ILE   B CG2  1 
ATOM   4328 C CD1  . ILE   B 1 23  ? 47.075 -23.630 -6.466  1.00 14.21 ?  23  ILE   B CD1  1 
ATOM   4329 H H    . ILE   B 1 23  ? 50.401 -27.063 -7.637  1.00 14.99 ?  23  ILE   B H    1 
ATOM   4330 H HA   . ILE   B 1 23  ? 49.435 -25.267 -9.253  1.00 14.14 ?  23  ILE   B HA   1 
ATOM   4331 H HB   . ILE   B 1 23  ? 48.410 -25.813 -7.222  1.00 14.77 ?  23  ILE   B HB   1 
ATOM   4332 H HG12 . ILE   B 1 23  ? 48.770 -23.022 -7.409  1.00 15.95 ?  23  ILE   B HG12 1 
ATOM   4333 H HG13 . ILE   B 1 23  ? 47.787 -23.830 -8.360  1.00 15.95 ?  23  ILE   B HG13 1 
ATOM   4334 H HG21 . ILE   B 1 23  ? 49.152 -25.020 -5.217  1.00 16.13 ?  23  ILE   B HG21 1 
ATOM   4335 H HG22 . ILE   B 1 23  ? 50.360 -25.797 -5.893  1.00 16.13 ?  23  ILE   B HG22 1 
ATOM   4336 H HG23 . ILE   B 1 23  ? 50.322 -24.210 -5.923  1.00 16.13 ?  23  ILE   B HG23 1 
ATOM   4337 H HD11 . ILE   B 1 23  ? 46.540 -22.862 -6.713  1.00 17.03 ?  23  ILE   B HD11 1 
ATOM   4338 H HD12 . ILE   B 1 23  ? 46.529 -24.432 -6.471  1.00 17.03 ?  23  ILE   B HD12 1 
ATOM   4339 H HD13 . ILE   B 1 23  ? 47.465 -23.499 -5.589  1.00 17.03 ?  23  ILE   B HD13 1 
ATOM   4340 N N    . VAL   B 1 24  ? 52.225 -24.420 -8.021  1.00 12.04 ?  24  VAL   B N    1 
ATOM   4341 C CA   . VAL   B 1 24  ? 53.301 -23.441 -8.189  1.00 12.48 ?  24  VAL   B CA   1 
ATOM   4342 C C    . VAL   B 1 24  ? 53.755 -23.395 -9.642  1.00 12.88 ?  24  VAL   B C    1 
ATOM   4343 O O    . VAL   B 1 24  ? 53.902 -22.318 -10.235 1.00 13.33 ?  24  VAL   B O    1 
ATOM   4344 C CB   . VAL   B 1 24  ? 54.476 -23.761 -7.246  1.00 13.22 ?  24  VAL   B CB   1 
ATOM   4345 C CG1  . VAL   B 1 24  ? 55.682 -22.885 -7.581  1.00 14.04 ?  24  VAL   B CG1  1 
ATOM   4346 C CG2  . VAL   B 1 24  ? 54.061 -23.574 -5.801  1.00 14.73 ?  24  VAL   B CG2  1 
ATOM   4347 H H    . VAL   B 1 24  ? 52.433 -25.107 -7.548  1.00 14.43 ?  24  VAL   B H    1 
ATOM   4348 H HA   . VAL   B 1 24  ? 52.966 -22.566 -7.954  1.00 14.96 ?  24  VAL   B HA   1 
ATOM   4349 H HB   . VAL   B 1 24  ? 54.738 -24.691 -7.361  1.00 15.85 ?  24  VAL   B HB   1 
ATOM   4350 H HG11 . VAL   B 1 24  ? 56.262 -22.841 -6.806  1.00 16.82 ?  24  VAL   B HG11 1 
ATOM   4351 H HG12 . VAL   B 1 24  ? 56.155 -23.279 -8.328  1.00 16.82 ?  24  VAL   B HG12 1 
ATOM   4352 H HG13 . VAL   B 1 24  ? 55.367 -21.997 -7.810  1.00 16.82 ?  24  VAL   B HG13 1 
ATOM   4353 H HG21 . VAL   B 1 24  ? 54.790 -23.848 -5.223  1.00 17.65 ?  24  VAL   B HG21 1 
ATOM   4354 H HG22 . VAL   B 1 24  ? 53.854 -22.639 -5.653  1.00 17.65 ?  24  VAL   B HG22 1 
ATOM   4355 H HG23 . VAL   B 1 24  ? 53.277 -24.119 -5.623  1.00 17.65 ?  24  VAL   B HG23 1 
ATOM   4356 N N    . GLU   B 1 25  ? 54.019 -24.565 -10.227 1.00 13.96 ?  25  GLU   B N    1 
ATOM   4357 C CA   . GLU   B 1 25  ? 54.409 -24.601 -11.631 1.00 15.29 ?  25  GLU   B CA   1 
ATOM   4358 C C    . GLU   B 1 25  ? 53.303 -24.050 -12.516 1.00 14.15 ?  25  GLU   B C    1 
ATOM   4359 O O    . GLU   B 1 25  ? 53.572 -23.329 -13.487 1.00 14.96 ?  25  GLU   B O    1 
ATOM   4360 C CB   . GLU   B 1 25  ? 54.781 -26.028 -12.028 1.00 18.48 ?  25  GLU   B CB   1 
ATOM   4361 C CG   . GLU   B 1 25  ? 56.061 -26.500 -11.362 1.00 23.73 ?  25  GLU   B CG   1 
ATOM   4362 C CD   . GLU   B 1 25  ? 57.187 -25.475 -11.427 1.00 29.10 ?  25  GLU   B CD   1 
ATOM   4363 O OE1  . GLU   B 1 25  ? 57.534 -25.036 -12.545 1.00 30.95 ?  25  GLU   B OE1  1 
ATOM   4364 O OE2  . GLU   B 1 25  ? 57.715 -25.092 -10.356 1.00 30.79 -1 25  GLU   B OE2  1 
ATOM   4365 H H    . GLU   B 1 25  ? 53.980 -25.336 -9.840  1.00 16.73 ?  25  GLU   B H    1 
ATOM   4366 H HA   . GLU   B 1 25  ? 55.175 -24.026 -11.755 1.00 18.33 ?  25  GLU   B HA   1 
ATOM   4367 H HB2  . GLU   B 1 25  ? 54.065 -26.631 -11.759 1.00 22.15 ?  25  GLU   B HB2  1 
ATOM   4368 H HB3  . GLU   B 1 25  ? 54.902 -26.070 -12.989 1.00 22.15 ?  25  GLU   B HB3  1 
ATOM   4369 H HG2  . GLU   B 1 25  ? 55.886 -26.668 -10.430 1.00 28.45 ?  25  GLU   B HG2  1 
ATOM   4370 H HG3  . GLU   B 1 25  ? 56.365 -27.304 -11.807 1.00 28.45 ?  25  GLU   B HG3  1 
ATOM   4371 N N    . GLU   B 1 26  ? 52.049 -24.353 -12.179 1.00 13.22 ?  26  GLU   B N    1 
ATOM   4372 C CA   . GLU   B 1 26  ? 50.922 -23.817 -12.936 1.00 13.66 ?  26  GLU   B CA   1 
ATOM   4373 C C    . GLU   B 1 26  ? 50.885 -22.300 -12.855 1.00 13.19 ?  26  GLU   B C    1 
ATOM   4374 O O    . GLU   B 1 26  ? 50.698 -21.619 -13.869 1.00 14.59 ?  26  GLU   B O    1 
ATOM   4375 C CB   . GLU   B 1 26  ? 49.605 -24.390 -12.406 1.00 15.38 ?  26  GLU   B CB   1 
ATOM   4376 C CG   . GLU   B 1 26  ? 49.199 -25.703 -13.019 1.00 18.45 ?  26  GLU   B CG   1 
ATOM   4377 C CD   . GLU   B 1 26  ? 49.007 -25.622 -14.523 1.00 20.10 ?  26  GLU   B CD   1 
ATOM   4378 O OE1  . GLU   B 1 26  ? 48.073 -24.935 -14.993 1.00 20.21 ?  26  GLU   B OE1  1 
ATOM   4379 O OE2  . GLU   B 1 26  ? 49.793 -26.264 -15.234 1.00 21.77 -1 26  GLU   B OE2  1 
ATOM   4380 H H    . GLU   B 1 26  ? 51.824 -24.867 -11.520 1.00 15.84 ?  26  GLU   B H    1 
ATOM   4381 H HA   . GLU   B 1 26  ? 51.016 -24.068 -13.863 1.00 16.36 ?  26  GLU   B HA   1 
ATOM   4382 H HB2  . GLU   B 1 26  ? 49.686 -24.527 -11.447 1.00 18.43 ?  26  GLU   B HB2  1 
ATOM   4383 H HB3  . GLU   B 1 26  ? 48.896 -23.749 -12.580 1.00 18.43 ?  26  GLU   B HB3  1 
ATOM   4384 H HG2  . GLU   B 1 26  ? 49.892 -26.351 -12.849 1.00 22.12 ?  26  GLU   B HG2  1 
ATOM   4385 H HG3  . GLU   B 1 26  ? 48.361 -25.991 -12.622 1.00 22.12 ?  26  GLU   B HG3  1 
ATOM   4386 N N    . ALA   B 1 27  ? 51.032 -21.753 -11.648 1.00 12.40 ?  27  ALA   B N    1 
ATOM   4387 C CA   . ALA   B 1 27  ? 50.993 -20.303 -11.497 1.00 12.73 ?  27  ALA   B CA   1 
ATOM   4388 C C    . ALA   B 1 27  ? 52.072 -19.638 -12.346 1.00 13.91 ?  27  ALA   B C    1 
ATOM   4389 O O    . ALA   B 1 27  ? 51.823 -18.621 -13.007 1.00 14.70 ?  27  ALA   B O    1 
ATOM   4390 C CB   . ALA   B 1 27  ? 51.131 -19.921 -10.023 1.00 13.24 ?  27  ALA   B CB   1 
ATOM   4391 H H    . ALA   B 1 27  ? 51.151 -22.189 -10.912 1.00 14.85 ?  27  ALA   B H    1 
ATOM   4392 H HA   . ALA   B 1 27  ? 50.136 -19.977 -11.804 1.00 15.25 ?  27  ALA   B HA   1 
ATOM   4393 H HB1  . ALA   B 1 27  ? 51.095 -18.953 -9.940  1.00 15.87 ?  27  ALA   B HB1  1 
ATOM   4394 H HB2  . ALA   B 1 27  ? 50.398 -20.318 -9.524  1.00 15.87 ?  27  ALA   B HB2  1 
ATOM   4395 H HB3  . ALA   B 1 27  ? 51.977 -20.249 -9.684  1.00 15.87 ?  27  ALA   B HB3  1 
ATOM   4396 N N    . LYS   B 1 28  ? 53.278 -20.203 -12.349 1.00 15.01 ?  28  LYS   B N    1 
ATOM   4397 C CA   . LYS   B 1 28  ? 54.366 -19.598 -13.108 1.00 16.59 ?  28  LYS   B CA   1 
ATOM   4398 C C    . LYS   B 1 28  ? 54.115 -19.663 -14.611 1.00 17.20 ?  28  LYS   B C    1 
ATOM   4399 O O    . LYS   B 1 28  ? 54.538 -18.762 -15.346 1.00 18.46 ?  28  LYS   B O    1 
ATOM   4400 C CB   . LYS   B 1 28  ? 55.707 -20.232 -12.718 1.00 19.24 ?  28  LYS   B CB   1 
ATOM   4401 C CG   . LYS   B 1 28  ? 56.124 -19.889 -11.289 1.00 22.73 ?  28  LYS   B CG   1 
ATOM   4402 C CD   . LYS   B 1 28  ? 57.543 -20.329 -10.957 1.00 26.75 ?  28  LYS   B CD   1 
ATOM   4403 C CE   . LYS   B 1 28  ? 57.612 -21.800 -10.624 1.00 29.88 ?  28  LYS   B CE   1 
ATOM   4404 N NZ   . LYS   B 1 28  ? 58.957 -22.175 -10.098 1.00 31.40 ?  28  LYS   B NZ   1 
ATOM   4405 H H    . LYS   B 1 28  ? 53.493 -20.920 -11.924 1.00 17.98 ?  28  LYS   B H    1 
ATOM   4406 H HA   . LYS   B 1 28  ? 54.418 -18.659 -12.871 1.00 19.88 ?  28  LYS   B HA   1 
ATOM   4407 H HB2  . LYS   B 1 28  ? 55.634 -21.195 -12.782 1.00 23.06 ?  28  LYS   B HB2  1 
ATOM   4408 H HB3  . LYS   B 1 28  ? 56.398 -19.907 -13.315 1.00 23.06 ?  28  LYS   B HB3  1 
ATOM   4409 H HG2  . LYS   B 1 28  ? 56.071 -18.926 -11.170 1.00 27.25 ?  28  LYS   B HG2  1 
ATOM   4410 H HG3  . LYS   B 1 28  ? 55.519 -20.329 -10.672 1.00 27.25 ?  28  LYS   B HG3  1 
ATOM   4411 H HD2  . LYS   B 1 28  ? 58.115 -20.161 -11.722 1.00 32.07 ?  28  LYS   B HD2  1 
ATOM   4412 H HD3  . LYS   B 1 28  ? 57.858 -19.826 -10.188 1.00 32.07 ?  28  LYS   B HD3  1 
ATOM   4413 H HE2  . LYS   B 1 28  ? 56.951 -22.006 -9.945  1.00 35.83 ?  28  LYS   B HE2  1 
ATOM   4414 H HE3  . LYS   B 1 28  ? 57.443 -22.320 -11.425 1.00 35.83 ?  28  LYS   B HE3  1 
ATOM   4415 H HZ1  . LYS   B 1 28  ? 58.978 -23.044 -9.907  1.00 37.65 ?  28  LYS   B HZ1  1 
ATOM   4416 H HZ2  . LYS   B 1 28  ? 59.582 -21.997 -10.705 1.00 37.65 ?  28  LYS   B HZ2  1 
ATOM   4417 H HZ3  . LYS   B 1 28  ? 59.133 -21.713 -9.357  1.00 37.65 ?  28  LYS   B HZ3  1 
ATOM   4418 N N    . LYS   B 1 29  ? 53.407 -20.694 -15.079 1.00 18.20 ?  29  LYS   B N    1 
ATOM   4419 C CA   . LYS   B 1 29  ? 53.118 -20.822 -16.506 1.00 21.08 ?  29  LYS   B CA   1 
ATOM   4420 C C    . LYS   B 1 29  ? 51.883 -20.027 -16.926 1.00 19.87 ?  29  LYS   B C    1 
ATOM   4421 O O    . LYS   B 1 29  ? 51.898 -19.360 -17.967 1.00 21.22 ?  29  LYS   B O    1 
ATOM   4422 C CB   . LYS   B 1 29  ? 52.949 -22.298 -16.871 1.00 25.92 ?  29  LYS   B CB   1 
ATOM   4423 C CG   . LYS   B 1 29  ? 52.816 -22.549 -18.363 1.00 30.29 ?  29  LYS   B CG   1 
ATOM   4424 C CD   . LYS   B 1 29  ? 53.056 -24.010 -18.715 1.00 33.88 ?  29  LYS   B CD   1 
ATOM   4425 C CE   . LYS   B 1 29  ? 51.943 -24.906 -18.198 1.00 36.32 ?  29  LYS   B CE   1 
ATOM   4426 N NZ   . LYS   B 1 29  ? 52.196 -26.340 -18.519 1.00 37.52 ?  29  LYS   B NZ   1 
ATOM   4427 H H    . LYS   B 1 29  ? 53.093 -21.332 -14.591 1.00 21.81 ?  29  LYS   B H    1 
ATOM   4428 H HA   . LYS   B 1 29  ? 53.871 -20.479 -17.003 1.00 25.27 ?  29  LYS   B HA   1 
ATOM   4429 H HB2  . LYS   B 1 29  ? 53.726 -22.788 -16.557 1.00 31.08 ?  29  LYS   B HB2  1 
ATOM   4430 H HB3  . LYS   B 1 29  ? 52.151 -22.639 -16.440 1.00 31.08 ?  29  LYS   B HB3  1 
ATOM   4431 H HG2  . LYS   B 1 29  ? 51.918 -22.312 -18.646 1.00 36.33 ?  29  LYS   B HG2  1 
ATOM   4432 H HG3  . LYS   B 1 29  ? 53.468 -22.010 -18.837 1.00 36.33 ?  29  LYS   B HG3  1 
ATOM   4433 H HD2  . LYS   B 1 29  ? 53.098 -24.105 -19.680 1.00 40.63 ?  29  LYS   B HD2  1 
ATOM   4434 H HD3  . LYS   B 1 29  ? 53.891 -24.303 -18.315 1.00 40.63 ?  29  LYS   B HD3  1 
ATOM   4435 H HE2  . LYS   B 1 29  ? 51.882 -24.818 -17.234 1.00 43.56 ?  29  LYS   B HE2  1 
ATOM   4436 H HE3  . LYS   B 1 29  ? 51.105 -24.646 -18.612 1.00 43.56 ?  29  LYS   B HE3  1 
ATOM   4437 H HZ1  . LYS   B 1 29  ? 51.533 -26.844 -18.207 1.00 45.00 ?  29  LYS   B HZ1  1 
ATOM   4438 H HZ2  . LYS   B 1 29  ? 52.253 -26.449 -19.401 1.00 45.00 ?  29  LYS   B HZ2  1 
ATOM   4439 H HZ3  . LYS   B 1 29  ? 52.960 -26.604 -18.146 1.00 45.00 ?  29  LYS   B HZ3  1 
ATOM   4440 N N    . VAL   B 1 30  ? 50.806 -20.102 -16.138 1.00 18.38 ?  30  VAL   B N    1 
ATOM   4441 C CA   . VAL   B 1 30  ? 49.516 -19.506 -16.501 1.00 18.74 ?  30  VAL   B CA   1 
ATOM   4442 C C    . VAL   B 1 30  ? 49.522 -17.995 -16.335 1.00 18.42 ?  30  VAL   B C    1 
ATOM   4443 O O    . VAL   B 1 30  ? 48.783 -17.282 -17.028 1.00 19.28 ?  30  VAL   B O    1 
ATOM   4444 C CB   . VAL   B 1 30  ? 48.420 -20.127 -15.613 1.00 19.68 ?  30  VAL   B CB   1 
ATOM   4445 C CG1  . VAL   B 1 30  ? 47.124 -19.327 -15.694 1.00 19.94 ?  30  VAL   B CG1  1 
ATOM   4446 C CG2  . VAL   B 1 30  ? 48.191 -21.584 -15.981 1.00 20.38 ?  30  VAL   B CG2  1 
ATOM   4447 H H    . VAL   B 1 30  ? 50.788 -20.514 -15.378 1.00 22.04 ?  30  VAL   B H    1 
ATOM   4448 H HA   . VAL   B 1 30  ? 49.309 -19.730 -17.424 1.00 22.46 ?  30  VAL   B HA   1 
ATOM   4449 H HB   . VAL   B 1 30  ? 48.715 -20.109 -14.689 1.00 23.59 ?  30  VAL   B HB   1 
ATOM   4450 H HG11 . VAL   B 1 30  ? 46.385 -19.910 -15.456 1.00 23.90 ?  30  VAL   B HG11 1 
ATOM   4451 H HG12 . VAL   B 1 30  ? 47.166 -18.585 -15.073 1.00 23.90 ?  30  VAL   B HG12 1 
ATOM   4452 H HG13 . VAL   B 1 30  ? 47.002 -19.008 -16.598 1.00 23.90 ?  30  VAL   B HG13 1 
ATOM   4453 H HG21 . VAL   B 1 30  ? 47.501 -21.955 -15.404 1.00 24.43 ?  30  VAL   B HG21 1 
ATOM   4454 H HG22 . VAL   B 1 30  ? 47.904 -21.635 -16.907 1.00 24.43 ?  30  VAL   B HG22 1 
ATOM   4455 H HG23 . VAL   B 1 30  ? 49.018 -22.074 -15.863 1.00 24.43 ?  30  VAL   B HG23 1 
ATOM   4456 N N    . LYS   B 1 31  ? 50.290 -17.499 -15.385 1.00 18.05 ?  31  LYS   B N    1 
ATOM   4457 C CA   . LYS   B 1 31  ? 50.315 -16.090 -15.020 1.00 18.68 ?  31  LYS   B CA   1 
ATOM   4458 C C    . LYS   B 1 31  ? 48.911 -15.625 -14.636 1.00 16.34 ?  31  LYS   B C    1 
ATOM   4459 O O    . LYS   B 1 31  ? 48.360 -14.709 -15.261 1.00 17.50 ?  31  LYS   B O    1 
ATOM   4460 C CB   . LYS   B 1 31  ? 50.940 -15.267 -16.151 1.00 21.82 ?  31  LYS   B CB   1 
ATOM   4461 C CG   . LYS   B 1 31  ? 52.345 -15.750 -16.536 1.00 25.20 ?  31  LYS   B CG   1 
ATOM   4462 C CD   . LYS   B 1 31  ? 52.909 -14.977 -17.710 1.00 28.46 ?  31  LYS   B CD   1 
ATOM   4463 C CE   . LYS   B 1 31  ? 54.379 -15.278 -17.900 1.00 31.07 ?  31  LYS   B CE   1 
ATOM   4464 N NZ   . LYS   B 1 31  ? 55.161 -14.879 -16.697 1.00 32.35 ?  31  LYS   B NZ   1 
ATOM   4465 H H    . LYS   B 1 31  ? 50.825 -17.986 -14.928 1.00 21.64 ?  31  LYS   B H    1 
ATOM   4466 H HA   . LYS   B 1 31  ? 50.874 -16.002 -14.244 1.00 22.39 ?  31  LYS   B HA   1 
ATOM   4467 H HB2  . LYS   B 1 31  ? 50.378 -15.326 -16.938 1.00 26.16 ?  31  LYS   B HB2  1 
ATOM   4468 H HB3  . LYS   B 1 31  ? 51.011 -14.348 -15.858 1.00 26.16 ?  31  LYS   B HB3  1 
ATOM   4469 H HG2  . LYS   B 1 31  ? 52.935 -15.635 -15.776 1.00 30.21 ?  31  LYS   B HG2  1 
ATOM   4470 H HG3  . LYS   B 1 31  ? 52.303 -16.689 -16.784 1.00 30.21 ?  31  LYS   B HG3  1 
ATOM   4471 H HD2  . LYS   B 1 31  ? 52.434 -15.235 -18.516 1.00 34.13 ?  31  LYS   B HD2  1 
ATOM   4472 H HD3  . LYS   B 1 31  ? 52.805 -14.029 -17.544 1.00 34.13 ?  31  LYS   B HD3  1 
ATOM   4473 H HE2  . LYS   B 1 31  ? 54.498 -16.231 -18.041 1.00 37.27 ?  31  LYS   B HE2  1 
ATOM   4474 H HE3  . LYS   B 1 31  ? 54.712 -14.780 -18.662 1.00 37.27 ?  31  LYS   B HE3  1 
ATOM   4475 H HZ1  . LYS   B 1 31  ? 56.031 -14.913 -16.875 1.00 38.80 ?  31  LYS   B HZ1  1 
ATOM   4476 H HZ2  . LYS   B 1 31  ? 54.946 -14.049 -16.457 1.00 38.80 ?  31  LYS   B HZ2  1 
ATOM   4477 H HZ3  . LYS   B 1 31  ? 54.982 -15.429 -16.020 1.00 38.80 ?  31  LYS   B HZ3  1 
ATOM   4478 N N    . PRO   B 1 32  ? 48.299 -16.237 -13.614 1.00 13.76 ?  32  PRO   B N    1 
ATOM   4479 C CA   . PRO   B 1 32  ? 46.917 -15.885 -13.270 1.00 12.97 ?  32  PRO   B CA   1 
ATOM   4480 C C    . PRO   B 1 32  ? 46.826 -14.535 -12.578 1.00 12.90 ?  32  PRO   B C    1 
ATOM   4481 O O    . PRO   B 1 32  ? 47.748 -14.101 -11.882 1.00 14.07 ?  32  PRO   B O    1 
ATOM   4482 C CB   . PRO   B 1 32  ? 46.510 -17.001 -12.303 1.00 13.22 ?  32  PRO   B CB   1 
ATOM   4483 C CG   . PRO   B 1 32  ? 47.800 -17.345 -11.616 1.00 13.50 ?  32  PRO   B CG   1 
ATOM   4484 C CD   . PRO   B 1 32  ? 48.858 -17.235 -12.677 1.00 13.56 ?  32  PRO   B CD   1 
ATOM   4485 H HA   . PRO   B 1 32  ? 46.346 -15.902 -14.055 1.00 15.54 ?  32  PRO   B HA   1 
ATOM   4486 H HB2  . PRO   B 1 32  ? 45.850 -16.674 -11.669 1.00 15.84 ?  32  PRO   B HB2  1 
ATOM   4487 H HB3  . PRO   B 1 32  ? 46.165 -17.765 -12.797 1.00 15.84 ?  32  PRO   B HB3  1 
ATOM   4488 H HG2  . PRO   B 1 32  ? 47.967 -16.711 -10.896 1.00 16.18 ?  32  PRO   B HG2  1 
ATOM   4489 H HG3  . PRO   B 1 32  ? 47.759 -18.250 -11.264 1.00 16.18 ?  32  PRO   B HG3  1 
ATOM   4490 H HD2  . PRO   B 1 32  ? 49.686 -16.909 -12.291 1.00 16.25 ?  32  PRO   B HD2  1 
ATOM   4491 H HD3  . PRO   B 1 32  ? 48.977 -18.087 -13.117 1.00 16.25 ?  32  PRO   B HD3  1 
ATOM   4492 N N    . THR   B 1 33  ? 45.667 -13.891 -12.743 1.00 12.44 ?  33  THR   B N    1 
ATOM   4493 C CA   . THR   B 1 33  ? 45.368 -12.712 -11.940 1.00 12.53 ?  33  THR   B CA   1 
ATOM   4494 C C    . THR   B 1 33  ? 45.310 -13.060 -10.460 1.00 12.50 ?  33  THR   B C    1 
ATOM   4495 O O    . THR   B 1 33  ? 45.782 -12.283 -9.617  1.00 13.18 ?  33  THR   B O    1 
ATOM   4496 C CB   . THR   B 1 33  ? 44.053 -12.082 -12.404 1.00 13.29 ?  33  THR   B CB   1 
ATOM   4497 O OG1  . THR   B 1 33  ? 44.119 -11.813 -13.807 1.00 13.44 ?  33  THR   B OG1  1 
ATOM   4498 C CG2  . THR   B 1 33  ? 43.763 -10.790 -11.650 1.00 14.58 ?  33  THR   B CG2  1 
ATOM   4499 H H    . THR   B 1 33  ? 45.048 -14.114 -13.296 1.00 14.90 ?  33  THR   B H    1 
ATOM   4500 H HA   . THR   B 1 33  ? 46.067 -12.055 -12.061 1.00 15.02 ?  33  THR   B HA   1 
ATOM   4501 H HB   . THR   B 1 33  ? 43.322 -12.700 -12.230 1.00 15.92 ?  33  THR   B HB   1 
ATOM   4502 H HG1  . THR   B 1 33  ? 43.398 -11.464 -14.070 1.00 16.10 ?  33  THR   B HG1  1 
ATOM   4503 H HG21 . THR   B 1 33  ? 43.011 -10.333 -12.056 1.00 17.47 ?  33  THR   B HG21 1 
ATOM   4504 H HG22 . THR   B 1 33  ? 43.553 -10.986 -10.724 1.00 17.47 ?  33  THR   B HG22 1 
ATOM   4505 H HG23 . THR   B 1 33  ? 44.540 -10.211 -11.684 1.00 17.47 ?  33  THR   B HG23 1 
ATOM   4506 N N    . VAL   B 1 34  ? 44.758 -14.230 -10.123 1.00 11.52 ?  34  VAL   B N    1 
ATOM   4507 C CA   . VAL   B 1 34  ? 44.569 -14.633 -8.732  1.00 11.02 ?  34  VAL   B CA   1 
ATOM   4508 C C    . VAL   B 1 34  ? 45.007 -16.079 -8.570  1.00 10.51 ?  34  VAL   B C    1 
ATOM   4509 O O    . VAL   B 1 34  ? 44.495 -16.969 -9.262  1.00 10.76 ?  34  VAL   B O    1 
ATOM   4510 C CB   . VAL   B 1 34  ? 43.096 -14.497 -8.290  1.00 12.05 ?  34  VAL   B CB   1 
ATOM   4511 C CG1  . VAL   B 1 34  ? 42.923 -14.980 -6.857  1.00 12.53 ?  34  VAL   B CG1  1 
ATOM   4512 C CG2  . VAL   B 1 34  ? 42.596 -13.064 -8.446  1.00 13.33 ?  34  VAL   B CG2  1 
ATOM   4513 H H    . VAL   B 1 34  ? 44.495 -14.820 -10.689 1.00 13.80 ?  34  VAL   B H    1 
ATOM   4514 H HA   . VAL   B 1 34  ? 45.113 -14.077 -8.151  1.00 13.20 ?  34  VAL   B HA   1 
ATOM   4515 H HB   . VAL   B 1 34  ? 42.547 -15.058 -8.860  1.00 14.44 ?  34  VAL   B HB   1 
ATOM   4516 H HG11 . VAL   B 1 34  ? 42.065 -14.665 -6.520  1.00 15.01 ?  34  VAL   B HG11 1 
ATOM   4517 H HG12 . VAL   B 1 34  ? 42.937 -15.952 -6.845  1.00 15.01 ?  34  VAL   B HG12 1 
ATOM   4518 H HG13 . VAL   B 1 34  ? 43.639 -14.628 -6.313  1.00 15.01 ?  34  VAL   B HG13 1 
ATOM   4519 H HG21 . VAL   B 1 34  ? 41.677 -13.014 -8.143  1.00 15.97 ?  34  VAL   B HG21 1 
ATOM   4520 H HG22 . VAL   B 1 34  ? 43.154 -12.477 -7.911  1.00 15.97 ?  34  VAL   B HG22 1 
ATOM   4521 H HG23 . VAL   B 1 34  ? 42.652 -12.811 -9.381  1.00 15.97 ?  34  VAL   B HG23 1 
ATOM   4522 N N    . VAL   B 1 35  ? 45.916 -16.322 -7.627  1.00 10.07 ?  35  VAL   B N    1 
ATOM   4523 C CA   . VAL   B 1 35  ? 46.157 -17.667 -7.111  1.00 9.74  ?  35  VAL   B CA   1 
ATOM   4524 C C    . VAL   B 1 35  ? 45.614 -17.727 -5.692  1.00 9.34  ?  35  VAL   B C    1 
ATOM   4525 O O    . VAL   B 1 35  ? 45.825 -16.799 -4.902  1.00 9.71  ?  35  VAL   B O    1 
ATOM   4526 C CB   . VAL   B 1 35  ? 47.640 -18.085 -7.195  1.00 10.21 ?  35  VAL   B CB   1 
ATOM   4527 C CG1  . VAL   B 1 35  ? 48.532 -17.230 -6.290  1.00 10.62 ?  35  VAL   B CG1  1 
ATOM   4528 C CG2  . VAL   B 1 35  ? 47.791 -19.582 -6.866  1.00 10.92 ?  35  VAL   B CG2  1 
ATOM   4529 H H    . VAL   B 1 35  ? 46.411 -15.720 -7.263  1.00 12.06 ?  35  VAL   B H    1 
ATOM   4530 H HA   . VAL   B 1 35  ? 45.646 -18.298 -7.645  1.00 11.66 ?  35  VAL   B HA   1 
ATOM   4531 H HB   . VAL   B 1 35  ? 47.944 -17.967 -8.110  1.00 12.23 ?  35  VAL   B HB   1 
ATOM   4532 H HG11 . VAL   B 1 35  ? 49.460 -17.459 -6.461  1.00 12.72 ?  35  VAL   B HG11 1 
ATOM   4533 H HG12 . VAL   B 1 35  ? 48.375 -16.299 -6.494  1.00 12.72 ?  35  VAL   B HG12 1 
ATOM   4534 H HG13 . VAL   B 1 35  ? 48.310 -17.415 -5.366  1.00 12.72 ?  35  VAL   B HG13 1 
ATOM   4535 H HG21 . VAL   B 1 35  ? 48.717 -19.842 -6.975  1.00 13.08 ?  35  VAL   B HG21 1 
ATOM   4536 H HG22 . VAL   B 1 35  ? 47.509 -19.736 -5.949  1.00 13.08 ?  35  VAL   B HG22 1 
ATOM   4537 H HG23 . VAL   B 1 35  ? 47.230 -20.100 -7.470  1.00 13.08 ?  35  VAL   B HG23 1 
ATOM   4538 N N    . VAL   B 1 36  ? 44.896 -18.805 -5.377  1.00 9.41  ?  36  VAL   B N    1 
ATOM   4539 C CA   . VAL   B 1 36  ? 44.344 -19.010 -4.047  1.00 9.27  ?  36  VAL   B CA   1 
ATOM   4540 C C    . VAL   B 1 36  ? 45.350 -19.775 -3.195  1.00 8.96  ?  36  VAL   B C    1 
ATOM   4541 O O    . VAL   B 1 36  ? 45.893 -20.804 -3.622  1.00 9.76  ?  36  VAL   B O    1 
ATOM   4542 C CB   . VAL   B 1 36  ? 43.008 -19.772 -4.130  1.00 9.44  ?  36  VAL   B CB   1 
ATOM   4543 C CG1  . VAL   B 1 36  ? 42.505 -20.133 -2.744  1.00 10.18 ?  36  VAL   B CG1  1 
ATOM   4544 C CG2  . VAL   B 1 36  ? 41.976 -18.940 -4.873  1.00 10.00 ?  36  VAL   B CG2  1 
ATOM   4545 H H    . VAL   B 1 36  ? 44.714 -19.443 -5.930  1.00 11.27 ?  36  VAL   B H    1 
ATOM   4546 H HA   . VAL   B 1 36  ? 44.180 -18.150 -3.633  1.00 11.09 ?  36  VAL   B HA   1 
ATOM   4547 H HB   . VAL   B 1 36  ? 43.143 -20.595 -4.622  1.00 11.31 ?  36  VAL   B HB   1 
ATOM   4548 H HG11 . VAL   B 1 36  ? 41.567 -20.366 -2.804  1.00 12.19 ?  36  VAL   B HG11 1 
ATOM   4549 H HG12 . VAL   B 1 36  ? 43.015 -20.878 -2.403  1.00 12.19 ?  36  VAL   B HG12 1 
ATOM   4550 H HG13 . VAL   B 1 36  ? 42.613 -19.359 -2.161  1.00 12.19 ?  36  VAL   B HG13 1 
ATOM   4551 H HG21 . VAL   B 1 36  ? 41.139 -19.425 -4.898  1.00 11.98 ?  36  VAL   B HG21 1 
ATOM   4552 H HG22 . VAL   B 1 36  ? 41.859 -18.095 -4.411  1.00 11.98 ?  36  VAL   B HG22 1 
ATOM   4553 H HG23 . VAL   B 1 36  ? 42.294 -18.779 -5.777  1.00 11.98 ?  36  VAL   B HG23 1 
ATOM   4554 N N    . ASN   B 1 37  ? 45.574 -19.282 -1.977  1.00 9.50  ?  37  ASN   B N    1 
ATOM   4555 C CA   . ASN   B 1 37  ? 46.329 -20.000 -0.964  1.00 9.57  ?  37  ASN   B CA   1 
ATOM   4556 C C    . ASN   B 1 37  ? 45.380 -20.676 0.018   1.00 9.39  ?  37  ASN   B C    1 
ATOM   4557 O O    . ASN   B 1 37  ? 44.362 -20.100 0.425   1.00 9.89  ?  37  ASN   B O    1 
ATOM   4558 C CB   . ASN   B 1 37  ? 47.261 -19.055 -0.205  1.00 9.54  ?  37  ASN   B CB   1 
ATOM   4559 C CG   . ASN   B 1 37  ? 48.114 -19.776 0.809   1.00 9.76  ?  37  ASN   B CG   1 
ATOM   4560 O OD1  . ASN   B 1 37  ? 48.455 -20.948 0.633   1.00 10.56 ?  37  ASN   B OD1  1 
ATOM   4561 N ND2  . ASN   B 1 37  ? 48.456 -19.083 1.882   1.00 10.07 ?  37  ASN   B ND2  1 
ATOM   4562 H H    . ASN   B 1 37  ? 45.285 -18.513 -1.705  1.00 11.38 ?  37  ASN   B H    1 
ATOM   4563 H HA   . ASN   B 1 37  ? 46.866 -20.687 -1.389  1.00 11.46 ?  37  ASN   B HA   1 
ATOM   4564 H HB2  . ASN   B 1 37  ? 47.853 -18.622 -0.839  1.00 11.43 ?  37  ASN   B HB2  1 
ATOM   4565 H HB3  . ASN   B 1 37  ? 46.733 -18.395 0.266   1.00 11.43 ?  37  ASN   B HB3  1 
ATOM   4566 H HD21 . ASN   B 1 37  ? 48.944 -19.449 2.488   1.00 12.05 ?  37  ASN   B HD21 1 
ATOM   4567 H HD22 . ASN   B 1 37  ? 48.203 -18.273 1.968   1.00 12.05 ?  37  ASN   B HD22 1 
ATOM   4568 N N    . ALA   B 1 38  ? 45.728 -21.913 0.386   1.00 9.69  ?  38  ALA   B N    1 
ATOM   4569 C CA   . ALA   B 1 38  ? 45.072 -22.668 1.458   1.00 10.04 ?  38  ALA   B CA   1 
ATOM   4570 C C    . ALA   B 1 38  ? 45.646 -22.182 2.789   1.00 9.93  ?  38  ALA   B C    1 
ATOM   4571 O O    . ALA   B 1 38  ? 46.548 -22.785 3.382   1.00 10.85 ?  38  ALA   B O    1 
ATOM   4572 C CB   . ALA   B 1 38  ? 45.301 -24.158 1.252   1.00 11.04 ?  38  ALA   B CB   1 
ATOM   4573 H H    . ALA   B 1 38  ? 46.372 -22.349 0.019   1.00 11.61 ?  38  ALA   B H    1 
ATOM   4574 H HA   . ALA   B 1 38  ? 44.116 -22.492 1.445   1.00 12.03 ?  38  ALA   B HA   1 
ATOM   4575 H HB1  . ALA   B 1 38  ? 44.855 -24.648 1.967   1.00 13.22 ?  38  ALA   B HB1  1 
ATOM   4576 H HB2  . ALA   B 1 38  ? 44.924 -24.423 0.396   1.00 13.22 ?  38  ALA   B HB2  1 
ATOM   4577 H HB3  . ALA   B 1 38  ? 46.249 -24.342 1.269   1.00 13.22 ?  38  ALA   B HB3  1 
ATOM   4578 N N    . ALA   B 1 39  ? 45.134 -21.036 3.242   1.00 9.95  ?  39  ALA   B N    1 
ATOM   4579 C CA   . ALA   B 1 39  ? 45.678 -20.299 4.371   1.00 10.15 ?  39  ALA   B CA   1 
ATOM   4580 C C    . ALA   B 1 39  ? 45.056 -20.747 5.691   1.00 10.51 ?  39  ALA   B C    1 
ATOM   4581 O O    . ALA   B 1 39  ? 44.025 -21.420 5.739   1.00 11.33 ?  39  ALA   B O    1 
ATOM   4582 C CB   . ALA   B 1 39  ? 45.440 -18.799 4.173   1.00 10.94 ?  39  ALA   B CB   1 
ATOM   4583 H H    . ALA   B 1 39  ? 44.448 -20.658 2.886   1.00 11.92 ?  39  ALA   B H    1 
ATOM   4584 H HA   . ALA   B 1 39  ? 46.633 -20.446 4.417   1.00 12.15 ?  39  ALA   B HA   1 
ATOM   4585 H HB1  . ALA   B 1 39  ? 45.806 -18.316 4.930   1.00 13.11 ?  39  ALA   B HB1  1 
ATOM   4586 H HB2  . ALA   B 1 39  ? 45.884 -18.511 3.355   1.00 13.11 ?  39  ALA   B HB2  1 
ATOM   4587 H HB3  . ALA   B 1 39  ? 44.487 -18.631 4.103   1.00 13.11 ?  39  ALA   B HB3  1 
ATOM   4588 N N    . ASN   B 1 40  ? 45.698 -20.330 6.780   1.00 11.24 ?  40  ASN   B N    1 
ATOM   4589 C CA   . ASN   B 1 40  ? 45.133 -20.380 8.121   1.00 11.93 ?  40  ASN   B CA   1 
ATOM   4590 C C    . ASN   B 1 40  ? 44.957 -18.954 8.653   1.00 11.64 ?  40  ASN   B C    1 
ATOM   4591 O O    . ASN   B 1 40  ? 45.371 -17.973 8.028   1.00 11.60 ?  40  ASN   B O    1 
ATOM   4592 C CB   . ASN   B 1 40  ? 45.976 -21.262 9.062   1.00 12.51 ?  40  ASN   B CB   1 
ATOM   4593 C CG   . ASN   B 1 40  ? 47.430 -20.863 9.102   1.00 13.87 ?  40  ASN   B CG   1 
ATOM   4594 O OD1  . ASN   B 1 40  ? 47.752 -19.682 9.162   1.00 15.56 ?  40  ASN   B OD1  1 
ATOM   4595 N ND2  . ASN   B 1 40  ? 48.317 -21.841 9.077   1.00 14.09 ?  40  ASN   B ND2  1 
ATOM   4596 H H    . ASN   B 1 40  ? 46.500 -20.012 6.763   1.00 13.46 ?  40  ASN   B H    1 
ATOM   4597 H HA   . ASN   B 1 40  ? 44.250 -20.771 8.067   1.00 14.29 ?  40  ASN   B HA   1 
ATOM   4598 H HB2  . ASN   B 1 40  ? 45.621 -21.188 9.960   1.00 14.99 ?  40  ASN   B HB2  1 
ATOM   4599 H HB3  . ASN   B 1 40  ? 45.924 -22.179 8.755   1.00 14.99 ?  40  ASN   B HB3  1 
ATOM   4600 H HD21 . ASN   B 1 40  ? 49.159 -21.666 9.101   1.00 16.89 ?  40  ASN   B HD21 1 
ATOM   4601 H HD22 . ASN   B 1 40  ? 48.049 -22.658 9.042   1.00 16.89 ?  40  ASN   B HD22 1 
ATOM   4602 N N    . VAL   B 1 41  ? 44.299 -18.834 9.811   1.00 12.02 ?  41  VAL   B N    1 
ATOM   4603 C CA   . VAL   B 1 41  ? 43.843 -17.517 10.269  1.00 12.72 ?  41  VAL   B CA   1 
ATOM   4604 C C    . VAL   B 1 41  ? 44.998 -16.571 10.573  1.00 12.55 ?  41  VAL   B C    1 
ATOM   4605 O O    . VAL   B 1 41  ? 44.824 -15.349 10.503  1.00 12.70 ?  41  VAL   B O    1 
ATOM   4606 C CB   . VAL   B 1 41  ? 42.855 -17.595 11.453  1.00 13.85 ?  41  VAL   B CB   1 
ATOM   4607 C CG1  . VAL   B 1 41  ? 41.565 -18.294 11.043  1.00 14.55 ?  41  VAL   B CG1  1 
ATOM   4608 C CG2  . VAL   B 1 41  ? 43.488 -18.266 12.660  1.00 14.87 ?  41  VAL   B CG2  1 
ATOM   4609 H H    . VAL   B 1 41  ? 44.105 -19.485 10.332  1.00 14.39 ?  41  VAL   B H    1 
ATOM   4610 H HA   . VAL   B 1 41  ? 43.353 -17.116 9.539   1.00 15.23 ?  41  VAL   B HA   1 
ATOM   4611 H HB   . VAL   B 1 41  ? 42.621 -16.692 11.718  1.00 16.60 ?  41  VAL   B HB   1 
ATOM   4612 H HG11 . VAL   B 1 41  ? 40.959 -18.308 11.802  1.00 17.43 ?  41  VAL   B HG11 1 
ATOM   4613 H HG12 . VAL   B 1 41  ? 41.165 -17.810 10.307  1.00 17.43 ?  41  VAL   B HG12 1 
ATOM   4614 H HG13 . VAL   B 1 41  ? 41.773 -19.202 10.772  1.00 17.43 ?  41  VAL   B HG13 1 
ATOM   4615 H HG21 . VAL   B 1 41  ? 42.830 -18.320 13.373  1.00 17.82 ?  41  VAL   B HG21 1 
ATOM   4616 H HG22 . VAL   B 1 41  ? 43.773 -19.161 12.411  1.00 17.82 ?  41  VAL   B HG22 1 
ATOM   4617 H HG23 . VAL   B 1 41  ? 44.249 -17.745 12.952  1.00 17.82 ?  41  VAL   B HG23 1 
ATOM   4618 N N    . TYR   B 1 42  ? 46.168 -17.090 10.943  1.00 12.84 ?  42  TYR   B N    1 
ATOM   4619 C CA   . TYR   B 1 42  ? 47.320 -16.239 11.216  1.00 13.69 ?  42  TYR   B CA   1 
ATOM   4620 C C    . TYR   B 1 42  ? 48.286 -16.158 10.039  1.00 12.73 ?  42  TYR   B C    1 
ATOM   4621 O O    . TYR   B 1 42  ? 49.376 -15.593 10.179  1.00 13.87 ?  42  TYR   B O    1 
ATOM   4622 C CB   . TYR   B 1 42  ? 48.021 -16.645 12.518  1.00 15.43 ?  42  TYR   B CB   1 
ATOM   4623 C CG   . TYR   B 1 42  ? 47.420 -15.971 13.747  1.00 16.01 ?  42  TYR   B CG   1 
ATOM   4624 C CD1  . TYR   B 1 42  ? 47.662 -14.629 14.016  1.00 15.10 ?  42  TYR   B CD1  1 
ATOM   4625 C CD2  . TYR   B 1 42  ? 46.608 -16.671 14.625  1.00 17.85 ?  42  TYR   B CD2  1 
ATOM   4626 C CE1  . TYR   B 1 42  ? 47.114 -14.004 15.126  1.00 16.30 ?  42  TYR   B CE1  1 
ATOM   4627 C CE2  . TYR   B 1 42  ? 46.059 -16.057 15.740  1.00 18.03 ?  42  TYR   B CE2  1 
ATOM   4628 C CZ   . TYR   B 1 42  ? 46.310 -14.721 15.986  1.00 18.24 ?  42  TYR   B CZ   1 
ATOM   4629 O OH   . TYR   B 1 42  ? 45.772 -14.100 17.094  1.00 21.05 ?  42  TYR   B OH   1 
ATOM   4630 H H    . TYR   B 1 42  ? 46.317 -17.935 11.033  1.00 15.38 ?  42  TYR   B H    1 
ATOM   4631 H HA   . TYR   B 1 42  ? 46.987 -15.340 11.354  1.00 16.40 ?  42  TYR   B HA   1 
ATOM   4632 H HB2  . TYR   B 1 42  ? 47.943 -17.602 12.631  1.00 18.49 ?  42  TYR   B HB2  1 
ATOM   4633 H HB3  . TYR   B 1 42  ? 48.955 -16.389 12.461  1.00 18.49 ?  42  TYR   B HB3  1 
ATOM   4634 H HD1  . TYR   B 1 42  ? 48.207 -14.139 13.431  1.00 18.09 ?  42  TYR   B HD1  1 
ATOM   4635 H HD2  . TYR   B 1 42  ? 46.430 -17.571 14.459  1.00 21.40 ?  42  TYR   B HD2  1 
ATOM   4636 H HE1  . TYR   B 1 42  ? 47.297 -13.106 15.286  1.00 19.54 ?  42  TYR   B HE1  1 
ATOM   4637 H HE2  . TYR   B 1 42  ? 45.518 -16.544 16.314  1.00 21.62 ?  42  TYR   B HE2  1 
ATOM   4638 H HH   . TYR   B 1 42  ? 46.017 -13.301 17.109  1.00 25.24 ?  42  TYR   B HH   1 
ATOM   4639 N N    . LEU   B 1 43  ? 47.888 -16.661 8.872   1.00 11.91 ?  43  LEU   B N    1 
ATOM   4640 C CA   . LEU   B 1 43  ? 48.706 -16.592 7.668   1.00 11.47 ?  43  LEU   B CA   1 
ATOM   4641 C C    . LEU   B 1 43  ? 50.115 -17.107 7.929   1.00 11.87 ?  43  LEU   B C    1 
ATOM   4642 O O    . LEU   B 1 43  ? 51.099 -16.516 7.486   1.00 12.62 ?  43  LEU   B O    1 
ATOM   4643 C CB   . LEU   B 1 43  ? 48.730 -15.189 7.063   1.00 11.63 ?  43  LEU   B CB   1 
ATOM   4644 C CG   . LEU   B 1 43  ? 47.375 -14.575 6.698   1.00 11.97 ?  43  LEU   B CG   1 
ATOM   4645 C CD1  . LEU   B 1 43  ? 47.592 -13.171 6.133   1.00 13.09 ?  43  LEU   B CD1  1 
ATOM   4646 C CD2  . LEU   B 1 43  ? 46.607 -15.455 5.708   1.00 12.11 ?  43  LEU   B CD2  1 
ATOM   4647 H H    . LEU   B 1 43  ? 47.137 -17.058 8.749   1.00 14.27 ?  43  LEU   B H    1 
ATOM   4648 H HA   . LEU   B 1 43  ? 48.309 -17.177 7.001   1.00 13.74 ?  43  LEU   B HA   1 
ATOM   4649 H HB2  . LEU   B 1 43  ? 49.158 -14.591 7.693   1.00 13.93 ?  43  LEU   B HB2  1 
ATOM   4650 H HB3  . LEU   B 1 43  ? 49.257 -15.221 6.244   1.00 13.93 ?  43  LEU   B HB3  1 
ATOM   4651 H HG   . LEU   B 1 43  ? 46.842 -14.495 7.502   1.00 14.35 ?  43  LEU   B HG   1 
ATOM   4652 H HD11 . LEU   B 1 43  ? 46.732 -12.785 5.905   1.00 15.68 ?  43  LEU   B HD11 1 
ATOM   4653 H HD12 . LEU   B 1 43  ? 48.031 -12.625 6.807   1.00 15.68 ?  43  LEU   B HD12 1 
ATOM   4654 H HD13 . LEU   B 1 43  ? 48.150 -13.230 5.342   1.00 15.68 ?  43  LEU   B HD13 1 
ATOM   4655 H HD21 . LEU   B 1 43  ? 45.805 -14.984 5.430   1.00 14.51 ?  43  LEU   B HD21 1 
ATOM   4656 H HD22 . LEU   B 1 43  ? 47.172 -15.629 4.940   1.00 14.51 ?  43  LEU   B HD22 1 
ATOM   4657 H HD23 . LEU   B 1 43  ? 46.371 -16.286 6.144   1.00 14.51 ?  43  LEU   B HD23 1 
ATOM   4658 N N    . LYS   B 1 44  ? 50.206 -18.235 8.638   1.00 11.70 ?  44  LYS   B N    1 
ATOM   4659 C CA   . LYS   B 1 44  ? 51.471 -18.914 8.882   1.00 12.57 ?  44  LYS   B CA   1 
ATOM   4660 C C    . LYS   B 1 44  ? 51.589 -20.027 7.849   1.00 11.82 ?  44  LYS   B C    1 
ATOM   4661 O O    . LYS   B 1 44  ? 50.888 -21.042 7.930   1.00 12.95 ?  44  LYS   B O    1 
ATOM   4662 C CB   . LYS   B 1 44  ? 51.530 -19.433 10.316  1.00 14.02 ?  44  LYS   B CB   1 
ATOM   4663 C CG   . LYS   B 1 44  ? 51.726 -18.320 11.346  1.00 16.67 ?  44  LYS   B CG   1 
ATOM   4664 C CD   . LYS   B 1 44  ? 52.950 -17.466 10.988  1.00 19.51 ?  44  LYS   B CD   1 
ATOM   4665 C CE   . LYS   B 1 44  ? 53.368 -16.530 12.096  1.00 22.12 ?  44  LYS   B CE   1 
ATOM   4666 N NZ   . LYS   B 1 44  ? 54.571 -15.727 11.743  1.00 23.20 ?  44  LYS   B NZ   1 
ATOM   4667 H H    . LYS   B 1 44  ? 49.530 -18.624 8.998   1.00 14.01 ?  44  LYS   B H    1 
ATOM   4668 H HA   . LYS   B 1 44  ? 52.204 -18.300 8.726   1.00 15.07 ?  44  LYS   B HA   1 
ATOM   4669 H HB2  . LYS   B 1 44  ? 50.690 -19.881 10.521  1.00 16.80 ?  44  LYS   B HB2  1 
ATOM   4670 H HB3  . LYS   B 1 44  ? 52.265 -20.054 10.400  1.00 16.80 ?  44  LYS   B HB3  1 
ATOM   4671 H HG2  . LYS   B 1 44  ? 50.944 -17.749 11.364  1.00 19.98 ?  44  LYS   B HG2  1 
ATOM   4672 H HG3  . LYS   B 1 44  ? 51.877 -18.716 12.223  1.00 19.98 ?  44  LYS   B HG3  1 
ATOM   4673 H HD2  . LYS   B 1 44  ? 53.693 -18.060 10.777  1.00 23.39 ?  44  LYS   B HD2  1 
ATOM   4674 H HD3  . LYS   B 1 44  ? 52.733 -16.924 10.212  1.00 23.39 ?  44  LYS   B HD3  1 
ATOM   4675 H HE2  . LYS   B 1 44  ? 52.644 -15.911 12.258  1.00 26.51 ?  44  LYS   B HE2  1 
ATOM   4676 H HE3  . LYS   B 1 44  ? 53.564 -17.045 12.892  1.00 26.51 ?  44  LYS   B HE3  1 
ATOM   4677 H HZ1  . LYS   B 1 44  ? 54.777 -15.179 12.415  1.00 27.82 ?  44  LYS   B HZ1  1 
ATOM   4678 H HZ2  . LYS   B 1 44  ? 55.264 -16.263 11.585  1.00 27.82 ?  44  LYS   B HZ2  1 
ATOM   4679 H HZ3  . LYS   B 1 44  ? 54.411 -15.239 11.015  1.00 27.82 ?  44  LYS   B HZ3  1 
ATOM   4680 N N    . HIS   B 1 45  ? 52.449 -19.810 6.856   1.00 11.72 ?  45  HIS   B N    1 
ATOM   4681 C CA   . HIS   B 1 45  ? 52.472 -20.640 5.652   1.00 11.73 ?  45  HIS   B CA   1 
ATOM   4682 C C    . HIS   B 1 45  ? 53.490 -21.766 5.809   1.00 13.76 ?  45  HIS   B C    1 
ATOM   4683 O O    . HIS   B 1 45  ? 54.544 -21.791 5.180   1.00 15.88 ?  45  HIS   B O    1 
ATOM   4684 C CB   . HIS   B 1 45  ? 52.790 -19.780 4.440   1.00 11.46 ?  45  HIS   B CB   1 
ATOM   4685 C CG   . HIS   B 1 45  ? 51.919 -18.577 4.327   1.00 11.55 ?  45  HIS   B CG   1 
ATOM   4686 N ND1  . HIS   B 1 45  ? 50.543 -18.653 4.266   1.00 11.38 ?  45  HIS   B ND1  1 
ATOM   4687 C CD2  . HIS   B 1 45  ? 52.237 -17.262 4.285   1.00 12.13 ?  45  HIS   B CD2  1 
ATOM   4688 C CE1  . HIS   B 1 45  ? 50.055 -17.428 4.178   1.00 11.54 ?  45  HIS   B CE1  1 
ATOM   4689 N NE2  . HIS   B 1 45  ? 51.059 -16.568 4.182   1.00 11.94 ?  45  HIS   B NE2  1 
ATOM   4690 H H    . HIS   B 1 45  ? 53.036 -19.180 6.854   1.00 14.04 ?  45  HIS   B H    1 
ATOM   4691 H HA   . HIS   B 1 45  ? 51.597 -21.037 5.520   1.00 14.05 ?  45  HIS   B HA   1 
ATOM   4692 H HB2  . HIS   B 1 45  ? 53.709 -19.481 4.497   1.00 13.73 ?  45  HIS   B HB2  1 
ATOM   4693 H HB3  . HIS   B 1 45  ? 52.667 -20.315 3.635   1.00 13.73 ?  45  HIS   B HB3  1 
ATOM   4694 H HD2  . HIS   B 1 45  ? 53.092 -16.901 4.316   1.00 14.54 ?  45  HIS   B HD2  1 
ATOM   4695 H HE1  . HIS   B 1 45  ? 49.151 -17.211 4.107   1.00 13.83 ?  45  HIS   B HE1  1 
ATOM   4696 H HE2  . HIS   B 1 45  ? 50.983 -15.712 4.140   1.00 14.31 ?  45  HIS   B HE2  1 
ATOM   4697 N N    A GLY   B 1 46  ? 53.131 -22.731 6.651   0.48 15.23 ?  46  GLY   B N    1 
ATOM   4698 N N    B GLY   B 1 46  ? 53.142 -22.721 6.664   0.52 15.26 ?  46  GLY   B N    1 
ATOM   4699 C CA   A GLY   B 1 46  ? 54.058 -23.780 7.034   0.48 16.55 ?  46  GLY   B CA   1 
ATOM   4700 C CA   B GLY   B 1 46  ? 54.068 -23.780 7.006   0.52 16.52 ?  46  GLY   B CA   1 
ATOM   4701 C C    A GLY   B 1 46  ? 54.118 -24.988 6.119   0.48 17.70 ?  46  GLY   B C    1 
ATOM   4702 C C    B GLY   B 1 46  ? 54.109 -24.932 6.020   0.52 17.69 ?  46  GLY   B C    1 
ATOM   4703 O O    A GLY   B 1 46  ? 55.203 -25.411 5.708   0.48 19.98 ?  46  GLY   B O    1 
ATOM   4704 O O    B GLY   B 1 46  ? 55.157 -25.240 5.443   0.52 19.72 ?  46  GLY   B O    1 
ATOM   4705 H H    A GLY   B 1 46  ? 52.355 -22.788 7.023   0.48 18.25 ?  46  GLY   B H    1 
ATOM   4706 H H    B GLY   B 1 46  ? 52.378 -22.766 7.063   0.52 18.28 ?  46  GLY   B H    1 
ATOM   4707 H HA2  A GLY   B 1 46  ? 54.948 -23.399 7.089   0.48 19.83 ?  46  GLY   B HA2  1 
ATOM   4708 H HA2  B GLY   B 1 46  ? 54.960 -23.405 7.074   0.52 19.81 ?  46  GLY   B HA2  1 
ATOM   4709 H HA3  A GLY   B 1 46  ? 53.816 -24.098 7.917   0.48 19.83 ?  46  GLY   B HA3  1 
ATOM   4710 H HA3  B GLY   B 1 46  ? 53.826 -24.135 7.877   0.52 19.81 ?  46  GLY   B HA3  1 
ATOM   4711 N N    . GLY   B 1 47  ? 52.964 -25.576 5.807   1.00 17.15 ?  47  GLY   B N    1 
ATOM   4712 C CA   . GLY   B 1 47  ? 52.917 -26.843 5.105   1.00 15.30 ?  47  GLY   B CA   1 
ATOM   4713 C C    . GLY   B 1 47  ? 51.975 -26.830 3.917   1.00 13.00 ?  47  GLY   B C    1 
ATOM   4714 O O    . GLY   B 1 47  ? 51.315 -25.828 3.632   1.00 12.89 ?  47  GLY   B O    1 
ATOM   4715 H H    A GLY   B 1 47  ? 52.192 -25.265 6.016   0.48 20.56 ?  47  GLY   B H    1 
ATOM   4716 H H    B GLY   B 1 47  ? 52.197 -25.299 6.074   0.52 20.56 ?  47  GLY   B H    1 
ATOM   4717 H HA2  . GLY   B 1 47  ? 53.804 -27.074 4.785   1.00 18.33 ?  47  GLY   B HA2  1 
ATOM   4718 H HA3  . GLY   B 1 47  ? 52.627 -27.536 5.717   1.00 18.33 ?  47  GLY   B HA3  1 
ATOM   4719 N N    . GLY   B 1 48  ? 51.936 -27.967 3.227   1.00 12.03 ?  48  GLY   B N    1 
ATOM   4720 C CA   . GLY   B 1 48  ? 51.011 -28.115 2.120   1.00 11.52 ?  48  GLY   B CA   1 
ATOM   4721 C C    . GLY   B 1 48  ? 51.150 -27.008 1.101   1.00 11.21 ?  48  GLY   B C    1 
ATOM   4722 O O    . GLY   B 1 48  ? 52.252 -26.545 0.790   1.00 11.77 ?  48  GLY   B O    1 
ATOM   4723 H H    . GLY   B 1 48  ? 52.435 -28.646 3.370   1.00 14.41 ?  48  GLY   B H    1 
ATOM   4724 H HA2  . GLY   B 1 48  ? 51.169 -28.962 1.676   1.00 13.80 ?  48  GLY   B HA2  1 
ATOM   4725 H HA3  . GLY   B 1 48  ? 50.102 -28.105 2.454   1.00 13.80 ?  48  GLY   B HA3  1 
ATOM   4726 N N    . VAL   B 1 49  ? 50.005 -26.581 0.563   1.00 11.05 ?  49  VAL   B N    1 
ATOM   4727 C CA   . VAL   B 1 49  ? 49.986 -25.552 -0.476  1.00 11.19 ?  49  VAL   B CA   1 
ATOM   4728 C C    . VAL   B 1 49  ? 50.644 -24.265 0.014   1.00 10.36 ?  49  VAL   B C    1 
ATOM   4729 O O    . VAL   B 1 49  ? 51.432 -23.643 -0.706  1.00 11.18 ?  49  VAL   B O    1 
ATOM   4730 C CB   . VAL   B 1 49  ? 48.544 -25.304 -0.959  1.00 12.41 ?  49  VAL   B CB   1 
ATOM   4731 C CG1  . VAL   B 1 49  ? 48.474 -24.049 -1.818  1.00 12.84 ?  49  VAL   B CG1  1 
ATOM   4732 C CG2  . VAL   B 1 49  ? 48.015 -26.512 -1.729  1.00 13.58 ?  49  VAL   B CG2  1 
ATOM   4733 H H    . VAL   B 1 49  ? 49.225 -26.872 0.775   1.00 13.24 ?  49  VAL   B H    1 
ATOM   4734 H HA   . VAL   B 1 49  ? 50.495 -25.868 -1.240  1.00 13.40 ?  49  VAL   B HA   1 
ATOM   4735 H HB   . VAL   B 1 49  ? 47.972 -25.170 -0.190  1.00 14.86 ?  49  VAL   B HB   1 
ATOM   4736 H HG11 . VAL   B 1 49  ? 47.649 -24.065 -2.331  1.00 15.38 ?  49  VAL   B HG11 1 
ATOM   4737 H HG12 . VAL   B 1 49  ? 48.484 -23.268 -1.242  1.00 15.38 ?  49  VAL   B HG12 1 
ATOM   4738 H HG13 . VAL   B 1 49  ? 49.234 -24.031 -2.418  1.00 15.38 ?  49  VAL   B HG13 1 
ATOM   4739 H HG21 . VAL   B 1 49  ? 47.105 -26.330 -2.017  1.00 16.28 ?  49  VAL   B HG21 1 
ATOM   4740 H HG22 . VAL   B 1 49  ? 48.580 -26.662 -2.507  1.00 16.28 ?  49  VAL   B HG22 1 
ATOM   4741 H HG23 . VAL   B 1 49  ? 48.033 -27.287 -1.152  1.00 16.28 ?  49  VAL   B HG23 1 
ATOM   4742 N N    . ALA   B 1 50  ? 50.300 -23.823 1.223   1.00 10.40 ?  50  ALA   B N    1 
ATOM   4743 C CA   . ALA   B 1 50  ? 50.818 -22.545 1.703   1.00 10.34 ?  50  ALA   B CA   1 
ATOM   4744 C C    . ALA   B 1 50  ? 52.338 -22.571 1.808   1.00 10.61 ?  50  ALA   B C    1 
ATOM   4745 O O    . ALA   B 1 50  ? 53.015 -21.603 1.437   1.00 10.74 ?  50  ALA   B O    1 
ATOM   4746 C CB   . ALA   B 1 50  ? 50.193 -22.196 3.050   1.00 10.80 ?  50  ALA   B CB   1 
ATOM   4747 H H    . ALA   B 1 50  ? 49.789 -24.236 1.774   1.00 12.45 ?  50  ALA   B H    1 
ATOM   4748 H HA   . ALA   B 1 50  ? 50.584 -21.851 1.073   1.00 12.39 ?  50  ALA   B HA   1 
ATOM   4749 H HB1  . ALA   B 1 50  ? 50.549 -21.343 3.353   1.00 12.94 ?  50  ALA   B HB1  1 
ATOM   4750 H HB2  . ALA   B 1 50  ? 49.232 -22.133 2.945   1.00 12.94 ?  50  ALA   B HB2  1 
ATOM   4751 H HB3  . ALA   B 1 50  ? 50.412 -22.889 3.693   1.00 12.94 ?  50  ALA   B HB3  1 
ATOM   4752 N N    . GLY   B 1 51  ? 52.893 -23.661 2.332   1.00 10.88 ?  51  GLY   B N    1 
ATOM   4753 C CA   . GLY   B 1 51  ? 54.338 -23.759 2.406   1.00 11.49 ?  51  GLY   B CA   1 
ATOM   4754 C C    . GLY   B 1 51  ? 54.987 -23.712 1.040   1.00 11.60 ?  51  GLY   B C    1 
ATOM   4755 O O    . GLY   B 1 51  ? 56.025 -23.073 0.861   1.00 12.21 ?  51  GLY   B O    1 
ATOM   4756 H H    . GLY   B 1 51  ? 52.468 -24.340 2.640   1.00 13.03 ?  51  GLY   B H    1 
ATOM   4757 H HA2  . GLY   B 1 51  ? 54.689 -23.021 2.932   1.00 13.77 ?  51  GLY   B HA2  1 
ATOM   4758 H HA3  . GLY   B 1 51  ? 54.588 -24.590 2.837   1.00 13.77 ?  51  GLY   B HA3  1 
ATOM   4759 N N    . ALA   B 1 52  ? 54.381 -24.377 0.054   1.00 11.17 ?  52  ALA   B N    1 
ATOM   4760 C CA   . ALA   B 1 52  ? 54.941 -24.381 -1.293  1.00 11.52 ?  52  ALA   B CA   1 
ATOM   4761 C C    . ALA   B 1 52  ? 54.863 -23.002 -1.938  1.00 10.97 ?  52  ALA   B C    1 
ATOM   4762 O O    . ALA   B 1 52  ? 55.830 -22.545 -2.564  1.00 11.70 ?  52  ALA   B O    1 
ATOM   4763 C CB   . ALA   B 1 52  ? 54.231 -25.425 -2.154  1.00 12.36 ?  52  ALA   B CB   1 
ATOM   4764 H H    . ALA   B 1 52  ? 53.644 -24.818 0.137   1.00 13.38 ?  52  ALA   B H    1 
ATOM   4765 H HA   . ALA   B 1 52  ? 55.874 -24.629 -1.238  1.00 13.80 ?  52  ALA   B HA   1 
ATOM   4766 H HB1  . ALA   B 1 52  ? 54.618 -25.418 -3.044  1.00 14.81 ?  52  ALA   B HB1  1 
ATOM   4767 H HB2  . ALA   B 1 52  ? 54.353 -26.301 -1.750  1.00 14.81 ?  52  ALA   B HB2  1 
ATOM   4768 H HB3  . ALA   B 1 52  ? 53.287 -25.213 -2.201  1.00 14.81 ?  52  ALA   B HB3  1 
ATOM   4769 N N    . LEU   B 1 53  ? 53.719 -22.329 -1.813  1.00 10.62 ?  53  LEU   B N    1 
ATOM   4770 C CA   . LEU   B 1 53  ? 53.604 -20.992 -2.385  1.00 10.68 ?  53  LEU   B CA   1 
ATOM   4771 C C    . LEU   B 1 53  ? 54.604 -20.048 -1.735  1.00 10.77 ?  53  LEU   B C    1 
ATOM   4772 O O    . LEU   B 1 53  ? 55.306 -19.296 -2.419  1.00 11.49 ?  53  LEU   B O    1 
ATOM   4773 C CB   . LEU   B 1 53  ? 52.178 -20.464 -2.218  1.00 11.25 ?  53  LEU   B CB   1 
ATOM   4774 C CG   . LEU   B 1 53  ? 51.046 -21.183 -2.962  1.00 11.55 ?  53  LEU   B CG   1 
ATOM   4775 C CD1  . LEU   B 1 53  ? 49.716 -20.557 -2.625  1.00 12.69 ?  53  LEU   B CD1  1 
ATOM   4776 C CD2  . LEU   B 1 53  ? 51.261 -21.165 -4.465  1.00 13.14 ?  53  LEU   B CD2  1 
ATOM   4777 H H    . LEU   B 1 53  ? 53.017 -22.616 -1.415  1.00 12.71 ?  53  LEU   B H    1 
ATOM   4778 H HA   . LEU   B 1 53  ? 53.802 -21.033 -3.336  1.00 12.79 ?  53  LEU   B HA   1 
ATOM   4779 H HB2  . LEU   B 1 53  ? 51.958 -20.495 -1.276  1.00 13.47 ?  53  LEU   B HB2  1 
ATOM   4780 H HB3  . LEU   B 1 53  ? 52.165 -19.542 -2.518  1.00 13.47 ?  53  LEU   B HB3  1 
ATOM   4781 H HG   . LEU   B 1 53  ? 51.014 -22.109 -2.675  1.00 13.83 ?  53  LEU   B HG   1 
ATOM   4782 H HD11 . LEU   B 1 53  ? 49.012 -21.026 -3.101  1.00 15.21 ?  53  LEU   B HD11 1 
ATOM   4783 H HD12 . LEU   B 1 53  ? 49.566 -20.625 -1.667  1.00 15.21 ?  53  LEU   B HD12 1 
ATOM   4784 H HD13 . LEU   B 1 53  ? 49.728 -19.623 -2.889  1.00 15.21 ?  53  LEU   B HD13 1 
ATOM   4785 H HD21 . LEU   B 1 53  ? 50.543 -21.653 -4.895  1.00 15.74 ?  53  LEU   B HD21 1 
ATOM   4786 H HD22 . LEU   B 1 53  ? 51.263 -20.245 -4.772  1.00 15.74 ?  53  LEU   B HD22 1 
ATOM   4787 H HD23 . LEU   B 1 53  ? 52.112 -21.584 -4.668  1.00 15.74 ?  53  LEU   B HD23 1 
ATOM   4788 N N    . ASN   B 1 54  ? 54.692 -20.074 -0.409  1.00 10.63 ?  54  ASN   B N    1 
ATOM   4789 C CA   . ASN   B 1 54  ? 55.610 -19.167 0.264   1.00 11.23 ?  54  ASN   B CA   1 
ATOM   4790 C C    . ASN   B 1 54  ? 57.053 -19.444 -0.139  1.00 11.87 ?  54  ASN   B C    1 
ATOM   4791 O O    . ASN   B 1 54  ? 57.832 -18.508 -0.367  1.00 12.21 ?  54  ASN   B O    1 
ATOM   4792 C CB   . ASN   B 1 54  ? 55.454 -19.260 1.774   1.00 11.96 ?  54  ASN   B CB   1 
ATOM   4793 C CG   . ASN   B 1 54  ? 56.429 -18.349 2.488   1.00 12.11 ?  54  ASN   B CG   1 
ATOM   4794 O OD1  . ASN   B 1 54  ? 56.448 -17.140 2.243   1.00 12.48 ?  54  ASN   B OD1  1 
ATOM   4795 N ND2  . ASN   B 1 54  ? 57.275 -18.924 3.334   1.00 13.61 ?  54  ASN   B ND2  1 
ATOM   4796 H H    . ASN   B 1 54  ? 54.244 -20.591 0.106   1.00 12.74 ?  54  ASN   B H    1 
ATOM   4797 H HA   . ASN   B 1 54  ? 55.402 -18.258 -0.002  1.00 13.46 ?  54  ASN   B HA   1 
ATOM   4798 H HB2  . ASN   B 1 54  ? 54.554 -18.992 2.018   1.00 14.33 ?  54  ASN   B HB2  1 
ATOM   4799 H HB3  . ASN   B 1 54  ? 55.624 -20.170 2.058   1.00 14.33 ?  54  ASN   B HB3  1 
ATOM   4800 H HD21 . ASN   B 1 54  ? 57.849 -18.445 3.762   1.00 16.31 ?  54  ASN   B HD21 1 
ATOM   4801 H HD22 . ASN   B 1 54  ? 57.239 -19.773 3.472   1.00 16.31 ?  54  ASN   B HD22 1 
ATOM   4802 N N    . LYS   B 1 55  ? 57.436 -20.722 -0.215  1.00 12.21 ?  55  LYS   B N    1 
ATOM   4803 C CA   . LYS   B 1 55  ? 58.796 -21.060 -0.621  1.00 13.52 ?  55  LYS   B CA   1 
ATOM   4804 C C    . LYS   B 1 55  ? 59.100 -20.514 -2.009  1.00 12.76 ?  55  LYS   B C    1 
ATOM   4805 O O    . LYS   B 1 55  ? 60.198 -20.002 -2.257  1.00 13.30 ?  55  LYS   B O    1 
ATOM   4806 C CB   . LYS   B 1 55  ? 58.988 -22.578 -0.579  1.00 14.59 ?  55  LYS   B CB   1 
ATOM   4807 C CG   . LYS   B 1 55  ? 60.369 -23.042 -0.995  1.00 18.45 ?  55  LYS   B CG   1 
ATOM   4808 C CD   . LYS   B 1 55  ? 60.524 -24.541 -0.822  1.00 21.57 ?  55  LYS   B CD   1 
ATOM   4809 C CE   . LYS   B 1 55  ? 60.559 -24.941 0.650   1.00 24.28 ?  55  LYS   B CE   1 
ATOM   4810 N NZ   . LYS   B 1 55  ? 60.991 -26.348 0.831   1.00 25.80 ?  55  LYS   B NZ   1 
ATOM   4811 H H    . LYS   B 1 55  ? 56.932 -21.397 -0.039  1.00 14.63 ?  55  LYS   B H    1 
ATOM   4812 H HA   . LYS   B 1 55  ? 59.421 -20.661 0.004   1.00 16.20 ?  55  LYS   B HA   1 
ATOM   4813 H HB2  . LYS   B 1 55  ? 58.830 -22.880 0.329   1.00 17.49 ?  55  LYS   B HB2  1 
ATOM   4814 H HB3  . LYS   B 1 55  ? 58.344 -22.987 -1.177  1.00 17.49 ?  55  LYS   B HB3  1 
ATOM   4815 H HG2  . LYS   B 1 55  ? 60.513 -22.831 -1.931  1.00 22.11 ?  55  LYS   B HG2  1 
ATOM   4816 H HG3  . LYS   B 1 55  ? 61.036 -22.601 -0.445  1.00 22.11 ?  55  LYS   B HG3  1 
ATOM   4817 H HD2  . LYS   B 1 55  ? 59.775 -24.994 -1.239  1.00 25.86 ?  55  LYS   B HD2  1 
ATOM   4818 H HD3  . LYS   B 1 55  ? 61.358 -24.829 -1.230  1.00 25.86 ?  55  LYS   B HD3  1 
ATOM   4819 H HE2  . LYS   B 1 55  ? 61.184 -24.363 1.121   1.00 29.11 ?  55  LYS   B HE2  1 
ATOM   4820 H HE3  . LYS   B 1 55  ? 59.669 -24.843 1.026   1.00 29.11 ?  55  LYS   B HE3  1 
ATOM   4821 H HZ1  . LYS   B 1 55  ? 60.928 -26.577 1.689   1.00 30.94 ?  55  LYS   B HZ1  1 
ATOM   4822 H HZ2  . LYS   B 1 55  ? 60.474 -26.886 0.348   1.00 30.94 ?  55  LYS   B HZ2  1 
ATOM   4823 H HZ3  . LYS   B 1 55  ? 61.836 -26.442 0.568   1.00 30.94 ?  55  LYS   B HZ3  1 
ATOM   4824 N N    . ALA   B 1 56  ? 58.133 -20.601 -2.927  1.00 12.47 ?  56  ALA   B N    1 
ATOM   4825 C CA   . ALA   B 1 56  ? 58.349 -20.085 -4.273  1.00 12.85 ?  56  ALA   B CA   1 
ATOM   4826 C C    . ALA   B 1 56  ? 58.619 -18.588 -4.261  1.00 13.00 ?  56  ALA   B C    1 
ATOM   4827 O O    . ALA   B 1 56  ? 59.351 -18.083 -5.124  1.00 14.16 ?  56  ALA   B O    1 
ATOM   4828 C CB   . ALA   B 1 56  ? 57.152 -20.421 -5.156  1.00 13.88 ?  56  ALA   B CB   1 
ATOM   4829 H H    . ALA   B 1 56  ? 57.356 -20.949 -2.796  1.00 14.94 ?  56  ALA   B H    1 
ATOM   4830 H HA   . ALA   B 1 56  ? 59.128 -20.516 -4.650  1.00 15.39 ?  56  ALA   B HA   1 
ATOM   4831 H HB1  . ALA   B 1 56  ? 57.314 -20.074 -6.050  1.00 16.64 ?  56  ALA   B HB1  1 
ATOM   4832 H HB2  . ALA   B 1 56  ? 57.048 -21.384 -5.191  1.00 16.64 ?  56  ALA   B HB2  1 
ATOM   4833 H HB3  . ALA   B 1 56  ? 56.357 -20.013 -4.783  1.00 16.64 ?  56  ALA   B HB3  1 
ATOM   4834 N N    . THR   B 1 57  ? 58.048 -17.867 -3.294  1.00 12.78 ?  57  THR   B N    1 
ATOM   4835 C CA   . THR   B 1 57  ? 58.283 -16.436 -3.169  1.00 12.80 ?  57  THR   B CA   1 
ATOM   4836 C C    . THR   B 1 57  ? 59.536 -16.110 -2.365  1.00 13.60 ?  57  THR   B C    1 
ATOM   4837 O O    . THR   B 1 57  ? 59.779 -14.933 -2.063  1.00 14.11 ?  57  THR   B O    1 
ATOM   4838 C CB   . THR   B 1 57  ? 57.086 -15.715 -2.530  1.00 12.31 ?  57  THR   B CB   1 
ATOM   4839 O OG1  . THR   B 1 57  ? 57.064 -15.938 -1.113  1.00 12.35 ?  57  THR   B OG1  1 
ATOM   4840 C CG2  . THR   B 1 57  ? 55.770 -16.143 -3.160  1.00 12.37 ?  57  THR   B CG2  1 
ATOM   4841 H H    . THR   B 1 57  ? 57.509 -18.186 -2.697  1.00 15.31 ?  57  THR   B H    1 
ATOM   4842 H HA   . THR   B 1 57  ? 58.395 -16.068 -4.060  1.00 15.34 ?  57  THR   B HA   1 
ATOM   4843 H HB   . THR   B 1 57  ? 57.180 -14.764 -2.688  1.00 14.75 ?  57  THR   B HB   1 
ATOM   4844 H HG1  . THR   B 1 57  ? 56.997 -16.763 -0.955  1.00 14.79 ?  57  THR   B HG1  1 
ATOM   4845 H HG21 . THR   B 1 57  ? 55.054 -15.565 -2.866  1.00 14.82 ?  57  THR   B HG21 1 
ATOM   4846 H HG22 . THR   B 1 57  ? 55.836 -16.105 -4.127  1.00 14.82 ?  57  THR   B HG22 1 
ATOM   4847 H HG23 . THR   B 1 57  ? 55.561 -17.057 -2.900  1.00 14.82 ?  57  THR   B HG23 1 
ATOM   4848 N N    . ASN   B 1 58  ? 60.339 -17.112 -2.016  1.00 14.09 ?  58  ASN   B N    1 
ATOM   4849 C CA   . ASN   B 1 58  ? 61.536 -16.887 -1.215  1.00 16.33 ?  58  ASN   B CA   1 
ATOM   4850 C C    . ASN   B 1 58  ? 61.194 -16.185 0.099   1.00 14.58 ?  58  ASN   B C    1 
ATOM   4851 O O    . ASN   B 1 58  ? 61.927 -15.309 0.566   1.00 15.30 ?  58  ASN   B O    1 
ATOM   4852 C CB   . ASN   B 1 58  ? 62.609 -16.124 -2.002  1.00 22.61 ?  58  ASN   B CB   1 
ATOM   4853 C CG   . ASN   B 1 58  ? 63.980 -16.225 -1.361  1.00 29.68 ?  58  ASN   B CG   1 
ATOM   4854 O OD1  . ASN   B 1 58  ? 64.297 -17.215 -0.703  1.00 32.32 ?  58  ASN   B OD1  1 
ATOM   4855 N ND2  . ASN   B 1 58  ? 64.800 -15.196 -1.549  1.00 32.59 ?  58  ASN   B ND2  1 
ATOM   4856 H H    . ASN   B 1 58  ? 60.209 -17.936 -2.233  1.00 16.89 ?  58  ASN   B H    1 
ATOM   4857 H HA   . ASN   B 1 58  ? 61.912 -17.752 -0.995  1.00 19.57 ?  58  ASN   B HA   1 
ATOM   4858 H HB2  . ASN   B 1 58  ? 62.672 -16.494 -2.902  1.00 27.11 ?  58  ASN   B HB2  1 
ATOM   4859 H HB3  . ASN   B 1 58  ? 62.372 -15.188 -2.048  1.00 27.11 ?  58  ASN   B HB3  1 
ATOM   4860 H HD21 . ASN   B 1 58  ? 65.591 -15.206 -1.207  1.00 39.09 ?  58  ASN   B HD21 1 
ATOM   4861 H HD22 . ASN   B 1 58  ? 64.542 -14.519 -2.012  1.00 39.09 ?  58  ASN   B HD22 1 
ATOM   4862 N N    . ASN   B 1 59  ? 60.067 -16.575 0.699   1.00 13.77 ?  59  ASN   B N    1 
ATOM   4863 C CA   . ASN   B 1 59  ? 59.588 -16.109 2.002   1.00 13.81 ?  59  ASN   B CA   1 
ATOM   4864 C C    . ASN   B 1 59  ? 58.993 -14.701 1.951   1.00 13.32 ?  59  ASN   B C    1 
ATOM   4865 O O    . ASN   B 1 59  ? 58.565 -14.194 3.000   1.00 13.53 ?  59  ASN   B O    1 
ATOM   4866 C CB   . ASN   B 1 59  ? 60.660 -16.176 3.108   1.00 14.94 ?  59  ASN   B CB   1 
ATOM   4867 C CG   . ASN   B 1 59  ? 60.067 -16.350 4.490   1.00 16.55 ?  59  ASN   B CG   1 
ATOM   4868 O OD1  . ASN   B 1 59  ? 59.243 -17.237 4.714   1.00 16.78 ?  59  ASN   B OD1  1 
ATOM   4869 N ND2  . ASN   B 1 59  ? 60.487 -15.504 5.428   1.00 17.41 ?  59  ASN   B ND2  1 
ATOM   4870 H H    . ASN   B 1 59  ? 59.536 -17.152 0.345   1.00 16.50 ?  59  ASN   B H    1 
ATOM   4871 H HA   . ASN   B 1 59  ? 58.878 -16.706 2.275   1.00 16.55 ?  59  ASN   B HA   1 
ATOM   4872 H HB2  . ASN   B 1 59  ? 61.243 -16.934 2.947   1.00 17.90 ?  59  ASN   B HB2  1 
ATOM   4873 H HB3  . ASN   B 1 59  ? 61.172 -15.355 3.109   1.00 17.90 ?  59  ASN   B HB3  1 
ATOM   4874 H HD21 . ASN   B 1 59  ? 60.174 -15.555 6.229   1.00 20.87 ?  59  ASN   B HD21 1 
ATOM   4875 H HD22 . ASN   B 1 59  ? 61.063 -14.898 5.231   1.00 20.87 ?  59  ASN   B HD22 1 
ATOM   4876 N N    . ALA   B 1 60  ? 58.938 -14.049 0.784   1.00 13.12 ?  60  ALA   B N    1 
ATOM   4877 C CA   . ALA   B 1 60  ? 58.340 -12.720 0.723   1.00 13.42 ?  60  ALA   B CA   1 
ATOM   4878 C C    . ALA   B 1 60  ? 56.870 -12.749 1.121   1.00 12.39 ?  60  ALA   B C    1 
ATOM   4879 O O    . ALA   B 1 60  ? 56.370 -11.797 1.733   1.00 12.62 ?  60  ALA   B O    1 
ATOM   4880 C CB   . ALA   B 1 60  ? 58.509 -12.128 -0.677  1.00 13.88 ?  60  ALA   B CB   1 
ATOM   4881 H H    . ALA   B 1 60  ? 59.236 -14.356 0.036   1.00 15.72 ?  60  ALA   B H    1 
ATOM   4882 H HA   . ALA   B 1 60  ? 58.805 -12.145 1.346   1.00 16.08 ?  60  ALA   B HA   1 
ATOM   4883 H HB1  . ALA   B 1 60  ? 58.107 -11.248 -0.696  1.00 16.63 ?  60  ALA   B HB1  1 
ATOM   4884 H HB2  . ALA   B 1 60  ? 59.457 -12.065 -0.881  1.00 16.63 ?  60  ALA   B HB2  1 
ATOM   4885 H HB3  . ALA   B 1 60  ? 58.073 -12.709 -1.322  1.00 16.63 ?  60  ALA   B HB3  1 
ATOM   4886 N N    . MET   B 1 61  ? 56.164 -13.830 0.785   1.00 12.05 ?  61  MET   B N    1 
ATOM   4887 C CA   . MET   B 1 61  ? 54.768 -13.952 1.181   1.00 11.56 ?  61  MET   B CA   1 
ATOM   4888 C C    . MET   B 1 61  ? 54.630 -13.965 2.701   1.00 11.71 ?  61  MET   B C    1 
ATOM   4889 O O    . MET   B 1 61  ? 53.729 -13.325 3.255   1.00 11.61 ?  61  MET   B O    1 
ATOM   4890 C CB   . MET   B 1 61  ? 54.185 -15.218 0.547   1.00 11.64 ?  61  MET   B CB   1 
ATOM   4891 C CG   . MET   B 1 61  ? 52.743 -15.507 0.947   1.00 11.38 ?  61  MET   B CG   1 
ATOM   4892 S SD   . MET   B 1 61  ? 52.102 -17.013 0.187   1.00 11.74 ?  61  MET   B SD   1 
ATOM   4893 C CE   . MET   B 1 61  ? 51.848 -16.434 -1.488  1.00 12.73 ?  61  MET   B CE   1 
ATOM   4894 H H    . MET   B 1 61  ? 56.471 -14.502 0.336   1.00 14.44 ?  61  MET   B H    1 
ATOM   4895 H HA   . MET   B 1 61  ? 54.277 -13.198 0.824   1.00 13.85 ?  61  MET   B HA   1 
ATOM   4896 H HB2  . MET   B 1 61  ? 54.206 -15.127 -0.421  1.00 13.94 ?  61  MET   B HB2  1 
ATOM   4897 H HB3  . MET   B 1 61  ? 54.722 -15.981 0.812   1.00 13.94 ?  61  MET   B HB3  1 
ATOM   4898 H HG2  . MET   B 1 61  ? 52.691 -15.623 1.911   1.00 13.63 ?  61  MET   B HG2  1 
ATOM   4899 H HG3  . MET   B 1 61  ? 52.178 -14.768 0.673   1.00 13.63 ?  61  MET   B HG3  1 
ATOM   4900 H HE1  . MET   B 1 61  ? 51.475 -17.157 -2.017  1.00 15.25 ?  61  MET   B HE1  1 
ATOM   4901 H HE2  . MET   B 1 61  ? 51.236 -15.682 -1.477  1.00 15.25 ?  61  MET   B HE2  1 
ATOM   4902 H HE3  . MET   B 1 61  ? 52.702 -16.160 -1.862  1.00 15.25 ?  61  MET   B HE3  1 
ATOM   4903 N N    . GLN   B 1 62  ? 55.513 -14.685 3.399   1.00 11.71 ?  62  GLN   B N    1 
ATOM   4904 C CA   . GLN   B 1 62  ? 55.406 -14.752 4.854   1.00 12.14 ?  62  GLN   B CA   1 
ATOM   4905 C C    . GLN   B 1 62  ? 55.692 -13.401 5.496   1.00 12.12 ?  62  GLN   B C    1 
ATOM   4906 O O    . GLN   B 1 62  ? 55.004 -12.999 6.441   1.00 12.42 ?  62  GLN   B O    1 
ATOM   4907 C CB   . GLN   B 1 62  ? 56.354 -15.814 5.412   1.00 12.19 ?  62  GLN   B CB   1 
ATOM   4908 C CG   . GLN   B 1 62  ? 56.136 -16.081 6.889   1.00 12.60 ?  62  GLN   B CG   1 
ATOM   4909 C CD   . GLN   B 1 62  ? 54.761 -16.671 7.133   1.00 12.12 ?  62  GLN   B CD   1 
ATOM   4910 O OE1  . GLN   B 1 62  ? 54.498 -17.815 6.767   1.00 12.39 ?  62  GLN   B OE1  1 
ATOM   4911 N NE2  . GLN   B 1 62  ? 53.858 -15.878 7.702   1.00 12.71 ?  62  GLN   B NE2  1 
ATOM   4912 H H    . GLN   B 1 62  ? 56.165 -15.134 3.058   1.00 14.03 ?  62  GLN   B H    1 
ATOM   4913 H HA   . GLN   B 1 62  ? 54.500 -15.004 5.084   1.00 14.55 ?  62  GLN   B HA   1 
ATOM   4914 H HB2  . GLN   B 1 62  ? 56.218 -16.645 4.933   1.00 14.61 ?  62  GLN   B HB2  1 
ATOM   4915 H HB3  . GLN   B 1 62  ? 57.271 -15.511 5.294   1.00 14.61 ?  62  GLN   B HB3  1 
ATOM   4916 H HG2  . GLN   B 1 62  ? 56.799 -16.714 7.200   1.00 15.09 ?  62  GLN   B HG2  1 
ATOM   4917 H HG3  . GLN   B 1 62  ? 56.207 -15.248 7.383   1.00 15.09 ?  62  GLN   B HG3  1 
ATOM   4918 H HE21 . GLN   B 1 62  ? 54.076 -15.079 7.938   1.00 15.23 ?  62  GLN   B HE21 1 
ATOM   4919 H HE22 . GLN   B 1 62  ? 53.066 -16.171 7.856   1.00 15.23 ?  62  GLN   B HE22 1 
ATOM   4920 N N    . VAL   B 1 63  ? 56.703 -12.685 5.003   1.00 12.82 ?  63  VAL   B N    1 
ATOM   4921 C CA   . VAL   B 1 63  ? 57.014 -11.373 5.564   1.00 13.54 ?  63  VAL   B CA   1 
ATOM   4922 C C    . VAL   B 1 63  ? 55.827 -10.436 5.384   1.00 13.10 ?  63  VAL   B C    1 
ATOM   4923 O O    . VAL   B 1 63  ? 55.416 -9.730  6.315   1.00 13.76 ?  63  VAL   B O    1 
ATOM   4924 C CB   . VAL   B 1 63  ? 58.302 -10.818 4.936   1.00 14.78 ?  63  VAL   B CB   1 
ATOM   4925 C CG1  . VAL   B 1 63  ? 58.531 -9.381  5.372   1.00 15.38 ?  63  VAL   B CG1  1 
ATOM   4926 C CG2  . VAL   B 1 63  ? 59.491 -11.682 5.340   1.00 15.32 ?  63  VAL   B CG2  1 
ATOM   4927 H H    . VAL   B 1 63  ? 57.213 -12.931 4.350   1.00 15.36 ?  63  VAL   B H    1 
ATOM   4928 H HA   . VAL   B 1 63  ? 57.170 -11.473 6.513   1.00 16.23 ?  63  VAL   B HA   1 
ATOM   4929 H HB   . VAL   B 1 63  ? 58.233 -10.836 3.970   1.00 17.71 ?  63  VAL   B HB   1 
ATOM   4930 H HG11 . VAL   B 1 63  ? 59.451 -9.137  5.185   1.00 18.43 ?  63  VAL   B HG11 1 
ATOM   4931 H HG12 . VAL   B 1 63  ? 57.929 -8.802  4.883   1.00 18.43 ?  63  VAL   B HG12 1 
ATOM   4932 H HG13 . VAL   B 1 63  ? 58.361 -9.312  6.326   1.00 18.43 ?  63  VAL   B HG13 1 
ATOM   4933 H HG21 . VAL   B 1 63  ? 60.301 -11.315 4.954   1.00 18.35 ?  63  VAL   B HG21 1 
ATOM   4934 H HG22 . VAL   B 1 63  ? 59.562 -11.689 6.310   1.00 18.35 ?  63  VAL   B HG22 1 
ATOM   4935 H HG23 . VAL   B 1 63  ? 59.350 -12.586 5.017   1.00 18.35 ?  63  VAL   B HG23 1 
ATOM   4936 N N    . GLU   B 1 64  ? 55.254 -10.421 4.177   1.00 12.51 ?  64  GLU   B N    1 
ATOM   4937 C CA   . GLU   B 1 64  ? 54.090 -9.582  3.904   1.00 12.31 ?  64  GLU   B CA   1 
ATOM   4938 C C    . GLU   B 1 64  ? 52.909 -9.980  4.784   1.00 12.13 ?  64  GLU   B C    1 
ATOM   4939 O O    . GLU   B 1 64  ? 52.174 -9.119  5.292   1.00 12.87 ?  64  GLU   B O    1 
ATOM   4940 C CB   . GLU   B 1 64  ? 53.723 -9.732  2.425   1.00 12.66 ?  64  GLU   B CB   1 
ATOM   4941 C CG   . GLU   B 1 64  ? 52.472 -8.982  1.997   1.00 12.71 ?  64  GLU   B CG   1 
ATOM   4942 C CD   . GLU   B 1 64  ? 51.911 -9.483  0.678   1.00 13.58 ?  64  GLU   B CD   1 
ATOM   4943 O OE1  . GLU   B 1 64  ? 52.079 -10.688 0.361   1.00 14.14 ?  64  GLU   B OE1  1 
ATOM   4944 O OE2  . GLU   B 1 64  ? 51.282 -8.664  -0.035  1.00 14.40 -1 64  GLU   B OE2  1 
ATOM   4945 H H    . GLU   B 1 64  ? 55.526 -10.887 3.500   1.00 14.99 ?  64  GLU   B H    1 
ATOM   4946 H HA   . GLU   B 1 64  ? 54.309 -8.656  4.072   1.00 14.75 ?  64  GLU   B HA   1 
ATOM   4947 H HB2  . GLU   B 1 64  ? 54.457 -9.399  1.881   1.00 15.16 ?  64  GLU   B HB2  1 
ATOM   4948 H HB3  . GLU   B 1 64  ? 53.578 -10.671 2.231   1.00 15.16 ?  64  GLU   B HB3  1 
ATOM   4949 H HG2  . GLU   B 1 64  ? 51.781 -9.081  2.670   1.00 15.22 ?  64  GLU   B HG2  1 
ATOM   4950 H HG3  . GLU   B 1 64  ? 52.692 -8.039  1.893   1.00 15.22 ?  64  GLU   B HG3  1 
ATOM   4951 N N    . SER   B 1 65  ? 52.713 -11.288 4.963   1.00 11.82 ?  65  SER   B N    1 
ATOM   4952 C CA   . SER   B 1 65  ? 51.609 -11.797 5.766   1.00 12.14 ?  65  SER   B CA   1 
ATOM   4953 C C    . SER   B 1 65  ? 51.755 -11.409 7.232   1.00 12.35 ?  65  SER   B C    1 
ATOM   4954 O O    . SER   B 1 65  ? 50.765 -11.036 7.875   1.00 12.65 ?  65  SER   B O    1 
ATOM   4955 C CB   . SER   B 1 65  ? 51.525 -13.316 5.629   1.00 12.06 ?  65  SER   B CB   1 
ATOM   4956 O OG   . SER   B 1 65  ? 51.181 -13.709 4.310   1.00 12.20 ?  65  SER   B OG   1 
ATOM   4957 H H    . SER   B 1 65  ? 53.212 -11.908 4.628   1.00 14.17 ?  65  SER   B H    1 
ATOM   4958 H HA   . SER   B 1 65  ? 50.777 -11.419 5.437   1.00 14.55 ?  65  SER   B HA   1 
ATOM   4959 H HB2  . SER   B 1 65  ? 52.381 -13.699 5.861   1.00 14.45 ?  65  SER   B HB2  1 
ATOM   4960 H HB3  . SER   B 1 65  ? 50.841 -13.644 6.239   1.00 14.45 ?  65  SER   B HB3  1 
ATOM   4961 H HG   . SER   B 1 65  ? 51.768 -13.429 3.769   1.00 14.61 ?  65  SER   B HG   1 
ATOM   4962 N N    . ASP   B 1 66  ? 52.967 -11.514 7.788   1.00 12.64 ?  66  ASP   B N    1 
ATOM   4963 C CA   . ASP   B 1 66  ? 53.164 -11.135 9.185   1.00 12.93 ?  66  ASP   B CA   1 
ATOM   4964 C C    . ASP   B 1 66  ? 52.860 -9.659  9.396   1.00 13.22 ?  66  ASP   B C    1 
ATOM   4965 O O    . ASP   B 1 66  ? 52.280 -9.274  10.419  1.00 13.45 ?  66  ASP   B O    1 
ATOM   4966 C CB   . ASP   B 1 66  ? 54.592 -11.453 9.627   1.00 14.21 ?  66  ASP   B CB   1 
ATOM   4967 C CG   . ASP   B 1 66  ? 54.851 -12.943 9.787   1.00 15.70 ?  66  ASP   B CG   1 
ATOM   4968 O OD1  . ASP   B 1 66  ? 53.898 -13.754 9.726   1.00 16.22 ?  66  ASP   B OD1  1 
ATOM   4969 O OD2  . ASP   B 1 66  ? 56.032 -13.308 9.982   1.00 18.39 -1 66  ASP   B OD2  1 
ATOM   4970 H H    . ASP   B 1 66  ? 53.669 -11.801 7.387   1.00 15.14 ?  66  ASP   B H    1 
ATOM   4971 H HA   . ASP   B 1 66  ? 52.558 -11.641 9.744   1.00 15.49 ?  66  ASP   B HA   1 
ATOM   4972 H HB2  . ASP   B 1 66  ? 55.214 -11.117 8.964   1.00 17.03 ?  66  ASP   B HB2  1 
ATOM   4973 H HB3  . ASP   B 1 66  ? 54.761 -11.026 10.485  1.00 17.03 ?  66  ASP   B HB3  1 
ATOM   4974 N N    . ASP   B 1 67  ? 53.236 -8.811  8.436   1.00 12.84 ?  67  ASP   B N    1 
ATOM   4975 C CA   . ASP   B 1 67  ? 52.891 -7.399  8.542   1.00 13.52 ?  67  ASP   B CA   1 
ATOM   4976 C C    . ASP   B 1 67  ? 51.381 -7.187  8.462   1.00 13.45 ?  67  ASP   B C    1 
ATOM   4977 O O    . ASP   B 1 67  ? 50.823 -6.377  9.214   1.00 14.05 ?  67  ASP   B O    1 
ATOM   4978 C CB   . ASP   B 1 67  ? 53.610 -6.604  7.460   1.00 14.85 ?  67  ASP   B CB   1 
ATOM   4979 C CG   . ASP   B 1 67  ? 53.177 -5.164  7.436   1.00 15.93 ?  67  ASP   B CG   1 
ATOM   4980 O OD1  . ASP   B 1 67  ? 53.680 -4.361  8.258   1.00 16.36 ?  67  ASP   B OD1  1 
ATOM   4981 O OD2  . ASP   B 1 67  ? 52.304 -4.864  6.604   1.00 16.76 -1 67  ASP   B OD2  1 
ATOM   4982 H H    . ASP   B 1 67  ? 53.692 -9.023  7.734   1.00 15.38 ?  67  ASP   B H    1 
ATOM   4983 H HA   . ASP   B 1 67  ? 53.199 -7.066  9.401   1.00 16.20 ?  67  ASP   B HA   1 
ATOM   4984 H HB2  . ASP   B 1 67  ? 54.565 -6.625  7.624   1.00 17.79 ?  67  ASP   B HB2  1 
ATOM   4985 H HB3  . ASP   B 1 67  ? 53.416 -7.004  6.592   1.00 17.79 ?  67  ASP   B HB3  1 
ATOM   4986 N N    . TYR   B 1 68  ? 50.699 -7.913  7.570   1.00 12.86 ?  68  TYR   B N    1 
ATOM   4987 C CA   . TYR   B 1 68  ? 49.242 -7.820  7.493   1.00 13.63 ?  68  TYR   B CA   1 
ATOM   4988 C C    . TYR   B 1 68  ? 48.600 -8.172  8.831   1.00 13.24 ?  68  TYR   B C    1 
ATOM   4989 O O    . TYR   B 1 68  ? 47.672 -7.491  9.283   1.00 13.95 ?  68  TYR   B O    1 
ATOM   4990 C CB   . TYR   B 1 68  ? 48.704 -8.727  6.380   1.00 14.57 ?  68  TYR   B CB   1 
ATOM   4991 C CG   . TYR   B 1 68  ? 47.196 -8.884  6.440   1.00 15.92 ?  68  TYR   B CG   1 
ATOM   4992 C CD1  . TYR   B 1 68  ? 46.607 -9.839  7.266   1.00 16.71 ?  68  TYR   B CD1  1 
ATOM   4993 C CD2  . TYR   B 1 68  ? 46.361 -8.055  5.709   1.00 16.97 ?  68  TYR   B CD2  1 
ATOM   4994 C CE1  . TYR   B 1 68  ? 45.242 -9.966  7.358   1.00 17.73 ?  68  TYR   B CE1  1 
ATOM   4995 C CE2  . TYR   B 1 68  ? 44.976 -8.188  5.785   1.00 17.40 ?  68  TYR   B CE2  1 
ATOM   4996 C CZ   . TYR   B 1 68  ? 44.437 -9.140  6.616   1.00 17.48 ?  68  TYR   B CZ   1 
ATOM   4997 O OH   . TYR   B 1 68  ? 43.072 -9.274  6.711   1.00 18.84 ?  68  TYR   B OH   1 
ATOM   4998 H H    . TYR   B 1 68  ? 51.055 -8.464  7.013   1.00 15.40 ?  68  TYR   B H    1 
ATOM   4999 H HA   . TYR   B 1 68  ? 49.004 -6.906  7.283   1.00 16.33 ?  68  TYR   B HA   1 
ATOM   5000 H HB2  . TYR   B 1 68  ? 48.928 -8.338  5.524   1.00 17.46 ?  68  TYR   B HB2  1 
ATOM   5001 H HB3  . TYR   B 1 68  ? 49.101 -9.605  6.468   1.00 17.46 ?  68  TYR   B HB3  1 
ATOM   5002 H HD1  . TYR   B 1 68  ? 47.149 -10.400 7.776   1.00 20.03 ?  68  TYR   B HD1  1 
ATOM   5003 H HD2  . TYR   B 1 68  ? 46.729 -7.406  5.160   1.00 20.34 ?  68  TYR   B HD2  1 
ATOM   5004 H HE1  . TYR   B 1 68  ? 44.862 -10.621 7.909   1.00 21.26 ?  68  TYR   B HE1  1 
ATOM   5005 H HE2  . TYR   B 1 68  ? 44.418 -7.629  5.293   1.00 20.86 ?  68  TYR   B HE2  1 
ATOM   5006 H HH   . TYR   B 1 68  ? 42.681 -8.723  6.208   1.00 22.59 ?  68  TYR   B HH   1 
ATOM   5007 N N    . ILE   B 1 69  ? 49.072 -9.248  9.469   1.00 13.46 ?  69  ILE   B N    1 
ATOM   5008 C CA   . ILE   B 1 69  ? 48.517 -9.682  10.750  1.00 14.04 ?  69  ILE   B CA   1 
ATOM   5009 C C    . ILE   B 1 69  ? 48.771 -8.642  11.833  1.00 13.77 ?  69  ILE   B C    1 
ATOM   5010 O O    . ILE   B 1 69  ? 47.895 -8.365  12.662  1.00 14.31 ?  69  ILE   B O    1 
ATOM   5011 C CB   . ILE   B 1 69  ? 49.092 -11.060 11.134  1.00 15.01 ?  69  ILE   B CB   1 
ATOM   5012 C CG1  . ILE   B 1 69  ? 48.558 -12.154 10.203  1.00 15.42 ?  69  ILE   B CG1  1 
ATOM   5013 C CG2  . ILE   B 1 69  ? 48.794 -11.389 12.590  1.00 16.26 ?  69  ILE   B CG2  1 
ATOM   5014 C CD1  . ILE   B 1 69  ? 47.085 -12.464 10.378  1.00 15.82 ?  69  ILE   B CD1  1 
ATOM   5015 H H    . ILE   B 1 69  ? 49.712 -9.742  9.184   1.00 16.13 ?  69  ILE   B H    1 
ATOM   5016 H HA   . ILE   B 1 69  ? 47.557 -9.777  10.659  1.00 16.82 ?  69  ILE   B HA   1 
ATOM   5017 H HB   . ILE   B 1 69  ? 50.055 -11.024 11.028  1.00 17.99 ?  69  ILE   B HB   1 
ATOM   5018 H HG12 . ILE   B 1 69  ? 48.693 -11.873 9.284   1.00 18.48 ?  69  ILE   B HG12 1 
ATOM   5019 H HG13 . ILE   B 1 69  ? 49.053 -12.973 10.368  1.00 18.48 ?  69  ILE   B HG13 1 
ATOM   5020 H HG21 . ILE   B 1 69  ? 48.932 -12.338 12.729  1.00 19.49 ?  69  ILE   B HG21 1 
ATOM   5021 H HG22 . ILE   B 1 69  ? 49.395 -10.883 13.158  1.00 19.49 ?  69  ILE   B HG22 1 
ATOM   5022 H HG23 . ILE   B 1 69  ? 47.874 -11.156 12.783  1.00 19.49 ?  69  ILE   B HG23 1 
ATOM   5023 H HD11 . ILE   B 1 69  ? 46.834 -13.154 9.746   1.00 18.96 ?  69  ILE   B HD11 1 
ATOM   5024 H HD12 . ILE   B 1 69  ? 46.931 -12.777 11.284  1.00 18.96 ?  69  ILE   B HD12 1 
ATOM   5025 H HD13 . ILE   B 1 69  ? 46.567 -11.662 10.212  1.00 18.96 ?  69  ILE   B HD13 1 
ATOM   5026 N N    . ALA   B 1 70  ? 49.970 -8.061  11.861  1.00 13.39 ?  70  ALA   B N    1 
ATOM   5027 C CA   . ALA   B 1 70  ? 50.254 -7.028  12.853  1.00 13.18 ?  70  ALA   B CA   1 
ATOM   5028 C C    . ALA   B 1 70  ? 49.263 -5.878  12.743  1.00 13.50 ?  70  ALA   B C    1 
ATOM   5029 O O    . ALA   B 1 70  ? 48.828 -5.326  13.759  1.00 13.96 ?  70  ALA   B O    1 
ATOM   5030 C CB   . ALA   B 1 70  ? 51.689 -6.527  12.692  1.00 13.66 ?  70  ALA   B CB   1 
ATOM   5031 H H    . ALA   B 1 70  ? 50.617 -8.244  11.332  1.00 16.05 ?  70  ALA   B H    1 
ATOM   5032 H HA   . ALA   B 1 70  ? 50.170 -7.407  13.742  1.00 15.79 ?  70  ALA   B HA   1 
ATOM   5033 H HB1  . ALA   B 1 70  ? 51.872 -5.860  13.372  1.00 16.37 ?  70  ALA   B HB1  1 
ATOM   5034 H HB2  . ALA   B 1 70  ? 52.299 -7.278  12.797  1.00 16.37 ?  70  ALA   B HB2  1 
ATOM   5035 H HB3  . ALA   B 1 70  ? 51.794 -6.140  11.810  1.00 16.37 ?  70  ALA   B HB3  1 
ATOM   5036 N N    . THR   B 1 71  ? 48.888 -5.512  11.520  1.00 14.01 ?  71  THR   B N    1 
ATOM   5037 C CA   . THR   B 1 71  ? 48.005 -4.371  11.307  1.00 14.95 ?  71  THR   B CA   1 
ATOM   5038 C C    . THR   B 1 71  ? 46.536 -4.728  11.505  1.00 15.60 ?  71  THR   B C    1 
ATOM   5039 O O    . THR   B 1 71  ? 45.761 -3.908  12.016  1.00 16.66 ?  71  THR   B O    1 
ATOM   5040 C CB   . THR   B 1 71  ? 48.237 -3.803  9.905   1.00 16.91 ?  71  THR   B CB   1 
ATOM   5041 O OG1  . THR   B 1 71  ? 49.565 -3.271  9.821   1.00 18.78 ?  71  THR   B OG1  1 
ATOM   5042 C CG2  . THR   B 1 71  ? 47.230 -2.702  9.576   1.00 17.86 ?  71  THR   B CG2  1 
ATOM   5043 H H    . THR   B 1 71  ? 49.129 -5.909  10.797  1.00 16.79 ?  71  THR   B H    1 
ATOM   5044 H HA   . THR   B 1 71  ? 48.228 -3.677  11.945  1.00 17.92 ?  71  THR   B HA   1 
ATOM   5045 H HB   . THR   B 1 71  ? 48.135 -4.512  9.249   1.00 20.27 ?  71  THR   B HB   1 
ATOM   5046 H HG1  . THR   B 1 71  ? 49.701 -2.956  9.052   1.00 22.51 ?  71  THR   B HG1  1 
ATOM   5047 H HG21 . THR   B 1 71  ? 47.538 -2.195  8.806   1.00 21.40 ?  71  THR   B HG21 1 
ATOM   5048 H HG22 . THR   B 1 71  ? 46.366 -3.088  9.372   1.00 21.40 ?  71  THR   B HG22 1 
ATOM   5049 H HG23 . THR   B 1 71  ? 47.142 -2.099  10.331  1.00 21.40 ?  71  THR   B HG23 1 
ATOM   5050 N N    . ASN   B 1 72  ? 46.136 -5.941  11.114  1.00 15.19 ?  72  ASN   B N    1 
ATOM   5051 C CA   . ASN   B 1 72  ? 44.731 -6.295  10.996  1.00 15.92 ?  72  ASN   B CA   1 
ATOM   5052 C C    . ASN   B 1 72  ? 44.259 -7.400  11.931  1.00 16.31 ?  72  ASN   B C    1 
ATOM   5053 O O    . ASN   B 1 72  ? 43.043 -7.559  12.094  1.00 17.34 ?  72  ASN   B O    1 
ATOM   5054 C CB   . ASN   B 1 72  ? 44.414 -6.709  9.550   1.00 16.61 ?  72  ASN   B CB   1 
ATOM   5055 C CG   . ASN   B 1 72  ? 44.705 -5.601  8.563   1.00 17.64 ?  72  ASN   B CG   1 
ATOM   5056 O OD1  . ASN   B 1 72  ? 45.709 -5.627  7.849   1.00 18.95 ?  72  ASN   B OD1  1 
ATOM   5057 N ND2  . ASN   B 1 72  ? 43.849 -4.597  8.548   1.00 18.88 ?  72  ASN   B ND2  1 
ATOM   5058 H H    . ASN   B 1 72  ? 46.675 -6.584  10.909  1.00 18.20 ?  72  ASN   B H    1 
ATOM   5059 H HA   . ASN   B 1 72  ? 44.204 -5.511  11.194  1.00 19.08 ?  72  ASN   B HA   1 
ATOM   5060 H HB2  . ASN   B 1 72  ? 44.959 -7.476  9.312   1.00 19.91 ?  72  ASN   B HB2  1 
ATOM   5061 H HB3  . ASN   B 1 72  ? 43.475 -6.933  9.485   1.00 19.91 ?  72  ASN   B HB3  1 
ATOM   5062 H HD21 . ASN   B 1 72  ? 43.966 -3.938  8.006   1.00 22.63 ?  72  ASN   B HD21 1 
ATOM   5063 H HD22 . ASN   B 1 72  ? 43.161 -4.607  9.066   1.00 22.63 ?  72  ASN   B HD22 1 
ATOM   5064 N N    . GLY   B 1 73  ? 45.161 -8.166  12.539  1.00 15.63 ?  73  GLY   B N    1 
ATOM   5065 C CA   . GLY   B 1 73  ? 44.761 -9.306  13.327  1.00 15.28 ?  73  GLY   B CA   1 
ATOM   5066 C C    . GLY   B 1 73  ? 44.383 -10.483 12.452  1.00 14.18 ?  73  GLY   B C    1 
ATOM   5067 O O    . GLY   B 1 73  ? 44.359 -10.387 11.222  1.00 13.73 ?  73  GLY   B O    1 
ATOM   5068 H H    . GLY   B 1 73  ? 46.016 -8.043  12.507  1.00 18.73 ?  73  GLY   B H    1 
ATOM   5069 H HA2  . GLY   B 1 73  ? 45.491 -9.571  13.912  1.00 18.31 ?  73  GLY   B HA2  1 
ATOM   5070 H HA3  . GLY   B 1 73  ? 43.998 -9.069  13.877  1.00 18.31 ?  73  GLY   B HA3  1 
ATOM   5071 N N    . PRO   B 1 74  ? 44.075 -11.614 13.082  1.00 14.48 ?  74  PRO   B N    1 
ATOM   5072 C CA   . PRO   B 1 74  ? 43.818 -12.840 12.324  1.00 13.71 ?  74  PRO   B CA   1 
ATOM   5073 C C    . PRO   B 1 74  ? 42.520 -12.771 11.533  1.00 13.13 ?  74  PRO   B C    1 
ATOM   5074 O O    . PRO   B 1 74  ? 41.583 -12.030 11.857  1.00 14.20 ?  74  PRO   B O    1 
ATOM   5075 C CB   . PRO   B 1 74  ? 43.737 -13.915 13.416  1.00 14.69 ?  74  PRO   B CB   1 
ATOM   5076 C CG   . PRO   B 1 74  ? 43.298 -13.168 14.638  1.00 16.14 ?  74  PRO   B CG   1 
ATOM   5077 C CD   . PRO   B 1 74  ? 43.987 -11.836 14.536  1.00 15.75 ?  74  PRO   B CD   1 
ATOM   5078 H HA   . PRO   B 1 74  ? 44.559 -13.034 11.729  1.00 16.43 ?  74  PRO   B HA   1 
ATOM   5079 H HB2  . PRO   B 1 74  ? 43.079 -14.587 13.166  1.00 17.61 ?  74  PRO   B HB2  1 
ATOM   5080 H HB3  . PRO   B 1 74  ? 44.607 -14.319 13.549  1.00 17.61 ?  74  PRO   B HB3  1 
ATOM   5081 H HG2  . PRO   B 1 74  ? 42.332 -13.061 14.630  1.00 19.35 ?  74  PRO   B HG2  1 
ATOM   5082 H HG3  . PRO   B 1 74  ? 43.582 -13.647 15.434  1.00 19.35 ?  74  PRO   B HG3  1 
ATOM   5083 H HD2  . PRO   B 1 74  ? 43.448 -11.148 14.962  1.00 18.88 ?  74  PRO   B HD2  1 
ATOM   5084 H HD3  . PRO   B 1 74  ? 44.873 -11.886 14.925  1.00 18.88 ?  74  PRO   B HD3  1 
ATOM   5085 N N    . LEU   B 1 75  ? 42.484 -13.577 10.473  1.00 12.37 ?  75  LEU   B N    1 
ATOM   5086 C CA   . LEU   B 1 75  ? 41.269 -13.797 9.710   1.00 12.50 ?  75  LEU   B CA   1 
ATOM   5087 C C    . LEU   B 1 75  ? 40.306 -14.663 10.518  1.00 12.90 ?  75  LEU   B C    1 
ATOM   5088 O O    . LEU   B 1 75  ? 40.649 -15.195 11.574  1.00 14.05 ?  75  LEU   B O    1 
ATOM   5089 C CB   . LEU   B 1 75  ? 41.597 -14.511 8.397   1.00 12.50 ?  75  LEU   B CB   1 
ATOM   5090 C CG   . LEU   B 1 75  ? 42.449 -13.758 7.368   1.00 14.23 ?  75  LEU   B CG   1 
ATOM   5091 C CD1  . LEU   B 1 75  ? 42.627 -14.595 6.106   1.00 15.44 ?  75  LEU   B CD1  1 
ATOM   5092 C CD2  . LEU   B 1 75  ? 41.867 -12.418 7.025   1.00 17.34 ?  75  LEU   B CD2  1 
ATOM   5093 H H    . LEU   B 1 75  ? 43.160 -14.016 10.173  1.00 14.82 ?  75  LEU   B H    1 
ATOM   5094 H HA   . LEU   B 1 75  ? 40.838 -12.954 9.513   1.00 14.97 ?  75  LEU   B HA   1 
ATOM   5095 H HB2  . LEU   B 1 75  ? 42.072 -15.332 8.612   1.00 14.98 ?  75  LEU   B HB2  1 
ATOM   5096 H HB3  . LEU   B 1 75  ? 40.762 -14.739 7.959   1.00 14.98 ?  75  LEU   B HB3  1 
ATOM   5097 H HG   . LEU   B 1 75  ? 43.331 -13.615 7.744   1.00 17.05 ?  75  LEU   B HG   1 
ATOM   5098 H HD11 . LEU   B 1 75  ? 43.173 -14.101 5.472   1.00 18.51 ?  75  LEU   B HD11 1 
ATOM   5099 H HD12 . LEU   B 1 75  ? 43.065 -15.431 6.335   1.00 18.51 ?  75  LEU   B HD12 1 
ATOM   5100 H HD13 . LEU   B 1 75  ? 41.756 -14.776 5.718   1.00 18.51 ?  75  LEU   B HD13 1 
ATOM   5101 H HD21 . LEU   B 1 75  ? 42.387 -12.023 6.309   1.00 20.79 ?  75  LEU   B HD21 1 
ATOM   5102 H HD22 . LEU   B 1 75  ? 40.948 -12.538 6.744   1.00 20.79 ?  75  LEU   B HD22 1 
ATOM   5103 H HD23 . LEU   B 1 75  ? 41.903 -11.851 7.813   1.00 20.79 ?  75  LEU   B HD23 1 
ATOM   5104 N N    . LYS   B 1 76  ? 39.079 -14.784 10.009  1.00 13.74 ?  76  LYS   B N    1 
ATOM   5105 C CA   . LYS   B 1 76  ? 38.101 -15.753 10.490  1.00 15.30 ?  76  LYS   B CA   1 
ATOM   5106 C C    . LYS   B 1 76  ? 38.171 -17.013 9.628   1.00 13.33 ?  76  LYS   B C    1 
ATOM   5107 O O    . LYS   B 1 76  ? 38.428 -16.939 8.428   1.00 12.93 ?  76  LYS   B O    1 
ATOM   5108 C CB   . LYS   B 1 76  ? 36.678 -15.187 10.354  1.00 18.12 ?  76  LYS   B CB   1 
ATOM   5109 C CG   . LYS   B 1 76  ? 36.418 -13.792 10.945  1.00 20.27 ?  76  LYS   B CG   1 
ATOM   5110 C CD   . LYS   B 1 76  ? 35.018 -13.267 10.568  1.00 21.85 ?  76  LYS   B CD   1 
ATOM   5111 C CE   . LYS   B 1 76  ? 34.767 -11.870 11.111  1.00 24.06 ?  76  LYS   B CE   1 
ATOM   5112 N NZ   . LYS   B 1 76  ? 33.471 -11.302 10.641  1.00 24.83 ?  76  LYS   B NZ   1 
ATOM   5113 H H    . LYS   B 1 76  ? 38.780 -14.302 9.363   1.00 16.47 ?  76  LYS   B H    1 
ATOM   5114 H HA   . LYS   B 1 76  ? 38.272 -15.986 11.420  1.00 18.34 ?  76  LYS   B HA   1 
ATOM   5115 H HB2  . LYS   B 1 76  ? 36.463 -15.140 9.409   1.00 21.72 ?  76  LYS   B HB2  1 
ATOM   5116 H HB3  . LYS   B 1 76  ? 36.065 -15.798 10.790  1.00 21.72 ?  76  LYS   B HB3  1 
ATOM   5117 H HG2  . LYS   B 1 76  ? 36.478 -13.838 11.911  1.00 24.31 ?  76  LYS   B HG2  1 
ATOM   5118 H HG3  . LYS   B 1 76  ? 37.080 -13.171 10.598  1.00 24.31 ?  76  LYS   B HG3  1 
ATOM   5119 H HD2  . LYS   B 1 76  ? 34.941 -13.235 9.601   1.00 26.19 ?  76  LYS   B HD2  1 
ATOM   5120 H HD3  . LYS   B 1 76  ? 34.347 -13.862 10.937  1.00 26.19 ?  76  LYS   B HD3  1 
ATOM   5121 H HE2  . LYS   B 1 76  ? 34.747 -11.906 12.080  1.00 28.84 ?  76  LYS   B HE2  1 
ATOM   5122 H HE3  . LYS   B 1 76  ? 35.479 -11.282 10.815  1.00 28.84 ?  76  LYS   B HE3  1 
ATOM   5123 H HZ1  . LYS   B 1 76  ? 33.356 -10.484 10.978  1.00 29.78 ?  76  LYS   B HZ1  1 
ATOM   5124 H HZ2  . LYS   B 1 76  ? 33.463 -11.249 9.752   1.00 29.78 ?  76  LYS   B HZ2  1 
ATOM   5125 H HZ3  . LYS   B 1 76  ? 32.796 -11.818 10.906  1.00 29.78 ?  76  LYS   B HZ3  1 
ATOM   5126 N N    . VAL   B 1 77  ? 37.914 -18.177 10.238  1.00 13.66 ?  77  VAL   B N    1 
ATOM   5127 C CA   . VAL   B 1 77  ? 37.706 -19.377 9.430   1.00 13.68 ?  77  VAL   B CA   1 
ATOM   5128 C C    . VAL   B 1 77  ? 36.511 -19.132 8.519   1.00 12.70 ?  77  VAL   B C    1 
ATOM   5129 O O    . VAL   B 1 77  ? 35.449 -18.681 8.969   1.00 12.91 ?  77  VAL   B O    1 
ATOM   5130 C CB   . VAL   B 1 77  ? 37.509 -20.621 10.312  1.00 14.67 ?  77  VAL   B CB   1 
ATOM   5131 C CG1  . VAL   B 1 77  ? 37.199 -21.835 9.444   1.00 15.29 ?  77  VAL   B CG1  1 
ATOM   5132 C CG2  . VAL   B 1 77  ? 38.746 -20.877 11.165  1.00 15.70 ?  77  VAL   B CG2  1 
ATOM   5133 H H    . VAL   B 1 77  ? 37.858 -18.293 11.087  1.00 16.37 ?  77  VAL   B H    1 
ATOM   5134 H HA   . VAL   B 1 77  ? 38.482 -19.521 8.872   1.00 16.40 ?  77  VAL   B HA   1 
ATOM   5135 H HB   . VAL   B 1 77  ? 36.757 -20.471 10.907  1.00 17.58 ?  77  VAL   B HB   1 
ATOM   5136 H HG11 . VAL   B 1 77  ? 37.271 -22.634 9.987   1.00 18.33 ?  77  VAL   B HG11 1 
ATOM   5137 H HG12 . VAL   B 1 77  ? 36.295 -21.754 9.096   1.00 18.33 ?  77  VAL   B HG12 1 
ATOM   5138 H HG13 . VAL   B 1 77  ? 37.834 -21.870 8.713   1.00 18.33 ?  77  VAL   B HG13 1 
ATOM   5139 H HG21 . VAL   B 1 77  ? 38.603 -21.678 11.689  1.00 18.82 ?  77  VAL   B HG21 1 
ATOM   5140 H HG22 . VAL   B 1 77  ? 39.511 -20.990 10.581  1.00 18.82 ?  77  VAL   B HG22 1 
ATOM   5141 H HG23 . VAL   B 1 77  ? 38.886 -20.116 11.751  1.00 18.82 ?  77  VAL   B HG23 1 
ATOM   5142 N N    . GLY   B 1 78  ? 36.689 -19.399 7.225   1.00 12.66 ?  78  GLY   B N    1 
ATOM   5143 C CA   . GLY   B 1 78  ? 35.708 -19.078 6.217   1.00 12.10 ?  78  GLY   B CA   1 
ATOM   5144 C C    . GLY   B 1 78  ? 35.955 -17.762 5.514   1.00 11.48 ?  78  GLY   B C    1 
ATOM   5145 O O    . GLY   B 1 78  ? 35.285 -17.482 4.514   1.00 12.02 ?  78  GLY   B O    1 
ATOM   5146 H H    . GLY   B 1 78  ? 37.399 -19.770 6.906   1.00 15.16 ?  78  GLY   B H    1 
ATOM   5147 H HA2  . GLY   B 1 78  ? 35.699 -19.777 5.547   1.00 14.50 ?  78  GLY   B HA2  1 
ATOM   5148 H HA3  . GLY   B 1 78  ? 34.830 -19.038 6.627   1.00 14.50 ?  78  GLY   B HA3  1 
ATOM   5149 N N    . GLY   B 1 79  ? 36.905 -16.960 6.002   1.00 11.57 ?  79  GLY   B N    1 
ATOM   5150 C CA   . GLY   B 1 79  ? 37.203 -15.661 5.437   1.00 11.40 ?  79  GLY   B CA   1 
ATOM   5151 C C    . GLY   B 1 79  ? 38.445 -15.676 4.553   1.00 10.73 ?  79  GLY   B C    1 
ATOM   5152 O O    . GLY   B 1 79  ? 39.057 -16.712 4.303   1.00 11.57 ?  79  GLY   B O    1 
ATOM   5153 H H    . GLY   B 1 79  ? 37.401 -17.156 6.672   1.00 13.86 ?  79  GLY   B H    1 
ATOM   5154 H HA2  . GLY   B 1 79  ? 36.451 -15.356 4.900   1.00 13.66 ?  79  GLY   B HA2  1 
ATOM   5155 H HA3  . GLY   B 1 79  ? 37.349 -15.021 6.147   1.00 13.66 ?  79  GLY   B HA3  1 
ATOM   5156 N N    . SER   B 1 80  ? 38.819 -14.482 4.084   1.00 11.19 ?  80  SER   B N    1 
ATOM   5157 C CA   . SER   B 1 80  ? 39.930 -14.342 3.152   1.00 11.12 ?  80  SER   B CA   1 
ATOM   5158 C C    . SER   B 1 80  ? 40.509 -12.935 3.224   1.00 11.32 ?  80  SER   B C    1 
ATOM   5159 O O    . SER   B 1 80  ? 39.887 -12.004 3.745   1.00 12.25 ?  80  SER   B O    1 
ATOM   5160 C CB   . SER   B 1 80  ? 39.483 -14.617 1.712   1.00 11.40 ?  80  SER   B CB   1 
ATOM   5161 O OG   . SER   B 1 80  ? 38.642 -13.588 1.213   1.00 12.66 ?  80  SER   B OG   1 
ATOM   5162 H H    . SER   B 1 80  ? 38.443 -13.739 4.294   1.00 13.40 ?  80  SER   B H    1 
ATOM   5163 H HA   . SER   B 1 80  ? 40.619 -14.975 3.393   1.00 13.32 ?  80  SER   B HA   1 
ATOM   5164 H HB2  . SER   B 1 80  ? 40.265 -14.679 1.144   1.00 13.66 ?  80  SER   B HB2  1 
ATOM   5165 H HB3  . SER   B 1 80  ? 38.993 -15.456 1.688   1.00 13.66 ?  80  SER   B HB3  1 
ATOM   5166 H HG   . SER   B 1 80  ? 37.953 -13.523 1.698   1.00 15.17 ?  80  SER   B HG   1 
ATOM   5167 N N    . CYS   B 1 81  ? 41.695 -12.785 2.636   1.00 10.81 ?  81  CYS   B N    1 
ATOM   5168 C CA   . CYS   B 1 81  ? 42.237 -11.470 2.329   1.00 10.80 ?  81  CYS   B CA   1 
ATOM   5169 C C    . CYS   B 1 81  ? 43.016 -11.547 1.026   1.00 10.27 ?  81  CYS   B C    1 
ATOM   5170 O O    . CYS   B 1 81  ? 43.539 -12.603 0.654   1.00 11.31 ?  81  CYS   B O    1 
ATOM   5171 C CB   . CYS   B 1 81  ? 43.120 -10.916 3.454   1.00 11.70 ?  81  CYS   B CB   1 
ATOM   5172 S SG   . CYS   B 1 81  ? 44.642 -11.858 3.718   1.00 12.32 ?  81  CYS   B SG   1 
ATOM   5173 H H    . CYS   B 1 81  ? 42.200 -13.437 2.397   1.00 12.95 ?  81  CYS   B H    1 
ATOM   5174 H HA   . CYS   B 1 81  ? 41.500 -10.851 2.194   1.00 12.93 ?  81  CYS   B HA   1 
ATOM   5175 H HB2  . CYS   B 1 81  ? 43.367 -10.004 3.237   1.00 14.01 ?  81  CYS   B HB2  1 
ATOM   5176 H HB3  . CYS   B 1 81  ? 42.609 -10.927 4.281   1.00 14.01 ?  81  CYS   B HB3  1 
ATOM   5177 H HG   . CYS   B 1 81  ? 45.258 -11.355 4.620   1.00 14.76 ?  81  CYS   B HG   1 
ATOM   5178 N N    . VAL   B 1 82  ? 43.110 -10.405 0.351   1.00 10.68 ?  82  VAL   B N    1 
ATOM   5179 C CA   . VAL   B 1 82  ? 43.875 -10.278 -0.885  1.00 10.80 ?  82  VAL   B CA   1 
ATOM   5180 C C    . VAL   B 1 82  ? 45.214 -9.640  -0.561  1.00 11.23 ?  82  VAL   B C    1 
ATOM   5181 O O    . VAL   B 1 82  ? 45.263 -8.528  -0.016  1.00 12.01 ?  82  VAL   B O    1 
ATOM   5182 C CB   . VAL   B 1 82  ? 43.133 -9.432  -1.930  1.00 12.10 ?  82  VAL   B CB   1 
ATOM   5183 C CG1  . VAL   B 1 82  ? 43.986 -9.279  -3.182  1.00 13.70 ?  82  VAL   B CG1  1 
ATOM   5184 C CG2  . VAL   B 1 82  ? 41.781 -10.037 -2.254  1.00 12.95 ?  82  VAL   B CG2  1 
ATOM   5185 H H    . VAL   B 1 82  ? 42.724 -9.672  0.589   1.00 12.79 ?  82  VAL   B H    1 
ATOM   5186 H HA   . VAL   B 1 82  ? 44.034 -11.157 -1.260  1.00 12.94 ?  82  VAL   B HA   1 
ATOM   5187 H HB   . VAL   B 1 82  ? 42.979 -8.548  -1.567  1.00 14.49 ?  82  VAL   B HB   1 
ATOM   5188 H HG11 . VAL   B 1 82  ? 43.427 -8.970  -3.910  1.00 16.41 ?  82  VAL   B HG11 1 
ATOM   5189 H HG12 . VAL   B 1 82  ? 44.690 -8.632  -3.010  1.00 16.41 ?  82  VAL   B HG12 1 
ATOM   5190 H HG13 . VAL   B 1 82  ? 44.375 -10.139 -3.407  1.00 16.41 ?  82  VAL   B HG13 1 
ATOM   5191 H HG21 . VAL   B 1 82  ? 41.353 -9.504  -2.944  1.00 15.51 ?  82  VAL   B HG21 1 
ATOM   5192 H HG22 . VAL   B 1 82  ? 41.906 -10.945 -2.570  1.00 15.51 ?  82  VAL   B HG22 1 
ATOM   5193 H HG23 . VAL   B 1 82  ? 41.233 -10.038 -1.453  1.00 15.51 ?  82  VAL   B HG23 1 
ATOM   5194 N N    . LEU   B 1 83  ? 46.294 -10.323 -0.925  1.00 10.85 ?  83  LEU   B N    1 
ATOM   5195 C CA   . LEU   B 1 83  ? 47.648 -9.807  -0.789  1.00 10.81 ?  83  LEU   B CA   1 
ATOM   5196 C C    . LEU   B 1 83  ? 48.356 -9.932  -2.138  1.00 10.46 ?  83  LEU   B C    1 
ATOM   5197 O O    . LEU   B 1 83  ? 47.760 -10.339 -3.142  1.00 10.79 ?  83  LEU   B O    1 
ATOM   5198 C CB   . LEU   B 1 83  ? 48.394 -10.490 0.367   1.00 10.95 ?  83  LEU   B CB   1 
ATOM   5199 C CG   . LEU   B 1 83  ? 47.887 -10.133 1.768   1.00 12.57 ?  83  LEU   B CG   1 
ATOM   5200 C CD1  . LEU   B 1 83  ? 48.529 -11.012 2.824   1.00 13.13 ?  83  LEU   B CD1  1 
ATOM   5201 C CD2  . LEU   B 1 83  ? 48.088 -8.651  2.103   1.00 13.15 ?  83  LEU   B CD2  1 
ATOM   5202 H H    . LEU   B 1 83  ? 46.261 -11.118 -1.263  1.00 13.00 ?  83  LEU   B H    1 
ATOM   5203 H HA   . LEU   B 1 83  ? 47.592 -8.865  -0.583  1.00 12.95 ?  83  LEU   B HA   1 
ATOM   5204 H HB2  . LEU   B 1 83  ? 48.314 -11.447 0.265   1.00 13.11 ?  83  LEU   B HB2  1 
ATOM   5205 H HB3  . LEU   B 1 83  ? 49.327 -10.232 0.321   1.00 13.11 ?  83  LEU   B HB3  1 
ATOM   5206 H HG   . LEU   B 1 83  ? 46.937 -10.302 1.797   1.00 15.06 ?  83  LEU   B HG   1 
ATOM   5207 H HD11 . LEU   B 1 83  ? 48.185 -10.765 3.698   1.00 15.74 ?  83  LEU   B HD11 1 
ATOM   5208 H HD12 . LEU   B 1 83  ? 48.309 -11.942 2.637   1.00 15.74 ?  83  LEU   B HD12 1 
ATOM   5209 H HD13 . LEU   B 1 83  ? 49.491 -10.893 2.802   1.00 15.74 ?  83  LEU   B HD13 1 
ATOM   5210 H HD21 . LEU   B 1 83  ? 47.873 -8.506  3.039   1.00 15.75 ?  83  LEU   B HD21 1 
ATOM   5211 H HD22 . LEU   B 1 83  ? 49.011 -8.408  1.935   1.00 15.75 ?  83  LEU   B HD22 1 
ATOM   5212 H HD23 . LEU   B 1 83  ? 47.499 -8.118  1.545   1.00 15.75 ?  83  LEU   B HD23 1 
ATOM   5213 N N    . SER   B 1 84  ? 49.634 -9.558  -2.178  1.00 11.91 ?  84  SER   B N    1 
ATOM   5214 C CA   . SER   B 1 84  ? 50.369 -9.657  -3.430  1.00 12.15 ?  84  SER   B CA   1 
ATOM   5215 C C    . SER   B 1 84  ? 50.521 -11.112 -3.865  1.00 11.07 ?  84  SER   B C    1 
ATOM   5216 O O    . SER   B 1 84  ? 50.624 -12.028 -3.044  1.00 10.96 ?  84  SER   B O    1 
ATOM   5217 C CB   . SER   B 1 84  ? 51.767 -9.059  -3.277  1.00 14.09 ?  84  SER   B CB   1 
ATOM   5218 O OG   . SER   B 1 84  ? 52.522 -9.272  -4.456  1.00 15.80 ?  84  SER   B OG   1 
ATOM   5219 H H    . SER   B 1 84  ? 50.084 -9.241  -1.512  1.00 14.26 ?  84  SER   B H    1 
ATOM   5220 H HA   . SER   B 1 84  ? 49.900 -9.172  -4.124  1.00 14.56 ?  84  SER   B HA   1 
ATOM   5221 H HB2  . SER   B 1 84  ? 51.688 -8.102  -3.116  1.00 16.88 ?  84  SER   B HB2  1 
ATOM   5222 H HB3  . SER   B 1 84  ? 52.220 -9.484  -2.537  1.00 16.88 ?  84  SER   B HB3  1 
ATOM   5223 H HG   . SER   B 1 84  ? 53.285 -8.932  -4.381  1.00 18.94 ?  84  SER   B HG   1 
ATOM   5224 N N    . GLY   B 1 85  ? 50.586 -11.313 -5.177  1.00 12.16 ?  85  GLY   B N    1 
ATOM   5225 C CA   . GLY   B 1 85  ? 50.929 -12.600 -5.734  1.00 12.57 ?  85  GLY   B CA   1 
ATOM   5226 C C    . GLY   B 1 85  ? 52.401 -12.808 -6.019  1.00 12.01 ?  85  GLY   B C    1 
ATOM   5227 O O    . GLY   B 1 85  ? 52.769 -13.897 -6.465  1.00 12.33 ?  85  GLY   B O    1 
ATOM   5228 H H    . GLY   B 1 85  ? 50.441 -10.709 -5.766  1.00 14.57 ?  85  GLY   B H    1 
ATOM   5229 H HA2  . GLY   B 1 85  ? 50.646 -13.297 -5.117  1.00 15.05 ?  85  GLY   B HA2  1 
ATOM   5230 H HA3  . GLY   B 1 85  ? 50.453 -12.724 -6.562  1.00 15.05 ?  85  GLY   B HA3  1 
ATOM   5231 N N    . HIS   B 1 86  ? 53.259 -11.818 -5.782  1.00 11.95 ?  86  HIS   B N    1 
ATOM   5232 C CA   . HIS   B 1 86  ? 54.719 -12.002 -5.860  1.00 11.91 ?  86  HIS   B CA   1 
ATOM   5233 C C    . HIS   B 1 86  ? 55.089 -12.507 -7.254  1.00 12.00 ?  86  HIS   B C    1 
ATOM   5234 O O    . HIS   B 1 86  ? 54.703 -11.881 -8.254  1.00 13.07 ?  86  HIS   B O    1 
ATOM   5235 C CB   . HIS   B 1 86  ? 55.202 -12.852 -4.684  1.00 12.10 ?  86  HIS   B CB   1 
ATOM   5236 C CG   . HIS   B 1 86  ? 54.890 -12.249 -3.355  1.00 12.57 ?  86  HIS   B CG   1 
ATOM   5237 N ND1  . HIS   B 1 86  ? 55.719 -11.336 -2.738  1.00 13.89 ?  86  HIS   B ND1  1 
ATOM   5238 C CD2  . HIS   B 1 86  ? 53.816 -12.396 -2.544  1.00 12.73 ?  86  HIS   B CD2  1 
ATOM   5239 C CE1  . HIS   B 1 86  ? 55.165 -10.950 -1.602  1.00 13.79 ?  86  HIS   B CE1  1 
ATOM   5240 N NE2  . HIS   B 1 86  ? 54.008 -11.573 -1.463  1.00 13.07 ?  86  HIS   B NE2  1 
ATOM   5241 H H    . HIS   B 1 86  ? 53.026 -11.019 -5.577  1.00 14.32 ?  86  HIS   B H    1 
ATOM   5242 H HA   . HIS   B 1 86  ? 55.136 -11.134 -5.758  1.00 14.27 ?  86  HIS   B HA   1 
ATOM   5243 H HB2  . HIS   B 1 86  ? 54.775 -13.722 -4.725  1.00 14.50 ?  86  HIS   B HB2  1 
ATOM   5244 H HB3  . HIS   B 1 86  ? 56.166 -12.955 -4.741  1.00 14.50 ?  86  HIS   B HB3  1 
ATOM   5245 H HD2  . HIS   B 1 86  ? 53.074 -12.938 -2.697  1.00 15.25 ?  86  HIS   B HD2  1 
ATOM   5246 H HE1  . HIS   B 1 86  ? 55.538 -10.350 -0.998  1.00 16.52 ?  86  HIS   B HE1  1 
ATOM   5247 H HE2  . HIS   B 1 86  ? 53.476 -11.492 -0.792  1.00 15.66 ?  86  HIS   B HE2  1 
ATOM   5248 N N    . ASN   B 1 87  ? 55.859 -13.590 -7.371  1.00 12.52 ?  87  ASN   B N    1 
ATOM   5249 C CA   . ASN   B 1 87  ? 56.251 -14.161 -8.652  1.00 13.00 ?  87  ASN   B CA   1 
ATOM   5250 C C    . ASN   B 1 87  ? 55.269 -15.208 -9.154  1.00 12.57 ?  87  ASN   B C    1 
ATOM   5251 O O    . ASN   B 1 87  ? 55.580 -15.925 -10.109 1.00 14.24 ?  87  ASN   B O    1 
ATOM   5252 C CB   . ASN   B 1 87  ? 57.645 -14.791 -8.542  1.00 15.19 ?  87  ASN   B CB   1 
ATOM   5253 C CG   . ASN   B 1 87  ? 57.703 -15.908 -7.505  1.00 16.01 ?  87  ASN   B CG   1 
ATOM   5254 O OD1  . ASN   B 1 87  ? 57.058 -15.830 -6.453  1.00 14.79 ?  87  ASN   B OD1  1 
ATOM   5255 N ND2  . ASN   B 1 87  ? 58.448 -16.974 -7.818  1.00 17.94 ?  87  ASN   B ND2  1 
ATOM   5256 H H    . ASN   B 1 87  ? 56.181 -14.025 -6.698  1.00 15.00 ?  87  ASN   B H    1 
ATOM   5257 H HA   . ASN   B 1 87  ? 56.297 -13.455 -9.311  1.00 15.57 ?  87  ASN   B HA   1 
ATOM   5258 H HB2  . ASN   B 1 87  ? 57.892 -15.166 -9.406  1.00 18.20 ?  87  ASN   B HB2  1 
ATOM   5259 H HB3  . ASN   B 1 87  ? 58.282 -14.109 -8.284  1.00 18.20 ?  87  ASN   B HB3  1 
ATOM   5260 H HD21 . ASN   B 1 87  ? 58.518 -17.629 -7.268  1.00 21.50 ?  87  ASN   B HD21 1 
ATOM   5261 H HD22 . ASN   B 1 87  ? 58.877 -16.995 -8.567  1.00 21.50 ?  87  ASN   B HD22 1 
ATOM   5262 N N    . LEU   B 1 88  ? 54.090 -15.305 -8.538  1.00 11.77 ?  88  LEU   B N    1 
ATOM   5263 C CA   . LEU   B 1 88  ? 53.108 -16.336 -8.856  1.00 11.98 ?  88  LEU   B CA   1 
ATOM   5264 C C    . LEU   B 1 88  ? 51.877 -15.820 -9.581  1.00 11.58 ?  88  LEU   B C    1 
ATOM   5265 O O    . LEU   B 1 88  ? 51.270 -16.573 -10.353 1.00 13.53 ?  88  LEU   B O    1 
ATOM   5266 C CB   . LEU   B 1 88  ? 52.638 -17.018 -7.567  1.00 12.78 ?  88  LEU   B CB   1 
ATOM   5267 C CG   . LEU   B 1 88  ? 53.756 -17.655 -6.750  1.00 15.30 ?  88  LEU   B CG   1 
ATOM   5268 C CD1  . LEU   B 1 88  ? 53.246 -18.046 -5.374  1.00 17.17 ?  88  LEU   B CD1  1 
ATOM   5269 C CD2  . LEU   B 1 88  ? 54.308 -18.852 -7.492  1.00 18.33 ?  88  LEU   B CD2  1 
ATOM   5270 H H    . LEU   B 1 88  ? 53.832 -14.770 -7.910  1.00 14.10 ?  88  LEU   B H    1 
ATOM   5271 H HA   . LEU   B 1 88  ? 53.522 -17.004 -9.416  1.00 14.35 ?  88  LEU   B HA   1 
ATOM   5272 H HB2  . LEU   B 1 88  ? 52.203 -16.354 -7.003  1.00 15.31 ?  88  LEU   B HB2  1 
ATOM   5273 H HB3  . LEU   B 1 88  ? 52.005 -17.714 -7.796  1.00 15.31 ?  88  LEU   B HB3  1 
ATOM   5274 H HG   . LEU   B 1 88  ? 54.472 -17.010 -6.634  1.00 18.34 ?  88  LEU   B HG   1 
ATOM   5275 H HD11 . LEU   B 1 88  ? 53.896 -18.628 -4.950  1.00 20.59 ?  88  LEU   B HD11 1 
ATOM   5276 H HD12 . LEU   B 1 88  ? 53.120 -17.246 -4.842  1.00 20.59 ?  88  LEU   B HD12 1 
ATOM   5277 H HD13 . LEU   B 1 88  ? 52.401 -18.513 -5.475  1.00 20.59 ?  88  LEU   B HD13 1 
ATOM   5278 H HD21 . LEU   B 1 88  ? 54.948 -19.305 -6.920  1.00 21.97 ?  88  LEU   B HD21 1 
ATOM   5279 H HD22 . LEU   B 1 88  ? 53.580 -19.448 -7.715  1.00 21.97 ?  88  LEU   B HD22 1 
ATOM   5280 H HD23 . LEU   B 1 88  ? 54.749 -18.547 -8.301  1.00 21.97 ?  88  LEU   B HD23 1 
ATOM   5281 N N    . ALA   B 1 89  ? 51.470 -14.584 -9.319  1.00 10.64 ?  89  ALA   B N    1 
ATOM   5282 C CA   . ALA   B 1 89  ? 50.179 -14.094 -9.776  1.00 10.78 ?  89  ALA   B CA   1 
ATOM   5283 C C    . ALA   B 1 89  ? 50.152 -12.601 -9.510  1.00 11.29 ?  89  ALA   B C    1 
ATOM   5284 O O    . ALA   B 1 89  ? 50.990 -12.077 -8.775  1.00 11.98 ?  89  ALA   B O    1 
ATOM   5285 C CB   . ALA   B 1 89  ? 49.041 -14.751 -9.006  1.00 11.24 ?  89  ALA   B CB   1 
ATOM   5286 H H    . ALA   B 1 89  ? 51.920 -14.001 -8.863  1.00 12.74 ?  89  ALA   B H    1 
ATOM   5287 H HA   . ALA   B 1 89  ? 50.068 -14.256 -10.723 1.00 12.91 ?  89  ALA   B HA   1 
ATOM   5288 H HB1  . ALA   B 1 89  ? 48.193 -14.413 -9.344  1.00 13.46 ?  89  ALA   B HB1  1 
ATOM   5289 H HB2  . ALA   B 1 89  ? 49.087 -15.710 -9.133  1.00 13.46 ?  89  ALA   B HB2  1 
ATOM   5290 H HB3  . ALA   B 1 89  ? 49.128 -14.536 -8.064  1.00 13.46 ?  89  ALA   B HB3  1 
ATOM   5291 N N    . LYS   B 1 90  ? 49.151 -11.918 -10.065 1.00 12.16 ?  90  LYS   B N    1 
ATOM   5292 C CA   . LYS   B 1 90  ? 48.960 -10.530 -9.664  1.00 12.29 ?  90  LYS   B CA   1 
ATOM   5293 C C    . LYS   B 1 90  ? 48.641 -10.453 -8.177  1.00 12.08 ?  90  LYS   B C    1 
ATOM   5294 O O    . LYS   B 1 90  ? 49.270 -9.684  -7.431  1.00 13.92 ?  90  LYS   B O    1 
ATOM   5295 C CB   . LYS   B 1 90  ? 47.878 -9.870  -10.517 1.00 13.90 ?  90  LYS   B CB   1 
ATOM   5296 C CG   . LYS   B 1 90  ? 47.597 -8.422  -10.154 1.00 14.85 ?  90  LYS   B CG   1 
ATOM   5297 C CD   . LYS   B 1 90  ? 48.800 -7.528  -10.283 1.00 17.52 ?  90  LYS   B CD   1 
ATOM   5298 C CE   . LYS   B 1 90  ? 48.370 -6.091  -10.071 1.00 19.76 ?  90  LYS   B CE   1 
ATOM   5299 N NZ   . LYS   B 1 90  ? 49.527 -5.177  -9.942  1.00 19.99 ?  90  LYS   B NZ   1 
ATOM   5300 H H    . LYS   B 1 90  ? 48.599 -12.222 -10.650 1.00 14.56 ?  90  LYS   B H    1 
ATOM   5301 H HA   . LYS   B 1 90  ? 49.787 -10.050 -9.812  1.00 14.73 ?  90  LYS   B HA   1 
ATOM   5302 H HB2  . LYS   B 1 90  ? 48.160 -9.890  -11.448 1.00 16.66 ?  90  LYS   B HB2  1 
ATOM   5303 H HB3  . LYS   B 1 90  ? 47.052 -10.368 -10.419 1.00 16.66 ?  90  LYS   B HB3  1 
ATOM   5304 H HG2  . LYS   B 1 90  ? 46.907 -8.082  -10.744 1.00 17.80 ?  90  LYS   B HG2  1 
ATOM   5305 H HG3  . LYS   B 1 90  ? 47.288 -8.383  -9.234  1.00 17.80 ?  90  LYS   B HG3  1 
ATOM   5306 H HD2  . LYS   B 1 90  ? 49.457 -7.759  -9.606  1.00 21.01 ?  90  LYS   B HD2  1 
ATOM   5307 H HD3  . LYS   B 1 90  ? 49.180 -7.614  -11.172 1.00 21.01 ?  90  LYS   B HD3  1 
ATOM   5308 H HE2  . LYS   B 1 90  ? 47.843 -5.796  -10.832 1.00 23.69 ?  90  LYS   B HE2  1 
ATOM   5309 H HE3  . LYS   B 1 90  ? 47.848 -6.025  -9.258  1.00 23.69 ?  90  LYS   B HE3  1 
ATOM   5310 H HZ1  . LYS   B 1 90  ? 49.251 -4.338  -9.821  1.00 23.97 ?  90  LYS   B HZ1  1 
ATOM   5311 H HZ2  . LYS   B 1 90  ? 50.033 -5.414  -9.248  1.00 23.97 ?  90  LYS   B HZ2  1 
ATOM   5312 H HZ3  . LYS   B 1 90  ? 50.029 -5.206  -10.681 1.00 23.97 ?  90  LYS   B HZ3  1 
ATOM   5313 N N    . HIS   B 1 91  ? 47.684 -11.270 -7.731  1.00 10.70 ?  91  HIS   B N    1 
ATOM   5314 C CA   . HIS   B 1 91  ? 47.217 -11.291 -6.358  1.00 10.81 ?  91  HIS   B CA   1 
ATOM   5315 C C    . HIS   B 1 91  ? 47.217 -12.716 -5.833  1.00 10.18 ?  91  HIS   B C    1 
ATOM   5316 O O    . HIS   B 1 91  ? 46.980 -13.671 -6.578  1.00 10.76 ?  91  HIS   B O    1 
ATOM   5317 C CB   . HIS   B 1 91  ? 45.760 -10.818 -6.265  1.00 12.52 ?  91  HIS   B CB   1 
ATOM   5318 C CG   . HIS   B 1 91  ? 45.538 -9.418  -6.721  1.00 15.81 ?  91  HIS   B CG   1 
ATOM   5319 N ND1  . HIS   B 1 91  ? 46.126 -8.334  -6.109  1.00 18.37 ?  91  HIS   B ND1  1 
ATOM   5320 C CD2  . HIS   B 1 91  ? 44.759 -8.918  -7.707  1.00 18.16 ?  91  HIS   B CD2  1 
ATOM   5321 C CE1  . HIS   B 1 91  ? 45.740 -7.224  -6.715  1.00 19.43 ?  91  HIS   B CE1  1 
ATOM   5322 N NE2  . HIS   B 1 91  ? 44.904 -7.551  -7.684  1.00 19.27 ?  91  HIS   B NE2  1 
ATOM   5323 H H    . HIS   B 1 91  ? 47.277 -11.844 -8.229  1.00 12.82 ?  91  HIS   B H    1 
ATOM   5324 H HA   . HIS   B 1 91  ? 47.776 -10.726 -5.794  1.00 12.95 ?  91  HIS   B HA   1 
ATOM   5325 H HB2  . HIS   B 1 91  ? 45.208 -11.396 -6.817  1.00 15.01 ?  91  HIS   B HB2  1 
ATOM   5326 H HB3  . HIS   B 1 91  ? 45.467 -10.875 -5.341  1.00 15.01 ?  91  HIS   B HB3  1 
ATOM   5327 H HD1  . HIS   B 1 91  ? 46.671 -8.372  -5.443  1.00 22.02 ?  91  HIS   B HD1  1 
ATOM   5328 H HD2  . HIS   B 1 91  ? 44.233 -9.400  -8.300  1.00 21.76 ?  91  HIS   B HD2  1 
ATOM   5329 H HE1  . HIS   B 1 91  ? 46.006 -6.360  -6.489  1.00 23.30 ?  91  HIS   B HE1  1 
ATOM   5330 N N    . CYS   B 1 92  ? 47.419 -12.849 -4.532  1.00 10.03 ?  92  CYS   B N    1 
ATOM   5331 C CA   . CYS   B 1 92  ? 47.120 -14.085 -3.826  1.00 9.82  ?  92  CYS   B CA   1 
ATOM   5332 C C    . CYS   B 1 92  ? 45.902 -13.856 -2.942  1.00 9.46  ?  92  CYS   B C    1 
ATOM   5333 O O    . CYS   B 1 92  ? 45.903 -12.959 -2.088  1.00 10.30 ?  92  CYS   B O    1 
ATOM   5334 C CB   . CYS   B 1 92  ? 48.299 -14.554 -2.981  1.00 10.41 ?  92  CYS   B CB   1 
ATOM   5335 S SG   . CYS   B 1 92  ? 47.948 -16.086 -2.075  1.00 10.50 ?  92  CYS   B SG   1 
ATOM   5336 H H    . CYS   B 1 92  ? 47.747 -12.230 -4.024  1.00 12.01 ?  92  CYS   B H    1 
ATOM   5337 H HA   . CYS   B 1 92  ? 46.918 -14.781 -4.473  1.00 11.76 ?  92  CYS   B HA   1 
ATOM   5338 H HB2  . CYS   B 1 92  ? 49.061 -14.716 -3.554  1.00 12.47 ?  92  CYS   B HB2  1 
ATOM   5339 H HB3  . CYS   B 1 92  ? 48.510 -13.867 -2.329  1.00 12.47 ?  92  CYS   B HB3  1 
ATOM   5340 H HG   . CYS   B 1 92  ? 48.917 -16.398 -1.453  1.00 12.57 ?  92  CYS   B HG   1 
ATOM   5341 N N    . LEU   B 1 93  ? 44.862 -14.656 -3.163  1.00 9.28  ?  93  LEU   B N    1 
ATOM   5342 C CA   . LEU   B 1 93  ? 43.691 -14.677 -2.298  1.00 9.39  ?  93  LEU   B CA   1 
ATOM   5343 C C    . LEU   B 1 93  ? 43.923 -15.749 -1.238  1.00 9.18  ?  93  LEU   B C    1 
ATOM   5344 O O    . LEU   B 1 93  ? 43.872 -16.952 -1.534  1.00 9.74  ?  93  LEU   B O    1 
ATOM   5345 C CB   . LEU   B 1 93  ? 42.430 -14.968 -3.106  1.00 10.14 ?  93  LEU   B CB   1 
ATOM   5346 C CG   . LEU   B 1 93  ? 41.129 -14.995 -2.304  1.00 10.56 ?  93  LEU   B CG   1 
ATOM   5347 C CD1  . LEU   B 1 93  ? 40.771 -13.611 -1.811  1.00 11.11 ?  93  LEU   B CD1  1 
ATOM   5348 C CD2  . LEU   B 1 93  ? 39.996 -15.580 -3.140  1.00 10.53 ?  93  LEU   B CD2  1 
ATOM   5349 H H    . LEU   B 1 93  ? 44.815 -15.220 -3.822  1.00 11.12 ?  93  LEU   B H    1 
ATOM   5350 H HA   . LEU   B 1 93  ? 43.595 -13.817 -1.863  1.00 11.24 ?  93  LEU   B HA   1 
ATOM   5351 H HB2  . LEU   B 1 93  ? 42.336 -14.278 -3.788  1.00 12.15 ?  93  LEU   B HB2  1 
ATOM   5352 H HB3  . LEU   B 1 93  ? 42.526 -15.830 -3.533  1.00 12.15 ?  93  LEU   B HB3  1 
ATOM   5353 H HG   . LEU   B 1 93  ? 41.246 -15.562 -1.533  1.00 12.65 ?  93  LEU   B HG   1 
ATOM   5354 H HD11 . LEU   B 1 93  ? 39.915 -13.645 -1.357  1.00 13.31 ?  93  LEU   B HD11 1 
ATOM   5355 H HD12 . LEU   B 1 93  ? 41.458 -13.304 -1.197  1.00 13.31 ?  93  LEU   B HD12 1 
ATOM   5356 H HD13 . LEU   B 1 93  ? 40.716 -13.004 -2.569  1.00 13.31 ?  93  LEU   B HD13 1 
ATOM   5357 H HD21 . LEU   B 1 93  ? 39.183 -15.580 -2.614  1.00 12.61 ?  93  LEU   B HD21 1 
ATOM   5358 H HD22 . LEU   B 1 93  ? 39.876 -15.033 -3.935  1.00 12.61 ?  93  LEU   B HD22 1 
ATOM   5359 H HD23 . LEU   B 1 93  ? 40.230 -16.485 -3.395  1.00 12.61 ?  93  LEU   B HD23 1 
ATOM   5360 N N    . HIS   B 1 94  ? 44.191 -15.318 -0.011  1.00 9.08  ?  94  HIS   B N    1 
ATOM   5361 C CA   . HIS   B 1 94  ? 44.411 -16.228 1.107   1.00 9.29  ?  94  HIS   B CA   1 
ATOM   5362 C C    . HIS   B 1 94  ? 43.048 -16.589 1.681   1.00 9.68  ?  94  HIS   B C    1 
ATOM   5363 O O    . HIS   B 1 94  ? 42.371 -15.720 2.234   1.00 11.11 ?  94  HIS   B O    1 
ATOM   5364 C CB   . HIS   B 1 94  ? 45.280 -15.546 2.162   1.00 9.89  ?  94  HIS   B CB   1 
ATOM   5365 C CG   . HIS   B 1 94  ? 46.665 -15.246 1.691   1.00 9.86  ?  94  HIS   B CG   1 
ATOM   5366 N ND1  . HIS   B 1 94  ? 47.693 -16.158 1.783   1.00 10.09 ?  94  HIS   B ND1  1 
ATOM   5367 C CD2  . HIS   B 1 94  ? 47.176 -14.138 1.101   1.00 9.99  ?  94  HIS   B CD2  1 
ATOM   5368 C CE1  . HIS   B 1 94  ? 48.783 -15.611 1.273   1.00 10.20 ?  94  HIS   B CE1  1 
ATOM   5369 N NE2  . HIS   B 1 94  ? 48.498 -14.390 0.850   1.00 10.28 ?  94  HIS   B NE2  1 
ATOM   5370 H H    . HIS   B 1 94  ? 44.262 -14.484 0.198   1.00 10.88 ?  94  HIS   B H    1 
ATOM   5371 H HA   . HIS   B 1 94  ? 44.850 -17.035 0.797   1.00 11.13 ?  94  HIS   B HA   1 
ATOM   5372 H HB2  . HIS   B 1 94  ? 44.866 -14.711 2.415   1.00 11.85 ?  94  HIS   B HB2  1 
ATOM   5373 H HB3  . HIS   B 1 94  ? 45.349 -16.133 2.930   1.00 11.85 ?  94  HIS   B HB3  1 
ATOM   5374 H HD2  . HIS   B 1 94  ? 46.722 -13.358 0.899   1.00 11.97 ?  94  HIS   B HD2  1 
ATOM   5375 H HE1  . HIS   B 1 94  ? 49.620 -16.028 1.221   1.00 12.21 ?  94  HIS   B HE1  1 
ATOM   5376 H HE2  . HIS   B 1 94  ? 49.060 -13.850 0.487   1.00 12.31 ?  94  HIS   B HE2  1 
ATOM   5377 N N    . VAL   B 1 95  ? 42.623 -17.845 1.529   1.00 9.79  ?  95  VAL   B N    1 
ATOM   5378 C CA   . VAL   B 1 95  ? 41.295 -18.288 1.958   1.00 10.01 ?  95  VAL   B CA   1 
ATOM   5379 C C    . VAL   B 1 95  ? 41.463 -19.322 3.052   1.00 9.81  ?  95  VAL   B C    1 
ATOM   5380 O O    . VAL   B 1 95  ? 42.231 -20.275 2.887   1.00 10.47 ?  95  VAL   B O    1 
ATOM   5381 C CB   . VAL   B 1 95  ? 40.480 -18.894 0.798   1.00 9.89  ?  95  VAL   B CB   1 
ATOM   5382 C CG1  . VAL   B 1 95  ? 39.101 -19.352 1.287   1.00 10.92 ?  95  VAL   B CG1  1 
ATOM   5383 C CG2  . VAL   B 1 95  ? 40.357 -17.905 -0.343  1.00 10.18 ?  95  VAL   B CG2  1 
ATOM   5384 H H    . VAL   B 1 95  ? 43.090 -18.473 1.173   1.00 11.73 ?  95  VAL   B H    1 
ATOM   5385 H HA   . VAL   B 1 95  ? 40.801 -17.538 2.325   1.00 11.99 ?  95  VAL   B HA   1 
ATOM   5386 H HB   . VAL   B 1 95  ? 40.943 -19.669 0.463   1.00 11.84 ?  95  VAL   B HB   1 
ATOM   5387 H HG11 . VAL   B 1 95  ? 38.540 -19.547 0.515   1.00 13.08 ?  95  VAL   B HG11 1 
ATOM   5388 H HG12 . VAL   B 1 95  ? 39.201 -20.152 1.826   1.00 13.08 ?  95  VAL   B HG12 1 
ATOM   5389 H HG13 . VAL   B 1 95  ? 38.694 -18.646 1.814   1.00 13.08 ?  95  VAL   B HG13 1 
ATOM   5390 H HG21 . VAL   B 1 95  ? 39.784 -18.287 -1.027  1.00 12.19 ?  95  VAL   B HG21 1 
ATOM   5391 H HG22 . VAL   B 1 95  ? 39.965 -17.083 -0.007  1.00 12.19 ?  95  VAL   B HG22 1 
ATOM   5392 H HG23 . VAL   B 1 95  ? 41.237 -17.732 -0.703  1.00 12.19 ?  95  VAL   B HG23 1 
ATOM   5393 N N    . VAL   B 1 96  ? 40.724 -19.159 4.145   1.00 10.29 ?  96  VAL   B N    1 
ATOM   5394 C CA   . VAL   B 1 96  ? 40.804 -20.075 5.282   1.00 10.88 ?  96  VAL   B CA   1 
ATOM   5395 C C    . VAL   B 1 96  ? 39.618 -21.035 5.234   1.00 11.15 ?  96  VAL   B C    1 
ATOM   5396 O O    . VAL   B 1 96  ? 38.498 -20.684 5.615   1.00 11.95 ?  96  VAL   B O    1 
ATOM   5397 C CB   . VAL   B 1 96  ? 40.854 -19.326 6.616   1.00 11.74 ?  96  VAL   B CB   1 
ATOM   5398 C CG1  . VAL   B 1 96  ? 41.031 -20.321 7.764   1.00 12.41 ?  96  VAL   B CG1  1 
ATOM   5399 C CG2  . VAL   B 1 96  ? 41.971 -18.288 6.619   1.00 12.24 ?  96  VAL   B CG2  1 
ATOM   5400 H H    . VAL   B 1 96  ? 40.154 -18.528 4.254   1.00 12.32 ?  96  VAL   B H    1 
ATOM   5401 H HA   . VAL   B 1 96  ? 41.612 -20.606 5.210   1.00 13.03 ?  96  VAL   B HA   1 
ATOM   5402 H HB   . VAL   B 1 96  ? 40.013 -18.864 6.754   1.00 14.07 ?  96  VAL   B HB   1 
ATOM   5403 H HG11 . VAL   B 1 96  ? 41.218 -19.828 8.582   1.00 14.87 ?  96  VAL   B HG11 1 
ATOM   5404 H HG12 . VAL   B 1 96  ? 40.217 -20.835 7.871   1.00 14.87 ?  96  VAL   B HG12 1 
ATOM   5405 H HG13 . VAL   B 1 96  ? 41.774 -20.910 7.561   1.00 14.87 ?  96  VAL   B HG13 1 
ATOM   5406 H HG21 . VAL   B 1 96  ? 42.024 -17.878 7.501   1.00 14.66 ?  96  VAL   B HG21 1 
ATOM   5407 H HG22 . VAL   B 1 96  ? 42.811 -18.720 6.407   1.00 14.66 ?  96  VAL   B HG22 1 
ATOM   5408 H HG23 . VAL   B 1 96  ? 41.773 -17.605 5.956   1.00 14.66 ?  96  VAL   B HG23 1 
ATOM   5409 N N    . GLY   B 1 97  ? 39.857 -22.268 4.797   1.00 11.20 ?  97  GLY   B N    1 
ATOM   5410 C CA   . GLY   B 1 97  ? 38.878 -23.320 4.948   1.00 11.35 ?  97  GLY   B CA   1 
ATOM   5411 C C    . GLY   B 1 97  ? 38.982 -23.925 6.332   1.00 12.00 ?  97  GLY   B C    1 
ATOM   5412 O O    . GLY   B 1 97  ? 40.019 -23.799 6.997   1.00 12.59 ?  97  GLY   B O    1 
ATOM   5413 H H    . GLY   B 1 97  ? 40.589 -22.514 4.415   1.00 13.41 ?  97  GLY   B H    1 
ATOM   5414 H HA2  . GLY   B 1 97  ? 37.986 -22.956 4.819   1.00 13.60 ?  97  GLY   B HA2  1 
ATOM   5415 H HA3  . GLY   B 1 97  ? 39.030 -24.010 4.279   1.00 13.60 ?  97  GLY   B HA3  1 
ATOM   5416 N N    . PRO   B 1 98  ? 37.932 -24.607 6.793   1.00 12.60 ?  98  PRO   B N    1 
ATOM   5417 C CA   . PRO   B 1 98  ? 38.026 -25.306 8.079   1.00 13.35 ?  98  PRO   B CA   1 
ATOM   5418 C C    . PRO   B 1 98  ? 39.052 -26.427 8.034   1.00 13.06 ?  98  PRO   B C    1 
ATOM   5419 O O    . PRO   B 1 98  ? 39.167 -27.156 7.050   1.00 13.48 ?  98  PRO   B O    1 
ATOM   5420 C CB   . PRO   B 1 98  ? 36.609 -25.851 8.286   1.00 13.66 ?  98  PRO   B CB   1 
ATOM   5421 C CG   . PRO   B 1 98  ? 36.056 -25.991 6.908   1.00 13.35 ?  98  PRO   B CG   1 
ATOM   5422 C CD   . PRO   B 1 98  ? 36.623 -24.817 6.149   1.00 12.76 ?  98  PRO   B CD   1 
ATOM   5423 H HA   . PRO   B 1 98  ? 38.249 -24.680 8.782   1.00 16.00 ?  98  PRO   B HA   1 
ATOM   5424 H HB2  . PRO   B 1 98  ? 36.658 -26.714 8.730   1.00 16.37 ?  98  PRO   B HB2  1 
ATOM   5425 H HB3  . PRO   B 1 98  ? 36.090 -25.222 8.804   1.00 16.37 ?  98  PRO   B HB3  1 
ATOM   5426 H HG2  . PRO   B 1 98  ? 36.357 -26.833 6.523   1.00 16.00 ?  98  PRO   B HG2  1 
ATOM   5427 H HG3  . PRO   B 1 98  ? 35.090 -25.955 6.942   1.00 16.00 ?  98  PRO   B HG3  1 
ATOM   5428 H HD2  . PRO   B 1 98  ? 36.727 -25.042 5.207   1.00 15.29 ?  98  PRO   B HD2  1 
ATOM   5429 H HD3  . PRO   B 1 98  ? 36.062 -24.035 6.265   1.00 15.29 ?  98  PRO   B HD3  1 
ATOM   5430 N N    . ASN   B 1 99  ? 39.798 -26.556 9.122   1.00 13.74 ?  99  ASN   B N    1 
ATOM   5431 C CA   . ASN   B 1 99  ? 40.778 -27.625 9.285   1.00 14.41 ?  99  ASN   B CA   1 
ATOM   5432 C C    . ASN   B 1 99  ? 40.141 -28.706 10.158  1.00 16.18 ?  99  ASN   B C    1 
ATOM   5433 O O    . ASN   B 1 99  ? 40.039 -28.556 11.379  1.00 17.02 ?  99  ASN   B O    1 
ATOM   5434 C CB   . ASN   B 1 99  ? 42.054 -27.073 9.907   1.00 14.75 ?  99  ASN   B CB   1 
ATOM   5435 C CG   . ASN   B 1 99  ? 43.175 -28.086 9.923   1.00 15.87 ?  99  ASN   B CG   1 
ATOM   5436 O OD1  . ASN   B 1 99  ? 42.936 -29.277 10.081  1.00 16.67 ?  99  ASN   B OD1  1 
ATOM   5437 N ND2  . ASN   B 1 99  ? 44.404 -27.621 9.757   1.00 16.36 ?  99  ASN   B ND2  1 
ATOM   5438 H H    . ASN   B 1 99  ? 39.758 -26.017 9.792   1.00 16.46 ?  99  ASN   B H    1 
ATOM   5439 H HA   . ASN   B 1 99  ? 40.992 -28.007 8.420   1.00 17.27 ?  99  ASN   B HA   1 
ATOM   5440 H HB2  . ASN   B 1 99  ? 42.350 -26.305 9.400   1.00 17.67 ?  99  ASN   B HB2  1 
ATOM   5441 H HB3  . ASN   B 1 99  ? 41.868 -26.814 10.826  1.00 17.67 ?  99  ASN   B HB3  1 
ATOM   5442 H HD21 . ASN   B 1 99  ? 45.073 -28.164 9.758   1.00 19.61 ?  99  ASN   B HD21 1 
ATOM   5443 H HD22 . ASN   B 1 99  ? 44.532 -26.781 9.647   1.00 19.61 ?  99  ASN   B HD22 1 
ATOM   5444 N N    A VAL   B 1 100 ? 39.691 -29.789 9.520   0.48 18.04 ?  100 VAL   B N    1 
ATOM   5445 N N    B VAL   B 1 100 ? 39.698 -29.791 9.516   0.52 17.94 ?  100 VAL   B N    1 
ATOM   5446 C CA   A VAL   B 1 100 ? 39.066 -30.881 10.261  0.48 20.50 ?  100 VAL   B CA   1 
ATOM   5447 C CA   B VAL   B 1 100 ? 39.066 -30.892 10.238  0.52 20.36 ?  100 VAL   B CA   1 
ATOM   5448 C C    A VAL   B 1 100 ? 40.065 -31.542 11.199  0.48 20.97 ?  100 VAL   B C    1 
ATOM   5449 C C    B VAL   B 1 100 ? 40.056 -31.575 11.171  0.52 20.73 ?  100 VAL   B C    1 
ATOM   5450 O O    A VAL   B 1 100 ? 39.691 -32.027 12.274  0.48 21.41 ?  100 VAL   B O    1 
ATOM   5451 O O    B VAL   B 1 100 ? 39.664 -32.115 12.214  0.52 20.94 ?  100 VAL   B O    1 
ATOM   5452 C CB   A VAL   B 1 100 ? 38.431 -31.894 9.290   0.48 22.69 ?  100 VAL   B CB   1 
ATOM   5453 C CB   B VAL   B 1 100 ? 38.433 -31.884 9.244   0.52 22.62 ?  100 VAL   B CB   1 
ATOM   5454 C CG1  A VAL   B 1 100 ? 37.966 -33.134 10.041  0.48 23.63 ?  100 VAL   B CG1  1 
ATOM   5455 C CG1  B VAL   B 1 100 ? 37.905 -33.113 9.973   0.52 23.63 ?  100 VAL   B CG1  1 
ATOM   5456 C CG2  A VAL   B 1 100 ? 37.272 -31.253 8.546   0.48 23.38 ?  100 VAL   B CG2  1 
ATOM   5457 C CG2  B VAL   B 1 100 ? 37.320 -31.207 8.465   0.52 23.33 ?  100 VAL   B CG2  1 
ATOM   5458 H H    A VAL   B 1 100 ? 39.732 -29.909 8.669   0.48 21.62 ?  100 VAL   B H    1 
ATOM   5459 H H    B VAL   B 1 100 ? 39.746 -29.906 8.664   0.52 21.51 ?  100 VAL   B H    1 
ATOM   5460 H HA   A VAL   B 1 100 ? 38.351 -30.513 10.804  0.48 24.58 ?  100 VAL   B HA   1 
ATOM   5461 H HA   B VAL   B 1 100 ? 38.350 -30.530 10.783  0.52 24.41 ?  100 VAL   B HA   1 
ATOM   5462 H HB   A VAL   B 1 100 ? 39.095 -32.169 8.640   0.48 27.21 ?  100 VAL   B HB   1 
ATOM   5463 H HB   B VAL   B 1 100 ? 39.110 -32.179 8.614   0.52 27.12 ?  100 VAL   B HB   1 
ATOM   5464 H HG11 A VAL   B 1 100 ? 37.365 -33.639 9.471   0.48 28.33 ?  100 VAL   B HG11 1 
ATOM   5465 H HG11 B VAL   B 1 100 ? 37.329 -33.612 9.371   0.52 28.34 ?  100 VAL   B HG11 1 
ATOM   5466 H HG12 A VAL   B 1 100 ? 38.737 -33.678 10.270  0.48 28.33 ?  100 VAL   B HG12 1 
ATOM   5467 H HG12 B VAL   B 1 100 ? 38.652 -33.669 10.247  0.52 28.34 ?  100 VAL   B HG12 1 
ATOM   5468 H HG13 A VAL   B 1 100 ? 37.502 -32.861 10.848  0.48 28.33 ?  100 VAL   B HG13 1 
ATOM   5469 H HG13 B VAL   B 1 100 ? 37.400 -32.828 10.750  0.52 28.34 ?  100 VAL   B HG13 1 
ATOM   5470 H HG21 A VAL   B 1 100 ? 36.879 -31.909 7.949   0.48 28.03 ?  100 VAL   B HG21 1 
ATOM   5471 H HG21 B VAL   B 1 100 ? 36.912 -31.856 7.870   0.52 27.97 ?  100 VAL   B HG21 1 
ATOM   5472 H HG22 A VAL   B 1 100 ? 36.610 -30.954 9.190   0.48 28.03 ?  100 VAL   B HG22 1 
ATOM   5473 H HG22 B VAL   B 1 100 ? 36.658 -30.871 9.090   0.52 27.97 ?  100 VAL   B HG22 1 
ATOM   5474 H HG23 A VAL   B 1 100 ? 37.602 -30.497 8.037   0.48 28.03 ?  100 VAL   B HG23 1 
ATOM   5475 H HG23 B VAL   B 1 100 ? 37.693 -30.475 7.952   0.52 27.97 ?  100 VAL   B HG23 1 
ATOM   5476 N N    . ASN   B 1 101 ? 41.343 -31.589 10.810  1.00 21.31 ?  101 ASN   B N    1 
ATOM   5477 C CA   . ASN   B 1 101 ? 42.368 -32.127 11.702  1.00 23.57 ?  101 ASN   B CA   1 
ATOM   5478 C C    . ASN   B 1 101 ? 42.522 -31.297 12.972  1.00 25.95 ?  101 ASN   B C    1 
ATOM   5479 O O    . ASN   B 1 101 ? 43.090 -31.790 13.955  1.00 27.11 ?  101 ASN   B O    1 
ATOM   5480 C CB   . ASN   B 1 101 ? 43.705 -32.257 10.963  1.00 23.91 ?  101 ASN   B CB   1 
ATOM   5481 C CG   . ASN   B 1 101 ? 43.701 -33.388 9.944   1.00 23.91 ?  101 ASN   B CG   1 
ATOM   5482 O OD1  . ASN   B 1 101 ? 43.045 -34.405 10.139  1.00 24.84 ?  101 ASN   B OD1  1 
ATOM   5483 N ND2  . ASN   B 1 101 ? 44.437 -33.212 8.856   1.00 23.59 ?  101 ASN   B ND2  1 
ATOM   5484 H H    A ASN   B 1 101 ? 41.631 -31.330 10.041  0.48 25.55 ?  101 ASN   B H    1 
ATOM   5485 H H    B ASN   B 1 101 ? 41.640 -31.306 10.053  0.52 25.55 ?  101 ASN   B H    1 
ATOM   5486 H HA   . ASN   B 1 101 ? 42.101 -33.013 11.974  1.00 28.26 ?  101 ASN   B HA   1 
ATOM   5487 H HB2  . ASN   B 1 101 ? 43.897 -31.433 10.489  1.00 28.66 ?  101 ASN   B HB2  1 
ATOM   5488 H HB3  . ASN   B 1 101 ? 44.408 -32.437 11.609  1.00 28.66 ?  101 ASN   B HB3  1 
ATOM   5489 H HD21 . ASN   B 1 101 ? 44.465 -33.826 8.254   1.00 28.28 ?  101 ASN   B HD21 1 
ATOM   5490 H HD22 . ASN   B 1 101 ? 44.881 -32.485 8.750   1.00 28.28 ?  101 ASN   B HD22 1 
ATOM   5491 N N    A LYS   B 1 102 ? 42.062 -30.045 12.963  0.48 27.22 ?  102 LYS   B N    1 
ATOM   5492 N N    B LYS   B 1 102 ? 42.009 -30.065 12.982  0.52 27.03 ?  102 LYS   B N    1 
ATOM   5493 C CA   A LYS   B 1 102 ? 42.050 -29.195 14.146  0.48 28.82 ?  102 LYS   B CA   1 
ATOM   5494 C CA   B LYS   B 1 102 ? 41.945 -29.236 14.179  0.52 28.49 ?  102 LYS   B CA   1 
ATOM   5495 C C    A LYS   B 1 102 ? 40.683 -29.160 14.816  0.48 28.46 ?  102 LYS   B C    1 
ATOM   5496 C C    B LYS   B 1 102 ? 40.554 -29.224 14.805  0.52 28.12 ?  102 LYS   B C    1 
ATOM   5497 O O    A LYS   B 1 102 ? 40.469 -28.351 15.724  0.48 28.71 ?  102 LYS   B O    1 
ATOM   5498 O O    B LYS   B 1 102 ? 40.323 -28.477 15.761  0.52 28.53 ?  102 LYS   B O    1 
ATOM   5499 C CB   A LYS   B 1 102 ? 42.469 -27.767 13.788  0.48 30.91 ?  102 LYS   B CB   1 
ATOM   5500 C CB   B LYS   B 1 102 ? 42.358 -27.797 13.859  0.52 30.52 ?  102 LYS   B CB   1 
ATOM   5501 C CG   A LYS   B 1 102 ? 43.933 -27.588 13.419  0.48 32.92 ?  102 LYS   B CG   1 
ATOM   5502 C CG   B LYS   B 1 102 ? 43.800 -27.614 13.419  0.52 32.49 ?  102 LYS   B CG   1 
ATOM   5503 C CD   A LYS   B 1 102 ? 44.215 -26.128 13.086  0.48 34.75 ?  102 LYS   B CD   1 
ATOM   5504 C CD   B LYS   B 1 102 ? 44.034 -26.169 13.003  0.52 34.28 ?  102 LYS   B CD   1 
ATOM   5505 C CE   A LYS   B 1 102 ? 45.681 -25.884 12.767  0.48 36.11 ?  102 LYS   B CE   1 
ATOM   5506 C CE   B LYS   B 1 102 ? 45.495 -25.882 12.707  0.52 35.58 ?  102 LYS   B CE   1 
ATOM   5507 N NZ   A LYS   B 1 102 ? 45.935 -24.456 12.420  0.48 36.89 ?  102 LYS   B NZ   1 
ATOM   5508 N NZ   B LYS   B 1 102 ? 45.691 -24.457 12.311  0.52 36.33 ?  102 LYS   B NZ   1 
ATOM   5509 H H    A LYS   B 1 102 ? 41.740 -29.657 12.264  0.48 32.64 ?  102 LYS   B H    1 
ATOM   5510 H H    B LYS   B 1 102 ? 41.679 -29.679 12.288  0.52 32.42 ?  102 LYS   B H    1 
ATOM   5511 H HA   A LYS   B 1 102 ? 42.694 -29.539 14.784  0.48 34.56 ?  102 LYS   B HA   1 
ATOM   5512 H HA   B LYS   B 1 102 ? 42.568 -29.582 14.836  0.52 34.17 ?  102 LYS   B HA   1 
ATOM   5513 H HB2  A LYS   B 1 102 ? 41.941 -27.470 13.033  0.48 37.07 ?  102 LYS   B HB2  1 
ATOM   5514 H HB2  B LYS   B 1 102 ? 41.793 -27.465 13.146  0.52 36.60 ?  102 LYS   B HB2  1 
ATOM   5515 H HB3  A LYS   B 1 102 ? 42.293 -27.194 14.552  0.48 37.07 ?  102 LYS   B HB3  1 
ATOM   5516 H HB3  B LYS   B 1 102 ? 42.229 -27.255 14.655  0.52 36.60 ?  102 LYS   B HB3  1 
ATOM   5517 H HG2  A LYS   B 1 102 ? 44.492 -27.845 14.169  0.48 39.48 ?  102 LYS   B HG2  1 
ATOM   5518 H HG2  B LYS   B 1 102 ? 44.397 -27.823 14.156  0.52 38.96 ?  102 LYS   B HG2  1 
ATOM   5519 H HG3  A LYS   B 1 102 ? 44.140 -28.126 12.640  0.48 39.48 ?  102 LYS   B HG3  1 
ATOM   5520 H HG3  B LYS   B 1 102 ? 43.985 -28.188 12.659  0.52 38.96 ?  102 LYS   B HG3  1 
ATOM   5521 H HD2  A LYS   B 1 102 ? 43.691 -25.872 12.311  0.48 41.68 ?  102 LYS   B HD2  1 
ATOM   5522 H HD2  B LYS   B 1 102 ? 43.522 -25.983 12.200  0.52 41.11 ?  102 LYS   B HD2  1 
ATOM   5523 H HD3  A LYS   B 1 102 ? 43.976 -25.576 13.847  0.48 41.68 ?  102 LYS   B HD3  1 
ATOM   5524 H HD3  B LYS   B 1 102 ? 43.751 -25.582 13.722  0.52 41.11 ?  102 LYS   B HD3  1 
ATOM   5525 H HE2  A LYS   B 1 102 ? 46.219 -26.109 13.542  0.48 43.31 ?  102 LYS   B HE2  1 
ATOM   5526 H HE2  B LYS   B 1 102 ? 46.025 -26.053 13.502  0.52 42.68 ?  102 LYS   B HE2  1 
ATOM   5527 H HE3  A LYS   B 1 102 ? 45.939 -26.431 12.009  0.48 43.31 ?  102 LYS   B HE3  1 
ATOM   5528 H HE3  B LYS   B 1 102 ? 45.793 -26.446 11.976  0.52 42.68 ?  102 LYS   B HE3  1 
ATOM   5529 H HZ1  A LYS   B 1 102 ? 46.797 -24.335 12.237  0.48 44.25 ?  102 LYS   B HZ1  1 
ATOM   5530 H HZ1  B LYS   B 1 102 ? 46.550 -24.303 12.141  0.52 43.57 ?  102 LYS   B HZ1  1 
ATOM   5531 H HZ2  A LYS   B 1 102 ? 45.453 -24.225 11.708  0.48 44.25 ?  102 LYS   B HZ2  1 
ATOM   5532 H HZ2  B LYS   B 1 102 ? 45.214 -24.277 11.581  0.52 43.57 ?  102 LYS   B HZ2  1 
ATOM   5533 H HZ3  A LYS   B 1 102 ? 45.707 -23.932 13.103  0.48 44.25 ?  102 LYS   B HZ3  1 
ATOM   5534 H HZ3  B LYS   B 1 102 ? 45.425 -23.920 12.969  0.52 43.57 ?  102 LYS   B HZ3  1 
ATOM   5535 N N    A GLY   B 1 103 ? 39.751 -30.005 14.380  0.48 28.09 ?  103 GLY   B N    1 
ATOM   5536 N N    B GLY   B 1 103 ? 39.622 -30.017 14.282  0.52 27.56 ?  103 GLY   B N    1 
ATOM   5537 C CA   A GLY   B 1 103 ? 38.419 -30.039 14.945  0.48 27.98 ?  103 GLY   B CA   1 
ATOM   5538 C CA   B GLY   B 1 103 ? 38.281 -30.078 14.831  0.52 27.28 ?  103 GLY   B CA   1 
ATOM   5539 C C    A GLY   B 1 103 ? 37.483 -28.958 14.452  0.48 27.42 ?  103 GLY   B C    1 
ATOM   5540 C C    B GLY   B 1 103 ? 37.352 -28.967 14.395  0.52 26.44 ?  103 GLY   B C    1 
ATOM   5541 O O    A GLY   B 1 103 ? 36.358 -28.858 14.959  0.48 28.02 ?  103 GLY   B O    1 
ATOM   5542 O O    B GLY   B 1 103 ? 36.278 -28.812 14.988  0.52 27.16 ?  103 GLY   B O    1 
ATOM   5543 H H    A GLY   B 1 103 ? 39.876 -30.575 13.749  0.48 33.69 ?  103 GLY   B H    1 
ATOM   5544 H H    B GLY   B 1 103 ? 39.748 -30.534 13.608  0.52 33.05 ?  103 GLY   B H    1 
ATOM   5545 H HA2  A GLY   B 1 103 ? 38.019 -30.900 14.746  0.48 33.56 ?  103 GLY   B HA2  1 
ATOM   5546 H HA2  B GLY   B 1 103 ? 37.878 -30.921 14.573  0.52 32.71 ?  103 GLY   B HA2  1 
ATOM   5547 H HA3  A GLY   B 1 103 ? 38.487 -29.959 15.910  0.48 33.56 ?  103 GLY   B HA3  1 
ATOM   5548 H HA3  B GLY   B 1 103 ? 38.340 -30.061 15.800  0.52 32.71 ?  103 GLY   B HA3  1 
ATOM   5549 N N    A GLU   B 1 104 ? 37.902 -28.148 13.484  0.48 26.00 ?  104 GLU   B N    1 
ATOM   5550 N N    B GLU   B 1 104 ? 37.721 -28.191 13.381  0.52 24.51 ?  104 GLU   B N    1 
ATOM   5551 C CA   A GLU   B 1 104 ? 37.063 -27.061 13.006  0.48 24.78 ?  104 GLU   B CA   1 
ATOM   5552 C CA   B GLU   B 1 104 ? 36.887 -27.085 12.937  0.52 22.89 ?  104 GLU   B CA   1 
ATOM   5553 C C    A GLU   B 1 104 ? 35.884 -27.604 12.196  0.48 25.24 ?  104 GLU   B C    1 
ATOM   5554 C C    B GLU   B 1 104 ? 35.726 -27.595 12.087  0.52 23.01 ?  104 GLU   B C    1 
ATOM   5555 O O    A GLU   B 1 104 ? 35.926 -28.705 11.638  0.48 25.70 ?  104 GLU   B O    1 
ATOM   5556 O O    B GLU   B 1 104 ? 35.802 -28.656 11.460  0.52 23.77 ?  104 GLU   B O    1 
ATOM   5557 C CB   A GLU   B 1 104 ? 37.900 -26.066 12.200  0.48 23.47 ?  104 GLU   B CB   1 
ATOM   5558 C CB   B GLU   B 1 104 ? 37.735 -26.064 12.175  0.52 21.57 ?  104 GLU   B CB   1 
ATOM   5559 C CG   A GLU   B 1 104 ? 38.998 -25.419 13.040  0.48 22.38 ?  104 GLU   B CG   1 
ATOM   5560 C CG   B GLU   B 1 104 ? 38.840 -25.481 13.047  0.52 20.48 ?  104 GLU   B CG   1 
ATOM   5561 C CD   A GLU   B 1 104 ? 39.938 -24.536 12.242  0.48 21.40 ?  104 GLU   B CD   1 
ATOM   5562 C CD   B GLU   B 1 104 ? 39.815 -24.588 12.310  0.52 19.32 ?  104 GLU   B CD   1 
ATOM   5563 O OE1  A GLU   B 1 104 ? 39.914 -24.584 10.994  0.48 20.14 ?  104 GLU   B OE1  1 
ATOM   5564 O OE1  B GLU   B 1 104 ? 39.814 -24.557 11.061  0.52 18.36 ?  104 GLU   B OE1  1 
ATOM   5565 O OE2  A GLU   B 1 104 ? 40.713 -23.791 12.879  0.48 22.18 -1 104 GLU   B OE2  1 
ATOM   5566 O OE2  B GLU   B 1 104 ? 40.600 -23.915 13.009  0.52 19.47 -1 104 GLU   B OE2  1 
ATOM   5567 H H    A GLU   B 1 104 ? 38.669 -28.204 13.099  0.48 31.18 ?  104 GLU   B H    1 
ATOM   5568 H H    B GLU   B 1 104 ? 38.453 -28.283 12.940  0.52 29.39 ?  104 GLU   B H    1 
ATOM   5569 H HA   A GLU   B 1 104 ? 36.702 -26.589 13.771  0.48 29.71 ?  104 GLU   B HA   1 
ATOM   5570 H HA   B GLU   B 1 104 ? 36.516 -26.641 13.716  0.52 27.45 ?  104 GLU   B HA   1 
ATOM   5571 H HB2  A GLU   B 1 104 ? 38.323 -26.528 11.460  0.48 28.14 ?  104 GLU   B HB2  1 
ATOM   5572 H HB2  B GLU   B 1 104 ? 38.147 -26.498 11.414  0.52 25.86 ?  104 GLU   B HB2  1 
ATOM   5573 H HB3  A GLU   B 1 104 ? 37.323 -25.360 11.868  0.48 28.14 ?  104 GLU   B HB3  1 
ATOM   5574 H HB3  B GLU   B 1 104 ? 37.166 -25.336 11.881  0.52 25.86 ?  104 GLU   B HB3  1 
ATOM   5575 H HG2  A GLU   B 1 104 ? 38.588 -24.872 13.729  0.48 26.83 ?  104 GLU   B HG2  1 
ATOM   5576 H HG2  B GLU   B 1 104 ? 38.437 -24.954 13.755  0.52 24.56 ?  104 GLU   B HG2  1 
ATOM   5577 H HG3  A GLU   B 1 104 ? 39.534 -26.116 13.451  0.48 26.83 ?  104 GLU   B HG3  1 
ATOM   5578 H HG3  B GLU   B 1 104 ? 39.355 -26.206 13.432  0.52 24.56 ?  104 GLU   B HG3  1 
ATOM   5579 N N    A ASP   B 1 105 ? 34.815 -26.811 12.149  0.48 25.33 ?  105 ASP   B N    1 
ATOM   5580 N N    B ASP   B 1 105 ? 34.638 -26.827 12.081  0.52 22.54 ?  105 ASP   B N    1 
ATOM   5581 C CA   A ASP   B 1 105 ? 33.535 -27.262 11.615  0.48 25.78 ?  105 ASP   B CA   1 
ATOM   5582 C CA   B ASP   B 1 105 ? 33.378 -27.296 11.516  0.52 22.78 ?  105 ASP   B CA   1 
ATOM   5583 C C    A ASP   B 1 105 ? 33.576 -27.296 10.091  0.48 24.34 ?  105 ASP   B C    1 
ATOM   5584 C C    B ASP   B 1 105 ? 33.441 -27.314 9.993   0.52 21.08 ?  105 ASP   B C    1 
ATOM   5585 O O    A ASP   B 1 105 ? 33.749 -26.258 9.443   0.48 23.96 ?  105 ASP   B O    1 
ATOM   5586 O O    B ASP   B 1 105 ? 33.574 -26.265 9.355   0.52 19.98 ?  105 ASP   B O    1 
ATOM   5587 C CB   A ASP   B 1 105 ? 32.425 -26.331 12.095  0.48 27.68 ?  105 ASP   B CB   1 
ATOM   5588 C CB   B ASP   B 1 105 ? 32.233 -26.404 11.990  0.52 24.71 ?  105 ASP   B CB   1 
ATOM   5589 C CG   A ASP   B 1 105 ? 31.051 -26.776 11.640  0.48 29.37 ?  105 ASP   B CG   1 
ATOM   5590 C CG   B ASP   B 1 105 ? 30.868 -27.000 11.690  0.52 26.14 ?  105 ASP   B CG   1 
ATOM   5591 O OD1  A ASP   B 1 105 ? 30.931 -27.897 11.102  0.48 29.69 ?  105 ASP   B OD1  1 
ATOM   5592 O OD1  B ASP   B 1 105 ? 30.799 -27.965 10.900  0.52 26.50 ?  105 ASP   B OD1  1 
ATOM   5593 O OD2  A ASP   B 1 105 ? 30.090 -25.997 11.813  0.48 30.38 -1 105 ASP   B OD2  1 
ATOM   5594 O OD2  B ASP   B 1 105 ? 29.865 -26.515 12.255  0.52 26.42 -1 105 ASP   B OD2  1 
ATOM   5595 H H    A ASP   B 1 105 ? 34.808 -25.997 12.428  0.48 30.37 ?  105 ASP   B H    1 
ATOM   5596 H H    B ASP   B 1 105 ? 34.608 -26.028 12.399  0.52 27.02 ?  105 ASP   B H    1 
ATOM   5597 H HA   A ASP   B 1 105 ? 33.349 -28.158 11.938  0.48 30.91 ?  105 ASP   B HA   1 
ATOM   5598 H HA   B ASP   B 1 105 ? 33.206 -28.198 11.821  0.52 27.31 ?  105 ASP   B HA   1 
ATOM   5599 H HB2  A ASP   B 1 105 ? 32.440 -26.296 13.067  0.48 33.19 ?  105 ASP   B HB2  1 
ATOM   5600 H HB2  B ASP   B 1 105 ? 32.302 -26.282 12.950  0.52 29.63 ?  105 ASP   B HB2  1 
ATOM   5601 H HB3  A ASP   B 1 105 ? 32.571 -25.446 11.731  0.48 33.19 ?  105 ASP   B HB3  1 
ATOM   5602 H HB3  B ASP   B 1 105 ? 32.296 -25.542 11.544  0.52 29.63 ?  105 ASP   B HB3  1 
ATOM   5603 N N    A ILE   B 1 106 ? 33.389 -28.491 9.522   0.48 23.72 ?  106 ILE   B N    1 
ATOM   5604 N N    B ILE   B 1 106 ? 33.315 -28.512 9.412   0.52 21.05 ?  106 ILE   B N    1 
ATOM   5605 C CA   A ILE   B 1 106 ? 33.388 -28.665 8.073   0.48 22.81 ?  106 ILE   B CA   1 
ATOM   5606 C CA   B ILE   B 1 106 ? 33.317 -28.669 7.962   0.52 20.48 ?  106 ILE   B CA   1 
ATOM   5607 C C    A ILE   B 1 106 ? 32.289 -27.851 7.399   0.48 21.83 ?  106 ILE   B C    1 
ATOM   5608 C C    B ILE   B 1 106 ? 32.213 -27.851 7.304   0.52 19.46 ?  106 ILE   B C    1 
ATOM   5609 O O    A ILE   B 1 106 ? 32.388 -27.546 6.205   0.48 21.09 ?  106 ILE   B O    1 
ATOM   5610 O O    B ILE   B 1 106 ? 32.303 -27.532 6.113   0.52 17.88 ?  106 ILE   B O    1 
ATOM   5611 C CB   A ILE   B 1 106 ? 33.284 -30.171 7.737   0.48 23.25 ?  106 ILE   B CB   1 
ATOM   5612 C CB   B ILE   B 1 106 ? 33.223 -30.172 7.609   0.52 21.51 ?  106 ILE   B CB   1 
ATOM   5613 C CG1  A ILE   B 1 106 ? 33.507 -30.420 6.244   0.48 23.22 ?  106 ILE   B CG1  1 
ATOM   5614 C CG1  B ILE   B 1 106 ? 33.504 -30.406 6.124   0.52 21.98 ?  106 ILE   B CG1  1 
ATOM   5615 C CG2  A ILE   B 1 106 ? 31.933 -30.728 8.169   0.48 23.86 ?  106 ILE   B CG2  1 
ATOM   5616 C CG2  B ILE   B 1 106 ? 31.855 -30.729 7.982   0.52 22.21 ?  106 ILE   B CG2  1 
ATOM   5617 C CD1  A ILE   B 1 106 ? 34.861 -29.970 5.752   0.48 23.00 ?  106 ILE   B CD1  1 
ATOM   5618 C CD1  B ILE   B 1 106 ? 34.874 -29.947 5.690   0.52 22.08 ?  106 ILE   B CD1  1 
ATOM   5619 H H    A ILE   B 1 106 ? 33.267 -29.218 9.960   0.48 28.44 ?  106 ILE   B H    1 
ATOM   5620 H H    B ILE   B 1 106 ? 33.232 -29.248 9.843   0.52 25.23 ?  106 ILE   B H    1 
ATOM   5621 H HA   A ILE   B 1 106 ? 34.236 -28.345 7.732   0.48 27.35 ?  106 ILE   B HA   1 
ATOM   5622 H HA   B ILE   B 1 106 ? 34.161 -28.337 7.625   0.52 24.55 ?  106 ILE   B HA   1 
ATOM   5623 H HB   A ILE   B 1 106 ? 33.975 -30.641 8.228   0.48 27.88 ?  106 ILE   B HB   1 
ATOM   5624 H HB   B ILE   B 1 106 ? 33.893 -30.649 8.123   0.52 25.78 ?  106 ILE   B HB   1 
ATOM   5625 H HG12 A ILE   B 1 106 ? 33.436 -31.374 6.072   0.48 27.84 ?  106 ILE   B HG12 1 
ATOM   5626 H HG12 B ILE   B 1 106 ? 33.442 -31.357 5.939   0.52 26.35 ?  106 ILE   B HG12 1 
ATOM   5627 H HG13 A ILE   B 1 106 ? 32.833 -29.945 5.737   0.48 27.84 ?  106 ILE   B HG13 1 
ATOM   5628 H HG13 B ILE   B 1 106 ? 32.849 -29.925 5.598   0.52 26.35 ?  106 ILE   B HG13 1 
ATOM   5629 H HG21 A ILE   B 1 106 ? 31.940 -31.692 8.060   0.48 28.61 ?  106 ILE   B HG21 1 
ATOM   5630 H HG21 B ILE   B 1 106 ? 31.876 -31.696 7.906   0.52 26.63 ?  106 ILE   B HG21 1 
ATOM   5631 H HG22 A ILE   B 1 106 ? 31.782 -30.502 9.100   0.48 28.61 ?  106 ILE   B HG22 1 
ATOM   5632 H HG22 B ILE   B 1 106 ? 31.651 -30.475 8.896   0.52 26.63 ?  106 ILE   B HG22 1 
ATOM   5633 H HG23 A ILE   B 1 106 ? 31.237 -30.339 7.617   0.48 28.61 ?  106 ILE   B HG23 1 
ATOM   5634 H HG23 B ILE   B 1 106 ? 31.188 -30.364 7.381   0.52 26.63 ?  106 ILE   B HG23 1 
ATOM   5635 H HD11 A ILE   B 1 106 ? 35.027 -30.361 4.880   0.48 27.58 ?  106 ILE   B HD11 1 
ATOM   5636 H HD11 B ILE   B 1 106 ? 35.086 -30.351 4.835   0.52 26.47 ?  106 ILE   B HD11 1 
ATOM   5637 H HD12 A ILE   B 1 106 ? 34.868 -29.002 5.685   0.48 27.58 ?  106 ILE   B HD12 1 
ATOM   5638 H HD12 B ILE   B 1 106 ? 34.873 -28.980 5.607   0.52 26.47 ?  106 ILE   B HD12 1 
ATOM   5639 H HD13 A ILE   B 1 106 ? 35.540 -30.264 6.380   0.48 27.58 ?  106 ILE   B HD13 1 
ATOM   5640 H HD13 B ILE   B 1 106 ? 35.526 -30.222 6.355   0.52 26.47 ?  106 ILE   B HD13 1 
ATOM   5641 N N    A GLN   B 1 107 ? 31.241 -27.478 8.138   0.48 22.14 ?  107 GLN   B N    1 
ATOM   5642 N N    B GLN   B 1 107 ? 31.174 -27.486 8.056   0.52 20.52 ?  107 GLN   B N    1 
ATOM   5643 C CA   A GLN   B 1 107 ? 30.152 -26.704 7.550   0.48 22.53 ?  107 GLN   B CA   1 
ATOM   5644 C CA   B GLN   B 1 107 ? 30.100 -26.670 7.503   0.52 21.67 ?  107 GLN   B CA   1 
ATOM   5645 C C    A GLN   B 1 107 ? 30.625 -25.358 7.016   0.48 20.56 ?  107 GLN   B C    1 
ATOM   5646 C C    B GLN   B 1 107 ? 30.592 -25.306 7.033   0.52 20.20 ?  107 GLN   B C    1 
ATOM   5647 O O    A GLN   B 1 107 ? 29.990 -24.804 6.114   0.48 20.97 ?  107 GLN   B O    1 
ATOM   5648 O O    B GLN   B 1 107 ? 29.939 -24.686 6.189   0.52 20.92 ?  107 GLN   B O    1 
ATOM   5649 C CB   A GLN   B 1 107 ? 29.042 -26.504 8.586   0.48 25.64 ?  107 GLN   B CB   1 
ATOM   5650 C CB   B GLN   B 1 107 ? 28.985 -26.509 8.541   0.52 25.16 ?  107 GLN   B CB   1 
ATOM   5651 C CG   A GLN   B 1 107 ? 27.724 -25.982 8.020   0.48 28.83 ?  107 GLN   B CG   1 
ATOM   5652 C CG   B GLN   B 1 107 ? 27.658 -26.012 7.981   0.52 28.72 ?  107 GLN   B CG   1 
ATOM   5653 C CD   A GLN   B 1 107 ? 27.682 -24.468 7.910   0.48 31.27 ?  107 GLN   B CD   1 
ATOM   5654 C CD   B GLN   B 1 107 ? 27.556 -24.498 7.955   0.52 31.43 ?  107 GLN   B CD   1 
ATOM   5655 O OE1  A GLN   B 1 107 ? 28.524 -23.767 8.475   0.48 32.23 ?  107 GLN   B OE1  1 
ATOM   5656 O OE1  B GLN   B 1 107 ? 28.386 -23.796 8.535   0.52 32.48 ?  107 GLN   B OE1  1 
ATOM   5657 N NE2  A GLN   B 1 107 ? 26.695 -23.956 7.180   0.48 32.14 ?  107 GLN   B NE2  1 
ATOM   5658 N NE2  B GLN   B 1 107 ? 26.530 -23.986 7.283   0.52 32.42 ?  107 GLN   B NE2  1 
ATOM   5659 H H    A GLN   B 1 107 ? 31.144 -27.652 8.971   0.48 26.55 ?  107 GLN   B H    1 
ATOM   5660 H H    B GLN   B 1 107 ? 31.069 -27.697 8.880   0.52 24.60 ?  107 GLN   B H    1 
ATOM   5661 H HA   A GLN   B 1 107 ? 29.779 -27.205 6.809   0.48 27.01 ?  107 GLN   B HA   1 
ATOM   5662 H HA   B GLN   B 1 107 ? 29.724 -27.129 6.736   0.52 25.99 ?  107 GLN   B HA   1 
ATOM   5663 H HB2  A GLN   B 1 107 ? 28.859 -27.356 9.007   0.48 30.75 ?  107 GLN   B HB2  1 
ATOM   5664 H HB2  B GLN   B 1 107 ? 28.822 -27.370 8.951   0.52 30.16 ?  107 GLN   B HB2  1 
ATOM   5665 H HB3  A GLN   B 1 107 ? 29.350 -25.870 9.251   0.48 30.75 ?  107 GLN   B HB3  1 
ATOM   5666 H HB3  B GLN   B 1 107 ? 29.278 -25.877 9.216   0.52 30.16 ?  107 GLN   B HB3  1 
ATOM   5667 H HG2  A GLN   B 1 107 ? 27.592 -26.347 7.132   0.48 34.57 ?  107 GLN   B HG2  1 
ATOM   5668 H HG2  B GLN   B 1 107 ? 27.556 -26.332 7.071   0.52 34.44 ?  107 GLN   B HG2  1 
ATOM   5669 H HG3  A GLN   B 1 107 ? 26.998 -26.262 8.603   0.48 34.57 ?  107 GLN   B HG3  1 
ATOM   5670 H HG3  B GLN   B 1 107 ? 26.934 -26.354 8.533   0.52 34.44 ?  107 GLN   B HG3  1 
ATOM   5671 H HE21 A GLN   B 1 107 ? 26.126 -24.478 6.798   0.48 38.54 ?  107 GLN   B HE21 1 
ATOM   5672 H HE21 B GLN   B 1 107 ? 25.970 -24.507 6.888   0.52 38.88 ?  107 GLN   B HE21 1 
ATOM   5673 H HE22 A GLN   B 1 107 ? 26.622 -23.104 7.089   0.48 38.54 ?  107 GLN   B HE22 1 
ATOM   5674 H HE22 B GLN   B 1 107 ? 26.425 -23.133 7.241   0.52 38.88 ?  107 GLN   B HE22 1 
ATOM   5675 N N    . LEU   B 1 108 ? 31.732 -24.830 7.540   1.00 18.49 ?  108 LEU   B N    1 
ATOM   5676 C CA   . LEU   B 1 108 ? 32.274 -23.538 7.122   1.00 16.42 ?  108 LEU   B CA   1 
ATOM   5677 C C    . LEU   B 1 108 ? 32.928 -23.568 5.749   1.00 14.58 ?  108 LEU   B C    1 
ATOM   5678 O O    . LEU   B 1 108 ? 33.362 -22.514 5.260   1.00 14.21 ?  108 LEU   B O    1 
ATOM   5679 C CB   . LEU   B 1 108 ? 33.281 -23.044 8.157   1.00 17.14 ?  108 LEU   B CB   1 
ATOM   5680 C CG   . LEU   B 1 108 ? 32.672 -22.661 9.502   1.00 18.45 ?  108 LEU   B CG   1 
ATOM   5681 C CD1  . LEU   B 1 108 ? 33.738 -22.547 10.577  1.00 18.50 ?  108 LEU   B CD1  1 
ATOM   5682 C CD2  . LEU   B 1 108 ? 31.917 -21.350 9.364   1.00 20.19 ?  108 LEU   B CD2  1 
ATOM   5683 H H    A LEU   B 1 108 ? 32.188 -25.207 8.164   0.48 22.17 ?  108 LEU   B H    1 
ATOM   5684 H H    B LEU   B 1 108 ? 32.203 -25.234 8.136   0.52 22.17 ?  108 LEU   B H    1 
ATOM   5685 H HA   . LEU   B 1 108 ? 31.547 -22.898 7.086   1.00 19.68 ?  108 LEU   B HA   1 
ATOM   5686 H HB2  . LEU   B 1 108 ? 33.928 -23.743 8.320   1.00 20.55 ?  108 LEU   B HB2  1 
ATOM   5687 H HB3  . LEU   B 1 108 ? 33.726 -22.258 7.805   1.00 20.55 ?  108 LEU   B HB3  1 
ATOM   5688 H HG   . LEU   B 1 108 ? 32.037 -23.344 9.776   1.00 22.12 ?  108 LEU   B HG   1 
ATOM   5689 H HD11 . LEU   B 1 108 ? 33.313 -22.345 11.427  1.00 22.17 ?  108 LEU   B HD11 1 
ATOM   5690 H HD12 . LEU   B 1 108 ? 34.215 -23.389 10.639  1.00 22.17 ?  108 LEU   B HD12 1 
ATOM   5691 H HD13 . LEU   B 1 108 ? 34.352 -21.834 10.339  1.00 22.17 ?  108 LEU   B HD13 1 
ATOM   5692 H HD21 . LEU   B 1 108 ? 31.617 -21.063 10.241  1.00 24.20 ?  108 LEU   B HD21 1 
ATOM   5693 H HD22 . LEU   B 1 108 ? 32.510 -20.684 8.983   1.00 24.20 ?  108 LEU   B HD22 1 
ATOM   5694 H HD23 . LEU   B 1 108 ? 31.152 -21.484 8.782   1.00 24.20 ?  108 LEU   B HD23 1 
ATOM   5695 N N    . LEU   B 1 109 ? 32.998 -24.739 5.122   1.00 13.68 ?  109 LEU   B N    1 
ATOM   5696 C CA   . LEU   B 1 109 ? 33.638 -24.847 3.820   1.00 13.19 ?  109 LEU   B CA   1 
ATOM   5697 C C    . LEU   B 1 109 ? 32.875 -24.066 2.755   1.00 12.21 ?  109 LEU   B C    1 
ATOM   5698 O O    . LEU   B 1 109 ? 33.493 -23.471 1.864   1.00 12.01 ?  109 LEU   B O    1 
ATOM   5699 C CB   . LEU   B 1 109 ? 33.772 -26.322 3.447   1.00 13.07 ?  109 LEU   B CB   1 
ATOM   5700 C CG   . LEU   B 1 109 ? 34.548 -26.647 2.177   1.00 12.58 ?  109 LEU   B CG   1 
ATOM   5701 C CD1  . LEU   B 1 109 ? 35.935 -26.015 2.186   1.00 12.73 ?  109 LEU   B CD1  1 
ATOM   5702 C CD2  . LEU   B 1 109 ? 34.666 -28.153 2.026   1.00 13.66 ?  109 LEU   B CD2  1 
ATOM   5703 H H    . LEU   B 1 109 ? 32.690 -25.481 5.426   1.00 16.39 ?  109 LEU   B H    1 
ATOM   5704 H HA   . LEU   B 1 109 ? 34.527 -24.472 3.875   1.00 15.80 ?  109 LEU   B HA   1 
ATOM   5705 H HB2  . LEU   B 1 109 ? 34.223 -26.776 4.177   1.00 15.66 ?  109 LEU   B HB2  1 
ATOM   5706 H HB3  . LEU   B 1 109 ? 32.884 -26.693 3.340   1.00 15.66 ?  109 LEU   B HB3  1 
ATOM   5707 H HG   . LEU   B 1 109 ? 34.065 -26.310 1.406   1.00 15.07 ?  109 LEU   B HG   1 
ATOM   5708 H HD11 . LEU   B 1 109 ? 36.447 -26.360 1.433   1.00 15.25 ?  109 LEU   B HD11 1 
ATOM   5709 H HD12 . LEU   B 1 109 ? 35.846 -25.055 2.108   1.00 15.25 ?  109 LEU   B HD12 1 
ATOM   5710 H HD13 . LEU   B 1 109 ? 36.382 -26.244 3.016   1.00 15.25 ?  109 LEU   B HD13 1 
ATOM   5711 H HD21 . LEU   B 1 109 ? 35.228 -28.352 1.260   1.00 16.37 ?  109 LEU   B HD21 1 
ATOM   5712 H HD22 . LEU   B 1 109 ? 35.060 -28.521 2.830   1.00 16.37 ?  109 LEU   B HD22 1 
ATOM   5713 H HD23 . LEU   B 1 109 ? 33.780 -28.527 1.890   1.00 16.37 ?  109 LEU   B HD23 1 
ATOM   5714 N N    . LYS   B 1 110 ? 31.541 -24.030 2.827   1.00 12.42 ?  110 LYS   B N    1 
ATOM   5715 C CA   . LYS   B 1 110 ? 30.788 -23.265 1.838   1.00 12.35 ?  110 LYS   B CA   1 
ATOM   5716 C C    . LYS   B 1 110 ? 31.125 -21.779 1.931   1.00 11.93 ?  110 LYS   B C    1 
ATOM   5717 O O    . LYS   B 1 110 ? 31.382 -21.126 0.915   1.00 11.53 ?  110 LYS   B O    1 
ATOM   5718 C CB   . LYS   B 1 110 ? 29.281 -23.510 1.985   1.00 12.95 ?  110 LYS   B CB   1 
ATOM   5719 C CG   . LYS   B 1 110 ? 28.471 -22.880 0.857   1.00 13.35 ?  110 LYS   B CG   1 
ATOM   5720 C CD   . LYS   B 1 110 ? 27.018 -23.322 0.867   1.00 13.74 ?  110 LYS   B CD   1 
ATOM   5721 C CE   . LYS   B 1 110 ? 26.256 -22.800 -0.351  1.00 14.21 ?  110 LYS   B CE   1 
ATOM   5722 N NZ   . LYS   B 1 110 ? 26.597 -23.515 -1.607  1.00 14.51 ?  110 LYS   B NZ   1 
ATOM   5723 H H    . LYS   B 1 110 ? 31.063 -24.435 3.414   1.00 14.89 ?  110 LYS   B H    1 
ATOM   5724 H HA   . LYS   B 1 110 ? 31.044 -23.565 0.951   1.00 14.79 ?  110 LYS   B HA   1 
ATOM   5725 H HB2  . LYS   B 1 110 ? 29.113 -24.469 1.973   1.00 15.52 ?  110 LYS   B HB2  1 
ATOM   5726 H HB3  . LYS   B 1 110 ? 28.975 -23.133 2.823   1.00 15.52 ?  110 LYS   B HB3  1 
ATOM   5727 H HG2  . LYS   B 1 110 ? 28.480 -21.915 0.955   1.00 16.00 ?  110 LYS   B HG2  1 
ATOM   5728 H HG3  . LYS   B 1 110 ? 28.848 -23.134 0.004   1.00 16.00 ?  110 LYS   B HG3  1 
ATOM   5729 H HD2  . LYS   B 1 110 ? 26.974 -24.297 0.855   1.00 16.46 ?  110 LYS   B HD2  1 
ATOM   5730 H HD3  . LYS   B 1 110 ? 26.576 -22.986 1.665   1.00 16.46 ?  110 LYS   B HD3  1 
ATOM   5731 H HE2  . LYS   B 1 110 ? 25.302 -22.910 -0.199  1.00 17.03 ?  110 LYS   B HE2  1 
ATOM   5732 H HE3  . LYS   B 1 110 ? 26.467 -21.866 -0.472  1.00 17.03 ?  110 LYS   B HE3  1 
ATOM   5733 H HZ1  . LYS   B 1 110 ? 26.135 -23.179 -2.286  1.00 17.39 ?  110 LYS   B HZ1  1 
ATOM   5734 H HZ2  . LYS   B 1 110 ? 27.468 -23.430 -1.777  1.00 17.39 ?  110 LYS   B HZ2  1 
ATOM   5735 H HZ3  . LYS   B 1 110 ? 26.405 -24.383 -1.527  1.00 17.39 ?  110 LYS   B HZ3  1 
ATOM   5736 N N    . SER   B 1 111 ? 31.147 -21.229 3.151   1.00 12.26 ?  111 SER   B N    1 
ATOM   5737 C CA   . SER   B 1 111 ? 31.539 -19.832 3.331   1.00 12.26 ?  111 SER   B CA   1 
ATOM   5738 C C    . SER   B 1 111 ? 32.924 -19.570 2.747   1.00 11.57 ?  111 SER   B C    1 
ATOM   5739 O O    . SER   B 1 111 ? 33.155 -18.530 2.114   1.00 11.78 ?  111 SER   B O    1 
ATOM   5740 C CB   . SER   B 1 111 ? 31.522 -19.475 4.816   1.00 13.76 ?  111 SER   B CB   1 
ATOM   5741 O OG   . SER   B 1 111 ? 30.210 -19.512 5.342   1.00 15.46 ?  111 SER   B OG   1 
ATOM   5742 H H    . SER   B 1 111 ? 30.953 -21.647 3.877   1.00 14.69 ?  111 SER   B H    1 
ATOM   5743 H HA   . SER   B 1 111 ? 30.906 -19.264 2.874   1.00 14.69 ?  111 SER   B HA   1 
ATOM   5744 H HB2  . SER   B 1 111 ? 32.068 -20.114 5.302   1.00 16.49 ?  111 SER   B HB2  1 
ATOM   5745 H HB3  . SER   B 1 111 ? 31.875 -18.583 4.931   1.00 16.49 ?  111 SER   B HB3  1 
ATOM   5746 H HG   . SER   B 1 111 ? 30.219 -19.317 6.164   1.00 18.53 ?  111 SER   B HG   1 
ATOM   5747 N N    . ALA   B 1 112 ? 33.863 -20.491 2.967   1.00 11.63 ?  112 ALA   B N    1 
ATOM   5748 C CA   . ALA   B 1 112 ? 35.208 -20.319 2.432   1.00 11.41 ?  112 ALA   B CA   1 
ATOM   5749 C C    . ALA   B 1 112 ? 35.182 -20.218 0.910   1.00 10.86 ?  112 ALA   B C    1 
ATOM   5750 O O    . ALA   B 1 112 ? 35.814 -19.327 0.323   1.00 11.07 ?  112 ALA   B O    1 
ATOM   5751 C CB   . ALA   B 1 112 ? 36.105 -21.466 2.909   1.00 11.98 ?  112 ALA   B CB   1 
ATOM   5752 H H    . ALA   B 1 112 ? 33.744 -21.219 3.418   1.00 13.93 ?  112 ALA   B H    1 
ATOM   5753 H HA   . ALA   B 1 112 ? 35.577 -19.494 2.778   1.00 13.67 ?  112 ALA   B HA   1 
ATOM   5754 H HB1  . ALA   B 1 112 ? 37.000 -21.336 2.551   1.00 14.36 ?  112 ALA   B HB1  1 
ATOM   5755 H HB2  . ALA   B 1 112 ? 36.139 -21.460 3.881   1.00 14.36 ?  112 ALA   B HB2  1 
ATOM   5756 H HB3  . ALA   B 1 112 ? 35.744 -22.308 2.596   1.00 14.36 ?  112 ALA   B HB3  1 
ATOM   5757 N N    . TYR   B 1 113 ? 34.453 -21.121 0.246   1.00 10.86 ?  113 TYR   B N    1 
ATOM   5758 C CA   . TYR   B 1 113 ? 34.375 -21.068 -1.208  1.00 10.43 ?  113 TYR   B CA   1 
ATOM   5759 C C    . TYR   B 1 113 ? 33.672 -19.816 -1.720  1.00 10.50 ?  113 TYR   B C    1 
ATOM   5760 O O    . TYR   B 1 113 ? 33.943 -19.386 -2.843  1.00 10.49 ?  113 TYR   B O    1 
ATOM   5761 C CB   . TYR   B 1 113 ? 33.705 -22.330 -1.764  1.00 10.90 ?  113 TYR   B CB   1 
ATOM   5762 C CG   . TYR   B 1 113 ? 34.661 -23.479 -2.022  1.00 10.93 ?  113 TYR   B CG   1 
ATOM   5763 C CD1  . TYR   B 1 113 ? 35.651 -23.374 -2.988  1.00 11.35 ?  113 TYR   B CD1  1 
ATOM   5764 C CD2  . TYR   B 1 113 ? 34.555 -24.669 -1.318  1.00 11.20 ?  113 TYR   B CD2  1 
ATOM   5765 C CE1  . TYR   B 1 113 ? 36.528 -24.402 -3.233  1.00 11.50 ?  113 TYR   B CE1  1 
ATOM   5766 C CE2  . TYR   B 1 113 ? 35.425 -25.720 -1.558  1.00 11.29 ?  113 TYR   B CE2  1 
ATOM   5767 C CZ   . TYR   B 1 113 ? 36.410 -25.581 -2.522  1.00 11.24 ?  113 TYR   B CZ   1 
ATOM   5768 O OH   . TYR   B 1 113 ? 37.294 -26.597 -2.804  1.00 11.90 ?  113 TYR   B OH   1 
ATOM   5769 H H    . TYR   B 1 113 ? 34.003 -21.761 0.612   1.00 13.01 ?  113 TYR   B H    1 
ATOM   5770 H HA   . TYR   B 1 113 ? 35.278 -21.052 -1.553  1.00 12.50 ?  113 TYR   B HA   1 
ATOM   5771 H HB2  . TYR   B 1 113 ? 33.039 -22.640 -1.124  1.00 13.05 ?  113 TYR   B HB2  1 
ATOM   5772 H HB3  . TYR   B 1 113 ? 33.270 -22.110 -2.602  1.00 13.05 ?  113 TYR   B HB3  1 
ATOM   5773 H HD1  . TYR   B 1 113 ? 35.734 -22.580 -3.470  1.00 13.60 ?  113 TYR   B HD1  1 
ATOM   5774 H HD2  . TYR   B 1 113 ? 33.891 -24.761 -0.675  1.00 13.42 ?  113 TYR   B HD2  1 
ATOM   5775 H HE1  . TYR   B 1 113 ? 37.184 -24.314 -3.888  1.00 13.78 ?  113 TYR   B HE1  1 
ATOM   5776 H HE2  . TYR   B 1 113 ? 35.339 -26.515 -1.082  1.00 13.53 ?  113 TYR   B HE2  1 
ATOM   5777 H HH   . TYR   B 1 113 ? 37.123 -27.265 -2.318  1.00 14.25 ?  113 TYR   B HH   1 
ATOM   5778 N N    . GLU   B 1 114 ? 32.745 -19.242 -0.944  1.00 10.51 ?  114 GLU   B N    1 
ATOM   5779 C CA   . GLU   B 1 114 ? 32.067 -18.033 -1.398  1.00 10.50 ?  114 GLU   B CA   1 
ATOM   5780 C C    . GLU   B 1 114 ? 33.050 -16.908 -1.687  1.00 10.32 ?  114 GLU   B C    1 
ATOM   5781 O O    . GLU   B 1 114 ? 32.769 -16.041 -2.518  1.00 10.64 ?  114 GLU   B O    1 
ATOM   5782 C CB   . GLU   B 1 114 ? 31.003 -17.607 -0.386  1.00 11.20 ?  114 GLU   B CB   1 
ATOM   5783 C CG   . GLU   B 1 114 ? 29.780 -18.531 -0.453  1.00 11.46 ?  114 GLU   B CG   1 
ATOM   5784 C CD   . GLU   B 1 114 ? 28.760 -18.345 0.654   1.00 11.33 ?  114 GLU   B CD   1 
ATOM   5785 O OE1  . GLU   B 1 114 ? 29.056 -17.728 1.699   1.00 11.78 ?  114 GLU   B OE1  1 
ATOM   5786 O OE2  . GLU   B 1 114 ? 27.632 -18.869 0.482   1.00 12.24 -1 114 GLU   B OE2  1 
ATOM   5787 H H    . GLU   B 1 114 ? 32.490 -19.539 -0.174  1.00 12.59 ?  114 GLU   B H    1 
ATOM   5788 H HA   . GLU   B 1 114 ? 31.612 -18.230 -2.225  1.00 12.58 ?  114 GLU   B HA   1 
ATOM   5789 H HB2  . GLU   B 1 114 ? 31.369 -17.654 0.511   1.00 13.41 ?  114 GLU   B HB2  1 
ATOM   5790 H HB3  . GLU   B 1 114 ? 30.710 -16.706 -0.585  1.00 13.41 ?  114 GLU   B HB3  1 
ATOM   5791 H HG2  . GLU   B 1 114 ? 29.328 -18.380 -1.294  1.00 13.72 ?  114 GLU   B HG2  1 
ATOM   5792 H HG3  . GLU   B 1 114 ? 30.091 -19.451 -0.411  1.00 13.72 ?  114 GLU   B HG3  1 
ATOM   5793 N N    . ASN   B 1 115 ? 34.211 -16.901 -1.028  1.00 10.35 ?  115 ASN   B N    1 
ATOM   5794 C CA   . ASN   B 1 115 ? 35.204 -15.870 -1.326  1.00 10.27 ?  115 ASN   B CA   1 
ATOM   5795 C C    . ASN   B 1 115 ? 35.617 -15.891 -2.789  1.00 10.24 ?  115 ASN   B C    1 
ATOM   5796 O O    . ASN   B 1 115 ? 36.002 -14.848 -3.342  1.00 10.52 ?  115 ASN   B O    1 
ATOM   5797 C CB   . ASN   B 1 115 ? 36.444 -16.055 -0.448  1.00 11.24 ?  115 ASN   B CB   1 
ATOM   5798 C CG   . ASN   B 1 115 ? 36.177 -15.794 1.018   1.00 11.74 ?  115 ASN   B CG   1 
ATOM   5799 O OD1  . ASN   B 1 115 ? 36.172 -14.647 1.466   1.00 13.14 ?  115 ASN   B OD1  1 
ATOM   5800 N ND2  . ASN   B 1 115 ? 36.013 -16.865 1.786   1.00 11.54 ?  115 ASN   B ND2  1 
ATOM   5801 H H    . ASN   B 1 115 ? 34.443 -17.455 -0.409  1.00 12.39 ?  115 ASN   B H    1 
ATOM   5802 H HA   . ASN   B 1 115 ? 34.833 -14.993 -1.129  1.00 12.30 ?  115 ASN   B HA   1 
ATOM   5803 H HB2  . ASN   B 1 115 ? 36.762 -16.970 -0.539  1.00 13.46 ?  115 ASN   B HB2  1 
ATOM   5804 H HB3  . ASN   B 1 115 ? 37.138 -15.440 -0.740  1.00 13.46 ?  115 ASN   B HB3  1 
ATOM   5805 H HD21 . ASN   B 1 115 ? 35.869 -16.772 2.627   1.00 13.83 ?  115 ASN   B HD21 1 
ATOM   5806 H HD22 . ASN   B 1 115 ? 36.036 -17.655 1.439   1.00 13.83 ?  115 ASN   B HD22 1 
ATOM   5807 N N    . PHE   B 1 116 ? 35.587 -17.070 -3.424  1.00 9.72  ?  116 PHE   B N    1 
ATOM   5808 C CA   . PHE   B 1 116 ? 36.021 -17.160 -4.812  1.00 10.04 ?  116 PHE   B CA   1 
ATOM   5809 C C    . PHE   B 1 116 ? 35.125 -16.331 -5.722  1.00 9.90  ?  116 PHE   B C    1 
ATOM   5810 O O    . PHE   B 1 116 ? 35.560 -15.908 -6.799  1.00 10.37 ?  116 PHE   B O    1 
ATOM   5811 C CB   . PHE   B 1 116 ? 35.990 -18.605 -5.336  1.00 10.36 ?  116 PHE   B CB   1 
ATOM   5812 C CG   . PHE   B 1 116 ? 37.061 -19.559 -4.794  1.00 9.89  ?  116 PHE   B CG   1 
ATOM   5813 C CD1  . PHE   B 1 116 ? 37.716 -19.377 -3.584  1.00 10.53 ?  116 PHE   B CD1  1 
ATOM   5814 C CD2  . PHE   B 1 116 ? 37.364 -20.696 -5.532  1.00 10.34 ?  116 PHE   B CD2  1 
ATOM   5815 C CE1  . PHE   B 1 116 ? 38.654 -20.312 -3.134  1.00 10.64 ?  116 PHE   B CE1  1 
ATOM   5816 C CE2  . PHE   B 1 116 ? 38.297 -21.627 -5.088  1.00 10.42 ?  116 PHE   B CE2  1 
ATOM   5817 C CZ   . PHE   B 1 116 ? 38.938 -21.438 -3.891  1.00 10.23 ?  116 PHE   B CZ   1 
ATOM   5818 H H    . PHE   B 1 116 ? 35.317 -17.814 -3.079  1.00 11.64 ?  116 PHE   B H    1 
ATOM   5819 H HA   . PHE   B 1 116 ? 36.926 -16.829 -4.888  1.00 12.02 ?  116 PHE   B HA   1 
ATOM   5820 H HB2  . PHE   B 1 116 ? 35.124 -18.990 -5.114  1.00 12.41 ?  116 PHE   B HB2  1 
ATOM   5821 H HB3  . PHE   B 1 116 ? 36.086 -18.579 -6.301  1.00 12.41 ?  116 PHE   B HB3  1 
ATOM   5822 H HD1  . PHE   B 1 116 ? 37.522 -18.623 -3.067  1.00 12.62 ?  116 PHE   B HD1  1 
ATOM   5823 H HD2  . PHE   B 1 116 ? 36.925 -20.846 -6.339  1.00 12.38 ?  116 PHE   B HD2  1 
ATOM   5824 H HE1  . PHE   B 1 116 ? 39.093 -20.169 -2.325  1.00 12.75 ?  116 PHE   B HE1  1 
ATOM   5825 H HE2  . PHE   B 1 116 ? 38.486 -22.379 -5.601  1.00 12.48 ?  116 PHE   B HE2  1 
ATOM   5826 H HZ   . PHE   B 1 116 ? 39.574 -22.046 -3.594  1.00 12.26 ?  116 PHE   B HZ   1 
ATOM   5827 N N    . ASN   B 1 117 ? 33.854 -16.138 -5.341  1.00 10.47 ?  117 ASN   B N    1 
ATOM   5828 C CA   . ASN   B 1 117 ? 32.915 -15.438 -6.217  1.00 10.36 ?  117 ASN   B CA   1 
ATOM   5829 C C    . ASN   B 1 117 ? 33.229 -13.960 -6.375  1.00 11.09 ?  117 ASN   B C    1 
ATOM   5830 O O    . ASN   B 1 117 ? 32.636 -13.309 -7.241  1.00 12.11 ?  117 ASN   B O    1 
ATOM   5831 C CB   . ASN   B 1 117 ? 31.487 -15.657 -5.742  1.00 10.68 ?  117 ASN   B CB   1 
ATOM   5832 C CG   . ASN   B 1 117 ? 31.037 -17.068 -5.999  1.00 10.88 ?  117 ASN   B CG   1 
ATOM   5833 O OD1  . ASN   B 1 117 ? 31.396 -17.657 -7.023  1.00 11.73 ?  117 ASN   B OD1  1 
ATOM   5834 N ND2  . ASN   B 1 117 ? 30.304 -17.642 -5.061  1.00 10.79 ?  117 ASN   B ND2  1 
ATOM   5835 H H    . ASN   B 1 117 ? 33.521 -16.397 -4.587  1.00 12.55 ?  117 ASN   B H    1 
ATOM   5836 H HA   . ASN   B 1 117 ? 32.986 -15.837 -7.095  1.00 12.41 ?  117 ASN   B HA   1 
ATOM   5837 H HB2  . ASN   B 1 117 ? 31.436 -15.491 -4.785  1.00 12.79 ?  117 ASN   B HB2  1 
ATOM   5838 H HB3  . ASN   B 1 117 ? 30.897 -15.047 -6.216  1.00 12.79 ?  117 ASN   B HB3  1 
ATOM   5839 H HD21 . ASN   B 1 117 ? 30.024 -18.448 -5.170  1.00 12.93 ?  117 ASN   B HD21 1 
ATOM   5840 H HD22 . ASN   B 1 117 ? 30.082 -17.202 -4.357  1.00 12.93 ?  117 ASN   B HD22 1 
ATOM   5841 N N    . GLN   B 1 118 ? 34.155 -13.427 -5.588  1.00 10.69 ?  118 GLN   B N    1 
ATOM   5842 C CA   . GLN   B 1 118 ? 34.578 -12.039 -5.727  1.00 11.12 ?  118 GLN   B CA   1 
ATOM   5843 C C    . GLN   B 1 118 ? 35.651 -11.847 -6.795  1.00 11.42 ?  118 GLN   B C    1 
ATOM   5844 O O    . GLN   B 1 118 ? 36.122 -10.718 -6.977  1.00 12.73 ?  118 GLN   B O    1 
ATOM   5845 C CB   . GLN   B 1 118 ? 35.054 -11.504 -4.376  1.00 11.85 ?  118 GLN   B CB   1 
ATOM   5846 C CG   . GLN   B 1 118 ? 33.975 -11.540 -3.310  1.00 12.12 ?  118 GLN   B CG   1 
ATOM   5847 C CD   . GLN   B 1 118 ? 32.800 -10.638 -3.642  1.00 12.08 ?  118 GLN   B CD   1 
ATOM   5848 O OE1  . GLN   B 1 118 ? 32.978 -9.499  -4.090  1.00 12.48 ?  118 GLN   B OE1  1 
ATOM   5849 N NE2  . GLN   B 1 118 ? 31.588 -11.137 -3.426  1.00 11.99 ?  118 GLN   B NE2  1 
ATOM   5850 H H    . GLN   B 1 118 ? 34.571 -13.848 -4.960  1.00 12.80 ?  118 GLN   B H    1 
ATOM   5851 H HA   . GLN   B 1 118 ? 33.813 -11.510 -5.997  1.00 13.32 ?  118 GLN   B HA   1 
ATOM   5852 H HB2  . GLN   B 1 118 ? 35.800 -12.037 -4.065  1.00 14.20 ?  118 GLN   B HB2  1 
ATOM   5853 H HB3  . GLN   B 1 118 ? 35.335 -10.576 -4.481  1.00 14.20 ?  118 GLN   B HB3  1 
ATOM   5854 H HG2  . GLN   B 1 118 ? 33.645 -12.448 -3.224  1.00 14.52 ?  118 GLN   B HG2  1 
ATOM   5855 H HG3  . GLN   B 1 118 ? 34.351 -11.244 -2.465  1.00 14.52 ?  118 GLN   B HG3  1 
ATOM   5856 H HE21 . GLN   B 1 118 ? 31.504 -11.936 -3.115  1.00 14.36 ?  118 GLN   B HE21 1 
ATOM   5857 H HE22 . GLN   B 1 118 ? 30.899 -10.665 -3.601  1.00 14.36 ?  118 GLN   B HE22 1 
ATOM   5858 N N    . HIS   B 1 119 ? 36.021 -12.908 -7.520  1.00 10.48 ?  119 HIS   B N    1 
ATOM   5859 C CA   . HIS   B 1 119 ? 37.061 -12.864 -8.541  1.00 10.90 ?  119 HIS   B CA   1 
ATOM   5860 C C    . HIS   B 1 119 ? 36.583 -13.596 -9.781  1.00 11.05 ?  119 HIS   B C    1 
ATOM   5861 O O    . HIS   B 1 119 ? 36.079 -14.716 -9.681  1.00 11.63 ?  119 HIS   B O    1 
ATOM   5862 C CB   . HIS   B 1 119 ? 38.347 -13.483 -7.999  1.00 11.66 ?  119 HIS   B CB   1 
ATOM   5863 C CG   . HIS   B 1 119 ? 38.823 -12.778 -6.777  1.00 12.69 ?  119 HIS   B CG   1 
ATOM   5864 N ND1  . HIS   B 1 119 ? 39.613 -11.651 -6.833  1.00 14.23 ?  119 HIS   B ND1  1 
ATOM   5865 C CD2  . HIS   B 1 119 ? 38.525 -12.969 -5.471  1.00 14.25 ?  119 HIS   B CD2  1 
ATOM   5866 C CE1  . HIS   B 1 119 ? 39.815 -11.204 -5.608  1.00 15.69 ?  119 HIS   B CE1  1 
ATOM   5867 N NE2  . HIS   B 1 119 ? 39.160 -11.979 -4.764  1.00 15.80 ?  119 HIS   B NE2  1 
ATOM   5868 H H    . HIS   B 1 119 ? 35.663 -13.688 -7.442  1.00 12.56 ?  119 HIS   B H    1 
ATOM   5869 H HA   . HIS   B 1 119 ? 37.240 -11.937 -8.784  1.00 13.06 ?  119 HIS   B HA   1 
ATOM   5870 H HB2  . HIS   B 1 119 ? 38.184 -14.412 -7.776  1.00 13.96 ?  119 HIS   B HB2  1 
ATOM   5871 H HB3  . HIS   B 1 119 ? 39.042 -13.421 -8.679  1.00 13.96 ?  119 HIS   B HB3  1 
ATOM   5872 H HD2  . HIS   B 1 119 ? 37.989 -13.647 -5.125  1.00 17.07 ?  119 HIS   B HD2  1 
ATOM   5873 H HE1  . HIS   B 1 119 ? 40.345 -10.479 -5.377  1.00 18.80 ?  119 HIS   B HE1  1 
ATOM   5874 H HE2  . HIS   B 1 119 ? 39.158 -11.901 -3.909  1.00 18.94 ?  119 HIS   B HE2  1 
ATOM   5875 N N    . GLU   B 1 120 ? 36.737 -12.976 -10.951 1.00 11.62 ?  120 GLU   B N    1 
ATOM   5876 C CA   . GLU   B 1 120 ? 36.149 -13.562 -12.153 1.00 13.01 ?  120 GLU   B CA   1 
ATOM   5877 C C    . GLU   B 1 120 ? 36.827 -14.867 -12.562 1.00 11.95 ?  120 GLU   B C    1 
ATOM   5878 O O    . GLU   B 1 120 ? 36.170 -15.745 -13.136 1.00 12.01 ?  120 GLU   B O    1 
ATOM   5879 C CB   . GLU   B 1 120 ? 36.174 -12.560 -13.305 1.00 17.49 ?  120 GLU   B CB   1 
ATOM   5880 C CG   . GLU   B 1 120 ? 35.212 -11.404 -13.118 1.00 23.86 ?  120 GLU   B CG   1 
ATOM   5881 C CD   . GLU   B 1 120 ? 35.095 -10.527 -14.349 1.00 29.98 ?  120 GLU   B CD   1 
ATOM   5882 O OE1  . GLU   B 1 120 ? 36.120 -10.312 -15.029 1.00 32.22 ?  120 GLU   B OE1  1 
ATOM   5883 O OE2  . GLU   B 1 120 ? 33.973 -10.062 -14.639 1.00 32.82 -1 120 GLU   B OE2  1 
ATOM   5884 H H    . GLU   B 1 120 ? 37.157 -12.234 -11.076 1.00 13.92 ?  120 GLU   B H    1 
ATOM   5885 H HA   . GLU   B 1 120 ? 35.220 -13.768 -11.971 1.00 15.58 ?  120 GLU   B HA   1 
ATOM   5886 H HB2  . GLU   B 1 120 ? 37.066 -12.194 -13.388 1.00 20.97 ?  120 GLU   B HB2  1 
ATOM   5887 H HB3  . GLU   B 1 120 ? 35.927 -13.019 -14.126 1.00 20.97 ?  120 GLU   B HB3  1 
ATOM   5888 H HG2  . GLU   B 1 120 ? 34.328 -11.754 -12.932 1.00 28.61 ?  120 GLU   B HG2  1 
ATOM   5889 H HG3  . GLU   B 1 120 ? 35.518 -10.858 -12.378 1.00 28.61 ?  120 GLU   B HG3  1 
ATOM   5890 N N    . VAL   B 1 121 ? 38.125 -15.008 -12.295 1.00 11.53 ?  121 VAL   B N    1 
ATOM   5891 C CA   . VAL   B 1 121 ? 38.873 -16.215 -12.641 1.00 11.54 ?  121 VAL   B CA   1 
ATOM   5892 C C    . VAL   B 1 121 ? 39.984 -16.418 -11.617 1.00 10.92 ?  121 VAL   B C    1 
ATOM   5893 O O    . VAL   B 1 121 ? 40.667 -15.460 -11.227 1.00 11.47 ?  121 VAL   B O    1 
ATOM   5894 C CB   . VAL   B 1 121 ? 39.398 -16.170 -14.095 1.00 12.80 ?  121 VAL   B CB   1 
ATOM   5895 C CG1  . VAL   B 1 121 ? 40.269 -14.946 -14.342 1.00 14.02 ?  121 VAL   B CG1  1 
ATOM   5896 C CG2  . VAL   B 1 121 ? 40.139 -17.457 -14.440 1.00 14.54 ?  121 VAL   B CG2  1 
ATOM   5897 H H    . VAL   B 1 121 ? 38.605 -14.403 -11.914 1.00 13.82 ?  121 VAL   B H    1 
ATOM   5898 H HA   . VAL   B 1 121 ? 38.265 -16.969 -12.578 1.00 13.82 ?  121 VAL   B HA   1 
ATOM   5899 H HB   . VAL   B 1 121 ? 38.633 -16.107 -14.695 1.00 15.33 ?  121 VAL   B HB   1 
ATOM   5900 H HG11 . VAL   B 1 121 ? 40.575 -14.956 -15.263 1.00 16.81 ?  121 VAL   B HG11 1 
ATOM   5901 H HG12 . VAL   B 1 121 ? 39.744 -14.144 -14.180 1.00 16.81 ?  121 VAL   B HG12 1 
ATOM   5902 H HG13 . VAL   B 1 121 ? 41.028 -14.971 -13.740 1.00 16.81 ?  121 VAL   B HG13 1 
ATOM   5903 H HG21 . VAL   B 1 121 ? 40.339 -17.460 -15.391 1.00 17.42 ?  121 VAL   B HG21 1 
ATOM   5904 H HG22 . VAL   B 1 121 ? 40.964 -17.493 -13.932 1.00 17.42 ?  121 VAL   B HG22 1 
ATOM   5905 H HG23 . VAL   B 1 121 ? 39.578 -18.216 -14.220 1.00 17.42 ?  121 VAL   B HG23 1 
ATOM   5906 N N    . LEU   B 1 122 ? 40.168 -17.675 -11.186 1.00 10.34 ?  122 LEU   B N    1 
ATOM   5907 C CA   . LEU   B 1 122 ? 41.148 -18.022 -10.161 1.00 10.30 ?  122 LEU   B CA   1 
ATOM   5908 C C    . LEU   B 1 122 ? 41.811 -19.349 -10.490 1.00 9.93  ?  122 LEU   B C    1 
ATOM   5909 O O    . LEU   B 1 122 ? 41.158 -20.273 -10.991 1.00 11.01 ?  122 LEU   B O    1 
ATOM   5910 C CB   . LEU   B 1 122 ? 40.489 -18.250 -8.786  1.00 11.78 ?  122 LEU   B CB   1 
ATOM   5911 C CG   . LEU   B 1 122 ? 39.460 -17.224 -8.302  1.00 11.82 ?  122 LEU   B CG   1 
ATOM   5912 C CD1  . LEU   B 1 122 ? 38.053 -17.574 -8.763  1.00 12.83 ?  122 LEU   B CD1  1 
ATOM   5913 C CD2  . LEU   B 1 122 ? 39.513 -17.097 -6.800  1.00 11.35 ?  122 LEU   B CD2  1 
ATOM   5914 H H    . LEU   B 1 122 ? 39.723 -18.353 -11.478 1.00 12.39 ?  122 LEU   B H    1 
ATOM   5915 H HA   . LEU   B 1 122 ? 41.822 -17.329 -10.088 1.00 12.33 ?  122 LEU   B HA   1 
ATOM   5916 H HB2  . LEU   B 1 122 ? 40.046 -19.106 -8.803  1.00 14.11 ?  122 LEU   B HB2  1 
ATOM   5917 H HB3  . LEU   B 1 122 ? 41.195 -18.266 -8.119  1.00 14.11 ?  122 LEU   B HB3  1 
ATOM   5918 H HG   . LEU   B 1 122 ? 39.678 -16.356 -8.675  1.00 14.16 ?  122 LEU   B HG   1 
ATOM   5919 H HD11 . LEU   B 1 122 ? 37.430 -16.917 -8.408  1.00 15.38 ?  122 LEU   B HD11 1 
ATOM   5920 H HD12 . LEU   B 1 122 ? 38.025 -17.556 -9.734  1.00 15.38 ?  122 LEU   B HD12 1 
ATOM   5921 H HD13 . LEU   B 1 122 ? 37.822 -18.456 -8.441  1.00 15.38 ?  122 LEU   B HD13 1 
ATOM   5922 H HD21 . LEU   B 1 122 ? 38.829 -16.473 -6.505  1.00 13.60 ?  122 LEU   B HD21 1 
ATOM   5923 H HD22 . LEU   B 1 122 ? 39.360 -17.967 -6.400  1.00 13.60 ?  122 LEU   B HD22 1 
ATOM   5924 H HD23 . LEU   B 1 122 ? 40.390 -16.766 -6.542  1.00 13.60 ?  122 LEU   B HD23 1 
ATOM   5925 N N    . LEU   B 1 123 ? 43.096 -19.450 -10.131 1.00 10.11 ?  123 LEU   B N    1 
ATOM   5926 C CA   . LEU   B 1 123 ? 43.814 -20.718 -10.005 1.00 9.94  ?  123 LEU   B CA   1 
ATOM   5927 C C    . LEU   B 1 123 ? 43.777 -21.110 -8.534  1.00 9.84  ?  123 LEU   B C    1 
ATOM   5928 O O    . LEU   B 1 123 ? 44.129 -20.289 -7.682  1.00 10.21 ?  123 LEU   B O    1 
ATOM   5929 C CB   . LEU   B 1 123 ? 45.267 -20.529 -10.442 1.00 10.50 ?  123 LEU   B CB   1 
ATOM   5930 C CG   . LEU   B 1 123 ? 46.206 -21.716 -10.201 1.00 10.66 ?  123 LEU   B CG   1 
ATOM   5931 C CD1  . LEU   B 1 123 ? 45.786 -22.948 -11.006 1.00 11.32 ?  123 LEU   B CD1  1 
ATOM   5932 C CD2  . LEU   B 1 123 ? 47.634 -21.321 -10.551 1.00 11.33 ?  123 LEU   B CD2  1 
ATOM   5933 H H    . LEU   B 1 123 ? 43.588 -18.770 -9.937  1.00 12.11 ?  123 LEU   B H    1 
ATOM   5934 H HA   . LEU   B 1 123 ? 43.391 -21.410 -10.540 1.00 11.91 ?  123 LEU   B HA   1 
ATOM   5935 H HB2  . LEU   B 1 123 ? 45.275 -20.347 -11.396 1.00 12.57 ?  123 LEU   B HB2  1 
ATOM   5936 H HB3  . LEU   B 1 123 ? 45.633 -19.771 -9.966  1.00 12.57 ?  123 LEU   B HB3  1 
ATOM   5937 H HG   . LEU   B 1 123 ? 46.188 -21.957 -9.261  1.00 12.76 ?  123 LEU   B HG   1 
ATOM   5938 H HD11 . LEU   B 1 123 ? 46.420 -23.660 -10.846 1.00 13.56 ?  123 LEU   B HD11 1 
ATOM   5939 H HD12 . LEU   B 1 123 ? 44.899 -23.218 -10.723 1.00 13.56 ?  123 LEU   B HD12 1 
ATOM   5940 H HD13 . LEU   B 1 123 ? 45.776 -22.714 -11.948 1.00 13.56 ?  123 LEU   B HD13 1 
ATOM   5941 H HD21 . LEU   B 1 123 ? 48.218 -22.077 -10.393 1.00 13.58 ?  123 LEU   B HD21 1 
ATOM   5942 H HD22 . LEU   B 1 123 ? 47.668 -21.060 -11.483 1.00 13.58 ?  123 LEU   B HD22 1 
ATOM   5943 H HD23 . LEU   B 1 123 ? 47.897 -20.575 -9.987  1.00 13.58 ?  123 LEU   B HD23 1 
ATOM   5944 N N    . ALA   B 1 124 ? 43.344 -22.336 -8.223  1.00 9.54  ?  124 ALA   B N    1 
ATOM   5945 C CA   . ALA   B 1 124 ? 43.076 -22.657 -6.829  1.00 9.72  ?  124 ALA   B CA   1 
ATOM   5946 C C    . ALA   B 1 124 ? 43.360 -24.117 -6.506  1.00 9.52  ?  124 ALA   B C    1 
ATOM   5947 O O    . ALA   B 1 124 ? 43.237 -24.993 -7.372  1.00 10.11 ?  124 ALA   B O    1 
ATOM   5948 C CB   . ALA   B 1 124 ? 41.619 -22.352 -6.464  1.00 10.11 ?  124 ALA   B CB   1 
ATOM   5949 H H    . ALA   B 1 124 ? 43.176 -22.970 -8.787  1.00 11.43 ?  124 ALA   B H    1 
ATOM   5950 H HA   . ALA   B 1 124 ? 43.651 -22.106 -6.279  1.00 11.63 ?  124 ALA   B HA   1 
ATOM   5951 H HB1  . ALA   B 1 124 ? 41.470 -22.573 -5.532  1.00 12.11 ?  124 ALA   B HB1  1 
ATOM   5952 H HB2  . ALA   B 1 124 ? 41.455 -21.403 -6.607  1.00 12.11 ?  124 ALA   B HB2  1 
ATOM   5953 H HB3  . ALA   B 1 124 ? 41.033 -22.875 -7.029  1.00 12.11 ?  124 ALA   B HB3  1 
ATOM   5954 N N    . PRO   B 1 125 ? 43.647 -24.411 -5.240  1.00 9.90  ?  125 PRO   B N    1 
ATOM   5955 C CA   . PRO   B 1 125 ? 43.584 -25.775 -4.716  1.00 10.41 ?  125 PRO   B CA   1 
ATOM   5956 C C    . PRO   B 1 125 ? 42.181 -26.055 -4.181  1.00 10.73 ?  125 PRO   B C    1 
ATOM   5957 O O    . PRO   B 1 125 ? 41.381 -25.142 -3.965  1.00 10.91 ?  125 PRO   B O    1 
ATOM   5958 C CB   . PRO   B 1 125 ? 44.560 -25.697 -3.536  1.00 11.43 ?  125 PRO   B CB   1 
ATOM   5959 C CG   . PRO   B 1 125 ? 44.291 -24.313 -2.964  1.00 11.56 ?  125 PRO   B CG   1 
ATOM   5960 C CD   . PRO   B 1 125 ? 43.961 -23.441 -4.173  1.00 10.43 ?  125 PRO   B CD   1 
ATOM   5961 H HA   . PRO   B 1 125 ? 43.867 -26.440 -5.358  1.00 12.47 ?  125 PRO   B HA   1 
ATOM   5962 H HB2  . PRO   B 1 125 ? 44.354 -26.384 -2.877  1.00 13.70 ?  125 PRO   B HB2  1 
ATOM   5963 H HB3  . PRO   B 1 125 ? 45.473 -25.769 -3.843  1.00 13.70 ?  125 PRO   B HB3  1 
ATOM   5964 H HG2  . PRO   B 1 125 ? 43.531 -24.345 -2.352  1.00 13.85 ?  125 PRO   B HG2  1 
ATOM   5965 H HG3  . PRO   B 1 125 ? 45.078 -23.980 -2.503  1.00 13.85 ?  125 PRO   B HG3  1 
ATOM   5966 H HD2  . PRO   B 1 125 ? 43.193 -22.874 -3.991  1.00 12.50 ?  125 PRO   B HD2  1 
ATOM   5967 H HD3  . PRO   B 1 125 ? 44.736 -22.904 -4.423  1.00 12.50 ?  125 PRO   B HD3  1 
ATOM   5968 N N    . LEU   B 1 126 ? 41.914 -27.335 -3.910  1.00 11.05 ?  126 LEU   B N    1 
ATOM   5969 C CA   . LEU   B 1 126 ? 40.685 -27.704 -3.211  1.00 11.30 ?  126 LEU   B CA   1 
ATOM   5970 C C    . LEU   B 1 126 ? 40.791 -27.303 -1.745  1.00 11.58 ?  126 LEU   B C    1 
ATOM   5971 O O    . LEU   B 1 126 ? 41.673 -27.770 -1.020  1.00 13.17 ?  126 LEU   B O    1 
ATOM   5972 C CB   . LEU   B 1 126 ? 40.422 -29.199 -3.333  1.00 12.40 ?  126 LEU   B CB   1 
ATOM   5973 C CG   . LEU   B 1 126 ? 39.893 -29.671 -4.689  1.00 13.42 ?  126 LEU   B CG   1 
ATOM   5974 C CD1  . LEU   B 1 126 ? 39.963 -31.184 -4.781  1.00 15.13 ?  126 LEU   B CD1  1 
ATOM   5975 C CD2  . LEU   B 1 126 ? 38.471 -29.183 -4.933  1.00 13.67 ?  126 LEU   B CD2  1 
ATOM   5976 H H    . LEU   B 1 126 ? 42.426 -28.002 -4.104  1.00 13.24 ?  126 LEU   B H    1 
ATOM   5977 H HA   . LEU   B 1 126 ? 39.941 -27.224 -3.604  1.00 13.54 ?  126 LEU   B HA   1 
ATOM   5978 H HB2  . LEU   B 1 126 ? 41.247 -29.671 -3.163  1.00 14.86 ?  126 LEU   B HB2  1 
ATOM   5979 H HB3  . LEU   B 1 126 ? 39.760 -29.446 -2.667  1.00 14.86 ?  126 LEU   B HB3  1 
ATOM   5980 H HG   . LEU   B 1 126 ? 40.459 -29.303 -5.389  1.00 16.08 ?  126 LEU   B HG   1 
ATOM   5981 H HD11 . LEU   B 1 126 ? 39.621 -31.460 -5.646  1.00 18.13 ?  126 LEU   B HD11 1 
ATOM   5982 H HD12 . LEU   B 1 126 ? 40.884 -31.462 -4.681  1.00 18.13 ?  126 LEU   B HD12 1 
ATOM   5983 H HD13 . LEU   B 1 126 ? 39.420 -31.564 -4.073  1.00 18.13 ?  126 LEU   B HD13 1 
ATOM   5984 H HD21 . LEU   B 1 126 ? 38.136 -29.577 -5.755  1.00 16.38 ?  126 LEU   B HD21 1 
ATOM   5985 H HD22 . LEU   B 1 126 ? 37.911 -29.445 -4.187  1.00 16.38 ?  126 LEU   B HD22 1 
ATOM   5986 H HD23 . LEU   B 1 126 ? 38.476 -28.213 -5.015  1.00 16.38 ?  126 LEU   B HD23 1 
ATOM   5987 N N    . LEU   B 1 127 ? 39.863 -26.466 -1.297  1.00 11.32 ?  127 LEU   B N    1 
ATOM   5988 C CA   . LEU   B 1 127 ? 39.907 -25.972 0.070   1.00 11.87 ?  127 LEU   B CA   1 
ATOM   5989 C C    . LEU   B 1 127 ? 39.642 -27.095 1.064   1.00 11.59 ?  127 LEU   B C    1 
ATOM   5990 O O    . LEU   B 1 127 ? 38.824 -27.997 0.833   1.00 11.61 ?  127 LEU   B O    1 
ATOM   5991 C CB   . LEU   B 1 127 ? 38.876 -24.859 0.274   1.00 12.22 ?  127 LEU   B CB   1 
ATOM   5992 C CG   . LEU   B 1 127 ? 39.058 -23.591 -0.564  1.00 12.60 ?  127 LEU   B CG   1 
ATOM   5993 C CD1  . LEU   B 1 127 ? 37.942 -22.627 -0.239  1.00 13.26 ?  127 LEU   B CD1  1 
ATOM   5994 C CD2  . LEU   B 1 127 ? 40.419 -22.950 -0.324  1.00 13.16 ?  127 LEU   B CD2  1 
ATOM   5995 H H    . LEU   B 1 127 ? 39.207 -26.159 -1.764  1.00 13.56 ?  127 LEU   B H    1 
ATOM   5996 H HA   . LEU   B 1 127 ? 40.786 -25.605 0.251   1.00 14.22 ?  127 LEU   B HA   1 
ATOM   5997 H HB2  . LEU   B 1 127 ? 37.995 -25.214 0.069   1.00 14.64 ?  127 LEU   B HB2  1 
ATOM   5998 H HB3  . LEU   B 1 127 ? 38.897 -24.588 1.208   1.00 14.64 ?  127 LEU   B HB3  1 
ATOM   5999 H HG   . LEU   B 1 127 ? 38.984 -23.816 -1.502  1.00 15.10 ?  127 LEU   B HG   1 
ATOM   6000 H HD11 . LEU   B 1 127 ? 38.056 -21.817 -0.765  1.00 15.89 ?  127 LEU   B HD11 1 
ATOM   6001 H HD12 . LEU   B 1 127 ? 37.089 -23.037 -0.450  1.00 15.89 ?  127 LEU   B HD12 1 
ATOM   6002 H HD13 . LEU   B 1 127 ? 37.975 -22.407 0.708   1.00 15.89 ?  127 LEU   B HD13 1 
ATOM   6003 H HD21 . LEU   B 1 127 ? 40.453 -22.095 -0.782  1.00 15.76 ?  127 LEU   B HD21 1 
ATOM   6004 H HD22 . LEU   B 1 127 ? 40.546 -22.819 0.629   1.00 15.76 ?  127 LEU   B HD22 1 
ATOM   6005 H HD23 . LEU   B 1 127 ? 41.108 -23.538 -0.671  1.00 15.76 ?  127 LEU   B HD23 1 
ATOM   6006 N N    . SER   B 1 128 ? 40.330 -27.011 2.195   1.00 11.44 ?  128 SER   B N    1 
ATOM   6007 C CA   . SER   B 1 128 ? 40.224 -27.935 3.315   1.00 12.08 ?  128 SER   B CA   1 
ATOM   6008 C C    . SER   B 1 128 ? 40.717 -29.341 2.988   1.00 12.69 ?  128 SER   B C    1 
ATOM   6009 O O    . SER   B 1 128 ? 40.621 -30.223 3.839   1.00 14.10 ?  128 SER   B O    1 
ATOM   6010 C CB   . SER   B 1 128 ? 38.821 -27.947 3.941   1.00 12.50 ?  128 SER   B CB   1 
ATOM   6011 O OG   . SER   B 1 128 ? 38.492 -26.674 4.498   1.00 13.29 ?  128 SER   B OG   1 
ATOM   6012 H H    . SER   B 1 128 ? 40.904 -26.385 2.344   1.00 13.71 ?  128 SER   B H    1 
ATOM   6013 H HA   . SER   B 1 128 ? 40.809 -27.600 4.004   1.00 14.47 ?  128 SER   B HA   1 
ATOM   6014 H HB2  . SER   B 1 128 ? 38.164 -28.174 3.263   1.00 14.98 ?  128 SER   B HB2  1 
ATOM   6015 H HB3  . SER   B 1 128 ? 38.797 -28.620 4.651   1.00 14.98 ?  128 SER   B HB3  1 
ATOM   6016 H HG   . SER   B 1 128 ? 39.054 -26.480 5.095   1.00 15.92 ?  128 SER   B HG   1 
ATOM   6017 N N    . ALA   B 1 129 ? 41.300 -29.555 1.807   1.00 13.06 ?  129 ALA   B N    1 
ATOM   6018 C CA   . ALA   B 1 129 ? 41.848 -30.851 1.445   1.00 14.16 ?  129 ALA   B CA   1 
ATOM   6019 C C    . ALA   B 1 129 ? 43.229 -31.036 2.059   1.00 13.23 ?  129 ALA   B C    1 
ATOM   6020 O O    . ALA   B 1 129 ? 43.789 -30.135 2.700   1.00 13.27 ?  129 ALA   B O    1 
ATOM   6021 C CB   . ALA   B 1 129 ? 41.918 -30.999 -0.073  1.00 15.98 ?  129 ALA   B CB   1 
ATOM   6022 H H    . ALA   B 1 129 ? 41.387 -28.954 1.196   1.00 15.64 ?  129 ALA   B H    1 
ATOM   6023 H HA   . ALA   B 1 129 ? 41.269 -31.545 1.791   1.00 16.96 ?  129 ALA   B HA   1 
ATOM   6024 H HB1  . ALA   B 1 129 ? 42.278 -31.873 -0.286  1.00 19.15 ?  129 ALA   B HB1  1 
ATOM   6025 H HB2  . ALA   B 1 129 ? 41.026 -30.908 -0.438  1.00 19.15 ?  129 ALA   B HB2  1 
ATOM   6026 H HB3  . ALA   B 1 129 ? 42.496 -30.306 -0.430  1.00 19.15 ?  129 ALA   B HB3  1 
ATOM   6027 N N    . GLY   B 1 130 ? 43.783 -32.227 1.848   1.00 13.66 ?  130 GLY   B N    1 
ATOM   6028 C CA   . GLY   B 1 130 ? 45.170 -32.467 2.202   1.00 14.32 ?  130 GLY   B CA   1 
ATOM   6029 C C    . GLY   B 1 130 ? 45.378 -32.363 3.693   1.00 14.31 ?  130 GLY   B C    1 
ATOM   6030 O O    . GLY   B 1 130 ? 44.678 -33.003 4.491   1.00 15.32 ?  130 GLY   B O    1 
ATOM   6031 H H    . GLY   B 1 130 ? 43.380 -32.903 1.499   1.00 16.37 ?  130 GLY   B H    1 
ATOM   6032 H HA2  . GLY   B 1 130 ? 45.433 -33.355 1.908   1.00 17.16 ?  130 GLY   B HA2  1 
ATOM   6033 H HA3  . GLY   B 1 130 ? 45.739 -31.816 1.761   1.00 17.16 ?  130 GLY   B HA3  1 
ATOM   6034 N N    . ILE   B 1 131 ? 46.350 -31.535 4.084   1.00 14.45 ?  131 ILE   B N    1 
ATOM   6035 C CA   . ILE   B 1 131 ? 46.694 -31.395 5.488   1.00 15.36 ?  131 ILE   B CA   1 
ATOM   6036 C C    . ILE   B 1 131 ? 45.569 -30.795 6.315   1.00 14.67 ?  131 ILE   B C    1 
ATOM   6037 O O    . ILE   B 1 131 ? 45.629 -30.860 7.543   1.00 16.25 ?  131 ILE   B O    1 
ATOM   6038 C CB   . ILE   B 1 131 ? 48.019 -30.621 5.691   1.00 17.21 ?  131 ILE   B CB   1 
ATOM   6039 C CG1  . ILE   B 1 131 ? 47.856 -29.136 5.333   1.00 18.16 ?  131 ILE   B CG1  1 
ATOM   6040 C CG2  . ILE   B 1 131 ? 49.143 -31.270 4.888   1.00 18.18 ?  131 ILE   B CG2  1 
ATOM   6041 C CD1  . ILE   B 1 131 ? 49.097 -28.307 5.615   1.00 19.18 ?  131 ILE   B CD1  1 
ATOM   6042 H H    . ILE   B 1 131 ? 46.829 -31.057 3.553   1.00 17.32 ?  131 ILE   B H    1 
ATOM   6043 H HA   . ILE   B 1 131 ? 46.844 -32.287 5.840   1.00 18.41 ?  131 ILE   B HA   1 
ATOM   6044 H HB   . ILE   B 1 131 ? 48.253 -30.678 6.630   1.00 20.63 ?  131 ILE   B HB   1 
ATOM   6045 H HG12 . ILE   B 1 131 ? 47.651 -29.063 4.389   1.00 21.76 ?  131 ILE   B HG12 1 
ATOM   6046 H HG13 . ILE   B 1 131 ? 47.128 -28.760 5.857   1.00 21.76 ?  131 ILE   B HG13 1 
ATOM   6047 H HG21 . ILE   B 1 131 ? 49.987 -30.879 5.159   1.00 21.79 ?  131 ILE   B HG21 1 
ATOM   6048 H HG22 . ILE   B 1 131 ? 49.143 -32.221 5.064   1.00 21.79 ?  131 ILE   B HG22 1 
ATOM   6049 H HG23 . ILE   B 1 131 ? 48.987 -31.106 3.945   1.00 21.79 ?  131 ILE   B HG23 1 
ATOM   6050 H HD11 . ILE   B 1 131 ? 48.884 -27.372 5.479   1.00 22.99 ?  131 ILE   B HD11 1 
ATOM   6051 H HD12 . ILE   B 1 131 ? 49.371 -28.456 6.533   1.00 22.99 ?  131 ILE   B HD12 1 
ATOM   6052 H HD13 . ILE   B 1 131 ? 49.800 -28.582 5.009   1.00 22.99 ?  131 ILE   B HD13 1 
ATOM   6053 N N    . PHE   B 1 132 ? 44.548 -30.213 5.676   1.00 13.38 ?  132 PHE   B N    1 
ATOM   6054 C CA   . PHE   B 1 132 ? 43.382 -29.715 6.397   1.00 13.90 ?  132 PHE   B CA   1 
ATOM   6055 C C    . PHE   B 1 132 ? 42.359 -30.810 6.712   1.00 14.80 ?  132 PHE   B C    1 
ATOM   6056 O O    . PHE   B 1 132 ? 41.440 -30.567 7.502   1.00 16.78 ?  132 PHE   B O    1 
ATOM   6057 C CB   . PHE   B 1 132 ? 42.713 -28.579 5.612   1.00 13.33 ?  132 PHE   B CB   1 
ATOM   6058 C CG   . PHE   B 1 132 ? 43.408 -27.233 5.732   1.00 13.26 ?  132 PHE   B CG   1 
ATOM   6059 C CD1  . PHE   B 1 132 ? 44.698 -27.043 5.257   1.00 14.04 ?  132 PHE   B CD1  1 
ATOM   6060 C CD2  . PHE   B 1 132 ? 42.737 -26.143 6.275   1.00 12.75 ?  132 PHE   B CD2  1 
ATOM   6061 C CE1  . PHE   B 1 132 ? 45.311 -25.803 5.356   1.00 14.65 ?  132 PHE   B CE1  1 
ATOM   6062 C CE2  . PHE   B 1 132 ? 43.343 -24.907 6.368   1.00 13.46 ?  132 PHE   B CE2  1 
ATOM   6063 C CZ   . PHE   B 1 132 ? 44.626 -24.739 5.909   1.00 14.52 ?  132 PHE   B CZ   1 
ATOM   6064 H H    . PHE   B 1 132 ? 44.512 -30.096 4.824   1.00 16.03 ?  132 PHE   B H    1 
ATOM   6065 H HA   . PHE   B 1 132 ? 43.682 -29.346 7.239   1.00 16.66 ?  132 PHE   B HA   1 
ATOM   6066 H HB2  . PHE   B 1 132 ? 42.702 -28.818 4.676   1.00 15.97 ?  132 PHE   B HB2  1 
ATOM   6067 H HB3  . PHE   B 1 132 ? 41.803 -28.473 5.938   1.00 15.97 ?  132 PHE   B HB3  1 
ATOM   6068 H HD1  . PHE   B 1 132 ? 45.162 -27.763 4.887   1.00 16.83 ?  132 PHE   B HD1  1 
ATOM   6069 H HD2  . PHE   B 1 132 ? 41.865 -26.257 6.586   1.00 15.27 ?  132 PHE   B HD2  1 
ATOM   6070 H HE1  . PHE   B 1 132 ? 46.179 -25.686 5.046   1.00 17.56 ?  132 PHE   B HE1  1 
ATOM   6071 H HE2  . PHE   B 1 132 ? 42.880 -24.190 6.744   1.00 16.13 ?  132 PHE   B HE2  1 
ATOM   6072 H HZ   . PHE   B 1 132 ? 45.034 -23.902 5.977   1.00 17.40 ?  132 PHE   B HZ   1 
ATOM   6073 N N    . GLY   B 1 133 ? 42.478 -32.003 6.118   1.00 14.71 ?  133 GLY   B N    1 
ATOM   6074 C CA   . GLY   B 1 133 ? 41.772 -33.175 6.604   1.00 15.46 ?  133 GLY   B CA   1 
ATOM   6075 C C    . GLY   B 1 133 ? 40.376 -33.434 6.073   1.00 15.91 ?  133 GLY   B C    1 
ATOM   6076 O O    . GLY   B 1 133 ? 39.792 -34.458 6.433   1.00 17.92 ?  133 GLY   B O    1 
ATOM   6077 H H    . GLY   B 1 133 ? 42.971 -32.155 5.428   1.00 17.62 ?  133 GLY   B H    1 
ATOM   6078 H HA2  . GLY   B 1 133 ? 42.304 -33.959 6.400   1.00 18.52 ?  133 GLY   B HA2  1 
ATOM   6079 H HA3  . GLY   B 1 133 ? 41.706 -33.111 7.570   1.00 18.52 ?  133 GLY   B HA3  1 
ATOM   6080 N N    . ALA   B 1 134 ? 39.810 -32.562 5.247   1.00 14.91 ?  134 ALA   B N    1 
ATOM   6081 C CA   . ALA   B 1 134 ? 38.485 -32.835 4.709   1.00 15.02 ?  134 ALA   B CA   1 
ATOM   6082 C C    . ALA   B 1 134 ? 38.568 -33.829 3.554   1.00 14.69 ?  134 ALA   B C    1 
ATOM   6083 O O    . ALA   B 1 134 ? 39.622 -34.030 2.943   1.00 15.95 ?  134 ALA   B O    1 
ATOM   6084 C CB   . ALA   B 1 134 ? 37.811 -31.549 4.230   1.00 15.82 ?  134 ALA   B CB   1 
ATOM   6085 H H    . ALA   B 1 134 ? 40.163 -31.818 4.989   1.00 17.87 ?  134 ALA   B H    1 
ATOM   6086 H HA   . ALA   B 1 134 ? 37.933 -33.221 5.408   1.00 18.00 ?  134 ALA   B HA   1 
ATOM   6087 H HB1  . ALA   B 1 134 ? 36.927 -31.764 3.893   1.00 18.96 ?  134 ALA   B HB1  1 
ATOM   6088 H HB2  . ALA   B 1 134 ? 37.740 -30.932 4.975   1.00 18.96 ?  134 ALA   B HB2  1 
ATOM   6089 H HB3  . ALA   B 1 134 ? 38.347 -31.156 3.524   1.00 18.96 ?  134 ALA   B HB3  1 
ATOM   6090 N N    . ASP   B 1 135 ? 37.437 -34.456 3.263   1.00 15.14 ?  135 ASP   B N    1 
ATOM   6091 C CA   . ASP   B 1 135 ? 37.342 -35.354 2.122   1.00 15.90 ?  135 ASP   B CA   1 
ATOM   6092 C C    . ASP   B 1 135 ? 37.444 -34.522 0.850   1.00 14.70 ?  135 ASP   B C    1 
ATOM   6093 O O    . ASP   B 1 135 ? 36.585 -33.660 0.619   1.00 14.29 ?  135 ASP   B O    1 
ATOM   6094 C CB   . ASP   B 1 135 ? 35.998 -36.077 2.178   1.00 17.59 ?  135 ASP   B CB   1 
ATOM   6095 C CG   . ASP   B 1 135 ? 35.805 -37.072 1.049   1.00 19.55 ?  135 ASP   B CG   1 
ATOM   6096 O OD1  . ASP   B 1 135 ? 36.663 -37.140 0.143   1.00 19.58 ?  135 ASP   B OD1  1 
ATOM   6097 O OD2  . ASP   B 1 135 ? 34.793 -37.810 1.086   1.00 22.27 -1 135 ASP   B OD2  1 
ATOM   6098 H H    . ASP   B 1 135 ? 36.707 -34.373 3.708   1.00 18.15 ?  135 ASP   B H    1 
ATOM   6099 H HA   . ASP   B 1 135 ? 38.060 -36.008 2.158   1.00 19.06 ?  135 ASP   B HA   1 
ATOM   6100 H HB2  . ASP   B 1 135 ? 35.944 -36.564 3.010   1.00 21.08 ?  135 ASP   B HB2  1 
ATOM   6101 H HB3  . ASP   B 1 135 ? 35.293 -35.417 2.124   1.00 21.08 ?  135 ASP   B HB3  1 
ATOM   6102 N N    . PRO   B 1 136 ? 38.458 -34.732 0.006   1.00 15.07 ?  136 PRO   B N    1 
ATOM   6103 C CA   . PRO   B 1 136 ? 38.564 -33.910 -1.210  1.00 14.20 ?  136 PRO   B CA   1 
ATOM   6104 C C    . PRO   B 1 136 ? 37.375 -34.058 -2.143  1.00 13.32 ?  136 PRO   B C    1 
ATOM   6105 O O    . PRO   B 1 136 ? 37.052 -33.105 -2.862  1.00 12.91 ?  136 PRO   B O    1 
ATOM   6106 C CB   . PRO   B 1 136 ? 39.879 -34.384 -1.848  1.00 15.41 ?  136 PRO   B CB   1 
ATOM   6107 C CG   . PRO   B 1 136 ? 40.087 -35.765 -1.299  1.00 16.55 ?  136 PRO   B CG   1 
ATOM   6108 C CD   . PRO   B 1 136 ? 39.546 -35.720 0.100   1.00 16.11 ?  136 PRO   B CD   1 
ATOM   6109 H HA   . PRO   B 1 136 ? 38.655 -32.974 -0.973  1.00 17.02 ?  136 PRO   B HA   1 
ATOM   6110 H HB2  . PRO   B 1 136 ? 39.787 -34.410 -2.815  1.00 18.47 ?  136 PRO   B HB2  1 
ATOM   6111 H HB3  . PRO   B 1 136 ? 40.602 -33.795 -1.587  1.00 18.47 ?  136 PRO   B HB3  1 
ATOM   6112 H HG2  . PRO   B 1 136 ? 39.597 -36.411 -1.831  1.00 19.83 ?  136 PRO   B HG2  1 
ATOM   6113 H HG3  . PRO   B 1 136 ? 41.034 -35.976 -1.289  1.00 19.83 ?  136 PRO   B HG3  1 
ATOM   6114 H HD2  . PRO   B 1 136 ? 39.193 -36.584 0.359   1.00 19.31 ?  136 PRO   B HD2  1 
ATOM   6115 H HD3  . PRO   B 1 136 ? 40.225 -35.410 0.723   1.00 19.31 ?  136 PRO   B HD3  1 
ATOM   6116 N N    . ILE   B 1 137 ? 36.715 -35.223 -2.155  1.00 13.79 ?  137 ILE   B N    1 
ATOM   6117 C CA   . ILE   B 1 137 ? 35.498 -35.389 -2.948  1.00 14.24 ?  137 ILE   B CA   1 
ATOM   6118 C C    . ILE   B 1 137 ? 34.420 -34.422 -2.473  1.00 13.76 ?  137 ILE   B C    1 
ATOM   6119 O O    . ILE   B 1 137 ? 33.707 -33.810 -3.278  1.00 13.55 ?  137 ILE   B O    1 
ATOM   6120 C CB   . ILE   B 1 137 ? 35.027 -36.854 -2.887  1.00 16.39 ?  137 ILE   B CB   1 
ATOM   6121 C CG1  . ILE   B 1 137 ? 36.034 -37.752 -3.611  1.00 18.60 ?  137 ILE   B CG1  1 
ATOM   6122 C CG2  . ILE   B 1 137 ? 33.628 -36.997 -3.484  1.00 17.09 ?  137 ILE   B CG2  1 
ATOM   6123 C CD1  . ILE   B 1 137 ? 35.722 -39.225 -3.523  1.00 20.91 ?  137 ILE   B CD1  1 
ATOM   6124 H H    . ILE   B 1 137 ? 36.954 -35.925 -1.723  1.00 16.52 ?  137 ILE   B H    1 
ATOM   6125 H HA   . ILE   B 1 137 ? 35.694 -35.181 -3.876  1.00 17.07 ?  137 ILE   B HA   1 
ATOM   6126 H HB   . ILE   B 1 137 ? 34.987 -37.123 -1.959  1.00 19.65 ?  137 ILE   B HB   1 
ATOM   6127 H HG12 . ILE   B 1 137 ? 36.050 -37.507 -4.550  1.00 22.29 ?  137 ILE   B HG12 1 
ATOM   6128 H HG13 . ILE   B 1 137 ? 36.910 -37.609 -3.220  1.00 22.29 ?  137 ILE   B HG13 1 
ATOM   6129 H HG21 . ILE   B 1 137 ? 33.387 -37.938 -3.525  1.00 20.48 ?  137 ILE   B HG21 1 
ATOM   6130 H HG22 . ILE   B 1 137 ? 32.987 -36.532 -2.926  1.00 20.48 ?  137 ILE   B HG22 1 
ATOM   6131 H HG23 . ILE   B 1 137 ? 33.624 -36.622 -4.379  1.00 20.48 ?  137 ILE   B HG23 1 
ATOM   6132 H HD11 . ILE   B 1 137 ? 36.427 -39.710 -3.973  1.00 25.07 ?  137 ILE   B HD11 1 
ATOM   6133 H HD12 . ILE   B 1 137 ? 35.679 -39.486 -2.589  1.00 25.07 ?  137 ILE   B HD12 1 
ATOM   6134 H HD13 . ILE   B 1 137 ? 34.875 -39.405 -3.958  1.00 25.07 ?  137 ILE   B HD13 1 
ATOM   6135 N N    . HIS   B 1 138 ? 34.286 -34.270 -1.157  1.00 13.98 ?  138 HIS   B N    1 
ATOM   6136 C CA   . HIS   B 1 138 ? 33.335 -33.305 -0.621  1.00 14.47 ?  138 HIS   B CA   1 
ATOM   6137 C C    . HIS   B 1 138 ? 33.755 -31.875 -0.937  1.00 13.70 ?  138 HIS   B C    1 
ATOM   6138 O O    . HIS   B 1 138 ? 32.908 -31.030 -1.243  1.00 14.23 ?  138 HIS   B O    1 
ATOM   6139 C CB   . HIS   B 1 138 ? 33.205 -33.486 0.882   1.00 15.82 ?  138 HIS   B CB   1 
ATOM   6140 C CG   . HIS   B 1 138 ? 32.276 -32.503 1.517   1.00 16.61 ?  138 HIS   B CG   1 
ATOM   6141 N ND1  . HIS   B 1 138 ? 30.933 -32.444 1.212   1.00 17.96 ?  138 HIS   B ND1  1 
ATOM   6142 C CD2  . HIS   B 1 138 ? 32.501 -31.522 2.422   1.00 17.10 ?  138 HIS   B CD2  1 
ATOM   6143 C CE1  . HIS   B 1 138 ? 30.369 -31.476 1.912   1.00 18.05 ?  138 HIS   B CE1  1 
ATOM   6144 N NE2  . HIS   B 1 138 ? 31.298 -30.902 2.655   1.00 17.59 ?  138 HIS   B NE2  1 
ATOM   6145 H H    . HIS   B 1 138 ? 34.724 -34.710 -0.566  1.00 16.75 ?  138 HIS   B H    1 
ATOM   6146 H HA   . HIS   B 1 138 ? 32.466 -33.460 -1.023  1.00 17.35 ?  138 HIS   B HA   1 
ATOM   6147 H HB2  . HIS   B 1 138 ? 32.863 -34.373 1.063   1.00 18.96 ?  138 HIS   B HB2  1 
ATOM   6148 H HB3  . HIS   B 1 138 ? 34.077 -33.374 1.289   1.00 18.96 ?  138 HIS   B HB3  1 
ATOM   6149 H HD1  . HIS   B 1 138 ? 30.525 -32.962 0.659   1.00 21.53 ?  138 HIS   B HD1  1 
ATOM   6150 H HD2  . HIS   B 1 138 ? 33.312 -31.308 2.820   1.00 20.50 ?  138 HIS   B HD2  1 
ATOM   6151 H HE1  . HIS   B 1 138 ? 29.465 -31.246 1.892   1.00 21.64 ?  138 HIS   B HE1  1 
ATOM   6152 N N    . SER   B 1 139 ? 35.051 -31.573 -0.856  1.00 13.28 ?  139 SER   B N    1 
ATOM   6153 C CA   . SER   B 1 139 ? 35.495 -30.227 -1.184  1.00 12.43 ?  139 SER   B CA   1 
ATOM   6154 C C    . SER   B 1 139 ? 35.156 -29.878 -2.624  1.00 11.80 ?  139 SER   B C    1 
ATOM   6155 O O    . SER   B 1 139 ? 34.703 -28.764 -2.906  1.00 11.73 ?  139 SER   B O    1 
ATOM   6156 C CB   . SER   B 1 139 ? 36.992 -30.092 -0.927  1.00 12.87 ?  139 SER   B CB   1 
ATOM   6157 O OG   . SER   B 1 139 ? 37.392 -28.760 -1.182  1.00 12.75 ?  139 SER   B OG   1 
ATOM   6158 H H    . SER   B 1 139 ? 35.671 -32.121 -0.632  1.00 15.91 ?  139 SER   B H    1 
ATOM   6159 H HA   . SER   B 1 139 ? 35.037 -29.599 -0.615  1.00 14.89 ?  139 SER   B HA   1 
ATOM   6160 H HB2  . SER   B 1 139 ? 37.181 -30.307 -0.001  1.00 15.42 ?  139 SER   B HB2  1 
ATOM   6161 H HB3  . SER   B 1 139 ? 37.480 -30.693 -1.516  1.00 15.42 ?  139 SER   B HB3  1 
ATOM   6162 H HG   . SER   B 1 139 ? 38.221 -28.674 -1.049  1.00 15.28 ?  139 SER   B HG   1 
ATOM   6163 N N    . LEU   B 1 140 ? 35.357 -30.821 -3.550  1.00 11.43 ?  140 LEU   B N    1 
ATOM   6164 C CA   . LEU   B 1 140 ? 34.997 -30.577 -4.940  1.00 11.51 ?  140 LEU   B CA   1 
ATOM   6165 C C    . LEU   B 1 140 ? 33.496 -30.346 -5.081  1.00 11.93 ?  140 LEU   B C    1 
ATOM   6166 O O    . LEU   B 1 140 ? 33.066 -29.463 -5.827  1.00 12.32 ?  140 LEU   B O    1 
ATOM   6167 C CB   . LEU   B 1 140 ? 35.466 -31.741 -5.817  1.00 11.30 ?  140 LEU   B CB   1 
ATOM   6168 C CG   . LEU   B 1 140 ? 35.117 -31.630 -7.298  1.00 11.60 ?  140 LEU   B CG   1 
ATOM   6169 C CD1  . LEU   B 1 140 ? 35.671 -30.354 -7.920  1.00 12.70 ?  140 LEU   B CD1  1 
ATOM   6170 C CD2  . LEU   B 1 140 ? 35.607 -32.866 -8.051  1.00 12.93 ?  140 LEU   B CD2  1 
ATOM   6171 H H    . LEU   B 1 140 ? 35.696 -31.596 -3.401  1.00 13.69 ?  140 LEU   B H    1 
ATOM   6172 H HA   . LEU   B 1 140 ? 35.450 -29.778 -5.248  1.00 13.79 ?  140 LEU   B HA   1 
ATOM   6173 H HB2  . LEU   B 1 140 ? 36.431 -31.809 -5.752  1.00 13.54 ?  140 LEU   B HB2  1 
ATOM   6174 H HB3  . LEU   B 1 140 ? 35.061 -32.560 -5.489  1.00 13.54 ?  140 LEU   B HB3  1 
ATOM   6175 H HG   . LEU   B 1 140 ? 34.153 -31.598 -7.388  1.00 13.89 ?  140 LEU   B HG   1 
ATOM   6176 H HD11 . LEU   B 1 140 ? 35.516 -30.378 -8.879  1.00 15.22 ?  140 LEU   B HD11 1 
ATOM   6177 H HD12 . LEU   B 1 140 ? 35.214 -29.588 -7.535  1.00 15.22 ?  140 LEU   B HD12 1 
ATOM   6178 H HD13 . LEU   B 1 140 ? 36.620 -30.298 -7.741  1.00 15.22 ?  140 LEU   B HD13 1 
ATOM   6179 H HD21 . LEU   B 1 140 ? 35.372 -32.771 -8.992  1.00 15.49 ?  140 LEU   B HD21 1 
ATOM   6180 H HD22 . LEU   B 1 140 ? 36.565 -32.935 -7.955  1.00 15.49 ?  140 LEU   B HD22 1 
ATOM   6181 H HD23 . LEU   B 1 140 ? 35.172 -33.648 -7.682  1.00 15.49 ?  140 LEU   B HD23 1 
ATOM   6182 N N    . ARG   B 1 141 ? 32.688 -31.141 -4.379  1.00 12.37 ?  141 ARG   B N    1 
ATOM   6183 C CA   . ARG   B 1 141 ? 31.236 -30.963 -4.368  1.00 13.30 ?  141 ARG   B CA   1 
ATOM   6184 C C    . ARG   B 1 141 ? 30.855 -29.553 -3.935  1.00 13.11 ?  141 ARG   B C    1 
ATOM   6185 O O    . ARG   B 1 141 ? 30.052 -28.874 -4.591  1.00 13.04 ?  141 ARG   B O    1 
ATOM   6186 C CB   . ARG   B 1 141 ? 30.646 -31.996 -3.400  1.00 15.10 ?  141 ARG   B CB   1 
ATOM   6187 C CG   . ARG   B 1 141 ? 29.194 -31.849 -3.024  1.00 17.13 ?  141 ARG   B CG   1 
ATOM   6188 C CD   . ARG   B 1 141 ? 28.322 -32.475 -4.037  1.00 19.03 ?  141 ARG   B CD   1 
ATOM   6189 N NE   . ARG   B 1 141 ? 28.069 -31.591 -5.167  1.00 19.99 ?  141 ARG   B NE   1 
ATOM   6190 C CZ   . ARG   B 1 141 ? 28.143 -31.949 -6.442  1.00 19.60 ?  141 ARG   B CZ   1 
ATOM   6191 N NH1  . ARG   B 1 141 ? 28.602 -33.138 -6.805  1.00 19.71 ?  141 ARG   B NH1  1 
ATOM   6192 N NH2  . ARG   B 1 141 ? 27.716 -31.099 -7.375  1.00 20.76 ?  141 ARG   B NH2  1 
ATOM   6193 H H    . ARG   B 1 141 ? 32.960 -31.801 -3.902  1.00 14.82 ?  141 ARG   B H    1 
ATOM   6194 H HA   . ARG   B 1 141 ? 30.875 -31.127 -5.252  1.00 15.94 ?  141 ARG   B HA   1 
ATOM   6195 H HB2  . ARG   B 1 141 ? 30.755 -32.879 -3.796  1.00 18.10 ?  141 ARG   B HB2  1 
ATOM   6196 H HB3  . ARG   B 1 141 ? 31.157 -31.964 -2.576  1.00 18.10 ?  141 ARG   B HB3  1 
ATOM   6197 H HG2  . ARG   B 1 141 ? 29.043 -32.281 -2.173  1.00 20.53 ?  141 ARG   B HG2  1 
ATOM   6198 H HG3  . ARG   B 1 141 ? 28.962 -30.903 -2.957  1.00 20.53 ?  141 ARG   B HG3  1 
ATOM   6199 H HD2  . ARG   B 1 141 ? 28.742 -33.289 -4.358  1.00 22.81 ?  141 ARG   B HD2  1 
ATOM   6200 H HD3  . ARG   B 1 141 ? 27.477 -32.690 -3.622  1.00 22.81 ?  141 ARG   B HD3  1 
ATOM   6201 H HE   . ARG   B 1 141 ? 27.822 -30.783 -4.990  1.00 23.97 ?  141 ARG   B HE   1 
ATOM   6202 H HH11 . ARG   B 1 141 ? 28.867 -33.699 -6.215  1.00 23.63 ?  141 ARG   B HH11 1 
ATOM   6203 H HH12 . ARG   B 1 141 ? 28.646 -33.336 -7.638  1.00 23.63 ?  141 ARG   B HH12 1 
ATOM   6204 H HH21 . ARG   B 1 141 ? 27.414 -30.323 -7.151  1.00 24.89 ?  141 ARG   B HH21 1 
ATOM   6205 H HH22 . ARG   B 1 141 ? 27.773 -31.309 -8.208  1.00 24.89 ?  141 ARG   B HH22 1 
ATOM   6206 N N    . VAL   B 1 142 ? 31.399 -29.105 -2.805  1.00 12.43 ?  142 VAL   B N    1 
ATOM   6207 C CA   . VAL   B 1 142 ? 31.059 -27.773 -2.317  1.00 12.49 ?  142 VAL   B CA   1 
ATOM   6208 C C    . VAL   B 1 142 ? 31.537 -26.711 -3.300  1.00 12.25 ?  142 VAL   B C    1 
ATOM   6209 O O    . VAL   B 1 142 ? 30.834 -25.727 -3.564  1.00 12.99 ?  142 VAL   B O    1 
ATOM   6210 C CB   . VAL   B 1 142 ? 31.594 -27.552 -0.889  1.00 12.94 ?  142 VAL   B CB   1 
ATOM   6211 C CG1  . VAL   B 1 142 ? 31.285 -26.130 -0.416  1.00 13.20 ?  142 VAL   B CG1  1 
ATOM   6212 C CG2  . VAL   B 1 142 ? 31.000 -28.566 0.069   1.00 13.66 ?  142 VAL   B CG2  1 
ATOM   6213 H H    . VAL   B 1 142 ? 31.950 -29.541 -2.312  1.00 14.89 ?  142 VAL   B H    1 
ATOM   6214 H HA   . VAL   B 1 142 ? 30.098 -27.702 -2.271  1.00 14.96 ?  142 VAL   B HA   1 
ATOM   6215 H HB   . VAL   B 1 142 ? 32.557 -27.665 -0.884  1.00 15.50 ?  142 VAL   B HB   1 
ATOM   6216 H HG11 . VAL   B 1 142 ? 31.464 -26.069 0.535   1.00 15.81 ?  142 VAL   B HG11 1 
ATOM   6217 H HG12 . VAL   B 1 142 ? 31.850 -25.505 -0.898  1.00 15.81 ?  142 VAL   B HG12 1 
ATOM   6218 H HG13 . VAL   B 1 142 ? 30.351 -25.936 -0.589  1.00 15.81 ?  142 VAL   B HG13 1 
ATOM   6219 H HG21 . VAL   B 1 142 ? 31.321 -28.386 0.965   1.00 16.36 ?  142 VAL   B HG21 1 
ATOM   6220 H HG22 . VAL   B 1 142 ? 30.031 -28.494 0.045   1.00 16.36 ?  142 VAL   B HG22 1 
ATOM   6221 H HG23 . VAL   B 1 142 ? 31.269 -29.457 -0.207  1.00 16.36 ?  142 VAL   B HG23 1 
ATOM   6222 N N    . CYS   B 1 143 ? 32.720 -26.908 -3.882  1.00 11.77 ?  143 CYS   B N    1 
ATOM   6223 C CA   . CYS   B 1 143 ? 33.217 -25.970 -4.883  1.00 11.79 ?  143 CYS   B CA   1 
ATOM   6224 C C    . CYS   B 1 143 ? 32.222 -25.824 -6.028  1.00 11.82 ?  143 CYS   B C    1 
ATOM   6225 O O    . CYS   B 1 143 ? 31.818 -24.713 -6.387  1.00 11.87 ?  143 CYS   B O    1 
ATOM   6226 C CB   . CYS   B 1 143 ? 34.574 -26.459 -5.404  1.00 12.06 ?  143 CYS   B CB   1 
ATOM   6227 S SG   . CYS   B 1 143 ? 35.335 -25.359 -6.614  1.00 12.41 ?  143 CYS   B SG   1 
ATOM   6228 H H    . CYS   B 1 143 ? 33.248 -27.565 -3.720  1.00 14.10 ?  143 CYS   B H    1 
ATOM   6229 H HA   . CYS   B 1 143 ? 33.348 -25.096 -4.476  1.00 14.13 ?  143 CYS   B HA   1 
ATOM   6230 H HB2  . CYS   B 1 143 ? 35.189 -26.549 -4.660  1.00 14.45 ?  143 CYS   B HB2  1 
ATOM   6231 H HB3  . CYS   B 1 143 ? 34.452 -27.321 -5.828  1.00 14.45 ?  143 CYS   B HB3  1 
ATOM   6232 H HG   . CYS   B 1 143 ? 36.400 -25.807 -6.936  1.00 14.86 ?  143 CYS   B HG   1 
ATOM   6233 N N    . VAL   B 1 144 ? 31.821 -26.947 -6.620  1.00 12.20 ?  144 VAL   B N    1 
ATOM   6234 C CA   . VAL   B 1 144 ? 30.919 -26.892 -7.764  1.00 13.11 ?  144 VAL   B CA   1 
ATOM   6235 C C    . VAL   B 1 144 ? 29.581 -26.273 -7.390  1.00 13.22 ?  144 VAL   B C    1 
ATOM   6236 O O    . VAL   B 1 144 ? 28.965 -25.567 -8.200  1.00 14.68 ?  144 VAL   B O    1 
ATOM   6237 C CB   . VAL   B 1 144 ? 30.760 -28.299 -8.352  1.00 15.35 ?  144 VAL   B CB   1 
ATOM   6238 C CG1  . VAL   B 1 144 ? 29.495 -28.410 -9.198  1.00 17.62 ?  144 VAL   B CG1  1 
ATOM   6239 C CG2  . VAL   B 1 144 ? 32.013 -28.691 -9.143  1.00 15.76 ?  144 VAL   B CG2  1 
ATOM   6240 H H    . VAL   B 1 144 ? 32.044 -27.739 -6.374  1.00 14.61 ?  144 VAL   B H    1 
ATOM   6241 H HA   . VAL   B 1 144 ? 31.315 -26.340 -8.451  1.00 15.70 ?  144 VAL   B HA   1 
ATOM   6242 H HB   . VAL   B 1 144 ? 30.670 -28.939 -7.625  1.00 18.40 ?  144 VAL   B HB   1 
ATOM   6243 H HG11 . VAL   B 1 144 ? 29.570 -29.188 -9.778  1.00 21.12 ?  144 VAL   B HG11 1 
ATOM   6244 H HG12 . VAL   B 1 144 ? 28.731 -28.517 -8.611  1.00 21.12 ?  144 VAL   B HG12 1 
ATOM   6245 H HG13 . VAL   B 1 144 ? 29.401 -27.611 -9.735  1.00 21.12 ?  144 VAL   B HG13 1 
ATOM   6246 H HG21 . VAL   B 1 144 ? 31.897 -29.584 -9.507  1.00 18.89 ?  144 VAL   B HG21 1 
ATOM   6247 H HG22 . VAL   B 1 144 ? 32.135 -28.056 -9.870  1.00 18.89 ?  144 VAL   B HG22 1 
ATOM   6248 H HG23 . VAL   B 1 144 ? 32.777 -28.669 -8.552  1.00 18.89 ?  144 VAL   B HG23 1 
ATOM   6249 N N    . ASP   B 1 145 ? 29.107 -26.517 -6.172  1.00 13.21 ?  145 ASP   B N    1 
ATOM   6250 C CA   . ASP   B 1 145 ? 27.795 -26.048 -5.755  1.00 13.83 ?  145 ASP   B CA   1 
ATOM   6251 C C    . ASP   B 1 145 ? 27.817 -24.626 -5.203  1.00 13.67 ?  145 ASP   B C    1 
ATOM   6252 O O    . ASP   B 1 145 ? 26.754 -24.090 -4.872  1.00 15.12 ?  145 ASP   B O    1 
ATOM   6253 C CB   . ASP   B 1 145 ? 27.205 -26.974 -4.684  1.00 15.16 ?  145 ASP   B CB   1 
ATOM   6254 C CG   . ASP   B 1 145 ? 26.846 -28.350 -5.209  1.00 16.53 ?  145 ASP   B CG   1 
ATOM   6255 O OD1  . ASP   B 1 145 ? 26.765 -28.538 -6.439  1.00 16.91 ?  145 ASP   B OD1  1 
ATOM   6256 O OD2  . ASP   B 1 145 ? 26.647 -29.246 -4.366  1.00 19.26 -1 145 ASP   B OD2  1 
ATOM   6257 H H    . ASP   B 1 145 ? 29.539 -26.949 -5.567  1.00 15.82 ?  145 ASP   B H    1 
ATOM   6258 H HA   . ASP   B 1 145 ? 27.205 -26.050 -6.524  1.00 16.57 ?  145 ASP   B HA   1 
ATOM   6259 H HB2  . ASP   B 1 145 ? 27.853 -27.102 -3.985  1.00 18.17 ?  145 ASP   B HB2  1 
ATOM   6260 H HB3  . ASP   B 1 145 ? 26.398 -26.566 -4.332  1.00 18.17 ?  145 ASP   B HB3  1 
ATOM   6261 N N    . THR   B 1 146 ? 28.990 -24.010 -5.081  1.00 12.30 ?  146 THR   B N    1 
ATOM   6262 C CA   . THR   B 1 146 ? 29.114 -22.690 -4.467  1.00 11.99 ?  146 THR   B CA   1 
ATOM   6263 C C    . THR   B 1 146 ? 29.758 -21.659 -5.376  1.00 11.62 ?  146 THR   B C    1 
ATOM   6264 O O    . THR   B 1 146 ? 29.308 -20.500 -5.417  1.00 12.34 ?  146 THR   B O    1 
ATOM   6265 C CB   . THR   B 1 146 ? 29.949 -22.797 -3.182  1.00 12.29 ?  146 THR   B CB   1 
ATOM   6266 O OG1  . THR   B 1 146 ? 29.384 -23.791 -2.324  1.00 12.37 ?  146 THR   B OG1  1 
ATOM   6267 C CG2  . THR   B 1 146 ? 30.015 -21.464 -2.451  1.00 12.46 ?  146 THR   B CG2  1 
ATOM   6268 H H    . THR   B 1 146 ? 29.741 -24.336 -5.349  1.00 14.74 ?  146 THR   B H    1 
ATOM   6269 H HA   . THR   B 1 146 ? 28.237 -22.365 -4.228  1.00 14.37 ?  146 THR   B HA   1 
ATOM   6270 H HB   . THR   B 1 146 ? 30.856 -23.052 -3.410  1.00 14.72 ?  146 THR   B HB   1 
ATOM   6271 H HG1  . THR   B 1 146 ? 29.413 -24.548 -2.707  1.00 14.82 ?  146 THR   B HG1  1 
ATOM   6272 H HG21 . THR   B 1 146 ? 30.369 -21.593 -1.559  1.00 14.93 ?  146 THR   B HG21 1 
ATOM   6273 H HG22 . THR   B 1 146 ? 30.596 -20.849 -2.932  1.00 14.93 ?  146 THR   B HG22 1 
ATOM   6274 H HG23 . THR   B 1 146 ? 29.130 -21.076 -2.388  1.00 14.93 ?  146 THR   B HG23 1 
ATOM   6275 N N    . VAL   B 1 147 ? 30.825 -22.031 -6.070  1.00 11.57 ?  147 VAL   B N    1 
ATOM   6276 C CA   . VAL   B 1 147 ? 31.555 -21.089 -6.903  1.00 11.42 ?  147 VAL   B CA   1 
ATOM   6277 C C    . VAL   B 1 147 ? 30.834 -20.954 -8.233  1.00 11.48 ?  147 VAL   B C    1 
ATOM   6278 O O    . VAL   B 1 147 ? 30.472 -21.955 -8.865  1.00 12.36 ?  147 VAL   B O    1 
ATOM   6279 C CB   . VAL   B 1 147 ? 33.009 -21.550 -7.100  1.00 11.53 ?  147 VAL   B CB   1 
ATOM   6280 C CG1  . VAL   B 1 147 ? 33.768 -20.526 -7.921  1.00 11.88 ?  147 VAL   B CG1  1 
ATOM   6281 C CG2  . VAL   B 1 147 ? 33.686 -21.753 -5.754  1.00 11.72 ?  147 VAL   B CG2  1 
ATOM   6282 H H    . VAL   B 1 147 ? 31.150 -22.828 -6.079  1.00 13.86 ?  147 VAL   B H    1 
ATOM   6283 H HA   . VAL   B 1 147 ? 31.572 -20.220 -6.470  1.00 13.69 ?  147 VAL   B HA   1 
ATOM   6284 H HB   . VAL   B 1 147 ? 33.017 -22.398 -7.577  1.00 13.82 ?  147 VAL   B HB   1 
ATOM   6285 H HG11 . VAL   B 1 147 ? 34.714 -20.741 -7.897  1.00 14.23 ?  147 VAL   B HG11 1 
ATOM   6286 H HG12 . VAL   B 1 147 ? 33.448 -20.551 -8.836  1.00 14.23 ?  147 VAL   B HG12 1 
ATOM   6287 H HG13 . VAL   B 1 147 ? 33.620 -19.646 -7.540  1.00 14.23 ?  147 VAL   B HG13 1 
ATOM   6288 H HG21 . VAL   B 1 147 ? 34.624 -21.960 -5.898  1.00 14.04 ?  147 VAL   B HG21 1 
ATOM   6289 H HG22 . VAL   B 1 147 ? 33.607 -20.936 -5.235  1.00 14.04 ?  147 VAL   B HG22 1 
ATOM   6290 H HG23 . VAL   B 1 147 ? 33.256 -22.485 -5.285  1.00 14.04 ?  147 VAL   B HG23 1 
ATOM   6291 N N    . ARG   B 1 148 ? 30.621 -19.705 -8.652  1.00 11.42 ?  148 ARG   B N    1 
ATOM   6292 C CA   . ARG   B 1 148 ? 30.005 -19.384 -9.929  1.00 11.81 ?  148 ARG   B CA   1 
ATOM   6293 C C    . ARG   B 1 148 ? 30.969 -18.722 -10.900 1.00 12.00 ?  148 ARG   B C    1 
ATOM   6294 O O    . ARG   B 1 148 ? 30.694 -18.702 -12.101 1.00 13.77 ?  148 ARG   B O    1 
ATOM   6295 C CB   . ARG   B 1 148 ? 28.775 -18.488 -9.717  1.00 12.42 ?  148 ARG   B CB   1 
ATOM   6296 C CG   . ARG   B 1 148 ? 27.677 -19.183 -8.923  1.00 12.83 ?  148 ARG   B CG   1 
ATOM   6297 C CD   . ARG   B 1 148 ? 26.493 -18.274 -8.607  1.00 13.59 ?  148 ARG   B CD   1 
ATOM   6298 N NE   . ARG   B 1 148 ? 26.893 -17.084 -7.863  1.00 13.54 ?  148 ARG   B NE   1 
ATOM   6299 C CZ   . ARG   B 1 148 ? 27.174 -17.057 -6.566  1.00 12.65 ?  148 ARG   B CZ   1 
ATOM   6300 N NH1  . ARG   B 1 148 ? 27.089 -18.142 -5.810  1.00 12.80 ?  148 ARG   B NH1  1 
ATOM   6301 N NH2  . ARG   B 1 148 ? 27.580 -15.914 -6.016  1.00 12.82 ?  148 ARG   B NH2  1 
ATOM   6302 H H    . ARG   B 1 148 ? 30.849 -19.005 -8.198  1.00 13.68 ?  148 ARG   B H    1 
ATOM   6303 H HA   . ARG   B 1 148 ? 29.702 -20.206 -10.337 1.00 14.15 ?  148 ARG   B HA   1 
ATOM   6304 H HB2  . ARG   B 1 148 ? 29.043 -17.692 -9.226  1.00 14.89 ?  148 ARG   B HB2  1 
ATOM   6305 H HB3  . ARG   B 1 148 ? 28.414 -18.237 -10.581 1.00 14.89 ?  148 ARG   B HB3  1 
ATOM   6306 H HG2  . ARG   B 1 148 ? 27.341 -19.935 -9.442  1.00 15.37 ?  148 ARG   B HG2  1 
ATOM   6307 H HG3  . ARG   B 1 148 ? 28.042 -19.502 -8.084  1.00 15.37 ?  148 ARG   B HG3  1 
ATOM   6308 H HD2  . ARG   B 1 148 ? 26.087 -17.982 -9.436  1.00 16.28 ?  148 ARG   B HD2  1 
ATOM   6309 H HD3  . ARG   B 1 148 ? 25.850 -18.763 -8.072  1.00 16.28 ?  148 ARG   B HD3  1 
ATOM   6310 H HE   . ARG   B 1 148 ? 26.964 -16.349 -8.295  1.00 16.22 ?  148 ARG   B HE   1 
ATOM   6311 H HH11 . ARG   B 1 148 ? 26.824 -18.888 -6.148  1.00 15.34 ?  148 ARG   B HH11 1 
ATOM   6312 H HH12 . ARG   B 1 148 ? 27.270 -18.099 -4.967  1.00 15.34 ?  148 ARG   B HH12 1 
ATOM   6313 H HH21 . ARG   B 1 148 ? 27.648 -15.207 -6.497  1.00 15.36 ?  148 ARG   B HH21 1 
ATOM   6314 H HH22 . ARG   B 1 148 ? 27.767 -15.880 -5.176  1.00 15.36 ?  148 ARG   B HH22 1 
ATOM   6315 N N    . THR   B 1 149 ? 32.073 -18.167 -10.408 1.00 11.71 ?  149 THR   B N    1 
ATOM   6316 C CA   . THR   B 1 149 ? 33.119 -17.617 -11.253 1.00 11.90 ?  149 THR   B CA   1 
ATOM   6317 C C    . THR   B 1 149 ? 34.012 -18.755 -11.753 1.00 11.55 ?  149 THR   B C    1 
ATOM   6318 O O    . THR   B 1 149 ? 33.819 -19.926 -11.411 1.00 11.95 ?  149 THR   B O    1 
ATOM   6319 C CB   . THR   B 1 149 ? 33.890 -16.563 -10.472 1.00 11.67 ?  149 THR   B CB   1 
ATOM   6320 O OG1  . THR   B 1 149 ? 34.332 -17.155 -9.248  1.00 12.06 ?  149 THR   B OG1  1 
ATOM   6321 C CG2  . THR   B 1 149 ? 33.000 -15.357 -10.188 1.00 12.89 ?  149 THR   B CG2  1 
ATOM   6322 H H    . THR   B 1 149 ? 32.236 -18.093 -9.570  1.00 14.03 ?  149 THR   B H    1 
ATOM   6323 H HA   . THR   B 1 149 ? 32.715 -17.187 -12.025 1.00 14.26 ?  149 THR   B HA   1 
ATOM   6324 H HB   . THR   B 1 149 ? 34.659 -16.280 -10.988 1.00 13.98 ?  149 THR   B HB   1 
ATOM   6325 H HG1  . THR   B 1 149 ? 34.756 -16.587 -8.790  1.00 14.44 ?  149 THR   B HG1  1 
ATOM   6326 H HG21 . THR   B 1 149 ? 33.509 -14.683 -9.707  1.00 15.44 ?  149 THR   B HG21 1 
ATOM   6327 H HG22 . THR   B 1 149 ? 32.688 -14.975 -11.024 1.00 15.44 ?  149 THR   B HG22 1 
ATOM   6328 H HG23 . THR   B 1 149 ? 32.239 -15.621 -9.655  1.00 15.44 ?  149 THR   B HG23 1 
ATOM   6329 N N    . ASN   B 1 150 ? 34.981 -18.430 -12.602 1.00 11.55 ?  150 ASN   B N    1 
ATOM   6330 C CA   . ASN   B 1 150 ? 35.747 -19.457 -13.299 1.00 11.88 ?  150 ASN   B CA   1 
ATOM   6331 C C    . ASN   B 1 150 ? 36.904 -19.907 -12.420 1.00 11.78 ?  150 ASN   B C    1 
ATOM   6332 O O    . ASN   B 1 150 ? 37.826 -19.132 -12.145 1.00 12.42 ?  150 ASN   B O    1 
ATOM   6333 C CB   . ASN   B 1 150 ? 36.224 -18.928 -14.644 1.00 13.19 ?  150 ASN   B CB   1 
ATOM   6334 C CG   . ASN   B 1 150 ? 35.080 -18.706 -15.593 1.00 16.15 ?  150 ASN   B CG   1 
ATOM   6335 O OD1  . ASN   B 1 150 ? 34.184 -19.536 -15.682 1.00 17.75 ?  150 ASN   B OD1  1 
ATOM   6336 N ND2  . ASN   B 1 150 ? 35.077 -17.573 -16.279 1.00 17.57 ?  150 ASN   B ND2  1 
ATOM   6337 H H    . ASN   B 1 150 ? 35.223 -17.622 -12.789 1.00 13.83 ?  150 ASN   B H    1 
ATOM   6338 H HA   . ASN   B 1 150 ? 35.167 -20.222 -13.470 1.00 14.23 ?  150 ASN   B HA   1 
ATOM   6339 H HB2  . ASN   B 1 150 ? 36.670 -18.076 -14.512 1.00 15.80 ?  150 ASN   B HB2  1 
ATOM   6340 H HB3  . ASN   B 1 150 ? 36.832 -19.566 -15.046 1.00 15.80 ?  150 ASN   B HB3  1 
ATOM   6341 H HD21 . ASN   B 1 150 ? 34.442 -17.406 -16.838 1.00 21.05 ?  150 ASN   B HD21 1 
ATOM   6342 H HD22 . ASN   B 1 150 ? 35.721 -17.009 -16.186 1.00 21.05 ?  150 ASN   B HD22 1 
ATOM   6343 N N    . VAL   B 1 151 ? 36.860 -21.159 -11.979 1.00 11.37 ?  151 VAL   B N    1 
ATOM   6344 C CA   . VAL   B 1 151 ? 37.877 -21.693 -11.088 1.00 11.37 ?  151 VAL   B CA   1 
ATOM   6345 C C    . VAL   B 1 151 ? 38.592 -22.862 -11.758 1.00 11.34 ?  151 VAL   B C    1 
ATOM   6346 O O    . VAL   B 1 151 ? 37.960 -23.796 -12.273 1.00 12.11 ?  151 VAL   B O    1 
ATOM   6347 C CB   . VAL   B 1 151 ? 37.317 -22.023 -9.690  1.00 12.52 ?  151 VAL   B CB   1 
ATOM   6348 C CG1  . VAL   B 1 151 ? 36.166 -23.024 -9.762  1.00 13.36 ?  151 VAL   B CG1  1 
ATOM   6349 C CG2  . VAL   B 1 151 ? 38.431 -22.505 -8.767  1.00 13.03 ?  151 VAL   B CG2  1 
ATOM   6350 H H    . VAL   B 1 151 ? 36.242 -21.726 -12.193 1.00 13.62 ?  151 VAL   B H    1 
ATOM   6351 H HA   . VAL   B 1 151 ? 38.540 -20.999 -10.958 1.00 13.62 ?  151 VAL   B HA   1 
ATOM   6352 H HB   . VAL   B 1 151 ? 36.961 -21.206 -9.306  1.00 15.00 ?  151 VAL   B HB   1 
ATOM   6353 H HG11 . VAL   B 1 151 ? 35.850 -23.209 -8.864  1.00 16.00 ?  151 VAL   B HG11 1 
ATOM   6354 H HG12 . VAL   B 1 151 ? 35.449 -22.648 -10.295 1.00 16.00 ?  151 VAL   B HG12 1 
ATOM   6355 H HG13 . VAL   B 1 151 ? 36.486 -23.846 -10.173 1.00 16.00 ?  151 VAL   B HG13 1 
ATOM   6356 H HG21 . VAL   B 1 151 ? 38.082 -22.584 -7.865  1.00 15.62 ?  151 VAL   B HG21 1 
ATOM   6357 H HG22 . VAL   B 1 151 ? 38.751 -23.367 -9.074  1.00 15.62 ?  151 VAL   B HG22 1 
ATOM   6358 H HG23 . VAL   B 1 151 ? 39.157 -21.858 -8.782  1.00 15.62 ?  151 VAL   B HG23 1 
ATOM   6359 N N    . TYR   B 1 152 ? 39.917 -22.769 -11.769 1.00 10.75 ?  152 TYR   B N    1 
ATOM   6360 C CA   . TYR   B 1 152 ? 40.830 -23.746 -12.343 1.00 10.97 ?  152 TYR   B CA   1 
ATOM   6361 C C    . TYR   B 1 152 ? 41.548 -24.418 -11.178 1.00 10.30 ?  152 TYR   B C    1 
ATOM   6362 O O    . TYR   B 1 152 ? 42.382 -23.797 -10.515 1.00 10.89 ?  152 TYR   B O    1 
ATOM   6363 C CB   . TYR   B 1 152 ? 41.798 -23.032 -13.290 1.00 11.74 ?  152 TYR   B CB   1 
ATOM   6364 C CG   . TYR   B 1 152 ? 41.117 -22.570 -14.559 1.00 12.11 ?  152 TYR   B CG   1 
ATOM   6365 C CD1  . TYR   B 1 152 ? 40.443 -21.353 -14.624 1.00 12.49 ?  152 TYR   B CD1  1 
ATOM   6366 C CD2  . TYR   B 1 152 ? 41.131 -23.371 -15.690 1.00 13.14 ?  152 TYR   B CD2  1 
ATOM   6367 C CE1  . TYR   B 1 152 ? 39.804 -20.953 -15.789 1.00 13.70 ?  152 TYR   B CE1  1 
ATOM   6368 C CE2  . TYR   B 1 152 ? 40.501 -22.983 -16.853 1.00 13.87 ?  152 TYR   B CE2  1 
ATOM   6369 C CZ   . TYR   B 1 152 ? 39.838 -21.771 -16.902 1.00 14.03 ?  152 TYR   B CZ   1 
ATOM   6370 O OH   . TYR   B 1 152 ? 39.214 -21.392 -18.066 1.00 16.59 ?  152 TYR   B OH   1 
ATOM   6371 H H    . TYR   B 1 152 ? 40.340 -22.097 -11.425 1.00 12.88 ?  152 TYR   B H    1 
ATOM   6372 H HA   . TYR   B 1 152 ? 40.331 -24.414 -12.841 1.00 13.14 ?  152 TYR   B HA   1 
ATOM   6373 H HB2  . TYR   B 1 152 ? 42.161 -22.253 -12.837 1.00 14.07 ?  152 TYR   B HB2  1 
ATOM   6374 H HB3  . TYR   B 1 152 ? 42.514 -23.640 -13.529 1.00 14.07 ?  152 TYR   B HB3  1 
ATOM   6375 H HD1  . TYR   B 1 152 ? 40.411 -20.803 -13.874 1.00 14.97 ?  152 TYR   B HD1  1 
ATOM   6376 H HD2  . TYR   B 1 152 ? 41.577 -24.189 -15.661 1.00 15.74 ?  152 TYR   B HD2  1 
ATOM   6377 H HE1  . TYR   B 1 152 ? 39.356 -20.139 -15.823 1.00 16.42 ?  152 TYR   B HE1  1 
ATOM   6378 H HE2  . TYR   B 1 152 ? 40.531 -23.535 -17.599 1.00 16.62 ?  152 TYR   B HE2  1 
ATOM   6379 H HH   . TYR   B 1 152 ? 39.324 -21.988 -18.651 1.00 19.88 ?  152 TYR   B HH   1 
ATOM   6380 N N    . LEU   B 1 153 ? 41.181 -25.674 -10.907 1.00 10.71 ?  153 LEU   B N    1 
ATOM   6381 C CA   . LEU   B 1 153 ? 41.687 -26.423 -9.766  1.00 10.09 ?  153 LEU   B CA   1 
ATOM   6382 C C    . LEU   B 1 153 ? 42.922 -27.220 -10.159 1.00 10.30 ?  153 LEU   B C    1 
ATOM   6383 O O    . LEU   B 1 153 ? 42.908 -27.950 -11.152 1.00 11.34 ?  153 LEU   B O    1 
ATOM   6384 C CB   . LEU   B 1 153 ? 40.605 -27.379 -9.255  1.00 10.94 ?  153 LEU   B CB   1 
ATOM   6385 C CG   . LEU   B 1 153 ? 39.343 -26.724 -8.693  1.00 11.61 ?  153 LEU   B CG   1 
ATOM   6386 C CD1  . LEU   B 1 153 ? 38.255 -27.778 -8.554  1.00 12.18 ?  153 LEU   B CD1  1 
ATOM   6387 C CD2  . LEU   B 1 153 ? 39.624 -26.059 -7.355  1.00 12.49 ?  153 LEU   B CD2  1 
ATOM   6388 H H    . LEU   B 1 153 ? 40.618 -26.120 -11.384 1.00 12.83 ?  153 LEU   B H    1 
ATOM   6389 H HA   . LEU   B 1 153 ? 41.918 -25.810 -9.054  1.00 12.08 ?  153 LEU   B HA   1 
ATOM   6390 H HB2  . LEU   B 1 153 ? 40.330 -27.952 -9.985  1.00 13.10 ?  153 LEU   B HB2  1 
ATOM   6391 H HB3  . LEU   B 1 153 ? 40.985 -27.921 -8.545  1.00 13.10 ?  153 LEU   B HB3  1 
ATOM   6392 H HG   . LEU   B 1 153 ? 39.026 -26.044 -9.308  1.00 13.90 ?  153 LEU   B HG   1 
ATOM   6393 H HD11 . LEU   B 1 153 ? 37.444 -27.357 -8.216  1.00 14.59 ?  153 LEU   B HD11 1 
ATOM   6394 H HD12 . LEU   B 1 153 ? 38.081 -28.170 -9.423  1.00 14.59 ?  153 LEU   B HD12 1 
ATOM   6395 H HD13 . LEU   B 1 153 ? 38.551 -28.461 -7.934  1.00 14.59 ?  153 LEU   B HD13 1 
ATOM   6396 H HD21 . LEU   B 1 153 ? 38.801 -25.680 -7.005  1.00 14.96 ?  153 LEU   B HD21 1 
ATOM   6397 H HD22 . LEU   B 1 153 ? 39.969 -26.723 -6.736  1.00 14.96 ?  153 LEU   B HD22 1 
ATOM   6398 H HD23 . LEU   B 1 153 ? 40.281 -25.356 -7.483  1.00 14.96 ?  153 LEU   B HD23 1 
ATOM   6399 N N    . ALA   B 1 154 ? 43.974 -27.109 -9.357  1.00 10.49 ?  154 ALA   B N    1 
ATOM   6400 C CA   . ALA   B 1 154 ? 45.205 -27.869 -9.532  1.00 11.61 ?  154 ALA   B CA   1 
ATOM   6401 C C    . ALA   B 1 154 ? 45.262 -28.947 -8.456  1.00 12.04 ?  154 ALA   B C    1 
ATOM   6402 O O    . ALA   B 1 154 ? 45.178 -28.648 -7.257  1.00 13.44 ?  154 ALA   B O    1 
ATOM   6403 C CB   . ALA   B 1 154 ? 46.423 -26.949 -9.453  1.00 12.75 ?  154 ALA   B CB   1 
ATOM   6404 H H    . ALA   B 1 154 ? 43.999 -26.572 -8.684  1.00 12.57 ?  154 ALA   B H    1 
ATOM   6405 H HA   . ALA   B 1 154 ? 45.203 -28.297 -10.402 1.00 13.91 ?  154 ALA   B HA   1 
ATOM   6406 H HB1  . ALA   B 1 154 ? 47.228 -27.473 -9.571  1.00 15.28 ?  154 ALA   B HB1  1 
ATOM   6407 H HB2  . ALA   B 1 154 ? 46.361 -26.276 -10.154 1.00 15.28 ?  154 ALA   B HB2  1 
ATOM   6408 H HB3  . ALA   B 1 154 ? 46.436 -26.512 -8.584  1.00 15.28 ?  154 ALA   B HB3  1 
ATOM   6409 N N    . VAL   B 1 155 ? 45.383 -30.198 -8.888  1.00 11.32 ?  155 VAL   B N    1 
ATOM   6410 C CA   . VAL   B 1 155 ? 45.489 -31.348 -7.997  1.00 11.50 ?  155 VAL   B CA   1 
ATOM   6411 C C    . VAL   B 1 155 ? 46.832 -32.023 -8.269  1.00 11.41 ?  155 VAL   B C    1 
ATOM   6412 O O    . VAL   B 1 155 ? 47.073 -32.520 -9.377  1.00 13.13 ?  155 VAL   B O    1 
ATOM   6413 C CB   . VAL   B 1 155 ? 44.330 -32.336 -8.203  1.00 13.24 ?  155 VAL   B CB   1 
ATOM   6414 C CG1  . VAL   B 1 155 ? 44.503 -33.539 -7.286  1.00 13.27 ?  155 VAL   B CG1  1 
ATOM   6415 C CG2  . VAL   B 1 155 ? 42.992 -31.647 -7.970  1.00 13.89 ?  155 VAL   B CG2  1 
ATOM   6416 H H    . VAL   B 1 155 ? 45.415 -30.411 -9.722  1.00 13.56 ?  155 VAL   B H    1 
ATOM   6417 H HA   . VAL   B 1 155 ? 45.478 -31.050 -7.076  1.00 13.77 ?  155 VAL   B HA   1 
ATOM   6418 H HB   . VAL   B 1 155 ? 44.350 -32.653 -9.120  1.00 15.87 ?  155 VAL   B HB   1 
ATOM   6419 H HG11 . VAL   B 1 155 ? 43.677 -34.042 -7.265  1.00 15.90 ?  155 VAL   B HG11 1 
ATOM   6420 H HG12 . VAL   B 1 155 ? 45.222 -34.102 -7.628  1.00 15.90 ?  155 VAL   B HG12 1 
ATOM   6421 H HG13 . VAL   B 1 155 ? 44.728 -33.229 -6.394  1.00 15.90 ?  155 VAL   B HG13 1 
ATOM   6422 H HG21 . VAL   B 1 155 ? 42.284 -32.302 -8.055  1.00 16.64 ?  155 VAL   B HG21 1 
ATOM   6423 H HG22 . VAL   B 1 155 ? 42.989 -31.267 -7.077  1.00 16.64 ?  155 VAL   B HG22 1 
ATOM   6424 H HG23 . VAL   B 1 155 ? 42.880 -30.945 -8.629  1.00 16.64 ?  155 VAL   B HG23 1 
ATOM   6425 N N    . PHE   B 1 156 ? 47.697 -32.056 -7.253  1.00 11.79 ?  156 PHE   B N    1 
ATOM   6426 C CA   . PHE   B 1 156 ? 49.074 -32.509 -7.446  1.00 12.95 ?  156 PHE   B CA   1 
ATOM   6427 C C    . PHE   B 1 156 ? 49.170 -34.008 -7.725  1.00 13.90 ?  156 PHE   B C    1 
ATOM   6428 O O    . PHE   B 1 156 ? 49.907 -34.435 -8.624  1.00 15.66 ?  156 PHE   B O    1 
ATOM   6429 C CB   . PHE   B 1 156 ? 49.900 -32.142 -6.214  1.00 13.07 ?  156 PHE   B CB   1 
ATOM   6430 C CG   . PHE   B 1 156 ? 51.322 -32.603 -6.274  1.00 13.64 ?  156 PHE   B CG   1 
ATOM   6431 C CD1  . PHE   B 1 156 ? 52.207 -32.047 -7.179  1.00 15.65 ?  156 PHE   B CD1  1 
ATOM   6432 C CD2  . PHE   B 1 156 ? 51.780 -33.579 -5.411  1.00 13.75 ?  156 PHE   B CD2  1 
ATOM   6433 C CE1  . PHE   B 1 156 ? 53.525 -32.458 -7.230  1.00 16.56 ?  156 PHE   B CE1  1 
ATOM   6434 C CE2  . PHE   B 1 156 ? 53.101 -33.997 -5.458  1.00 15.27 ?  156 PHE   B CE2  1 
ATOM   6435 C CZ   . PHE   B 1 156 ? 53.966 -33.434 -6.371  1.00 16.19 ?  156 PHE   B CZ   1 
ATOM   6436 H H    . PHE   B 1 156 ? 47.509 -31.831 -6.444  1.00 14.12 ?  156 PHE   B H    1 
ATOM   6437 H HA   . PHE   B 1 156 ? 49.451 -32.037 -8.205  1.00 15.52 ?  156 PHE   B HA   1 
ATOM   6438 H HB2  . PHE   B 1 156 ? 49.911 -31.177 -6.120  1.00 15.66 ?  156 PHE   B HB2  1 
ATOM   6439 H HB3  . PHE   B 1 156 ? 49.494 -32.544 -5.432  1.00 15.66 ?  156 PHE   B HB3  1 
ATOM   6440 H HD1  . PHE   B 1 156 ? 51.911 -31.384 -7.763  1.00 18.76 ?  156 PHE   B HD1  1 
ATOM   6441 H HD2  . PHE   B 1 156 ? 51.197 -33.963 -4.796  1.00 16.47 ?  156 PHE   B HD2  1 
ATOM   6442 H HE1  . PHE   B 1 156 ? 54.109 -32.078 -7.849  1.00 19.84 ?  156 PHE   B HE1  1 
ATOM   6443 H HE2  . PHE   B 1 156 ? 53.401 -34.663 -4.879  1.00 18.29 ?  156 PHE   B HE2  1 
ATOM   6444 H HZ   . PHE   B 1 156 ? 54.853 -33.717 -6.408  1.00 19.40 ?  156 PHE   B HZ   1 
ATOM   6445 N N    . ASP   B 1 157 ? 48.499 -34.826 -6.923  1.00 14.09 ?  157 ASP   B N    1 
ATOM   6446 C CA   . ASP   B 1 157 ? 48.646 -36.275 -7.010  1.00 15.30 ?  157 ASP   B CA   1 
ATOM   6447 C C    . ASP   B 1 157 ? 47.736 -36.829 -8.102  1.00 15.46 ?  157 ASP   B C    1 
ATOM   6448 O O    . ASP   B 1 157 ? 46.509 -36.709 -8.012  1.00 14.87 ?  157 ASP   B O    1 
ATOM   6449 C CB   . ASP   B 1 157 ? 48.284 -36.886 -5.663  1.00 16.64 ?  157 ASP   B CB   1 
ATOM   6450 C CG   . ASP   B 1 157 ? 48.428 -38.400 -5.645  1.00 18.50 ?  157 ASP   B CG   1 
ATOM   6451 O OD1  . ASP   B 1 157 ? 48.757 -39.002 -6.693  1.00 19.01 ?  157 ASP   B OD1  1 
ATOM   6452 O OD2  . ASP   B 1 157 ? 48.227 -38.987 -4.566  1.00 20.32 -1 157 ASP   B OD2  1 
ATOM   6453 H H    . ASP   B 1 157 ? 47.963 -34.563 -6.313  1.00 16.88 ?  157 ASP   B H    1 
ATOM   6454 H HA   . ASP   B 1 157 ? 49.568 -36.505 -7.223  1.00 18.34 ?  157 ASP   B HA   1 
ATOM   6455 H HB2  . ASP   B 1 157 ? 48.859 -36.504 -4.985  1.00 19.94 ?  157 ASP   B HB2  1 
ATOM   6456 H HB3  . ASP   B 1 157 ? 47.355 -36.669 -5.467  1.00 19.94 ?  157 ASP   B HB3  1 
ATOM   6457 N N    . LYS   B 1 158 ? 48.340 -37.442 -9.127  1.00 16.33 ?  158 LYS   B N    1 
ATOM   6458 C CA   . LYS   B 1 158 ? 47.565 -38.041 -10.215 1.00 17.36 ?  158 LYS   B CA   1 
ATOM   6459 C C    . LYS   B 1 158 ? 46.506 -39.013 -9.693  1.00 16.82 ?  158 LYS   B C    1 
ATOM   6460 O O    . LYS   B 1 158 ? 45.402 -39.100 -10.244 1.00 17.18 ?  158 LYS   B O    1 
ATOM   6461 C CB   . LYS   B 1 158 ? 48.513 -38.752 -11.188 1.00 19.23 ?  158 LYS   B CB   1 
ATOM   6462 C CG   . LYS   B 1 158 ? 47.836 -39.649 -12.212 1.00 21.17 ?  158 LYS   B CG   1 
ATOM   6463 C CD   . LYS   B 1 158 ? 46.982 -38.871 -13.189 1.00 23.29 ?  158 LYS   B CD   1 
ATOM   6464 C CE   . LYS   B 1 158 ? 46.415 -39.795 -14.254 1.00 25.04 ?  158 LYS   B CE   1 
ATOM   6465 N NZ   . LYS   B 1 158 ? 45.334 -39.141 -15.045 1.00 25.12 ?  158 LYS   B NZ   1 
ATOM   6466 H H    . LYS   B 1 158 ? 49.193 -37.527 -9.213  1.00 19.57 ?  158 LYS   B H    1 
ATOM   6467 H HA   . LYS   B 1 158 ? 47.113 -37.337 -10.707 1.00 20.81 ?  158 LYS   B HA   1 
ATOM   6468 H HB2  . LYS   B 1 158 ? 49.014 -38.078 -11.683 1.00 23.06 ?  158 LYS   B HB2  1 
ATOM   6469 H HB3  . LYS   B 1 158 ? 49.129 -39.299 -10.679 1.00 23.06 ?  158 LYS   B HB3  1 
ATOM   6470 H HG2  . LYS   B 1 158 ? 48.521 -40.111 -12.723 1.00 25.38 ?  158 LYS   B HG2  1 
ATOM   6471 H HG3  . LYS   B 1 158 ? 47.274 -40.303 -11.765 1.00 25.38 ?  158 LYS   B HG3  1 
ATOM   6472 H HD2  . LYS   B 1 158 ? 46.244 -38.456 -12.717 1.00 27.92 ?  158 LYS   B HD2  1 
ATOM   6473 H HD3  . LYS   B 1 158 ? 47.526 -38.198 -13.629 1.00 27.92 ?  158 LYS   B HD3  1 
ATOM   6474 H HE2  . LYS   B 1 158 ? 47.120 -40.052 -14.865 1.00 30.02 ?  158 LYS   B HE2  1 
ATOM   6475 H HE3  . LYS   B 1 158 ? 46.040 -40.582 -13.826 1.00 30.02 ?  158 LYS   B HE3  1 
ATOM   6476 H HZ1  . LYS   B 1 158 ? 45.021 -39.705 -15.657 1.00 30.12 ?  158 LYS   B HZ1  1 
ATOM   6477 H HZ2  . LYS   B 1 158 ? 44.668 -38.899 -14.506 1.00 30.12 ?  158 LYS   B HZ2  1 
ATOM   6478 H HZ3  . LYS   B 1 158 ? 45.653 -38.418 -15.453 1.00 30.12 ?  158 LYS   B HZ3  1 
ATOM   6479 N N    . ASN   B 1 159 ? 46.828 -39.776 -8.648  1.00 16.72 ?  159 ASN   B N    1 
ATOM   6480 C CA   . ASN   B 1 159 ? 45.866 -40.753 -8.148  1.00 17.38 ?  159 ASN   B CA   1 
ATOM   6481 C C    . ASN   B 1 159 ? 44.668 -40.077 -7.481  1.00 16.55 ?  159 ASN   B C    1 
ATOM   6482 O O    . ASN   B 1 159 ? 43.534 -40.564 -7.595  1.00 16.81 ?  159 ASN   B O    1 
ATOM   6483 C CB   . ASN   B 1 159 ? 46.559 -41.729 -7.209  1.00 19.04 ?  159 ASN   B CB   1 
ATOM   6484 C CG   . ASN   B 1 159 ? 47.595 -42.567 -7.918  1.00 21.21 ?  159 ASN   B CG   1 
ATOM   6485 O OD1  . ASN   B 1 159 ? 47.350 -43.083 -9.016  1.00 22.30 ?  159 ASN   B OD1  1 
ATOM   6486 N ND2  . ASN   B 1 159 ? 48.762 -42.720 -7.295  1.00 21.88 ?  159 ASN   B ND2  1 
ATOM   6487 H H    . ASN   B 1 159 ? 47.577 -39.744 -8.230  1.00 20.04 ?  159 ASN   B H    1 
ATOM   6488 H HA   . ASN   B 1 159 ? 45.532 -41.258 -8.906  1.00 20.83 ?  159 ASN   B HA   1 
ATOM   6489 H HB2  . ASN   B 1 159 ? 47.004 -41.237 -6.505  1.00 22.82 ?  159 ASN   B HB2  1 
ATOM   6490 H HB3  . ASN   B 1 159 ? 45.899 -42.331 -6.837  1.00 22.82 ?  159 ASN   B HB3  1 
ATOM   6491 H HD21 . ASN   B 1 159 ? 49.391 -43.186 -7.657  1.00 26.24 ?  159 ASN   B HD21 1 
ATOM   6492 H HD22 . ASN   B 1 159 ? 48.891 -42.356 -6.526  1.00 26.24 ?  159 ASN   B HD22 1 
ATOM   6493 N N    . LEU   B 1 160 ? 44.884 -38.951 -6.793  1.00 15.71 ?  160 LEU   B N    1 
ATOM   6494 C CA   . LEU   B 1 160 ? 43.749 -38.216 -6.248  1.00 14.87 ?  160 LEU   B CA   1 
ATOM   6495 C C    . LEU   B 1 160 ? 42.959 -37.549 -7.363  1.00 14.15 ?  160 LEU   B C    1 
ATOM   6496 O O    . LEU   B 1 160 ? 41.720 -37.550 -7.347  1.00 13.77 ?  160 LEU   B O    1 
ATOM   6497 C CB   . LEU   B 1 160 ? 44.209 -37.180 -5.222  1.00 14.79 ?  160 LEU   B CB   1 
ATOM   6498 C CG   . LEU   B 1 160 ? 43.080 -36.282 -4.695  1.00 14.84 ?  160 LEU   B CG   1 
ATOM   6499 C CD1  . LEU   B 1 160 ? 41.950 -37.108 -4.085  1.00 15.72 ?  160 LEU   B CD1  1 
ATOM   6500 C CD2  . LEU   B 1 160 ? 43.611 -35.275 -3.691  1.00 14.98 ?  160 LEU   B CD2  1 
ATOM   6501 H H    . LEU   B 1 160 ? 45.663 -38.598 -6.640  1.00 18.82 ?  160 LEU   B H    1 
ATOM   6502 H HA   . LEU   B 1 160 ? 43.167 -38.842 -5.803  1.00 17.82 ?  160 LEU   B HA   1 
ATOM   6503 H HB2  . LEU   B 1 160 ? 44.602 -37.647 -4.464  1.00 17.72 ?  160 LEU   B HB2  1 
ATOM   6504 H HB3  . LEU   B 1 160 ? 44.882 -36.608 -5.631  1.00 17.72 ?  160 LEU   B HB3  1 
ATOM   6505 H HG   . LEU   B 1 160 ? 42.713 -35.783 -5.436  1.00 17.79 ?  160 LEU   B HG   1 
ATOM   6506 H HD11 . LEU   B 1 160 ? 41.317 -36.505 -3.666  1.00 18.83 ?  160 LEU   B HD11 1 
ATOM   6507 H HD12 . LEU   B 1 160 ? 41.509 -37.613 -4.786  1.00 18.83 ?  160 LEU   B HD12 1 
ATOM   6508 H HD13 . LEU   B 1 160 ? 42.320 -37.712 -3.422  1.00 18.83 ?  160 LEU   B HD13 1 
ATOM   6509 H HD21 . LEU   B 1 160 ? 42.879 -34.713 -3.395  1.00 17.96 ?  160 LEU   B HD21 1 
ATOM   6510 H HD22 . LEU   B 1 160 ? 43.991 -35.750 -2.935  1.00 17.96 ?  160 LEU   B HD22 1 
ATOM   6511 H HD23 . LEU   B 1 160 ? 44.294 -34.733 -4.118  1.00 17.96 ?  160 LEU   B HD23 1 
ATOM   6512 N N    . TYR   B 1 161 ? 43.661 -36.984 -8.346  1.00 14.10 ?  161 TYR   B N    1 
ATOM   6513 C CA   . TYR   B 1 161 ? 42.994 -36.414 -9.509  1.00 13.95 ?  161 TYR   B CA   1 
ATOM   6514 C C    . TYR   B 1 161 ? 42.055 -37.431 -10.140 1.00 14.14 ?  161 TYR   B C    1 
ATOM   6515 O O    . TYR   B 1 161 ? 40.889 -37.132 -10.407 1.00 13.99 ?  161 TYR   B O    1 
ATOM   6516 C CB   . TYR   B 1 161 ? 44.043 -35.931 -10.518 1.00 14.59 ?  161 TYR   B CB   1 
ATOM   6517 C CG   . TYR   B 1 161 ? 43.475 -35.465 -11.838 1.00 15.22 ?  161 TYR   B CG   1 
ATOM   6518 C CD1  . TYR   B 1 161 ? 43.079 -34.143 -12.014 1.00 15.50 ?  161 TYR   B CD1  1 
ATOM   6519 C CD2  . TYR   B 1 161 ? 43.316 -36.345 -12.905 1.00 15.89 ?  161 TYR   B CD2  1 
ATOM   6520 C CE1  . TYR   B 1 161 ? 42.553 -33.712 -13.206 1.00 16.59 ?  161 TYR   B CE1  1 
ATOM   6521 C CE2  . TYR   B 1 161 ? 42.786 -35.921 -14.103 1.00 17.23 ?  161 TYR   B CE2  1 
ATOM   6522 C CZ   . TYR   B 1 161 ? 42.410 -34.600 -14.250 1.00 17.10 ?  161 TYR   B CZ   1 
ATOM   6523 O OH   . TYR   B 1 161 ? 41.877 -34.159 -15.435 1.00 19.07 ?  161 TYR   B OH   1 
ATOM   6524 H H    . TYR   B 1 161 ? 44.518 -36.920 -8.368  1.00 16.89 ?  161 TYR   B H    1 
ATOM   6525 H HA   . TYR   B 1 161 ? 42.464 -35.647 -9.236  1.00 16.71 ?  161 TYR   B HA   1 
ATOM   6526 H HB2  . TYR   B 1 161 ? 44.526 -35.182 -10.132 1.00 17.48 ?  161 TYR   B HB2  1 
ATOM   6527 H HB3  . TYR   B 1 161 ? 44.656 -36.655 -10.705 1.00 17.48 ?  161 TYR   B HB3  1 
ATOM   6528 H HD1  . TYR   B 1 161 ? 43.178 -33.537 -11.317 1.00 18.57 ?  161 TYR   B HD1  1 
ATOM   6529 H HD2  . TYR   B 1 161 ? 43.567 -37.237 -12.811 1.00 19.05 ?  161 TYR   B HD2  1 
ATOM   6530 H HE1  . TYR   B 1 161 ? 42.300 -32.820 -13.307 1.00 19.88 ?  161 TYR   B HE1  1 
ATOM   6531 H HE2  . TYR   B 1 161 ? 42.685 -36.519 -14.812 1.00 20.66 ?  161 TYR   B HE2  1 
ATOM   6532 H HH   . TYR   B 1 161 ? 41.843 -34.795 -15.987 1.00 22.86 ?  161 TYR   B HH   1 
ATOM   6533 N N    . ASP   B 1 162 ? 42.550 -38.651 -10.368 1.00 14.76 ?  162 ASP   B N    1 
ATOM   6534 C CA   . ASP   B 1 162 ? 41.727 -39.687 -10.986 1.00 15.20 ?  162 ASP   B CA   1 
ATOM   6535 C C    . ASP   B 1 162 ? 40.518 -40.027 -10.124 1.00 14.47 ?  162 ASP   B C    1 
ATOM   6536 O O    . ASP   B 1 162 ? 39.420 -40.244 -10.647 1.00 14.75 ?  162 ASP   B O    1 
ATOM   6537 C CB   . ASP   B 1 162 ? 42.562 -40.944 -11.231 1.00 16.54 ?  162 ASP   B CB   1 
ATOM   6538 C CG   . ASP   B 1 162 ? 43.571 -40.779 -12.354 1.00 17.93 ?  162 ASP   B CG   1 
ATOM   6539 O OD1  . ASP   B 1 162 ? 43.449 -39.835 -13.159 1.00 17.99 ?  162 ASP   B OD1  1 
ATOM   6540 O OD2  . ASP   B 1 162 ? 44.482 -41.627 -12.446 1.00 19.82 -1 162 ASP   B OD2  1 
ATOM   6541 H H    . ASP   B 1 162 ? 43.352 -38.892 -10.183 1.00 17.69 ?  162 ASP   B H    1 
ATOM   6542 H HA   . ASP   B 1 162 ? 41.406 -39.367 -11.843 1.00 18.22 ?  162 ASP   B HA   1 
ATOM   6543 H HB2  . ASP   B 1 162 ? 43.052 -41.160 -10.422 1.00 19.82 ?  162 ASP   B HB2  1 
ATOM   6544 H HB3  . ASP   B 1 162 ? 41.973 -41.671 -11.471 1.00 19.82 ?  162 ASP   B HB3  1 
ATOM   6545 N N    A LYS   B 1 163 ? 40.700 -40.101 -8.804  0.48 14.34 ?  163 LYS   B N    1 
ATOM   6546 N N    B LYS   B 1 163 ? 40.701 -40.094 -8.804  0.52 14.04 ?  163 LYS   B N    1 
ATOM   6547 C CA   A LYS   B 1 163 ? 39.567 -40.381 -7.927  0.48 15.06 ?  163 LYS   B CA   1 
ATOM   6548 C CA   B LYS   B 1 163 ? 39.578 -40.376 -7.914  0.52 14.56 ?  163 LYS   B CA   1 
ATOM   6549 C C    A LYS   B 1 163 ? 38.525 -39.268 -7.997  0.48 13.78 ?  163 LYS   B C    1 
ATOM   6550 C C    B LYS   B 1 163 ? 38.530 -39.269 -7.972  0.52 13.54 ?  163 LYS   B C    1 
ATOM   6551 O O    A LYS   B 1 163 ? 37.316 -39.536 -8.034  0.48 14.39 ?  163 LYS   B O    1 
ATOM   6552 O O    B LYS   B 1 163 ? 37.321 -39.542 -7.970  0.52 14.31 ?  163 LYS   B O    1 
ATOM   6553 C CB   A LYS   B 1 163 ? 40.044 -40.574 -6.488  0.48 17.68 ?  163 LYS   B CB   1 
ATOM   6554 C CB   B LYS   B 1 163 ? 40.083 -40.556 -6.483  0.52 16.87 ?  163 LYS   B CB   1 
ATOM   6555 C CG   A LYS   B 1 163 ? 38.968 -41.148 -5.583  0.48 21.17 ?  163 LYS   B CG   1 
ATOM   6556 C CG   B LYS   B 1 163 ? 39.006 -41.018 -5.524  0.52 20.38 ?  163 LYS   B CG   1 
ATOM   6557 C CD   A LYS   B 1 163 ? 39.365 -41.125 -4.120  0.48 24.39 ?  163 LYS   B CD   1 
ATOM   6558 C CD   B LYS   B 1 163 ? 39.548 -41.296 -4.135  0.52 23.87 ?  163 LYS   B CD   1 
ATOM   6559 C CE   A LYS   B 1 163 ? 38.292 -41.785 -3.269  0.48 26.54 ?  163 LYS   B CE   1 
ATOM   6560 C CE   B LYS   B 1 163 ? 38.512 -42.042 -3.309  0.52 26.28 ?  163 LYS   B CE   1 
ATOM   6561 N NZ   A LYS   B 1 163 ? 38.406 -41.424 -1.830  0.48 27.69 ?  163 LYS   B NZ   1 
ATOM   6562 N NZ   B LYS   B 1 163 ? 38.501 -41.613 -1.884  0.52 27.52 ?  163 LYS   B NZ   1 
ATOM   6563 H H    A LYS   B 1 163 ? 41.455 -39.997 -8.405  0.48 17.18 ?  163 LYS   B H    1 
ATOM   6564 H H    B LYS   B 1 163 ? 41.457 -39.984 -8.408  0.52 16.83 ?  163 LYS   B H    1 
ATOM   6565 H HA   A LYS   B 1 163 ? 39.146 -41.204 -8.215  0.48 18.05 ?  163 LYS   B HA   1 
ATOM   6566 H HA   B LYS   B 1 163 ? 39.159 -41.205 -8.191  0.52 17.45 ?  163 LYS   B HA   1 
ATOM   6567 H HB2  A LYS   B 1 163 ? 40.796 -41.191 -6.484  0.48 21.19 ?  163 LYS   B HB2  1 
ATOM   6568 H HB2  B LYS   B 1 163 ? 40.790 -41.224 -6.480  0.52 20.22 ?  163 LYS   B HB2  1 
ATOM   6569 H HB3  A LYS   B 1 163 ? 40.316 -39.719 -6.126  0.48 21.19 ?  163 LYS   B HB3  1 
ATOM   6570 H HB3  B LYS   B 1 163 ? 40.427 -39.711 -6.160  0.52 20.22 ?  163 LYS   B HB3  1 
ATOM   6571 H HG2  A LYS   B 1 163 ? 38.157 -40.625 -5.680  0.48 25.38 ?  163 LYS   B HG2  1 
ATOM   6572 H HG2  B LYS   B 1 163 ? 38.328 -40.329 -5.449  0.52 24.43 ?  163 LYS   B HG2  1 
ATOM   6573 H HG3  A LYS   B 1 163 ? 38.799 -42.071 -5.834  0.48 25.38 ?  163 LYS   B HG3  1 
ATOM   6574 H HG3  B LYS   B 1 163 ? 38.609 -41.839 -5.861  0.52 24.43 ?  163 LYS   B HG3  1 
ATOM   6575 H HD2  A LYS   B 1 163 ? 40.194 -41.617 -4.002  0.48 29.25 ?  163 LYS   B HD2  1 
ATOM   6576 H HD2  B LYS   B 1 163 ? 40.345 -41.845 -4.201  0.52 28.63 ?  163 LYS   B HD2  1 
ATOM   6577 H HD3  A LYS   B 1 163 ? 39.471 -40.207 -3.827  0.48 29.25 ?  163 LYS   B HD3  1 
ATOM   6578 H HD3  B LYS   B 1 163 ? 39.749 -40.457 -3.692  0.52 28.63 ?  163 LYS   B HD3  1 
ATOM   6579 H HE2  A LYS   B 1 163 ? 37.416 -41.515 -3.586  0.48 31.83 ?  163 LYS   B HE2  1 
ATOM   6580 H HE2  B LYS   B 1 163 ? 37.631 -41.877 -3.682  0.52 31.52 ?  163 LYS   B HE2  1 
ATOM   6581 H HE3  A LYS   B 1 163 ? 38.382 -42.747 -3.342  0.48 31.83 ?  163 LYS   B HE3  1 
ATOM   6582 H HE3  B LYS   B 1 163 ? 38.711 -42.992 -3.336  0.52 31.52 ?  163 LYS   B HE3  1 
ATOM   6583 H HZ1  A LYS   B 1 163 ? 37.762 -41.825 -1.365  0.48 33.20 ?  163 LYS   B HZ1  1 
ATOM   6584 H HZ1  B LYS   B 1 163 ? 37.883 -42.070 -1.435  0.52 33.00 ?  163 LYS   B HZ1  1 
ATOM   6585 H HZ2  A LYS   B 1 163 ? 39.196 -41.683 -1.515  0.48 33.20 ?  163 LYS   B HZ2  1 
ATOM   6586 H HZ2  B LYS   B 1 163 ? 39.296 -41.761 -1.516  0.52 33.00 ?  163 LYS   B HZ2  1 
ATOM   6587 H HZ3  A LYS   B 1 163 ? 38.328 -40.543 -1.731  0.48 33.20 ?  163 LYS   B HZ3  1 
ATOM   6588 H HZ3  B LYS   B 1 163 ? 38.313 -40.745 -1.831  0.52 33.00 ?  163 LYS   B HZ3  1 
ATOM   6589 N N    . LEU   B 1 164 ? 38.979 -38.012 -8.020  1.00 12.90 ?  164 LEU   B N    1 
ATOM   6590 C CA   . LEU   B 1 164 ? 38.062 -36.877 -8.079  1.00 12.63 ?  164 LEU   B CA   1 
ATOM   6591 C C    . LEU   B 1 164 ? 37.286 -36.859 -9.389  1.00 12.74 ?  164 LEU   B C    1 
ATOM   6592 O O    . LEU   B 1 164 ? 36.064 -36.658 -9.394  1.00 13.83 ?  164 LEU   B O    1 
ATOM   6593 C CB   . LEU   B 1 164 ? 38.859 -35.584 -7.918  1.00 12.13 ?  164 LEU   B CB   1 
ATOM   6594 C CG   . LEU   B 1 164 ? 39.380 -35.310 -6.511  1.00 12.97 ?  164 LEU   B CG   1 
ATOM   6595 C CD1  . LEU   B 1 164 ? 40.482 -34.259 -6.553  1.00 13.38 ?  164 LEU   B CD1  1 
ATOM   6596 C CD2  . LEU   B 1 164 ? 38.250 -34.863 -5.601  1.00 14.81 ?  164 LEU   B CD2  1 
ATOM   6597 H H    A LEU   B 1 164 ? 39.813 -37.793 -8.005  0.48 15.45 ?  164 LEU   B H    1 
ATOM   6598 H H    B LEU   B 1 164 ? 39.813 -37.791 -8.022  0.52 15.45 ?  164 LEU   B H    1 
ATOM   6599 H HA   . LEU   B 1 164 ? 37.428 -36.941 -7.352  1.00 15.14 ?  164 LEU   B HA   1 
ATOM   6600 H HB2  . LEU   B 1 164 ? 39.627 -35.617 -8.513  1.00 14.54 ?  164 LEU   B HB2  1 
ATOM   6601 H HB3  . LEU   B 1 164 ? 38.291 -34.839 -8.168  1.00 14.54 ?  164 LEU   B HB3  1 
ATOM   6602 H HG   . LEU   B 1 164 ? 39.763 -36.121 -6.149  1.00 15.54 ?  164 LEU   B HG   1 
ATOM   6603 H HD11 . LEU   B 1 164 ? 40.796 -34.091 -5.649  1.00 16.03 ?  164 LEU   B HD11 1 
ATOM   6604 H HD12 . LEU   B 1 164 ? 41.216 -34.587 -7.099  1.00 16.03 ?  164 LEU   B HD12 1 
ATOM   6605 H HD13 . LEU   B 1 164 ? 40.128 -33.440 -6.935  1.00 16.03 ?  164 LEU   B HD13 1 
ATOM   6606 H HD21 . LEU   B 1 164 ? 38.614 -34.637 -4.730  1.00 17.74 ?  164 LEU   B HD21 1 
ATOM   6607 H HD22 . LEU   B 1 164 ? 37.817 -34.087 -5.989  1.00 17.74 ?  164 LEU   B HD22 1 
ATOM   6608 H HD23 . LEU   B 1 164 ? 37.613 -35.589 -5.513  1.00 17.74 ?  164 LEU   B HD23 1 
ATOM   6609 N N    . VAL   B 1 165 ? 37.982 -37.041 -10.514 1.00 13.79 ?  165 VAL   B N    1 
ATOM   6610 C CA   . VAL   B 1 165 ? 37.337 -36.978 -11.822 1.00 15.00 ?  165 VAL   B CA   1 
ATOM   6611 C C    . VAL   B 1 165 ? 36.424 -38.179 -12.015 1.00 16.26 ?  165 VAL   B C    1 
ATOM   6612 O O    . VAL   B 1 165 ? 35.265 -38.046 -12.428 1.00 17.10 ?  165 VAL   B O    1 
ATOM   6613 C CB   . VAL   B 1 165 ? 38.392 -36.887 -12.942 1.00 15.79 ?  165 VAL   B CB   1 
ATOM   6614 C CG1  . VAL   B 1 165 ? 37.738 -36.971 -14.305 1.00 17.27 ?  165 VAL   B CG1  1 
ATOM   6615 C CG2  . VAL   B 1 165 ? 39.203 -35.608 -12.822 1.00 15.45 ?  165 VAL   B CG2  1 
ATOM   6616 H H    . VAL   B 1 165 ? 38.829 -37.196 -10.543 1.00 16.52 ?  165 VAL   B H    1 
ATOM   6617 H HA   . VAL   B 1 165 ? 36.793 -36.180 -11.869 1.00 17.97 ?  165 VAL   B HA   1 
ATOM   6618 H HB   . VAL   B 1 165 ? 39.010 -37.634 -12.858 1.00 18.92 ?  165 VAL   B HB   1 
ATOM   6619 H HG11 . VAL   B 1 165 ? 38.373 -36.681 -14.976 1.00 20.70 ?  165 VAL   B HG11 1 
ATOM   6620 H HG12 . VAL   B 1 165 ? 37.482 -37.893 -14.472 1.00 20.70 ?  165 VAL   B HG12 1 
ATOM   6621 H HG13 . VAL   B 1 165 ? 36.958 -36.401 -14.312 1.00 20.70 ?  165 VAL   B HG13 1 
ATOM   6622 H HG21 . VAL   B 1 165 ? 39.851 -35.572 -13.545 1.00 18.52 ?  165 VAL   B HG21 1 
ATOM   6623 H HG22 . VAL   B 1 165 ? 38.605 -34.847 -12.879 1.00 18.52 ?  165 VAL   B HG22 1 
ATOM   6624 H HG23 . VAL   B 1 165 ? 39.665 -35.601 -11.968 1.00 18.52 ?  165 VAL   B HG23 1 
ATOM   6625 N N    . SER   B 1 166 ? 36.938 -39.373 -11.710 1.00 16.84 ?  166 SER   B N    1 
ATOM   6626 C CA   . SER   B 1 166 ? 36.184 -40.585 -11.991 1.00 18.01 ?  166 SER   B CA   1 
ATOM   6627 C C    . SER   B 1 166 ? 34.919 -40.667 -11.152 1.00 18.17 ?  166 SER   B C    1 
ATOM   6628 O O    . SER   B 1 166 ? 33.947 -41.281 -11.588 1.00 19.62 ?  166 SER   B O    1 
ATOM   6629 C CB   . SER   B 1 166 ? 37.049 -41.836 -11.801 1.00 18.62 ?  166 SER   B CB   1 
ATOM   6630 O OG   . SER   B 1 166 ? 37.393 -42.036 -10.443 1.00 18.39 ?  166 SER   B OG   1 
ATOM   6631 H H    . SER   B 1 166 ? 37.714 -39.505 -11.354 1.00 20.19 ?  166 SER   B H    1 
ATOM   6632 H HA   . SER   B 1 166 ? 35.917 -40.569 -12.923 1.00 21.59 ?  166 SER   B HA   1 
ATOM   6633 H HB2  . SER   B 1 166 ? 36.553 -42.612 -12.114 1.00 22.31 ?  166 SER   B HB2  1 
ATOM   6634 H HB3  . SER   B 1 166 ? 37.863 -41.742 -12.324 1.00 22.31 ?  166 SER   B HB3  1 
ATOM   6635 H HG   . SER   B 1 166 ? 37.836 -41.382 -10.162 1.00 22.05 ?  166 SER   B HG   1 
ATOM   6636 N N    . SER   B 1 167 ? 34.896 -40.060 -9.965  1.00 17.11 ?  167 SER   B N    1 
ATOM   6637 C CA   . SER   B 1 167 ? 33.735 -40.116 -9.082  1.00 16.66 ?  167 SER   B CA   1 
ATOM   6638 C C    . SER   B 1 167 ? 32.812 -38.901 -9.186  1.00 16.30 ?  167 SER   B C    1 
ATOM   6639 O O    . SER   B 1 167 ? 31.735 -38.905 -8.574  1.00 16.61 ?  167 SER   B O    1 
ATOM   6640 C CB   . SER   B 1 167 ? 34.175 -40.298 -7.623  1.00 16.68 ?  167 SER   B CB   1 
ATOM   6641 O OG   . SER   B 1 167 ? 34.817 -39.137 -7.115  1.00 16.42 ?  167 SER   B OG   1 
ATOM   6642 H H    . SER   B 1 167 ? 35.550 -39.605 -9.650  1.00 20.50 ?  167 SER   B H    1 
ATOM   6643 H HA   . SER   B 1 167 ? 33.209 -40.898 -9.327  1.00 19.97 ?  167 SER   B HA   1 
ATOM   6644 H HB2  . SER   B 1 167 ? 33.390 -40.492 -7.086  1.00 19.99 ?  167 SER   B HB2  1 
ATOM   6645 H HB3  . SER   B 1 167 ? 34.794 -41.048 -7.578  1.00 19.99 ?  167 SER   B HB3  1 
ATOM   6646 H HG   . SER   B 1 167 ? 35.494 -38.964 -7.580  1.00 19.69 ?  167 SER   B HG   1 
ATOM   6647 N N    . PHE   B 1 168 ? 33.192 -37.866 -9.941  1.00 16.30 ?  168 PHE   B N    1 
ATOM   6648 C CA   . PHE   B 1 168 ? 32.356 -36.668 -10.007 1.00 15.90 ?  168 PHE   B CA   1 
ATOM   6649 C C    . PHE   B 1 168 ? 31.038 -36.930 -10.730 1.00 13.76 ?  168 PHE   B C    1 
ATOM   6650 O O    . PHE   B 1 168 ? 30.002 -36.327 -10.392 1.00 14.50 ?  168 PHE   B O    1 
ATOM   6651 C CB   . PHE   B 1 168 ? 33.120 -35.535 -10.686 1.00 16.85 ?  168 PHE   B CB   1 
ATOM   6652 C CG   . PHE   B 1 168 ? 32.321 -34.281 -10.814 1.00 17.18 ?  168 PHE   B CG   1 
ATOM   6653 C CD1  . PHE   B 1 168 ? 31.999 -33.535 -9.687  1.00 18.48 ?  168 PHE   B CD1  1 
ATOM   6654 C CD2  . PHE   B 1 168 ? 31.883 -33.844 -12.046 1.00 16.82 ?  168 PHE   B CD2  1 
ATOM   6655 C CE1  . PHE   B 1 168 ? 31.243 -32.379 -9.789  1.00 19.08 ?  168 PHE   B CE1  1 
ATOM   6656 C CE2  . PHE   B 1 168 ? 31.139 -32.678 -12.160 1.00 17.58 ?  168 PHE   B CE2  1 
ATOM   6657 C CZ   . PHE   B 1 168 ? 30.817 -31.946 -11.028 1.00 18.24 ?  168 PHE   B CZ   1 
ATOM   6658 H H    . PHE   B 1 168 ? 33.913 -37.835 -10.412 1.00 19.53 ?  168 PHE   B H    1 
ATOM   6659 H HA   . PHE   B 1 168 ? 32.145 -36.388 -9.107  1.00 19.06 ?  168 PHE   B HA   1 
ATOM   6660 H HB2  . PHE   B 1 168 ? 33.909 -35.328 -10.161 1.00 20.20 ?  168 PHE   B HB2  1 
ATOM   6661 H HB3  . PHE   B 1 168 ? 33.376 -35.810 -11.577 1.00 20.20 ?  168 PHE   B HB3  1 
ATOM   6662 H HD1  . PHE   B 1 168 ? 32.277 -33.828 -8.850  1.00 22.15 ?  168 PHE   B HD1  1 
ATOM   6663 H HD2  . PHE   B 1 168 ? 32.095 -34.324 -12.808 1.00 20.16 ?  168 PHE   B HD2  1 
ATOM   6664 H HE1  . PHE   B 1 168 ? 31.028 -31.890 -9.026  1.00 22.87 ?  168 PHE   B HE1  1 
ATOM   6665 H HE2  . PHE   B 1 168 ? 30.848 -32.389 -12.998 1.00 21.07 ?  168 PHE   B HE2  1 
ATOM   6666 H HZ   . PHE   B 1 168 ? 30.311 -31.167 -11.108 1.00 21.86 ?  168 PHE   B HZ   1 
ATOM   6667 N N    . LEU   B 1 169 ? 31.061 -37.814 -11.724 1.00 14.10 ?  169 LEU   B N    1 
ATOM   6668 C CA   . LEU   B 1 169 ? 29.880 -38.113 -12.522 1.00 16.45 ?  169 LEU   B CA   1 
ATOM   6669 C C    . LEU   B 1 169 ? 29.887 -39.542 -13.047 1.00 19.05 ?  169 LEU   B C    1 
ATOM   6670 O O    . LEU   B 1 169 ? 28.976 -39.943 -13.775 1.00 21.65 ?  169 LEU   B O    1 
ATOM   6671 C CB   . LEU   B 1 169 ? 29.804 -37.160 -13.710 1.00 18.44 ?  169 LEU   B CB   1 
ATOM   6672 C CG   . LEU   B 1 169 ? 28.555 -36.285 -13.800 1.00 21.76 ?  169 LEU   B CG   1 
ATOM   6673 C CD1  . LEU   B 1 169 ? 28.525 -35.552 -15.125 1.00 22.99 ?  169 LEU   B CD1  1 
ATOM   6674 C CD2  . LEU   B 1 169 ? 27.296 -37.104 -13.616 1.00 21.67 ?  169 LEU   B CD2  1 
ATOM   6675 O OXT  . LEU   B 1 169 ? 30.806 -40.308 -12.771 1.00 19.68 -1 169 LEU   B OXT  1 
ATOM   6676 H H    . LEU   B 1 169 ? 31.761 -38.258 -11.965 1.00 16.90 ?  169 LEU   B H    1 
ATOM   6677 H HA   . LEU   B 1 169 ? 29.092 -37.990 -11.972 1.00 19.71 ?  169 LEU   B HA   1 
ATOM   6678 H HB2  . LEU   B 1 169 ? 30.569 -36.566 -13.675 1.00 22.10 ?  169 LEU   B HB2  1 
ATOM   6679 H HB3  . LEU   B 1 169 ? 29.843 -37.685 -14.526 1.00 22.10 ?  169 LEU   B HB3  1 
ATOM   6680 H HG   . LEU   B 1 169 ? 28.585 -35.619 -13.094 1.00 26.09 ?  169 LEU   B HG   1 
ATOM   6681 H HD11 . LEU   B 1 169 ? 27.741 -34.983 -15.152 1.00 27.57 ?  169 LEU   B HD11 1 
ATOM   6682 H HD12 . LEU   B 1 169 ? 29.328 -35.015 -15.205 1.00 27.57 ?  169 LEU   B HD12 1 
ATOM   6683 H HD13 . LEU   B 1 169 ? 28.488 -36.204 -15.842 1.00 27.57 ?  169 LEU   B HD13 1 
ATOM   6684 H HD21 . LEU   B 1 169 ? 26.550 -36.637 -14.020 1.00 25.98 ?  169 LEU   B HD21 1 
ATOM   6685 H HD22 . LEU   B 1 169 ? 27.418 -37.968 -14.043 1.00 25.98 ?  169 LEU   B HD22 1 
ATOM   6686 H HD23 . LEU   B 1 169 ? 27.137 -37.226 -12.667 1.00 25.98 ?  169 LEU   B HD23 1 
HETATM 6687 S S    B DMS   C 2 .   ? 6.476  4.390   4.343   0.52 17.88 ?  301 DMS   A S    1 
HETATM 6688 O O    B DMS   C 2 .   ? 5.697  3.115   4.570   0.52 15.55 ?  301 DMS   A O    1 
HETATM 6689 C C1   B DMS   C 2 .   ? 7.719  4.553   5.667   0.52 17.76 ?  301 DMS   A C1   1 
HETATM 6690 C C2   B DMS   C 2 .   ? 5.390  5.787   4.793   0.52 17.84 ?  301 DMS   A C2   1 
HETATM 6691 H H11  B DMS   C 2 .   ? 7.170  4.563   6.543   0.52 21.28 ?  301 DMS   A H11  1 
HETATM 6692 H H12  B DMS   C 2 .   ? 8.358  3.736   5.596   0.52 21.28 ?  301 DMS   A H12  1 
HETATM 6693 H H13  B DMS   C 2 .   ? 8.211  5.455   5.493   0.52 21.28 ?  301 DMS   A H13  1 
HETATM 6694 H H21  B DMS   C 2 .   ? 5.846  6.655   4.440   0.52 21.38 ?  301 DMS   A H21  1 
HETATM 6695 H H22  B DMS   C 2 .   ? 5.343  5.758   5.830   0.52 21.38 ?  301 DMS   A H22  1 
HETATM 6696 H H23  B DMS   C 2 .   ? 4.463  5.618   4.350   0.52 21.38 ?  301 DMS   A H23  1 
HETATM 6697 S S    B DMS   D 2 .   ? 9.050  0.279   -3.130  0.52 29.48 ?  302 DMS   A S    1 
HETATM 6698 O O    B DMS   D 2 .   ? 10.439 0.397   -3.713  0.52 29.43 ?  302 DMS   A O    1 
HETATM 6699 C C1   B DMS   D 2 .   ? 7.965  -0.313  -4.460  0.52 29.57 ?  302 DMS   A C1   1 
HETATM 6700 C C2   B DMS   D 2 .   ? 8.447  1.979   -2.924  0.52 28.74 ?  302 DMS   A C2   1 
HETATM 6701 H H11  B DMS   D 2 .   ? 7.069  -0.563  -4.005  0.52 35.46 ?  302 DMS   A H11  1 
HETATM 6702 H H12  B DMS   D 2 .   ? 7.896  0.490   -5.099  0.52 35.46 ?  302 DMS   A H12  1 
HETATM 6703 H H13  B DMS   D 2 .   ? 8.439  -1.136  -4.893  0.52 35.46 ?  302 DMS   A H13  1 
HETATM 6704 H H21  B DMS   D 2 .   ? 9.145  2.490   -2.343  0.52 34.46 ?  302 DMS   A H21  1 
HETATM 6705 H H22  B DMS   D 2 .   ? 8.393  2.340   -3.891  0.52 34.46 ?  302 DMS   A H22  1 
HETATM 6706 H H23  B DMS   D 2 .   ? 7.526  1.894   -2.464  0.52 34.46 ?  302 DMS   A H23  1 
HETATM 6707 N N2   B A1A9E E 3 .   ? 14.842 -0.068  4.287   0.52 8.89  ?  303 A1A9E A N2   1 
HETATM 6708 C C3   B A1A9E E 3 .   ? 14.039 0.279   0.071   0.52 11.77 ?  303 A1A9E A C3   1 
HETATM 6709 C C6   B A1A9E E 3 .   ? 14.874 1.110   3.606   0.52 9.01  ?  303 A1A9E A C6   1 
HETATM 6710 C C9   B A1A9E E 3 .   ? 15.168 2.318   4.298   0.52 8.75  ?  303 A1A9E A C9   1 
HETATM 6711 C C12  B A1A9E E 3 .   ? 14.500 2.252   1.397   0.52 11.27 ?  303 A1A9E A C12  1 
HETATM 6712 C C1   B A1A9E E 3 .   ? 11.596 1.709   -0.803  0.52 14.19 ?  303 A1A9E A C1   1 
HETATM 6713 C C10  B A1A9E E 3 .   ? 15.327 3.738   4.063   0.52 9.87  ?  303 A1A9E A C10  1 
HETATM 6714 C C11  B A1A9E E 3 .   ? 15.624 4.364   5.255   0.52 9.66  ?  303 A1A9E A C11  1 
HETATM 6715 C C2   B A1A9E E 3 .   ? 13.777 1.784   0.133   0.52 12.44 ?  303 A1A9E A C2   1 
HETATM 6716 C C4   B A1A9E E 3 .   ? 14.182 -0.179  1.536   0.52 10.87 ?  303 A1A9E A C4   1 
HETATM 6717 C C5   B A1A9E E 3 .   ? 12.896 -0.967  2.062   0.52 10.75 ?  303 A1A9E A C5   1 
HETATM 6718 C C7   B A1A9E E 3 .   ? 15.076 -0.037  5.633   0.52 9.08  ?  303 A1A9E A C7   1 
HETATM 6719 C C8   B A1A9E E 3 .   ? 15.393 2.173   5.690   0.52 8.93  ?  303 A1A9E A C8   1 
HETATM 6720 N N1   B A1A9E E 3 .   ? 14.605 1.054   2.261   0.52 10.35 ?  303 A1A9E A N1   1 
HETATM 6721 N N3   B A1A9E E 3 .   ? 15.361 1.010   6.395   0.52 9.38  ?  303 A1A9E A N3   1 
HETATM 6722 N N4   B A1A9E E 3 .   ? 15.659 3.399   6.273   0.52 9.67  ?  303 A1A9E A N4   1 
HETATM 6723 O O1   B A1A9E E 3 .   ? 12.404 1.978   0.308   0.52 13.19 ?  303 A1A9E A O1   1 
HETATM 6724 O O2   B A1A9E E 3 .   ? 11.836 -0.036  2.193   0.52 11.26 ?  303 A1A9E A O2   1 
HETATM 6725 H H7   B A1A9E E 3 .   ? 14.919 0.034   -0.548  0.52 14.10 ?  303 A1A9E A H7   1 
HETATM 6726 H H6   B A1A9E E 3 .   ? 13.228 -0.271  -0.448  0.52 14.10 ?  303 A1A9E A H6   1 
HETATM 6727 H H16  B A1A9E E 3 .   ? 13.837 2.963   1.918   0.52 13.50 ?  303 A1A9E A H16  1 
HETATM 6728 H H15  B A1A9E E 3 .   ? 15.443 2.784   1.175   0.52 13.50 ?  303 A1A9E A H15  1 
HETATM 6729 H H4   B A1A9E E 3 .   ? 10.647 2.210   -0.620  0.52 17.01 ?  303 A1A9E A H4   1 
HETATM 6730 H H5   B A1A9E E 3 .   ? 11.364 0.638   -0.953  0.52 17.01 ?  303 A1A9E A H5   1 
HETATM 6731 H H3   B A1A9E E 3 .   ? 11.989 2.093   -1.760  0.52 17.01 ?  303 A1A9E A H3   1 
HETATM 6732 H H12  B A1A9E E 3 .   ? 15.239 4.287   3.148   0.52 11.82 ?  303 A1A9E A H12  1 
HETATM 6733 H H13  B A1A9E E 3 .   ? 15.815 5.397   5.514   0.52 11.57 ?  303 A1A9E A H13  1 
HETATM 6734 H H1   B A1A9E E 3 .   ? 14.161 2.314   -0.780  0.52 14.90 ?  303 A1A9E A H1   1 
HETATM 6735 H H2   B A1A9E E 3 .   ? 15.037 -0.866  1.600   0.52 13.03 ?  303 A1A9E A H2   1 
HETATM 6736 H H8   B A1A9E E 3 .   ? 13.096 -1.467  3.025   0.52 12.88 ?  303 A1A9E A H8   1 
HETATM 6737 H H9   B A1A9E E 3 .   ? 12.605 -1.760  1.337   0.52 12.88 ?  303 A1A9E A H9   1 
HETATM 6738 H H11  B A1A9E E 3 .   ? 15.042 -0.968  6.240   0.52 10.87 ?  303 A1A9E A H11  1 
HETATM 6739 H H14  B A1A9E E 3 .   ? 15.861 3.547   7.254   0.52 11.58 ?  303 A1A9E A H14  1 
HETATM 6740 H H10  B A1A9E E 3 .   ? 11.016 -0.516  2.049   0.52 13.49 ?  303 A1A9E A H10  1 
HETATM 6741 O O    . HOH   F 4 .   ? 1.053  -4.044  0.037   1.00 28.84 ?  401 HOH   A O    1 
HETATM 6742 O O    . HOH   F 4 .   ? 14.676 -4.574  20.544  1.00 46.68 ?  402 HOH   A O    1 
HETATM 6743 O O    A HOH   F 4 .   ? 12.217 0.241   14.895  0.48 21.31 ?  403 HOH   A O    1 
HETATM 6744 O O    . HOH   F 4 .   ? 13.592 -15.274 -7.664  1.00 27.12 ?  404 HOH   A O    1 
HETATM 6745 O O    A HOH   F 4 .   ? 4.629  3.954   0.650   0.48 19.48 ?  405 HOH   A O    1 
HETATM 6746 O O    . HOH   F 4 .   ? 19.834 -12.260 -9.210  1.00 23.45 ?  406 HOH   A O    1 
HETATM 6747 O O    . HOH   F 4 .   ? -0.707 -8.153  2.200   1.00 44.89 ?  407 HOH   A O    1 
HETATM 6748 O O    . HOH   F 4 .   ? 34.388 -1.922  12.496  1.00 35.24 ?  408 HOH   A O    1 
HETATM 6749 O O    A HOH   F 4 .   ? -0.547 -3.059  3.109   0.48 28.21 ?  409 HOH   A O    1 
HETATM 6750 O O    . HOH   F 4 .   ? 15.235 -7.955  -9.933  1.00 23.34 ?  410 HOH   A O    1 
HETATM 6751 O O    . HOH   F 4 .   ? 18.850 -21.923 6.994   1.00 34.22 ?  411 HOH   A O    1 
HETATM 6752 O O    . HOH   F 4 .   ? 14.939 3.681   17.801  1.00 32.73 ?  412 HOH   A O    1 
HETATM 6753 O O    . HOH   F 4 .   ? 15.016 -12.123 18.783  1.00 32.19 ?  413 HOH   A O    1 
HETATM 6754 O O    B HOH   F 4 .   ? 3.033  2.955   -1.465  0.52 19.44 ?  414 HOH   A O    1 
HETATM 6755 O O    . HOH   F 4 .   ? 28.165 -6.353  19.727  1.00 36.36 ?  415 HOH   A O    1 
HETATM 6756 O O    . HOH   F 4 .   ? 42.395 10.527  5.257   1.00 19.88 ?  416 HOH   A O    1 
HETATM 6757 O O    . HOH   F 4 .   ? 33.843 -0.948  -8.833  1.00 27.37 ?  417 HOH   A O    1 
HETATM 6758 O O    A HOH   F 4 .   ? 28.827 0.525   -9.657  0.48 14.53 ?  418 HOH   A O    1 
HETATM 6759 O O    . HOH   F 4 .   ? 14.670 -13.943 16.769  1.00 20.80 ?  419 HOH   A O    1 
HETATM 6760 O O    . HOH   F 4 .   ? 26.749 11.425  1.759   1.00 16.33 ?  420 HOH   A O    1 
HETATM 6761 O O    . HOH   F 4 .   ? 22.198 -19.338 11.242  1.00 35.34 ?  421 HOH   A O    1 
HETATM 6762 O O    . HOH   F 4 .   ? 16.947 -19.236 4.861   1.00 15.33 ?  422 HOH   A O    1 
HETATM 6763 O O    A HOH   F 4 .   ? 6.871  -8.160  11.847  0.48 12.95 ?  423 HOH   A O    1 
HETATM 6764 O O    . HOH   F 4 .   ? 22.718 12.490  1.698   1.00 16.29 ?  424 HOH   A O    1 
HETATM 6765 O O    . HOH   F 4 .   ? 22.307 5.325   18.990  1.00 35.81 ?  425 HOH   A O    1 
HETATM 6766 O O    . HOH   F 4 .   ? 26.387 -19.298 -1.855  1.00 13.25 ?  426 HOH   A O    1 
HETATM 6767 O O    B HOH   F 4 .   ? 5.001  3.476   0.321   0.52 13.37 ?  427 HOH   A O    1 
HETATM 6768 O O    . HOH   F 4 .   ? 13.077 -1.402  -6.738  1.00 19.17 ?  428 HOH   A O    1 
HETATM 6769 O O    . HOH   F 4 .   ? 30.169 -13.275 -8.620  1.00 20.45 ?  429 HOH   A O    1 
HETATM 6770 O O    . HOH   F 4 .   ? 36.144 -5.084  -0.570  1.00 29.36 ?  430 HOH   A O    1 
HETATM 6771 O O    . HOH   F 4 .   ? 30.925 -18.124 7.799   1.00 19.25 ?  431 HOH   A O    1 
HETATM 6772 O O    . HOH   F 4 .   ? 9.781  -21.244 5.705   1.00 21.15 ?  432 HOH   A O    1 
HETATM 6773 O O    A HOH   F 4 .   ? 14.205 0.586   6.830   0.48 25.92 ?  433 HOH   A O    1 
HETATM 6774 O O    . HOH   F 4 .   ? 27.246 13.807  3.025   1.00 29.06 ?  434 HOH   A O    1 
HETATM 6775 O O    . HOH   F 4 .   ? 7.999  -12.304 -1.059  1.00 19.27 ?  435 HOH   A O    1 
HETATM 6776 O O    . HOH   F 4 .   ? 38.068 -1.360  -1.933  1.00 17.06 ?  436 HOH   A O    1 
HETATM 6777 O O    A HOH   F 4 .   ? 17.429 -1.683  0.467   0.48 18.09 ?  437 HOH   A O    1 
HETATM 6778 O O    . HOH   F 4 .   ? 44.244 7.057   6.421   1.00 26.21 ?  438 HOH   A O    1 
HETATM 6779 O O    . HOH   F 4 .   ? 20.528 -19.699 -5.114  1.00 28.70 ?  439 HOH   A O    1 
HETATM 6780 O O    A HOH   F 4 .   ? 14.566 -3.630  3.115   0.48 18.06 ?  440 HOH   A O    1 
HETATM 6781 O O    . HOH   F 4 .   ? 13.837 -4.899  17.343  1.00 23.61 ?  441 HOH   A O    1 
HETATM 6782 O O    . HOH   F 4 .   ? 9.073  -10.202 19.306  1.00 37.73 ?  442 HOH   A O    1 
HETATM 6783 O O    . HOH   F 4 .   ? 28.452 -10.595 -13.900 1.00 46.85 ?  443 HOH   A O    1 
HETATM 6784 O O    . HOH   F 4 .   ? 21.116 -2.305  -2.187  1.00 15.67 ?  444 HOH   A O    1 
HETATM 6785 O O    B HOH   F 4 .   ? 9.132  4.424   0.451   0.52 17.82 ?  445 HOH   A O    1 
HETATM 6786 O O    . HOH   F 4 .   ? 38.256 10.119  7.185   1.00 36.52 ?  446 HOH   A O    1 
HETATM 6787 O O    A HOH   F 4 .   ? 14.012 -4.518  -11.719 0.48 20.97 ?  447 HOH   A O    1 
HETATM 6788 O O    . HOH   F 4 .   ? 8.019  -21.362 3.925   1.00 39.88 ?  448 HOH   A O    1 
HETATM 6789 O O    . HOH   F 4 .   ? 21.766 -13.621 -8.234  1.00 23.77 ?  449 HOH   A O    1 
HETATM 6790 O O    . HOH   F 4 .   ? 18.431 5.067   -15.099 1.00 40.19 ?  450 HOH   A O    1 
HETATM 6791 O O    . HOH   F 4 .   ? 38.520 4.928   6.932   1.00 15.22 ?  451 HOH   A O    1 
HETATM 6792 O O    B HOH   F 4 .   ? 23.937 2.035   -6.626  0.52 24.66 ?  452 HOH   A O    1 
HETATM 6793 O O    . HOH   F 4 .   ? 28.246 -0.045  -13.359 1.00 34.87 ?  453 HOH   A O    1 
HETATM 6794 O O    . HOH   F 4 .   ? 37.082 -2.851  9.744   1.00 39.26 ?  454 HOH   A O    1 
HETATM 6795 O O    . HOH   F 4 .   ? 18.625 -19.414 13.528  1.00 45.08 ?  455 HOH   A O    1 
HETATM 6796 O O    . HOH   F 4 .   ? 37.323 11.904  5.012   1.00 28.76 ?  456 HOH   A O    1 
HETATM 6797 O O    . HOH   F 4 .   ? 31.747 8.120   14.916  1.00 24.37 ?  457 HOH   A O    1 
HETATM 6798 O O    A HOH   F 4 .   ? 11.000 -0.350  1.959   0.48 24.02 ?  458 HOH   A O    1 
HETATM 6799 O O    . HOH   F 4 .   ? 37.549 2.678   10.191  1.00 26.41 ?  459 HOH   A O    1 
HETATM 6800 O O    . HOH   F 4 .   ? 43.860 8.403   -3.073  1.00 23.65 ?  460 HOH   A O    1 
HETATM 6801 O O    . HOH   F 4 .   ? 14.272 -21.148 -4.328  1.00 31.47 ?  461 HOH   A O    1 
HETATM 6802 O O    . HOH   F 4 .   ? 39.650 -1.024  -5.225  1.00 19.66 ?  462 HOH   A O    1 
HETATM 6803 O O    B HOH   F 4 .   ? 4.103  2.423   2.457   0.52 13.75 ?  463 HOH   A O    1 
HETATM 6804 O O    . HOH   F 4 .   ? 31.675 -9.284  -6.711  1.00 19.66 ?  464 HOH   A O    1 
HETATM 6805 O O    . HOH   F 4 .   ? 17.117 -17.896 -5.093  1.00 28.57 ?  465 HOH   A O    1 
HETATM 6806 O O    . HOH   F 4 .   ? 16.390 -21.981 0.960   1.00 28.56 ?  466 HOH   A O    1 
HETATM 6807 O O    . HOH   F 4 .   ? 35.685 -12.686 6.809   1.00 15.14 ?  467 HOH   A O    1 
HETATM 6808 O O    . HOH   F 4 .   ? 23.428 11.355  4.218   1.00 12.59 ?  468 HOH   A O    1 
HETATM 6809 O O    . HOH   F 4 .   ? 23.902 -2.078  -2.018  1.00 9.78  ?  469 HOH   A O    1 
HETATM 6810 O O    . HOH   F 4 .   ? 18.541 9.381   9.198   1.00 23.24 ?  470 HOH   A O    1 
HETATM 6811 O O    . HOH   F 4 .   ? 30.981 -13.912 -2.505  1.00 12.45 ?  471 HOH   A O    1 
HETATM 6812 O O    . HOH   F 4 .   ? 42.484 4.215   5.284   1.00 27.33 ?  472 HOH   A O    1 
HETATM 6813 O O    . HOH   F 4 .   ? 33.593 -7.163  4.235   1.00 15.24 ?  473 HOH   A O    1 
HETATM 6814 O O    . HOH   F 4 .   ? 13.962 -22.987 7.445   1.00 18.50 ?  474 HOH   A O    1 
HETATM 6815 O O    . HOH   F 4 .   ? 14.471 -0.355  -12.257 1.00 26.61 ?  475 HOH   A O    1 
HETATM 6816 O O    . HOH   F 4 .   ? 30.777 3.033   8.300   1.00 11.31 ?  476 HOH   A O    1 
HETATM 6817 O O    . HOH   F 4 .   ? 21.826 -21.922 8.391   1.00 26.84 ?  477 HOH   A O    1 
HETATM 6818 O O    . HOH   F 4 .   ? 31.619 -7.247  -9.862  1.00 20.20 ?  478 HOH   A O    1 
HETATM 6819 O O    . HOH   F 4 .   ? 43.308 7.831   2.713   1.00 22.31 ?  479 HOH   A O    1 
HETATM 6820 O O    . HOH   F 4 .   ? 19.929 4.653   -7.599  1.00 19.08 ?  480 HOH   A O    1 
HETATM 6821 O O    . HOH   F 4 .   ? 24.303 -7.866  14.490  1.00 16.96 ?  481 HOH   A O    1 
HETATM 6822 O O    A HOH   F 4 .   ? 7.649  -6.273  -6.506  0.48 30.93 ?  482 HOH   A O    1 
HETATM 6823 O O    . HOH   F 4 .   ? 10.416 -22.103 -1.143  1.00 41.68 ?  483 HOH   A O    1 
HETATM 6824 O O    . HOH   F 4 .   ? 27.490 -10.720 14.086  1.00 17.15 ?  484 HOH   A O    1 
HETATM 6825 O O    . HOH   F 4 .   ? 22.582 -11.903 21.808  1.00 39.28 ?  485 HOH   A O    1 
HETATM 6826 O O    . HOH   F 4 .   ? 24.622 -17.591 12.675  1.00 23.94 ?  486 HOH   A O    1 
HETATM 6827 O O    . HOH   F 4 .   ? 8.892  -12.075 17.144  1.00 38.57 ?  487 HOH   A O    1 
HETATM 6828 O O    . HOH   F 4 .   ? 27.514 2.213   18.788  1.00 24.61 ?  488 HOH   A O    1 
HETATM 6829 O O    B HOH   F 4 .   ? 15.239 -2.883  3.574   0.52 10.87 ?  489 HOH   A O    1 
HETATM 6830 O O    . HOH   F 4 .   ? 21.238 10.159  15.192  1.00 32.93 ?  490 HOH   A O    1 
HETATM 6831 O O    . HOH   F 4 .   ? 37.479 -2.013  5.732   1.00 24.46 ?  491 HOH   A O    1 
HETATM 6832 O O    . HOH   F 4 .   ? 15.441 11.826  8.065   1.00 43.92 ?  492 HOH   A O    1 
HETATM 6833 O O    A HOH   F 4 .   ? 17.026 -18.112 15.039  0.48 19.35 ?  493 HOH   A O    1 
HETATM 6834 O O    A HOH   F 4 .   ? 15.731 -0.928  5.297   0.48 25.16 ?  494 HOH   A O    1 
HETATM 6835 O O    B HOH   F 4 .   ? 21.113 2.833   0.306   0.52 10.73 ?  495 HOH   A O    1 
HETATM 6836 O O    . HOH   F 4 .   ? 24.271 3.606   -1.711  1.00 14.20 ?  496 HOH   A O    1 
HETATM 6837 O O    B HOH   F 4 .   ? 11.873 -2.035  -3.971  0.52 14.31 ?  497 HOH   A O    1 
HETATM 6838 O O    . HOH   F 4 .   ? 26.821 4.182   -0.594  1.00 11.69 ?  498 HOH   A O    1 
HETATM 6839 O O    . HOH   F 4 .   ? 32.724 -9.260  5.954   1.00 19.02 ?  499 HOH   A O    1 
HETATM 6840 O O    . HOH   F 4 .   ? 30.946 6.167   -12.246 1.00 27.97 ?  500 HOH   A O    1 
HETATM 6841 O O    A HOH   F 4 .   ? 24.523 2.090   -6.946  0.48 13.24 ?  501 HOH   A O    1 
HETATM 6842 O O    A HOH   F 4 .   ? 11.669 -10.716 -10.071 0.48 29.78 ?  502 HOH   A O    1 
HETATM 6843 O O    B HOH   F 4 .   ? 17.037 -1.605  1.090   0.52 17.13 ?  503 HOH   A O    1 
HETATM 6844 O O    . HOH   F 4 .   ? 27.125 -3.300  19.364  1.00 34.83 ?  504 HOH   A O    1 
HETATM 6845 O O    . HOH   F 4 .   ? 30.056 -10.221 12.975  1.00 21.14 ?  505 HOH   A O    1 
HETATM 6846 O O    A HOH   F 4 .   ? 24.031 4.003   -4.869  0.48 17.46 ?  506 HOH   A O    1 
HETATM 6847 O O    B HOH   F 4 .   ? 14.775 7.240   7.416   0.52 15.89 ?  507 HOH   A O    1 
HETATM 6848 O O    . HOH   F 4 .   ? 16.210 16.672  8.573   1.00 38.47 ?  508 HOH   A O    1 
HETATM 6849 O O    A HOH   F 4 .   ? 21.284 3.187   -0.306  0.48 9.18  ?  509 HOH   A O    1 
HETATM 6850 O O    . HOH   F 4 .   ? 18.749 -0.672  -1.639  1.00 13.68 ?  510 HOH   A O    1 
HETATM 6851 O O    . HOH   F 4 .   ? 19.453 -11.169 24.183  1.00 59.79 ?  511 HOH   A O    1 
HETATM 6852 O O    A HOH   F 4 .   ? 5.235  2.659   5.302   0.48 30.03 ?  512 HOH   A O    1 
HETATM 6853 O O    A HOH   F 4 .   ? 15.114 -21.609 14.125  0.48 13.27 ?  513 HOH   A O    1 
HETATM 6854 O O    . HOH   F 4 .   ? 20.491 -20.032 2.695   1.00 18.18 ?  514 HOH   A O    1 
HETATM 6855 O O    . HOH   F 4 .   ? 9.603  -16.315 -2.021  1.00 27.01 ?  515 HOH   A O    1 
HETATM 6856 O O    . HOH   F 4 .   ? 44.803 -0.628  3.024   1.00 35.81 ?  516 HOH   A O    1 
HETATM 6857 O O    . HOH   F 4 .   ? 16.170 -14.136 20.333  1.00 45.85 ?  517 HOH   A O    1 
HETATM 6858 O O    . HOH   F 4 .   ? 27.813 0.875   -7.095  1.00 12.99 ?  518 HOH   A O    1 
HETATM 6859 O O    . HOH   F 4 .   ? 41.528 1.587   4.944   1.00 33.74 ?  519 HOH   A O    1 
HETATM 6860 O O    . HOH   F 4 .   ? 30.291 -12.995 13.492  1.00 19.65 ?  520 HOH   A O    1 
HETATM 6861 O O    . HOH   F 4 .   ? 34.876 -5.183  -3.089  1.00 17.43 ?  521 HOH   A O    1 
HETATM 6862 O O    B HOH   F 4 .   ? 10.845 1.997   12.373  0.52 18.33 ?  522 HOH   A O    1 
HETATM 6863 O O    . HOH   F 4 .   ? 22.721 7.929   18.506  1.00 42.21 ?  523 HOH   A O    1 
HETATM 6864 O O    . HOH   F 4 .   ? 23.808 -20.228 -1.393  1.00 16.11 ?  524 HOH   A O    1 
HETATM 6865 O O    . HOH   F 4 .   ? 14.348 -24.672 11.628  1.00 40.72 ?  525 HOH   A O    1 
HETATM 6866 O O    A HOH   F 4 .   ? 25.641 -0.735  -7.297  0.48 10.91 ?  526 HOH   A O    1 
HETATM 6867 O O    . HOH   F 4 .   ? 10.349 -13.671 -1.709  1.00 17.06 ?  527 HOH   A O    1 
HETATM 6868 O O    A HOH   F 4 .   ? 10.962 1.548   12.782  0.48 17.04 ?  528 HOH   A O    1 
HETATM 6869 O O    . HOH   F 4 .   ? 40.828 -8.198  -6.726  1.00 36.35 ?  529 HOH   A O    1 
HETATM 6870 O O    . HOH   F 4 .   ? 30.833 1.692   16.734  1.00 19.10 ?  530 HOH   A O    1 
HETATM 6871 O O    . HOH   F 4 .   ? 23.869 -15.632 -9.279  1.00 27.99 ?  531 HOH   A O    1 
HETATM 6872 O O    . HOH   F 4 .   ? 32.532 -4.295  -9.922  1.00 27.53 ?  532 HOH   A O    1 
HETATM 6873 O O    . HOH   F 4 .   ? 36.719 -4.951  5.327   1.00 23.66 ?  533 HOH   A O    1 
HETATM 6874 O O    A HOH   F 4 .   ? 6.669  -3.389  12.901  0.48 22.75 ?  534 HOH   A O    1 
HETATM 6875 O O    B HOH   F 4 .   ? 11.430 6.367   9.949   0.52 23.31 ?  535 HOH   A O    1 
HETATM 6876 O O    A HOH   F 4 .   ? 6.391  -5.601  11.184  0.48 13.63 ?  536 HOH   A O    1 
HETATM 6877 O O    . HOH   F 4 .   ? 18.669 -2.368  -16.598 1.00 45.80 ?  537 HOH   A O    1 
HETATM 6878 O O    . HOH   F 4 .   ? 11.618 -10.646 16.970  1.00 21.37 ?  538 HOH   A O    1 
HETATM 6879 O O    B HOH   F 4 .   ? 11.431 0.373   14.676  0.52 24.77 ?  539 HOH   A O    1 
HETATM 6880 O O    B HOH   F 4 .   ? 5.548  0.106   -1.979  0.52 22.59 ?  540 HOH   A O    1 
HETATM 6881 O O    . HOH   F 4 .   ? 15.777 2.147   24.816  1.00 46.49 ?  541 HOH   A O    1 
HETATM 6882 O O    A HOH   F 4 .   ? 3.523  -9.454  9.723   0.48 24.41 ?  542 HOH   A O    1 
HETATM 6883 O O    . HOH   F 4 .   ? 15.894 6.987   3.025   1.00 14.94 ?  543 HOH   A O    1 
HETATM 6884 O O    . HOH   F 4 .   ? 27.503 -5.568  -13.977 1.00 41.01 ?  544 HOH   A O    1 
HETATM 6885 O O    . HOH   F 4 .   ? 32.435 -10.657 3.211   1.00 30.16 ?  545 HOH   A O    1 
HETATM 6886 O O    . HOH   F 4 .   ? 20.530 -17.805 24.763  1.00 52.64 ?  546 HOH   A O    1 
HETATM 6887 O O    . HOH   F 4 .   ? 23.665 -8.143  17.116  1.00 21.29 ?  547 HOH   A O    1 
HETATM 6888 O O    . HOH   F 4 .   ? 18.283 -16.010 16.441  1.00 38.70 ?  548 HOH   A O    1 
HETATM 6889 O O    . HOH   F 4 .   ? 23.240 -20.935 1.237   1.00 18.03 ?  549 HOH   A O    1 
HETATM 6890 O O    A HOH   F 4 .   ? 18.799 2.067   -0.714  0.48 9.86  ?  550 HOH   A O    1 
HETATM 6891 O O    A HOH   F 4 .   ? 13.959 -0.315  3.489   0.48 46.35 ?  551 HOH   A O    1 
HETATM 6892 O O    . HOH   F 4 .   ? 23.201 7.577   -3.141  1.00 38.78 ?  552 HOH   A O    1 
HETATM 6893 O O    . HOH   F 4 .   ? 34.329 -8.083  -0.572  1.00 32.46 ?  553 HOH   A O    1 
HETATM 6894 O O    B HOH   F 4 .   ? 23.674 3.888   -4.439  0.52 15.85 ?  554 HOH   A O    1 
HETATM 6895 O O    . HOH   F 4 .   ? 31.239 -12.760 -0.008  1.00 18.45 ?  555 HOH   A O    1 
HETATM 6896 O O    B HOH   F 4 .   ? 15.812 3.313   -1.933  0.52 12.15 ?  556 HOH   A O    1 
HETATM 6897 O O    B HOH   F 4 .   ? 16.678 6.323   -2.293  0.52 21.64 ?  557 HOH   A O    1 
HETATM 6898 O O    A HOH   F 4 .   ? 16.195 2.985   -1.402  0.48 8.28  ?  558 HOH   A O    1 
HETATM 6899 O O    B HOH   F 4 .   ? 20.570 4.567   -2.379  0.52 28.31 ?  559 HOH   A O    1 
HETATM 6900 O O    . HOH   F 4 .   ? 30.530 14.755  2.869   1.00 18.73 ?  560 HOH   A O    1 
HETATM 6901 O O    . HOH   F 4 .   ? 21.432 -14.693 18.116  1.00 47.58 ?  561 HOH   A O    1 
HETATM 6902 O O    . HOH   F 4 .   ? 21.252 -9.199  21.394  1.00 46.89 ?  562 HOH   A O    1 
HETATM 6903 O O    . HOH   F 4 .   ? 24.868 5.509   20.848  1.00 45.82 ?  563 HOH   A O    1 
HETATM 6904 O O    . HOH   F 4 .   ? 29.850 -16.085 10.610  1.00 34.93 ?  564 HOH   A O    1 
HETATM 6905 O O    B HOH   F 4 .   ? 18.082 2.067   -0.433  0.52 13.88 ?  565 HOH   A O    1 
HETATM 6906 O O    . HOH   F 4 .   ? 37.561 -8.711  -3.243  1.00 24.32 ?  566 HOH   A O    1 
HETATM 6907 O O    A HOH   F 4 .   ? -1.502 -4.925  7.647   0.48 39.51 ?  567 HOH   A O    1 
HETATM 6908 O O    . HOH   F 4 .   ? 25.318 8.230   -4.741  1.00 32.77 ?  568 HOH   A O    1 
HETATM 6909 O O    . HOH   F 4 .   ? 8.029  -3.225  -5.886  1.00 51.13 ?  569 HOH   A O    1 
HETATM 6910 O O    . HOH   F 4 .   ? 19.822 -17.351 -5.078  1.00 25.56 ?  570 HOH   A O    1 
HETATM 6911 O O    . HOH   F 4 .   ? 27.722 7.006   -6.465  1.00 33.74 ?  571 HOH   A O    1 
HETATM 6912 O O    . HOH   F 4 .   ? 32.309 -15.951 10.918  1.00 37.27 ?  572 HOH   A O    1 
HETATM 6913 O O    . HOH   F 4 .   ? 29.685 -1.952  -12.738 1.00 43.89 ?  573 HOH   A O    1 
HETATM 6914 O O    B HOH   F 4 .   ? 5.236  -2.469  -2.652  0.52 27.05 ?  574 HOH   A O    1 
HETATM 6915 O O    . HOH   F 4 .   ? 26.809 11.561  -1.265  1.00 32.28 ?  575 HOH   A O    1 
HETATM 6916 O O    . HOH   F 4 .   ? 27.356 -11.380 16.656  1.00 38.08 ?  576 HOH   A O    1 
HETATM 6917 O O    . HOH   F 4 .   ? 39.541 -7.060  -3.685  1.00 42.29 ?  577 HOH   A O    1 
HETATM 6918 O O    . HOH   F 4 .   ? 23.117 -22.371 -3.312  1.00 32.82 ?  578 HOH   A O    1 
HETATM 6919 O O    . HOH   F 4 .   ? 24.560 14.571  7.920   1.00 34.38 ?  579 HOH   A O    1 
HETATM 6920 O O    . HOH   F 4 .   ? 21.727 5.213   -5.697  1.00 31.82 ?  580 HOH   A O    1 
HETATM 6921 O O    . HOH   F 4 .   ? 28.600 -7.820  -15.261 1.00 47.30 ?  581 HOH   A O    1 
HETATM 6922 O O    . HOH   F 4 .   ? 11.105 -14.918 -6.230  1.00 32.61 ?  582 HOH   A O    1 
HETATM 6923 O O    . HOH   F 4 .   ? 15.788 -17.103 -7.022  1.00 33.78 ?  583 HOH   A O    1 
HETATM 6924 O O    . HOH   F 4 .   ? 18.794 10.858  11.482  1.00 33.32 ?  584 HOH   A O    1 
HETATM 6925 O O    . HOH   F 4 .   ? 15.676 -21.493 3.706   1.00 25.12 ?  585 HOH   A O    1 
HETATM 6926 O O    . HOH   F 4 .   ? 18.031 -16.407 -8.853  1.00 40.45 ?  586 HOH   A O    1 
HETATM 6927 O O    . HOH   F 4 .   ? 11.939 -13.376 16.405  1.00 42.79 ?  587 HOH   A O    1 
HETATM 6928 O O    . HOH   F 4 .   ? 23.459 13.727  5.591   1.00 19.76 ?  588 HOH   A O    1 
HETATM 6929 O O    . HOH   F 4 .   ? 25.711 10.728  -3.703  1.00 27.89 ?  589 HOH   A O    1 
HETATM 6930 O O    . HOH   F 4 .   ? 28.935 8.923   17.553  1.00 35.97 ?  590 HOH   A O    1 
HETATM 6931 O O    . HOH   F 4 .   ? 12.208 1.560   17.422  1.00 39.26 ?  591 HOH   A O    1 
HETATM 6932 O O    . HOH   F 4 .   ? 14.152 -10.317 -11.005 1.00 33.34 ?  592 HOH   A O    1 
HETATM 6933 O O    . HOH   F 4 .   ? 35.173 7.439   12.313  1.00 43.61 ?  593 HOH   A O    1 
HETATM 6934 O O    . HOH   F 4 .   ? 16.804 -20.520 16.130  1.00 30.86 ?  594 HOH   A O    1 
HETATM 6935 O O    . HOH   F 4 .   ? 15.963 -6.557  -11.978 1.00 43.17 ?  595 HOH   A O    1 
HETATM 6936 O O    . HOH   F 4 .   ? 28.437 -4.511  -12.213 1.00 34.79 ?  596 HOH   A O    1 
HETATM 6937 O O    . HOH   F 4 .   ? 30.801 0.697   19.204  1.00 38.59 ?  597 HOH   A O    1 
HETATM 6938 O O    . HOH   F 4 .   ? 17.359 -18.662 19.844  1.00 52.73 ?  598 HOH   A O    1 
HETATM 6939 O O    . HOH   F 4 .   ? 40.864 -3.960  -0.407  1.00 38.26 ?  599 HOH   A O    1 
HETATM 6940 O O    . HOH   F 4 .   ? 23.090 11.790  -4.079  1.00 18.87 ?  600 HOH   A O    1 
HETATM 6941 O O    B HOH   F 4 .   ? 5.417  6.105   1.055   0.52 18.63 ?  601 HOH   A O    1 
HETATM 6942 O O    . HOH   F 4 .   ? 44.446 10.419  -1.559  1.00 30.74 ?  602 HOH   A O    1 
HETATM 6943 O O    . HOH   F 4 .   ? 41.644 9.325   -4.080  1.00 30.00 ?  603 HOH   A O    1 
HETATM 6944 O O    . HOH   F 4 .   ? 39.128 2.389   7.456   1.00 32.60 ?  604 HOH   A O    1 
HETATM 6945 O O    . HOH   F 4 .   ? 23.335 -12.909 19.364  1.00 43.55 ?  605 HOH   A O    1 
HETATM 6946 O O    . HOH   F 4 .   ? 40.437 -0.211  -7.768  1.00 34.32 ?  606 HOH   A O    1 
HETATM 6947 O O    . HOH   F 4 .   ? 13.902 -25.187 8.934   1.00 30.34 ?  607 HOH   A O    1 
HETATM 6948 O O    . HOH   F 4 .   ? 31.395 -0.498  -10.544 1.00 29.38 ?  608 HOH   A O    1 
HETATM 6949 O O    . HOH   F 4 .   ? 18.379 -23.200 1.830   1.00 39.55 ?  609 HOH   A O    1 
HETATM 6950 O O    . HOH   F 4 .   ? 16.133 -23.365 5.798   1.00 27.34 ?  610 HOH   A O    1 
HETATM 6951 O O    . HOH   F 4 .   ? 19.934 -22.332 4.137   1.00 27.57 ?  611 HOH   A O    1 
HETATM 6952 O O    . HOH   F 4 .   ? 30.701 -5.718  -11.807 1.00 47.71 ?  612 HOH   A O    1 
HETATM 6953 O O    . HOH   F 4 .   ? 37.346 -6.642  7.532   1.00 23.32 ?  613 HOH   A O    1 
HETATM 6954 O O    B HOH   F 4 .   ? 3.164  6.378   2.477   0.52 22.14 ?  614 HOH   A O    1 
HETATM 6955 O O    . HOH   F 4 .   ? 23.067 -23.761 1.638   1.00 30.98 ?  615 HOH   A O    1 
HETATM 6956 O O    . HOH   F 4 .   ? 30.755 5.780   -14.667 1.00 31.31 ?  616 HOH   A O    1 
HETATM 6957 O O    . HOH   F 4 .   ? 39.515 0.020   6.637   1.00 27.15 ?  617 HOH   A O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 38.034 13.824  6.812   1.00 43.32 ?  618 HOH   A O    1 
HETATM 6959 O O    B HOH   F 4 .   ? 14.478 7.843   4.989   0.52 22.20 ?  619 HOH   A O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 20.452 -16.099 -7.471  1.00 27.70 ?  620 HOH   A O    1 
HETATM 6961 O O    B HOH   F 4 .   ? 7.885  6.847   1.900   0.52 22.19 ?  621 HOH   A O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 28.980 14.378  0.920   1.00 49.18 ?  622 HOH   A O    1 
HETATM 6963 O O    . HOH   F 4 .   ? 21.982 -24.024 4.392   1.00 26.33 ?  623 HOH   A O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 36.468 -6.544  10.210  1.00 42.65 ?  624 HOH   A O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 17.341 -6.451  -14.268 1.00 39.45 ?  625 HOH   A O    1 
HETATM 6966 O O    . HOH   F 4 .   ? 23.925 8.959   -7.070  1.00 39.80 ?  626 HOH   A O    1 
HETATM 6967 O O    A HOH   F 4 .   ? 14.785 8.669   4.944   0.48 35.99 ?  627 HOH   A O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 15.836 -12.286 27.460  1.00 45.58 ?  628 HOH   A O    1 
HETATM 6969 O O    . HOH   F 4 .   ? 16.251 -21.135 18.811  1.00 39.10 ?  629 HOH   A O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 14.661 -22.802 19.899  1.00 38.23 ?  630 HOH   A O    1 
HETATM 6971 O O    . HOH   G 4 .   ? 29.699 -22.378 5.353   1.00 20.31 ?  201 HOH   B O    1 
HETATM 6972 O O    . HOH   G 4 .   ? 48.043 -6.874  15.579  1.00 39.72 ?  202 HOH   B O    1 
HETATM 6973 O O    . HOH   G 4 .   ? 52.854 -13.405 -20.349 1.00 35.90 ?  203 HOH   B O    1 
HETATM 6974 O O    . HOH   G 4 .   ? 49.338 -22.606 -19.661 1.00 46.65 ?  204 HOH   B O    1 
HETATM 6975 O O    . HOH   G 4 .   ? 47.244 -7.482  -3.972  1.00 36.70 ?  205 HOH   B O    1 
HETATM 6976 O O    . HOH   G 4 .   ? 41.355 -7.821  5.483   1.00 38.37 ?  206 HOH   B O    1 
HETATM 6977 O O    . HOH   G 4 .   ? 27.805 -41.786 -15.144 1.00 31.90 ?  207 HOH   B O    1 
HETATM 6978 O O    . HOH   G 4 .   ? 41.854 -35.979 -17.264 1.00 28.35 ?  208 HOH   B O    1 
HETATM 6979 O O    . HOH   G 4 .   ? 37.847 -39.422 -0.244  1.00 36.27 ?  209 HOH   B O    1 
HETATM 6980 O O    . HOH   G 4 .   ? 59.036 -18.793 6.799   1.00 32.32 ?  210 HOH   B O    1 
HETATM 6981 O O    . HOH   G 4 .   ? 27.612 -29.153 -1.937  1.00 35.94 ?  211 HOH   B O    1 
HETATM 6982 O O    . HOH   G 4 .   ? 44.420 -7.198  2.093   1.00 32.87 ?  212 HOH   B O    1 
HETATM 6983 O O    . HOH   G 4 .   ? 56.215 -19.710 7.434   1.00 32.31 ?  213 HOH   B O    1 
HETATM 6984 O O    . HOH   G 4 .   ? 35.901 -43.168 -8.576  1.00 25.55 ?  214 HOH   B O    1 
HETATM 6985 O O    . HOH   G 4 .   ? 30.166 -40.992 -8.153  1.00 14.76 ?  215 HOH   B O    1 
HETATM 6986 O O    . HOH   G 4 .   ? 54.380 -9.309  -8.785  1.00 18.08 ?  216 HOH   B O    1 
HETATM 6987 O O    . HOH   G 4 .   ? 50.297 -3.244  7.265   1.00 31.97 ?  217 HOH   B O    1 
HETATM 6988 O O    . HOH   G 4 .   ? 55.433 -16.467 -14.330 1.00 34.46 ?  218 HOH   B O    1 
HETATM 6989 O O    . HOH   G 4 .   ? 58.162 -12.910 8.430   1.00 32.54 ?  219 HOH   B O    1 
HETATM 6990 O O    . HOH   G 4 .   ? 57.643 -24.391 4.969   1.00 32.05 ?  220 HOH   B O    1 
HETATM 6991 O O    . HOH   G 4 .   ? 57.199 -26.858 -7.692  1.00 40.11 ?  221 HOH   B O    1 
HETATM 6992 O O    . HOH   G 4 .   ? 29.747 -26.279 3.879   1.00 28.20 ?  222 HOH   B O    1 
HETATM 6993 O O    . HOH   G 4 .   ? 57.373 -16.235 -12.102 1.00 18.07 ?  223 HOH   B O    1 
HETATM 6994 O O    . HOH   G 4 .   ? 30.744 -28.708 4.247   1.00 24.49 ?  224 HOH   B O    1 
HETATM 6995 O O    . HOH   G 4 .   ? 50.657 -6.046  0.236   1.00 24.49 ?  225 HOH   B O    1 
HETATM 6996 O O    . HOH   G 4 .   ? 56.652 -30.753 -7.788  1.00 29.63 ?  226 HOH   B O    1 
HETATM 6997 O O    . HOH   G 4 .   ? 48.068 -24.451 -17.662 1.00 28.15 ?  227 HOH   B O    1 
HETATM 6998 O O    . HOH   G 4 .   ? 34.473 -36.330 -7.221  1.00 16.28 ?  228 HOH   B O    1 
HETATM 6999 O O    . HOH   G 4 .   ? 41.484 -39.140 -14.897 1.00 20.12 ?  229 HOH   B O    1 
HETATM 7000 O O    . HOH   G 4 .   ? 44.947 -43.473 -10.510 1.00 25.78 ?  230 HOH   B O    1 
HETATM 7001 O O    . HOH   G 4 .   ? 29.694 -34.182 -0.468  1.00 33.19 ?  231 HOH   B O    1 
HETATM 7002 O O    . HOH   G 4 .   ? 40.506 -16.057 14.147  1.00 26.77 ?  232 HOH   B O    1 
HETATM 7003 O O    . HOH   G 4 .   ? 37.216 -19.550 -18.105 1.00 37.18 ?  233 HOH   B O    1 
HETATM 7004 O O    . HOH   G 4 .   ? 41.267 -9.632  13.100  1.00 23.04 ?  234 HOH   B O    1 
HETATM 7005 O O    . HOH   G 4 .   ? 51.488 -13.882 11.000  1.00 26.40 ?  235 HOH   B O    1 
HETATM 7006 O O    . HOH   G 4 .   ? 25.377 -25.952 -1.422  1.00 29.53 ?  236 HOH   B O    1 
HETATM 7007 O O    . HOH   G 4 .   ? 45.042 -34.901 6.788   1.00 36.02 ?  237 HOH   B O    1 
HETATM 7008 O O    . HOH   G 4 .   ? 51.641 -6.489  4.500   1.00 19.65 ?  238 HOH   B O    1 
HETATM 7009 O O    . HOH   G 4 .   ? 39.243 -10.876 6.165   1.00 26.92 ?  239 HOH   B O    1 
HETATM 7010 O O    . HOH   G 4 .   ? 34.986 -7.970  -3.006  1.00 18.73 ?  240 HOH   B O    1 
HETATM 7011 O O    . HOH   G 4 .   ? 50.630 -12.934 -0.450  1.00 11.52 ?  241 HOH   B O    1 
HETATM 7012 O O    . HOH   G 4 .   ? 28.349 -19.666 -13.170 1.00 25.55 ?  242 HOH   B O    1 
HETATM 7013 O O    . HOH   G 4 .   ? 42.529 -22.846 3.826   1.00 11.00 ?  243 HOH   B O    1 
HETATM 7014 O O    . HOH   G 4 .   ? 41.769 -23.460 9.298   1.00 15.58 ?  244 HOH   B O    1 
HETATM 7015 O O    . HOH   G 4 .   ? 42.474 -25.328 2.590   1.00 13.77 ?  245 HOH   B O    1 
HETATM 7016 O O    . HOH   G 4 .   ? 31.740 -17.835 -14.502 1.00 28.55 ?  246 HOH   B O    1 
HETATM 7017 O O    . HOH   G 4 .   ? 43.045 -43.205 -8.229  1.00 27.61 ?  247 HOH   B O    1 
HETATM 7018 O O    . HOH   G 4 .   ? 46.356 -1.522  13.273  1.00 28.78 ?  248 HOH   B O    1 
HETATM 7019 O O    . HOH   G 4 .   ? 43.189 -32.297 -17.114 1.00 20.72 ?  249 HOH   B O    1 
HETATM 7020 O O    . HOH   G 4 .   ? 57.504 -24.362 -3.816  1.00 20.45 ?  250 HOH   B O    1 
HETATM 7021 O O    . HOH   G 4 .   ? 39.387 -11.069 0.330   1.00 16.53 ?  251 HOH   B O    1 
HETATM 7022 O O    . HOH   G 4 .   ? 38.378 -10.988 -2.296  1.00 17.85 ?  252 HOH   B O    1 
HETATM 7023 O O    . HOH   G 4 .   ? 44.428 -27.721 -0.692  1.00 22.47 ?  253 HOH   B O    1 
HETATM 7024 O O    . HOH   G 4 .   ? 48.517 -36.448 -15.515 1.00 41.70 ?  254 HOH   B O    1 
HETATM 7025 O O    . HOH   G 4 .   ? 32.817 -43.807 -11.369 1.00 16.89 ?  255 HOH   B O    1 
HETATM 7026 O O    . HOH   G 4 .   ? 33.428 -17.013 8.042   1.00 18.13 ?  256 HOH   B O    1 
HETATM 7027 O O    . HOH   G 4 .   ? 30.772 -15.733 2.608   1.00 12.70 ?  257 HOH   B O    1 
HETATM 7028 O O    . HOH   G 4 .   ? 34.775 -24.568 13.798  1.00 29.19 ?  258 HOH   B O    1 
HETATM 7029 O O    . HOH   G 4 .   ? 29.665 -25.211 -10.879 1.00 14.80 ?  259 HOH   B O    1 
HETATM 7030 O O    . HOH   G 4 .   ? 34.114 -18.480 11.408  1.00 22.74 ?  260 HOH   B O    1 
HETATM 7031 O O    . HOH   G 4 .   ? 58.066 -10.564 -4.042  1.00 20.33 ?  261 HOH   B O    1 
HETATM 7032 O O    . HOH   G 4 .   ? 50.924 -39.910 -8.208  1.00 26.76 ?  262 HOH   B O    1 
HETATM 7033 O O    . HOH   G 4 .   ? 49.275 -28.645 -6.894  1.00 14.08 ?  263 HOH   B O    1 
HETATM 7034 O O    . HOH   G 4 .   ? 56.123 -23.411 -14.646 1.00 24.85 ?  264 HOH   B O    1 
HETATM 7035 O O    . HOH   G 4 .   ? 40.235 -12.703 -11.497 1.00 14.25 ?  265 HOH   B O    1 
HETATM 7036 O O    . HOH   G 4 .   ? 27.104 -31.818 -10.019 1.00 22.18 ?  266 HOH   B O    1 
HETATM 7037 O O    . HOH   G 4 .   ? 57.389 -9.194  1.425   1.00 19.48 ?  267 HOH   B O    1 
HETATM 7038 O O    . HOH   G 4 .   ? 43.545 -15.372 18.263  1.00 32.04 ?  268 HOH   B O    1 
HETATM 7039 O O    . HOH   G 4 .   ? 42.256 -9.862  9.418   1.00 21.06 ?  269 HOH   B O    1 
HETATM 7040 O O    . HOH   G 4 .   ? 30.599 -42.177 -10.669 1.00 25.76 ?  270 HOH   B O    1 
HETATM 7041 O O    . HOH   G 4 .   ? 43.304 -15.772 -12.179 1.00 13.08 ?  271 HOH   B O    1 
HETATM 7042 O O    . HOH   G 4 .   ? 56.851 -8.677  8.509   1.00 19.81 ?  272 HOH   B O    1 
HETATM 7043 O O    . HOH   G 4 .   ? 47.910 -22.750 5.858   1.00 16.41 ?  273 HOH   B O    1 
HETATM 7044 O O    . HOH   G 4 .   ? 28.242 -34.337 -9.425  1.00 19.91 ?  274 HOH   B O    1 
HETATM 7045 O O    . HOH   G 4 .   ? 42.920 -20.334 -20.778 1.00 35.81 ?  275 HOH   B O    1 
HETATM 7046 O O    . HOH   G 4 .   ? 27.600 -26.698 -15.694 1.00 30.77 ?  276 HOH   B O    1 
HETATM 7047 O O    . HOH   G 4 .   ? 34.386 -12.774 2.630   1.00 22.96 ?  277 HOH   B O    1 
HETATM 7048 O O    . HOH   G 4 .   ? 49.757 -0.482  10.313  1.00 28.30 ?  278 HOH   B O    1 
HETATM 7049 O O    . HOH   G 4 .   ? 49.836 -24.691 5.772   1.00 31.23 ?  279 HOH   B O    1 
HETATM 7050 O O    . HOH   G 4 .   ? 33.507 -15.283 -14.015 1.00 20.08 ?  280 HOH   B O    1 
HETATM 7051 O O    . HOH   G 4 .   ? 38.801 -12.019 12.439  1.00 28.96 ?  281 HOH   B O    1 
HETATM 7052 O O    . HOH   G 4 .   ? 27.889 -22.859 -8.080  1.00 16.95 ?  282 HOH   B O    1 
HETATM 7053 O O    . HOH   G 4 .   ? 34.918 -33.360 -19.239 1.00 26.16 ?  283 HOH   B O    1 
HETATM 7054 O O    . HOH   G 4 .   ? 46.557 -31.230 -4.777  1.00 18.26 ?  284 HOH   B O    1 
HETATM 7055 O O    . HOH   G 4 .   ? 28.440 -30.819 -14.799 1.00 28.87 ?  285 HOH   B O    1 
HETATM 7056 O O    . HOH   G 4 .   ? 59.702 -15.273 8.170   1.00 31.85 ?  286 HOH   B O    1 
HETATM 7057 O O    . HOH   G 4 .   ? 42.307 -34.664 3.726   1.00 25.17 ?  287 HOH   B O    1 
HETATM 7058 O O    . HOH   G 4 .   ? 46.802 -29.463 9.759   1.00 31.42 ?  288 HOH   B O    1 
HETATM 7059 O O    . HOH   G 4 .   ? 48.324 -25.025 3.115   1.00 11.99 ?  289 HOH   B O    1 
HETATM 7060 O O    . HOH   G 4 .   ? 41.096 -5.531  11.510  1.00 45.84 ?  290 HOH   B O    1 
HETATM 7061 O O    . HOH   G 4 .   ? 52.481 -10.441 13.040  1.00 22.78 ?  291 HOH   B O    1 
HETATM 7062 O O    . HOH   G 4 .   ? 47.026 -33.959 -4.603  1.00 15.23 ?  292 HOH   B O    1 
HETATM 7063 O O    . HOH   G 4 .   ? 42.302 -9.880  -14.937 1.00 37.23 ?  293 HOH   B O    1 
HETATM 7064 O O    . HOH   G 4 .   ? 41.145 -24.423 15.798  1.00 39.23 ?  294 HOH   B O    1 
HETATM 7065 O O    . HOH   G 4 .   ? 53.151 -16.082 -12.652 1.00 28.51 ?  295 HOH   B O    1 
HETATM 7066 O O    . HOH   G 4 .   ? 51.206 -37.606 -9.482  1.00 23.68 ?  296 HOH   B O    1 
HETATM 7067 O O    . HOH   G 4 .   ? 45.357 -33.350 -15.942 1.00 21.02 ?  297 HOH   B O    1 
HETATM 7068 O O    . HOH   G 4 .   ? 48.618 -20.013 5.944   1.00 13.40 ?  298 HOH   B O    1 
HETATM 7069 O O    . HOH   G 4 .   ? 52.553 -35.632 -8.554  1.00 26.46 ?  299 HOH   B O    1 
HETATM 7070 O O    . HOH   G 4 .   ? 37.249 -35.669 7.154   1.00 31.74 ?  300 HOH   B O    1 
HETATM 7071 O O    . HOH   G 4 .   ? 42.605 -12.316 -18.532 1.00 28.18 ?  301 HOH   B O    1 
HETATM 7072 O O    . HOH   G 4 .   ? 44.529 -27.414 1.979   1.00 13.70 ?  302 HOH   B O    1 
HETATM 7073 O O    . HOH   G 4 .   ? 36.669 -12.729 -1.461  1.00 25.76 ?  303 HOH   B O    1 
HETATM 7074 O O    . HOH   G 4 .   ? 57.003 -12.102 12.449  1.00 39.87 ?  304 HOH   B O    1 
HETATM 7075 O O    . HOH   G 4 .   ? 43.946 -29.301 -4.699  1.00 23.01 ?  305 HOH   B O    1 
HETATM 7076 O O    . HOH   G 4 .   ? 37.441 -18.204 13.117  1.00 24.95 ?  306 HOH   B O    1 
HETATM 7077 O O    . HOH   G 4 .   ? 40.168 -10.793 -9.567  1.00 16.11 ?  307 HOH   B O    1 
HETATM 7078 O O    . HOH   G 4 .   ? 53.397 -30.155 4.503   1.00 17.04 ?  308 HOH   B O    1 
HETATM 7079 O O    . HOH   G 4 .   ? 62.612 -13.576 4.801   1.00 27.85 ?  309 HOH   B O    1 
HETATM 7080 O O    . HOH   G 4 .   ? 41.620 -8.080  1.353   1.00 24.91 ?  310 HOH   B O    1 
HETATM 7081 O O    . HOH   G 4 .   ? 37.741 -10.217 -10.779 1.00 16.44 ?  311 HOH   B O    1 
HETATM 7082 O O    . HOH   G 4 .   ? 38.258 -9.327  -13.264 1.00 24.93 ?  312 HOH   B O    1 
HETATM 7083 O O    . HOH   G 4 .   ? 25.886 -21.442 -3.575  1.00 15.32 ?  313 HOH   B O    1 
HETATM 7084 O O    . HOH   G 4 .   ? 34.896 -33.522 4.428   1.00 26.08 ?  314 HOH   B O    1 
HETATM 7085 O O    . HOH   G 4 .   ? 45.827 -40.352 -3.516  1.00 26.97 ?  315 HOH   B O    1 
HETATM 7086 O O    . HOH   G 4 .   ? 43.114 -21.394 10.690  1.00 15.40 ?  316 HOH   B O    1 
HETATM 7087 O O    . HOH   G 4 .   ? 32.758 -34.570 -5.973  1.00 15.41 ?  317 HOH   B O    1 
HETATM 7088 O O    . HOH   G 4 .   ? 57.603 -22.066 3.160   1.00 29.44 ?  318 HOH   B O    1 
HETATM 7089 O O    . HOH   G 4 .   ? 52.538 -29.183 -13.021 1.00 22.69 ?  319 HOH   B O    1 
HETATM 7090 O O    . HOH   G 4 .   ? 38.266 -12.843 7.897   1.00 18.03 ?  320 HOH   B O    1 
HETATM 7091 O O    . HOH   G 4 .   ? 26.261 -20.969 -6.285  1.00 15.65 ?  321 HOH   B O    1 
HETATM 7092 O O    . HOH   G 4 .   ? 48.119 -32.580 -16.638 1.00 40.09 ?  322 HOH   B O    1 
HETATM 7093 O O    . HOH   G 4 .   ? 37.254 -30.490 -21.091 1.00 27.52 ?  323 HOH   B O    1 
HETATM 7094 O O    . HOH   G 4 .   ? 62.810 -20.171 -0.792  1.00 35.27 ?  324 HOH   B O    1 
HETATM 7095 O O    . HOH   G 4 .   ? 27.906 -14.736 -9.435  1.00 29.15 ?  325 HOH   B O    1 
HETATM 7096 O O    . HOH   G 4 .   ? 44.464 -24.600 9.569   1.00 18.23 ?  326 HOH   B O    1 
HETATM 7097 O O    . HOH   G 4 .   ? 44.095 -1.721  7.686   1.00 43.33 ?  327 HOH   B O    1 
HETATM 7098 O O    . HOH   G 4 .   ? 59.862 -17.195 -10.474 1.00 32.60 ?  328 HOH   B O    1 
HETATM 7099 O O    . HOH   G 4 .   ? 36.621 -12.421 4.246   1.00 17.27 ?  329 HOH   B O    1 
HETATM 7100 O O    . HOH   G 4 .   ? 51.337 -32.887 -10.784 1.00 34.82 ?  330 HOH   B O    1 
HETATM 7101 O O    . HOH   G 4 .   ? 53.622 -12.552 -22.241 1.00 33.61 ?  331 HOH   B O    1 
HETATM 7102 O O    . HOH   G 4 .   ? 33.423 -31.132 11.066  1.00 34.17 ?  332 HOH   B O    1 
HETATM 7103 O O    . HOH   G 4 .   ? 47.041 -24.470 8.137   1.00 23.24 ?  333 HOH   B O    1 
HETATM 7104 O O    . HOH   G 4 .   ? 48.528 -11.861 -13.831 1.00 25.53 ?  334 HOH   B O    1 
HETATM 7105 O O    . HOH   G 4 .   ? 39.450 -23.530 -20.260 1.00 37.11 ?  335 HOH   B O    1 
HETATM 7106 O O    . HOH   G 4 .   ? 51.721 -5.942  -7.897  1.00 46.87 ?  336 HOH   B O    1 
HETATM 7107 O O    . HOH   G 4 .   ? 47.390 -27.401 2.012   1.00 13.51 ?  337 HOH   B O    1 
HETATM 7108 O O    . HOH   G 4 .   ? 42.888 -43.466 -14.374 1.00 36.22 ?  338 HOH   B O    1 
HETATM 7109 O O    . HOH   G 4 .   ? 43.032 -34.665 0.075   1.00 17.58 ?  339 HOH   B O    1 
HETATM 7110 O O    . HOH   G 4 .   ? 45.699 -36.200 -16.176 1.00 32.74 ?  340 HOH   B O    1 
HETATM 7111 O O    . HOH   G 4 .   ? 36.945 -15.008 -16.520 1.00 36.26 ?  341 HOH   B O    1 
HETATM 7112 O O    . HOH   G 4 .   ? 46.736 -19.918 12.292  1.00 30.98 ?  342 HOH   B O    1 
HETATM 7113 O O    . HOH   G 4 .   ? 38.465 -12.236 -16.210 1.00 38.12 ?  343 HOH   B O    1 
HETATM 7114 O O    . HOH   G 4 .   ? 32.919 -14.682 0.997   1.00 18.67 ?  344 HOH   B O    1 
HETATM 7115 O O    . HOH   G 4 .   ? 28.883 -42.951 -12.353 1.00 35.30 ?  345 HOH   B O    1 
HETATM 7116 O O    . HOH   G 4 .   ? 38.463 -22.361 15.023  1.00 40.07 ?  346 HOH   B O    1 
HETATM 7117 O O    . HOH   G 4 .   ? 39.743 -44.269 -11.246 1.00 34.39 ?  347 HOH   B O    1 
HETATM 7118 O O    . HOH   G 4 .   ? 37.059 -45.305 -9.765  1.00 37.11 ?  348 HOH   B O    1 
HETATM 7119 O O    . HOH   G 4 .   ? 40.405 -43.438 -9.129  1.00 24.86 ?  349 HOH   B O    1 
HETATM 7120 O O    . HOH   G 4 .   ? 34.523 -10.334 7.576   1.00 23.18 ?  350 HOH   B O    1 
HETATM 7121 O O    . HOH   G 4 .   ? 62.456 -20.119 -4.790  1.00 44.15 ?  351 HOH   B O    1 
HETATM 7122 O O    . HOH   G 4 .   ? 27.683 -26.579 -0.616  1.00 29.89 ?  352 HOH   B O    1 
HETATM 7123 O O    . HOH   G 4 .   ? 36.032 -8.589  -9.645  1.00 30.64 ?  353 HOH   B O    1 
HETATM 7124 O O    . HOH   G 4 .   ? 33.661 -9.263  -8.857  1.00 29.34 ?  354 HOH   B O    1 
HETATM 7125 O O    . HOH   G 4 .   ? 23.147 -23.604 6.814   1.00 35.56 ?  355 HOH   B O    1 
HETATM 7126 O O    . HOH   G 4 .   ? 55.605 -8.277  10.916  1.00 27.04 ?  356 HOH   B O    1 
HETATM 7127 O O    . HOH   G 4 .   ? 44.184 -37.332 -17.782 1.00 32.37 ?  357 HOH   B O    1 
HETATM 7128 O O    . HOH   G 4 .   ? 33.967 -7.845  11.439  1.00 38.99 ?  358 HOH   B O    1 
HETATM 7129 O O    . HOH   G 4 .   ? 56.399 -7.170  3.147   1.00 26.77 ?  359 HOH   B O    1 
HETATM 7130 O O    . HOH   G 4 .   ? 61.369 -19.845 1.633   1.00 33.90 ?  360 HOH   B O    1 
HETATM 7131 O O    . HOH   G 4 .   ? 43.076 -12.692 -21.182 1.00 36.93 ?  361 HOH   B O    1 
HETATM 7132 O O    . HOH   G 4 .   ? 40.212 -8.799  9.962   1.00 39.80 ?  362 HOH   B O    1 
HETATM 7133 O O    . HOH   G 4 .   ? 56.922 -21.528 -16.342 1.00 39.64 ?  363 HOH   B O    1 
HETATM 7134 O O    . HOH   G 4 .   ? 27.069 -25.936 -11.492 1.00 30.76 ?  364 HOH   B O    1 
HETATM 7135 O O    . HOH   G 4 .   ? 32.361 -23.602 14.052  1.00 41.91 ?  365 HOH   B O    1 
HETATM 7136 O O    . HOH   G 4 .   ? 36.111 -8.729  9.015   1.00 35.70 ?  366 HOH   B O    1 
HETATM 7137 O O    . HOH   G 4 .   ? 48.236 -26.472 8.851   1.00 39.17 ?  367 HOH   B O    1 
HETATM 7138 O O    . HOH   G 4 .   ? 40.034 -11.340 -13.974 1.00 29.79 ?  368 HOH   B O    1 
HETATM 7139 O O    . HOH   G 4 .   ? 54.153 -5.710  3.009   1.00 34.54 ?  369 HOH   B O    1 
HETATM 7140 O O    . HOH   G 4 .   ? 58.930 -10.435 9.234   1.00 39.55 ?  370 HOH   B O    1 
HETATM 7141 O O    . HOH   G 4 .   ? 41.811 -9.981  -17.401 1.00 50.85 ?  371 HOH   B O    1 
HETATM 7142 O O    . HOH   G 4 .   ? 51.936 -12.951 13.399  1.00 32.52 ?  372 HOH   B O    1 
HETATM 7143 O O    . HOH   G 4 .   ? 39.745 -7.042  7.888   1.00 41.41 ?  373 HOH   B O    1 
HETATM 7144 O O    . HOH   G 4 .   ? 38.042 -10.678 10.046  1.00 29.09 ?  374 HOH   B O    1 
HETATM 7145 O O    . HOH   G 4 .   ? 55.883 -7.705  -0.554  1.00 35.25 ?  375 HOH   B O    1 
HETATM 7146 O O    . HOH   G 4 .   ? 62.917 -12.312 7.005   1.00 36.16 ?  376 HOH   B O    1 
HETATM 7147 O O    . HOH   G 4 .   ? 40.015 -7.703  3.222   1.00 36.58 ?  377 HOH   B O    1 
HETATM 7148 O O    . HOH   G 4 .   ? 44.107 -5.592  -3.410  1.00 43.22 ?  378 HOH   B O    1 
HETATM 7149 O O    . HOH   G 4 .   ? 36.437 -22.702 13.335  1.00 25.61 ?  379 HOH   B O    1 
HETATM 7150 O O    . HOH   G 4 .   ? 39.684 -14.092 15.685  1.00 48.82 ?  380 HOH   B O    1 
HETATM 7151 O O    . HOH   G 4 .   ? 41.744 -6.735  -4.752  1.00 49.99 ?  381 HOH   B O    1 
HETATM 7152 O O    . HOH   G 4 .   ? 42.593 -17.097 -23.212 1.00 40.36 ?  382 HOH   B O    1 
HETATM 7153 O O    . HOH   G 4 .   ? 52.817 -29.887 7.150   1.00 22.41 ?  383 HOH   B O    1 
HETATM 7154 O O    . HOH   G 4 .   ? 60.369 -22.284 2.788   1.00 37.81 ?  384 HOH   B O    1 
HETATM 7155 O O    . HOH   G 4 .   ? 46.637 -5.354  2.945   1.00 38.04 ?  385 HOH   B O    1 
HETATM 7156 O O    . HOH   G 4 .   ? 35.184 -20.261 13.256  1.00 30.30 ?  386 HOH   B O    1 
HETATM 7157 O O    . HOH   G 4 .   ? 23.807 -20.692 -7.730  1.00 27.14 ?  387 HOH   B O    1 
HETATM 7158 O O    . HOH   G 4 .   ? 40.846 -9.790  15.826  1.00 44.33 ?  388 HOH   B O    1 
HETATM 7159 O O    . HOH   G 4 .   ? 35.183 -33.679 7.220   1.00 41.42 ?  389 HOH   B O    1 
HETATM 7160 O O    . HOH   G 4 .   ? 25.688 -18.745 -12.011 1.00 40.22 ?  390 HOH   B O    1 
HETATM 7161 O O    . HOH   G 4 .   ? 40.631 -6.586  -0.880  1.00 22.92 ?  391 HOH   B O    1 
HETATM 7162 O O    . HOH   G 4 .   ? 43.989 -31.701 -3.823  1.00 31.86 ?  392 HOH   B O    1 
HETATM 7163 O O    . HOH   G 4 .   ? 26.608 -27.981 -13.576 1.00 31.27 ?  393 HOH   B O    1 
HETATM 7164 O O    . HOH   G 4 .   ? 27.798 -27.075 2.106   1.00 29.94 ?  394 HOH   B O    1 
HETATM 7165 O O    . HOH   G 4 .   ? 45.656 -20.344 15.145  1.00 53.93 ?  395 HOH   B O    1 
HETATM 7166 O O    . HOH   G 4 .   ? 34.255 -33.377 9.622   1.00 32.77 ?  396 HOH   B O    1 
HETATM 7167 O O    . HOH   G 4 .   ? 24.552 -20.618 -10.554 1.00 35.50 ?  397 HOH   B O    1 
HETATM 7168 O O    . HOH   G 4 .   ? 26.834 -30.638 -12.702 1.00 25.37 ?  398 HOH   B O    1 
HETATM 7169 O O    . HOH   G 4 .   ? 50.587 -30.718 8.745   1.00 26.42 ?  399 HOH   B O    1 
HETATM 7170 O O    . HOH   G 4 .   ? 57.484 -6.431  -2.329  1.00 31.68 ?  400 HOH   B O    1 
HETATM 7171 O O    . HOH   G 4 .   ? 40.936 -11.797 -22.368 1.00 42.16 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.6075 0.6089 0.6452 0.0003  -0.0167 0.0530  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6092 0.6098 0.6443 0.0005  -0.0186 0.0546  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6044 0.6058 0.6346 -0.0014 -0.0167 0.0543  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6060 0.6065 0.6332 -0.0012 -0.0184 0.0559  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.5905 0.5932 0.6065 -0.0077 -0.0210 0.0639  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.5914 0.5936 0.6062 -0.0076 -0.0220 0.0649  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.5930 0.5955 0.6170 -0.0063 -0.0217 0.0644  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.5941 0.5962 0.6174 -0.0062 -0.0230 0.0657  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6121 0.6128 0.6436 0.0016  -0.0128 0.0477  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6143 0.6135 0.6403 0.0020  -0.0150 0.0497  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6149 0.6151 0.6450 0.0028  -0.0115 0.0453  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6172 0.6157 0.6413 0.0033  -0.0139 0.0474  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6145 0.6151 0.6449 0.0024  -0.0115 0.0457  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6168 0.6159 0.6408 0.0030  -0.0139 0.0479  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.5717 0.5763 0.5594 -0.0158 -0.0248 0.0733  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.5303 0.5389 0.4608 -0.0334 -0.0300 0.0892  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.4801 0.5021 0.4000 -0.0489 -0.0257 0.0767  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.4801 0.5031 0.3799 -0.0506 -0.0266 0.0840  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.5363 0.5362 0.4186 -0.0358 -0.0382 0.1173  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.5403 0.5318 0.3817 -0.0390 -0.0459 0.1422  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.5424 0.5280 0.3661 -0.0399 -0.0532 0.1549  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.5404 0.5304 0.3718 -0.0390 -0.0469 0.1502  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.4285 0.4615 0.3587 -0.0635 -0.0202 0.0568  5   SER   A N   
47   C CA  . SER   A 5   ? 0.3776 0.4221 0.3278 -0.0766 -0.0056 0.0323  5   SER   A CA  
48   C C   . SER   A 5   ? 0.3232 0.3729 0.2748 -0.0775 0.0118  0.0159  5   SER   A C   
49   O O   . SER   A 5   ? 0.3282 0.3832 0.2840 -0.0677 0.0101  -0.0004 5   SER   A O   
50   C CB  . SER   A 5   ? 0.3853 0.4323 0.3614 -0.0852 -0.0051 0.0265  5   SER   A CB  
51   O OG  . SER   A 5   ? 0.3901 0.4370 0.3761 -0.0912 -0.0021 0.0214  5   SER   A OG  
57   N N   A PHE   A 6   ? 0.2864 0.3355 0.2270 -0.0826 0.0274  0.0206  6   PHE   A N   
58   N N   B PHE   A 6   ? 0.2924 0.3470 0.2481 -0.0816 0.0235  0.0213  6   PHE   A N   
59   C CA  A PHE   A 6   ? 0.2545 0.2978 0.1847 -0.0819 0.0408  0.0302  6   PHE   A CA  
60   C CA  B PHE   A 6   ? 0.2633 0.3197 0.2233 -0.0828 0.0355  0.0356  6   PHE   A CA  
61   C C   A PHE   A 6   ? 0.2505 0.2913 0.1883 -0.0798 0.0552  0.0271  6   PHE   A C   
62   C C   B PHE   A 6   ? 0.2565 0.3095 0.2320 -0.0811 0.0499  0.0346  6   PHE   A C   
63   O O   A PHE   A 6   ? 0.2519 0.2907 0.2000 -0.0833 0.0606  0.0322  6   PHE   A O   
64   O O   B PHE   A 6   ? 0.2595 0.3104 0.2581 -0.0789 0.0518  0.0388  6   PHE   A O   
65   C CB  A PHE   A 6   ? 0.2355 0.2694 0.1654 -0.0726 0.0372  0.0344  6   PHE   A CB  
66   C CB  B PHE   A 6   ? 0.2469 0.3037 0.2066 -0.0797 0.0378  0.0485  6   PHE   A CB  
67   C CG  A PHE   A 6   ? 0.2203 0.2459 0.1683 -0.0597 0.0350  0.0259  6   PHE   A CG  
68   C CG  B PHE   A 6   ? 0.2354 0.2910 0.2109 -0.0730 0.0335  0.0452  6   PHE   A CG  
69   C CD1 A PHE   A 6   ? 0.2150 0.2365 0.1630 -0.0526 0.0286  0.0206  6   PHE   A CD1 
70   C CD1 B PHE   A 6   ? 0.2331 0.2862 0.2097 -0.0674 0.0305  0.0416  6   PHE   A CD1 
71   C CD2 A PHE   A 6   ? 0.2217 0.2398 0.1870 -0.0457 0.0385  0.0137  6   PHE   A CD2 
72   C CD2 B PHE   A 6   ? 0.2369 0.2890 0.2288 -0.0660 0.0294  0.0406  6   PHE   A CD2 
73   C CE1 A PHE   A 6   ? 0.2144 0.2348 0.1749 -0.0490 0.0350  0.0163  6   PHE   A CE1 
74   C CE1 B PHE   A 6   ? 0.2335 0.2849 0.2183 -0.0641 0.0324  0.0402  6   PHE   A CE1 
75   C CE2 A PHE   A 6   ? 0.2206 0.2346 0.1964 -0.0417 0.0401  0.0050  6   PHE   A CE2 
76   C CE2 B PHE   A 6   ? 0.2362 0.2876 0.2375 -0.0618 0.0271  0.0363  6   PHE   A CE2 
77   C CZ  A PHE   A 6   ? 0.2179 0.2332 0.1871 -0.0452 0.0364  0.0066  6   PHE   A CZ  
78   C CZ  B PHE   A 6   ? 0.2347 0.2848 0.2285 -0.0627 0.0270  0.0367  6   PHE   A CZ  
97   N N   A SER   A 7   ? 0.2472 0.2850 0.1944 -0.0710 0.0611  0.0213  7   SER   A N   
98   N N   B SER   A 7   ? 0.2511 0.2964 0.2229 -0.0782 0.0619  0.0319  7   SER   A N   
99   C CA  A SER   A 7   ? 0.2467 0.2817 0.2066 -0.0555 0.0572  0.0131  7   SER   A CA  
100  C CA  B SER   A 7   ? 0.2485 0.2862 0.2211 -0.0691 0.0612  0.0249  7   SER   A CA  
101  C C   A SER   A 7   ? 0.2280 0.2622 0.1895 -0.0459 0.0579  0.0124  7   SER   A C   
102  C C   B SER   A 7   ? 0.2256 0.2613 0.1966 -0.0626 0.0599  0.0300  7   SER   A C   
103  O O   A SER   A 7   ? 0.2347 0.2585 0.1960 -0.0459 0.0538  0.0112  7   SER   A O   
104  O O   B SER   A 7   ? 0.2288 0.2514 0.2006 -0.0682 0.0587  0.0390  7   SER   A O   
105  C CB  A SER   A 7   ? 0.2640 0.2964 0.2380 -0.0453 0.0510  0.0103  7   SER   A CB  
106  C CB  B SER   A 7   ? 0.2692 0.2984 0.2496 -0.0610 0.0566  0.0158  7   SER   A CB  
107  O OG  A SER   A 7   ? 0.2797 0.3065 0.2657 -0.0369 0.0445  0.0126  7   SER   A OG  
108  O OG  B SER   A 7   ? 0.2860 0.3068 0.2792 -0.0538 0.0530  0.0064  7   SER   A OG  
119  N N   A GLY   A 8   ? 0.2070 0.2482 0.1837 -0.0364 0.0560  0.0099  8   GLY   A N   
120  N N   B GLY   A 8   ? 0.2031 0.2460 0.1850 -0.0519 0.0499  0.0237  8   GLY   A N   
121  C CA  A GLY   A 8   ? 0.1896 0.2295 0.1832 -0.0294 0.0511  0.0149  8   GLY   A CA  
122  C CA  B GLY   A 8   ? 0.1902 0.2279 0.1857 -0.0415 0.0398  0.0248  8   GLY   A CA  
123  C C   A GLY   A 8   ? 0.1644 0.2112 0.1760 -0.0184 0.0488  0.0188  8   GLY   A C   
124  C C   B GLY   A 8   ? 0.1713 0.2123 0.1908 -0.0271 0.0348  0.0278  8   GLY   A C   
125  O O   A GLY   A 8   ? 0.1649 0.2165 0.1883 -0.0064 0.0469  0.0028  8   GLY   A O   
126  O O   B GLY   A 8   ? 0.1724 0.2167 0.2059 -0.0164 0.0308  0.0186  8   GLY   A O   
133  N N   A TYR   A 9   ? 0.1442 0.1943 0.1691 -0.0133 0.0442  0.0342  9   TYR   A N   
134  N N   B TYR   A 9   ? 0.1578 0.1968 0.1907 -0.0195 0.0300  0.0348  9   TYR   A N   
135  C CA  A TYR   A 9   ? 0.1341 0.1837 0.1588 -0.0102 0.0327  0.0396  9   TYR   A CA  
136  C CA  B TYR   A 9   ? 0.1500 0.1830 0.1781 -0.0202 0.0265  0.0453  9   TYR   A CA  
137  C C   A TYR   A 9   ? 0.1228 0.1814 0.1576 -0.0051 0.0405  0.0462  9   TYR   A C   
138  C C   B TYR   A 9   ? 0.1434 0.1667 0.1764 -0.0160 0.0349  0.0515  9   TYR   A C   
139  O O   A TYR   A 9   ? 0.1273 0.1928 0.1655 -0.0033 0.0288  0.0484  9   TYR   A O   
140  O O   B TYR   A 9   ? 0.1446 0.1698 0.1776 -0.0130 0.0344  0.0353  9   TYR   A O   
141  C CB  A TYR   A 9   ? 0.1329 0.1799 0.1625 -0.0148 0.0290  0.0266  9   TYR   A CB  
142  C CB  B TYR   A 9   ? 0.1442 0.1903 0.1793 -0.0225 0.0275  0.0395  9   TYR   A CB  
143  C CG  A TYR   A 9   ? 0.1392 0.1723 0.1625 -0.0046 0.0312  0.0158  9   TYR   A CG  
144  C CG  B TYR   A 9   ? 0.1461 0.1922 0.1789 -0.0121 0.0316  0.0330  9   TYR   A CG  
145  C CD1 A TYR   A 9   ? 0.1420 0.1692 0.1657 -0.0047 0.0326  0.0072  9   TYR   A CD1 
146  C CD1 B TYR   A 9   ? 0.1488 0.1915 0.1809 -0.0118 0.0345  0.0330  9   TYR   A CD1 
147  C CD2 A TYR   A 9   ? 0.1487 0.1644 0.1687 -0.0052 0.0295  0.0125  9   TYR   A CD2 
148  C CD2 B TYR   A 9   ? 0.1455 0.1852 0.1728 -0.0075 0.0323  0.0329  9   TYR   A CD2 
149  C CE1 A TYR   A 9   ? 0.1436 0.1650 0.1742 -0.0013 0.0291  -0.0069 9   TYR   A CE1 
150  C CE1 B TYR   A 9   ? 0.1465 0.1853 0.1782 -0.0100 0.0425  0.0304  9   TYR   A CE1 
151  C CE2 A TYR   A 9   ? 0.1534 0.1658 0.1731 -0.0082 0.0337  0.0025  9   TYR   A CE2 
152  C CE2 B TYR   A 9   ? 0.1435 0.1803 0.1648 -0.0034 0.0435  0.0288  9   TYR   A CE2 
153  C CZ  A TYR   A 9   ? 0.1498 0.1642 0.1800 -0.0119 0.0333  -0.0006 9   TYR   A CZ  
154  C CZ  B TYR   A 9   ? 0.1361 0.1727 0.1758 -0.0060 0.0452  0.0322  9   TYR   A CZ  
155  O OH  A TYR   A 9   ? 0.1553 0.1678 0.2036 -0.0143 0.0310  -0.0098 9   TYR   A OH  
156  O OH  B TYR   A 9   ? 0.1290 0.1664 0.1896 -0.0019 0.0438  0.0342  9   TYR   A OH  
175  N N   A LEU   A 10  ? 0.1250 0.1720 0.1610 -0.0079 0.0351  0.0360  10  LEU   A N   
176  N N   B LEU   A 10  ? 0.1426 0.1539 0.1795 -0.0150 0.0233  0.0572  10  LEU   A N   
177  C CA  A LEU   A 10  ? 0.1222 0.1705 0.1705 -0.0159 0.0227  0.0373  10  LEU   A CA  
178  C CA  B LEU   A 10  ? 0.1324 0.1530 0.1851 -0.0154 0.0120  0.0695  10  LEU   A CA  
179  C C   A LEU   A 10  ? 0.1240 0.1624 0.1645 -0.0224 0.0184  0.0285  10  LEU   A C   
180  C C   B LEU   A 10  ? 0.1296 0.1468 0.1878 -0.0170 0.0085  0.0654  10  LEU   A C   
181  O O   A LEU   A 10  ? 0.1296 0.1511 0.1526 -0.0237 0.0283  0.0298  10  LEU   A O   
182  O O   B LEU   A 10  ? 0.1298 0.1342 0.1811 -0.0191 0.0118  0.0572  10  LEU   A O   
183  C CB  A LEU   A 10  ? 0.1264 0.1748 0.1980 -0.0165 0.0188  0.0473  10  LEU   A CB  
184  C CB  B LEU   A 10  ? 0.1341 0.1557 0.2025 -0.0113 0.0039  0.0778  10  LEU   A CB  
185  C CG  A LEU   A 10  ? 0.1356 0.1809 0.2234 -0.0127 0.0078  0.0492  10  LEU   A CG  
186  C CG  B LEU   A 10  ? 0.1412 0.1623 0.2214 -0.0077 -0.0080 0.0727  10  LEU   A CG  
187  C CD1 A LEU   A 10  ? 0.1346 0.1789 0.2335 -0.0146 0.0161  0.0492  10  LEU   A CD1 
188  C CD1 B LEU   A 10  ? 0.1408 0.1605 0.2330 -0.0090 -0.0024 0.0625  10  LEU   A CD1 
189  C CD2 A LEU   A 10  ? 0.1521 0.1904 0.2287 -0.0162 0.0093  0.0460  10  LEU   A CD2 
190  C CD2 B LEU   A 10  ? 0.1569 0.1755 0.2301 -0.0082 -0.0132 0.0620  10  LEU   A CD2 
213  N N   A LYS   A 11  ? 0.1232 0.1647 0.1770 -0.0257 0.0093  0.0346  11  LYS   A N   
214  N N   B LYS   A 11  ? 0.1244 0.1479 0.1935 -0.0160 -0.0028 0.0751  11  LYS   A N   
215  C CA  A LYS   A 11  ? 0.1323 0.1633 0.1940 -0.0306 0.0108  0.0238  11  LYS   A CA  
216  C CA  B LYS   A 11  ? 0.1354 0.1441 0.2094 -0.0170 0.0001  0.0719  11  LYS   A CA  
217  C C   A LYS   A 11  ? 0.1271 0.1668 0.2015 -0.0322 0.0216  0.0185  11  LYS   A C   
218  C C   B LYS   A 11  ? 0.1273 0.1402 0.2065 -0.0161 0.0120  0.0617  11  LYS   A C   
219  O O   A LYS   A 11  ? 0.1305 0.1678 0.2186 -0.0439 0.0318  0.0150  11  LYS   A O   
220  O O   B LYS   A 11  ? 0.1113 0.1355 0.2089 -0.0154 -0.0004 0.0607  11  LYS   A O   
221  C CB  A LYS   A 11  ? 0.1409 0.1552 0.1961 -0.0361 0.0094  0.0149  11  LYS   A CB  
222  C CB  B LYS   A 11  ? 0.1523 0.1401 0.2206 -0.0229 -0.0040 0.0777  11  LYS   A CB  
223  C CG  A LYS   A 11  ? 0.1528 0.1519 0.2024 -0.0310 0.0075  0.0198  11  LYS   A CG  
224  C CG  B LYS   A 11  ? 0.1671 0.1421 0.2262 -0.0190 -0.0073 0.0810  11  LYS   A CG  
225  C CD  A LYS   A 11  ? 0.1615 0.1482 0.2094 -0.0299 0.0097  0.0184  11  LYS   A CD  
226  C CD  B LYS   A 11  ? 0.1838 0.1492 0.2307 -0.0220 -0.0027 0.0762  11  LYS   A CD  
227  C CE  A LYS   A 11  ? 0.1724 0.1489 0.2161 -0.0183 0.0094  0.0122  11  LYS   A CE  
228  C CE  B LYS   A 11  ? 0.1993 0.1540 0.2288 -0.0217 -0.0007 0.0776  11  LYS   A CE  
229  N NZ  A LYS   A 11  ? 0.1684 0.1444 0.2172 -0.0088 0.0104  0.0019  11  LYS   A NZ  
230  N NZ  B LYS   A 11  ? 0.2018 0.1576 0.2192 -0.0199 -0.0036 0.0689  11  LYS   A NZ  
257  N N   A LEU   A 12  ? 0.1208 0.1621 0.1950 -0.0317 0.0187  0.0193  12  LEU   A N   
258  N N   B LEU   A 12  ? 0.1334 0.1389 0.2106 -0.0201 0.0188  0.0433  12  LEU   A N   
259  C CA  A LEU   A 12  ? 0.1154 0.1679 0.1918 -0.0232 0.0222  0.0332  12  LEU   A CA  
260  C CA  B LEU   A 12  ? 0.1451 0.1557 0.2120 -0.0137 0.0152  0.0444  12  LEU   A CA  
261  C C   A LEU   A 12  ? 0.1151 0.1570 0.1873 -0.0282 0.0190  0.0367  12  LEU   A C   
262  C C   B LEU   A 12  ? 0.1573 0.1563 0.2131 -0.0241 0.0143  0.0347  12  LEU   A C   
263  O O   A LEU   A 12  ? 0.1288 0.1595 0.1874 -0.0222 0.0092  0.0341  12  LEU   A O   
264  O O   B LEU   A 12  ? 0.1659 0.1661 0.2112 -0.0226 0.0080  0.0220  12  LEU   A O   
265  C CB  A LEU   A 12  ? 0.1280 0.1777 0.2069 -0.0193 0.0293  0.0389  12  LEU   A CB  
266  C CB  B LEU   A 12  ? 0.1546 0.1592 0.2177 -0.0093 0.0075  0.0545  12  LEU   A CB  
267  C CG  A LEU   A 12  ? 0.1365 0.1856 0.2199 -0.0130 0.0445  0.0385  12  LEU   A CG  
268  C CG  B LEU   A 12  ? 0.1606 0.1637 0.2215 -0.0019 0.0056  0.0608  12  LEU   A CG  
269  C CD1 A LEU   A 12  ? 0.1456 0.1929 0.2353 -0.0065 0.0481  0.0389  12  LEU   A CD1 
270  C CD1 B LEU   A 12  ? 0.1713 0.1686 0.2390 0.0038  0.0118  0.0642  12  LEU   A CD1 
271  C CD2 A LEU   A 12  ? 0.1384 0.1908 0.2311 -0.0115 0.0455  0.0299  12  LEU   A CD2 
272  C CD2 B LEU   A 12  ? 0.1642 0.1671 0.2277 0.0006  -0.0006 0.0534  12  LEU   A CD2 
295  N N   A THR   A 13  ? 0.1019 0.1456 0.2016 -0.0235 0.0191  0.0353  13  THR   A N   
296  N N   B THR   A 13  ? 0.1601 0.1553 0.2310 -0.0223 0.0167  0.0290  13  THR   A N   
297  C CA  A THR   A 13  ? 0.1040 0.1411 0.2149 -0.0205 0.0177  0.0337  13  THR   A CA  
298  C CA  B THR   A 13  ? 0.1643 0.1571 0.2343 -0.0256 0.0212  0.0303  13  THR   A CA  
299  C C   A THR   A 13  ? 0.1119 0.1330 0.2110 -0.0202 0.0133  0.0264  13  THR   A C   
300  C C   B THR   A 13  ? 0.1717 0.1667 0.2398 -0.0383 0.0211  0.0307  13  THR   A C   
301  O O   A THR   A 13  ? 0.1184 0.1286 0.2044 -0.0039 0.0065  0.0284  13  THR   A O   
302  O O   B THR   A 13  ? 0.1771 0.1658 0.2526 -0.0433 0.0185  0.0309  13  THR   A O   
303  C CB  A THR   A 13  ? 0.1092 0.1514 0.2445 -0.0206 0.0198  0.0352  13  THR   A CB  
304  C CB  B THR   A 13  ? 0.1697 0.1555 0.2500 -0.0184 0.0238  0.0285  13  THR   A CB  
305  O OG1 A THR   A 13  ? 0.1057 0.1517 0.2591 -0.0161 0.0339  0.0422  13  THR   A OG1 
306  O OG1 B THR   A 13  ? 0.1737 0.1381 0.2634 -0.0143 0.0178  0.0296  13  THR   A OG1 
307  C CG2 A THR   A 13  ? 0.1233 0.1632 0.2526 -0.0150 0.0187  0.0305  13  THR   A CG2 
308  C CG2 B THR   A 13  ? 0.1766 0.1666 0.2527 -0.0080 0.0285  0.0205  13  THR   A CG2 
323  N N   A ASP   A 14  ? 0.1210 0.1272 0.2105 -0.0253 0.0047  0.0270  14  ASP   A N   
324  N N   B ASP   A 14  ? 0.1763 0.1711 0.2343 -0.0439 0.0165  0.0404  14  ASP   A N   
325  C CA  A ASP   A 14  ? 0.1282 0.1253 0.2070 -0.0140 0.0030  0.0334  14  ASP   A CA  
326  C CA  B ASP   A 14  ? 0.1850 0.1833 0.2510 -0.0343 0.0070  0.0432  14  ASP   A CA  
327  C C   A ASP   A 14  ? 0.1323 0.1211 0.1999 -0.0151 0.0028  0.0339  14  ASP   A C   
328  C C   B ASP   A 14  ? 0.1672 0.1751 0.2394 -0.0350 -0.0020 0.0454  14  ASP   A C   
329  O O   A ASP   A 14  ? 0.1452 0.1274 0.2024 -0.0159 0.0094  0.0343  14  ASP   A O   
330  O O   B ASP   A 14  ? 0.1708 0.1729 0.2485 -0.0339 -0.0049 0.0445  14  ASP   A O   
331  C CB  A ASP   A 14  ? 0.1446 0.1467 0.2210 -0.0124 0.0201  0.0457  14  ASP   A CB  
332  C CB  B ASP   A 14  ? 0.2153 0.2079 0.2958 -0.0261 0.0073  0.0462  14  ASP   A CB  
333  C CG  A ASP   A 14  ? 0.1655 0.1883 0.2547 -0.0067 0.0244  0.0395  14  ASP   A CG  
334  C CG  B ASP   A 14  ? 0.2394 0.2397 0.3408 -0.0191 0.0204  0.0516  14  ASP   A CG  
335  O OD1 A ASP   A 14  ? 0.1770 0.1969 0.2710 0.0106  0.0109  0.0281  14  ASP   A OD1 
336  O OD1 B ASP   A 14  ? 0.2511 0.2507 0.3561 -0.0114 0.0296  0.0584  14  ASP   A OD1 
337  O OD2 A ASP   A 14  ? 0.1834 0.2201 0.2647 -0.0069 0.0319  0.0420  14  ASP   A OD2 
338  O OD2 B ASP   A 14  ? 0.2535 0.2641 0.3665 -0.0155 0.0206  0.0450  14  ASP   A OD2 
347  N N   A ASN   A 15  ? 0.1263 0.1122 0.2052 -0.0183 0.0118  0.0391  15  ASN   A N   
348  N N   B ASN   A 15  ? 0.1525 0.1716 0.2377 -0.0290 0.0016  0.0476  15  ASN   A N   
349  C CA  A ASN   A 15  ? 0.1294 0.1132 0.2334 -0.0211 0.0077  0.0275  15  ASN   A CA  
350  C CA  B ASN   A 15  ? 0.1416 0.1660 0.2408 -0.0248 -0.0018 0.0405  15  ASN   A CA  
351  C C   A ASN   A 15  ? 0.1252 0.1113 0.2609 -0.0241 0.0144  0.0364  15  ASN   A C   
352  C C   B ASN   A 15  ? 0.1374 0.1563 0.2585 -0.0175 -0.0031 0.0410  15  ASN   A C   
353  O O   A ASN   A 15  ? 0.1325 0.1205 0.3044 -0.0290 0.0035  0.0346  15  ASN   A O   
354  O O   B ASN   A 15  ? 0.1428 0.1603 0.3013 -0.0135 -0.0122 0.0382  15  ASN   A O   
355  C CB  A ASN   A 15  ? 0.1314 0.1116 0.2303 -0.0108 0.0055  0.0205  15  ASN   A CB  
356  C CB  B ASN   A 15  ? 0.1359 0.1673 0.2308 -0.0200 0.0054  0.0390  15  ASN   A CB  
357  C CG  A ASN   A 15  ? 0.1331 0.1133 0.2368 -0.0113 0.0134  0.0115  15  ASN   A CG  
358  C CG  B ASN   A 15  ? 0.1329 0.1688 0.2348 -0.0151 0.0168  0.0265  15  ASN   A CG  
359  O OD1 A ASN   A 15  ? 0.1374 0.1152 0.2535 -0.0159 -0.0033 0.0157  15  ASN   A OD1 
360  O OD1 B ASN   A 15  ? 0.1364 0.1684 0.2586 -0.0217 0.0110  0.0282  15  ASN   A OD1 
361  N ND2 A ASN   A 15  ? 0.1347 0.1281 0.2323 -0.0147 0.0259  0.0077  15  ASN   A ND2 
362  N ND2 B ASN   A 15  ? 0.1330 0.1772 0.2250 -0.0126 0.0324  0.0190  15  ASN   A ND2 
375  N N   A VAL   A 16  ? 0.1247 0.1102 0.2483 -0.0204 0.0189  0.0407  16  VAL   A N   
376  N N   B VAL   A 16  ? 0.1382 0.1476 0.2336 -0.0139 -0.0006 0.0446  16  VAL   A N   
377  C CA  A VAL   A 16  ? 0.1186 0.1214 0.2382 -0.0193 0.0223  0.0343  16  VAL   A CA  
378  C CA  B VAL   A 16  ? 0.1367 0.1497 0.2192 -0.0124 0.0091  0.0407  16  VAL   A CA  
379  C C   A VAL   A 16  ? 0.1082 0.1229 0.2260 -0.0223 0.0112  0.0351  16  VAL   A C   
380  C C   B VAL   A 16  ? 0.1315 0.1461 0.2079 -0.0141 0.0139  0.0337  16  VAL   A C   
381  O O   A VAL   A 16  ? 0.1081 0.1303 0.2331 -0.0222 0.0119  0.0323  16  VAL   A O   
382  O O   B VAL   A 16  ? 0.1315 0.1489 0.2109 -0.0166 0.0232  0.0295  16  VAL   A O   
383  C CB  A VAL   A 16  ? 0.1328 0.1348 0.2440 -0.0031 0.0431  0.0339  16  VAL   A CB  
384  C CB  B VAL   A 16  ? 0.1465 0.1603 0.2258 -0.0023 0.0220  0.0453  16  VAL   A CB  
385  C CG1 A VAL   A 16  ? 0.1395 0.1445 0.2565 0.0069  0.0448  0.0245  16  VAL   A CG1 
386  C CG1 B VAL   A 16  ? 0.1535 0.1686 0.2342 0.0042  0.0259  0.0469  16  VAL   A CG1 
387  C CG2 A VAL   A 16  ? 0.1444 0.1416 0.2461 0.0034  0.0527  0.0379  16  VAL   A CG2 
388  C CG2 B VAL   A 16  ? 0.1550 0.1692 0.2390 0.0010  0.0304  0.0393  16  VAL   A CG2 
407  N N   A TYR   A 17  ? 0.1080 0.1172 0.2109 -0.0197 0.0082  0.0419  17  TYR   A N   
408  N N   B TYR   A 17  ? 0.1322 0.1406 0.1956 -0.0069 0.0177  0.0345  17  TYR   A N   
409  C CA  A TYR   A 17  ? 0.1089 0.1211 0.1860 -0.0250 0.0049  0.0496  17  TYR   A CA  
410  C CA  B TYR   A 17  ? 0.1365 0.1470 0.1841 -0.0054 0.0215  0.0367  17  TYR   A CA  
411  C C   A TYR   A 17  ? 0.1095 0.1263 0.1947 -0.0235 0.0101  0.0467  17  TYR   A C   
412  C C   B TYR   A 17  ? 0.1336 0.1326 0.1871 -0.0073 0.0271  0.0285  17  TYR   A C   
413  O O   A TYR   A 17  ? 0.1091 0.1324 0.2123 -0.0215 0.0157  0.0454  17  TYR   A O   
414  O O   B TYR   A 17  ? 0.1297 0.1261 0.2099 -0.0014 0.0391  0.0274  17  TYR   A O   
415  C CB  A TYR   A 17  ? 0.1286 0.1201 0.1798 -0.0286 -0.0094 0.0451  17  TYR   A CB  
416  C CB  B TYR   A 17  ? 0.1574 0.1675 0.2041 -0.0038 0.0124  0.0311  17  TYR   A CB  
417  C CG  A TYR   A 17  ? 0.1422 0.1277 0.1655 -0.0319 -0.0215 0.0318  17  TYR   A CG  
418  C CG  B TYR   A 17  ? 0.1754 0.1925 0.2187 -0.0023 0.0065  0.0259  17  TYR   A CG  
419  C CD1 A TYR   A 17  ? 0.1485 0.1362 0.1779 -0.0247 -0.0229 0.0285  17  TYR   A CD1 
420  C CD1 B TYR   A 17  ? 0.1852 0.2044 0.2379 0.0055  -0.0060 0.0268  17  TYR   A CD1 
421  C CD2 A TYR   A 17  ? 0.1468 0.1366 0.1484 -0.0336 -0.0240 0.0401  17  TYR   A CD2 
422  C CD2 B TYR   A 17  ? 0.1845 0.2089 0.2268 0.0016  0.0133  0.0320  17  TYR   A CD2 
423  C CE1 A TYR   A 17  ? 0.1423 0.1369 0.1838 -0.0308 -0.0235 0.0386  17  TYR   A CE1 
424  C CE1 B TYR   A 17  ? 0.1942 0.2157 0.2507 0.0053  -0.0012 0.0350  17  TYR   A CE1 
425  C CE2 A TYR   A 17  ? 0.1450 0.1340 0.1676 -0.0365 -0.0273 0.0390  17  TYR   A CE2 
426  C CE2 B TYR   A 17  ? 0.1950 0.2163 0.2453 0.0080  0.0064  0.0329  17  TYR   A CE2 
427  C CZ  A TYR   A 17  ? 0.1425 0.1332 0.1788 -0.0328 -0.0269 0.0397  17  TYR   A CZ  
428  C CZ  B TYR   A 17  ? 0.1987 0.2224 0.2588 0.0105  0.0008  0.0363  17  TYR   A CZ  
429  O OH  A TYR   A 17  ? 0.1491 0.1294 0.1745 -0.0302 -0.0235 0.0419  17  TYR   A OH  
430  O OH  B TYR   A 17  ? 0.2060 0.2343 0.2858 0.0154  -0.0048 0.0357  17  TYR   A OH  
449  N N   A ILE   A 18  ? 0.1122 0.1299 0.1873 -0.0223 0.0196  0.0533  18  ILE   A N   
450  N N   B ILE   A 18  ? 0.1392 0.1342 0.1772 -0.0070 0.0248  0.0328  18  ILE   A N   
451  C CA  A ILE   A 18  ? 0.1133 0.1357 0.1836 -0.0203 0.0326  0.0530  18  ILE   A CA  
452  C CA  B ILE   A 18  ? 0.1431 0.1367 0.1755 0.0018  0.0188  0.0328  18  ILE   A CA  
453  C C   A ILE   A 18  ? 0.1160 0.1414 0.1836 -0.0160 0.0312  0.0548  18  ILE   A C   
454  C C   B ILE   A 18  ? 0.1468 0.1455 0.1713 0.0026  0.0207  0.0361  18  ILE   A C   
455  O O   A ILE   A 18  ? 0.1047 0.1491 0.1909 -0.0188 0.0325  0.0617  18  ILE   A O   
456  O O   B ILE   A 18  ? 0.1486 0.1553 0.1717 -0.0088 0.0233  0.0359  18  ILE   A O   
457  C CB  A ILE   A 18  ? 0.1193 0.1495 0.1822 -0.0170 0.0439  0.0489  18  ILE   A CB  
458  C CB  B ILE   A 18  ? 0.1414 0.1417 0.1775 0.0121  0.0102  0.0409  18  ILE   A CB  
459  C CG1 A ILE   A 18  ? 0.1382 0.1631 0.1871 -0.0149 0.0426  0.0512  18  ILE   A CG1 
460  C CG1 B ILE   A 18  ? 0.1437 0.1479 0.1792 0.0252  0.0113  0.0467  18  ILE   A CG1 
461  C CG2 A ILE   A 18  ? 0.1196 0.1593 0.1916 -0.0257 0.0367  0.0432  18  ILE   A CG2 
462  C CG2 B ILE   A 18  ? 0.1420 0.1474 0.1853 0.0106  -0.0059 0.0408  18  ILE   A CG2 
463  C CD1 A ILE   A 18  ? 0.1579 0.1792 0.2119 -0.0122 0.0251  0.0444  18  ILE   A CD1 
464  C CD1 B ILE   A 18  ? 0.1495 0.1579 0.1887 0.0302  -0.0039 0.0562  18  ILE   A CD1 
487  N N   A LYS   A 19  ? 0.1313 0.1445 0.1791 -0.0107 0.0492  0.0473  19  LYS   A N   
488  N N   B LYS   A 19  ? 0.1500 0.1493 0.1804 0.0159  0.0452  0.0339  19  LYS   A N   
489  C CA  A LYS   A 19  ? 0.1467 0.1453 0.1779 -0.0138 0.0462  0.0394  19  LYS   A CA  
490  C CA  B LYS   A 19  ? 0.1531 0.1562 0.1878 0.0200  0.0515  0.0377  19  LYS   A CA  
491  C C   A LYS   A 19  ? 0.1490 0.1390 0.1695 -0.0118 0.0483  0.0449  19  LYS   A C   
492  C C   B LYS   A 19  ? 0.1441 0.1504 0.1811 0.0199  0.0535  0.0400  19  LYS   A C   
493  O O   A LYS   A 19  ? 0.1425 0.1376 0.1551 -0.0132 0.0371  0.0350  19  LYS   A O   
494  O O   B LYS   A 19  ? 0.1361 0.1453 0.1752 0.0146  0.0444  0.0358  19  LYS   A O   
495  C CB  A LYS   A 19  ? 0.1584 0.1638 0.1735 -0.0164 0.0452  0.0351  19  LYS   A CB  
496  C CB  B LYS   A 19  ? 0.1611 0.1777 0.1821 0.0250  0.0541  0.0443  19  LYS   A CB  
497  C CG  A LYS   A 19  ? 0.1744 0.1732 0.1746 -0.0183 0.0440  0.0256  19  LYS   A CG  
498  C CG  B LYS   A 19  ? 0.1731 0.1941 0.1953 0.0202  0.0520  0.0370  19  LYS   A CG  
499  C CD  A LYS   A 19  ? 0.1859 0.1810 0.1775 -0.0171 0.0425  0.0231  19  LYS   A CD  
500  C CD  B LYS   A 19  ? 0.1837 0.2101 0.2029 0.0178  0.0497  0.0307  19  LYS   A CD  
501  C CE  A LYS   A 19  ? 0.1919 0.1837 0.1806 -0.0172 0.0407  0.0195  19  LYS   A CE  
502  C CE  B LYS   A 19  ? 0.1938 0.2241 0.2059 0.0098  0.0483  0.0267  19  LYS   A CE  
503  N NZ  A LYS   A 19  ? 0.1940 0.1848 0.1833 -0.0152 0.0385  0.0190  19  LYS   A NZ  
504  N NZ  B LYS   A 19  ? 0.1992 0.2324 0.2062 0.0084  0.0446  0.0219  19  LYS   A NZ  
531  N N   A ASN   A 20  ? 0.1614 0.1391 0.1937 -0.0113 0.0570  0.0489  20  ASN   A N   
532  N N   B ASN   A 20  ? 0.1491 0.1558 0.1882 0.0187  0.0509  0.0364  20  ASN   A N   
533  C CA  A ASN   A 20  ? 0.1721 0.1529 0.2021 -0.0009 0.0631  0.0387  20  ASN   A CA  
534  C CA  B ASN   A 20  ? 0.1460 0.1682 0.1833 0.0213  0.0521  0.0303  20  ASN   A CA  
535  C C   A ASN   A 20  ? 0.1787 0.1506 0.1997 0.0014  0.0668  0.0417  20  ASN   A C   
536  C C   B ASN   A 20  ? 0.1566 0.1700 0.1852 0.0221  0.0604  0.0302  20  ASN   A C   
537  O O   A ASN   A 20  ? 0.1893 0.1500 0.1972 -0.0055 0.0641  0.0359  20  ASN   A O   
538  O O   B ASN   A 20  ? 0.1699 0.1802 0.1834 0.0198  0.0599  0.0265  20  ASN   A O   
539  C CB  A ASN   A 20  ? 0.1837 0.1676 0.2153 0.0083  0.0664  0.0337  20  ASN   A CB  
540  C CB  B ASN   A 20  ? 0.1423 0.1746 0.1816 0.0254  0.0461  0.0305  20  ASN   A CB  
541  C CG  A ASN   A 20  ? 0.1974 0.1773 0.2373 0.0146  0.0631  0.0244  20  ASN   A CG  
542  C CG  B ASN   A 20  ? 0.1398 0.1756 0.1771 0.0274  0.0332  0.0296  20  ASN   A CG  
543  O OD1 A ASN   A 20  ? 0.2139 0.1904 0.2586 0.0193  0.0665  0.0137  20  ASN   A OD1 
544  O OD1 B ASN   A 20  ? 0.1357 0.1765 0.1851 0.0302  0.0268  0.0256  20  ASN   A OD1 
545  N ND2 A ASN   A 20  ? 0.1972 0.1698 0.2463 0.0123  0.0561  0.0320  20  ASN   A ND2 
546  N ND2 B ASN   A 20  ? 0.1447 0.1762 0.1885 0.0194  0.0263  0.0376  20  ASN   A ND2 
559  N N   A ALA   A 21  ? 0.1794 0.1600 0.2019 0.0051  0.0626  0.0351  21  ALA   A N   
560  N N   B ALA   A 21  ? 0.1645 0.1735 0.1854 0.0171  0.0513  0.0168  21  ALA   A N   
561  C CA  A ALA   A 21  ? 0.1799 0.1595 0.2018 0.0057  0.0578  0.0370  21  ALA   A CA  
562  C CA  B ALA   A 21  ? 0.1718 0.1688 0.1868 0.0101  0.0451  0.0136  21  ALA   A CA  
563  C C   A ALA   A 21  ? 0.1725 0.1589 0.2023 -0.0008 0.0565  0.0345  21  ALA   A C   
564  C C   B ALA   A 21  ? 0.1608 0.1551 0.1718 0.0043  0.0529  0.0092  21  ALA   A C   
565  O O   A ALA   A 21  ? 0.1723 0.1693 0.2025 -0.0069 0.0543  0.0262  21  ALA   A O   
566  O O   B ALA   A 21  ? 0.1620 0.1559 0.1785 0.0085  0.0506  0.0033  21  ALA   A O   
567  C CB  A ALA   A 21  ? 0.1868 0.1698 0.2054 0.0072  0.0550  0.0376  21  ALA   A CB  
568  C CB  B ALA   A 21  ? 0.1903 0.1872 0.2146 0.0058  0.0286  0.0117  21  ALA   A CB  
579  N N   A ASP   A 22  ? 0.1734 0.1533 0.2076 -0.0003 0.0421  0.0387  22  ASP   A N   
580  N N   B ASP   A 22  ? 0.1580 0.1429 0.1611 0.0003  0.0470  0.0113  22  ASP   A N   
581  C CA  A ASP   A 22  ? 0.1776 0.1585 0.2017 0.0007  0.0277  0.0397  22  ASP   A CA  
582  C CA  B ASP   A 22  ? 0.1566 0.1433 0.1542 0.0008  0.0382  0.0078  22  ASP   A CA  
583  C C   A ASP   A 22  ? 0.1655 0.1607 0.1720 0.0018  0.0353  0.0432  22  ASP   A C   
584  C C   B ASP   A 22  ? 0.1484 0.1397 0.1281 -0.0081 0.0349  0.0102  22  ASP   A C   
585  O O   A ASP   A 22  ? 0.1673 0.1661 0.1636 0.0012  0.0374  0.0487  22  ASP   A O   
586  O O   B ASP   A 22  ? 0.1505 0.1395 0.1370 -0.0041 0.0283  0.0099  22  ASP   A O   
587  C CB  A ASP   A 22  ? 0.1939 0.1593 0.2299 0.0009  0.0189  0.0314  22  ASP   A CB  
588  C CB  B ASP   A 22  ? 0.1658 0.1477 0.1855 0.0126  0.0456  -0.0027 22  ASP   A CB  
589  C CG  A ASP   A 22  ? 0.2034 0.1625 0.2627 -0.0006 -0.0013 0.0273  22  ASP   A CG  
590  C CG  B ASP   A 22  ? 0.1774 0.1492 0.2156 0.0151  0.0517  -0.0055 22  ASP   A CG  
591  O OD1 A ASP   A 22  ? 0.2008 0.1576 0.2744 -0.0183 -0.0107 0.0250  22  ASP   A OD1 
592  O OD1 B ASP   A 22  ? 0.1836 0.1441 0.1893 0.0154  0.0560  0.0064  22  ASP   A OD1 
593  O OD2 A ASP   A 22  ? 0.2117 0.1734 0.2902 0.0159  -0.0075 0.0317  22  ASP   A OD2 
594  O OD2 B ASP   A 22  ? 0.1878 0.1652 0.2623 0.0116  0.0501  -0.0001 22  ASP   A OD2 
603  N N   A ILE   A 23  ? 0.1629 0.1642 0.1663 -0.0039 0.0355  0.0330  23  ILE   A N   
604  N N   B ILE   A 23  ? 0.1373 0.1390 0.1155 -0.0044 0.0241  0.0134  23  ILE   A N   
605  C CA  A ILE   A 23  ? 0.1654 0.1608 0.1492 -0.0028 0.0394  0.0294  23  ILE   A CA  
606  C CA  B ILE   A 23  ? 0.1390 0.1462 0.1199 -0.0093 0.0150  0.0121  23  ILE   A CA  
607  C C   A ILE   A 23  ? 0.1659 0.1559 0.1381 -0.0012 0.0498  0.0258  23  ILE   A C   
608  C C   B ILE   A 23  ? 0.1427 0.1561 0.1201 -0.0155 0.0187  -0.0023 23  ILE   A C   
609  O O   A ILE   A 23  ? 0.1744 0.1603 0.1376 0.0021  0.0385  0.0138  23  ILE   A O   
610  O O   B ILE   A 23  ? 0.1463 0.1555 0.1261 -0.0137 0.0231  0.0016  23  ILE   A O   
611  C CB  A ILE   A 23  ? 0.1723 0.1617 0.1415 -0.0014 0.0345  0.0198  23  ILE   A CB  
612  C CB  B ILE   A 23  ? 0.1303 0.1411 0.1091 -0.0081 0.0175  0.0137  23  ILE   A CB  
613  C CG1 A ILE   A 23  ? 0.1728 0.1586 0.1380 -0.0055 0.0378  0.0156  23  ILE   A CG1 
614  C CG1 B ILE   A 23  ? 0.1350 0.1466 0.1224 -0.0037 0.0072  0.0118  23  ILE   A CG1 
615  C CG2 A ILE   A 23  ? 0.1737 0.1635 0.1417 0.0031  0.0376  0.0181  23  ILE   A CG2 
616  C CG2 B ILE   A 23  ? 0.1283 0.1327 0.1159 -0.0060 0.0186  0.0174  23  ILE   A CG2 
617  C CD1 A ILE   A 23  ? 0.1742 0.1511 0.1519 -0.0075 0.0284  0.0068  23  ILE   A CD1 
618  C CD1 B ILE   A 23  ? 0.1327 0.1439 0.1402 0.0037  0.0055  0.0057  23  ILE   A CD1 
641  N N   A VAL   A 24  ? 0.1720 0.1563 0.1529 -0.0017 0.0467  0.0231  24  VAL   A N   
642  N N   B VAL   A 24  ? 0.1529 0.1636 0.1400 -0.0229 0.0118  -0.0149 24  VAL   A N   
643  C CA  A VAL   A 24  ? 0.1839 0.1701 0.1733 -0.0075 0.0462  0.0201  24  VAL   A CA  
644  C CA  B VAL   A 24  ? 0.1666 0.1728 0.1521 -0.0283 0.0063  -0.0088 24  VAL   A CA  
645  C C   A VAL   A 24  ? 0.1933 0.1875 0.1705 -0.0105 0.0525  0.0118  24  VAL   A C   
646  C C   B VAL   A 24  ? 0.1733 0.1821 0.1594 -0.0311 0.0132  -0.0273 24  VAL   A C   
647  O O   A VAL   A 24  ? 0.1995 0.1915 0.1671 -0.0076 0.0510  0.0112  24  VAL   A O   
648  O O   B VAL   A 24  ? 0.1735 0.1864 0.1654 -0.0256 0.0075  -0.0344 24  VAL   A O   
649  C CB  A VAL   A 24  ? 0.1852 0.1715 0.2006 -0.0024 0.0356  0.0309  24  VAL   A CB  
650  C CB  B VAL   A 24  ? 0.1762 0.1803 0.1820 -0.0352 0.0015  0.0106  24  VAL   A CB  
651  C CG1 A VAL   A 24  ? 0.1900 0.1757 0.2063 0.0018  0.0270  0.0268  24  VAL   A CG1 
652  C CG1 B VAL   A 24  ? 0.1868 0.1887 0.2031 -0.0366 -0.0184 0.0023  24  VAL   A CG1 
653  C CG2 A VAL   A 24  ? 0.1890 0.1728 0.2072 0.0021  0.0457  0.0445  24  VAL   A CG2 
654  C CG2 B VAL   A 24  ? 0.1827 0.1884 0.2013 -0.0261 0.0164  0.0255  24  VAL   A CG2 
673  N N   A GLU   A 25  ? 0.1979 0.2040 0.1706 -0.0183 0.0628  0.0022  25  GLU   A N   
674  N N   B GLU   A 25  ? 0.1796 0.1879 0.1661 -0.0294 0.0385  -0.0307 25  GLU   A N   
675  C CA  A GLU   A 25  ? 0.2115 0.2249 0.1801 -0.0169 0.0607  -0.0022 25  GLU   A CA  
676  C CA  B GLU   A 25  ? 0.1956 0.1996 0.1782 -0.0311 0.0604  -0.0288 25  GLU   A CA  
677  C C   A GLU   A 25  ? 0.1960 0.2252 0.1500 -0.0203 0.0663  -0.0039 25  GLU   A C   
678  C C   B GLU   A 25  ? 0.1901 0.1966 0.1396 -0.0297 0.0551  -0.0266 25  GLU   A C   
679  O O   A GLU   A 25  ? 0.1987 0.2275 0.1550 -0.0126 0.0649  -0.0037 25  GLU   A O   
680  O O   B GLU   A 25  ? 0.1940 0.2008 0.1376 -0.0262 0.0429  -0.0299 25  GLU   A O   
681  C CB  A GLU   A 25  ? 0.2386 0.2439 0.2160 -0.0176 0.0583  0.0024  25  GLU   A CB  
682  C CB  B GLU   A 25  ? 0.2189 0.2118 0.1996 -0.0335 0.0885  -0.0305 25  GLU   A CB  
683  C CG  A GLU   A 25  ? 0.2683 0.2621 0.2751 -0.0217 0.0479  0.0032  25  GLU   A CG  
684  C CG  B GLU   A 25  ? 0.2485 0.2305 0.2488 -0.0300 0.0894  -0.0338 25  GLU   A CG  
685  C CD  A GLU   A 25  ? 0.2911 0.2778 0.3295 -0.0261 0.0439  0.0058  25  GLU   A CD  
686  C CD  B GLU   A 25  ? 0.2719 0.2457 0.3034 -0.0322 0.0861  -0.0337 25  GLU   A CD  
687  O OE1 A GLU   A 25  ? 0.2980 0.2847 0.3440 -0.0262 0.0390  0.0021  25  GLU   A OE1 
688  O OE1 B GLU   A 25  ? 0.2792 0.2500 0.3167 -0.0333 0.0850  -0.0348 25  GLU   A OE1 
689  O OE2 A GLU   A 25  ? 0.3035 0.2845 0.3605 -0.0277 0.0380  0.0029  25  GLU   A OE2 
690  O OE2 B GLU   A 25  ? 0.2851 0.2509 0.3379 -0.0315 0.0836  -0.0297 25  GLU   A OE2 
703  N N   A GLU   A 26  ? 0.1836 0.2243 0.1496 -0.0327 0.0657  -0.0009 26  GLU   A N   
704  N N   B GLU   A 26  ? 0.1830 0.1884 0.1334 -0.0336 0.0508  -0.0240 26  GLU   A N   
705  C CA  A GLU   A 26  ? 0.1802 0.2263 0.1577 -0.0418 0.0633  0.0041  26  GLU   A CA  
706  C CA  B GLU   A 26  ? 0.1871 0.1853 0.1373 -0.0342 0.0410  -0.0156 26  GLU   A CA  
707  C C   A GLU   A 26  ? 0.1790 0.2210 0.1514 -0.0349 0.0660  0.0082  26  GLU   A C   
708  C C   B GLU   A 26  ? 0.1854 0.1869 0.1284 -0.0340 0.0328  -0.0145 26  GLU   A C   
709  O O   A GLU   A 26  ? 0.1849 0.2186 0.1545 -0.0349 0.0700  0.0138  26  GLU   A O   
710  O O   B GLU   A 26  ? 0.1915 0.1924 0.1443 -0.0288 0.0266  -0.0125 26  GLU   A O   
711  C CB  A GLU   A 26  ? 0.1833 0.2314 0.1702 -0.0509 0.0579  0.0109  26  GLU   A CB  
712  C CB  B GLU   A 26  ? 0.2002 0.1897 0.1566 -0.0391 0.0471  -0.0186 26  GLU   A CB  
713  C CG  A GLU   A 26  ? 0.1981 0.2421 0.2050 -0.0485 0.0519  0.0034  26  GLU   A CG  
714  C CG  B GLU   A 26  ? 0.2112 0.1923 0.1741 -0.0539 0.0645  -0.0158 26  GLU   A CG  
715  C CD  A GLU   A 26  ? 0.2106 0.2556 0.2363 -0.0462 0.0520  0.0035  26  GLU   A CD  
716  C CD  B GLU   A 26  ? 0.2262 0.1961 0.1821 -0.0702 0.0801  -0.0194 26  GLU   A CD  
717  O OE1 A GLU   A 26  ? 0.2157 0.2674 0.2504 -0.0407 0.0501  0.0082  26  GLU   A OE1 
718  O OE1 B GLU   A 26  ? 0.2284 0.2043 0.1745 -0.0732 0.0875  -0.0226 26  GLU   A OE1 
719  O OE2 A GLU   A 26  ? 0.2234 0.2641 0.2520 -0.0414 0.0496  0.0017  26  GLU   A OE2 
720  O OE2 B GLU   A 26  ? 0.2409 0.2076 0.1814 -0.0663 0.0919  -0.0179 26  GLU   A OE2 
733  N N   A ALA   A 27  ? 0.1749 0.2125 0.1540 -0.0338 0.0596  0.0067  27  ALA   A N   
734  N N   B ALA   A 27  ? 0.1776 0.1829 0.1301 -0.0424 0.0170  -0.0199 27  ALA   A N   
735  C CA  A ALA   A 27  ? 0.1879 0.2193 0.1486 -0.0342 0.0536  0.0182  27  ALA   A CA  
736  C CA  B ALA   A 27  ? 0.1828 0.1887 0.1320 -0.0427 0.0114  -0.0212 27  ALA   A CA  
737  C C   A ALA   A 27  ? 0.2121 0.2338 0.1561 -0.0374 0.0604  -0.0000 27  ALA   A C   
738  C C   B ALA   A 27  ? 0.2030 0.2029 0.1254 -0.0441 0.0118  -0.0354 27  ALA   A C   
739  O O   A ALA   A 27  ? 0.2169 0.2332 0.1542 -0.0424 0.0593  0.0001  27  ALA   A O   
740  O O   B ALA   A 27  ? 0.2097 0.2107 0.1281 -0.0463 -0.0025 -0.0252 27  ALA   A O   
741  C CB  A ALA   A 27  ? 0.1809 0.2154 0.1493 -0.0329 0.0443  0.0269  27  ALA   A CB  
742  C CB  B ALA   A 27  ? 0.1749 0.1856 0.1566 -0.0390 0.0092  -0.0119 27  ALA   A CB  
753  N N   A LYS   A 28  ? 0.2380 0.2534 0.1726 -0.0360 0.0485  -0.0108 28  LYS   A N   
754  N N   B LYS   A 28  ? 0.2258 0.2209 0.1474 -0.0437 0.0117  -0.0570 28  LYS   A N   
755  C CA  A LYS   A 28  ? 0.2678 0.2787 0.1974 -0.0322 0.0332  -0.0291 28  LYS   A CA  
756  C CA  B LYS   A 28  ? 0.2531 0.2497 0.1761 -0.0433 0.0196  -0.0631 28  LYS   A CA  
757  C C   A LYS   A 28  ? 0.2902 0.3010 0.1881 -0.0374 0.0353  -0.0290 28  LYS   A C   
758  C C   B LYS   A 28  ? 0.2805 0.2785 0.1703 -0.0448 0.0258  -0.0514 28  LYS   A C   
759  O O   A LYS   A 28  ? 0.2972 0.3092 0.2109 -0.0366 0.0192  -0.0219 28  LYS   A O   
760  O O   B LYS   A 28  ? 0.2914 0.2908 0.1994 -0.0429 0.0082  -0.0423 28  LYS   A O   
761  C CB  A LYS   A 28  ? 0.2757 0.2855 0.2253 -0.0218 0.0212  -0.0400 28  LYS   A CB  
762  C CB  B LYS   A 28  ? 0.2546 0.2545 0.1966 -0.0399 0.0251  -0.0716 28  LYS   A CB  
763  C CG  A LYS   A 28  ? 0.2844 0.2913 0.2607 -0.0145 0.0185  -0.0421 28  LYS   A CG  
764  C CG  B LYS   A 28  ? 0.2612 0.2642 0.2295 -0.0344 0.0242  -0.0755 28  LYS   A CG  
765  C CD  A LYS   A 28  ? 0.2939 0.2996 0.3049 -0.0107 0.0181  -0.0367 28  LYS   A CD  
766  C CD  B LYS   A 28  ? 0.2723 0.2781 0.2778 -0.0278 0.0237  -0.0712 28  LYS   A CD  
767  C CE  A LYS   A 28  ? 0.3005 0.3049 0.3379 -0.0093 0.0220  -0.0326 28  LYS   A CE  
768  C CE  B LYS   A 28  ? 0.2835 0.2897 0.3251 -0.0225 0.0231  -0.0699 28  LYS   A CE  
769  N NZ  A LYS   A 28  ? 0.3040 0.3073 0.3571 -0.0085 0.0270  -0.0322 28  LYS   A NZ  
770  N NZ  B LYS   A 28  ? 0.2919 0.2995 0.3578 -0.0179 0.0232  -0.0678 28  LYS   A NZ  
797  N N   A LYS   A 29  ? 0.3048 0.3172 0.1816 -0.0459 0.0559  -0.0241 29  LYS   A N   
798  N N   B LYS   A 29  ? 0.2939 0.2983 0.1606 -0.0516 0.0531  -0.0357 29  LYS   A N   
799  C CA  A LYS   A 29  ? 0.3242 0.3376 0.2072 -0.0523 0.0636  -0.0182 29  LYS   A CA  
800  C CA  B LYS   A 29  ? 0.3107 0.3191 0.1768 -0.0567 0.0679  -0.0243 29  LYS   A CA  
801  C C   A LYS   A 29  ? 0.3308 0.3359 0.1954 -0.0604 0.0593  -0.0137 29  LYS   A C   
802  C C   B LYS   A 29  ? 0.3129 0.3157 0.1516 -0.0650 0.0681  -0.0211 29  LYS   A C   
803  O O   A LYS   A 29  ? 0.3376 0.3439 0.2095 -0.0569 0.0543  -0.0105 29  LYS   A O   
804  O O   B LYS   A 29  ? 0.3195 0.3207 0.1635 -0.0561 0.0630  -0.0198 29  LYS   A O   
805  C CB  A LYS   A 29  ? 0.3360 0.3582 0.2584 -0.0474 0.0713  -0.0162 29  LYS   A CB  
806  C CB  B LYS   A 29  ? 0.3264 0.3456 0.2378 -0.0525 0.0757  -0.0180 29  LYS   A CB  
807  C CG  A LYS   A 29  ? 0.3495 0.3763 0.3224 -0.0422 0.0711  -0.0159 29  LYS   A CG  
808  C CG  B LYS   A 29  ? 0.3436 0.3678 0.3113 -0.0477 0.0734  -0.0149 29  LYS   A CG  
809  C CD  A LYS   A 29  ? 0.3622 0.3929 0.3873 -0.0370 0.0681  -0.0162 29  LYS   A CD  
810  C CD  B LYS   A 29  ? 0.3590 0.3870 0.3820 -0.0422 0.0706  -0.0138 29  LYS   A CD  
811  C CE  A LYS   A 29  ? 0.3711 0.4043 0.4310 -0.0327 0.0674  -0.0169 29  LYS   A CE  
812  C CE  B LYS   A 29  ? 0.3695 0.3997 0.4294 -0.0374 0.0698  -0.0135 29  LYS   A CE  
813  N NZ  A LYS   A 29  ? 0.3754 0.4110 0.4563 -0.0304 0.0656  -0.0178 29  LYS   A NZ  
814  N NZ  B LYS   A 29  ? 0.3746 0.4069 0.4571 -0.0348 0.0674  -0.0138 29  LYS   A NZ  
841  N N   A VAL   A 30  ? 0.3288 0.3241 0.1797 -0.0696 0.0620  -0.0068 30  VAL   A N   
842  N N   B VAL   A 30  ? 0.3031 0.3010 0.1319 -0.0793 0.0775  -0.0140 30  VAL   A N   
843  C CA  A VAL   A 30  ? 0.3293 0.3133 0.1878 -0.0767 0.0473  0.0081  30  VAL   A CA  
844  C CA  B VAL   A 30  ? 0.3025 0.2946 0.1481 -0.0928 0.0632  -0.0031 30  VAL   A CA  
845  C C   A VAL   A 30  ? 0.3345 0.3060 0.1716 -0.0759 0.0388  0.0120  30  VAL   A C   
846  C C   B VAL   A 30  ? 0.3074 0.2873 0.1264 -0.0927 0.0524  0.0095  30  VAL   A C   
847  O O   A VAL   A 30  ? 0.3375 0.3087 0.1746 -0.0764 0.0376  0.0155  30  VAL   A O   
848  O O   B VAL   A 30  ? 0.3106 0.2905 0.1325 -0.0913 0.0491  0.0133  30  VAL   A O   
849  C CB  A VAL   A 30  ? 0.3263 0.3094 0.2211 -0.0817 0.0366  0.0166  30  VAL   A CB  
850  C CB  B VAL   A 30  ? 0.2992 0.2965 0.2023 -0.0997 0.0461  -0.0044 30  VAL   A CB  
851  C CG1 A VAL   A 30  ? 0.3279 0.3081 0.2381 -0.0820 0.0281  0.0198  30  VAL   A CG1 
852  C CG1 B VAL   A 30  ? 0.3019 0.2982 0.2218 -0.1004 0.0340  -0.0037 30  VAL   A CG1 
853  C CG2 A VAL   A 30  ? 0.3244 0.3092 0.2379 -0.0849 0.0327  0.0163  30  VAL   A CG2 
854  C CG2 B VAL   A 30  ? 0.2982 0.3000 0.2287 -0.1020 0.0403  -0.0083 30  VAL   A CG2 
873  N N   A LYS   A 31  ? 0.3351 0.2961 0.1592 -0.0744 0.0292  0.0082  31  LYS   A N   
874  N N   B LYS   A 31  ? 0.3075 0.2783 0.1153 -0.0925 0.0431  0.0070  31  LYS   A N   
875  C CA  A LYS   A 31  ? 0.3416 0.2934 0.1716 -0.0666 0.0133  0.0065  31  LYS   A CA  
876  C CA  B LYS   A 31  ? 0.3206 0.2823 0.1327 -0.0798 0.0253  0.0057  31  LYS   A CA  
877  C C   A LYS   A 31  ? 0.3199 0.2710 0.1323 -0.0650 0.0066  0.0268  31  LYS   A C   
878  C C   B LYS   A 31  ? 0.3051 0.2658 0.1091 -0.0732 0.0154  0.0277  31  LYS   A C   
879  O O   A LYS   A 31  ? 0.3233 0.2731 0.1325 -0.0632 -0.0083 0.0402  31  LYS   A O   
880  O O   B LYS   A 31  ? 0.3017 0.2704 0.1222 -0.0745 0.0026  0.0358  31  LYS   A O   
881  C CB  A LYS   A 31  ? 0.3705 0.3151 0.2606 -0.0573 -0.0006 -0.0041 31  LYS   A CB  
882  C CB  B LYS   A 31  ? 0.3528 0.3061 0.2323 -0.0670 0.0103  -0.0027 31  LYS   A CB  
883  C CG  A LYS   A 31  ? 0.3991 0.3367 0.3634 -0.0459 -0.0150 -0.0099 31  LYS   A CG  
884  C CG  B LYS   A 31  ? 0.3864 0.3311 0.3486 -0.0515 -0.0060 -0.0062 31  LYS   A CG  
885  C CD  A LYS   A 31  ? 0.4215 0.3544 0.4441 -0.0362 -0.0257 -0.0139 31  LYS   A CD  
886  C CD  B LYS   A 31  ? 0.4130 0.3515 0.4352 -0.0382 -0.0176 -0.0087 31  LYS   A CD  
887  C CE  A LYS   A 31  ? 0.4368 0.3663 0.4953 -0.0285 -0.0338 -0.0176 31  LYS   A CE  
888  C CE  B LYS   A 31  ? 0.4310 0.3653 0.4879 -0.0277 -0.0264 -0.0122 31  LYS   A CE  
889  N NZ  A LYS   A 31  ? 0.4451 0.3715 0.5249 -0.0239 -0.0382 -0.0204 31  LYS   A NZ  
890  N NZ  B LYS   A 31  ? 0.4404 0.3720 0.5165 -0.0217 -0.0316 -0.0147 31  LYS   A NZ  
917  N N   . PRO   A 32  ? 0.2892 0.2445 0.1046 -0.0719 0.0148  0.0176  32  PRO   A N   
918  C CA  . PRO   A 32  ? 0.2751 0.2241 0.1300 -0.0654 0.0107  0.0253  32  PRO   A CA  
919  C C   . PRO   A 32  ? 0.2654 0.2209 0.1347 -0.0476 0.0015  0.0311  32  PRO   A C   
920  O O   . PRO   A 32  ? 0.2604 0.2090 0.1484 -0.0447 -0.0148 0.0333  32  PRO   A O   
921  C CB  . PRO   A 32  ? 0.2673 0.2258 0.1478 -0.0695 0.0102  0.0184  32  PRO   A CB  
922  C CG  . PRO   A 32  ? 0.2668 0.2272 0.1071 -0.0676 0.0061  0.0065  32  PRO   A CG  
923  C CD  . PRO   A 32  ? 0.2748 0.2336 0.0913 -0.0689 0.0122  0.0137  32  PRO   A CD  
931  N N   A THR   A 33  ? 0.2650 0.2217 0.1392 -0.0426 0.0092  0.0316  33  THR   A N   
932  N N   B THR   A 33  ? 0.2651 0.2230 0.1395 -0.0425 0.0101  0.0316  33  THR   A N   
933  C CA  A THR   A 33  ? 0.2593 0.2227 0.1504 -0.0365 0.0006  0.0310  33  THR   A CA  
934  C CA  B THR   A 33  ? 0.2592 0.2253 0.1481 -0.0363 0.0012  0.0313  33  THR   A CA  
935  C C   A THR   A 33  ? 0.2351 0.2067 0.1312 -0.0415 -0.0026 0.0304  33  THR   A C   
936  C C   B THR   A 33  ? 0.2340 0.2090 0.1286 -0.0402 -0.0023 0.0276  33  THR   A C   
937  O O   A THR   A 33  ? 0.2349 0.2051 0.1391 -0.0427 -0.0152 0.0327  33  THR   A O   
938  O O   B THR   A 33  ? 0.2318 0.2092 0.1343 -0.0392 -0.0158 0.0254  33  THR   A O   
939  C CB  A THR   A 33  ? 0.2773 0.2377 0.1742 -0.0272 -0.0038 0.0459  33  THR   A CB  
940  C CB  B THR   A 33  ? 0.2780 0.2417 0.1687 -0.0277 -0.0037 0.0506  33  THR   A CB  
941  O OG1 A THR   A 33  ? 0.2902 0.2476 0.1940 -0.0198 -0.0034 0.0498  33  THR   A OG1 
942  O OG1 B THR   A 33  ? 0.2917 0.2530 0.1917 -0.0208 0.0002  0.0602  33  THR   A OG1 
943  C CG2 A THR   A 33  ? 0.2800 0.2418 0.1847 -0.0231 -0.0080 0.0471  33  THR   A CG2 
944  C CG2 B THR   A 33  ? 0.2811 0.2463 0.1811 -0.0231 -0.0100 0.0509  33  THR   A CG2 
959  N N   . VAL   A 34  ? 0.2139 0.1930 0.1220 -0.0425 -0.0038 0.0294  34  VAL   A N   
960  C CA  . VAL   A 34  ? 0.1896 0.1719 0.1088 -0.0381 0.0065  0.0284  34  VAL   A CA  
961  C C   . VAL   A 34  ? 0.1768 0.1633 0.1205 -0.0348 0.0120  0.0204  34  VAL   A C   
962  O O   . VAL   A 34  ? 0.1787 0.1640 0.1391 -0.0450 0.0086  0.0268  34  VAL   A O   
963  C CB  . VAL   A 34  ? 0.1913 0.1668 0.1364 -0.0362 0.0126  0.0123  34  VAL   A CB  
964  C CG1 . VAL   A 34  ? 0.1990 0.1733 0.1408 -0.0305 0.0194  0.0006  34  VAL   A CG1 
965  C CG2 . VAL   A 34  ? 0.1992 0.1816 0.1770 -0.0242 0.0028  0.0137  34  VAL   A CG2 
976  N N   . VAL   A 35  ? 0.1617 0.1538 0.1151 -0.0361 0.0074  0.0142  35  VAL   A N   
977  C CA  . VAL   A 35  ? 0.1522 0.1533 0.1216 -0.0337 0.0149  0.0052  35  VAL   A CA  
978  C C   . VAL   A 35  ? 0.1409 0.1377 0.1171 -0.0262 0.0138  0.0023  35  VAL   A C   
979  O O   . VAL   A 35  ? 0.1336 0.1477 0.1291 -0.0291 0.0247  0.0015  35  VAL   A O   
980  C CB  . VAL   A 35  ? 0.1612 0.1541 0.1253 -0.0244 0.0301  -0.0023 35  VAL   A CB  
981  C CG1 . VAL   A 35  ? 0.1693 0.1514 0.1397 -0.0181 0.0231  -0.0071 35  VAL   A CG1 
982  C CG2 . VAL   A 35  ? 0.1584 0.1544 0.1466 -0.0189 0.0325  -0.0070 35  VAL   A CG2 
992  N N   . VAL   A 36  ? 0.1285 0.1322 0.1207 -0.0257 0.0202  0.0098  36  VAL   A N   
993  C CA  . VAL   A 36  ? 0.1242 0.1207 0.1210 -0.0169 0.0155  0.0024  36  VAL   A CA  
994  C C   . VAL   A 36  ? 0.1172 0.1195 0.1327 -0.0183 0.0194  -0.0029 36  VAL   A C   
995  O O   . VAL   A 36  ? 0.1260 0.1199 0.1514 -0.0135 0.0302  -0.0008 36  VAL   A O   
996  C CB  . VAL   A 36  ? 0.1211 0.1161 0.1327 -0.0173 0.0131  0.0018  36  VAL   A CB  
997  C CG1 . VAL   A 36  ? 0.1310 0.1205 0.1289 -0.0176 0.0202  -0.0074 36  VAL   A CG1 
998  C CG2 . VAL   A 36  ? 0.1334 0.1189 0.1512 -0.0181 0.0152  0.0033  36  VAL   A CG2 
1008 N N   . ASN   A 37  ? 0.1108 0.1140 0.1208 -0.0079 0.0099  0.0026  37  ASN   A N   
1009 C CA  . ASN   A 37  ? 0.1114 0.1115 0.1153 -0.0004 0.0206  0.0020  37  ASN   A CA  
1010 C C   . ASN   A 37  ? 0.1032 0.1152 0.1228 -0.0068 0.0159  0.0074  37  ASN   A C   
1011 O O   . ASN   A 37  ? 0.1167 0.1214 0.1242 0.0045  0.0148  -0.0027 37  ASN   A O   
1012 C CB  . ASN   A 37  ? 0.1104 0.1126 0.1163 -0.0045 0.0076  0.0026  37  ASN   A CB  
1013 C CG  . ASN   A 37  ? 0.1086 0.1073 0.1227 0.0003  0.0083  0.0029  37  ASN   A CG  
1014 O OD1 . ASN   A 37  ? 0.1097 0.1139 0.1568 -0.0009 0.0117  0.0090  37  ASN   A OD1 
1015 N ND2 . ASN   A 37  ? 0.1087 0.1134 0.1334 -0.0045 0.0047  0.0167  37  ASN   A ND2 
1022 N N   A ALA   A 38  ? 0.1097 0.1173 0.1259 -0.0033 0.0098  -0.0057 38  ALA   A N   
1023 N N   B ALA   A 38  ? 0.1123 0.1166 0.1294 -0.0047 0.0085  -0.0018 38  ALA   A N   
1024 C CA  A ALA   A 38  ? 0.1122 0.1220 0.1209 0.0011  0.0049  -0.0152 38  ALA   A CA  
1025 C CA  B ALA   A 38  ? 0.1174 0.1218 0.1271 -0.0021 0.0008  -0.0060 38  ALA   A CA  
1026 C C   A ALA   A 38  ? 0.1153 0.1209 0.1270 0.0042  -0.0008 -0.0097 38  ALA   A C   
1027 C C   B ALA   A 38  ? 0.1191 0.1192 0.1288 0.0023  -0.0043 -0.0066 38  ALA   A C   
1028 O O   A ALA   A 38  ? 0.1165 0.1229 0.1360 0.0084  -0.0022 -0.0052 38  ALA   A O   
1029 O O   B ALA   A 38  ? 0.1229 0.1196 0.1375 0.0037  -0.0116 -0.0040 38  ALA   A O   
1030 C CB  A ALA   A 38  ? 0.1163 0.1481 0.1283 -0.0089 -0.0049 -0.0230 38  ALA   A CB  
1031 C CB  B ALA   A 38  ? 0.1238 0.1489 0.1391 -0.0136 -0.0106 -0.0109 38  ALA   A CB  
1042 N N   . ALA   A 39  ? 0.1093 0.1175 0.1262 0.0066  0.0039  -0.0037 39  ALA   A N   
1043 C CA  . ALA   A 39  ? 0.1167 0.1126 0.1197 0.0007  0.0025  -0.0056 39  ALA   A CA  
1044 C C   . ALA   A 39  ? 0.1167 0.1099 0.1227 0.0030  -0.0014 -0.0014 39  ALA   A C   
1045 O O   . ALA   A 39  ? 0.1300 0.1163 0.1146 -0.0020 -0.0001 -0.0013 39  ALA   A O   
1046 C CB  . ALA   A 39  ? 0.1202 0.1343 0.1269 -0.0041 -0.0014 -0.0023 39  ALA   A CB  
1053 N N   . ASN   A 40  ? 0.1270 0.1137 0.1199 -0.0002 0.0128  -0.0028 40  ASN   A N   
1054 C CA  . ASN   A 40  ? 0.1367 0.1153 0.1309 0.0040  0.0049  -0.0022 40  ASN   A CA  
1055 C C   . ASN   A 40  ? 0.1364 0.1082 0.1157 -0.0007 0.0169  0.0124  40  ASN   A C   
1056 O O   . ASN   A 40  ? 0.1326 0.1134 0.1194 -0.0017 0.0162  0.0129  40  ASN   A O   
1057 C CB  . ASN   A 40  ? 0.1467 0.1225 0.1334 0.0060  -0.0058 0.0048  40  ASN   A CB  
1058 C CG  . ASN   A 40  ? 0.1530 0.1225 0.1581 0.0049  -0.0115 0.0121  40  ASN   A CG  
1059 O OD1 . ASN   A 40  ? 0.1612 0.1247 0.1915 0.0040  -0.0141 0.0022  40  ASN   A OD1 
1060 N ND2 . ASN   A 40  ? 0.1506 0.1306 0.1878 0.0084  -0.0076 -0.0026 40  ASN   A ND2 
1067 N N   . VAL   A 41  ? 0.1507 0.1143 0.1191 0.0013  0.0198  0.0155  41  VAL   A N   
1068 C CA  . VAL   A 41  ? 0.1519 0.1186 0.1404 0.0010  0.0326  0.0022  41  VAL   A CA  
1069 C C   . VAL   A 41  ? 0.1472 0.1168 0.1493 0.0013  0.0363  0.0106  41  VAL   A C   
1070 O O   . VAL   A 41  ? 0.1452 0.1136 0.1639 0.0057  0.0342  0.0006  41  VAL   A O   
1071 C CB  . VAL   A 41  ? 0.1627 0.1317 0.1472 -0.0084 0.0392  0.0019  41  VAL   A CB  
1072 C CG1 . VAL   A 41  ? 0.1726 0.1352 0.1445 -0.0013 0.0369  -0.0063 41  VAL   A CG1 
1073 C CG2 . VAL   A 41  ? 0.1907 0.1506 0.1452 -0.0159 0.0380  0.0029  41  VAL   A CG2 
1083 N N   . TYR   A 42  ? 0.1360 0.1096 0.1605 0.0004  0.0293  0.0181  42  TYR   A N   
1084 C CA  . TYR   A 42  ? 0.1372 0.1089 0.1488 0.0006  0.0262  0.0127  42  TYR   A CA  
1085 C C   . TYR   A 42  ? 0.1275 0.1115 0.1553 0.0012  0.0197  0.0170  42  TYR   A C   
1086 O O   . TYR   A 42  ? 0.1266 0.1144 0.1753 -0.0113 0.0159  -0.0004 42  TYR   A O   
1087 C CB  . TYR   A 42  ? 0.1593 0.1206 0.1528 -0.0064 0.0247  0.0235  42  TYR   A CB  
1088 C CG  . TYR   A 42  ? 0.1854 0.1333 0.1569 -0.0042 0.0186  0.0291  42  TYR   A CG  
1089 C CD1 . TYR   A 42  ? 0.1951 0.1451 0.1600 -0.0094 0.0277  0.0281  42  TYR   A CD1 
1090 C CD2 . TYR   A 42  ? 0.2029 0.1576 0.1732 -0.0013 0.0218  0.0131  42  TYR   A CD2 
1091 C CE1 . TYR   A 42  ? 0.2045 0.1594 0.1473 -0.0094 0.0342  0.0279  42  TYR   A CE1 
1092 C CE2 . TYR   A 42  ? 0.2121 0.1737 0.1716 -0.0130 0.0249  0.0137  42  TYR   A CE2 
1093 C CZ  . TYR   A 42  ? 0.2218 0.1735 0.1562 -0.0176 0.0372  0.0190  42  TYR   A CZ  
1094 O OH  . TYR   A 42  ? 0.2325 0.1956 0.1854 -0.0387 0.0386  0.0115  42  TYR   A OH  
1104 N N   . LEU   A 43  ? 0.1254 0.1116 0.1450 -0.0006 0.0127  0.0048  43  LEU   A N   
1105 C CA  . LEU   A 43  ? 0.1142 0.1115 0.1501 -0.0054 0.0104  0.0075  43  LEU   A CA  
1106 C C   . LEU   A 43  ? 0.1144 0.1134 0.1421 0.0020  0.0088  0.0023  43  LEU   A C   
1107 O O   . LEU   A 43  ? 0.1365 0.1161 0.1525 0.0045  -0.0052 -0.0046 43  LEU   A O   
1108 C CB  . LEU   A 43  ? 0.1194 0.1089 0.1568 -0.0058 0.0084  0.0008  43  LEU   A CB  
1109 C CG  . LEU   A 43  ? 0.1266 0.1085 0.1553 -0.0021 0.0088  0.0092  43  LEU   A CG  
1110 C CD1 . LEU   A 43  ? 0.1340 0.1223 0.1772 -0.0005 0.0018  0.0173  43  LEU   A CD1 
1111 C CD2 . LEU   A 43  ? 0.1439 0.1070 0.1551 -0.0035 -0.0002 0.0020  43  LEU   A CD2 
1123 N N   . LYS   A 44  ? 0.1272 0.1144 0.1374 0.0001  0.0035  0.0057  44  LYS   A N   
1124 C CA  . LYS   A 44  ? 0.1380 0.1165 0.1467 -0.0006 0.0078  0.0111  44  LYS   A CA  
1125 C C   . LYS   A 44  ? 0.1271 0.1136 0.1364 0.0056  -0.0061 0.0041  44  LYS   A C   
1126 O O   . LYS   A 44  ? 0.1363 0.1273 0.1462 0.0018  -0.0090 -0.0104 44  LYS   A O   
1127 C CB  . LYS   A 44  ? 0.1670 0.1373 0.1748 0.0072  0.0200  0.0309  44  LYS   A CB  
1128 C CG  . LYS   A 44  ? 0.2010 0.1684 0.2394 0.0003  0.0431  0.0417  44  LYS   A CG  
1129 C CD  . LYS   A 44  ? 0.2429 0.2250 0.3527 -0.0089 0.0360  0.0349  44  LYS   A CD  
1130 C CE  . LYS   A 44  ? 0.2621 0.2572 0.4226 -0.0126 0.0298  0.0315  44  LYS   A CE  
1131 N NZ  . LYS   A 44  ? 0.2730 0.2837 0.4561 -0.0133 0.0282  0.0267  44  LYS   A NZ  
1145 N N   A HIS   A 45  ? 0.1154 0.1025 0.1389 0.0064  -0.0043 0.0011  45  HIS   A N   
1146 N N   B HIS   A 45  ? 0.1208 0.1102 0.1484 0.0045  -0.0113 0.0019  45  HIS   A N   
1147 C CA  A HIS   A 45  ? 0.1155 0.1040 0.1300 0.0038  -0.0008 0.0063  45  HIS   A CA  
1148 C CA  B HIS   A 45  ? 0.1262 0.1172 0.1485 0.0025  -0.0136 0.0069  45  HIS   A CA  
1149 C C   A HIS   A 45  ? 0.1240 0.1163 0.1397 0.0061  0.0086  0.0016  45  HIS   A C   
1150 C C   B HIS   A 45  ? 0.1375 0.1273 0.1651 0.0076  -0.0117 0.0086  45  HIS   A C   
1151 O O   A HIS   A 45  ? 0.1348 0.1072 0.1409 0.0046  0.0196  0.0026  45  HIS   A O   
1152 O O   B HIS   A 45  ? 0.1575 0.1395 0.1791 0.0225  -0.0112 0.0116  45  HIS   A O   
1153 C CB  A HIS   A 45  ? 0.1129 0.1032 0.1319 -0.0027 0.0045  0.0037  45  HIS   A CB  
1154 C CB  B HIS   A 45  ? 0.1256 0.1218 0.1479 -0.0042 -0.0056 -0.0003 45  HIS   A CB  
1155 C CG  A HIS   A 45  ? 0.1115 0.0931 0.1245 -0.0030 -0.0007 0.0115  45  HIS   A CG  
1156 C CG  B HIS   A 45  ? 0.1171 0.1199 0.1296 -0.0057 0.0008  -0.0011 45  HIS   A CG  
1157 N ND1 A HIS   A 45  ? 0.1099 0.1052 0.1273 -0.0060 -0.0088 0.0083  45  HIS   A ND1 
1158 N ND1 B HIS   A 45  ? 0.1123 0.1260 0.1481 -0.0030 0.0027  -0.0000 45  HIS   A ND1 
1159 C CD2 A HIS   A 45  ? 0.1185 0.1021 0.1412 -0.0066 -0.0043 0.0141  45  HIS   A CD2 
1160 C CD2 B HIS   A 45  ? 0.1084 0.1202 0.1237 -0.0035 -0.0005 -0.0002 45  HIS   A CD2 
1161 C CE1 A HIS   A 45  ? 0.1135 0.1130 0.1272 -0.0064 -0.0076 0.0174  45  HIS   A CE1 
1162 C CE1 B HIS   A 45  ? 0.1057 0.1184 0.1303 -0.0064 0.0043  -0.0067 45  HIS   A CE1 
1163 N NE2 A HIS   A 45  ? 0.1219 0.1141 0.1371 -0.0010 0.0016  0.0213  45  HIS   A NE2 
1164 N NE2 B HIS   A 45  ? 0.1035 0.1185 0.1114 -0.0016 -0.0002 -0.0030 45  HIS   A NE2 
1179 N N   A GLY   A 46  ? 0.1284 0.1282 0.1550 0.0103  -0.0051 0.0073  46  GLY   A N   
1180 N N   B GLY   A 46  ? 0.1311 0.1162 0.1690 -0.0033 -0.0179 0.0150  46  GLY   A N   
1181 C CA  A GLY   A 46  ? 0.1306 0.1350 0.1625 0.0082  -0.0129 0.0128  46  GLY   A CA  
1182 C CA  B GLY   A 46  ? 0.1340 0.1204 0.1746 -0.0022 -0.0197 0.0173  46  GLY   A CA  
1183 C C   A GLY   A 46  ? 0.1316 0.1383 0.1727 0.0204  -0.0214 0.0201  46  GLY   A C   
1184 C C   B GLY   A 46  ? 0.1333 0.1254 0.1881 0.0015  -0.0220 0.0188  46  GLY   A C   
1185 O O   A GLY   A 46  ? 0.1416 0.1497 0.2050 0.0262  -0.0261 0.0065  46  GLY   A O   
1186 O O   B GLY   A 46  ? 0.1434 0.1358 0.2194 0.0036  -0.0324 0.0005  46  GLY   A O   
1193 N N   A GLY   A 47  ? 0.1230 0.1314 0.1598 0.0210  -0.0144 0.0228  47  GLY   A N   
1194 N N   B GLY   A 47  ? 0.1367 0.1294 0.1783 0.0006  -0.0102 0.0202  47  GLY   A N   
1195 C CA  A GLY   A 47  ? 0.1300 0.1362 0.1593 0.0197  -0.0162 0.0164  47  GLY   A CA  
1196 C CA  B GLY   A 47  ? 0.1320 0.1362 0.1755 -0.0035 -0.0113 0.0219  47  GLY   A CA  
1197 C C   A GLY   A 47  ? 0.1247 0.1341 0.1450 0.0172  -0.0146 -0.0004 47  GLY   A C   
1198 C C   B GLY   A 47  ? 0.1194 0.1313 0.1515 0.0071  -0.0048 0.0186  47  GLY   A C   
1199 O O   A GLY   A 47  ? 0.1248 0.1291 0.1479 0.0136  -0.0136 0.0120  47  GLY   A O   
1200 O O   B GLY   A 47  ? 0.1118 0.1308 0.1493 0.0135  -0.0087 0.0262  47  GLY   A O   
1207 N N   A GLY   A 48  ? 0.1248 0.1392 0.1389 0.0204  -0.0146 -0.0026 48  GLY   A N   
1208 N N   B GLY   A 48  ? 0.1180 0.1306 0.1467 0.0111  0.0039  0.0194  48  GLY   A N   
1209 C CA  A GLY   A 48  ? 0.1118 0.1380 0.1372 0.0132  -0.0073 -0.0019 48  GLY   A CA  
1210 C CA  B GLY   A 48  ? 0.1178 0.1181 0.1297 0.0055  0.0029  0.0106  48  GLY   A CA  
1211 C C   A GLY   A 48  ? 0.1151 0.1332 0.1176 0.0095  0.0036  0.0003  48  GLY   A C   
1212 C C   B GLY   A 48  ? 0.1187 0.1138 0.1351 0.0025  0.0036  0.0085  48  GLY   A C   
1213 O O   A GLY   A 48  ? 0.1327 0.1325 0.1110 0.0102  -0.0119 -0.0048 48  GLY   A O   
1214 O O   B GLY   A 48  ? 0.1280 0.1152 0.1315 0.0031  0.0092  -0.0015 48  GLY   A O   
1221 N N   A VAL   A 49  ? 0.1137 0.1292 0.1275 0.0033  0.0011  0.0032  49  VAL   A N   
1222 N N   B VAL   A 49  ? 0.1091 0.1080 0.1029 0.0001  -0.0107 -0.0034 49  VAL   A N   
1223 C CA  A VAL   A 49  ? 0.1219 0.1273 0.1352 -0.0006 0.0011  0.0103  49  VAL   A CA  
1224 C CA  B VAL   A 49  ? 0.1136 0.1102 0.1024 -0.0016 -0.0076 -0.0013 49  VAL   A CA  
1225 C C   A VAL   A 49  ? 0.1173 0.1195 0.1214 0.0028  0.0033  0.0101  49  VAL   A C   
1226 C C   B VAL   A 49  ? 0.1076 0.1080 0.1176 -0.0033 -0.0022 -0.0109 49  VAL   A C   
1227 O O   A VAL   A 49  ? 0.1212 0.1240 0.1206 0.0015  0.0045  -0.0012 49  VAL   A O   
1228 O O   B VAL   A 49  ? 0.1089 0.1129 0.1279 -0.0103 0.0059  -0.0102 49  VAL   A O   
1229 C CB  A VAL   A 49  ? 0.1295 0.1226 0.1395 -0.0087 0.0021  0.0061  49  VAL   A CB  
1230 C CB  B VAL   A 49  ? 0.1123 0.1133 0.1299 -0.0057 -0.0096 0.0014  49  VAL   A CB  
1231 C CG1 A VAL   A 49  ? 0.1359 0.1242 0.1463 -0.0130 0.0101  0.0018  49  VAL   A CG1 
1232 C CG1 B VAL   A 49  ? 0.1090 0.1166 0.1450 0.0034  -0.0122 0.0081  49  VAL   A CG1 
1233 C CG2 A VAL   A 49  ? 0.1399 0.1259 0.1396 -0.0179 0.0021  0.0057  49  VAL   A CG2 
1234 C CG2 B VAL   A 49  ? 0.1274 0.1212 0.1478 -0.0133 -0.0228 0.0043  49  VAL   A CG2 
1253 N N   A ALA   A 50  ? 0.1109 0.1224 0.1267 0.0011  -0.0018 0.0066  50  ALA   A N   
1254 N N   B ALA   A 50  ? 0.1124 0.1061 0.1176 -0.0024 -0.0001 -0.0077 50  ALA   A N   
1255 C CA  A ALA   A 50  ? 0.1091 0.1228 0.1329 -0.0008 -0.0022 0.0088  50  ALA   A CA  
1256 C CA  B ALA   A 50  ? 0.1041 0.0994 0.1170 -0.0010 0.0016  -0.0041 50  ALA   A CA  
1257 C C   A ALA   A 50  ? 0.1064 0.1224 0.1162 -0.0050 0.0019  0.0044  50  ALA   A C   
1258 C C   B ALA   A 50  ? 0.1031 0.1037 0.1141 0.0002  0.0022  -0.0083 50  ALA   A C   
1259 O O   A ALA   A 50  ? 0.1068 0.1237 0.1098 -0.0045 -0.0069 0.0087  50  ALA   A O   
1260 O O   B ALA   A 50  ? 0.1077 0.1159 0.1068 0.0016  0.0052  -0.0167 50  ALA   A O   
1261 C CB  A ALA   A 50  ? 0.1026 0.1306 0.1378 -0.0059 0.0062  -0.0089 50  ALA   A CB  
1262 C CB  B ALA   A 50  ? 0.1044 0.0974 0.1221 0.0002  -0.0015 -0.0001 50  ALA   A CB  
1273 N N   A GLY   A 51  ? 0.1144 0.1234 0.1171 0.0021  -0.0076 0.0002  51  GLY   A N   
1274 N N   B GLY   A 51  ? 0.1097 0.1016 0.1395 0.0033  -0.0042 -0.0105 51  GLY   A N   
1275 C CA  A GLY   A 51  ? 0.1191 0.1160 0.1053 0.0063  -0.0108 0.0063  51  GLY   A CA  
1276 C CA  B GLY   A 51  ? 0.1237 0.1010 0.1423 -0.0013 -0.0051 -0.0059 51  GLY   A CA  
1277 C C   A GLY   A 51  ? 0.1116 0.1111 0.0975 0.0010  0.0009  0.0013  51  GLY   A C   
1278 C C   B GLY   A 51  ? 0.1240 0.1109 0.1387 0.0029  0.0010  0.0016  51  GLY   A C   
1279 O O   A GLY   A 51  ? 0.1121 0.1109 0.1057 -0.0037 0.0048  0.0067  51  GLY   A O   
1280 O O   B GLY   A 51  ? 0.1299 0.1237 0.1359 0.0018  0.0015  0.0023  51  GLY   A O   
1287 N N   A ALA   A 52  ? 0.1128 0.1150 0.0997 0.0027  -0.0019 -0.0039 52  ALA   A N   
1288 N N   B ALA   A 52  ? 0.1218 0.1140 0.1423 -0.0005 0.0050  -0.0008 52  ALA   A N   
1289 C CA  A ALA   A 52  ? 0.1117 0.1200 0.1068 0.0004  -0.0074 0.0109  52  ALA   A CA  
1290 C CA  B ALA   A 52  ? 0.1142 0.1177 0.1460 0.0002  0.0080  0.0093  52  ALA   A CA  
1291 C C   A ALA   A 52  ? 0.1116 0.1242 0.1134 -0.0052 0.0037  0.0130  52  ALA   A C   
1292 C C   B ALA   A 52  ? 0.1090 0.1171 0.1315 -0.0061 0.0077  -0.0044 52  ALA   A C   
1293 O O   A ALA   A 52  ? 0.1242 0.1342 0.1192 -0.0002 -0.0113 0.0104  52  ALA   A O   
1294 O O   B ALA   A 52  ? 0.1160 0.1181 0.1430 -0.0040 0.0069  -0.0073 52  ALA   A O   
1295 C CB  A ALA   A 52  ? 0.1234 0.1238 0.1123 -0.0012 -0.0143 0.0205  52  ALA   A CB  
1296 C CB  B ALA   A 52  ? 0.1185 0.1272 0.1685 0.0057  -0.0010 0.0120  52  ALA   A CB  
1307 N N   A LEU   A 53  ? 0.1090 0.1282 0.1204 -0.0031 0.0004  0.0126  53  LEU   A N   
1308 N N   B LEU   A 53  ? 0.1042 0.1194 0.1277 -0.0035 0.0116  -0.0023 53  LEU   A N   
1309 C CA  A LEU   A 53  ? 0.1154 0.1357 0.1191 -0.0014 0.0010  0.0072  53  LEU   A CA  
1310 C CA  B LEU   A 53  ? 0.1104 0.1209 0.1103 -0.0028 0.0077  -0.0089 53  LEU   A CA  
1311 C C   A LEU   A 53  ? 0.1171 0.1455 0.1048 0.0096  0.0022  0.0087  53  LEU   A C   
1312 C C   B LEU   A 53  ? 0.1202 0.1239 0.1209 -0.0033 0.0063  -0.0188 53  LEU   A C   
1313 O O   A LEU   A 53  ? 0.1330 0.1549 0.0990 0.0006  0.0029  0.0086  53  LEU   A O   
1314 O O   B LEU   A 53  ? 0.1309 0.1346 0.1439 -0.0164 0.0028  -0.0176 53  LEU   A O   
1315 C CB  A LEU   A 53  ? 0.1216 0.1367 0.1483 -0.0027 -0.0028 0.0078  53  LEU   A CB  
1316 C CB  B LEU   A 53  ? 0.1060 0.1217 0.1041 -0.0030 -0.0021 -0.0081 53  LEU   A CB  
1317 C CG  A LEU   A 53  ? 0.1222 0.1320 0.1541 -0.0012 0.0030  0.0104  53  LEU   A CG  
1318 C CG  B LEU   A 53  ? 0.1148 0.1254 0.1231 -0.0039 -0.0014 -0.0062 53  LEU   A CG  
1319 C CD1 A LEU   A 53  ? 0.1191 0.1386 0.1563 0.0026  -0.0047 0.0145  53  LEU   A CD1 
1320 C CD1 B LEU   A 53  ? 0.1252 0.1352 0.1204 0.0001  -0.0014 -0.0059 53  LEU   A CD1 
1321 C CD2 A LEU   A 53  ? 0.1266 0.1393 0.1633 -0.0100 0.0029  0.0190  53  LEU   A CD2 
1322 C CD2 B LEU   A 53  ? 0.1253 0.1320 0.1342 -0.0033 0.0012  -0.0125 53  LEU   A CD2 
1345 N N   A ASN   A 54  ? 0.1117 0.1363 0.1031 0.0133  -0.0055 0.0104  54  ASN   A N   
1346 N N   B ASN   A 54  ? 0.1204 0.1081 0.1377 -0.0125 0.0125  -0.0231 54  ASN   A N   
1347 C CA  A ASN   A 54  ? 0.1081 0.1362 0.1173 0.0133  -0.0080 0.0169  54  ASN   A CA  
1348 C CA  B ASN   A 54  ? 0.1214 0.1073 0.1481 -0.0175 0.0085  -0.0215 54  ASN   A CA  
1349 C C   A ASN   A 54  ? 0.1113 0.1377 0.1413 0.0059  0.0029  0.0118  54  ASN   A C   
1350 C C   B ASN   A 54  ? 0.1239 0.1152 0.1514 -0.0177 0.0046  -0.0201 54  ASN   A C   
1351 O O   A ASN   A 54  ? 0.1153 0.1436 0.1420 0.0024  -0.0004 0.0069  54  ASN   A O   
1352 O O   B ASN   A 54  ? 0.1221 0.1156 0.1202 -0.0155 0.0093  -0.0232 54  ASN   A O   
1353 C CB  A ASN   A 54  ? 0.0997 0.1416 0.1281 0.0154  -0.0077 0.0123  54  ASN   A CB  
1354 C CB  B ASN   A 54  ? 0.1163 0.1089 0.1541 -0.0197 0.0160  -0.0237 54  ASN   A CB  
1355 C CG  A ASN   A 54  ? 0.1033 0.1433 0.1436 0.0154  -0.0128 0.0016  54  ASN   A CG  
1356 C CG  B ASN   A 54  ? 0.1170 0.1055 0.1540 -0.0155 0.0106  -0.0142 54  ASN   A CG  
1357 O OD1 A ASN   A 54  ? 0.1041 0.1476 0.1480 0.0160  -0.0165 -0.0060 54  ASN   A OD1 
1358 O OD1 B ASN   A 54  ? 0.1171 0.1076 0.1442 -0.0166 -0.0003 -0.0064 54  ASN   A OD1 
1359 N ND2 A ASN   A 54  ? 0.1089 0.1504 0.1627 0.0023  -0.0228 0.0077  54  ASN   A ND2 
1360 N ND2 B ASN   A 54  ? 0.1221 0.1123 0.1711 -0.0191 0.0036  -0.0096 54  ASN   A ND2 
1373 N N   A LYS   A 55  ? 0.1091 0.1315 0.1544 0.0082  -0.0000 -0.0007 55  LYS   A N   
1374 N N   B LYS   A 55  ? 0.1267 0.1291 0.1664 -0.0125 -0.0049 -0.0349 55  LYS   A N   
1375 C CA  A LYS   A 55  ? 0.1131 0.1309 0.1689 0.0102  -0.0007 -0.0181 55  LYS   A CA  
1376 C CA  B LYS   A 55  ? 0.1389 0.1496 0.1936 -0.0010 -0.0039 -0.0425 55  LYS   A CA  
1377 C C   A LYS   A 55  ? 0.1169 0.1405 0.1704 0.0009  0.0112  -0.0352 55  LYS   A C   
1378 C C   B LYS   A 55  ? 0.1308 0.1506 0.1864 -0.0059 0.0064  -0.0417 55  LYS   A C   
1379 O O   A LYS   A 55  ? 0.1267 0.1500 0.1666 0.0019  0.0110  -0.0434 55  LYS   A O   
1380 O O   B LYS   A 55  ? 0.1418 0.1599 0.1872 -0.0045 0.0033  -0.0439 55  LYS   A O   
1381 C CB  A LYS   A 55  ? 0.1112 0.1328 0.1834 0.0191  -0.0033 -0.0316 55  LYS   A CB  
1382 C CB  B LYS   A 55  ? 0.1584 0.1766 0.2420 0.0114  0.0011  -0.0417 55  LYS   A CB  
1383 C CG  A LYS   A 55  ? 0.1139 0.1392 0.1811 0.0200  0.0068  -0.0307 55  LYS   A CG  
1384 C CG  B LYS   A 55  ? 0.1851 0.2117 0.2905 0.0190  -0.0005 -0.0313 55  LYS   A CG  
1385 C CD  A LYS   A 55  ? 0.1201 0.1564 0.1716 0.0293  0.0129  -0.0341 55  LYS   A CD  
1386 C CD  B LYS   A 55  ? 0.2135 0.2431 0.3339 0.0201  -0.0077 -0.0198 55  LYS   A CD  
1387 C CE  A LYS   A 55  ? 0.1439 0.1773 0.1654 0.0402  0.0033  -0.0331 55  LYS   A CE  
1388 C CE  B LYS   A 55  ? 0.2270 0.2658 0.3564 0.0201  -0.0176 -0.0102 55  LYS   A CE  
1389 N NZ  A LYS   A 55  ? 0.1539 0.1800 0.1629 0.0447  -0.0103 -0.0265 55  LYS   A NZ  
1390 N NZ  B LYS   A 55  ? 0.2296 0.2737 0.3615 0.0251  -0.0282 -0.0071 55  LYS   A NZ  
1417 N N   . ALA   A 56  ? 0.1271 0.1544 0.1825 -0.0048 0.0149  -0.0436 56  ALA   A N   
1418 C CA  . ALA   A 56  ? 0.1389 0.1677 0.1682 -0.0130 0.0175  -0.0420 56  ALA   A CA  
1419 C C   . ALA   A 56  ? 0.1489 0.1831 0.1469 -0.0140 0.0182  -0.0435 56  ALA   A C   
1420 O O   . ALA   A 56  ? 0.1563 0.2141 0.1546 -0.0023 0.0310  -0.0340 56  ALA   A O   
1421 C CB  . ALA   A 56  ? 0.1472 0.1868 0.1833 -0.0217 0.0232  -0.0216 56  ALA   A CB  
1428 N N   . THR   A 57  ? 0.1303 0.1552 0.1450 -0.0144 0.0204  -0.0288 57  THR   A N   
1429 C CA  . THR   A 57  ? 0.1376 0.1561 0.1400 -0.0130 0.0081  -0.0269 57  THR   A CA  
1430 C C   . THR   A 57  ? 0.1414 0.1649 0.1422 -0.0106 0.0086  -0.0353 57  THR   A C   
1431 O O   . THR   A 57  ? 0.1392 0.1658 0.1643 -0.0164 -0.0022 -0.0382 57  THR   A O   
1432 C CB  . THR   A 57  ? 0.1353 0.1523 0.1367 -0.0136 0.0061  -0.0252 57  THR   A CB  
1433 O OG1 . THR   A 57  ? 0.1220 0.1470 0.1398 -0.0114 0.0075  -0.0211 57  THR   A OG1 
1434 C CG2 . THR   A 57  ? 0.1454 0.1566 0.1345 -0.0114 0.0050  -0.0212 57  THR   A CG2 
1442 N N   . ASN   A 58  ? 0.1433 0.1551 0.1684 -0.0108 0.0142  -0.0445 58  ASN   A N   
1443 C CA  . ASN   A 58  ? 0.1568 0.1484 0.1848 -0.0103 0.0185  -0.0512 58  ASN   A CA  
1444 C C   . ASN   A 58  ? 0.1340 0.1393 0.1819 -0.0037 0.0107  -0.0381 58  ASN   A C   
1445 O O   . ASN   A 58  ? 0.1377 0.1456 0.1935 -0.0167 0.0026  -0.0413 58  ASN   A O   
1446 C CB  . ASN   A 58  ? 0.1966 0.1728 0.2130 -0.0218 0.0341  -0.0634 58  ASN   A CB  
1447 C CG  . ASN   A 58  ? 0.2342 0.1975 0.2826 -0.0179 0.0273  -0.0468 58  ASN   A CG  
1448 O OD1 . ASN   A 58  ? 0.2555 0.1926 0.3190 0.0132  0.0540  -0.0372 58  ASN   A OD1 
1449 N ND2 . ASN   A 58  ? 0.2448 0.2091 0.3015 -0.0188 0.0171  -0.0501 58  ASN   A ND2 
1456 N N   . ASN   A 59  ? 0.1255 0.1311 0.1646 -0.0065 0.0004  -0.0304 59  ASN   A N   
1457 C CA  . ASN   A 59  ? 0.1266 0.1219 0.1685 -0.0097 0.0009  -0.0188 59  ASN   A CA  
1458 C C   . ASN   A 59  ? 0.1221 0.1242 0.1518 -0.0078 -0.0044 -0.0137 59  ASN   A C   
1459 O O   . ASN   A 59  ? 0.1206 0.1296 0.1485 -0.0085 0.0071  -0.0075 59  ASN   A O   
1460 C CB  . ASN   A 59  ? 0.1313 0.1241 0.1733 -0.0073 -0.0134 -0.0279 59  ASN   A CB  
1461 C CG  . ASN   A 59  ? 0.1325 0.1225 0.1688 -0.0056 -0.0225 -0.0110 59  ASN   A CG  
1462 O OD1 . ASN   A 59  ? 0.1451 0.1289 0.1634 -0.0138 -0.0170 -0.0015 59  ASN   A OD1 
1463 N ND2 . ASN   A 59  ? 0.1443 0.1263 0.1821 -0.0116 -0.0122 -0.0092 59  ASN   A ND2 
1470 N N   . ALA   A 60  ? 0.1170 0.1326 0.1485 -0.0085 -0.0030 -0.0175 60  ALA   A N   
1471 C CA  . ALA   A 60  ? 0.1195 0.1307 0.1417 -0.0054 -0.0126 -0.0161 60  ALA   A CA  
1472 C C   . ALA   A 60  ? 0.1218 0.1239 0.1445 -0.0058 -0.0063 -0.0074 60  ALA   A C   
1473 O O   . ALA   A 60  ? 0.1145 0.1282 0.1707 -0.0057 -0.0054 -0.0205 60  ALA   A O   
1474 C CB  . ALA   A 60  ? 0.1365 0.1451 0.1585 -0.0086 -0.0157 -0.0325 60  ALA   A CB  
1480 N N   . MET   A 61  ? 0.1172 0.1219 0.1382 -0.0062 0.0007  -0.0094 61  MET   A N   
1481 C CA  . MET   A 61  ? 0.1198 0.1199 0.1389 -0.0085 0.0050  -0.0098 61  MET   A CA  
1482 C C   . MET   A 61  ? 0.1134 0.1153 0.1434 -0.0106 0.0028  -0.0096 61  MET   A C   
1483 O O   . MET   A 61  ? 0.1164 0.1142 0.1459 -0.0085 0.0077  -0.0045 61  MET   A O   
1484 C CB  . MET   A 61  ? 0.1201 0.1163 0.1396 -0.0071 0.0054  -0.0026 61  MET   A CB  
1485 C CG  . MET   A 61  ? 0.1174 0.1234 0.1418 -0.0045 0.0024  -0.0085 61  MET   A CG  
1486 S SD  . MET   A 61  ? 0.1227 0.1282 0.1783 -0.0131 0.0036  -0.0264 61  MET   A SD  
1487 C CE  . MET   A 61  ? 0.1428 0.1424 0.1978 -0.0194 0.0185  -0.0135 61  MET   A CE  
1497 N N   . GLN   A 62  ? 0.1140 0.1085 0.1494 -0.0082 -0.0004 -0.0083 62  GLN   A N   
1498 C CA  . GLN   A 62  ? 0.1186 0.1057 0.1483 -0.0034 -0.0018 -0.0035 62  GLN   A CA  
1499 C C   . GLN   A 62  ? 0.1182 0.1030 0.1588 -0.0038 0.0119  -0.0060 62  GLN   A C   
1500 O O   . GLN   A 62  ? 0.1237 0.1196 0.1443 -0.0055 0.0107  -0.0083 62  GLN   A O   
1501 C CB  . GLN   A 62  ? 0.1207 0.1106 0.1543 -0.0022 0.0018  -0.0099 62  GLN   A CB  
1502 C CG  . GLN   A 62  ? 0.1268 0.1100 0.1480 -0.0054 -0.0019 0.0004  62  GLN   A CG  
1503 C CD  . GLN   A 62  ? 0.1340 0.1162 0.1496 -0.0020 0.0023  0.0061  62  GLN   A CD  
1504 O OE1 . GLN   A 62  ? 0.1322 0.1238 0.1609 -0.0043 0.0005  -0.0034 62  GLN   A OE1 
1505 N NE2 . GLN   A 62  ? 0.1387 0.1192 0.1502 0.0002  -0.0066 -0.0113 62  GLN   A NE2 
1514 N N   . VAL   A 63  ? 0.1136 0.1178 0.1614 -0.0099 0.0080  -0.0252 63  VAL   A N   
1515 C CA  . VAL   A 63  ? 0.1204 0.1261 0.1829 -0.0137 0.0014  -0.0196 63  VAL   A CA  
1516 C C   . VAL   A 63  ? 0.1091 0.1248 0.1684 -0.0155 -0.0007 -0.0229 63  VAL   A C   
1517 O O   . VAL   A 63  ? 0.1097 0.1235 0.1886 -0.0183 0.0012  -0.0140 63  VAL   A O   
1518 C CB  . VAL   A 63  ? 0.1268 0.1404 0.2121 -0.0157 -0.0031 -0.0439 63  VAL   A CB  
1519 C CG1 . VAL   A 63  ? 0.1481 0.1599 0.2409 -0.0156 -0.0115 -0.0609 63  VAL   A CG1 
1520 C CG2 . VAL   A 63  ? 0.1415 0.1337 0.2340 -0.0159 0.0081  -0.0447 63  VAL   A CG2 
1530 N N   . GLU   A 64  ? 0.1116 0.1310 0.1568 -0.0049 -0.0050 -0.0210 64  GLU   A N   
1531 C CA  . GLU   A 64  ? 0.1110 0.1318 0.1489 -0.0070 -0.0026 -0.0107 64  GLU   A CA  
1532 C C   . GLU   A 64  ? 0.1088 0.1210 0.1467 -0.0094 0.0038  0.0028  64  GLU   A C   
1533 O O   . GLU   A 64  ? 0.1110 0.1262 0.1595 -0.0064 0.0031  -0.0064 64  GLU   A O   
1534 C CB  . GLU   A 64  ? 0.1221 0.1367 0.1562 -0.0071 -0.0029 -0.0127 64  GLU   A CB  
1535 C CG  . GLU   A 64  ? 0.1260 0.1394 0.1652 -0.0134 0.0073  -0.0056 64  GLU   A CG  
1536 C CD  . GLU   A 64  ? 0.1372 0.1490 0.1651 -0.0130 0.0167  -0.0121 64  GLU   A CD  
1537 O OE1 . GLU   A 64  ? 0.1340 0.1614 0.1866 -0.0232 0.0202  -0.0036 64  GLU   A OE1 
1538 O OE2 . GLU   A 64  ? 0.1559 0.1518 0.1593 -0.0257 0.0029  0.0027  64  GLU   A OE2 
1545 N N   . SER   A 65  ? 0.1107 0.1238 0.1440 -0.0009 0.0021  -0.0056 65  SER   A N   
1546 C CA  . SER   A 65  ? 0.1174 0.1149 0.1389 -0.0065 0.0015  -0.0064 65  SER   A CA  
1547 C C   . SER   A 65  ? 0.1158 0.1240 0.1485 -0.0074 0.0041  -0.0052 65  SER   A C   
1548 O O   . SER   A 65  ? 0.1207 0.1281 0.1568 -0.0001 0.0159  -0.0107 65  SER   A O   
1549 C CB  . SER   A 65  ? 0.1173 0.1165 0.1452 -0.0058 0.0072  -0.0014 65  SER   A CB  
1550 O OG  . SER   A 65  ? 0.1137 0.1304 0.1488 -0.0098 -0.0104 0.0062  65  SER   A OG  
1556 N N   . ASP   A 66  ? 0.1185 0.1196 0.1458 -0.0071 0.0093  -0.0008 66  ASP   A N   
1557 C CA  . ASP   A 66  ? 0.1296 0.1274 0.1686 -0.0045 0.0114  0.0114  66  ASP   A CA  
1558 C C   . ASP   A 66  ? 0.1269 0.1216 0.1618 -0.0055 0.0139  0.0089  66  ASP   A C   
1559 O O   . ASP   A 66  ? 0.1318 0.1352 0.1750 -0.0069 0.0244  0.0152  66  ASP   A O   
1560 C CB  . ASP   A 66  ? 0.1358 0.1311 0.2012 0.0011  0.0051  0.0238  66  ASP   A CB  
1561 C CG  . ASP   A 66  ? 0.1567 0.1460 0.2362 -0.0016 -0.0002 0.0461  66  ASP   A CG  
1562 O OD1 . ASP   A 66  ? 0.1551 0.1751 0.2173 -0.0076 -0.0111 0.0462  66  ASP   A OD1 
1563 O OD2 . ASP   A 66  ? 0.1756 0.1585 0.3166 0.0209  -0.0215 0.0205  66  ASP   A OD2 
1568 N N   . ASP   A 67  ? 0.1161 0.1263 0.1751 -0.0041 0.0079  0.0041  67  ASP   A N   
1569 C CA  . ASP   A 67  ? 0.1152 0.1434 0.1899 -0.0064 0.0092  0.0137  67  ASP   A CA  
1570 C C   . ASP   A 67  ? 0.1186 0.1407 0.1872 -0.0042 0.0116  0.0167  67  ASP   A C   
1571 O O   . ASP   A 67  ? 0.1159 0.1480 0.2091 -0.0016 0.0246  0.0271  67  ASP   A O   
1572 C CB  . ASP   A 67  ? 0.1261 0.1474 0.2149 -0.0066 -0.0115 0.0143  67  ASP   A CB  
1573 C CG  . ASP   A 67  ? 0.1256 0.1623 0.2430 -0.0107 -0.0257 0.0209  67  ASP   A CG  
1574 O OD1 . ASP   A 67  ? 0.1288 0.1778 0.3275 -0.0124 -0.0291 0.0328  67  ASP   A OD1 
1575 O OD2 . ASP   A 67  ? 0.1262 0.1627 0.2348 -0.0017 -0.0164 0.0183  67  ASP   A OD2 
1580 N N   A TYR   A 68  ? 0.1177 0.1306 0.1811 -0.0011 0.0162  0.0174  68  TYR   A N   
1581 N N   B TYR   A 68  ? 0.1189 0.1340 0.1767 0.0002  0.0107  0.0223  68  TYR   A N   
1582 C CA  A TYR   A 68  ? 0.1246 0.1250 0.1766 -0.0026 0.0257  0.0112  68  TYR   A CA  
1583 C CA  B TYR   A 68  ? 0.1284 0.1324 0.1702 -0.0007 0.0149  0.0180  68  TYR   A CA  
1584 C C   A TYR   A 68  ? 0.1205 0.1226 0.1733 -0.0011 0.0273  0.0128  68  TYR   A C   
1585 C C   B TYR   A 68  ? 0.1218 0.1278 0.1727 -0.0010 0.0242  0.0142  68  TYR   A C   
1586 O O   A TYR   A 68  ? 0.1224 0.1237 0.1757 0.0064  0.0283  0.0148  68  TYR   A O   
1587 O O   B TYR   A 68  ? 0.1253 0.1323 0.1776 0.0081  0.0294  0.0138  68  TYR   A O   
1588 C CB  A TYR   A 68  ? 0.1304 0.1179 0.1905 0.0037  0.0403  0.0078  68  TYR   A CB  
1589 C CB  B TYR   A 68  ? 0.1375 0.1300 0.1779 0.0044  0.0189  0.0229  68  TYR   A CB  
1590 C CG  A TYR   A 68  ? 0.1352 0.1252 0.2042 0.0010  0.0600  0.0114  68  TYR   A CG  
1591 C CG  B TYR   A 68  ? 0.1468 0.1394 0.1785 0.0042  0.0269  0.0267  68  TYR   A CG  
1592 C CD1 A TYR   A 68  ? 0.1379 0.1338 0.2265 -0.0168 0.0522  -0.0094 68  TYR   A CD1 
1593 C CD1 B TYR   A 68  ? 0.1546 0.1450 0.1817 0.0007  0.0181  0.0179  68  TYR   A CD1 
1594 C CD2 A TYR   A 68  ? 0.1537 0.1284 0.2230 0.0097  0.0579  0.0088  68  TYR   A CD2 
1595 C CD2 B TYR   A 68  ? 0.1589 0.1419 0.1731 0.0025  0.0191  0.0231  68  TYR   A CD2 
1596 C CE1 A TYR   A 68  ? 0.1430 0.1447 0.2565 -0.0222 0.0476  -0.0262 68  TYR   A CE1 
1597 C CE1 B TYR   A 68  ? 0.1608 0.1423 0.1625 0.0023  0.0134  0.0325  68  TYR   A CE1 
1598 C CE2 A TYR   A 68  ? 0.1508 0.1378 0.2414 0.0050  0.0673  -0.0039 68  TYR   A CE2 
1599 C CE2 B TYR   A 68  ? 0.1557 0.1435 0.1402 -0.0012 0.0248  0.0149  68  TYR   A CE2 
1600 C CZ  A TYR   A 68  ? 0.1446 0.1432 0.2704 -0.0185 0.0456  -0.0325 68  TYR   A CZ  
1601 C CZ  B TYR   A 68  ? 0.1657 0.1387 0.1302 -0.0001 0.0196  0.0327  68  TYR   A CZ  
1602 O OH  A TYR   A 68  ? 0.1593 0.1548 0.3059 -0.0146 0.0171  -0.0633 68  TYR   A OH  
1603 O OH  B TYR   A 68  ? 0.1908 0.1358 0.1260 0.0013  0.0047  0.0338  68  TYR   A OH  
1622 N N   . ILE   A 69  ? 0.1164 0.1201 0.1738 -0.0009 0.0202  0.0165  69  ILE   A N   
1623 C CA  . ILE   A 69  ? 0.1273 0.1245 0.1574 0.0006  0.0144  0.0034  69  ILE   A CA  
1624 C C   . ILE   A 69  ? 0.1316 0.1246 0.1532 0.0002  0.0189  0.0186  69  ILE   A C   
1625 O O   . ILE   A 69  ? 0.1444 0.1365 0.1509 -0.0039 0.0249  0.0132  69  ILE   A O   
1626 C CB  . ILE   A 69  ? 0.1332 0.1485 0.1640 0.0026  0.0138  -0.0073 69  ILE   A CB  
1627 C CG1 . ILE   A 69  ? 0.1365 0.1594 0.1675 0.0039  0.0127  -0.0171 69  ILE   A CG1 
1628 C CG2 . ILE   A 69  ? 0.1575 0.1681 0.1875 0.0119  -0.0049 -0.0039 69  ILE   A CG2 
1629 C CD1 . ILE   A 69  ? 0.1376 0.1667 0.1793 0.0017  0.0182  -0.0194 69  ILE   A CD1 
1642 N N   . ALA   A 70  ? 0.1332 0.1227 0.1685 -0.0085 0.0194  0.0151  70  ALA   A N   
1643 C CA  . ALA   A 70  ? 0.1371 0.1373 0.1779 -0.0166 0.0252  0.0132  70  ALA   A CA  
1644 C C   . ALA   A 70  ? 0.1367 0.1531 0.1884 -0.0106 0.0361  0.0138  70  ALA   A C   
1645 O O   . ALA   A 70  ? 0.1529 0.1809 0.2093 0.0053  0.0509  0.0307  70  ALA   A O   
1646 C CB  . ALA   A 70  ? 0.1396 0.1408 0.2026 -0.0220 0.0216  0.0119  70  ALA   A CB  
1652 N N   . THR   A 71  ? 0.1269 0.1480 0.1764 -0.0040 0.0267  0.0146  71  THR   A N   
1653 C CA  . THR   A 71  ? 0.1337 0.1665 0.2036 0.0024  0.0218  0.0167  71  THR   A CA  
1654 C C   . THR   A 71  ? 0.1311 0.1646 0.2154 0.0089  0.0326  0.0155  71  THR   A C   
1655 O O   . THR   A 71  ? 0.1359 0.1900 0.2548 0.0043  0.0403  -0.0082 71  THR   A O   
1656 C CB  . THR   A 71  ? 0.1588 0.1857 0.2122 0.0120  -0.0092 0.0267  71  THR   A CB  
1657 O OG1 . THR   A 71  ? 0.1907 0.2014 0.2186 0.0034  -0.0358 0.0150  71  THR   A OG1 
1658 C CG2 . THR   A 71  ? 0.1727 0.2014 0.2322 0.0187  -0.0139 0.0434  71  THR   A CG2 
1666 N N   . ASN   A 72  ? 0.1339 0.1433 0.1925 0.0063  0.0270  0.0164  72  ASN   A N   
1667 C CA  . ASN   A 72  ? 0.1383 0.1426 0.1937 0.0118  0.0340  0.0205  72  ASN   A CA  
1668 C C   . ASN   A 72  ? 0.1493 0.1428 0.1962 0.0044  0.0381  0.0102  72  ASN   A C   
1669 O O   . ASN   A 72  ? 0.1615 0.1438 0.2221 0.0143  0.0355  -0.0002 72  ASN   A O   
1670 C CB  . ASN   A 72  ? 0.1541 0.1449 0.1979 0.0058  0.0296  0.0159  72  ASN   A CB  
1671 C CG  . ASN   A 72  ? 0.1781 0.1598 0.1990 0.0214  0.0326  0.0238  72  ASN   A CG  
1672 O OD1 . ASN   A 72  ? 0.1976 0.1962 0.2178 0.0209  0.0416  0.0231  72  ASN   A OD1 
1673 N ND2 . ASN   A 72  ? 0.1943 0.1652 0.2050 0.0499  0.0125  0.0163  72  ASN   A ND2 
1680 N N   . GLY   A 73  ? 0.1502 0.1399 0.1796 0.0022  0.0388  0.0094  73  GLY   A N   
1681 C CA  . GLY   A 73  ? 0.1561 0.1369 0.1684 -0.0066 0.0424  0.0087  73  GLY   A CA  
1682 C C   . GLY   A 73  ? 0.1526 0.1313 0.1558 0.0004  0.0509  0.0160  73  GLY   A C   
1683 O O   . GLY   A 73  ? 0.1500 0.1414 0.1719 0.0126  0.0409  0.0259  73  GLY   A O   
1687 N N   . PRO   A 74  ? 0.1644 0.1343 0.1604 -0.0109 0.0396  0.0127  74  PRO   A N   
1688 C CA  . PRO   A 74  ? 0.1583 0.1355 0.1759 0.0001  0.0379  0.0129  74  PRO   A CA  
1689 C C   . PRO   A 74  ? 0.1466 0.1212 0.1616 0.0014  0.0251  0.0054  74  PRO   A C   
1690 O O   . PRO   A 74  ? 0.1560 0.1319 0.1734 0.0044  0.0294  -0.0098 74  PRO   A O   
1691 C CB  . PRO   A 74  ? 0.1713 0.1641 0.1986 0.0069  0.0330  0.0256  74  PRO   A CB  
1692 C CG  . PRO   A 74  ? 0.1990 0.1956 0.2325 -0.0174 0.0279  0.0152  74  PRO   A CG  
1693 C CD  . PRO   A 74  ? 0.1839 0.1724 0.1842 -0.0205 0.0333  0.0083  74  PRO   A CD  
1701 N N   . LEU   A 75  ? 0.1450 0.1147 0.1546 0.0053  0.0174  -0.0024 75  LEU   A N   
1702 C CA  . LEU   A 75  ? 0.1506 0.1105 0.1445 0.0014  0.0114  -0.0022 75  LEU   A CA  
1703 C C   . LEU   A 75  ? 0.1594 0.1244 0.1423 0.0063  0.0132  0.0008  75  LEU   A C   
1704 O O   . LEU   A 75  ? 0.1924 0.1369 0.1529 0.0120  0.0066  -0.0064 75  LEU   A O   
1705 C CB  . LEU   A 75  ? 0.1525 0.1200 0.1319 -0.0078 0.0028  0.0077  75  LEU   A CB  
1706 C CG  . LEU   A 75  ? 0.1674 0.1494 0.1343 -0.0337 0.0013  0.0132  75  LEU   A CG  
1707 C CD1 . LEU   A 75  ? 0.1765 0.1965 0.1426 -0.0282 -0.0053 -0.0018 75  LEU   A CD1 
1708 C CD2 . LEU   A 75  ? 0.1951 0.1933 0.1883 -0.0121 0.0026  0.0142  75  LEU   A CD2 
1720 N N   . LYS   A 76  ? 0.1604 0.1274 0.1591 -0.0040 0.0114  -0.0122 76  LYS   A N   
1721 C CA  . LYS   A 76  ? 0.1595 0.1480 0.1663 -0.0053 0.0140  -0.0214 76  LYS   A CA  
1722 C C   . LYS   A 76  ? 0.1554 0.1288 0.1328 0.0020  0.0112  -0.0094 76  LYS   A C   
1723 O O   . LYS   A 76  ? 0.1569 0.1214 0.1289 0.0021  0.0157  0.0004  76  LYS   A O   
1724 C CB  . LYS   A 76  ? 0.1562 0.1678 0.2243 -0.0010 0.0146  -0.0443 76  LYS   A CB  
1725 C CG  . LYS   A 76  ? 0.1667 0.1662 0.2847 0.0038  0.0186  -0.0477 76  LYS   A CG  
1726 C CD  . LYS   A 76  ? 0.1724 0.1619 0.3382 0.0096  0.0165  -0.0613 76  LYS   A CD  
1727 C CE  . LYS   A 76  ? 0.1944 0.1854 0.4070 0.0029  0.0184  -0.0659 76  LYS   A CE  
1728 N NZ  . LYS   A 76  ? 0.1984 0.1788 0.4531 -0.0130 0.0118  -0.0735 76  LYS   A NZ  
1742 N N   . VAL   A 77  ? 0.1606 0.1321 0.1308 0.0014  0.0221  -0.0015 77  VAL   A N   
1743 C CA  . VAL   A 77  ? 0.1621 0.1382 0.1273 0.0075  0.0210  -0.0022 77  VAL   A CA  
1744 C C   . VAL   A 77  ? 0.1540 0.1340 0.1288 0.0120  0.0142  -0.0037 77  VAL   A C   
1745 O O   . VAL   A 77  ? 0.1572 0.1384 0.1283 0.0146  0.0228  -0.0161 77  VAL   A O   
1746 C CB  . VAL   A 77  ? 0.1813 0.1581 0.1308 0.0063  0.0163  0.0073  77  VAL   A CB  
1747 C CG1 . VAL   A 77  ? 0.1763 0.1691 0.1557 0.0163  0.0091  0.0038  77  VAL   A CG1 
1748 C CG2 . VAL   A 77  ? 0.2069 0.1710 0.1511 0.0018  0.0010  0.0187  77  VAL   A CG2 
1758 N N   . GLY   A 78  ? 0.1494 0.1279 0.1295 0.0075  0.0223  -0.0111 78  GLY   A N   
1759 C CA  . GLY   A 78  ? 0.1419 0.1304 0.1386 0.0044  0.0167  0.0018  78  GLY   A CA  
1760 C C   . GLY   A 78  ? 0.1331 0.1193 0.1345 0.0072  0.0161  0.0011  78  GLY   A C   
1761 O O   . GLY   A 78  ? 0.1358 0.1216 0.1656 0.0028  0.0200  0.0092  78  GLY   A O   
1765 N N   . GLY   A 79  ? 0.1400 0.1161 0.1358 0.0059  0.0164  0.0033  79  GLY   A N   
1766 C CA  . GLY   A 79  ? 0.1318 0.1168 0.1398 0.0024  0.0181  0.0042  79  GLY   A CA  
1767 C C   . GLY   A 79  ? 0.1215 0.1129 0.1331 0.0010  0.0091  0.0031  79  GLY   A C   
1768 O O   . GLY   A 79  ? 0.1247 0.1310 0.1446 0.0197  0.0104  -0.0025 79  GLY   A O   
1772 N N   . SER   A 80  ? 0.1179 0.1277 0.1468 0.0012  0.0180  -0.0076 80  SER   A N   
1773 C CA  . SER   A 80  ? 0.1191 0.1216 0.1394 -0.0044 0.0098  -0.0051 80  SER   A CA  
1774 C C   . SER   A 80  ? 0.1138 0.1217 0.1377 -0.0025 0.0060  0.0081  80  SER   A C   
1775 O O   . SER   A 80  ? 0.1171 0.1410 0.1632 0.0038  0.0126  -0.0036 80  SER   A O   
1776 C CB  . SER   A 80  ? 0.1305 0.1233 0.1587 -0.0085 0.0049  0.0081  80  SER   A CB  
1777 O OG  . SER   A 80  ? 0.1555 0.1278 0.1881 -0.0011 -0.0019 0.0082  80  SER   A OG  
1783 N N   . CYS   A 81  ? 0.1120 0.1160 0.1390 -0.0033 -0.0013 0.0091  81  CYS   A N   
1784 C CA  . CYS   A 81  ? 0.1092 0.1246 0.1413 -0.0047 -0.0071 0.0160  81  CYS   A CA  
1785 C C   . CYS   A 81  ? 0.1101 0.1207 0.1357 -0.0084 0.0015  0.0224  81  CYS   A C   
1786 O O   . CYS   A 81  ? 0.1118 0.1513 0.1458 -0.0006 0.0052  0.0220  81  CYS   A O   
1787 C CB  . CYS   A 81  ? 0.1211 0.1301 0.1584 -0.0121 0.0050  0.0174  81  CYS   A CB  
1788 S SG  . CYS   A 81  ? 0.1338 0.1220 0.1523 -0.0137 0.0042  0.0086  81  CYS   A SG  
1794 N N   . VAL   A 82  ? 0.1184 0.1284 0.1367 -0.0012 -0.0128 0.0095  82  VAL   A N   
1795 C CA  . VAL   A 82  ? 0.1281 0.1338 0.1238 0.0014  -0.0054 0.0142  82  VAL   A CA  
1796 C C   . VAL   A 82  ? 0.1295 0.1429 0.1280 -0.0021 -0.0098 0.0156  82  VAL   A C   
1797 O O   . VAL   A 82  ? 0.1234 0.1511 0.1620 0.0022  -0.0002 0.0007  82  VAL   A O   
1798 C CB  . VAL   A 82  ? 0.1601 0.1511 0.1397 -0.0004 -0.0003 0.0202  82  VAL   A CB  
1799 C CG1 . VAL   A 82  ? 0.1863 0.1694 0.1667 0.0014  0.0061  0.0140  82  VAL   A CG1 
1800 C CG2 . VAL   A 82  ? 0.1628 0.1528 0.1573 -0.0049 -0.0011 0.0214  82  VAL   A CG2 
1810 N N   . LEU   A 83  ? 0.1227 0.1350 0.1216 -0.0078 -0.0080 0.0042  83  LEU   A N   
1811 C CA  . LEU   A 83  ? 0.1268 0.1386 0.1351 -0.0145 -0.0046 0.0032  83  LEU   A CA  
1812 C C   . LEU   A 83  ? 0.1343 0.1420 0.1187 -0.0127 -0.0108 0.0073  83  LEU   A C   
1813 O O   . LEU   A 83  ? 0.1424 0.1466 0.1324 -0.0163 -0.0002 0.0102  83  LEU   A O   
1814 C CB  . LEU   A 83  ? 0.1321 0.1406 0.1309 -0.0142 -0.0071 0.0068  83  LEU   A CB  
1815 C CG  . LEU   A 83  ? 0.1452 0.1492 0.1349 -0.0130 0.0057  0.0001  83  LEU   A CG  
1816 C CD1 . LEU   A 83  ? 0.1569 0.1513 0.1554 -0.0251 -0.0033 0.0131  83  LEU   A CD1 
1817 C CD2 . LEU   A 83  ? 0.1468 0.1635 0.1517 -0.0118 0.0124  0.0104  83  LEU   A CD2 
1829 N N   . SER   A 84  ? 0.1415 0.1498 0.1264 -0.0131 0.0003  0.0052  84  SER   A N   
1830 C CA  . SER   A 84  ? 0.1545 0.1577 0.1221 -0.0152 -0.0014 0.0079  84  SER   A CA  
1831 C C   . SER   A 84  ? 0.1597 0.1497 0.1154 -0.0233 0.0031  0.0085  84  SER   A C   
1832 O O   . SER   A 84  ? 0.1545 0.1581 0.1161 -0.0171 0.0010  -0.0003 84  SER   A O   
1833 C CB  . SER   A 84  ? 0.1627 0.1786 0.1306 -0.0168 -0.0015 -0.0001 84  SER   A CB  
1834 O OG  . SER   A 84  ? 0.1648 0.1956 0.1435 -0.0143 -0.0053 -0.0185 84  SER   A OG  
1840 N N   . GLY   A 85  ? 0.1765 0.1692 0.1124 -0.0233 0.0182  0.0006  85  GLY   A N   
1841 C CA  . GLY   A 85  ? 0.1777 0.1804 0.1295 -0.0311 0.0233  -0.0111 85  GLY   A CA  
1842 C C   . GLY   A 85  ? 0.1763 0.1821 0.1212 -0.0302 0.0203  -0.0142 85  GLY   A C   
1843 O O   . GLY   A 85  ? 0.1770 0.1916 0.1406 -0.0301 0.0253  -0.0172 85  GLY   A O   
1847 N N   . HIS   A 86  ? 0.1774 0.1743 0.1223 -0.0270 0.0149  -0.0095 86  HIS   A N   
1848 C CA  . HIS   A 86  ? 0.1918 0.1830 0.1149 -0.0280 0.0137  -0.0047 86  HIS   A CA  
1849 C C   . HIS   A 86  ? 0.2149 0.1943 0.1344 -0.0277 0.0183  -0.0113 86  HIS   A C   
1850 O O   . HIS   A 86  ? 0.2275 0.2135 0.1283 -0.0199 0.0238  -0.0180 86  HIS   A O   
1851 C CB  . HIS   A 86  ? 0.1876 0.1701 0.1353 -0.0195 0.0198  -0.0075 86  HIS   A CB  
1852 C CG  . HIS   A 86  ? 0.1766 0.1651 0.1342 -0.0107 0.0084  -0.0020 86  HIS   A CG  
1853 N ND1 . HIS   A 86  ? 0.1849 0.1626 0.1698 -0.0254 0.0007  -0.0024 86  HIS   A ND1 
1854 C CD2 . HIS   A 86  ? 0.1726 0.1625 0.1269 -0.0003 0.0132  0.0016  86  HIS   A CD2 
1855 C CE1 . HIS   A 86  ? 0.1782 0.1618 0.1556 -0.0184 0.0252  0.0087  86  HIS   A CE1 
1856 N NE2 . HIS   A 86  ? 0.1701 0.1586 0.1414 -0.0037 0.0211  0.0205  86  HIS   A NE2 
1864 N N   A ASN   A 87  ? 0.2261 0.2018 0.1433 -0.0271 0.0345  -0.0164 87  ASN   A N   
1865 N N   B ASN   A 87  ? 0.2129 0.1995 0.1389 -0.0308 0.0347  -0.0276 87  ASN   A N   
1866 C CA  A ASN   A 87  ? 0.2391 0.2106 0.1542 -0.0188 0.0484  -0.0104 87  ASN   A CA  
1867 C CA  B ASN   A 87  ? 0.2152 0.2068 0.1478 -0.0226 0.0526  -0.0316 87  ASN   A CA  
1868 C C   A ASN   A 87  ? 0.2383 0.2196 0.1806 -0.0174 0.0608  0.0014  87  ASN   A C   
1869 C C   B ASN   A 87  ? 0.2036 0.2142 0.1378 -0.0212 0.0547  -0.0190 87  ASN   A C   
1870 O O   A ASN   A 87  ? 0.2493 0.2271 0.2030 -0.0152 0.0731  0.0053  87  ASN   A O   
1871 O O   B ASN   A 87  ? 0.2047 0.2158 0.1237 -0.0185 0.0507  -0.0079 87  ASN   A O   
1872 C CB  A ASN   A 87  ? 0.2502 0.2165 0.1554 -0.0148 0.0479  -0.0136 87  ASN   A CB  
1873 C CB  B ASN   A 87  ? 0.2319 0.2137 0.1664 -0.0157 0.0698  -0.0430 87  ASN   A CB  
1874 C CG  A ASN   A 87  ? 0.2566 0.2216 0.1619 -0.0146 0.0431  -0.0086 87  ASN   A CG  
1875 C CG  B ASN   A 87  ? 0.2430 0.2202 0.1737 -0.0127 0.0833  -0.0394 87  ASN   A CG  
1876 O OD1 A ASN   A 87  ? 0.2566 0.2160 0.1547 -0.0126 0.0351  -0.0064 87  ASN   A OD1 
1877 O OD1 B ASN   A 87  ? 0.2489 0.2172 0.1724 -0.0069 0.0835  -0.0378 87  ASN   A OD1 
1878 N ND2 A ASN   A 87  ? 0.2624 0.2377 0.1734 -0.0137 0.0422  -0.0069 87  ASN   A ND2 
1879 N ND2 B ASN   A 87  ? 0.2486 0.2359 0.1813 -0.0083 0.0916  -0.0396 87  ASN   A ND2 
1892 N N   A LEU   A 88  ? 0.2235 0.2168 0.1856 -0.0220 0.0520  0.0038  88  LEU   A N   
1893 N N   B LEU   A 88  ? 0.1912 0.2135 0.1409 -0.0278 0.0535  -0.0213 88  LEU   A N   
1894 C CA  A LEU   A 88  ? 0.2096 0.2143 0.1872 -0.0270 0.0442  0.0095  88  LEU   A CA  
1895 C CA  B LEU   A 88  ? 0.1835 0.2149 0.1489 -0.0293 0.0493  -0.0162 88  LEU   A CA  
1896 C C   A LEU   A 88  ? 0.2008 0.2109 0.1673 -0.0312 0.0409  0.0146  88  LEU   A C   
1897 C C   B LEU   A 88  ? 0.1846 0.2104 0.1416 -0.0328 0.0453  0.0014  88  LEU   A C   
1898 O O   A LEU   A 88  ? 0.2062 0.2161 0.1728 -0.0322 0.0387  0.0238  88  LEU   A O   
1899 O O   B LEU   A 88  ? 0.1866 0.2168 0.1587 -0.0342 0.0447  0.0032  88  LEU   A O   
1900 C CB  A LEU   A 88  ? 0.2102 0.2151 0.2078 -0.0335 0.0277  0.0150  88  LEU   A CB  
1901 C CB  B LEU   A 88  ? 0.1818 0.2181 0.1611 -0.0317 0.0396  -0.0329 88  LEU   A CB  
1902 C CG  A LEU   A 88  ? 0.2187 0.2226 0.2328 -0.0332 0.0176  0.0130  88  LEU   A CG  
1903 C CG  B LEU   A 88  ? 0.1913 0.2282 0.1829 -0.0288 0.0375  -0.0416 88  LEU   A CG  
1904 C CD1 A LEU   A 88  ? 0.2230 0.2271 0.2358 -0.0294 0.0140  0.0127  88  LEU   A CD1 
1905 C CD1 B LEU   A 88  ? 0.1937 0.2314 0.1850 -0.0264 0.0396  -0.0480 88  LEU   A CD1 
1906 C CD2 A LEU   A 88  ? 0.2255 0.2296 0.2518 -0.0311 0.0141  0.0059  88  LEU   A CD2 
1907 C CD2 B LEU   A 88  ? 0.1996 0.2383 0.2101 -0.0228 0.0306  -0.0442 88  LEU   A CD2 
1930 N N   . ALA   A 89  ? 0.1919 0.2019 0.1472 -0.0294 0.0400  -0.0002 89  ALA   A N   
1931 C CA  . ALA   A 89  ? 0.1991 0.2066 0.1250 -0.0282 0.0264  0.0139  89  ALA   A CA  
1932 C C   . ALA   A 89  ? 0.2064 0.2120 0.1296 -0.0265 0.0095  0.0016  89  ALA   A C   
1933 O O   . ALA   A 89  ? 0.2073 0.2089 0.1622 -0.0384 0.0022  -0.0201 89  ALA   A O   
1934 C CB  . ALA   A 89  ? 0.1962 0.2066 0.1258 -0.0253 0.0167  0.0161  89  ALA   A CB  
1941 N N   . LYS   A 90  ? 0.2193 0.2267 0.1275 -0.0318 -0.0087 0.0103  90  LYS   A N   
1942 C CA  . LYS   A 90  ? 0.2280 0.2409 0.1325 -0.0274 -0.0221 0.0146  90  LYS   A CA  
1943 C C   . LYS   A 90  ? 0.2089 0.2195 0.1290 -0.0295 -0.0153 0.0008  90  LYS   A C   
1944 O O   . LYS   A 90  ? 0.2051 0.2288 0.1603 -0.0359 -0.0155 -0.0130 90  LYS   A O   
1945 C CB  . LYS   A 90  ? 0.2578 0.2723 0.1598 -0.0273 -0.0330 0.0261  90  LYS   A CB  
1946 C CG  . LYS   A 90  ? 0.2940 0.3068 0.2640 -0.0258 -0.0312 0.0276  90  LYS   A CG  
1947 C CD  . LYS   A 90  ? 0.3339 0.3423 0.3660 -0.0280 -0.0195 0.0284  90  LYS   A CD  
1948 C CE  . LYS   A 90  ? 0.3633 0.3695 0.4453 -0.0286 -0.0086 0.0271  90  LYS   A CE  
1949 N NZ  . LYS   A 90  ? 0.3773 0.3818 0.4941 -0.0279 -0.0046 0.0252  90  LYS   A NZ  
1963 N N   . HIS   A 91  ? 0.1898 0.1905 0.0996 -0.0309 -0.0172 0.0069  91  HIS   A N   
1964 C CA  . HIS   A 91  ? 0.1798 0.1713 0.1041 -0.0233 -0.0188 0.0116  91  HIS   A CA  
1965 C C   . HIS   A 91  ? 0.1576 0.1585 0.1017 -0.0230 -0.0041 0.0124  91  HIS   A C   
1966 O O   . HIS   A 91  ? 0.1584 0.1699 0.1172 -0.0233 0.0079  0.0087  91  HIS   A O   
1967 C CB  . HIS   A 91  ? 0.1936 0.1956 0.1510 -0.0014 -0.0293 0.0076  91  HIS   A CB  
1968 C CG  . HIS   A 91  ? 0.2292 0.2390 0.2331 0.0144  -0.0543 -0.0037 91  HIS   A CG  
1969 N ND1 . HIS   A 91  ? 0.2371 0.2643 0.2852 0.0209  -0.0624 -0.0162 91  HIS   A ND1 
1970 C CD2 . HIS   A 91  ? 0.2512 0.2591 0.2558 0.0233  -0.0665 0.0083  91  HIS   A CD2 
1971 C CE1 . HIS   A 91  ? 0.2494 0.2714 0.2880 0.0218  -0.0687 -0.0094 91  HIS   A CE1 
1972 N NE2 . HIS   A 91  ? 0.2600 0.2742 0.2856 0.0251  -0.0686 -0.0015 91  HIS   A NE2 
1980 N N   . CYS   A 92  ? 0.1479 0.1499 0.1194 -0.0212 -0.0060 0.0105  92  CYS   A N   
1981 C CA  . CYS   A 92  ? 0.1384 0.1403 0.1185 -0.0182 0.0052  0.0065  92  CYS   A CA  
1982 C C   . CYS   A 92  ? 0.1258 0.1350 0.1182 -0.0169 0.0077  0.0069  92  CYS   A C   
1983 O O   . CYS   A 92  ? 0.1236 0.1430 0.1294 -0.0183 0.0081  -0.0002 92  CYS   A O   
1984 C CB  . CYS   A 92  ? 0.1382 0.1399 0.1301 -0.0108 0.0006  -0.0007 92  CYS   A CB  
1985 S SG  . CYS   A 92  ? 0.1314 0.1300 0.1344 -0.0165 0.0049  0.0025  92  CYS   A SG  
1991 N N   . LEU   A 93  ? 0.1268 0.1261 0.1178 -0.0129 0.0141  0.0063  93  LEU   A N   
1992 C CA  . LEU   A 93  ? 0.1215 0.1189 0.1165 -0.0067 0.0124  0.0071  93  LEU   A CA  
1993 C C   . LEU   A 93  ? 0.1169 0.1097 0.1163 -0.0046 0.0128  0.0016  93  LEU   A C   
1994 O O   . LEU   A 93  ? 0.1118 0.1210 0.1259 -0.0068 0.0070  0.0047  93  LEU   A O   
1995 C CB  . LEU   A 93  ? 0.1298 0.1199 0.1344 -0.0079 0.0045  0.0126  93  LEU   A CB  
1996 C CG  . LEU   A 93  ? 0.1295 0.1216 0.1399 -0.0030 0.0082  0.0172  93  LEU   A CG  
1997 C CD1 . LEU   A 93  ? 0.1383 0.1208 0.1711 -0.0025 0.0166  0.0113  93  LEU   A CD1 
1998 C CD2 . LEU   A 93  ? 0.1376 0.1235 0.1486 -0.0087 0.0001  0.0106  93  LEU   A CD2 
2010 N N   . HIS   A 94  ? 0.1049 0.1097 0.1230 -0.0057 0.0074  0.0134  94  HIS   A N   
2011 C CA  . HIS   A 94  ? 0.1041 0.1163 0.1150 -0.0066 0.0049  0.0068  94  HIS   A CA  
2012 C C   . HIS   A 94  ? 0.1023 0.1119 0.1216 -0.0039 0.0019  0.0045  94  HIS   A C   
2013 O O   . HIS   A 94  ? 0.1074 0.1304 0.1514 -0.0024 0.0063  -0.0154 94  HIS   A O   
2014 C CB  . HIS   A 94  ? 0.1066 0.1080 0.1228 -0.0061 0.0014  0.0100  94  HIS   A CB  
2015 C CG  . HIS   A 94  ? 0.1136 0.1075 0.1202 -0.0073 0.0021  0.0123  94  HIS   A CG  
2016 N ND1 . HIS   A 94  ? 0.1103 0.1086 0.1281 -0.0052 0.0043  0.0084  94  HIS   A ND1 
2017 C CD2 . HIS   A 94  ? 0.1194 0.1184 0.1206 -0.0099 0.0009  0.0023  94  HIS   A CD2 
2018 C CE1 . HIS   A 94  ? 0.1144 0.1121 0.1328 -0.0102 -0.0081 0.0006  94  HIS   A CE1 
2019 N NE2 . HIS   A 94  ? 0.1238 0.1158 0.1198 -0.0116 -0.0035 -0.0010 94  HIS   A NE2 
2027 N N   . VAL   A 95  ? 0.1052 0.1109 0.0970 -0.0023 0.0073  0.0012  95  VAL   A N   
2028 C CA  . VAL   A 95  ? 0.1081 0.1074 0.1062 -0.0039 0.0094  -0.0039 95  VAL   A CA  
2029 C C   . VAL   A 95  ? 0.1114 0.1051 0.0983 -0.0072 0.0055  0.0054  95  VAL   A C   
2030 O O   . VAL   A 95  ? 0.1157 0.1156 0.1119 0.0088  0.0105  0.0033  95  VAL   A O   
2031 C CB  . VAL   A 95  ? 0.1168 0.1108 0.1298 -0.0070 0.0070  0.0004  95  VAL   A CB  
2032 C CG1 . VAL   A 95  ? 0.1335 0.1168 0.1276 -0.0078 0.0089  -0.0047 95  VAL   A CG1 
2033 C CG2 . VAL   A 95  ? 0.1107 0.1181 0.1416 -0.0147 0.0062  0.0142  95  VAL   A CG2 
2043 N N   A VAL   A 96  ? 0.1189 0.1160 0.1053 -0.0046 0.0120  0.0031  96  VAL   A N   
2044 N N   B VAL   A 96  ? 0.1160 0.1055 0.0953 0.0037  0.0053  0.0028  96  VAL   A N   
2045 C CA  A VAL   A 96  ? 0.1295 0.1235 0.1206 -0.0063 0.0175  0.0009  96  VAL   A CA  
2046 C CA  B VAL   A 96  ? 0.1214 0.1010 0.1058 0.0087  0.0068  0.0028  96  VAL   A CA  
2047 C C   A VAL   A 96  ? 0.1311 0.1289 0.1202 -0.0044 0.0174  0.0050  96  VAL   A C   
2048 C C   B VAL   A 96  ? 0.1253 0.1068 0.1120 0.0125  -0.0016 0.0031  96  VAL   A C   
2049 O O   A VAL   A 96  ? 0.1422 0.1419 0.1298 -0.0089 0.0262  -0.0034 96  VAL   A O   
2050 O O   B VAL   A 96  ? 0.1331 0.1148 0.1362 0.0023  0.0065  -0.0125 96  VAL   A O   
2051 C CB  A VAL   A 96  ? 0.1371 0.1294 0.1349 -0.0109 0.0179  0.0003  96  VAL   A CB  
2052 C CB  B VAL   A 96  ? 0.1203 0.1029 0.1067 0.0099  0.0113  0.0017  96  VAL   A CB  
2053 C CG1 A VAL   A 96  ? 0.1455 0.1405 0.1380 -0.0117 0.0129  -0.0067 96  VAL   A CG1 
2054 C CG1 B VAL   A 96  ? 0.1190 0.1141 0.0984 0.0108  0.0072  0.0041  96  VAL   A CG1 
2055 C CG2 A VAL   A 96  ? 0.1384 0.1333 0.1436 -0.0212 0.0129  0.0019  96  VAL   A CG2 
2056 C CG2 B VAL   A 96  ? 0.1261 0.1081 0.1180 -0.0099 0.0122  -0.0020 96  VAL   A CG2 
2075 N N   A GLY   A 97  ? 0.1250 0.1264 0.1335 -0.0043 0.0122  0.0030  97  GLY   A N   
2076 N N   B GLY   A 97  ? 0.1233 0.1140 0.1262 0.0090  -0.0049 0.0019  97  GLY   A N   
2077 C CA  A GLY   A 97  ? 0.1294 0.1356 0.1327 -0.0039 0.0033  0.0013  97  GLY   A CA  
2078 C CA  B GLY   A 97  ? 0.1346 0.1295 0.1376 -0.0045 -0.0107 0.0046  97  GLY   A CA  
2079 C C   A GLY   A 97  ? 0.1300 0.1484 0.1143 0.0014  0.0054  -0.0048 97  GLY   A C   
2080 C C   B GLY   A 97  ? 0.1421 0.1500 0.1370 -0.0044 -0.0089 0.0044  97  GLY   A C   
2081 O O   A GLY   A 97  ? 0.1398 0.1449 0.1215 -0.0043 0.0102  -0.0037 97  GLY   A O   
2082 O O   B GLY   A 97  ? 0.1475 0.1469 0.1470 -0.0097 -0.0078 0.0219  97  GLY   A O   
2089 N N   A PRO   A 98  ? 0.1357 0.1622 0.1079 0.0059  -0.0038 -0.0017 98  PRO   A N   
2090 N N   B PRO   A 98  ? 0.1484 0.1664 0.1187 -0.0039 -0.0105 -0.0082 98  PRO   A N   
2091 C CA  A PRO   A 98  ? 0.1487 0.1852 0.1147 0.0055  -0.0054 -0.0011 98  PRO   A CA  
2092 C CA  B PRO   A 98  ? 0.1572 0.1905 0.1149 -0.0015 -0.0001 -0.0095 98  PRO   A CA  
2093 C C   A PRO   A 98  ? 0.1577 0.1918 0.1135 -0.0037 -0.0082 0.0180  98  PRO   A C   
2094 C C   B PRO   A 98  ? 0.1475 0.1955 0.1059 -0.0037 0.0032  0.0057  98  PRO   A C   
2095 O O   A PRO   A 98  ? 0.1519 0.1692 0.1292 0.0005  -0.0088 0.0040  98  PRO   A O   
2096 O O   B PRO   A 98  ? 0.1416 0.1809 0.0981 -0.0035 0.0024  0.0060  98  PRO   A O   
2097 C CB  A PRO   A 98  ? 0.1576 0.1921 0.1168 0.0142  -0.0043 -0.0163 98  PRO   A CB  
2098 C CB  B PRO   A 98  ? 0.1702 0.1993 0.1173 0.0062  -0.0017 -0.0228 98  PRO   A CB  
2099 C CG  A PRO   A 98  ? 0.1524 0.1822 0.1274 0.0189  -0.0053 -0.0229 98  PRO   A CG  
2100 C CG  B PRO   A 98  ? 0.1642 0.1886 0.1253 0.0072  -0.0092 -0.0294 98  PRO   A CG  
2101 C CD  A PRO   A 98  ? 0.1410 0.1693 0.1256 0.0113  -0.0049 -0.0131 98  PRO   A CD  
2102 C CD  B PRO   A 98  ? 0.1541 0.1740 0.1263 -0.0004 -0.0102 -0.0226 98  PRO   A CD  
2117 N N   A ASN   A 99  ? 0.1731 0.2206 0.1110 -0.0107 -0.0035 0.0474  99  ASN   A N   
2118 N N   B ASN   A 99  ? 0.1414 0.2103 0.1084 -0.0003 0.0071  0.0166  99  ASN   A N   
2119 C CA  A ASN   A 99  ? 0.1974 0.2445 0.1255 -0.0162 -0.0106 0.0697  99  ASN   A CA  
2120 C CA  B ASN   A 99  ? 0.1525 0.2140 0.1131 0.0031  0.0132  0.0268  99  ASN   A CA  
2121 C C   A ASN   A 99  ? 0.2126 0.2708 0.1260 -0.0308 -0.0045 0.0787  99  ASN   A C   
2122 C C   B ASN   A 99  ? 0.1653 0.2195 0.1024 -0.0049 0.0189  0.0244  99  ASN   A C   
2123 O O   A ASN   A 99  ? 0.2205 0.2723 0.1214 -0.0254 -0.0111 0.0725  99  ASN   A O   
2124 O O   B ASN   A 99  ? 0.1692 0.2031 0.1161 -0.0029 0.0138  0.0190  99  ASN   A O   
2125 C CB  A ASN   A 99  ? 0.2018 0.2408 0.1650 -0.0114 -0.0265 0.0756  99  ASN   A CB  
2126 C CB  B ASN   A 99  ? 0.1476 0.2017 0.1225 0.0020  0.0052  0.0385  99  ASN   A CB  
2127 C CG  A ASN   A 99  ? 0.2065 0.2411 0.2055 -0.0062 -0.0358 0.0773  99  ASN   A CG  
2128 C CG  B ASN   A 99  ? 0.1479 0.1947 0.1508 -0.0012 -0.0083 0.0306  99  ASN   A CG  
2129 O OD1 A ASN   A 99  ? 0.2181 0.2454 0.2231 -0.0057 -0.0435 0.0764  99  ASN   A OD1 
2130 O OD1 B ASN   A 99  ? 0.1597 0.2035 0.1704 -0.0043 -0.0054 0.0238  99  ASN   A OD1 
2131 N ND2 A ASN   A 99  ? 0.2122 0.2382 0.2316 -0.0004 -0.0231 0.0714  99  ASN   A ND2 
2132 N ND2 B ASN   A 99  ? 0.1592 0.1841 0.1791 0.0038  -0.0033 0.0289  99  ASN   A ND2 
2145 N N   A VAL   A 100 ? 0.2240 0.2970 0.1560 -0.0426 -0.0065 0.0748  100 VAL   A N   
2146 N N   B VAL   A 100 ? 0.1813 0.2355 0.1081 -0.0098 0.0039  0.0127  100 VAL   A N   
2147 C CA  A VAL   A 100 ? 0.2345 0.3209 0.1788 -0.0491 -0.0051 0.0699  100 VAL   A CA  
2148 C CA  B VAL   A 100 ? 0.2002 0.2465 0.1375 -0.0070 -0.0167 0.0089  100 VAL   A CA  
2149 C C   A VAL   A 100 ? 0.2468 0.3372 0.1938 -0.0511 0.0003  0.0898  100 VAL   A C   
2150 C C   B VAL   A 100 ? 0.1955 0.2347 0.1024 -0.0013 -0.0249 0.0100  100 VAL   A C   
2151 O O   A VAL   A 100 ? 0.2509 0.3477 0.2029 -0.0500 0.0095  0.0958  100 VAL   A O   
2152 O O   B VAL   A 100 ? 0.2122 0.2297 0.1162 -0.0021 -0.0132 0.0079  100 VAL   A O   
2153 C CB  A VAL   A 100 ? 0.2349 0.3246 0.1932 -0.0533 -0.0078 0.0489  100 VAL   A CB  
2154 C CB  B VAL   A 100 ? 0.2264 0.2692 0.2047 -0.0167 -0.0279 0.0067  100 VAL   A CB  
2155 C CG1 A VAL   A 100 ? 0.2273 0.3268 0.1944 -0.0543 -0.0042 0.0444  100 VAL   A CG1 
2156 C CG1 B VAL   A 100 ? 0.2372 0.2842 0.2356 -0.0170 -0.0284 0.0078  100 VAL   A CG1 
2157 C CG2 A VAL   A 100 ? 0.2381 0.3263 0.2145 -0.0549 -0.0120 0.0360  100 VAL   A CG2 
2158 C CG2 B VAL   A 100 ? 0.2322 0.2738 0.2229 -0.0216 -0.0280 0.0069  100 VAL   A CG2 
2177 N N   A ASN   A 101 ? 0.2591 0.3443 0.2210 -0.0489 0.0039  0.0929  101 ASN   A N   
2178 N N   B ASN   A 101 ? 0.1837 0.2397 0.1041 0.0025  -0.0121 0.0322  101 ASN   A N   
2179 C CA  A ASN   A 101 ? 0.2758 0.3485 0.2420 -0.0444 0.0039  0.0915  101 ASN   A CA  
2180 C CA  B ASN   A 101 ? 0.1838 0.2521 0.1023 0.0054  -0.0025 0.0431  101 ASN   A CA  
2181 C C   A ASN   A 101 ? 0.2934 0.3557 0.2564 -0.0440 0.0100  0.0938  101 ASN   A C   
2182 C C   B ASN   A 101 ? 0.1951 0.2696 0.1097 -0.0032 0.0136  0.0595  101 ASN   A C   
2183 O O   A ASN   A 101 ? 0.3036 0.3589 0.2784 -0.0405 0.0102  0.0895  101 ASN   A O   
2184 O O   B ASN   A 101 ? 0.2012 0.2726 0.1453 0.0013  0.0130  0.0458  101 ASN   A O   
2185 C CB  A ASN   A 101 ? 0.2713 0.3426 0.2519 -0.0421 0.0012  0.0825  101 ASN   A CB  
2186 C CB  B ASN   A 101 ? 0.1756 0.2525 0.1159 0.0075  -0.0043 0.0366  101 ASN   A CB  
2187 C CG  A ASN   A 101 ? 0.2679 0.3358 0.2592 -0.0428 0.0008  0.0684  101 ASN   A CG  
2188 C CG  B ASN   A 101 ? 0.1699 0.2531 0.1327 0.0058  -0.0166 0.0316  101 ASN   A CG  
2189 O OD1 A ASN   A 101 ? 0.2683 0.3347 0.2642 -0.0418 0.0038  0.0528  101 ASN   A OD1 
2190 O OD1 B ASN   A 101 ? 0.1760 0.2580 0.1495 0.0057  -0.0246 0.0054  101 ASN   A OD1 
2191 N ND2 A ASN   A 101 ? 0.2669 0.3336 0.2627 -0.0432 -0.0023 0.0670  101 ASN   A ND2 
2192 N ND2 B ASN   A 101 ? 0.1626 0.2516 0.1377 0.0000  -0.0005 0.0406  101 ASN   A ND2 
2205 N N   A LYS   A 102 ? 0.2965 0.3575 0.2624 -0.0482 0.0156  0.0867  102 LYS   A N   
2206 N N   B LYS   A 102 ? 0.1983 0.2858 0.1432 -0.0232 0.0229  0.0601  102 LYS   A N   
2207 C CA  A LYS   A 102 ? 0.3016 0.3584 0.2558 -0.0524 0.0154  0.0700  102 LYS   A CA  
2208 C CA  B LYS   A 102 ? 0.2231 0.3081 0.1672 -0.0345 0.0274  0.0557  102 LYS   A CA  
2209 C C   A LYS   A 102 ? 0.3048 0.3551 0.2321 -0.0509 0.0133  0.0674  102 LYS   A C   
2210 C C   B LYS   A 102 ? 0.2329 0.3158 0.1626 -0.0272 0.0498  0.0539  102 LYS   A C   
2211 O O   A LYS   A 102 ? 0.3094 0.3575 0.2256 -0.0466 0.0166  0.0719  102 LYS   A O   
2212 O O   B LYS   A 102 ? 0.2301 0.3181 0.1800 -0.0279 0.0583  0.0561  102 LYS   A O   
2213 C CB  A LYS   A 102 ? 0.3051 0.3629 0.2738 -0.0578 0.0162  0.0510  102 LYS   A CB  
2214 C CB  B LYS   A 102 ? 0.2422 0.3222 0.2034 -0.0514 0.0079  0.0428  102 LYS   A CB  
2215 C CG  A LYS   A 102 ? 0.3091 0.3662 0.2874 -0.0627 0.0171  0.0320  102 LYS   A CG  
2216 C CG  B LYS   A 102 ? 0.2633 0.3369 0.2343 -0.0617 -0.0138 0.0234  102 LYS   A CG  
2217 C CD  A LYS   A 102 ? 0.3147 0.3706 0.3011 -0.0646 0.0163  0.0120  102 LYS   A CD  
2218 C CD  B LYS   A 102 ? 0.2813 0.3494 0.2653 -0.0674 -0.0301 0.0090  102 LYS   A CD  
2219 C CE  A LYS   A 102 ? 0.3200 0.3739 0.3132 -0.0653 0.0147  -0.0039 102 LYS   A CE  
2220 C CE  B LYS   A 102 ? 0.2933 0.3567 0.2816 -0.0709 -0.0404 0.0000  102 LYS   A CE  
2221 N NZ  A LYS   A 102 ? 0.3232 0.3761 0.3174 -0.0663 0.0155  -0.0153 102 LYS   A NZ  
2222 N NZ  B LYS   A 102 ? 0.2985 0.3597 0.2901 -0.0740 -0.0447 -0.0033 102 LYS   A NZ  
2249 N N   A GLY   A 103 ? 0.3050 0.3525 0.2312 -0.0481 0.0062  0.0442  103 GLY   A N   
2250 N N   B GLY   A 103 ? 0.2499 0.3207 0.1698 -0.0172 0.0493  0.0371  103 GLY   A N   
2251 C CA  A GLY   A 103 ? 0.3054 0.3463 0.2188 -0.0474 0.0077  0.0274  103 GLY   A CA  
2252 C CA  B GLY   A 103 ? 0.2621 0.3253 0.2018 -0.0096 0.0586  0.0120  103 GLY   A CA  
2253 C C   A GLY   A 103 ? 0.3023 0.3405 0.2051 -0.0482 0.0121  0.0092  103 GLY   A C   
2254 C C   B GLY   A 103 ? 0.2693 0.3262 0.2266 -0.0025 0.0753  -0.0120 103 GLY   A C   
2255 O O   A GLY   A 103 ? 0.3088 0.3461 0.2352 -0.0467 0.0085  0.0050  103 GLY   A O   
2256 O O   B GLY   A 103 ? 0.2793 0.3306 0.2420 0.0039  0.0785  -0.0197 103 GLY   A O   
2263 N N   A GLU   A 104 ? 0.2922 0.3287 0.1575 -0.0501 0.0179  -0.0006 104 GLU   A N   
2264 N N   B GLU   A 104 ? 0.2681 0.3248 0.2252 -0.0029 0.0810  -0.0223 104 GLU   A N   
2265 C CA  A GLU   A 104 ? 0.2750 0.3155 0.1264 -0.0562 0.0280  -0.0125 104 GLU   A CA  
2266 C CA  B GLU   A 104 ? 0.2637 0.3228 0.2404 -0.0016 0.0872  -0.0371 104 GLU   A CA  
2267 C C   A GLU   A 104 ? 0.2789 0.3187 0.1336 -0.0618 0.0278  -0.0325 104 GLU   A C   
2268 C C   B GLU   A 104 ? 0.2852 0.3309 0.2536 -0.0070 0.0763  -0.0614 104 GLU   A C   
2269 O O   A GLU   A 104 ? 0.2779 0.3129 0.1384 -0.0632 0.0234  -0.0338 104 GLU   A O   
2270 O O   B GLU   A 104 ? 0.2893 0.3297 0.2651 -0.0072 0.0668  -0.0761 104 GLU   A O   
2271 C CB  A GLU   A 104 ? 0.2555 0.3032 0.1082 -0.0533 0.0237  0.0041  104 GLU   A CB  
2272 C CB  B GLU   A 104 ? 0.2436 0.3127 0.2557 -0.0014 0.0903  -0.0242 104 GLU   A CB  
2273 C CG  A GLU   A 104 ? 0.2374 0.2923 0.0989 -0.0483 0.0177  0.0191  104 GLU   A CG  
2274 C CG  B GLU   A 104 ? 0.2250 0.3035 0.2818 -0.0043 0.0899  -0.0142 104 GLU   A CG  
2275 C CD  A GLU   A 104 ? 0.2217 0.2870 0.1002 -0.0389 0.0123  0.0264  104 GLU   A CD  
2276 C CD  B GLU   A 104 ? 0.2107 0.2928 0.3036 -0.0103 0.0859  -0.0060 104 GLU   A CD  
2277 O OE1 A GLU   A 104 ? 0.2094 0.2825 0.0829 -0.0334 -0.0038 0.0364  104 GLU   A OE1 
2278 O OE1 B GLU   A 104 ? 0.1882 0.2864 0.2957 -0.0105 0.0878  -0.0033 104 GLU   A OE1 
2279 O OE2 A GLU   A 104 ? 0.2257 0.2822 0.1041 -0.0354 0.0119  0.0314  104 GLU   A OE2 
2280 O OE2 B GLU   A 104 ? 0.2243 0.2923 0.3329 -0.0139 0.0812  -0.0073 104 GLU   A OE2 
2293 N N   A ASP   A 105 ? 0.2843 0.3285 0.1546 -0.0649 0.0306  -0.0471 105 ASP   A N   
2294 N N   B ASP   A 105 ? 0.2983 0.3407 0.2540 -0.0120 0.0732  -0.0732 105 ASP   A N   
2295 C CA  A ASP   A 105 ? 0.2845 0.3376 0.2004 -0.0614 0.0334  -0.0629 105 ASP   A CA  
2296 C CA  B ASP   A 105 ? 0.3078 0.3485 0.2574 -0.0248 0.0646  -0.0819 105 ASP   A CA  
2297 C C   A ASP   A 105 ? 0.2583 0.3396 0.1675 -0.0698 0.0252  -0.0741 105 ASP   A C   
2298 C C   B ASP   A 105 ? 0.2988 0.3529 0.2490 -0.0311 0.0525  -0.0892 105 ASP   A C   
2299 O O   A ASP   A 105 ? 0.2392 0.3191 0.1326 -0.0603 0.0244  -0.0888 105 ASP   A O   
2300 O O   B ASP   A 105 ? 0.2969 0.3520 0.2445 -0.0297 0.0549  -0.0898 105 ASP   A O   
2301 C CB  A ASP   A 105 ? 0.3092 0.3470 0.2738 -0.0549 0.0360  -0.0682 105 ASP   A CB  
2302 C CB  B ASP   A 105 ? 0.3238 0.3530 0.2871 -0.0291 0.0626  -0.0831 105 ASP   A CB  
2303 C CG  A ASP   A 105 ? 0.3277 0.3549 0.3365 -0.0483 0.0346  -0.0706 105 ASP   A CG  
2304 C CG  B ASP   A 105 ? 0.3364 0.3545 0.3064 -0.0315 0.0591  -0.0879 105 ASP   A CG  
2305 O OD1 A ASP   A 105 ? 0.3352 0.3587 0.3470 -0.0467 0.0299  -0.0764 105 ASP   A OD1 
2306 O OD1 B ASP   A 105 ? 0.3406 0.3550 0.2973 -0.0301 0.0642  -0.0919 105 ASP   A OD1 
2307 O OD2 A ASP   A 105 ? 0.3368 0.3564 0.3729 -0.0480 0.0346  -0.0671 105 ASP   A OD2 
2308 O OD2 B ASP   A 105 ? 0.3429 0.3570 0.3311 -0.0331 0.0482  -0.0883 105 ASP   A OD2 
2317 N N   A ILE   A 106 ? 0.2482 0.3448 0.1818 -0.0776 0.0081  -0.0653 106 ILE   A N   
2318 N N   B ILE   A 106 ? 0.2915 0.3606 0.2594 -0.0404 0.0240  -0.0917 106 ILE   A N   
2319 C CA  A ILE   A 106 ? 0.2338 0.3484 0.2013 -0.0902 -0.0093 -0.0620 106 ILE   A CA  
2320 C CA  B ILE   A 106 ? 0.2773 0.3626 0.2730 -0.0458 0.0098  -0.0979 106 ILE   A CA  
2321 C C   A ILE   A 106 ? 0.2214 0.3419 0.2140 -0.1072 -0.0102 -0.0845 106 ILE   A C   
2322 C C   B ILE   A 106 ? 0.2633 0.3455 0.2679 -0.0534 0.0220  -0.1318 106 ILE   A C   
2323 O O   A ILE   A 106 ? 0.2021 0.3424 0.2133 -0.1164 -0.0128 -0.0806 106 ILE   A O   
2324 O O   B ILE   A 106 ? 0.2489 0.3397 0.2590 -0.0562 0.0296  -0.1476 106 ILE   A O   
2325 C CB  A ILE   A 106 ? 0.2351 0.3563 0.2299 -0.0779 -0.0162 -0.0280 106 ILE   A CB  
2326 C CB  B ILE   A 106 ? 0.2778 0.3759 0.2978 -0.0430 -0.0110 -0.0719 106 ILE   A CB  
2327 C CG1 A ILE   A 106 ? 0.2318 0.3597 0.2608 -0.0652 -0.0199 -0.0077 106 ILE   A CG1 
2328 C CG1 B ILE   A 106 ? 0.2749 0.3847 0.3142 -0.0368 -0.0194 -0.0593 106 ILE   A CG1 
2329 C CG2 A ILE   A 106 ? 0.2346 0.3555 0.2324 -0.0794 -0.0171 -0.0169 106 ILE   A CG2 
2330 C CG2 B ILE   A 106 ? 0.2786 0.3778 0.3045 -0.0452 -0.0160 -0.0671 106 ILE   A CG2 
2331 C CD1 A ILE   A 106 ? 0.2350 0.3601 0.2743 -0.0538 -0.0140 0.0021  106 ILE   A CD1 
2332 C CD1 B ILE   A 106 ? 0.2750 0.3870 0.3189 -0.0313 -0.0180 -0.0542 106 ILE   A CD1 
2355 N N   A GLN   A 107 ? 0.2343 0.3306 0.2489 -0.1050 -0.0020 -0.1069 107 GLN   A N   
2356 N N   B GLN   A 107 ? 0.2642 0.3372 0.2948 -0.0548 0.0313  -0.1381 107 GLN   A N   
2357 C CA  A GLN   A 107 ? 0.2538 0.3208 0.3149 -0.0873 0.0250  -0.1111 107 GLN   A CA  
2358 C CA  B GLN   A 107 ? 0.2657 0.3249 0.3359 -0.0524 0.0436  -0.1294 107 GLN   A CA  
2359 C C   A GLN   A 107 ? 0.2358 0.2868 0.3189 -0.0752 0.0506  -0.1061 107 GLN   A C   
2360 C C   B GLN   A 107 ? 0.2371 0.2914 0.3292 -0.0539 0.0583  -0.1135 107 GLN   A C   
2361 O O   A GLN   A 107 ? 0.2365 0.2759 0.3596 -0.0815 0.0614  -0.1084 107 GLN   A O   
2362 O O   B GLN   A 107 ? 0.2327 0.2846 0.3764 -0.0455 0.0740  -0.1099 107 GLN   A O   
2363 C CB  A GLN   A 107 ? 0.2874 0.3421 0.3904 -0.0822 0.0221  -0.1031 107 GLN   A CB  
2364 C CB  B GLN   A 107 ? 0.2964 0.3499 0.4121 -0.0503 0.0379  -0.1151 107 GLN   A CB  
2365 C CG  A GLN   A 107 ? 0.3168 0.3625 0.4691 -0.0763 0.0170  -0.0879 107 GLN   A CG  
2366 C CG  B GLN   A 107 ? 0.3248 0.3716 0.4911 -0.0485 0.0278  -0.0928 107 GLN   A CG  
2367 C CD  A GLN   A 107 ? 0.3401 0.3785 0.5360 -0.0705 0.0150  -0.0723 107 GLN   A CD  
2368 C CD  B GLN   A 107 ? 0.3477 0.3890 0.5598 -0.0467 0.0190  -0.0731 107 GLN   A CD  
2369 O OE1 A GLN   A 107 ? 0.3484 0.3842 0.5627 -0.0696 0.0152  -0.0681 107 GLN   A OE1 
2370 O OE1 B GLN   A 107 ? 0.3566 0.3947 0.5868 -0.0465 0.0168  -0.0663 107 GLN   A OE1 
2371 N NE2 A GLN   A 107 ? 0.3484 0.3842 0.5586 -0.0693 0.0142  -0.0681 107 GLN   A NE2 
2372 N NE2 B GLN   A 107 ? 0.3561 0.3947 0.5831 -0.0463 0.0161  -0.0671 107 GLN   A NE2 
2389 N N   . LEU   A 108 ? 0.2116 0.2538 0.2766 -0.0591 0.0578  -0.1099 108 LEU   A N   
2390 C CA  . LEU   A 108 ? 0.1830 0.1982 0.2352 -0.0280 0.0558  -0.0524 108 LEU   A CA  
2391 C C   . LEU   A 108 ? 0.1540 0.1467 0.2238 -0.0053 0.0442  -0.0169 108 LEU   A C   
2392 O O   . LEU   A 108 ? 0.1462 0.1348 0.2470 -0.0032 0.0366  -0.0056 108 LEU   A O   
2393 C CB  . LEU   A 108 ? 0.1895 0.2041 0.2067 -0.0332 0.0542  -0.0406 108 LEU   A CB  
2394 C CG  . LEU   A 108 ? 0.2042 0.2253 0.2256 -0.0326 0.0645  -0.0351 108 LEU   A CG  
2395 C CD1 . LEU   A 108 ? 0.2257 0.2292 0.2249 -0.0373 0.0611  -0.0306 108 LEU   A CD1 
2396 C CD2 . LEU   A 108 ? 0.2093 0.2503 0.2808 -0.0256 0.0603  -0.0205 108 LEU   A CD2 
2409 N N   . LEU   A 109 ? 0.1419 0.1396 0.2037 -0.0004 0.0341  -0.0091 109 LEU   A N   
2410 C CA  . LEU   A 109 ? 0.1365 0.1297 0.1843 -0.0005 0.0136  -0.0015 109 LEU   A CA  
2411 C C   . LEU   A 109 ? 0.1251 0.1260 0.1779 -0.0042 0.0129  -0.0132 109 LEU   A C   
2412 O O   . LEU   A 109 ? 0.1326 0.1196 0.1979 -0.0004 -0.0030 -0.0215 109 LEU   A O   
2413 C CB  . LEU   A 109 ? 0.1379 0.1435 0.1921 0.0059  0.0080  0.0056  109 LEU   A CB  
2414 C CG  . LEU   A 109 ? 0.1328 0.1459 0.1945 0.0025  0.0062  0.0115  109 LEU   A CG  
2415 C CD1 . LEU   A 109 ? 0.1395 0.1348 0.2038 0.0044  0.0060  -0.0135 109 LEU   A CD1 
2416 C CD2 . LEU   A 109 ? 0.1366 0.1705 0.2116 -0.0022 0.0056  0.0104  109 LEU   A CD2 
2428 N N   . LYS   A 110 ? 0.1294 0.1251 0.1637 -0.0060 0.0084  -0.0079 110 LYS   A N   
2429 C CA  . LYS   A 110 ? 0.1281 0.1247 0.1816 -0.0093 0.0059  -0.0077 110 LYS   A CA  
2430 C C   . LYS   A 110 ? 0.1296 0.1160 0.1632 -0.0091 0.0080  -0.0185 110 LYS   A C   
2431 O O   . LYS   A 110 ? 0.1262 0.1166 0.1719 -0.0081 0.0126  -0.0182 110 LYS   A O   
2432 C CB  . LYS   A 110 ? 0.1330 0.1281 0.1963 -0.0082 0.0027  -0.0141 110 LYS   A CB  
2433 C CG  . LYS   A 110 ? 0.1331 0.1254 0.1969 -0.0065 -0.0040 -0.0163 110 LYS   A CG  
2434 C CD  . LYS   A 110 ? 0.1391 0.1303 0.2081 -0.0146 0.0001  -0.0219 110 LYS   A CD  
2435 C CE  . LYS   A 110 ? 0.1498 0.1343 0.2300 -0.0064 0.0173  -0.0206 110 LYS   A CE  
2436 N NZ  . LYS   A 110 ? 0.1543 0.1371 0.2430 -0.0185 0.0226  -0.0253 110 LYS   A NZ  
2450 N N   . SER   A 111 ? 0.1265 0.1130 0.1746 -0.0020 0.0076  -0.0083 111 SER   A N   
2451 C CA  . SER   A 111 ? 0.1229 0.1205 0.1729 -0.0048 0.0170  -0.0035 111 SER   A CA  
2452 C C   . SER   A 111 ? 0.1192 0.1126 0.1753 -0.0102 0.0101  -0.0060 111 SER   A C   
2453 O O   . SER   A 111 ? 0.1302 0.1119 0.1868 -0.0058 0.0126  -0.0031 111 SER   A O   
2454 C CB  . SER   A 111 ? 0.1371 0.1398 0.1794 -0.0024 0.0208  -0.0121 111 SER   A CB  
2455 O OG  . SER   A 111 ? 0.1808 0.1612 0.1843 0.0058  0.0210  -0.0196 111 SER   A OG  
2461 N N   . ALA   A 112 ? 0.1184 0.1076 0.1806 -0.0043 0.0176  -0.0117 112 ALA   A N   
2462 C CA  . ALA   A 112 ? 0.1253 0.1075 0.1721 -0.0057 0.0184  -0.0167 112 ALA   A CA  
2463 C C   . ALA   A 112 ? 0.1161 0.1065 0.1841 -0.0041 0.0149  -0.0182 112 ALA   A C   
2464 O O   . ALA   A 112 ? 0.1210 0.1103 0.1794 -0.0139 0.0188  -0.0076 112 ALA   A O   
2465 C CB  . ALA   A 112 ? 0.1348 0.1053 0.1853 -0.0015 0.0043  -0.0182 112 ALA   A CB  
2471 N N   . TYR   A 113 ? 0.1130 0.1107 0.1803 -0.0038 0.0122  -0.0116 113 TYR   A N   
2472 C CA  . TYR   A 113 ? 0.1103 0.1118 0.1768 -0.0048 0.0235  -0.0064 113 TYR   A CA  
2473 C C   . TYR   A 113 ? 0.1080 0.1138 0.1688 -0.0135 0.0222  -0.0075 113 TYR   A C   
2474 O O   . TYR   A 113 ? 0.1114 0.1179 0.1781 -0.0070 0.0250  -0.0071 113 TYR   A O   
2475 C CB  . TYR   A 113 ? 0.1149 0.1235 0.1690 -0.0092 0.0071  -0.0030 113 TYR   A CB  
2476 C CG  . TYR   A 113 ? 0.1155 0.1277 0.1572 -0.0143 0.0151  0.0029  113 TYR   A CG  
2477 C CD1 . TYR   A 113 ? 0.1210 0.1315 0.1384 -0.0087 0.0187  0.0066  113 TYR   A CD1 
2478 C CD2 . TYR   A 113 ? 0.1247 0.1328 0.1495 -0.0147 0.0152  -0.0054 113 TYR   A CD2 
2479 C CE1 . TYR   A 113 ? 0.1200 0.1314 0.1432 -0.0112 0.0168  0.0107  113 TYR   A CE1 
2480 C CE2 . TYR   A 113 ? 0.1215 0.1397 0.1472 -0.0163 0.0095  0.0029  113 TYR   A CE2 
2481 C CZ  . TYR   A 113 ? 0.1187 0.1352 0.1390 -0.0051 0.0139  0.0120  113 TYR   A CZ  
2482 O OH  . TYR   A 113 ? 0.1176 0.1442 0.1680 0.0035  0.0141  0.0127  113 TYR   A OH  
2492 N N   . GLU   A 114 ? 0.1130 0.1114 0.1725 -0.0076 0.0166  -0.0049 114 GLU   A N   
2493 C CA  . GLU   A 114 ? 0.1170 0.1047 0.1784 0.0013  0.0124  -0.0085 114 GLU   A CA  
2494 C C   . GLU   A 114 ? 0.1128 0.1110 0.1741 0.0026  0.0183  -0.0066 114 GLU   A C   
2495 O O   . GLU   A 114 ? 0.1220 0.1109 0.1712 -0.0013 0.0148  -0.0025 114 GLU   A O   
2496 C CB  . GLU   A 114 ? 0.1154 0.1084 0.1838 -0.0055 0.0087  -0.0005 114 GLU   A CB  
2497 C CG  . GLU   A 114 ? 0.1261 0.1106 0.1804 0.0039  0.0150  -0.0070 114 GLU   A CG  
2498 C CD  . GLU   A 114 ? 0.1307 0.1149 0.1750 -0.0062 0.0117  -0.0090 114 GLU   A CD  
2499 O OE1 . GLU   A 114 ? 0.1341 0.1107 0.1776 -0.0066 0.0159  -0.0123 114 GLU   A OE1 
2500 O OE2 . GLU   A 114 ? 0.1495 0.1200 0.1888 -0.0135 0.0100  -0.0213 114 GLU   A OE2 
2507 N N   . ASN   A 115 ? 0.1180 0.1081 0.1689 -0.0069 0.0150  -0.0056 115 ASN   A N   
2508 C CA  . ASN   A 115 ? 0.1231 0.1116 0.1650 -0.0099 0.0204  0.0014  115 ASN   A CA  
2509 C C   . ASN   A 115 ? 0.1215 0.1095 0.1608 -0.0113 0.0102  0.0010  115 ASN   A C   
2510 O O   . ASN   A 115 ? 0.1217 0.1235 0.1620 -0.0110 0.0176  0.0072  115 ASN   A O   
2511 C CB  . ASN   A 115 ? 0.1275 0.1220 0.1473 -0.0193 0.0143  -0.0058 115 ASN   A CB  
2512 C CG  . ASN   A 115 ? 0.1237 0.1444 0.1614 -0.0168 0.0208  -0.0070 115 ASN   A CG  
2513 O OD1 . ASN   A 115 ? 0.1268 0.2364 0.1850 -0.0144 0.0271  0.0127  115 ASN   A OD1 
2514 N ND2 . ASN   A 115 ? 0.1248 0.1234 0.1656 -0.0177 0.0259  0.0015  115 ASN   A ND2 
2521 N N   . PHE   A 116 ? 0.1168 0.1152 0.1670 -0.0073 0.0123  0.0053  116 PHE   A N   
2522 C CA  . PHE   A 116 ? 0.1174 0.1226 0.1586 -0.0063 0.0231  0.0064  116 PHE   A CA  
2523 C C   . PHE   A 116 ? 0.1191 0.1257 0.1530 -0.0153 0.0254  0.0161  116 PHE   A C   
2524 O O   . PHE   A 116 ? 0.1232 0.1350 0.1614 -0.0052 0.0220  0.0145  116 PHE   A O   
2525 C CB  . PHE   A 116 ? 0.1192 0.1163 0.1732 -0.0087 0.0176  0.0088  116 PHE   A CB  
2526 C CG  . PHE   A 116 ? 0.1157 0.1130 0.1518 -0.0104 0.0206  -0.0036 116 PHE   A CG  
2527 C CD1 . PHE   A 116 ? 0.1250 0.1152 0.1612 -0.0069 0.0237  -0.0009 116 PHE   A CD1 
2528 C CD2 . PHE   A 116 ? 0.1206 0.1220 0.1742 -0.0058 0.0175  0.0046  116 PHE   A CD2 
2529 C CE1 . PHE   A 116 ? 0.1249 0.1168 0.1627 -0.0135 0.0186  -0.0059 116 PHE   A CE1 
2530 C CE2 . PHE   A 116 ? 0.1173 0.1211 0.1737 -0.0055 0.0221  -0.0047 116 PHE   A CE2 
2531 C CZ  . PHE   A 116 ? 0.1206 0.1131 0.1578 -0.0070 0.0097  -0.0012 116 PHE   A CZ  
2541 N N   . ASN   A 117 ? 0.1213 0.1171 0.1749 -0.0083 0.0216  0.0089  117 ASN   A N   
2542 C CA  . ASN   A 117 ? 0.1216 0.1186 0.1875 -0.0060 0.0231  0.0170  117 ASN   A CA  
2543 C C   . ASN   A 117 ? 0.1222 0.1306 0.1885 -0.0075 0.0261  0.0170  117 ASN   A C   
2544 O O   . ASN   A 117 ? 0.1345 0.1314 0.2231 -0.0092 0.0061  0.0303  117 ASN   A O   
2545 C CB  . ASN   A 117 ? 0.1203 0.1191 0.1879 -0.0066 0.0195  0.0157  117 ASN   A CB  
2546 C CG  . ASN   A 117 ? 0.1218 0.1150 0.1833 -0.0075 0.0219  0.0184  117 ASN   A CG  
2547 O OD1 . ASN   A 117 ? 0.1275 0.1348 0.2018 -0.0161 0.0264  0.0078  117 ASN   A OD1 
2548 N ND2 . ASN   A 117 ? 0.1166 0.1223 0.1922 -0.0017 0.0205  0.0094  117 ASN   A ND2 
2555 N N   . GLN   A 118 ? 0.1193 0.1269 0.1876 -0.0096 0.0137  0.0198  118 GLN   A N   
2556 C CA  . GLN   A 118 ? 0.1252 0.1392 0.1792 -0.0134 0.0048  0.0089  118 GLN   A CA  
2557 C C   . GLN   A 118 ? 0.1328 0.1430 0.1689 -0.0146 0.0030  0.0134  118 GLN   A C   
2558 O O   . GLN   A 118 ? 0.1354 0.1791 0.1900 -0.0022 -0.0039 0.0008  118 GLN   A O   
2559 C CB  . GLN   A 118 ? 0.1254 0.1383 0.1890 -0.0058 0.0154  0.0126  118 GLN   A CB  
2560 C CG  . GLN   A 118 ? 0.1216 0.1409 0.1967 -0.0066 0.0229  0.0154  118 GLN   A CG  
2561 C CD  . GLN   A 118 ? 0.1216 0.1418 0.2046 -0.0015 0.0155  0.0123  118 GLN   A CD  
2562 O OE1 . GLN   A 118 ? 0.1288 0.1492 0.2211 0.0049  0.0049  0.0008  118 GLN   A OE1 
2563 N NE2 . GLN   A 118 ? 0.1297 0.1367 0.1964 -0.0011 0.0033  0.0119  118 GLN   A NE2 
2572 N N   . HIS   A 119 ? 0.1361 0.1408 0.1550 -0.0112 0.0102  0.0163  119 HIS   A N   
2573 C CA  . HIS   A 119 ? 0.1402 0.1511 0.1627 -0.0140 0.0107  0.0249  119 HIS   A CA  
2574 C C   . HIS   A 119 ? 0.1540 0.1655 0.1702 -0.0129 0.0130  0.0263  119 HIS   A C   
2575 O O   . HIS   A 119 ? 0.1560 0.1664 0.1728 -0.0273 0.0143  0.0265  119 HIS   A O   
2576 C CB  . HIS   A 119 ? 0.1499 0.1528 0.1852 -0.0127 0.0248  0.0281  119 HIS   A CB  
2577 C CG  . HIS   A 119 ? 0.1525 0.1544 0.2135 -0.0055 0.0270  0.0324  119 HIS   A CG  
2578 N ND1 . HIS   A 119 ? 0.1634 0.1707 0.2638 -0.0143 0.0136  0.0145  119 HIS   A ND1 
2579 C CD2 . HIS   A 119 ? 0.1619 0.1577 0.2253 0.0091  0.0447  0.0449  119 HIS   A CD2 
2580 C CE1 . HIS   A 119 ? 0.1635 0.1644 0.2722 -0.0170 0.0348  0.0315  119 HIS   A CE1 
2581 N NE2 . HIS   A 119 ? 0.1714 0.1617 0.2600 0.0003  0.0565  0.0425  119 HIS   A NE2 
2589 N N   A GLU   A 120 ? 0.1610 0.1841 0.1758 -0.0084 0.0123  0.0398  120 GLU   A N   
2590 N N   B GLU   A 120 ? 0.1583 0.1814 0.1714 -0.0074 0.0143  0.0472  120 GLU   A N   
2591 C CA  A GLU   A 120 ? 0.1813 0.2063 0.2060 -0.0038 0.0197  0.0613  120 GLU   A CA  
2592 C CA  B GLU   A 120 ? 0.1777 0.2019 0.1998 -0.0022 0.0249  0.0753  120 GLU   A CA  
2593 C C   A GLU   A 120 ? 0.1693 0.1973 0.1816 -0.0128 0.0216  0.0567  120 GLU   A C   
2594 C C   B GLU   A 120 ? 0.1653 0.1906 0.1776 -0.0147 0.0250  0.0700  120 GLU   A C   
2595 O O   A GLU   A 120 ? 0.1678 0.1923 0.1923 -0.0112 0.0188  0.0503  120 GLU   A O   
2596 O O   B GLU   A 120 ? 0.1603 0.1771 0.1827 -0.0169 0.0247  0.0768  120 GLU   A O   
2597 C CB  A GLU   A 120 ? 0.2230 0.2456 0.2748 0.0058  0.0238  0.0824  120 GLU   A CB  
2598 C CB  B GLU   A 120 ? 0.2206 0.2433 0.2663 0.0102  0.0335  0.1019  120 GLU   A CB  
2599 C CG  A GLU   A 120 ? 0.2724 0.2853 0.3737 0.0151  0.0263  0.0785  120 GLU   A CG  
2600 C CG  B GLU   A 120 ? 0.2725 0.2858 0.3716 0.0210  0.0385  0.1006  120 GLU   A CG  
2601 C CD  A GLU   A 120 ? 0.3106 0.3173 0.4551 0.0231  0.0339  0.0682  120 GLU   A CD  
2602 C CD  B GLU   A 120 ? 0.3125 0.3201 0.4578 0.0297  0.0509  0.0926  120 GLU   A CD  
2603 O OE1 A GLU   A 120 ? 0.3257 0.3302 0.4834 0.0250  0.0373  0.0614  120 GLU   A OE1 
2604 O OE1 B GLU   A 120 ? 0.3293 0.3351 0.4919 0.0315  0.0539  0.0851  120 GLU   A OE1 
2605 O OE2 A GLU   A 120 ? 0.3252 0.3291 0.4865 0.0244  0.0331  0.0668  120 GLU   A OE2 
2606 O OE2 B GLU   A 120 ? 0.3267 0.3323 0.4871 0.0306  0.0551  0.0933  120 GLU   A OE2 
2619 N N   . VAL   A 121 ? 0.1617 0.1979 0.1631 -0.0174 0.0251  0.0495  121 VAL   A N   
2620 C CA  . VAL   A 121 ? 0.1638 0.2040 0.1476 -0.0188 0.0375  0.0493  121 VAL   A CA  
2621 C C   . VAL   A 121 ? 0.1525 0.1874 0.1437 -0.0226 0.0351  0.0244  121 VAL   A C   
2622 O O   . VAL   A 121 ? 0.1589 0.1891 0.1622 -0.0296 0.0219  0.0228  121 VAL   A O   
2623 C CB  . VAL   A 121 ? 0.2007 0.2427 0.1860 -0.0022 0.0440  0.0528  121 VAL   A CB  
2624 C CG1 . VAL   A 121 ? 0.2072 0.2598 0.1834 0.0057  0.0500  0.0487  121 VAL   A CG1 
2625 C CG2 . VAL   A 121 ? 0.2192 0.2576 0.2162 -0.0091 0.0313  0.0424  121 VAL   A CG2 
2636 N N   . LEU   A 122 ? 0.1453 0.1650 0.1513 -0.0296 0.0283  0.0175  122 LEU   A N   
2637 C CA  . LEU   A 122 ? 0.1501 0.1519 0.1579 -0.0271 0.0343  0.0153  122 LEU   A CA  
2638 C C   . LEU   A 122 ? 0.1437 0.1440 0.1530 -0.0308 0.0260  0.0122  122 LEU   A C   
2639 O O   . LEU   A 122 ? 0.1492 0.1482 0.1855 -0.0298 0.0147  0.0192  122 LEU   A O   
2640 C CB  . LEU   A 122 ? 0.1723 0.1567 0.1942 -0.0142 0.0260  0.0270  122 LEU   A CB  
2641 C CG  . LEU   A 122 ? 0.1828 0.1560 0.1791 -0.0144 0.0340  0.0191  122 LEU   A CG  
2642 C CD1 . LEU   A 122 ? 0.1934 0.1547 0.2011 -0.0238 0.0376  0.0146  122 LEU   A CD1 
2643 C CD2 . LEU   A 122 ? 0.1751 0.1441 0.1619 -0.0112 0.0447  0.0187  122 LEU   A CD2 
2655 N N   A LEU   A 123 ? 0.1463 0.1443 0.1535 -0.0270 0.0289  0.0099  123 LEU   A N   
2656 N N   B LEU   A 123 ? 0.1427 0.1447 0.1341 -0.0292 0.0243  0.0114  123 LEU   A N   
2657 C CA  A LEU   A 123 ? 0.1468 0.1402 0.1373 -0.0249 0.0261  0.0102  123 LEU   A CA  
2658 C CA  B LEU   A 123 ? 0.1446 0.1395 0.1190 -0.0291 0.0168  0.0062  123 LEU   A CA  
2659 C C   A LEU   A 123 ? 0.1360 0.1256 0.1350 -0.0265 0.0295  0.0153  123 LEU   A C   
2660 C C   B LEU   A 123 ? 0.1446 0.1354 0.1022 -0.0232 0.0128  -0.0009 123 LEU   A C   
2661 O O   A LEU   A 123 ? 0.1352 0.1229 0.1386 -0.0335 0.0330  -0.0001 123 LEU   A O   
2662 O O   B LEU   A 123 ? 0.1407 0.1438 0.0998 -0.0311 0.0147  -0.0168 123 LEU   A O   
2663 C CB  A LEU   A 123 ? 0.1587 0.1566 0.1291 -0.0225 0.0327  0.0078  123 LEU   A CB  
2664 C CB  B LEU   A 123 ? 0.1450 0.1472 0.1242 -0.0341 0.0152  0.0110  123 LEU   A CB  
2665 C CG  A LEU   A 123 ? 0.1637 0.1684 0.1349 -0.0174 0.0379  -0.0002 123 LEU   A CG  
2666 C CG  B LEU   A 123 ? 0.1486 0.1559 0.1282 -0.0323 0.0095  0.0083  123 LEU   A CG  
2667 C CD1 A LEU   A 123 ? 0.1647 0.1724 0.1337 -0.0122 0.0379  -0.0023 123 LEU   A CD1 
2668 C CD1 B LEU   A 123 ? 0.1515 0.1601 0.1434 -0.0258 0.0058  -0.0012 123 LEU   A CD1 
2669 C CD2 A LEU   A 123 ? 0.1674 0.1757 0.1351 -0.0139 0.0304  -0.0025 123 LEU   A CD2 
2670 C CD2 B LEU   A 123 ? 0.1522 0.1647 0.1327 -0.0295 0.0003  -0.0037 123 LEU   A CD2 
2693 N N   A ALA   A 124 ? 0.1219 0.1186 0.1500 -0.0233 0.0366  0.0221  124 ALA   A N   
2694 N N   B ALA   A 124 ? 0.1417 0.1248 0.1165 -0.0141 0.0171  0.0070  124 ALA   A N   
2695 C CA  A ALA   A 124 ? 0.1069 0.1165 0.1417 -0.0134 0.0348  0.0221  124 ALA   A CA  
2696 C CA  B ALA   A 124 ? 0.1414 0.1268 0.1350 -0.0139 0.0049  0.0075  124 ALA   A CA  
2697 C C   A ALA   A 124 ? 0.1037 0.1254 0.1383 -0.0136 0.0360  0.0168  124 ALA   A C   
2698 C C   B ALA   A 124 ? 0.1321 0.1195 0.1419 -0.0107 0.0066  0.0121  124 ALA   A C   
2699 O O   A ALA   A 124 ? 0.1033 0.1331 0.1448 -0.0170 0.0410  0.0276  124 ALA   A O   
2700 O O   B ALA   A 124 ? 0.1339 0.1232 0.1593 0.0013  -0.0054 0.0206  124 ALA   A O   
2701 C CB  A ALA   A 124 ? 0.1042 0.1125 0.1423 -0.0108 0.0256  0.0171  124 ALA   A CB  
2702 C CB  B ALA   A 124 ? 0.1531 0.1312 0.1598 -0.0161 0.0034  0.0016  124 ALA   A CB  
2713 N N   A PRO   A 125 ? 0.1000 0.1286 0.1425 -0.0077 0.0296  0.0165  125 PRO   A N   
2714 N N   B PRO   A 125 ? 0.1201 0.1166 0.1246 -0.0090 0.0071  0.0144  125 PRO   A N   
2715 C CA  A PRO   A 125 ? 0.1117 0.1329 0.1486 -0.0053 0.0161  0.0101  125 PRO   A CA  
2716 C CA  B PRO   A 125 ? 0.1206 0.1172 0.1294 -0.0120 0.0097  0.0061  125 PRO   A CA  
2717 C C   A PRO   A 125 ? 0.1072 0.1369 0.1488 -0.0142 0.0197  0.0117  125 PRO   A C   
2718 C C   B PRO   A 125 ? 0.1217 0.1185 0.1280 -0.0104 0.0002  0.0042  125 PRO   A C   
2719 O O   A PRO   A 125 ? 0.1147 0.1346 0.1598 -0.0091 0.0147  0.0029  125 PRO   A O   
2720 O O   B PRO   A 125 ? 0.1252 0.1135 0.1416 -0.0067 -0.0026 0.0072  125 PRO   A O   
2721 C CB  A PRO   A 125 ? 0.1175 0.1336 0.1497 -0.0047 0.0103  0.0085  125 PRO   A CB  
2722 C CB  B PRO   A 125 ? 0.1188 0.1174 0.1258 -0.0110 0.0147  0.0076  125 PRO   A CB  
2723 C CG  A PRO   A 125 ? 0.1191 0.1275 0.1553 -0.0002 0.0094  0.0202  125 PRO   A CG  
2724 C CG  B PRO   A 125 ? 0.1141 0.1135 0.1243 -0.0054 0.0228  0.0138  125 PRO   A CG  
2725 C CD  A PRO   A 125 ? 0.1085 0.1322 0.1481 -0.0048 0.0206  0.0226  125 PRO   A CD  
2726 C CD  B PRO   A 125 ? 0.1090 0.1087 0.1224 -0.0101 0.0229  0.0198  125 PRO   A CD  
2741 N N   A LEU   A 126 ? 0.1082 0.1452 0.1626 -0.0127 0.0226  0.0094  126 LEU   A N   
2742 N N   B LEU   A 126 ? 0.1266 0.1308 0.1265 -0.0031 -0.0005 -0.0029 126 LEU   A N   
2743 C CA  A LEU   A 126 ? 0.1150 0.1489 0.1677 -0.0107 0.0145  0.0107  126 LEU   A CA  
2744 C CA  B LEU   A 126 ? 0.1263 0.1298 0.1442 -0.0081 0.0019  -0.0093 126 LEU   A CA  
2745 C C   A LEU   A 126 ? 0.1189 0.1423 0.1518 -0.0046 0.0028  0.0048  126 LEU   A C   
2746 C C   B LEU   A 126 ? 0.1333 0.1257 0.1334 -0.0019 0.0040  -0.0133 126 LEU   A C   
2747 O O   A LEU   A 126 ? 0.1257 0.1400 0.1578 0.0048  0.0113  0.0001  126 LEU   A O   
2748 O O   B LEU   A 126 ? 0.1524 0.1270 0.1704 0.0014  0.0099  -0.0032 126 LEU   A O   
2749 C CB  A LEU   A 126 ? 0.1224 0.1620 0.1800 -0.0127 0.0108  0.0113  126 LEU   A CB  
2750 C CB  B LEU   A 126 ? 0.1320 0.1447 0.1664 -0.0148 -0.0108 -0.0080 126 LEU   A CB  
2751 C CG  A LEU   A 126 ? 0.1300 0.1751 0.1819 -0.0166 0.0189  0.0089  126 LEU   A CG  
2752 C CG  B LEU   A 126 ? 0.1397 0.1583 0.1705 -0.0181 -0.0171 -0.0034 126 LEU   A CG  
2753 C CD1 A LEU   A 126 ? 0.1355 0.1862 0.2002 -0.0173 0.0093  0.0140  126 LEU   A CD1 
2754 C CD1 B LEU   A 126 ? 0.1444 0.1631 0.1757 -0.0215 -0.0217 -0.0122 126 LEU   A CD1 
2755 C CD2 A LEU   A 126 ? 0.1346 0.1687 0.1685 -0.0268 0.0194  0.0185  126 LEU   A CD2 
2756 C CD2 B LEU   A 126 ? 0.1390 0.1623 0.1706 -0.0261 -0.0138 0.0086  126 LEU   A CD2 
2779 N N   A LEU   A 127 ? 0.1152 0.1423 0.1437 0.0047  0.0014  0.0141  127 LEU   A N   
2780 N N   B LEU   A 127 ? 0.1306 0.1343 0.1433 0.0043  0.0014  -0.0137 127 LEU   A N   
2781 C CA  A LEU   A 127 ? 0.1127 0.1377 0.1342 0.0031  -0.0014 0.0130  127 LEU   A CA  
2782 C CA  B LEU   A 127 ? 0.1328 0.1349 0.1416 0.0009  -0.0110 -0.0146 127 LEU   A CA  
2783 C C   A LEU   A 127 ? 0.1161 0.1344 0.1386 -0.0015 -0.0050 0.0003  127 LEU   A C   
2784 C C   B LEU   A 127 ? 0.1334 0.1240 0.1299 -0.0033 -0.0091 -0.0131 127 LEU   A C   
2785 O O   A LEU   A 127 ? 0.1289 0.1359 0.1318 -0.0096 -0.0016 0.0074  127 LEU   A O   
2786 O O   B LEU   A 127 ? 0.1419 0.1229 0.1325 -0.0032 -0.0092 -0.0131 127 LEU   A O   
2787 C CB  A LEU   A 127 ? 0.1157 0.1420 0.1302 0.0055  0.0007  0.0090  127 LEU   A CB  
2788 C CB  B LEU   A 127 ? 0.1332 0.1549 0.1508 0.0060  -0.0015 -0.0076 127 LEU   A CB  
2789 C CG  A LEU   A 127 ? 0.1204 0.1561 0.1430 0.0102  -0.0032 0.0088  127 LEU   A CG  
2790 C CG  B LEU   A 127 ? 0.1315 0.1754 0.1702 0.0145  -0.0032 0.0103  127 LEU   A CG  
2791 C CD1 A LEU   A 127 ? 0.1284 0.1520 0.1583 0.0115  -0.0080 0.0061  127 LEU   A CD1 
2792 C CD1 B LEU   A 127 ? 0.1396 0.1774 0.1862 0.0127  0.0024  0.0232  127 LEU   A CD1 
2793 C CD2 A LEU   A 127 ? 0.1231 0.1652 0.1469 0.0179  -0.0118 -0.0004 127 LEU   A CD2 
2794 C CD2 B LEU   A 127 ? 0.1354 0.1883 0.1632 0.0162  -0.0138 0.0197  127 LEU   A CD2 
2817 N N   A SER   A 128 ? 0.1157 0.1359 0.1440 -0.0038 -0.0161 0.0055  128 SER   A N   
2818 N N   B SER   A 128 ? 0.1333 0.1276 0.1262 -0.0029 -0.0034 -0.0021 128 SER   A N   
2819 C CA  A SER   A 128 ? 0.1274 0.1367 0.1510 -0.0082 -0.0140 0.0041  128 SER   A CA  
2820 C CA  B SER   A 128 ? 0.1455 0.1354 0.1279 -0.0006 -0.0019 0.0032  128 SER   A CA  
2821 C C   A SER   A 128 ? 0.1298 0.1284 0.1495 -0.0128 -0.0173 0.0095  128 SER   A C   
2822 C C   B SER   A 128 ? 0.1461 0.1397 0.1404 -0.0008 -0.0034 0.0027  128 SER   A C   
2823 O O   A SER   A 128 ? 0.1315 0.1252 0.1499 -0.0225 -0.0158 0.0174  128 SER   A O   
2824 O O   B SER   A 128 ? 0.1606 0.1565 0.1699 -0.0027 -0.0009 0.0048  128 SER   A O   
2825 C CB  A SER   A 128 ? 0.1269 0.1409 0.1449 -0.0116 -0.0152 0.0077  128 SER   A CB  
2826 C CB  B SER   A 128 ? 0.1495 0.1393 0.1257 0.0034  -0.0108 -0.0014 128 SER   A CB  
2827 O OG  A SER   A 128 ? 0.1256 0.1464 0.1564 -0.0130 -0.0046 0.0156  128 SER   A OG  
2828 O OG  B SER   A 128 ? 0.1537 0.1371 0.1329 0.0064  -0.0080 -0.0054 128 SER   A OG  
2839 N N   A ALA   A 129 ? 0.1286 0.1291 0.1621 -0.0091 -0.0145 0.0144  129 ALA   A N   
2840 N N   B ALA   A 129 ? 0.1341 0.1386 0.1496 0.0037  -0.0035 0.0115  129 ALA   A N   
2841 C CA  A ALA   A 129 ? 0.1354 0.1404 0.1748 -0.0065 -0.0017 0.0185  129 ALA   A CA  
2842 C CA  B ALA   A 129 ? 0.1327 0.1313 0.1485 -0.0035 -0.0063 0.0123  129 ALA   A CA  
2843 C C   A ALA   A 129 ? 0.1421 0.1420 0.1553 -0.0016 0.0058  0.0138  129 ALA   A C   
2844 C C   B ALA   A 129 ? 0.1349 0.1305 0.1300 -0.0088 -0.0163 0.0124  129 ALA   A C   
2845 O O   A ALA   A 129 ? 0.1486 0.1479 0.1559 -0.0069 0.0013  0.0250  129 ALA   A O   
2846 O O   B ALA   A 129 ? 0.1370 0.1322 0.1403 -0.0164 -0.0180 0.0097  129 ALA   A O   
2847 C CB  A ALA   A 129 ? 0.1351 0.1549 0.1834 -0.0070 0.0049  0.0179  129 ALA   A CB  
2848 C CB  B ALA   A 129 ? 0.1373 0.1303 0.1700 0.0002  0.0009  0.0144  129 ALA   A CB  
2859 N N   A GLY   A 130 ? 0.1430 0.1398 0.1576 0.0037  0.0114  0.0090  130 GLY   A N   
2860 N N   B GLY   A 130 ? 0.1411 0.1338 0.1347 -0.0078 -0.0243 0.0192  130 GLY   A N   
2861 C CA  A GLY   A 130 ? 0.1475 0.1427 0.1407 0.0073  0.0161  0.0007  130 GLY   A CA  
2862 C CA  B GLY   A 130 ? 0.1556 0.1410 0.1243 -0.0066 -0.0296 0.0197  130 GLY   A CA  
2863 C C   A GLY   A 130 ? 0.1506 0.1383 0.1322 0.0077  0.0130  -0.0103 130 GLY   A C   
2864 C C   B GLY   A 130 ? 0.1674 0.1446 0.1283 -0.0162 -0.0392 0.0134  130 GLY   A C   
2865 O O   A GLY   A 130 ? 0.1559 0.1422 0.1303 0.0040  0.0058  -0.0098 130 GLY   A O   
2866 O O   B GLY   A 130 ? 0.1679 0.1452 0.1200 -0.0254 -0.0373 0.0169  130 GLY   A O   
2873 N N   A ILE   A 131 ? 0.1552 0.1302 0.1315 0.0018  0.0061  -0.0059 131 ILE   A N   
2874 N N   B ILE   A 131 ? 0.1772 0.1468 0.1580 -0.0236 -0.0447 0.0202  131 ILE   A N   
2875 C CA  A ILE   A 131 ? 0.1570 0.1338 0.1046 -0.0043 -0.0060 -0.0075 131 ILE   A CA  
2876 C CA  B ILE   A 131 ? 0.1893 0.1606 0.1863 -0.0298 -0.0414 0.0313  131 ILE   A CA  
2877 C C   A ILE   A 131 ? 0.1502 0.1287 0.1088 -0.0011 -0.0073 -0.0036 131 ILE   A C   
2878 C C   B ILE   A 131 ? 0.1817 0.1721 0.1508 -0.0208 -0.0345 0.0497  131 ILE   A C   
2879 O O   A ILE   A 131 ? 0.1550 0.1127 0.1079 0.0055  -0.0049 -0.0078 131 ILE   A O   
2880 O O   B ILE   A 131 ? 0.1859 0.1906 0.1552 -0.0107 -0.0275 0.0576  131 ILE   A O   
2881 C CB  A ILE   A 131 ? 0.1739 0.1491 0.1226 -0.0156 -0.0111 -0.0099 131 ILE   A CB  
2882 C CB  B ILE   A 131 ? 0.2126 0.1724 0.2343 -0.0382 -0.0452 0.0331  131 ILE   A CB  
2883 C CG1 A ILE   A 131 ? 0.1792 0.1711 0.1316 -0.0234 -0.0189 -0.0028 131 ILE   A CG1 
2884 C CG1 B ILE   A 131 ? 0.2225 0.1914 0.2693 -0.0434 -0.0450 0.0396  131 ILE   A CG1 
2885 C CG2 A ILE   A 131 ? 0.1870 0.1399 0.1268 -0.0069 -0.0054 -0.0195 131 ILE   A CG2 
2886 C CG2 B ILE   A 131 ? 0.2257 0.1572 0.2386 -0.0310 -0.0441 0.0388  131 ILE   A CG2 
2887 C CD1 A ILE   A 131 ? 0.1849 0.1810 0.1487 -0.0242 -0.0203 -0.0051 131 ILE   A CD1 
2888 C CD1 B ILE   A 131 ? 0.2300 0.2030 0.2860 -0.0460 -0.0490 0.0424  131 ILE   A CD1 
2911 N N   A PHE   A 132 ? 0.1469 0.1362 0.1110 0.0007  0.0011  0.0012  132 PHE   A N   
2912 N N   B PHE   A 132 ? 0.1784 0.1659 0.1326 -0.0208 -0.0227 0.0395  132 PHE   A N   
2913 C CA  A PHE   A 132 ? 0.1503 0.1457 0.1053 -0.0045 0.0006  -0.0041 132 PHE   A CA  
2914 C CA  B PHE   A 132 ? 0.1821 0.1752 0.1219 -0.0159 -0.0220 0.0227  132 PHE   A CA  
2915 C C   A PHE   A 132 ? 0.1552 0.1558 0.1128 0.0058  0.0066  -0.0087 132 PHE   A C   
2916 C C   B PHE   A 132 ? 0.1874 0.1946 0.1293 -0.0089 -0.0259 0.0165  132 PHE   A C   
2917 O O   A PHE   A 132 ? 0.1649 0.1678 0.1300 0.0153  0.0036  -0.0260 132 PHE   A O   
2918 O O   B PHE   A 132 ? 0.2011 0.1997 0.1495 -0.0063 -0.0288 0.0143  132 PHE   A O   
2919 C CB  A PHE   A 132 ? 0.1490 0.1370 0.1087 -0.0081 -0.0040 -0.0008 132 PHE   A CB  
2920 C CB  B PHE   A 132 ? 0.1791 0.1684 0.1218 -0.0092 -0.0234 0.0188  132 PHE   A CB  
2921 C CG  A PHE   A 132 ? 0.1511 0.1384 0.1218 -0.0001 -0.0136 0.0032  132 PHE   A CG  
2922 C CG  B PHE   A 132 ? 0.1781 0.1635 0.1279 0.0029  -0.0247 0.0131  132 PHE   A CG  
2923 C CD1 A PHE   A 132 ? 0.1551 0.1481 0.1539 0.0036  -0.0225 -0.0050 132 PHE   A CD1 
2924 C CD1 B PHE   A 132 ? 0.1766 0.1716 0.1478 0.0078  -0.0300 -0.0022 132 PHE   A CD1 
2925 C CD2 A PHE   A 132 ? 0.1528 0.1402 0.1450 0.0007  -0.0141 0.0000  132 PHE   A CD2 
2926 C CD2 B PHE   A 132 ? 0.1765 0.1643 0.1359 0.0082  -0.0214 0.0144  132 PHE   A CD2 
2927 C CE1 A PHE   A 132 ? 0.1616 0.1556 0.1747 0.0027  -0.0223 -0.0067 132 PHE   A CE1 
2928 C CE1 B PHE   A 132 ? 0.1763 0.1766 0.1453 0.0070  -0.0193 -0.0076 132 PHE   A CE1 
2929 C CE2 A PHE   A 132 ? 0.1539 0.1471 0.1633 0.0042  -0.0222 -0.0012 132 PHE   A CE2 
2930 C CE2 B PHE   A 132 ? 0.1741 0.1657 0.1246 0.0121  -0.0203 0.0197  132 PHE   A CE2 
2931 C CZ  A PHE   A 132 ? 0.1577 0.1542 0.1737 0.0023  -0.0266 -0.0048 132 PHE   A CZ  
2932 C CZ  B PHE   A 132 ? 0.1720 0.1710 0.1272 0.0080  -0.0190 0.0081  132 PHE   A CZ  
2951 N N   A GLY   A 133 ? 0.1550 0.1571 0.1215 0.0015  -0.0043 -0.0069 133 GLY   A N   
2952 N N   B GLY   A 133 ? 0.1862 0.2111 0.1372 -0.0106 -0.0338 0.0009  133 GLY   A N   
2953 C CA  A GLY   A 133 ? 0.1619 0.1564 0.1315 0.0008  -0.0076 -0.0150 133 GLY   A CA  
2954 C CA  B GLY   A 133 ? 0.1900 0.2296 0.1550 -0.0100 -0.0365 -0.0084 133 GLY   A CA  
2955 C C   A GLY   A 133 ? 0.1716 0.1622 0.1351 0.0012  -0.0159 -0.0202 133 GLY   A C   
2956 C C   B GLY   A 133 ? 0.1912 0.2438 0.1678 -0.0121 -0.0340 -0.0191 133 GLY   A C   
2957 O O   A GLY   A 133 ? 0.1842 0.1665 0.1383 0.0101  -0.0239 -0.0376 133 GLY   A O   
2958 O O   B GLY   A 133 ? 0.2060 0.2554 0.2031 -0.0062 -0.0262 -0.0341 133 GLY   A O   
2965 N N   A ALA   A 134 ? 0.1716 0.1549 0.1365 0.0032  -0.0015 -0.0264 134 ALA   A N   
2966 N N   B ALA   A 134 ? 0.1863 0.2442 0.1671 -0.0224 -0.0251 -0.0244 134 ALA   A N   
2967 C CA  A ALA   A 134 ? 0.1704 0.1520 0.1433 0.0070  0.0031  -0.0248 134 ALA   A CA  
2968 C CA  B ALA   A 134 ? 0.1808 0.2476 0.1713 -0.0255 -0.0223 -0.0311 134 ALA   A CA  
2969 C C   A ALA   A 134 ? 0.1685 0.1507 0.1401 -0.0004 0.0055  -0.0089 134 ALA   A C   
2970 C C   B ALA   A 134 ? 0.1791 0.2555 0.1635 -0.0274 -0.0066 -0.0421 134 ALA   A C   
2971 O O   A ALA   A 134 ? 0.1778 0.1514 0.1650 -0.0025 0.0209  -0.0098 134 ALA   A O   
2972 O O   B ALA   A 134 ? 0.1902 0.2577 0.1779 -0.0251 -0.0013 -0.0512 134 ALA   A O   
2973 C CB  A ALA   A 134 ? 0.1727 0.1534 0.1805 0.0159  0.0054  -0.0237 134 ALA   A CB  
2974 C CB  B ALA   A 134 ? 0.1833 0.2405 0.1850 -0.0259 -0.0234 -0.0265 134 ALA   A CB  
2985 N N   A ASP   A 135 ? 0.1649 0.1582 0.1294 -0.0093 -0.0033 -0.0047 135 ASP   A N   
2986 N N   B ASP   A 135 ? 0.1765 0.2592 0.1521 -0.0256 -0.0008 -0.0320 135 ASP   A N   
2987 C CA  A ASP   A 135 ? 0.1615 0.1693 0.1643 -0.0171 -0.0170 -0.0110 135 ASP   A CA  
2988 C CA  B ASP   A 135 ? 0.1794 0.2621 0.1558 -0.0236 -0.0018 -0.0260 135 ASP   A CA  
2989 C C   A ASP   A 135 ? 0.1536 0.1649 0.1602 -0.0121 -0.0143 -0.0091 135 ASP   A C   
2990 C C   B ASP   A 135 ? 0.1744 0.2485 0.1393 -0.0133 -0.0022 -0.0176 135 ASP   A C   
2991 O O   A ASP   A 135 ? 0.1504 0.1551 0.1652 -0.0113 -0.0158 -0.0004 135 ASP   A O   
2992 O O   B ASP   A 135 ? 0.1761 0.2488 0.1486 -0.0079 -0.0009 -0.0072 135 ASP   A O   
2993 C CB  A ASP   A 135 ? 0.1809 0.1938 0.2190 -0.0334 -0.0303 -0.0162 135 ASP   A CB  
2994 C CB  B ASP   A 135 ? 0.1935 0.2774 0.1932 -0.0331 0.0004  -0.0327 135 ASP   A CB  
2995 C CG  A ASP   A 135 ? 0.1951 0.2186 0.2615 -0.0448 -0.0369 -0.0274 135 ASP   A CG  
2996 C CG  B ASP   A 135 ? 0.2057 0.2894 0.2314 -0.0432 -0.0017 -0.0387 135 ASP   A CG  
2997 O OD1 A ASP   A 135 ? 0.1942 0.2288 0.2732 -0.0408 -0.0404 -0.0176 135 ASP   A OD1 
2998 O OD1 B ASP   A 135 ? 0.2076 0.2933 0.2352 -0.0527 -0.0127 -0.0390 135 ASP   A OD1 
2999 O OD2 A ASP   A 135 ? 0.2104 0.2348 0.2941 -0.0492 -0.0275 -0.0452 135 ASP   A OD2 
3000 O OD2 B ASP   A 135 ? 0.2205 0.2926 0.2677 -0.0447 0.0096  -0.0421 135 ASP   A OD2 
3009 N N   A PRO   A 136 ? 0.1450 0.1640 0.1600 -0.0085 -0.0034 -0.0077 136 PRO   A N   
3010 N N   B PRO   A 136 ? 0.1650 0.2350 0.1402 -0.0083 -0.0029 -0.0136 136 PRO   A N   
3011 C CA  A PRO   A 136 ? 0.1404 0.1661 0.1674 -0.0126 0.0008  -0.0122 136 PRO   A CA  
3012 C CA  B PRO   A 136 ? 0.1569 0.2212 0.1473 -0.0120 -0.0064 -0.0170 136 PRO   A CA  
3013 C C   A PRO   A 136 ? 0.1295 0.1654 0.1696 -0.0121 0.0109  -0.0103 136 PRO   A C   
3014 C C   B PRO   A 136 ? 0.1435 0.2088 0.1515 -0.0056 -0.0131 -0.0213 136 PRO   A C   
3015 O O   A PRO   A 136 ? 0.1282 0.1627 0.1661 -0.0100 0.0259  -0.0116 136 PRO   A O   
3016 O O   B PRO   A 136 ? 0.1460 0.2064 0.1499 -0.0039 -0.0130 -0.0176 136 PRO   A O   
3017 C CB  A PRO   A 136 ? 0.1516 0.1623 0.1761 -0.0090 -0.0066 -0.0108 136 PRO   A CB  
3018 C CB  B PRO   A 136 ? 0.1684 0.2247 0.1525 -0.0077 -0.0045 -0.0126 136 PRO   A CB  
3019 C CG  A PRO   A 136 ? 0.1630 0.1663 0.1877 -0.0041 -0.0058 -0.0097 136 PRO   A CG  
3020 C CG  B PRO   A 136 ? 0.1768 0.2316 0.1558 -0.0044 -0.0089 -0.0182 136 PRO   A CG  
3021 C CD  A PRO   A 136 ? 0.1576 0.1647 0.1832 -0.0039 0.0002  -0.0027 136 PRO   A CD  
3022 C CD  B PRO   A 136 ? 0.1764 0.2340 0.1486 -0.0048 -0.0034 -0.0164 136 PRO   A CD  
3037 N N   A ILE   A 137 ? 0.1260 0.1655 0.1883 -0.0109 0.0063  -0.0178 137 ILE   A N   
3038 N N   B ILE   A 137 ? 0.1326 0.2030 0.1815 -0.0046 -0.0201 -0.0240 137 ILE   A N   
3039 C CA  A ILE   A 137 ? 0.1331 0.1673 0.1984 -0.0125 0.0044  -0.0273 137 ILE   A CA  
3040 C CA  B ILE   A 137 ? 0.1336 0.2076 0.2044 -0.0091 -0.0189 -0.0202 137 ILE   A CA  
3041 C C   A ILE   A 137 ? 0.1338 0.1626 0.1977 -0.0127 0.0081  -0.0282 137 ILE   A C   
3042 C C   B ILE   A 137 ? 0.1413 0.2048 0.1969 -0.0118 -0.0184 -0.0177 137 ILE   A C   
3043 O O   A ILE   A 137 ? 0.1349 0.1638 0.2091 -0.0168 0.0206  -0.0183 137 ILE   A O   
3044 O O   B ILE   A 137 ? 0.1462 0.2019 0.2002 -0.0160 -0.0120 -0.0183 137 ILE   A O   
3045 C CB  A ILE   A 137 ? 0.1439 0.1755 0.2161 -0.0133 -0.0047 -0.0357 137 ILE   A CB  
3046 C CB  B ILE   A 137 ? 0.1305 0.2157 0.2270 -0.0087 -0.0166 -0.0306 137 ILE   A CB  
3047 C CG1 A ILE   A 137 ? 0.1483 0.1925 0.2371 -0.0056 -0.0093 -0.0279 137 ILE   A CG1 
3048 C CG1 B ILE   A 137 ? 0.1329 0.2199 0.2359 -0.0008 -0.0155 -0.0371 137 ILE   A CG1 
3049 C CG2 A ILE   A 137 ? 0.1557 0.1729 0.2325 -0.0130 -0.0128 -0.0435 137 ILE   A CG2 
3050 C CG2 B ILE   A 137 ? 0.1309 0.2176 0.2375 -0.0077 -0.0145 -0.0376 137 ILE   A CG2 
3051 C CD1 A ILE   A 137 ? 0.1579 0.2040 0.2540 0.0022  -0.0116 -0.0244 137 ILE   A CD1 
3052 C CD1 B ILE   A 137 ? 0.1380 0.2248 0.2526 0.0101  -0.0110 -0.0431 137 ILE   A CD1 
3075 N N   A HIS   A 138 ? 0.1325 0.1634 0.1835 -0.0153 0.0106  -0.0349 138 HIS   A N   
3076 N N   B HIS   A 138 ? 0.1439 0.2013 0.1777 -0.0102 -0.0147 -0.0221 138 HIS   A N   
3077 C CA  A HIS   A 138 ? 0.1360 0.1586 0.1700 -0.0099 0.0112  -0.0298 138 HIS   A CA  
3078 C CA  B HIS   A 138 ? 0.1542 0.2011 0.1697 -0.0041 -0.0018 -0.0324 138 HIS   A CA  
3079 C C   A HIS   A 138 ? 0.1290 0.1511 0.1777 -0.0028 0.0089  -0.0204 138 HIS   A C   
3080 C C   B HIS   A 138 ? 0.1412 0.1850 0.1643 -0.0087 0.0030  -0.0231 138 HIS   A C   
3081 O O   A HIS   A 138 ? 0.1345 0.1504 0.1845 -0.0052 0.0071  -0.0165 138 HIS   A O   
3082 O O   B HIS   A 138 ? 0.1443 0.1854 0.1676 -0.0156 0.0012  -0.0154 138 HIS   A O   
3083 C CB  A HIS   A 138 ? 0.1363 0.1631 0.1591 -0.0078 0.0109  -0.0468 138 HIS   A CB  
3084 C CB  B HIS   A 138 ? 0.1783 0.2139 0.1798 -0.0072 -0.0105 -0.0358 138 HIS   A CB  
3085 C CG  A HIS   A 138 ? 0.1472 0.1693 0.1720 -0.0149 0.0061  -0.0566 138 HIS   A CG  
3086 C CG  B HIS   A 138 ? 0.1963 0.2239 0.2019 -0.0033 -0.0065 -0.0434 138 HIS   A CG  
3087 N ND1 A HIS   A 138 ? 0.1567 0.1756 0.2000 -0.0146 0.0057  -0.0603 138 HIS   A ND1 
3088 N ND1 B HIS   A 138 ? 0.2043 0.2280 0.2155 -0.0013 0.0019  -0.0433 138 HIS   A ND1 
3089 C CD2 A HIS   A 138 ? 0.1500 0.1702 0.1762 -0.0135 0.0095  -0.0601 138 HIS   A CD2 
3090 C CD2 B HIS   A 138 ? 0.2046 0.2310 0.2152 -0.0013 0.0016  -0.0418 138 HIS   A CD2 
3091 C CE1 A HIS   A 138 ? 0.1578 0.1774 0.1970 -0.0095 0.0056  -0.0656 138 HIS   A CE1 
3092 C CE1 B HIS   A 138 ? 0.2101 0.2320 0.2252 0.0018  0.0055  -0.0430 138 HIS   A CE1 
3093 N NE2 A HIS   A 138 ? 0.1547 0.1752 0.1788 -0.0042 0.0102  -0.0699 138 HIS   A NE2 
3094 N NE2 B HIS   A 138 ? 0.2087 0.2335 0.2164 0.0010  0.0103  -0.0433 138 HIS   A NE2 
3109 N N   A SER   A 139 ? 0.1224 0.1433 0.1677 -0.0037 0.0095  -0.0143 139 SER   A N   
3110 N N   B SER   A 139 ? 0.1312 0.1730 0.1558 -0.0032 0.0002  -0.0160 139 SER   A N   
3111 C CA  A SER   A 139 ? 0.1179 0.1515 0.1644 -0.0049 0.0135  -0.0142 139 SER   A CA  
3112 C CA  B SER   A 139 ? 0.1249 0.1627 0.1444 -0.0080 0.0067  -0.0036 139 SER   A CA  
3113 C C   A SER   A 139 ? 0.1181 0.1549 0.1733 -0.0147 0.0105  -0.0083 139 SER   A C   
3114 C C   B SER   A 139 ? 0.1208 0.1576 0.1549 -0.0213 0.0112  -0.0007 139 SER   A C   
3115 O O   A SER   A 139 ? 0.1120 0.1466 0.1873 -0.0190 0.0076  0.0052  139 SER   A O   
3116 O O   B SER   A 139 ? 0.1121 0.1498 0.1550 -0.0285 0.0165  -0.0054 139 SER   A O   
3117 C CB  A SER   A 139 ? 0.1148 0.1504 0.1519 -0.0055 0.0032  -0.0161 139 SER   A CB  
3118 C CB  B SER   A 139 ? 0.1148 0.1538 0.1258 0.0062  0.0114  -0.0135 139 SER   A CB  
3119 O OG  A SER   A 139 ? 0.1212 0.1473 0.1563 -0.0177 0.0097  -0.0062 139 SER   A OG  
3120 O OG  B SER   A 139 ? 0.1146 0.1394 0.1284 0.0020  0.0127  -0.0045 139 SER   A OG  
3131 N N   . LEU   A 140 ? 0.1206 0.1651 0.1678 -0.0169 0.0071  0.0094  140 LEU   A N   
3132 C CA  . LEU   A 140 ? 0.1233 0.1569 0.1781 -0.0174 0.0064  0.0021  140 LEU   A CA  
3133 C C   . LEU   A 140 ? 0.1118 0.1655 0.1839 -0.0196 0.0110  -0.0081 140 LEU   A C   
3134 O O   . LEU   A 140 ? 0.1167 0.1628 0.2122 -0.0147 0.0139  -0.0058 140 LEU   A O   
3135 C CB  . LEU   A 140 ? 0.1210 0.1612 0.1795 -0.0181 0.0155  0.0095  140 LEU   A CB  
3136 C CG  . LEU   A 140 ? 0.1260 0.1725 0.1947 -0.0256 0.0248  0.0152  140 LEU   A CG  
3137 C CD1 . LEU   A 140 ? 0.1303 0.1727 0.2054 -0.0238 0.0259  0.0185  140 LEU   A CD1 
3138 C CD2 . LEU   A 140 ? 0.1288 0.1879 0.2172 -0.0160 0.0378  0.0225  140 LEU   A CD2 
3151 N N   . ARG   A 141 ? 0.1191 0.1752 0.2027 -0.0244 0.0131  -0.0198 141 ARG   A N   
3152 C CA  . ARG   A 141 ? 0.1384 0.1936 0.2241 -0.0338 0.0039  -0.0382 141 ARG   A CA  
3153 C C   . ARG   A 141 ? 0.1375 0.1792 0.2175 -0.0243 0.0044  -0.0350 141 ARG   A C   
3154 O O   . ARG   A 141 ? 0.1357 0.1734 0.2322 -0.0229 0.0164  -0.0386 141 ARG   A O   
3155 C CB  . ARG   A 141 ? 0.1528 0.2165 0.2438 -0.0419 -0.0007 -0.0485 141 ARG   A CB  
3156 C CG  . ARG   A 141 ? 0.1802 0.2349 0.2712 -0.0460 0.0079  -0.0532 141 ARG   A CG  
3157 C CD  . ARG   A 141 ? 0.2014 0.2496 0.2907 -0.0504 0.0108  -0.0493 141 ARG   A CD  
3158 N NE  . ARG   A 141 ? 0.2000 0.2608 0.3063 -0.0530 0.0068  -0.0363 141 ARG   A NE  
3159 C CZ  . ARG   A 141 ? 0.1980 0.2755 0.3134 -0.0597 0.0083  -0.0209 141 ARG   A CZ  
3160 N NH1 . ARG   A 141 ? 0.1923 0.2807 0.3007 -0.0617 0.0234  -0.0290 141 ARG   A NH1 
3161 N NH2 . ARG   A 141 ? 0.2065 0.2832 0.3335 -0.0546 0.0011  -0.0069 141 ARG   A NH2 
3175 N N   . VAL   A 142 ? 0.1255 0.1766 0.2094 -0.0234 0.0118  -0.0341 142 VAL   A N   
3176 C CA  . VAL   A 142 ? 0.1318 0.1689 0.2113 -0.0189 0.0155  -0.0279 142 VAL   A CA  
3177 C C   . VAL   A 142 ? 0.1121 0.1538 0.2062 -0.0224 0.0257  -0.0166 142 VAL   A C   
3178 O O   . VAL   A 142 ? 0.1243 0.1491 0.2113 -0.0085 0.0201  -0.0178 142 VAL   A O   
3179 C CB  . VAL   A 142 ? 0.1392 0.1797 0.2088 -0.0195 0.0204  -0.0298 142 VAL   A CB  
3180 C CG1 . VAL   A 142 ? 0.1391 0.1746 0.2005 -0.0201 0.0274  -0.0248 142 VAL   A CG1 
3181 C CG2 . VAL   A 142 ? 0.1530 0.1927 0.2240 -0.0094 0.0268  -0.0246 142 VAL   A CG2 
3191 N N   . CYS   A 143 ? 0.1188 0.1444 0.1903 -0.0194 0.0223  -0.0104 143 CYS   A N   
3192 C CA  . CYS   A 143 ? 0.1159 0.1384 0.1898 -0.0176 0.0172  -0.0069 143 CYS   A CA  
3193 C C   . CYS   A 143 ? 0.1209 0.1382 0.1952 -0.0137 0.0200  0.0068  143 CYS   A C   
3194 O O   . CYS   A 143 ? 0.1227 0.1394 0.1997 -0.0098 0.0188  0.0153  143 CYS   A O   
3195 C CB  . CYS   A 143 ? 0.1255 0.1411 0.1904 -0.0137 0.0226  0.0056  143 CYS   A CB  
3196 S SG  . CYS   A 143 ? 0.1412 0.1476 0.1746 -0.0002 0.0153  0.0028  143 CYS   A SG  
3202 N N   . VAL   A 144 ? 0.1233 0.1406 0.2245 -0.0172 0.0237  0.0119  144 VAL   A N   
3203 C CA  . VAL   A 144 ? 0.1309 0.1531 0.2768 -0.0186 0.0423  0.0149  144 VAL   A CA  
3204 C C   . VAL   A 144 ? 0.1305 0.1452 0.2795 -0.0282 0.0160  0.0040  144 VAL   A C   
3205 O O   . VAL   A 144 ? 0.1407 0.1440 0.2924 -0.0207 0.0121  0.0098  144 VAL   A O   
3206 C CB  . VAL   A 144 ? 0.1554 0.1832 0.3514 -0.0012 0.0541  0.0315  144 VAL   A CB  
3207 C CG1 . VAL   A 144 ? 0.1775 0.2074 0.3923 -0.0088 0.0356  0.0340  144 VAL   A CG1 
3208 C CG2 . VAL   A 144 ? 0.1408 0.1875 0.3497 0.0005  0.0611  0.0432  144 VAL   A CG2 
3218 N N   . ASP   A 145 ? 0.1326 0.1409 0.2844 -0.0255 0.0134  -0.0149 145 ASP   A N   
3219 C CA  . ASP   A 145 ? 0.1394 0.1537 0.3013 -0.0262 0.0040  -0.0307 145 ASP   A CA  
3220 C C   . ASP   A 145 ? 0.1419 0.1448 0.2905 -0.0161 0.0140  -0.0323 145 ASP   A C   
3221 O O   . ASP   A 145 ? 0.1511 0.1556 0.3323 -0.0176 0.0095  -0.0615 145 ASP   A O   
3222 C CB  . ASP   A 145 ? 0.1541 0.1779 0.3259 -0.0301 -0.0086 -0.0373 145 ASP   A CB  
3223 C CG  . ASP   A 145 ? 0.1731 0.2057 0.3591 -0.0406 -0.0255 -0.0247 145 ASP   A CG  
3224 O OD1 . ASP   A 145 ? 0.1761 0.2103 0.3738 -0.0529 -0.0182 -0.0102 145 ASP   A OD1 
3225 O OD2 . ASP   A 145 ? 0.1798 0.2254 0.3713 -0.0413 -0.0408 -0.0249 145 ASP   A OD2 
3230 N N   . THR   A 146 ? 0.1277 0.1367 0.2356 -0.0205 0.0196  -0.0206 146 THR   A N   
3231 C CA  . THR   A 146 ? 0.1260 0.1354 0.2110 -0.0125 0.0202  -0.0232 146 THR   A CA  
3232 C C   . THR   A 146 ? 0.1213 0.1299 0.2156 -0.0089 0.0179  -0.0062 146 THR   A C   
3233 O O   . THR   A 146 ? 0.1382 0.1423 0.2194 -0.0025 0.0094  -0.0057 146 THR   A O   
3234 C CB  . THR   A 146 ? 0.1227 0.1331 0.1983 -0.0151 0.0187  -0.0223 146 THR   A CB  
3235 O OG1 . THR   A 146 ? 0.1200 0.1530 0.2098 -0.0054 0.0054  -0.0343 146 THR   A OG1 
3236 C CG2 . THR   A 146 ? 0.1245 0.1356 0.1992 -0.0114 0.0175  -0.0127 146 THR   A CG2 
3244 N N   . VAL   A 147 ? 0.1173 0.1323 0.2090 -0.0101 0.0229  0.0020  147 VAL   A N   
3245 C CA  . VAL   A 147 ? 0.1272 0.1331 0.2149 -0.0160 0.0360  0.0030  147 VAL   A CA  
3246 C C   . VAL   A 147 ? 0.1257 0.1236 0.2227 -0.0196 0.0266  0.0084  147 VAL   A C   
3247 O O   . VAL   A 147 ? 0.1291 0.1350 0.2419 -0.0202 0.0289  0.0117  147 VAL   A O   
3248 C CB  . VAL   A 147 ? 0.1376 0.1311 0.1877 -0.0207 0.0316  0.0062  147 VAL   A CB  
3249 C CG1 . VAL   A 147 ? 0.1647 0.1376 0.2002 -0.0154 0.0292  0.0155  147 VAL   A CG1 
3250 C CG2 . VAL   A 147 ? 0.1440 0.1372 0.1810 -0.0199 0.0221  0.0061  147 VAL   A CG2 
3260 N N   . ARG   A 148 ? 0.1262 0.1259 0.2323 -0.0194 0.0260  0.0191  148 ARG   A N   
3261 C CA  . ARG   A 148 ? 0.1360 0.1273 0.2231 -0.0182 0.0243  0.0245  148 ARG   A CA  
3262 C C   . ARG   A 148 ? 0.1466 0.1314 0.2248 -0.0219 0.0266  0.0373  148 ARG   A C   
3263 O O   . ARG   A 148 ? 0.1720 0.1484 0.2408 -0.0265 0.0314  0.0281  148 ARG   A O   
3264 C CB  . ARG   A 148 ? 0.1407 0.1351 0.2339 -0.0129 0.0300  0.0184  148 ARG   A CB  
3265 C CG  . ARG   A 148 ? 0.1571 0.1385 0.2603 -0.0173 0.0429  0.0170  148 ARG   A CG  
3266 C CD  . ARG   A 148 ? 0.1701 0.1325 0.2712 -0.0111 0.0503  0.0224  148 ARG   A CD  
3267 N NE  . ARG   A 148 ? 0.1650 0.1359 0.2705 0.0023  0.0572  0.0248  148 ARG   A NE  
3268 C CZ  . ARG   A 148 ? 0.1670 0.1316 0.2526 -0.0058 0.0560  0.0191  148 ARG   A CZ  
3269 N NH1 . ARG   A 148 ? 0.1700 0.1339 0.2567 -0.0212 0.0557  -0.0073 148 ARG   A NH1 
3270 N NH2 . ARG   A 148 ? 0.1643 0.1462 0.2577 0.0087  0.0657  0.0335  148 ARG   A NH2 
3284 N N   . THR   A 149 ? 0.1447 0.1397 0.2056 -0.0245 0.0047  0.0289  149 THR   A N   
3285 C CA  . THR   A 149 ? 0.1453 0.1445 0.2065 -0.0174 0.0145  0.0327  149 THR   A CA  
3286 C C   . THR   A 149 ? 0.1432 0.1452 0.1977 -0.0227 0.0192  0.0391  149 THR   A C   
3287 O O   . THR   A 149 ? 0.1390 0.1537 0.2071 -0.0228 0.0114  0.0326  149 THR   A O   
3288 C CB  . THR   A 149 ? 0.1438 0.1604 0.2004 -0.0182 0.0175  0.0274  149 THR   A CB  
3289 O OG1 . THR   A 149 ? 0.1479 0.1507 0.2107 -0.0272 0.0200  0.0216  149 THR   A OG1 
3290 C CG2 . THR   A 149 ? 0.1415 0.1727 0.2070 -0.0125 0.0144  0.0181  149 THR   A CG2 
3298 N N   . ASN   A 150 ? 0.1452 0.1480 0.1917 -0.0095 0.0154  0.0395  150 ASN   A N   
3299 C CA  . ASN   A 150 ? 0.1531 0.1589 0.2045 -0.0173 0.0270  0.0348  150 ASN   A CA  
3300 C C   . ASN   A 150 ? 0.1327 0.1519 0.2029 -0.0211 0.0191  0.0282  150 ASN   A C   
3301 O O   . ASN   A 150 ? 0.1479 0.1617 0.2354 -0.0200 0.0000  0.0314  150 ASN   A O   
3302 C CB  . ASN   A 150 ? 0.1907 0.1878 0.2318 -0.0186 0.0486  0.0478  150 ASN   A CB  
3303 C CG  . ASN   A 150 ? 0.2470 0.2218 0.2951 -0.0180 0.0277  0.0577  150 ASN   A CG  
3304 O OD1 . ASN   A 150 ? 0.2721 0.2307 0.3203 -0.0260 0.0226  0.0661  150 ASN   A OD1 
3305 N ND2 . ASN   A 150 ? 0.2749 0.2419 0.3430 -0.0082 0.0100  0.0576  150 ASN   A ND2 
3312 N N   . VAL   A 151 ? 0.1335 0.1372 0.1927 -0.0219 0.0131  0.0324  151 VAL   A N   
3313 C CA  . VAL   A 151 ? 0.1393 0.1344 0.1911 -0.0245 0.0245  0.0264  151 VAL   A CA  
3314 C C   . VAL   A 151 ? 0.1307 0.1314 0.2061 -0.0273 0.0217  0.0292  151 VAL   A C   
3315 O O   . VAL   A 151 ? 0.1373 0.1400 0.2352 -0.0271 0.0248  0.0115  151 VAL   A O   
3316 C CB  . VAL   A 151 ? 0.1671 0.1504 0.1896 -0.0051 0.0209  0.0240  151 VAL   A CB  
3317 C CG1 . VAL   A 151 ? 0.1650 0.1704 0.2264 -0.0074 0.0143  0.0208  151 VAL   A CG1 
3318 C CG2 . VAL   A 151 ? 0.1794 0.1602 0.1916 -0.0013 0.0368  0.0288  151 VAL   A CG2 
3328 N N   . TYR   A 152 ? 0.1306 0.1382 0.1930 -0.0256 0.0236  0.0316  152 TYR   A N   
3329 C CA  . TYR   A 152 ? 0.1334 0.1441 0.1642 -0.0224 0.0242  0.0308  152 TYR   A CA  
3330 C C   . TYR   A 152 ? 0.1317 0.1363 0.1488 -0.0194 0.0318  0.0264  152 TYR   A C   
3331 O O   . TYR   A 152 ? 0.1435 0.1308 0.1597 -0.0218 0.0308  0.0231  152 TYR   A O   
3332 C CB  . TYR   A 152 ? 0.1400 0.1536 0.1633 -0.0149 0.0253  0.0263  152 TYR   A CB  
3333 C CG  . TYR   A 152 ? 0.1540 0.1760 0.1676 -0.0202 0.0273  0.0391  152 TYR   A CG  
3334 C CD1 . TYR   A 152 ? 0.1626 0.1987 0.1912 -0.0152 0.0279  0.0488  152 TYR   A CD1 
3335 C CD2 . TYR   A 152 ? 0.1538 0.1853 0.1609 -0.0333 0.0155  0.0378  152 TYR   A CD2 
3336 C CE1 . TYR   A 152 ? 0.1832 0.2121 0.1982 -0.0096 0.0150  0.0615  152 TYR   A CE1 
3337 C CE2 . TYR   A 152 ? 0.1761 0.2049 0.1715 -0.0297 0.0136  0.0520  152 TYR   A CE2 
3338 C CZ  . TYR   A 152 ? 0.1931 0.2125 0.1838 -0.0203 0.0083  0.0746  152 TYR   A CZ  
3339 O OH  . TYR   A 152 ? 0.2197 0.2330 0.2187 -0.0092 0.0168  0.0863  152 TYR   A OH  
3349 N N   . LEU   A 153 ? 0.1291 0.1326 0.1597 -0.0215 0.0325  0.0274  153 LEU   A N   
3350 C CA  . LEU   A 153 ? 0.1293 0.1246 0.1663 -0.0116 0.0358  0.0257  153 LEU   A CA  
3351 C C   . LEU   A 153 ? 0.1363 0.1306 0.1757 -0.0102 0.0413  0.0340  153 LEU   A C   
3352 O O   . LEU   A 153 ? 0.1386 0.1366 0.1917 -0.0121 0.0491  0.0292  153 LEU   A O   
3353 C CB  . LEU   A 153 ? 0.1215 0.1329 0.1810 -0.0098 0.0294  0.0245  153 LEU   A CB  
3354 C CG  . LEU   A 153 ? 0.1280 0.1408 0.1774 -0.0096 0.0335  0.0228  153 LEU   A CG  
3355 C CD1 . LEU   A 153 ? 0.1322 0.1396 0.1941 -0.0093 0.0206  0.0172  153 LEU   A CD1 
3356 C CD2 . LEU   A 153 ? 0.1402 0.1456 0.1773 -0.0070 0.0358  0.0102  153 LEU   A CD2 
3368 N N   A ALA   A 154 ? 0.1361 0.1255 0.1746 -0.0108 0.0504  0.0282  154 ALA   A N   
3369 N N   B ALA   A 154 ? 0.1347 0.1306 0.1510 0.0009  0.0350  0.0266  154 ALA   A N   
3370 C CA  A ALA   A 154 ? 0.1366 0.1255 0.1638 -0.0138 0.0471  0.0210  154 ALA   A CA  
3371 C CA  B ALA   A 154 ? 0.1342 0.1344 0.1306 0.0004  0.0188  0.0224  154 ALA   A CA  
3372 C C   A ALA   A 154 ? 0.1446 0.1218 0.1514 -0.0119 0.0435  0.0131  154 ALA   A C   
3373 C C   B ALA   A 154 ? 0.1357 0.1297 0.1306 -0.0038 0.0146  0.0194  154 ALA   A C   
3374 O O   A ALA   A 154 ? 0.1514 0.1354 0.1621 -0.0202 0.0438  0.0071  154 ALA   A O   
3375 O O   B ALA   A 154 ? 0.1376 0.1340 0.1190 -0.0060 0.0175  0.0236  154 ALA   A O   
3376 C CB  A ALA   A 154 ? 0.1314 0.1305 0.1725 -0.0081 0.0312  0.0203  154 ALA   A CB  
3377 C CB  B ALA   A 154 ? 0.1410 0.1373 0.1203 0.0034  0.0001  0.0146  154 ALA   A CB  
3388 N N   A VAL   A 155 ? 0.1472 0.1221 0.1378 -0.0029 0.0482  0.0108  155 VAL   A N   
3389 N N   B VAL   A 155 ? 0.1360 0.1300 0.1405 -0.0088 0.0098  0.0227  155 VAL   A N   
3390 C CA  A VAL   A 155 ? 0.1546 0.1220 0.1558 -0.0041 0.0390  0.0168  155 VAL   A CA  
3391 C CA  B VAL   A 155 ? 0.1407 0.1299 0.1545 -0.0090 0.0011  0.0131  155 VAL   A CA  
3392 C C   A VAL   A 155 ? 0.1602 0.1240 0.1736 0.0032  0.0474  0.0274  155 VAL   A C   
3393 C C   B VAL   A 155 ? 0.1316 0.1308 0.1625 -0.0012 0.0022  0.0079  155 VAL   A C   
3394 O O   A VAL   A 155 ? 0.1584 0.1257 0.1713 0.0073  0.0573  0.0228  155 VAL   A O   
3395 O O   B VAL   A 155 ? 0.1306 0.1463 0.1572 0.0066  0.0021  0.0039  155 VAL   A O   
3396 C CB  A VAL   A 155 ? 0.1606 0.1241 0.1612 -0.0081 0.0174  0.0176  155 VAL   A CB  
3397 C CB  B VAL   A 155 ? 0.1455 0.1324 0.1442 -0.0162 -0.0099 0.0140  155 VAL   A CB  
3398 C CG1 A VAL   A 155 ? 0.1660 0.1343 0.1579 -0.0089 0.0159  0.0153  155 VAL   A CG1 
3399 C CG1 B VAL   A 155 ? 0.1435 0.1385 0.1493 -0.0257 -0.0191 0.0143  155 VAL   A CG1 
3400 C CG2 A VAL   A 155 ? 0.1641 0.1260 0.1643 -0.0090 0.0036  0.0240  155 VAL   A CG2 
3401 C CG2 B VAL   A 155 ? 0.1476 0.1323 0.1487 -0.0207 -0.0133 0.0105  155 VAL   A CG2 
3420 N N   A PHE   A 156 ? 0.1660 0.1304 0.2143 0.0059  0.0490  0.0457  156 PHE   A N   
3421 N N   B PHE   A 156 ? 0.1249 0.1247 0.1673 -0.0038 0.0036  0.0025  156 PHE   A N   
3422 C CA  A PHE   A 156 ? 0.1752 0.1413 0.2534 0.0071  0.0424  0.0539  156 PHE   A CA  
3423 C CA  B PHE   A 156 ? 0.1440 0.1239 0.1881 0.0023  -0.0046 0.0075  156 PHE   A CA  
3424 C C   A PHE   A 156 ? 0.1758 0.1536 0.2359 0.0161  0.0498  0.0487  156 PHE   A C   
3425 C C   B PHE   A 156 ? 0.1455 0.1326 0.1676 0.0024  -0.0050 0.0127  156 PHE   A C   
3426 O O   A PHE   A 156 ? 0.1695 0.1590 0.2332 0.0195  0.0582  0.0251  156 PHE   A O   
3427 O O   B PHE   A 156 ? 0.1512 0.1515 0.1892 0.0130  -0.0100 0.0016  156 PHE   A O   
3428 C CB  A PHE   A 156 ? 0.1898 0.1518 0.2978 0.0029  0.0274  0.0645  156 PHE   A CB  
3429 C CB  B PHE   A 156 ? 0.1497 0.1321 0.2281 0.0012  -0.0049 0.0198  156 PHE   A CB  
3430 C CG  A PHE   A 156 ? 0.2116 0.1658 0.3225 0.0053  0.0116  0.0639  156 PHE   A CG  
3431 C CG  B PHE   A 156 ? 0.1578 0.1384 0.2560 0.0040  0.0044  0.0415  156 PHE   A CG  
3432 C CD1 A PHE   A 156 ? 0.2236 0.1744 0.3282 0.0017  0.0077  0.0631  156 PHE   A CD1 
3433 C CD1 B PHE   A 156 ? 0.1747 0.1497 0.2742 -0.0017 -0.0080 0.0355  156 PHE   A CD1 
3434 C CD2 A PHE   A 156 ? 0.2235 0.1790 0.3348 0.0114  0.0063  0.0608  156 PHE   A CD2 
3435 C CD2 B PHE   A 156 ? 0.1699 0.1505 0.2716 0.0036  0.0095  0.0552  156 PHE   A CD2 
3436 C CE1 A PHE   A 156 ? 0.2322 0.1818 0.3344 0.0004  0.0129  0.0589  156 PHE   A CE1 
3437 C CE1 B PHE   A 156 ? 0.1799 0.1533 0.2859 -0.0059 -0.0137 0.0411  156 PHE   A CE1 
3438 C CE2 A PHE   A 156 ? 0.2320 0.1873 0.3420 0.0106  0.0075  0.0522  156 PHE   A CE2 
3439 C CE2 B PHE   A 156 ? 0.1725 0.1498 0.2754 0.0045  0.0095  0.0673  156 PHE   A CE2 
3440 C CZ  A PHE   A 156 ? 0.2348 0.1878 0.3407 0.0078  0.0142  0.0489  156 PHE   A CZ  
3441 C CZ  B PHE   A 156 ? 0.1726 0.1410 0.2807 -0.0055 -0.0045 0.0622  156 PHE   A CZ  
3460 N N   A ASP   A 157 ? 0.1834 0.1667 0.2389 0.0258  0.0476  0.0685  157 ASP   A N   
3461 N N   B ASP   A 157 ? 0.1396 0.1185 0.1469 0.0017  0.0047  0.0136  157 ASP   A N   
3462 C CA  A ASP   A 157 ? 0.1948 0.1852 0.2537 0.0270  0.0392  0.0795  157 ASP   A CA  
3463 C CA  B ASP   A 157 ? 0.1453 0.1223 0.1422 0.0009  0.0016  0.0206  157 ASP   A CA  
3464 C C   A ASP   A 157 ? 0.1976 0.1995 0.2558 0.0246  0.0554  0.0820  157 ASP   A C   
3465 C C   B ASP   A 157 ? 0.1529 0.1231 0.1507 -0.0070 0.0086  0.0180  157 ASP   A C   
3466 O O   A ASP   A 157 ? 0.1902 0.1983 0.2577 0.0258  0.0578  0.0772  157 ASP   A O   
3467 O O   B ASP   A 157 ? 0.1567 0.1255 0.1724 -0.0007 0.0078  0.0114  157 ASP   A O   
3468 C CB  A ASP   A 157 ? 0.2015 0.1957 0.2874 0.0311  0.0228  0.0732  157 ASP   A CB  
3469 C CB  B ASP   A 157 ? 0.1513 0.1225 0.1495 -0.0018 -0.0080 0.0226  157 ASP   A CB  
3470 C CG  A ASP   A 157 ? 0.2132 0.2075 0.3176 0.0267  0.0073  0.0763  157 ASP   A CG  
3471 C CG  B ASP   A 157 ? 0.1541 0.1258 0.1674 -0.0085 -0.0173 0.0281  157 ASP   A CG  
3472 O OD1 A ASP   A 157 ? 0.2268 0.2176 0.3473 0.0205  0.0008  0.0764  157 ASP   A OD1 
3473 O OD1 B ASP   A 157 ? 0.1579 0.1250 0.2009 -0.0048 -0.0250 0.0208  157 ASP   A OD1 
3474 O OD2 A ASP   A 157 ? 0.2105 0.2093 0.3259 0.0284  -0.0015 0.0728  157 ASP   A OD2 
3475 O OD2 B ASP   A 157 ? 0.1580 0.1380 0.1822 -0.0116 -0.0286 0.0510  157 ASP   A OD2 
3484 N N   A LYS   A 158 ? 0.2103 0.2190 0.2739 0.0233  0.0637  0.0775  158 LYS   A N   
3485 N N   B LYS   A 158 ? 0.1528 0.1248 0.1489 -0.0086 0.0047  0.0263  158 LYS   A N   
3486 C CA  A LYS   A 158 ? 0.2198 0.2421 0.2959 0.0173  0.0699  0.0663  158 LYS   A CA  
3487 C CA  B LYS   A 158 ? 0.1578 0.1394 0.1557 -0.0108 0.0069  0.0314  158 LYS   A CA  
3488 C C   A LYS   A 158 ? 0.2115 0.2461 0.2940 0.0144  0.0637  0.0680  158 LYS   A C   
3489 C C   B LYS   A 158 ? 0.1569 0.1253 0.1607 -0.0166 -0.0025 0.0276  158 LYS   A C   
3490 O O   A LYS   A 158 ? 0.2083 0.2471 0.3014 0.0108  0.0656  0.0723  158 LYS   A O   
3491 O O   B LYS   A 158 ? 0.1706 0.1235 0.1715 -0.0196 0.0068  0.0143  158 LYS   A O   
3492 C CB  A LYS   A 158 ? 0.2423 0.2605 0.3283 0.0132  0.0752  0.0566  158 LYS   A CB  
3493 C CB  B LYS   A 158 ? 0.1689 0.1656 0.1796 -0.0076 0.0152  0.0345  158 LYS   A CB  
3494 C CG  A LYS   A 158 ? 0.2663 0.2787 0.3576 0.0119  0.0766  0.0547  158 LYS   A CG  
3495 C CG  B LYS   A 158 ? 0.1845 0.1941 0.2102 -0.0107 0.0213  0.0258  158 LYS   A CG  
3496 C CD  A LYS   A 158 ? 0.2839 0.2937 0.3819 0.0144  0.0806  0.0551  158 LYS   A CD  
3497 C CD  B LYS   A 158 ? 0.1989 0.2228 0.2459 -0.0092 0.0223  0.0163  158 LYS   A CD  
3498 C CE  A LYS   A 158 ? 0.2930 0.3044 0.3953 0.0142  0.0867  0.0575  158 LYS   A CE  
3499 C CE  B LYS   A 158 ? 0.2048 0.2353 0.2616 -0.0035 0.0195  0.0138  158 LYS   A CE  
3500 N NZ  A LYS   A 158 ? 0.2965 0.3088 0.4003 0.0123  0.0924  0.0592  158 LYS   A NZ  
3501 N NZ  B LYS   A 158 ? 0.2108 0.2387 0.2757 0.0023  0.0238  0.0111  158 LYS   A NZ  
3528 N N   A ASN   A 159 ? 0.2064 0.2480 0.2913 0.0079  0.0545  0.0661  159 ASN   A N   
3529 N N   B ASN   A 159 ? 0.1617 0.1216 0.1730 -0.0150 -0.0171 0.0264  159 ASN   A N   
3530 C CA  A ASN   A 159 ? 0.2020 0.2459 0.2681 0.0011  0.0454  0.0666  159 ASN   A CA  
3531 C CA  B ASN   A 159 ? 0.1667 0.1251 0.1917 -0.0170 -0.0244 0.0232  159 ASN   A CA  
3532 C C   A ASN   A 159 ? 0.1947 0.2397 0.2520 0.0002  0.0468  0.0666  159 ASN   A C   
3533 C C   B ASN   A 159 ? 0.1730 0.1330 0.2041 -0.0189 -0.0216 0.0091  159 ASN   A C   
3534 O O   A ASN   A 159 ? 0.1846 0.2369 0.2504 0.0056  0.0385  0.0658  159 ASN   A O   
3535 O O   B ASN   A 159 ? 0.1723 0.1399 0.2177 -0.0197 -0.0254 0.0034  159 ASN   A O   
3536 C CB  A ASN   A 159 ? 0.2051 0.2503 0.2729 -0.0106 0.0337  0.0719  159 ASN   A CB  
3537 C CB  B ASN   A 159 ? 0.1759 0.1445 0.2046 -0.0118 -0.0356 0.0275  159 ASN   A CB  
3538 C CG  A ASN   A 159 ? 0.2109 0.2547 0.2820 -0.0167 0.0289  0.0724  159 ASN   A CG  
3539 C CG  B ASN   A 159 ? 0.1809 0.1669 0.2289 -0.0027 -0.0443 0.0211  159 ASN   A CG  
3540 O OD1 A ASN   A 159 ? 0.2158 0.2571 0.2985 -0.0190 0.0337  0.0722  159 ASN   A OD1 
3541 O OD1 B ASN   A 159 ? 0.1832 0.1839 0.2658 0.0061  -0.0298 0.0160  159 ASN   A OD1 
3542 N ND2 A ASN   A 159 ? 0.2082 0.2552 0.2751 -0.0200 0.0240  0.0721  159 ASN   A ND2 
3543 N ND2 B ASN   A 159 ? 0.1856 0.1769 0.2353 0.0095  -0.0577 0.0171  159 ASN   A ND2 
3556 N N   A LEU   A 160 ? 0.1967 0.2343 0.2412 -0.0020 0.0450  0.0685  160 LEU   A N   
3557 N N   B LEU   A 160 ? 0.1726 0.1241 0.1845 -0.0122 -0.0119 0.0096  160 LEU   A N   
3558 C CA  A LEU   A 160 ? 0.2012 0.2307 0.2245 -0.0044 0.0468  0.0727  160 LEU   A CA  
3559 C CA  B LEU   A 160 ? 0.1759 0.1336 0.1781 -0.0150 -0.0094 0.0162  160 LEU   A CA  
3560 C C   A LEU   A 160 ? 0.1955 0.2255 0.2216 -0.0036 0.0467  0.0845  160 LEU   A C   
3561 C C   B LEU   A 160 ? 0.1796 0.1317 0.1781 -0.0126 0.0016  0.0203  160 LEU   A C   
3562 O O   A LEU   A 160 ? 0.1885 0.2248 0.2260 -0.0096 0.0459  0.0987  160 LEU   A O   
3563 O O   B LEU   A 160 ? 0.1805 0.1382 0.1859 -0.0186 0.0098  0.0064  160 LEU   A O   
3564 C CB  A LEU   A 160 ? 0.2055 0.2286 0.2167 -0.0038 0.0462  0.0701  160 LEU   A CB  
3565 C CB  B LEU   A 160 ? 0.1824 0.1386 0.1751 -0.0176 -0.0142 0.0091  160 LEU   A CB  
3566 C CG  A LEU   A 160 ? 0.2098 0.2302 0.2295 -0.0035 0.0437  0.0484  160 LEU   A CG  
3567 C CG  B LEU   A 160 ? 0.1926 0.1572 0.1924 -0.0173 -0.0143 0.0100  160 LEU   A CG  
3568 C CD1 A LEU   A 160 ? 0.2099 0.2308 0.2409 -0.0036 0.0441  0.0403  160 LEU   A CD1 
3569 C CD1 B LEU   A 160 ? 0.2004 0.1628 0.2013 -0.0148 -0.0162 0.0213  160 LEU   A CD1 
3570 C CD2 A LEU   A 160 ? 0.2127 0.2301 0.2360 -0.0046 0.0412  0.0451  160 LEU   A CD2 
3571 C CD2 B LEU   A 160 ? 0.1949 0.1666 0.1949 -0.0185 -0.0187 0.0047  160 LEU   A CD2 
3594 N N   A TYR   A 161 ? 0.2005 0.2203 0.2164 0.0016  0.0517  0.0876  161 TYR   A N   
3595 N N   B TYR   A 161 ? 0.1730 0.1290 0.1715 -0.0030 0.0088  0.0219  161 TYR   A N   
3596 C CA  A TYR   A 161 ? 0.2004 0.2206 0.2184 0.0098  0.0568  0.0785  161 TYR   A CA  
3597 C CA  B TYR   A 161 ? 0.1762 0.1290 0.1782 0.0052  0.0167  0.0203  161 TYR   A CA  
3598 C C   A TYR   A 161 ? 0.2091 0.2278 0.2401 0.0154  0.0607  0.0771  161 TYR   A C   
3599 C C   B TYR   A 161 ? 0.1871 0.1277 0.1887 0.0044  0.0169  0.0159  161 TYR   A C   
3600 O O   A TYR   A 161 ? 0.2062 0.2250 0.2309 0.0157  0.0699  0.0826  161 TYR   A O   
3601 O O   B TYR   A 161 ? 0.1884 0.1279 0.1949 -0.0025 0.0161  0.0159  161 TYR   A O   
3602 C CB  A TYR   A 161 ? 0.1944 0.2202 0.2225 0.0099  0.0538  0.0567  161 TYR   A CB  
3603 C CB  B TYR   A 161 ? 0.1665 0.1434 0.1830 0.0071  0.0235  0.0136  161 TYR   A CB  
3604 C CG  A TYR   A 161 ? 0.1842 0.2181 0.2226 0.0139  0.0436  0.0420  161 TYR   A CG  
3605 C CG  B TYR   A 161 ? 0.1502 0.1548 0.1908 0.0159  0.0282  0.0261  161 TYR   A CG  
3606 C CD1 A TYR   A 161 ? 0.1775 0.2139 0.2237 0.0129  0.0417  0.0347  161 TYR   A CD1 
3607 C CD1 B TYR   A 161 ? 0.1445 0.1569 0.2034 0.0185  0.0324  0.0331  161 TYR   A CD1 
3608 C CD2 A TYR   A 161 ? 0.1784 0.2188 0.2231 0.0126  0.0373  0.0391  161 TYR   A CD2 
3609 C CD2 B TYR   A 161 ? 0.1397 0.1622 0.1973 0.0162  0.0216  0.0300  161 TYR   A CD2 
3610 C CE1 A TYR   A 161 ? 0.1735 0.2099 0.2234 0.0111  0.0347  0.0322  161 TYR   A CE1 
3611 C CE1 B TYR   A 161 ? 0.1336 0.1568 0.2031 0.0187  0.0268  0.0431  161 TYR   A CE1 
3612 C CE2 A TYR   A 161 ? 0.1740 0.2149 0.2249 0.0068  0.0335  0.0427  161 TYR   A CE2 
3613 C CE2 B TYR   A 161 ? 0.1250 0.1621 0.1914 0.0068  0.0282  0.0457  161 TYR   A CE2 
3614 C CZ  A TYR   A 161 ? 0.1802 0.2140 0.2267 0.0067  0.0277  0.0375  161 TYR   A CZ  
3615 C CZ  B TYR   A 161 ? 0.1334 0.1635 0.1828 0.0114  0.0207  0.0516  161 TYR   A CZ  
3616 O OH  A TYR   A 161 ? 0.1923 0.2162 0.2458 -0.0012 0.0166  0.0385  161 TYR   A OH  
3617 O OH  B TYR   A 161 ? 0.1416 0.1678 0.1709 0.0018  0.0161  0.0625  161 TYR   A OH  
3636 N N   A ASP   A 162 ? 0.2153 0.2380 0.2579 0.0200  0.0578  0.0779  162 ASP   A N   
3637 N N   B ASP   A 162 ? 0.1898 0.1251 0.1996 0.0029  0.0162  0.0187  162 ASP   A N   
3638 C CA  A ASP   A 162 ? 0.2148 0.2498 0.2622 0.0193  0.0587  0.0777  162 ASP   A CA  
3639 C CA  B ASP   A 162 ? 0.1961 0.1355 0.2094 0.0013  0.0120  0.0127  162 ASP   A CA  
3640 C C   A ASP   A 162 ? 0.2102 0.2520 0.2541 0.0135  0.0495  0.0838  162 ASP   A C   
3641 C C   B ASP   A 162 ? 0.1993 0.1309 0.2118 -0.0022 0.0068  0.0069  162 ASP   A C   
3642 O O   A ASP   A 162 ? 0.2070 0.2516 0.2521 0.0111  0.0485  0.0951  162 ASP   A O   
3643 O O   B ASP   A 162 ? 0.1911 0.1302 0.2313 -0.0054 0.0075  0.0025  162 ASP   A O   
3644 C CB  A ASP   A 162 ? 0.2163 0.2585 0.2767 0.0239  0.0659  0.0683  162 ASP   A CB  
3645 C CB  B ASP   A 162 ? 0.1980 0.1543 0.2319 0.0105  0.0146  0.0160  162 ASP   A CB  
3646 C CG  A ASP   A 162 ? 0.2201 0.2697 0.2859 0.0266  0.0655  0.0602  162 ASP   A CG  
3647 C CG  B ASP   A 162 ? 0.2037 0.1683 0.2476 0.0206  0.0153  0.0246  162 ASP   A CG  
3648 O OD1 A ASP   A 162 ? 0.2241 0.2739 0.2801 0.0303  0.0615  0.0587  162 ASP   A OD1 
3649 O OD1 B ASP   A 162 ? 0.2092 0.1782 0.2439 0.0221  0.0201  0.0333  162 ASP   A OD1 
3650 O OD2 A ASP   A 162 ? 0.2226 0.2756 0.3005 0.0280  0.0649  0.0550  162 ASP   A OD2 
3651 O OD2 B ASP   A 162 ? 0.2025 0.1728 0.2604 0.0237  0.0193  0.0217  162 ASP   A OD2 
3660 N N   A LYS   A 163 ? 0.2150 0.2571 0.2572 0.0120  0.0400  0.0750  163 LYS   A N   
3661 N N   B LYS   A 163 ? 0.2118 0.1359 0.2017 -0.0097 0.0064  0.0170  163 LYS   A N   
3662 C CA  A LYS   A 163 ? 0.2180 0.2619 0.2605 0.0065  0.0342  0.0635  163 LYS   A CA  
3663 C CA  B LYS   A 163 ? 0.2275 0.1497 0.2048 -0.0076 0.0104  0.0302  163 LYS   A CA  
3664 C C   A LYS   A 163 ? 0.2022 0.2456 0.2502 0.0059  0.0387  0.0578  163 LYS   A C   
3665 C C   B LYS   A 163 ? 0.2139 0.1412 0.1913 -0.0124 0.0109  0.0171  163 LYS   A C   
3666 O O   A LYS   A 163 ? 0.1977 0.2452 0.2621 0.0058  0.0429  0.0606  163 LYS   A O   
3667 O O   B LYS   A 163 ? 0.2043 0.1373 0.1837 -0.0246 0.0070  -0.0020 163 LYS   A O   
3668 C CB  A LYS   A 163 ? 0.2401 0.2834 0.2919 0.0060  0.0204  0.0492  163 LYS   A CB  
3669 C CB  B LYS   A 163 ? 0.2536 0.1774 0.2210 -0.0065 0.0239  0.0501  163 LYS   A CB  
3670 C CG  A LYS   A 163 ? 0.2587 0.3031 0.3333 0.0032  0.0076  0.0320  163 LYS   A CG  
3671 C CG  B LYS   A 163 ? 0.2827 0.2080 0.2690 -0.0032 0.0348  0.0609  163 LYS   A CG  
3672 C CD  A LYS   A 163 ? 0.2741 0.3209 0.3747 0.0004  -0.0057 0.0171  163 LYS   A CD  
3673 C CD  B LYS   A 163 ? 0.3059 0.2358 0.3181 -0.0024 0.0488  0.0634  163 LYS   A CD  
3674 C CE  A LYS   A 163 ? 0.2854 0.3332 0.4045 -0.0017 -0.0142 0.0070  163 LYS   A CE  
3675 C CE  B LYS   A 163 ? 0.3237 0.2585 0.3523 -0.0009 0.0583  0.0658  163 LYS   A CE  
3676 N NZ  A LYS   A 163 ? 0.2921 0.3413 0.4232 -0.0035 -0.0213 0.0036  163 LYS   A NZ  
3677 N NZ  B LYS   A 163 ? 0.3333 0.2701 0.3787 -0.0028 0.0631  0.0659  163 LYS   A NZ  
3704 N N   A LEU   A 164 ? 0.1830 0.2284 0.2260 0.0021  0.0424  0.0478  164 LEU   A N   
3705 N N   B LEU   A 164 ? 0.2062 0.1495 0.1915 -0.0074 0.0211  0.0225  164 LEU   A N   
3706 C CA  A LEU   A 164 ? 0.1680 0.2167 0.2108 -0.0021 0.0515  0.0329  164 LEU   A CA  
3707 C CA  B LEU   A 164 ? 0.2021 0.1588 0.2002 -0.0107 0.0320  0.0303  164 LEU   A CA  
3708 C C   A LEU   A 164 ? 0.1615 0.2157 0.2129 0.0051  0.0517  0.0255  164 LEU   A C   
3709 C C   B LEU   A 164 ? 0.1945 0.1542 0.2133 -0.0094 0.0275  0.0305  164 LEU   A C   
3710 O O   A LEU   A 164 ? 0.1496 0.2162 0.1974 0.0007  0.0604  0.0187  164 LEU   A O   
3711 O O   B LEU   A 164 ? 0.1867 0.1565 0.2291 -0.0199 0.0385  0.0299  164 LEU   A O   
3712 C CB  A LEU   A 164 ? 0.1627 0.2050 0.1944 -0.0110 0.0590  0.0264  164 LEU   A CB  
3713 C CB  B LEU   A 164 ? 0.2045 0.1743 0.2031 -0.0113 0.0403  0.0264  164 LEU   A CB  
3714 C CG  A LEU   A 164 ? 0.1687 0.1954 0.1902 -0.0140 0.0495  0.0237  164 LEU   A CG  
3715 C CG  B LEU   A 164 ? 0.2103 0.1848 0.2086 -0.0107 0.0424  0.0281  164 LEU   A CG  
3716 C CD1 A LEU   A 164 ? 0.1629 0.1862 0.1926 -0.0116 0.0507  0.0331  164 LEU   A CD1 
3717 C CD1 B LEU   A 164 ? 0.2118 0.1868 0.2184 -0.0086 0.0453  0.0304  164 LEU   A CD1 
3718 C CD2 A LEU   A 164 ? 0.1710 0.1919 0.1859 -0.0217 0.0457  0.0223  164 LEU   A CD2 
3719 C CD2 B LEU   A 164 ? 0.2112 0.1854 0.2089 -0.0189 0.0391  0.0312  164 LEU   A CD2 
3742 N N   A VAL   A 165 ? 0.1593 0.2132 0.2172 0.0093  0.0555  0.0369  165 VAL   A N   
3743 N N   B VAL   A 165 ? 0.1869 0.1505 0.2029 -0.0046 0.0239  0.0319  165 VAL   A N   
3744 C CA  A VAL   A 165 ? 0.1676 0.2180 0.2200 0.0104  0.0580  0.0487  165 VAL   A CA  
3745 C CA  B VAL   A 165 ? 0.1910 0.1570 0.2017 0.0018  0.0172  0.0330  165 VAL   A CA  
3746 C C   A VAL   A 165 ? 0.1717 0.2227 0.2231 0.0131  0.0507  0.0527  165 VAL   A C   
3747 C C   B VAL   A 165 ? 0.1852 0.1476 0.2042 0.0018  0.0224  0.0268  165 VAL   A C   
3748 O O   A VAL   A 165 ? 0.1633 0.2249 0.2171 0.0097  0.0633  0.0542  165 VAL   A O   
3749 O O   B VAL   A 165 ? 0.1812 0.1385 0.2186 -0.0033 0.0333  0.0227  165 VAL   A O   
3750 C CB  A VAL   A 165 ? 0.1788 0.2154 0.2234 0.0091  0.0554  0.0559  165 VAL   A CB  
3751 C CB  B VAL   A 165 ? 0.2063 0.1766 0.2017 0.0009  0.0093  0.0422  165 VAL   A CB  
3752 C CG1 A VAL   A 165 ? 0.1827 0.2159 0.2158 0.0071  0.0632  0.0580  165 VAL   A CG1 
3753 C CG1 B VAL   A 165 ? 0.2137 0.1860 0.1911 -0.0003 0.0100  0.0401  165 VAL   A CG1 
3754 C CG2 A VAL   A 165 ? 0.1825 0.2157 0.2354 0.0086  0.0481  0.0597  165 VAL   A CG2 
3755 C CG2 B VAL   A 165 ? 0.2082 0.1799 0.2114 0.0030  -0.0036 0.0529  165 VAL   A CG2 
3774 N N   A SER   A 166 ? 0.1765 0.2280 0.2342 0.0089  0.0431  0.0589  166 SER   A N   
3775 N N   B SER   A 166 ? 0.1779 0.1559 0.2136 -0.0030 0.0171  0.0187  166 SER   A N   
3776 C CA  A SER   A 166 ? 0.1924 0.2351 0.2434 0.0085  0.0362  0.0621  166 SER   A CA  
3777 C CA  B SER   A 166 ? 0.1851 0.1714 0.2292 0.0007  0.0128  0.0044  166 SER   A CA  
3778 C C   A SER   A 166 ? 0.2043 0.2423 0.2377 0.0036  0.0234  0.0491  166 SER   A C   
3779 C C   B SER   A 166 ? 0.1820 0.1673 0.2122 -0.0088 0.0155  0.0040  166 SER   A C   
3780 O O   A SER   A 166 ? 0.2109 0.2457 0.2445 0.0012  0.0177  0.0551  166 SER   A O   
3781 O O   B SER   A 166 ? 0.1985 0.1719 0.2275 -0.0150 -0.0012 0.0088  166 SER   A O   
3782 C CB  A SER   A 166 ? 0.2013 0.2367 0.2646 0.0143  0.0356  0.0799  166 SER   A CB  
3783 C CB  B SER   A 166 ? 0.1912 0.1968 0.2745 0.0104  -0.0006 0.0012  166 SER   A CB  
3784 O OG  A SER   A 166 ? 0.2152 0.2417 0.2943 0.0172  0.0311  0.0931  166 SER   A OG  
3785 O OG  B SER   A 166 ? 0.2039 0.2228 0.3180 0.0123  -0.0079 0.0071  166 SER   A OG  
3796 N N   A SER   A 167 ? 0.2112 0.2515 0.2342 0.0005  0.0214  0.0286  167 SER   A N   
3797 N N   B SER   A 167 ? 0.1730 0.1838 0.1941 -0.0071 0.0214  0.0061  167 SER   A N   
3798 C CA  A SER   A 167 ? 0.2217 0.2545 0.2430 -0.0059 0.0167  0.0143  167 SER   A CA  
3799 C CA  B SER   A 167 ? 0.1775 0.1952 0.1998 -0.0095 0.0071  0.0089  167 SER   A CA  
3800 C C   A SER   A 167 ? 0.2219 0.2531 0.2551 -0.0061 0.0190  0.0118  167 SER   A C   
3801 C C   B SER   A 167 ? 0.1794 0.1995 0.2354 -0.0079 0.0140  0.0154  167 SER   A C   
3802 O O   A SER   A 167 ? 0.2293 0.2581 0.2687 -0.0008 0.0181  0.0072  167 SER   A O   
3803 O O   B SER   A 167 ? 0.1918 0.2096 0.2538 -0.0011 0.0092  0.0081  167 SER   A O   
3804 C CB  A SER   A 167 ? 0.2307 0.2578 0.2499 -0.0116 0.0207  0.0108  167 SER   A CB  
3805 C CB  B SER   A 167 ? 0.1814 0.2015 0.1897 -0.0152 0.0024  0.0075  167 SER   A CB  
3806 O OG  A SER   A 167 ? 0.2351 0.2595 0.2661 -0.0161 0.0250  0.0055  167 SER   A OG  
3807 O OG  B SER   A 167 ? 0.1796 0.2031 0.1898 -0.0222 0.0148  0.0079  167 SER   A OG  
3818 N N   A PHE   A 168 ? 0.2159 0.2503 0.2697 -0.0061 0.0171  0.0158  168 PHE   A N   
3819 N N   B PHE   A 168 ? 0.1670 0.1969 0.2586 -0.0090 0.0278  0.0403  168 PHE   A N   
3820 C CA  A PHE   A 168 ? 0.2167 0.2513 0.2849 -0.0057 0.0120  0.0074  168 PHE   A CA  
3821 C CA  B PHE   A 168 ? 0.1617 0.2059 0.2902 -0.0128 0.0331  0.0376  168 PHE   A CA  
3822 C C   A PHE   A 168 ? 0.2366 0.2667 0.3105 -0.0015 0.0260  -0.0029 168 PHE   A C   
3823 C C   B PHE   A 168 ? 0.1673 0.2149 0.3141 -0.0231 0.0619  0.0212  168 PHE   A C   
3824 O O   A PHE   A 168 ? 0.2382 0.2656 0.3129 -0.0049 0.0270  0.0041  168 PHE   A O   
3825 O O   B PHE   A 168 ? 0.1720 0.2142 0.3361 -0.0273 0.0628  0.0269  168 PHE   A O   
3826 C CB  A PHE   A 168 ? 0.2045 0.2420 0.2767 -0.0083 -0.0030 0.0042  168 PHE   A CB  
3827 C CB  B PHE   A 168 ? 0.1590 0.2126 0.2962 -0.0067 0.0169  0.0504  168 PHE   A CB  
3828 C CG  A PHE   A 168 ? 0.1893 0.2320 0.2658 -0.0103 -0.0120 -0.0009 168 PHE   A CG  
3829 C CG  B PHE   A 168 ? 0.1518 0.2126 0.2959 -0.0076 0.0109  0.0628  168 PHE   A CG  
3830 C CD1 A PHE   A 168 ? 0.1846 0.2280 0.2698 -0.0126 -0.0140 -0.0012 168 PHE   A CD1 
3831 C CD1 B PHE   A 168 ? 0.1538 0.2119 0.3053 -0.0107 0.0145  0.0680  168 PHE   A CD1 
3832 C CD2 A PHE   A 168 ? 0.1839 0.2281 0.2642 -0.0089 -0.0107 -0.0061 168 PHE   A CD2 
3833 C CD2 B PHE   A 168 ? 0.1446 0.2133 0.2994 -0.0123 0.0228  0.0677  168 PHE   A CD2 
3834 C CE1 A PHE   A 168 ? 0.1786 0.2265 0.2680 -0.0138 -0.0158 -0.0032 168 PHE   A CE1 
3835 C CE1 B PHE   A 168 ? 0.1521 0.2143 0.3086 -0.0116 0.0188  0.0737  168 PHE   A CE1 
3836 C CE2 A PHE   A 168 ? 0.1844 0.2258 0.2676 -0.0056 -0.0102 -0.0043 168 PHE   A CE2 
3837 C CE2 B PHE   A 168 ? 0.1478 0.2099 0.3065 -0.0109 0.0231  0.0760  168 PHE   A CE2 
3838 C CZ  A PHE   A 168 ? 0.1822 0.2251 0.2697 -0.0107 -0.0147 -0.0075 168 PHE   A CZ  
3839 C CZ  B PHE   A 168 ? 0.1495 0.2121 0.3132 -0.0146 0.0214  0.0711  168 PHE   A CZ  
3858 N N   A LEU   A 169 ? 0.2615 0.2830 0.3393 0.0016  0.0291  -0.0197 169 LEU   A N   
3859 N N   B LEU   A 169 ? 0.1829 0.2304 0.3216 -0.0341 0.0670  -0.0031 169 LEU   A N   
3860 C CA  A LEU   A 169 ? 0.2918 0.3057 0.3769 0.0090  0.0237  -0.0291 169 LEU   A CA  
3861 C CA  B LEU   A 169 ? 0.2232 0.2593 0.3544 -0.0371 0.0520  -0.0167 169 LEU   A CA  
3862 C C   A LEU   A 169 ? 0.2945 0.3127 0.3975 0.0170  0.0230  -0.0254 169 LEU   A C   
3863 C C   B LEU   A 169 ? 0.2243 0.2681 0.3644 -0.0352 0.0442  -0.0067 169 LEU   A C   
3864 O O   A LEU   A 169 ? 0.2969 0.3156 0.3948 0.0232  0.0194  -0.0247 169 LEU   A O   
3865 O O   B LEU   A 169 ? 0.2293 0.2758 0.3607 -0.0235 0.0408  -0.0018 169 LEU   A O   
3866 C CB  A LEU   A 169 ? 0.3150 0.3218 0.3880 0.0072  0.0219  -0.0406 169 LEU   A CB  
3867 C CB  B LEU   A 169 ? 0.2592 0.2826 0.3695 -0.0376 0.0416  -0.0391 169 LEU   A CB  
3868 C CG  A LEU   A 169 ? 0.3327 0.3355 0.3978 0.0039  0.0198  -0.0523 169 LEU   A CG  
3869 C CG  B LEU   A 169 ? 0.2907 0.3048 0.3845 -0.0377 0.0350  -0.0581 169 LEU   A CG  
3870 C CD1 A LEU   A 169 ? 0.3389 0.3396 0.4040 0.0027  0.0168  -0.0551 169 LEU   A CD1 
3871 C CD1 B LEU   A 169 ? 0.3002 0.3111 0.3921 -0.0395 0.0300  -0.0633 169 LEU   A CD1 
3872 C CD2 A LEU   A 169 ? 0.3396 0.3411 0.3985 0.0010  0.0195  -0.0565 169 LEU   A CD2 
3873 C CD2 B LEU   A 169 ? 0.3032 0.3156 0.3877 -0.0362 0.0359  -0.0628 169 LEU   A CD2 
3874 O OXT A LEU   A 169 ? 0.2945 0.3177 0.4116 0.0184  0.0252  -0.0237 169 LEU   A OXT 
3875 O OXT B LEU   A 169 ? 0.2219 0.2737 0.3688 -0.0397 0.0363  -0.0027 169 LEU   A OXT 
3898 N N   A SER   B 1   ? 0.3728 0.3671 0.3812 -0.0752 -0.0753 0.0378  1   SER   B N   
3899 N N   B SER   B 1   ? 0.3696 0.3480 0.3455 -0.0874 -0.0782 0.0213  1   SER   B N   
3900 C CA  A SER   B 1   ? 0.3670 0.3647 0.3805 -0.0781 -0.0740 0.0374  1   SER   B CA  
3901 C CA  B SER   B 1   ? 0.3644 0.3499 0.3506 -0.0892 -0.0785 0.0196  1   SER   B CA  
3902 C C   A SER   B 1   ? 0.3469 0.3554 0.3672 -0.0815 -0.0751 0.0537  1   SER   B C   
3903 C C   B SER   B 1   ? 0.3472 0.3502 0.3385 -0.0868 -0.0821 0.0392  1   SER   B C   
3904 O O   A SER   B 1   ? 0.3540 0.3570 0.3567 -0.0768 -0.0711 0.0535  1   SER   B O   
3905 O O   B SER   B 1   ? 0.3494 0.3503 0.3211 -0.0848 -0.0836 0.0414  1   SER   B O   
3906 C CB  A SER   B 1   ? 0.3771 0.3690 0.3862 -0.0755 -0.0692 0.0243  1   SER   B CB  
3907 C CB  B SER   B 1   ? 0.3734 0.3494 0.3603 -0.0901 -0.0725 0.0012  1   SER   B CB  
3908 O OG  A SER   B 1   ? 0.3857 0.3757 0.4106 -0.0735 -0.0629 0.0189  1   SER   B OG  
3909 O OG  B SER   B 1   ? 0.3813 0.3535 0.3894 -0.0902 -0.0664 -0.0073 1   SER   B OG  
3924 N N   A MET   B 2   ? 0.3211 0.3424 0.3610 -0.0872 -0.0736 0.0819  2   MET   B N   
3925 N N   B MET   B 2   ? 0.3316 0.3494 0.3403 -0.0822 -0.0765 0.0678  2   MET   B N   
3926 C CA  A MET   B 2   ? 0.3002 0.3322 0.3629 -0.0803 -0.0704 0.1016  2   MET   B CA  
3927 C CA  B MET   B 2   ? 0.3207 0.3493 0.3475 -0.0669 -0.0680 0.0886  2   MET   B CA  
3928 C C   A MET   B 2   ? 0.2589 0.3017 0.3110 -0.0801 -0.0821 0.1297  2   MET   B C   
3929 C C   B MET   B 2   ? 0.2954 0.3288 0.3121 -0.0569 -0.0651 0.1057  2   MET   B C   
3930 O O   A MET   B 2   ? 0.2467 0.3028 0.2950 -0.0833 -0.0906 0.1400  2   MET   B O   
3931 O O   B MET   B 2   ? 0.2998 0.3387 0.3238 -0.0524 -0.0629 0.1037  2   MET   B O   
3932 C CB  A MET   B 2   ? 0.3258 0.3573 0.4287 -0.0624 -0.0529 0.0819  2   MET   B CB  
3933 C CB  B MET   B 2   ? 0.3402 0.3722 0.4037 -0.0529 -0.0604 0.0836  2   MET   B CB  
3934 C CG  A MET   B 2   ? 0.3482 0.3787 0.4903 -0.0441 -0.0374 0.0686  2   MET   B CG  
3935 C CG  B MET   B 2   ? 0.3572 0.3919 0.4541 -0.0392 -0.0526 0.0841  2   MET   B CG  
3936 S SD  A MET   B 2   ? 0.3684 0.3986 0.5499 -0.0281 -0.0264 0.0582  2   MET   B SD  
3937 S SD  B MET   B 2   ? 0.3729 0.4114 0.5010 -0.0269 -0.0504 0.0847  2   MET   B SD  
3938 C CE  A MET   B 2   ? 0.3728 0.4033 0.5514 -0.0250 -0.0208 0.0569  2   MET   B CE  
3939 C CE  B MET   B 2   ? 0.3755 0.4149 0.5055 -0.0255 -0.0469 0.0821  2   MET   B CE  
3958 N N   A VAL   B 3   ? 0.2312 0.2688 0.2900 -0.0810 -0.0803 0.1337  3   VAL   B N   
3959 N N   B VAL   B 3   ? 0.2648 0.2955 0.2809 -0.0569 -0.0620 0.1129  3   VAL   B N   
3960 C CA  A VAL   B 3   ? 0.2193 0.2393 0.2751 -0.0735 -0.0724 0.1190  3   VAL   B CA  
3961 C CA  B VAL   B 3   ? 0.2432 0.2642 0.2632 -0.0509 -0.0560 0.0980  3   VAL   B CA  
3962 C C   A VAL   B 3   ? 0.2032 0.2239 0.2354 -0.0629 -0.0634 0.1110  3   VAL   B C   
3963 C C   B VAL   B 3   ? 0.2179 0.2420 0.2270 -0.0454 -0.0512 0.0883  3   VAL   B C   
3964 O O   A VAL   B 3   ? 0.1973 0.2209 0.2341 -0.0631 -0.0601 0.1275  3   VAL   B O   
3965 O O   B VAL   B 3   ? 0.2163 0.2495 0.2222 -0.0326 -0.0510 0.0798  3   VAL   B O   
3966 C CB  A VAL   B 3   ? 0.2273 0.2363 0.3057 -0.0770 -0.0648 0.1038  3   VAL   B CB  
3967 C CB  B VAL   B 3   ? 0.2485 0.2583 0.2837 -0.0537 -0.0494 0.0903  3   VAL   B CB  
3968 C CG1 A VAL   B 3   ? 0.2297 0.2333 0.3196 -0.0820 -0.0624 0.0992  3   VAL   B CG1 
3969 C CG1 B VAL   B 3   ? 0.2491 0.2545 0.2944 -0.0584 -0.0479 0.0882  3   VAL   B CG1 
3970 C CG2 A VAL   B 3   ? 0.2323 0.2399 0.3167 -0.0718 -0.0603 0.1030  3   VAL   B CG2 
3971 C CG2 B VAL   B 3   ? 0.2530 0.2602 0.2858 -0.0492 -0.0491 0.0913  3   VAL   B CG2 
3990 N N   . ASN   B 4   ? 0.2005 0.2128 0.2070 -0.0541 -0.0543 0.0849  4   ASN   B N   
3991 C CA  . ASN   B 4   ? 0.1932 0.2082 0.1859 -0.0564 -0.0403 0.0450  4   ASN   B CA  
3992 C C   . ASN   B 4   ? 0.2067 0.2190 0.1779 -0.0617 -0.0249 0.0336  4   ASN   B C   
3993 O O   . ASN   B 4   ? 0.2098 0.2273 0.2018 -0.0600 -0.0243 0.0142  4   ASN   B O   
3994 C CB  . ASN   B 4   ? 0.1790 0.2003 0.1694 -0.0464 -0.0501 0.0394  4   ASN   B CB  
3995 C CG  . ASN   B 4   ? 0.1753 0.1855 0.1563 -0.0461 -0.0519 0.0312  4   ASN   B CG  
3996 O OD1 . ASN   B 4   ? 0.1791 0.1724 0.1674 -0.0477 -0.0483 0.0240  4   ASN   B OD1 
3997 N ND2 . ASN   B 4   ? 0.1909 0.1900 0.1705 -0.0289 -0.0401 0.0260  4   ASN   B ND2 
4005 N N   . SER   B 5   ? 0.2278 0.2362 0.1948 -0.0628 -0.0080 0.0336  5   SER   B N   
4006 C CA  . SER   B 5   ? 0.2537 0.2652 0.2321 -0.0513 0.0136  0.0322  5   SER   B CA  
4007 C C   . SER   B 5   ? 0.2639 0.2665 0.2521 -0.0632 0.0369  0.0347  5   SER   B C   
4008 O O   . SER   B 5   ? 0.2783 0.2659 0.3121 -0.0572 0.0544  0.0241  5   SER   B O   
4009 C CB  . SER   B 5   ? 0.2648 0.2864 0.2674 -0.0394 0.0139  0.0377  5   SER   B CB  
4010 O OG  . SER   B 5   ? 0.2810 0.3091 0.3172 -0.0245 0.0184  0.0395  5   SER   B OG  
4016 N N   . PHE   B 6   ? 0.2711 0.2770 0.2210 -0.0644 0.0403  0.0335  6   PHE   B N   
4017 C CA  . PHE   B 6   ? 0.2754 0.2750 0.2016 -0.0748 0.0430  0.0164  6   PHE   B CA  
4018 C C   . PHE   B 6   ? 0.3268 0.3032 0.2349 -0.0778 0.0626  -0.0091 6   PHE   B C   
4019 O O   . PHE   B 6   ? 0.3402 0.3348 0.2657 -0.0689 0.0422  -0.0224 6   PHE   B O   
4020 C CB  . PHE   B 6   ? 0.2401 0.2524 0.1769 -0.0671 0.0267  0.0157  6   PHE   B CB  
4021 C CG  . PHE   B 6   ? 0.2092 0.2237 0.1694 -0.0642 0.0138  0.0148  6   PHE   B CG  
4022 C CD1 . PHE   B 6   ? 0.2031 0.2016 0.1559 -0.0598 -0.0010 0.0127  6   PHE   B CD1 
4023 C CD2 . PHE   B 6   ? 0.1955 0.2226 0.1788 -0.0533 0.0059  0.0308  6   PHE   B CD2 
4024 C CE1 . PHE   B 6   ? 0.1987 0.1848 0.1722 -0.0470 -0.0060 0.0079  6   PHE   B CE1 
4025 C CE2 . PHE   B 6   ? 0.1914 0.2072 0.1958 -0.0445 0.0061  0.0325  6   PHE   B CE2 
4026 C CZ  . PHE   B 6   ? 0.1905 0.1898 0.1861 -0.0447 -0.0038 0.0175  6   PHE   B CZ  
4036 N N   A SER   B 7   ? 0.3442 0.2901 0.2429 -0.0899 0.0774  -0.0227 7   SER   B N   
4037 N N   B SER   B 7   ? 0.3444 0.2927 0.2433 -0.0888 0.0795  -0.0169 7   SER   B N   
4038 C CA  A SER   B 7   ? 0.3613 0.2885 0.2705 -0.0902 0.0874  -0.0339 7   SER   B CA  
4039 C CA  B SER   B 7   ? 0.3617 0.2943 0.2735 -0.0873 0.0910  -0.0227 7   SER   B CA  
4040 C C   A SER   B 7   ? 0.3583 0.2746 0.2601 -0.0931 0.0974  -0.0358 7   SER   B C   
4041 C C   B SER   B 7   ? 0.3593 0.2831 0.2606 -0.0893 0.0981  -0.0244 7   SER   B C   
4042 O O   A SER   B 7   ? 0.3617 0.2762 0.2764 -0.0943 0.0973  -0.0337 7   SER   B O   
4043 O O   B SER   B 7   ? 0.3628 0.2870 0.2773 -0.0900 0.0968  -0.0218 7   SER   B O   
4044 C CB  A SER   B 7   ? 0.3753 0.2980 0.3104 -0.0858 0.0918  -0.0397 7   SER   B CB  
4045 C CB  B SER   B 7   ? 0.3753 0.3043 0.3172 -0.0812 0.0973  -0.0260 7   SER   B CB  
4046 O OG  A SER   B 7   ? 0.3845 0.3071 0.3491 -0.0838 0.0893  -0.0415 7   SER   B OG  
4047 O OG  B SER   B 7   ? 0.3843 0.3138 0.3564 -0.0771 0.0941  -0.0260 7   SER   B OG  
4058 N N   A GLY   B 8   ? 0.3545 0.2606 0.2572 -0.0876 0.1029  -0.0405 8   GLY   B N   
4059 N N   B GLY   B 8   ? 0.3551 0.2692 0.2577 -0.0838 0.1018  -0.0308 8   GLY   B N   
4060 C CA  A GLY   B 8   ? 0.3454 0.2448 0.2594 -0.0856 0.1060  -0.0430 8   GLY   B CA  
4061 C CA  B GLY   B 8   ? 0.3453 0.2526 0.2597 -0.0822 0.1035  -0.0371 8   GLY   B CA  
4062 C C   A GLY   B 8   ? 0.3338 0.2247 0.2524 -0.0856 0.1044  -0.0450 8   GLY   B C   
4063 C C   B GLY   B 8   ? 0.3327 0.2317 0.2512 -0.0826 0.1001  -0.0439 8   GLY   B C   
4064 O O   A GLY   B 8   ? 0.3370 0.2227 0.2707 -0.0842 0.1098  -0.0462 8   GLY   B O   
4065 O O   B GLY   B 8   ? 0.3354 0.2373 0.2646 -0.0758 0.1016  -0.0479 8   GLY   B O   
4072 N N   . TYR   B 9   ? 0.3238 0.2132 0.2311 -0.0767 0.0918  -0.0535 9   TYR   B N   
4073 C CA  . TYR   B 9   ? 0.3033 0.1874 0.2037 -0.0602 0.0608  -0.0447 9   TYR   B CA  
4074 C C   . TYR   B 9   ? 0.2943 0.1933 0.1892 -0.0502 0.0324  -0.0286 9   TYR   B C   
4075 O O   . TYR   B 9   ? 0.3113 0.2145 0.2171 -0.0514 0.0252  -0.0113 9   TYR   B O   
4076 C CB  . TYR   B 9   ? 0.3015 0.1693 0.2133 -0.0463 0.0632  -0.0361 9   TYR   B CB  
4077 C CG  . TYR   B 9   ? 0.2919 0.1504 0.2217 -0.0543 0.0627  -0.0411 9   TYR   B CG  
4078 C CD1 . TYR   B 9   ? 0.2959 0.1559 0.2486 -0.0685 0.0665  -0.0391 9   TYR   B CD1 
4079 C CD2 . TYR   B 9   ? 0.2788 0.1477 0.2093 -0.0487 0.0569  -0.0431 9   TYR   B CD2 
4080 C CE1 . TYR   B 9   ? 0.2904 0.1587 0.2408 -0.0779 0.0730  -0.0490 9   TYR   B CE1 
4081 C CE2 . TYR   B 9   ? 0.2771 0.1523 0.2252 -0.0514 0.0569  -0.0430 9   TYR   B CE2 
4082 C CZ  . TYR   B 9   ? 0.2834 0.1683 0.2411 -0.0649 0.0669  -0.0567 9   TYR   B CZ  
4083 O OH  . TYR   B 9   ? 0.2778 0.1826 0.2599 -0.0765 0.0712  -0.0668 9   TYR   B OH  
4094 N N   . LEU   B 10  ? 0.2687 0.1733 0.1676 -0.0451 0.0080  -0.0311 10  LEU   B N   
4095 C CA  . LEU   B 10  ? 0.2654 0.1676 0.1625 -0.0497 -0.0146 -0.0244 10  LEU   B CA  
4096 C C   . LEU   B 10  ? 0.2439 0.1632 0.1629 -0.0554 -0.0314 -0.0240 10  LEU   B C   
4097 O O   . LEU   B 10  ? 0.2315 0.1595 0.1703 -0.0365 -0.0297 -0.0116 10  LEU   B O   
4098 C CB  . LEU   B 10  ? 0.2835 0.1664 0.1722 -0.0562 -0.0316 -0.0142 10  LEU   B CB  
4099 C CG  . LEU   B 10  ? 0.3039 0.1742 0.2082 -0.0542 -0.0562 -0.0051 10  LEU   B CG  
4100 C CD1 . LEU   B 10  ? 0.3177 0.1876 0.2376 -0.0509 -0.0522 -0.0066 10  LEU   B CD1 
4101 C CD2 . LEU   B 10  ? 0.3154 0.1820 0.2371 -0.0497 -0.0535 0.0071  10  LEU   B CD2 
4113 N N   . LYS   B 11  ? 0.2528 0.1950 0.1709 -0.0460 -0.0342 -0.0213 11  LYS   B N   
4114 C CA  . LYS   B 11  ? 0.2634 0.2247 0.1951 -0.0334 -0.0526 -0.0281 11  LYS   B CA  
4115 C C   . LYS   B 11  ? 0.2511 0.2050 0.2072 -0.0565 -0.0448 -0.0435 11  LYS   B C   
4116 O O   . LYS   B 11  ? 0.2680 0.2227 0.2396 -0.0683 -0.0340 -0.0724 11  LYS   B O   
4117 C CB  . LYS   B 11  ? 0.2940 0.2761 0.2509 -0.0066 -0.0519 -0.0191 11  LYS   B CB  
4118 C CG  . LYS   B 11  ? 0.3263 0.3112 0.3285 0.0083  -0.0431 -0.0208 11  LYS   B CG  
4119 C CD  . LYS   B 11  ? 0.3520 0.3379 0.4052 0.0133  -0.0347 -0.0277 11  LYS   B CD  
4120 C CE  . LYS   B 11  ? 0.3707 0.3552 0.4620 0.0131  -0.0266 -0.0333 11  LYS   B CE  
4121 N NZ  . LYS   B 11  ? 0.3800 0.3660 0.4955 0.0111  -0.0228 -0.0345 11  LYS   B NZ  
4135 N N   . LEU   B 12  ? 0.2232 0.1794 0.2050 -0.0500 -0.0403 -0.0357 12  LEU   B N   
4136 C CA  . LEU   B 12  ? 0.2109 0.1621 0.2239 -0.0437 -0.0369 -0.0316 12  LEU   B CA  
4137 C C   . LEU   B 12  ? 0.2021 0.1637 0.2344 -0.0485 -0.0500 -0.0251 12  LEU   B C   
4138 O O   . LEU   B 12  ? 0.2044 0.1685 0.2490 -0.0577 -0.0589 -0.0185 12  LEU   B O   
4139 C CB  . LEU   B 12  ? 0.2121 0.1424 0.2281 -0.0341 -0.0276 -0.0346 12  LEU   B CB  
4140 C CG  . LEU   B 12  ? 0.2077 0.1396 0.2384 -0.0333 -0.0256 -0.0265 12  LEU   B CG  
4141 C CD1 . LEU   B 12  ? 0.2159 0.1456 0.2430 -0.0196 -0.0206 -0.0190 12  LEU   B CD1 
4142 C CD2 . LEU   B 12  ? 0.2118 0.1400 0.2616 -0.0305 -0.0227 -0.0280 12  LEU   B CD2 
4154 N N   . THR   B 13  ? 0.1969 0.1661 0.2346 -0.0460 -0.0459 -0.0318 13  THR   B N   
4155 C CA  . THR   B 13  ? 0.1963 0.1744 0.2226 -0.0510 -0.0502 -0.0190 13  THR   B CA  
4156 C C   . THR   B 13  ? 0.2278 0.1892 0.2393 -0.0587 -0.0689 -0.0166 13  THR   B C   
4157 O O   . THR   B 13  ? 0.2404 0.1880 0.2632 -0.0632 -0.0274 -0.0188 13  THR   B O   
4158 C CB  . THR   B 13  ? 0.1785 0.1789 0.2234 -0.0471 -0.0553 -0.0171 13  THR   B CB  
4159 O OG1 . THR   B 13  ? 0.1733 0.1734 0.2368 -0.0370 -0.0464 -0.0206 13  THR   B OG1 
4160 C CG2 . THR   B 13  ? 0.1880 0.1914 0.2267 -0.0411 -0.0462 -0.0046 13  THR   B CG2 
4168 N N   A ASP   B 14  ? 0.2403 0.1997 0.2537 -0.0583 -0.0947 -0.0054 14  ASP   B N   
4169 N N   B ASP   B 14  ? 0.2423 0.2020 0.2510 -0.0547 -0.0930 -0.0030 14  ASP   B N   
4170 C CA  A ASP   B 14  ? 0.2506 0.2133 0.2822 -0.0586 -0.0989 0.0106  14  ASP   B CA  
4171 C CA  B ASP   B 14  ? 0.2545 0.2183 0.2785 -0.0518 -0.0944 0.0146  14  ASP   B CA  
4172 C C   A ASP   B 14  ? 0.2370 0.1961 0.2502 -0.0601 -0.0838 0.0101  14  ASP   B C   
4173 C C   B ASP   B 14  ? 0.2393 0.1988 0.2535 -0.0560 -0.0822 0.0116  14  ASP   B C   
4174 O O   A ASP   B 14  ? 0.2548 0.2102 0.2485 -0.0601 -0.0783 0.0165  14  ASP   B O   
4175 O O   B ASP   B 14  ? 0.2577 0.2122 0.2607 -0.0542 -0.0791 0.0164  14  ASP   B O   
4176 C CB  A ASP   B 14  ? 0.2692 0.2405 0.3508 -0.0579 -0.1062 0.0128  14  ASP   B CB  
4177 C CB  B ASP   B 14  ? 0.2769 0.2504 0.3412 -0.0446 -0.0945 0.0198  14  ASP   B CB  
4178 C CG  A ASP   B 14  ? 0.2895 0.2633 0.4191 -0.0565 -0.0990 0.0060  14  ASP   B CG  
4179 C CG  B ASP   B 14  ? 0.3009 0.2785 0.4051 -0.0373 -0.0807 0.0138  14  ASP   B CG  
4180 O OD1 A ASP   B 14  ? 0.2986 0.2701 0.4366 -0.0638 -0.0973 -0.0008 14  ASP   B OD1 
4181 O OD1 B ASP   B 14  ? 0.3118 0.2913 0.4210 -0.0372 -0.0702 0.0106  14  ASP   B OD1 
4182 O OD2 A ASP   B 14  ? 0.2960 0.2738 0.4535 -0.0555 -0.0923 0.0080  14  ASP   B OD2 
4183 O OD2 B ASP   B 14  ? 0.3089 0.2899 0.4352 -0.0381 -0.0773 0.0129  14  ASP   B OD2 
4192 N N   . ASN   B 15  ? 0.2060 0.1711 0.2243 -0.0487 -0.0802 0.0076  15  ASN   B N   
4193 C CA  . ASN   B 15  ? 0.1677 0.1488 0.2096 -0.0252 -0.0519 0.0006  15  ASN   B CA  
4194 C C   . ASN   B 15  ? 0.1515 0.1406 0.2058 -0.0184 -0.0372 -0.0068 15  ASN   B C   
4195 O O   . ASN   B 15  ? 0.1520 0.1344 0.2184 -0.0182 -0.0453 -0.0143 15  ASN   B O   
4196 C CB  . ASN   B 15  ? 0.1611 0.1544 0.2303 -0.0132 -0.0459 -0.0033 15  ASN   B CB  
4197 C CG  . ASN   B 15  ? 0.1535 0.1456 0.2305 -0.0174 -0.0300 0.0010  15  ASN   B CG  
4198 O OD1 . ASN   B 15  ? 0.1570 0.1721 0.2508 -0.0342 -0.0332 0.0078  15  ASN   B OD1 
4199 N ND2 . ASN   B 15  ? 0.1534 0.1291 0.2218 -0.0113 -0.0125 -0.0103 15  ASN   B ND2 
4207 N N   . VAL   B 16  ? 0.1504 0.1326 0.2004 -0.0266 -0.0417 -0.0024 16  VAL   B N   
4208 C CA  . VAL   B 16  ? 0.1543 0.1339 0.1847 -0.0220 -0.0319 -0.0200 16  VAL   B CA  
4209 C C   . VAL   B 16  ? 0.1562 0.1382 0.1858 -0.0288 -0.0330 -0.0135 16  VAL   B C   
4210 O O   . VAL   B 16  ? 0.1666 0.1526 0.1995 -0.0307 -0.0291 -0.0321 16  VAL   B O   
4211 C CB  . VAL   B 16  ? 0.1625 0.1378 0.1978 -0.0096 -0.0182 -0.0216 16  VAL   B CB  
4212 C CG1 . VAL   B 16  ? 0.1744 0.1272 0.2026 0.0022  -0.0181 -0.0154 16  VAL   B CG1 
4213 C CG2 . VAL   B 16  ? 0.1613 0.1451 0.2131 -0.0081 -0.0191 -0.0183 16  VAL   B CG2 
4223 N N   . TYR   B 17  ? 0.1612 0.1432 0.1797 -0.0265 -0.0318 -0.0156 17  TYR   B N   
4224 C CA  . TYR   B 17  ? 0.1677 0.1533 0.1764 -0.0276 -0.0271 -0.0011 17  TYR   B CA  
4225 C C   . TYR   B 17  ? 0.1592 0.1366 0.1721 -0.0307 -0.0147 -0.0113 17  TYR   B C   
4226 O O   . TYR   B 17  ? 0.1582 0.1409 0.1795 -0.0237 -0.0239 -0.0271 17  TYR   B O   
4227 C CB  . TYR   B 17  ? 0.1983 0.1917 0.1929 -0.0164 -0.0296 0.0290  17  TYR   B CB  
4228 C CG  . TYR   B 17  ? 0.2278 0.2350 0.2217 -0.0108 -0.0362 0.0319  17  TYR   B CG  
4229 C CD1 . TYR   B 17  ? 0.2465 0.2484 0.2357 -0.0040 -0.0491 0.0431  17  TYR   B CD1 
4230 C CD2 . TYR   B 17  ? 0.2478 0.2635 0.2430 -0.0035 -0.0477 0.0264  17  TYR   B CD2 
4231 C CE1 . TYR   B 17  ? 0.2621 0.2709 0.2481 0.0015  -0.0549 0.0342  17  TYR   B CE1 
4232 C CE2 . TYR   B 17  ? 0.2628 0.2809 0.2606 0.0082  -0.0585 0.0281  17  TYR   B CE2 
4233 C CZ  . TYR   B 17  ? 0.2747 0.2890 0.2655 0.0095  -0.0609 0.0349  17  TYR   B CZ  
4234 O OH  . TYR   B 17  ? 0.2931 0.3107 0.2969 0.0177  -0.0622 0.0361  17  TYR   B OH  
4244 N N   . ILE   B 18  ? 0.1721 0.1341 0.1567 -0.0303 -0.0109 -0.0144 18  ILE   B N   
4245 C CA  . ILE   B 18  ? 0.1726 0.1259 0.1491 -0.0299 -0.0194 -0.0154 18  ILE   B CA  
4246 C C   . ILE   B 18  ? 0.1857 0.1346 0.1461 -0.0329 -0.0065 -0.0222 18  ILE   B C   
4247 O O   . ILE   B 18  ? 0.2071 0.1537 0.1596 -0.0315 -0.0080 -0.0328 18  ILE   B O   
4248 C CB  . ILE   B 18  ? 0.1778 0.1320 0.1703 -0.0321 -0.0180 -0.0118 18  ILE   B CB  
4249 C CG1 . ILE   B 18  ? 0.1829 0.1344 0.1878 -0.0328 -0.0115 -0.0041 18  ILE   B CG1 
4250 C CG2 . ILE   B 18  ? 0.1837 0.1387 0.1759 -0.0386 -0.0096 -0.0101 18  ILE   B CG2 
4251 C CD1 . ILE   B 18  ? 0.1894 0.1654 0.2103 -0.0348 -0.0179 0.0194  18  ILE   B CD1 
4263 N N   . LYS   B 19  ? 0.1821 0.1354 0.1654 -0.0192 0.0193  -0.0311 19  LYS   B N   
4264 C CA  . LYS   B 19  ? 0.1929 0.1385 0.1737 -0.0207 0.0212  -0.0336 19  LYS   B CA  
4265 C C   . LYS   B 19  ? 0.1771 0.1397 0.1854 -0.0192 0.0195  -0.0293 19  LYS   B C   
4266 O O   . LYS   B 19  ? 0.1694 0.1371 0.1849 -0.0104 0.0112  -0.0301 19  LYS   B O   
4267 C CB  . LYS   B 19  ? 0.2110 0.1561 0.1829 -0.0301 0.0342  -0.0179 19  LYS   B CB  
4268 C CG  . LYS   B 19  ? 0.2362 0.1784 0.2019 -0.0327 0.0393  -0.0172 19  LYS   B CG  
4269 C CD  . LYS   B 19  ? 0.2605 0.2067 0.2209 -0.0470 0.0415  -0.0052 19  LYS   B CD  
4270 C CE  . LYS   B 19  ? 0.2825 0.2314 0.2514 -0.0475 0.0377  -0.0087 19  LYS   B CE  
4271 N NZ  . LYS   B 19  ? 0.2934 0.2449 0.2717 -0.0546 0.0390  -0.0065 19  LYS   B NZ  
4285 N N   . ASN   B 20  ? 0.1747 0.1541 0.2195 -0.0180 0.0263  -0.0422 20  ASN   B N   
4286 C CA  . ASN   B 20  ? 0.1790 0.1660 0.2362 -0.0131 0.0237  -0.0544 20  ASN   B CA  
4287 C C   . ASN   B 20  ? 0.1755 0.1796 0.2362 -0.0208 0.0381  -0.0626 20  ASN   B C   
4288 O O   . ASN   B 20  ? 0.1885 0.2134 0.2616 -0.0315 0.0402  -0.0613 20  ASN   B O   
4289 C CB  . ASN   B 20  ? 0.1989 0.1658 0.2578 0.0074  0.0187  -0.0579 20  ASN   B CB  
4290 C CG  . ASN   B 20  ? 0.2234 0.1697 0.2895 0.0379  0.0164  -0.0642 20  ASN   B CG  
4291 O OD1 . ASN   B 20  ? 0.2529 0.1998 0.3188 0.0562  0.0173  -0.0716 20  ASN   B OD1 
4292 N ND2 . ASN   B 20  ? 0.2175 0.1686 0.2931 0.0353  0.0059  -0.0672 20  ASN   B ND2 
4299 N N   . ALA   B 21  ? 0.1760 0.1636 0.2274 -0.0268 0.0493  -0.0522 21  ALA   B N   
4300 C CA  . ALA   B 21  ? 0.1867 0.1736 0.2466 -0.0315 0.0318  -0.0432 21  ALA   B CA  
4301 C C   . ALA   B 21  ? 0.1829 0.1546 0.2426 -0.0201 0.0207  -0.0308 21  ALA   B C   
4302 O O   . ALA   B 21  ? 0.1826 0.1444 0.2640 -0.0247 0.0190  -0.0232 21  ALA   B O   
4303 C CB  . ALA   B 21  ? 0.2041 0.2033 0.2612 -0.0422 0.0362  -0.0181 21  ALA   B CB  
4309 N N   . ASP   B 22  ? 0.1735 0.1434 0.2353 -0.0202 0.0156  -0.0314 22  ASP   B N   
4310 C CA  . ASP   B 22  ? 0.1694 0.1387 0.2278 -0.0074 0.0155  -0.0217 22  ASP   B CA  
4311 C C   . ASP   B 22  ? 0.1646 0.1351 0.1976 -0.0099 0.0125  -0.0092 22  ASP   B C   
4312 O O   . ASP   B 22  ? 0.1689 0.1382 0.2017 -0.0086 0.0044  0.0001  22  ASP   B O   
4313 C CB  . ASP   B 22  ? 0.1785 0.1465 0.2526 -0.0068 0.0172  -0.0033 22  ASP   B CB  
4314 C CG  . ASP   B 22  ? 0.1823 0.1612 0.3006 -0.0045 -0.0056 0.0013  22  ASP   B CG  
4315 O OD1 . ASP   B 22  ? 0.1981 0.1511 0.3123 0.0010  -0.0198 0.0009  22  ASP   B OD1 
4316 O OD2 . ASP   B 22  ? 0.1919 0.1901 0.3488 0.0061  -0.0255 -0.0081 22  ASP   B OD2 
4321 N N   . ILE   B 23  ? 0.1651 0.1279 0.1823 -0.0103 0.0061  0.0127  23  ILE   B N   
4322 C CA  . ILE   B 23  ? 0.1555 0.1289 0.1642 -0.0120 -0.0007 0.0055  23  ILE   B CA  
4323 C C   . ILE   B 23  ? 0.1473 0.1269 0.1622 -0.0082 -0.0091 0.0002  23  ILE   B C   
4324 O O   . ILE   B 23  ? 0.1476 0.1277 0.1565 -0.0110 -0.0002 -0.0002 23  ILE   B O   
4325 C CB  . ILE   B 23  ? 0.1532 0.1352 0.1802 -0.0151 0.0004  0.0095  23  ILE   B CB  
4326 C CG1 . ILE   B 23  ? 0.1530 0.1472 0.2057 -0.0139 0.0109  0.0178  23  ILE   B CG1 
4327 C CG2 . ILE   B 23  ? 0.1667 0.1554 0.1893 -0.0121 0.0038  0.0006  23  ILE   B CG2 
4328 C CD1 . ILE   B 23  ? 0.1621 0.1575 0.2203 -0.0100 0.0086  0.0121  23  ILE   B CD1 
4340 N N   . VAL   B 24  ? 0.1486 0.1316 0.1774 -0.0096 -0.0071 0.0006  24  VAL   B N   
4341 C CA  . VAL   B 24  ? 0.1474 0.1365 0.1904 -0.0075 -0.0148 -0.0004 24  VAL   B CA  
4342 C C   . VAL   B 24  ? 0.1472 0.1408 0.2013 -0.0112 -0.0098 0.0053  24  VAL   B C   
4343 O O   . VAL   B 24  ? 0.1486 0.1425 0.2152 -0.0152 -0.0062 0.0104  24  VAL   B O   
4344 C CB  . VAL   B 24  ? 0.1577 0.1496 0.1952 -0.0011 -0.0205 -0.0033 24  VAL   B CB  
4345 C CG1 . VAL   B 24  ? 0.1586 0.1598 0.2151 -0.0086 -0.0212 0.0000  24  VAL   B CG1 
4346 C CG2 . VAL   B 24  ? 0.1666 0.1780 0.2151 0.0069  -0.0231 -0.0102 24  VAL   B CG2 
4356 N N   . GLU   B 25  ? 0.1736 0.1483 0.2084 -0.0151 -0.0038 0.0063  25  GLU   B N   
4357 C CA  . GLU   B 25  ? 0.1823 0.1737 0.2252 -0.0050 0.0060  0.0008  25  GLU   B CA  
4358 C C   . GLU   B 25  ? 0.1725 0.1637 0.2014 -0.0106 0.0093  -0.0006 25  GLU   B C   
4359 O O   . GLU   B 25  ? 0.1762 0.1828 0.2097 -0.0077 0.0139  0.0079  25  GLU   B O   
4360 C CB  . GLU   B 25  ? 0.2147 0.2186 0.2687 0.0167  0.0091  0.0021  25  GLU   B CB  
4361 C CG  . GLU   B 25  ? 0.2518 0.2797 0.3701 0.0273  0.0019  -0.0018 25  GLU   B CG  
4362 C CD  . GLU   B 25  ? 0.2981 0.3406 0.4671 0.0243  -0.0033 -0.0041 25  GLU   B CD  
4363 O OE1 . GLU   B 25  ? 0.3139 0.3625 0.4995 0.0267  -0.0004 -0.0013 25  GLU   B OE1 
4364 O OE2 . GLU   B 25  ? 0.3073 0.3605 0.5018 0.0259  -0.0101 -0.0081 25  GLU   B OE2 
4371 N N   . GLU   B 26  ? 0.1720 0.1533 0.1770 -0.0252 -0.0006 0.0072  26  GLU   B N   
4372 C CA  . GLU   B 26  ? 0.1697 0.1704 0.1787 -0.0402 -0.0089 0.0114  26  GLU   B CA  
4373 C C   . GLU   B 26  ? 0.1523 0.1688 0.1800 -0.0259 0.0027  0.0273  26  GLU   B C   
4374 O O   . GLU   B 26  ? 0.1701 0.1942 0.1901 -0.0211 0.0038  0.0336  26  GLU   B O   
4375 C CB  . GLU   B 26  ? 0.2040 0.1918 0.1886 -0.0457 -0.0099 0.0174  26  GLU   B CB  
4376 C CG  . GLU   B 26  ? 0.2443 0.2229 0.2339 -0.0494 -0.0011 -0.0044 26  GLU   B CG  
4377 C CD  . GLU   B 26  ? 0.2718 0.2460 0.2460 -0.0691 0.0124  -0.0349 26  GLU   B CD  
4378 O OE1 . GLU   B 26  ? 0.2900 0.2333 0.2446 -0.0781 0.0475  -0.0305 26  GLU   B OE1 
4379 O OE2 . GLU   B 26  ? 0.2752 0.2856 0.2663 -0.0678 0.0165  -0.0238 26  GLU   B OE2 
4386 N N   . ALA   B 27  ? 0.1415 0.1523 0.1772 -0.0209 0.0043  0.0220  27  ALA   B N   
4387 C CA  . ALA   B 27  ? 0.1430 0.1485 0.1921 -0.0151 0.0054  0.0264  27  ALA   B CA  
4388 C C   . ALA   B 27  ? 0.1487 0.1605 0.2192 -0.0101 0.0134  0.0352  27  ALA   B C   
4389 O O   . ALA   B 27  ? 0.1611 0.1630 0.2344 0.0010  0.0171  0.0443  27  ALA   B O   
4390 C CB  . ALA   B 27  ? 0.1609 0.1372 0.2051 -0.0155 0.0016  0.0156  27  ALA   B CB  
4396 N N   . LYS   B 28  ? 0.1430 0.1720 0.2552 -0.0116 0.0166  0.0479  28  LYS   B N   
4397 C CA  . LYS   B 28  ? 0.1572 0.1983 0.2748 -0.0052 0.0537  0.0665  28  LYS   B CA  
4398 C C   . LYS   B 28  ? 0.1797 0.2137 0.2599 0.0001  0.0540  0.0657  28  LYS   B C   
4399 O O   . LYS   B 28  ? 0.2057 0.2204 0.2752 -0.0050 0.0594  0.0650  28  LYS   B O   
4400 C CB  . LYS   B 28  ? 0.1745 0.2312 0.3253 -0.0013 0.0763  0.0866  28  LYS   B CB  
4401 C CG  . LYS   B 28  ? 0.2088 0.2754 0.3793 0.0131  0.0792  0.0949  28  LYS   B CG  
4402 C CD  . LYS   B 28  ? 0.2557 0.3286 0.4321 0.0243  0.0988  0.0976  28  LYS   B CD  
4403 C CE  . LYS   B 28  ? 0.2934 0.3675 0.4742 0.0337  0.1056  0.1041  28  LYS   B CE  
4404 N NZ  . LYS   B 28  ? 0.3156 0.3831 0.4943 0.0417  0.1050  0.1124  28  LYS   B NZ  
4418 N N   . LYS   B 29  ? 0.1910 0.2409 0.2595 0.0192  0.0582  0.0544  29  LYS   B N   
4419 C CA  . LYS   B 29  ? 0.2386 0.2778 0.2843 0.0190  0.0549  0.0559  29  LYS   B CA  
4420 C C   . LYS   B 29  ? 0.2311 0.2819 0.2418 0.0175  0.0449  0.0717  29  LYS   B C   
4421 O O   . LYS   B 29  ? 0.2491 0.3025 0.2545 0.0195  0.0445  0.0736  29  LYS   B O   
4422 C CB  . LYS   B 29  ? 0.2970 0.3177 0.3703 0.0166  0.0463  0.0415  29  LYS   B CB  
4423 C CG  . LYS   B 29  ? 0.3434 0.3511 0.4566 0.0134  0.0471  0.0384  29  LYS   B CG  
4424 C CD  . LYS   B 29  ? 0.3814 0.3795 0.5262 0.0080  0.0526  0.0324  29  LYS   B CD  
4425 C CE  . LYS   B 29  ? 0.4085 0.3983 0.5730 0.0022  0.0588  0.0291  29  LYS   B CE  
4426 N NZ  . LYS   B 29  ? 0.4202 0.4046 0.6008 -0.0002 0.0614  0.0272  29  LYS   B NZ  
4440 N N   . VAL   B 30  ? 0.2067 0.2664 0.2253 0.0084  0.0390  0.0810  30  VAL   B N   
4441 C CA  . VAL   B 30  ? 0.1959 0.2584 0.2576 -0.0022 0.0117  0.0857  30  VAL   B CA  
4442 C C   . VAL   B 30  ? 0.1757 0.2564 0.2677 -0.0010 0.0253  0.1033  30  VAL   B C   
4443 O O   . VAL   B 30  ? 0.1932 0.2770 0.2623 0.0113  0.0283  0.1196  30  VAL   B O   
4444 C CB  . VAL   B 30  ? 0.2003 0.2507 0.2966 -0.0127 -0.0193 0.0709  30  VAL   B CB  
4445 C CG1 . VAL   B 30  ? 0.2010 0.2554 0.3012 -0.0144 -0.0151 0.0591  30  VAL   B CG1 
4446 C CG2 . VAL   B 30  ? 0.2105 0.2491 0.3147 -0.0134 -0.0296 0.0609  30  VAL   B CG2 
4456 N N   . LYS   B 31  ? 0.1644 0.2207 0.3009 -0.0154 0.0235  0.1110  31  LYS   B N   
4457 C CA  . LYS   B 31  ? 0.1568 0.2147 0.3382 -0.0308 0.0075  0.1097  31  LYS   B CA  
4458 C C   . LYS   B 31  ? 0.1454 0.1788 0.2968 -0.0285 -0.0208 0.0894  31  LYS   B C   
4459 O O   . LYS   B 31  ? 0.1537 0.1989 0.3125 -0.0184 -0.0107 0.1065  31  LYS   B O   
4460 C CB  . LYS   B 31  ? 0.1817 0.2564 0.3910 -0.0306 0.0340  0.1256  31  LYS   B CB  
4461 C CG  . LYS   B 31  ? 0.2219 0.3017 0.4337 -0.0257 0.0406  0.1241  31  LYS   B CG  
4462 C CD  . LYS   B 31  ? 0.2632 0.3490 0.4691 -0.0183 0.0363  0.1115  31  LYS   B CD  
4463 C CE  . LYS   B 31  ? 0.2950 0.3817 0.5039 -0.0138 0.0283  0.1002  31  LYS   B CE  
4464 N NZ  . LYS   B 31  ? 0.3119 0.3996 0.5176 -0.0075 0.0173  0.0901  31  LYS   B NZ  
4478 N N   . PRO   B 32  ? 0.1527 0.1429 0.2274 -0.0280 -0.0418 0.0469  32  PRO   B N   
4479 C CA  . PRO   B 32  ? 0.1647 0.1385 0.1896 -0.0268 -0.0337 0.0319  32  PRO   B CA  
4480 C C   . PRO   B 32  ? 0.1786 0.1343 0.1772 -0.0295 -0.0540 0.0318  32  PRO   B C   
4481 O O   . PRO   B 32  ? 0.1939 0.1382 0.2026 -0.0307 -0.0766 0.0229  32  PRO   B O   
4482 C CB  . PRO   B 32  ? 0.1801 0.1330 0.1892 -0.0326 -0.0306 0.0245  32  PRO   B CB  
4483 C CG  . PRO   B 32  ? 0.1931 0.1267 0.1932 -0.0249 -0.0469 0.0221  32  PRO   B CG  
4484 C CD  . PRO   B 32  ? 0.1792 0.1354 0.2007 -0.0211 -0.0593 0.0230  32  PRO   B CD  
4492 N N   . THR   B 33  ? 0.1772 0.1282 0.1672 -0.0286 -0.0512 0.0261  33  THR   B N   
4493 C CA  . THR   B 33  ? 0.1855 0.1300 0.1607 -0.0326 -0.0457 0.0241  33  THR   B CA  
4494 C C   . THR   B 33  ? 0.1848 0.1199 0.1701 -0.0291 -0.0467 0.0164  33  THR   B C   
4495 O O   . THR   B 33  ? 0.2086 0.1248 0.1673 -0.0400 -0.0548 0.0173  33  THR   B O   
4496 C CB  . THR   B 33  ? 0.1891 0.1423 0.1736 -0.0168 -0.0481 0.0256  33  THR   B CB  
4497 O OG1 . THR   B 33  ? 0.1835 0.1500 0.1771 -0.0184 -0.0463 0.0284  33  THR   B OG1 
4498 C CG2 . THR   B 33  ? 0.2099 0.1493 0.1948 -0.0035 -0.0532 0.0183  33  THR   B CG2 
4506 N N   . VAL   B 34  ? 0.1720 0.1166 0.1492 -0.0278 -0.0441 0.0130  34  VAL   B N   
4507 C CA  . VAL   B 34  ? 0.1556 0.1179 0.1450 -0.0210 -0.0412 0.0035  34  VAL   B CA  
4508 C C   . VAL   B 34  ? 0.1414 0.1121 0.1458 -0.0238 -0.0246 0.0059  34  VAL   B C   
4509 O O   . VAL   B 34  ? 0.1576 0.1114 0.1399 -0.0221 -0.0301 0.0048  34  VAL   B O   
4510 C CB  . VAL   B 34  ? 0.1593 0.1286 0.1699 -0.0076 -0.0405 0.0002  34  VAL   B CB  
4511 C CG1 . VAL   B 34  ? 0.1599 0.1407 0.1753 -0.0070 -0.0272 -0.0038 34  VAL   B CG1 
4512 C CG2 . VAL   B 34  ? 0.1664 0.1359 0.2042 -0.0021 -0.0312 0.0016  34  VAL   B CG2 
4522 N N   . VAL   B 35  ? 0.1365 0.1121 0.1339 -0.0198 -0.0171 0.0054  35  VAL   B N   
4523 C CA  . VAL   B 35  ? 0.1321 0.1090 0.1289 -0.0185 -0.0072 0.0006  35  VAL   B CA  
4524 C C   . VAL   B 35  ? 0.1181 0.1069 0.1299 -0.0152 -0.0055 0.0039  35  VAL   B C   
4525 O O   . VAL   B 35  ? 0.1255 0.1083 0.1351 -0.0238 -0.0036 -0.0025 35  VAL   B O   
4526 C CB  . VAL   B 35  ? 0.1313 0.1243 0.1322 -0.0190 -0.0024 0.0019  35  VAL   B CB  
4527 C CG1 . VAL   B 35  ? 0.1273 0.1355 0.1406 -0.0157 0.0005  0.0028  35  VAL   B CG1 
4528 C CG2 . VAL   B 35  ? 0.1346 0.1243 0.1562 -0.0062 -0.0009 0.0068  35  VAL   B CG2 
4538 N N   . VAL   B 36  ? 0.1198 0.1063 0.1314 -0.0165 -0.0125 0.0094  36  VAL   B N   
4539 C CA  . VAL   B 36  ? 0.1196 0.1011 0.1314 -0.0135 -0.0117 0.0034  36  VAL   B CA  
4540 C C   . VAL   B 36  ? 0.1163 0.1020 0.1219 -0.0136 -0.0108 -0.0006 36  VAL   B C   
4541 O O   . VAL   B 36  ? 0.1261 0.1125 0.1324 -0.0081 -0.0059 -0.0075 36  VAL   B O   
4542 C CB  . VAL   B 36  ? 0.1221 0.1094 0.1272 -0.0107 -0.0043 0.0017  36  VAL   B CB  
4543 C CG1 . VAL   B 36  ? 0.1221 0.1177 0.1469 -0.0177 -0.0053 0.0004  36  VAL   B CG1 
4544 C CG2 . VAL   B 36  ? 0.1256 0.1154 0.1391 -0.0160 -0.0097 0.0020  36  VAL   B CG2 
4554 N N   . ASN   B 37  ? 0.1204 0.1111 0.1296 -0.0042 -0.0091 0.0050  37  ASN   B N   
4555 C CA  . ASN   B 37  ? 0.1188 0.1141 0.1308 0.0020  -0.0085 0.0073  37  ASN   B CA  
4556 C C   . ASN   B 37  ? 0.1195 0.1135 0.1235 0.0019  -0.0095 0.0005  37  ASN   B C   
4557 O O   . ASN   B 37  ? 0.1263 0.1203 0.1294 0.0026  -0.0019 0.0032  37  ASN   B O   
4558 C CB  . ASN   B 37  ? 0.1202 0.1169 0.1254 -0.0046 -0.0098 0.0043  37  ASN   B CB  
4559 C CG  . ASN   B 37  ? 0.1254 0.1173 0.1282 -0.0034 -0.0124 0.0042  37  ASN   B CG  
4560 O OD1 . ASN   B 37  ? 0.1354 0.1257 0.1400 0.0015  -0.0113 0.0026  37  ASN   B OD1 
4561 N ND2 . ASN   B 37  ? 0.1304 0.1150 0.1370 -0.0017 -0.0178 0.0025  37  ASN   B ND2 
4568 N N   . ALA   B 38  ? 0.1298 0.1129 0.1256 0.0042  0.0041  0.0044  38  ALA   B N   
4569 C CA  . ALA   B 38  ? 0.1329 0.1152 0.1335 -0.0019 0.0026  0.0065  38  ALA   B CA  
4570 C C   . ALA   B 38  ? 0.1360 0.1123 0.1292 -0.0039 0.0049  0.0080  38  ALA   B C   
4571 O O   . ALA   B 38  ? 0.1481 0.1253 0.1387 0.0059  -0.0074 0.0061  38  ALA   B O   
4572 C CB  . ALA   B 38  ? 0.1544 0.1204 0.1447 -0.0071 0.0115  -0.0013 38  ALA   B CB  
4578 N N   . ALA   B 39  ? 0.1370 0.1181 0.1231 0.0044  -0.0014 0.0013  39  ALA   B N   
4579 C CA  . ALA   B 39  ? 0.1451 0.1235 0.1170 -0.0005 -0.0018 0.0025  39  ALA   B CA  
4580 C C   . ALA   B 39  ? 0.1490 0.1306 0.1198 0.0027  -0.0032 -0.0014 39  ALA   B C   
4581 O O   . ALA   B 39  ? 0.1476 0.1383 0.1447 -0.0055 0.0036  0.0051  39  ALA   B O   
4582 C CB  . ALA   B 39  ? 0.1527 0.1233 0.1397 -0.0083 -0.0025 -0.0043 39  ALA   B CB  
4588 N N   . ASN   B 40  ? 0.1544 0.1551 0.1174 -0.0074 -0.0014 -0.0112 40  ASN   B N   
4589 C CA  . ASN   B 40  ? 0.1636 0.1608 0.1289 -0.0055 -0.0067 -0.0100 40  ASN   B CA  
4590 C C   . ASN   B 40  ? 0.1644 0.1597 0.1182 -0.0010 -0.0116 -0.0098 40  ASN   B C   
4591 O O   . ASN   B 40  ? 0.1595 0.1539 0.1275 0.0052  -0.0095 -0.0062 40  ASN   B O   
4592 C CB  . ASN   B 40  ? 0.1713 0.1535 0.1506 0.0064  -0.0108 0.0027  40  ASN   B CB  
4593 C CG  . ASN   B 40  ? 0.1791 0.1553 0.1927 -0.0028 -0.0230 0.0049  40  ASN   B CG  
4594 O OD1 . ASN   B 40  ? 0.1753 0.1562 0.2597 -0.0051 -0.0389 0.0083  40  ASN   B OD1 
4595 N ND2 . ASN   B 40  ? 0.1822 0.1609 0.1923 0.0006  -0.0192 0.0100  40  ASN   B ND2 
4602 N N   . VAL   B 41  ? 0.1720 0.1618 0.1227 0.0049  -0.0009 -0.0102 41  VAL   B N   
4603 C CA  . VAL   B 41  ? 0.1827 0.1727 0.1277 0.0059  0.0013  -0.0265 41  VAL   B CA  
4604 C C   . VAL   B 41  ? 0.1763 0.1728 0.1277 0.0187  -0.0077 -0.0254 41  VAL   B C   
4605 O O   . VAL   B 41  ? 0.1727 0.1690 0.1409 0.0179  -0.0135 -0.0249 41  VAL   B O   
4606 C CB  . VAL   B 41  ? 0.1967 0.1863 0.1433 -0.0012 0.0130  -0.0355 41  VAL   B CB  
4607 C CG1 . VAL   B 41  ? 0.1958 0.1902 0.1667 -0.0109 0.0272  -0.0331 41  VAL   B CG1 
4608 C CG2 . VAL   B 41  ? 0.2090 0.2023 0.1537 -0.0091 0.0119  -0.0265 41  VAL   B CG2 
4618 N N   . TYR   B 42  ? 0.1824 0.1738 0.1316 0.0157  -0.0179 -0.0065 42  TYR   B N   
4619 C CA  . TYR   B 42  ? 0.1877 0.1817 0.1507 0.0178  -0.0306 -0.0143 42  TYR   B CA  
4620 C C   . TYR   B 42  ? 0.1717 0.1649 0.1470 0.0182  -0.0305 -0.0175 42  TYR   B C   
4621 O O   . TYR   B 42  ? 0.1808 0.1685 0.1779 0.0119  -0.0374 -0.0309 42  TYR   B O   
4622 C CB  . TYR   B 42  ? 0.2127 0.2083 0.1652 0.0081  -0.0325 -0.0090 42  TYR   B CB  
4623 C CG  . TYR   B 42  ? 0.2205 0.2235 0.1643 -0.0023 -0.0215 0.0025  42  TYR   B CG  
4624 C CD1 . TYR   B 42  ? 0.2226 0.2238 0.1272 -0.0065 -0.0078 -0.0015 42  TYR   B CD1 
4625 C CD2 . TYR   B 42  ? 0.2368 0.2377 0.2038 -0.0079 -0.0080 0.0063  42  TYR   B CD2 
4626 C CE1 . TYR   B 42  ? 0.2382 0.2366 0.1445 -0.0063 0.0012  0.0013  42  TYR   B CE1 
4627 C CE2 . TYR   B 42  ? 0.2460 0.2463 0.1929 -0.0054 0.0091  0.0230  42  TYR   B CE2 
4628 C CZ  . TYR   B 42  ? 0.2551 0.2558 0.1820 0.0040  0.0214  0.0144  42  TYR   B CZ  
4629 O OH  . TYR   B 42  ? 0.2858 0.2849 0.2291 0.0197  0.0391  0.0280  42  TYR   B OH  
4639 N N   . LEU   B 43  ? 0.1644 0.1494 0.1387 0.0079  -0.0144 -0.0158 43  LEU   B N   
4640 C CA  . LEU   B 43  ? 0.1622 0.1381 0.1355 0.0050  -0.0138 -0.0104 43  LEU   B CA  
4641 C C   . LEU   B 43  ? 0.1654 0.1410 0.1445 0.0027  -0.0094 -0.0080 43  LEU   B C   
4642 O O   . LEU   B 43  ? 0.1565 0.1450 0.1778 -0.0014 -0.0226 0.0070  43  LEU   B O   
4643 C CB  . LEU   B 43  ? 0.1644 0.1331 0.1444 0.0045  -0.0219 -0.0153 43  LEU   B CB  
4644 C CG  . LEU   B 43  ? 0.1678 0.1345 0.1527 0.0003  -0.0248 -0.0105 43  LEU   B CG  
4645 C CD1 . LEU   B 43  ? 0.1727 0.1338 0.1907 -0.0004 -0.0384 -0.0114 43  LEU   B CD1 
4646 C CD2 . LEU   B 43  ? 0.1609 0.1378 0.1614 -0.0070 -0.0276 -0.0041 43  LEU   B CD2 
4658 N N   . LYS   B 44  ? 0.1636 0.1424 0.1383 0.0076  -0.0068 -0.0108 44  LYS   B N   
4659 C CA  . LYS   B 44  ? 0.1805 0.1527 0.1446 0.0029  -0.0123 0.0041  44  LYS   B CA  
4660 C C   . LYS   B 44  ? 0.1672 0.1446 0.1373 0.0041  -0.0129 -0.0014 44  LYS   B C   
4661 O O   . LYS   B 44  ? 0.1807 0.1489 0.1623 -0.0025 -0.0084 0.0006  44  LYS   B O   
4662 C CB  . LYS   B 44  ? 0.2105 0.1708 0.1515 0.0083  -0.0286 -0.0004 44  LYS   B CB  
4663 C CG  . LYS   B 44  ? 0.2479 0.1973 0.1880 0.0048  -0.0559 -0.0026 44  LYS   B CG  
4664 C CD  . LYS   B 44  ? 0.2820 0.2192 0.2401 -0.0048 -0.0680 -0.0084 44  LYS   B CD  
4665 C CE  . LYS   B 44  ? 0.3107 0.2437 0.2858 -0.0101 -0.0731 -0.0008 44  LYS   B CE  
4666 N NZ  . LYS   B 44  ? 0.3214 0.2514 0.3087 -0.0092 -0.0827 0.0101  44  LYS   B NZ  
4680 N N   . HIS   B 45  ? 0.1620 0.1447 0.1387 -0.0014 -0.0143 0.0065  45  HIS   B N   
4681 C CA  . HIS   B 45  ? 0.1639 0.1416 0.1402 0.0082  -0.0112 -0.0027 45  HIS   B CA  
4682 C C   . HIS   B 45  ? 0.1863 0.1576 0.1789 0.0155  -0.0286 -0.0062 45  HIS   B C   
4683 O O   . HIS   B 45  ? 0.1900 0.1875 0.2261 0.0448  -0.0073 -0.0026 45  HIS   B O   
4684 C CB  . HIS   B 45  ? 0.1511 0.1463 0.1379 0.0011  -0.0075 -0.0153 45  HIS   B CB  
4685 C CG  . HIS   B 45  ? 0.1512 0.1416 0.1462 -0.0043 -0.0148 -0.0098 45  HIS   B CG  
4686 N ND1 . HIS   B 45  ? 0.1521 0.1352 0.1452 0.0010  -0.0147 -0.0110 45  HIS   B ND1 
4687 C CD2 . HIS   B 45  ? 0.1595 0.1440 0.1575 -0.0088 -0.0188 -0.0041 45  HIS   B CD2 
4688 C CE1 . HIS   B 45  ? 0.1610 0.1307 0.1468 -0.0068 -0.0279 -0.0029 45  HIS   B CE1 
4689 N NE2 . HIS   B 45  ? 0.1651 0.1400 0.1487 -0.0051 -0.0192 -0.0060 45  HIS   B NE2 
4697 N N   A GLY   B 46  ? 0.2009 0.1629 0.2150 0.0142  -0.0412 0.0067  46  GLY   B N   
4698 N N   B GLY   B 46  ? 0.2024 0.1654 0.2118 0.0143  -0.0418 0.0103  46  GLY   B N   
4699 C CA  A GLY   B 46  ? 0.2071 0.1739 0.2477 0.0125  -0.0500 0.0045  46  GLY   B CA  
4700 C CA  B GLY   B 46  ? 0.2098 0.1790 0.2391 0.0125  -0.0522 0.0116  46  GLY   B CA  
4701 C C   A GLY   B 46  ? 0.2052 0.1823 0.2851 0.0187  -0.0446 0.0005  46  GLY   B C   
4702 C C   B GLY   B 46  ? 0.2091 0.1901 0.2729 0.0187  -0.0477 0.0119  46  GLY   B C   
4703 O O   A GLY   B 46  ? 0.2145 0.1923 0.3525 0.0187  -0.0265 -0.0208 46  GLY   B O   
4704 O O   B GLY   B 46  ? 0.2226 0.2085 0.3182 0.0179  -0.0352 0.0110  46  GLY   B O   
4711 N N   . GLY   B 47  ? 0.2014 0.1897 0.2607 0.0083  -0.0328 -0.0002 47  GLY   B N   
4712 C CA  . GLY   B 47  ? 0.1886 0.1657 0.2269 0.0026  -0.0259 0.0002  47  GLY   B CA  
4713 C C   . GLY   B 47  ? 0.1666 0.1418 0.1854 0.0013  -0.0073 0.0071  47  GLY   B C   
4714 O O   . GLY   B 47  ? 0.1772 0.1252 0.1875 0.0039  -0.0045 0.0081  47  GLY   B O   
4719 N N   . GLY   B 48  ? 0.1444 0.1345 0.1782 0.0023  -0.0188 0.0133  48  GLY   B N   
4720 C CA  . GLY   B 48  ? 0.1420 0.1279 0.1677 -0.0018 -0.0122 0.0116  48  GLY   B CA  
4721 C C   . GLY   B 48  ? 0.1392 0.1218 0.1649 -0.0010 -0.0030 0.0005  48  GLY   B C   
4722 O O   . GLY   B 48  ? 0.1374 0.1256 0.1841 0.0036  -0.0114 -0.0001 48  GLY   B O   
4726 N N   . VAL   B 49  ? 0.1409 0.1263 0.1528 0.0101  -0.0032 0.0046  49  VAL   B N   
4727 C CA  . VAL   B 49  ? 0.1436 0.1372 0.1443 0.0123  -0.0061 -0.0077 49  VAL   B CA  
4728 C C   . VAL   B 49  ? 0.1328 0.1345 0.1264 0.0126  -0.0066 0.0037  49  VAL   B C   
4729 O O   . VAL   B 49  ? 0.1392 0.1336 0.1518 0.0047  0.0019  0.0083  49  VAL   B O   
4730 C CB  . VAL   B 49  ? 0.1449 0.1578 0.1686 0.0035  -0.0221 0.0015  49  VAL   B CB  
4731 C CG1 . VAL   B 49  ? 0.1506 0.1689 0.1682 0.0058  -0.0314 0.0116  49  VAL   B CG1 
4732 C CG2 . VAL   B 49  ? 0.1610 0.1641 0.1911 -0.0037 -0.0418 -0.0027 49  VAL   B CG2 
4742 N N   . ALA   B 50  ? 0.1330 0.1242 0.1379 0.0034  -0.0041 0.0056  50  ALA   B N   
4743 C CA  . ALA   B 50  ? 0.1318 0.1223 0.1389 0.0053  -0.0104 0.0094  50  ALA   B CA  
4744 C C   . ALA   B 50  ? 0.1386 0.1266 0.1379 0.0070  0.0001  0.0056  50  ALA   B C   
4745 O O   . ALA   B 50  ? 0.1359 0.1273 0.1449 0.0025  -0.0038 0.0042  50  ALA   B O   
4746 C CB  . ALA   B 50  ? 0.1418 0.1232 0.1453 -0.0029 -0.0004 0.0053  50  ALA   B CB  
4752 N N   . GLY   B 51  ? 0.1362 0.1300 0.1471 0.0101  -0.0118 0.0118  51  GLY   B N   
4753 C CA  . GLY   B 51  ? 0.1356 0.1369 0.1642 0.0155  -0.0175 0.0135  51  GLY   B CA  
4754 C C   . GLY   B 51  ? 0.1403 0.1325 0.1679 0.0178  -0.0115 0.0128  51  GLY   B C   
4755 O O   . GLY   B 51  ? 0.1394 0.1412 0.1833 0.0078  -0.0103 0.0071  51  GLY   B O   
4759 N N   . ALA   B 52  ? 0.1364 0.1286 0.1594 0.0179  -0.0078 0.0139  52  ALA   B N   
4760 C CA  . ALA   B 52  ? 0.1427 0.1350 0.1601 0.0182  -0.0002 0.0016  52  ALA   B CA  
4761 C C   . ALA   B 52  ? 0.1329 0.1338 0.1502 0.0032  -0.0022 0.0107  52  ALA   B C   
4762 O O   . ALA   B 52  ? 0.1372 0.1413 0.1661 0.0108  0.0010  0.0061  52  ALA   B O   
4763 C CB  . ALA   B 52  ? 0.1613 0.1422 0.1663 0.0063  0.0039  0.0031  52  ALA   B CB  
4769 N N   . LEU   B 53  ? 0.1308 0.1294 0.1432 0.0134  0.0000  0.0068  53  LEU   B N   
4770 C CA  . LEU   B 53  ? 0.1290 0.1381 0.1386 0.0111  -0.0064 0.0080  53  LEU   B CA  
4771 C C   . LEU   B 53  ? 0.1368 0.1321 0.1404 0.0093  -0.0017 0.0104  53  LEU   B C   
4772 O O   . LEU   B 53  ? 0.1461 0.1355 0.1551 -0.0011 0.0002  0.0141  53  LEU   B O   
4773 C CB  . LEU   B 53  ? 0.1267 0.1452 0.1555 0.0136  -0.0102 0.0129  53  LEU   B CB  
4774 C CG  . LEU   B 53  ? 0.1267 0.1562 0.1558 -0.0005 -0.0022 0.0235  53  LEU   B CG  
4775 C CD1 . LEU   B 53  ? 0.1343 0.1772 0.1708 0.0094  -0.0092 0.0105  53  LEU   B CD1 
4776 C CD2 . LEU   B 53  ? 0.1428 0.1817 0.1748 -0.0137 -0.0023 -0.0078 53  LEU   B CD2 
4788 N N   . ASN   B 54  ? 0.1343 0.1255 0.1442 0.0049  -0.0051 0.0117  54  ASN   B N   
4789 C CA  . ASN   B 54  ? 0.1374 0.1335 0.1560 0.0019  -0.0104 0.0032  54  ASN   B CA  
4790 C C   . ASN   B 54  ? 0.1364 0.1378 0.1769 0.0015  -0.0066 0.0111  54  ASN   B C   
4791 O O   . ASN   B 54  ? 0.1341 0.1432 0.1868 -0.0033 -0.0028 0.0045  54  ASN   B O   
4792 C CB  . ASN   B 54  ? 0.1416 0.1495 0.1633 0.0009  -0.0014 0.0044  54  ASN   B CB  
4793 C CG  . ASN   B 54  ? 0.1427 0.1587 0.1586 0.0040  -0.0093 0.0049  54  ASN   B CG  
4794 O OD1 . ASN   B 54  ? 0.1418 0.1561 0.1762 -0.0004 -0.0145 -0.0026 54  ASN   B OD1 
4795 N ND2 . ASN   B 54  ? 0.1523 0.1834 0.1815 -0.0047 -0.0315 0.0168  54  ASN   B ND2 
4802 N N   . LYS   B 55  ? 0.1315 0.1433 0.1891 0.0088  -0.0003 0.0123  55  LYS   B N   
4803 C CA  . LYS   B 55  ? 0.1444 0.1595 0.2099 0.0183  0.0012  0.0110  55  LYS   B CA  
4804 C C   . LYS   B 55  ? 0.1320 0.1543 0.1986 0.0153  0.0010  0.0046  55  LYS   B C   
4805 O O   . LYS   B 55  ? 0.1256 0.1683 0.2112 0.0107  0.0023  0.0019  55  LYS   B O   
4806 C CB  . LYS   B 55  ? 0.1550 0.1730 0.2264 0.0325  0.0127  0.0348  55  LYS   B CB  
4807 C CG  . LYS   B 55  ? 0.1951 0.2028 0.3030 0.0389  0.0271  0.0419  55  LYS   B CG  
4808 C CD  . LYS   B 55  ? 0.2261 0.2295 0.3640 0.0511  0.0382  0.0446  55  LYS   B CD  
4809 C CE  . LYS   B 55  ? 0.2482 0.2532 0.4212 0.0564  0.0495  0.0460  55  LYS   B CE  
4810 N NZ  . LYS   B 55  ? 0.2549 0.2726 0.4530 0.0567  0.0326  0.0504  55  LYS   B NZ  
4824 N N   . ALA   B 56  ? 0.1352 0.1589 0.1796 0.0066  -0.0024 0.0030  56  ALA   B N   
4825 C CA  . ALA   B 56  ? 0.1404 0.1728 0.1749 0.0096  0.0050  0.0088  56  ALA   B CA  
4826 C C   . ALA   B 56  ? 0.1454 0.1709 0.1774 0.0056  0.0102  0.0173  56  ALA   B C   
4827 O O   . ALA   B 56  ? 0.1591 0.1790 0.2000 0.0065  0.0210  0.0184  56  ALA   B O   
4828 C CB  . ALA   B 56  ? 0.1513 0.1939 0.1823 -0.0082 -0.0047 0.0089  56  ALA   B CB  
4834 N N   . THR   B 57  ? 0.1436 0.1599 0.1819 0.0030  0.0145  0.0218  57  THR   B N   
4835 C CA  . THR   B 57  ? 0.1469 0.1606 0.1788 0.0010  0.0160  0.0211  57  THR   B CA  
4836 C C   . THR   B 57  ? 0.1479 0.1719 0.1970 -0.0043 0.0166  0.0159  57  THR   B C   
4837 O O   . THR   B 57  ? 0.1510 0.1747 0.2104 -0.0196 0.0048  0.0108  57  THR   B O   
4838 C CB  . THR   B 57  ? 0.1517 0.1448 0.1714 -0.0012 0.0116  0.0160  57  THR   B CB  
4839 O OG1 . THR   B 57  ? 0.1483 0.1413 0.1796 -0.0028 0.0032  0.0114  57  THR   B OG1 
4840 C CG2 . THR   B 57  ? 0.1468 0.1521 0.1710 -0.0033 0.0079  0.0074  57  THR   B CG2 
4848 N N   . ASN   B 58  ? 0.1343 0.1864 0.2147 -0.0120 -0.0019 -0.0039 58  ASN   B N   
4849 C CA  . ASN   B 58  ? 0.1505 0.2199 0.2501 -0.0196 0.0123  0.0005  58  ASN   B CA  
4850 C C   . ASN   B 58  ? 0.1350 0.1994 0.2197 -0.0155 -0.0117 0.0054  58  ASN   B C   
4851 O O   . ASN   B 58  ? 0.1455 0.2120 0.2236 -0.0182 -0.0151 -0.0010 58  ASN   B O   
4852 C CB  . ASN   B 58  ? 0.2213 0.2833 0.3545 -0.0352 0.0339  0.0067  58  ASN   B CB  
4853 C CG  . ASN   B 58  ? 0.3060 0.3406 0.4810 -0.0369 0.0407  0.0234  58  ASN   B CG  
4854 O OD1 . ASN   B 58  ? 0.3455 0.3582 0.5242 -0.0396 0.0435  0.0304  58  ASN   B OD1 
4855 N ND2 . ASN   B 58  ? 0.3500 0.3610 0.5273 -0.0376 0.0434  0.0261  58  ASN   B ND2 
4862 N N   . ASN   B 59  ? 0.1326 0.1856 0.2050 -0.0083 -0.0082 0.0066  59  ASN   B N   
4863 C CA  . ASN   B 59  ? 0.1360 0.1836 0.2053 -0.0085 -0.0167 0.0141  59  ASN   B CA  
4864 C C   . ASN   B 59  ? 0.1348 0.1781 0.1933 -0.0144 -0.0144 0.0074  59  ASN   B C   
4865 O O   . ASN   B 59  ? 0.1413 0.1809 0.1919 -0.0194 -0.0157 0.0061  59  ASN   B O   
4866 C CB  . ASN   B 59  ? 0.1484 0.2059 0.2132 -0.0060 -0.0329 0.0182  59  ASN   B CB  
4867 C CG  . ASN   B 59  ? 0.1587 0.2286 0.2416 0.0006  -0.0427 0.0085  59  ASN   B CG  
4868 O OD1 . ASN   B 59  ? 0.1612 0.2367 0.2396 0.0024  -0.0389 0.0144  59  ASN   B OD1 
4869 N ND2 . ASN   B 59  ? 0.1687 0.2426 0.2503 -0.0051 -0.0442 0.0101  59  ASN   B ND2 
4876 N N   . ALA   B 60  ? 0.1383 0.1659 0.1942 -0.0189 -0.0104 -0.0011 60  ALA   B N   
4877 C CA  . ALA   B 60  ? 0.1522 0.1573 0.2002 -0.0181 -0.0095 0.0072  60  ALA   B CA  
4878 C C   . ALA   B 60  ? 0.1479 0.1474 0.1754 -0.0144 -0.0112 0.0103  60  ALA   B C   
4879 O O   . ALA   B 60  ? 0.1473 0.1519 0.1803 -0.0139 -0.0083 0.0006  60  ALA   B O   
4880 C CB  . ALA   B 60  ? 0.1605 0.1532 0.2136 -0.0143 -0.0151 0.0103  60  ALA   B CB  
4886 N N   . MET   B 61  ? 0.1408 0.1424 0.1746 -0.0138 -0.0107 0.0072  61  MET   B N   
4887 C CA  . MET   B 61  ? 0.1341 0.1358 0.1693 -0.0104 -0.0181 0.0104  61  MET   B CA  
4888 C C   . MET   B 61  ? 0.1387 0.1334 0.1728 -0.0112 -0.0207 0.0010  61  MET   B C   
4889 O O   . MET   B 61  ? 0.1488 0.1311 0.1613 -0.0017 -0.0154 -0.0132 61  MET   B O   
4890 C CB  . MET   B 61  ? 0.1333 0.1403 0.1686 -0.0087 -0.0166 -0.0013 61  MET   B CB  
4891 C CG  . MET   B 61  ? 0.1296 0.1371 0.1656 -0.0000 -0.0118 0.0005  61  MET   B CG  
4892 S SD  . MET   B 61  ? 0.1349 0.1371 0.1739 -0.0021 -0.0081 -0.0074 61  MET   B SD  
4893 C CE  . MET   B 61  ? 0.1377 0.1494 0.1964 0.0007  -0.0132 -0.0258 61  MET   B CE  
4903 N N   . GLN   B 62  ? 0.1375 0.1383 0.1693 -0.0040 -0.0248 0.0065  62  GLN   B N   
4904 C CA  . GLN   B 62  ? 0.1433 0.1420 0.1760 -0.0024 -0.0238 0.0039  62  GLN   B CA  
4905 C C   . GLN   B 62  ? 0.1405 0.1517 0.1684 -0.0074 -0.0298 -0.0049 62  GLN   B C   
4906 O O   . GLN   B 62  ? 0.1517 0.1531 0.1671 -0.0025 -0.0326 -0.0084 62  GLN   B O   
4907 C CB  . GLN   B 62  ? 0.1429 0.1495 0.1708 0.0008  -0.0208 0.0056  62  GLN   B CB  
4908 C CG  . GLN   B 62  ? 0.1499 0.1583 0.1704 0.0035  -0.0286 0.0001  62  GLN   B CG  
4909 C CD  . GLN   B 62  ? 0.1488 0.1541 0.1577 0.0033  -0.0304 0.0041  62  GLN   B CD  
4910 O OE1 . GLN   B 62  ? 0.1523 0.1469 0.1717 -0.0044 -0.0295 -0.0029 62  GLN   B OE1 
4911 N NE2 . GLN   B 62  ? 0.1515 0.1641 0.1673 -0.0011 -0.0228 -0.0084 62  GLN   B NE2 
4920 N N   . VAL   B 63  ? 0.1482 0.1525 0.1866 -0.0157 -0.0288 -0.0042 63  VAL   B N   
4921 C CA  . VAL   B 63  ? 0.1572 0.1526 0.2047 -0.0161 -0.0379 -0.0074 63  VAL   B CA  
4922 C C   . VAL   B 63  ? 0.1546 0.1454 0.1978 -0.0167 -0.0395 -0.0090 63  VAL   B C   
4923 O O   . VAL   B 63  ? 0.1688 0.1453 0.2087 -0.0147 -0.0442 -0.0132 63  VAL   B O   
4924 C CB  . VAL   B 63  ? 0.1563 0.1695 0.2357 -0.0234 -0.0329 -0.0119 63  VAL   B CB  
4925 C CG1 . VAL   B 63  ? 0.1622 0.1782 0.2440 -0.0331 -0.0281 -0.0165 63  VAL   B CG1 
4926 C CG2 . VAL   B 63  ? 0.1537 0.1790 0.2492 -0.0150 -0.0304 -0.0131 63  VAL   B CG2 
4936 N N   . GLU   B 64  ? 0.1523 0.1391 0.1840 -0.0129 -0.0307 -0.0067 64  GLU   B N   
4937 C CA  . GLU   B 64  ? 0.1540 0.1336 0.1802 -0.0133 -0.0390 -0.0156 64  GLU   B CA  
4938 C C   . GLU   B 64  ? 0.1559 0.1315 0.1735 -0.0073 -0.0360 -0.0167 64  GLU   B C   
4939 O O   . GLU   B 64  ? 0.1623 0.1425 0.1843 -0.0088 -0.0305 -0.0165 64  GLU   B O   
4940 C CB  . GLU   B 64  ? 0.1586 0.1382 0.1841 -0.0182 -0.0354 -0.0077 64  GLU   B CB  
4941 C CG  . GLU   B 64  ? 0.1616 0.1461 0.1751 -0.0229 -0.0337 -0.0181 64  GLU   B CG  
4942 C CD  . GLU   B 64  ? 0.1634 0.1586 0.1939 -0.0262 -0.0343 -0.0169 64  GLU   B CD  
4943 O OE1 . GLU   B 64  ? 0.1604 0.1671 0.2098 -0.0260 -0.0274 -0.0264 64  GLU   B OE1 
4944 O OE2 . GLU   B 64  ? 0.1796 0.1699 0.1976 -0.0357 -0.0574 -0.0167 64  GLU   B OE2 
4951 N N   . SER   B 65  ? 0.1528 0.1299 0.1667 -0.0094 -0.0249 -0.0169 65  SER   B N   
4952 C CA  . SER   B 65  ? 0.1573 0.1310 0.1730 -0.0060 -0.0210 -0.0123 65  SER   B CA  
4953 C C   . SER   B 65  ? 0.1565 0.1379 0.1746 0.0007  -0.0294 -0.0190 65  SER   B C   
4954 O O   . SER   B 65  ? 0.1596 0.1417 0.1795 0.0000  -0.0265 -0.0327 65  SER   B O   
4955 C CB  . SER   B 65  ? 0.1566 0.1363 0.1654 -0.0155 -0.0182 -0.0159 65  SER   B CB  
4956 O OG  . SER   B 65  ? 0.1612 0.1355 0.1668 -0.0120 -0.0153 -0.0187 65  SER   B OG  
4962 N N   . ASP   B 66  ? 0.1650 0.1462 0.1689 0.0024  -0.0288 -0.0243 66  ASP   B N   
4963 C CA  . ASP   B 66  ? 0.1735 0.1512 0.1665 0.0019  -0.0322 -0.0205 66  ASP   B CA  
4964 C C   . ASP   B 66  ? 0.1809 0.1517 0.1699 -0.0013 -0.0281 -0.0162 66  ASP   B C   
4965 O O   . ASP   B 66  ? 0.1810 0.1548 0.1751 -0.0015 -0.0343 -0.0213 66  ASP   B O   
4966 C CB  . ASP   B 66  ? 0.1918 0.1639 0.1843 0.0064  -0.0458 -0.0145 66  ASP   B CB  
4967 C CG  . ASP   B 66  ? 0.2182 0.1808 0.1974 0.0173  -0.0588 -0.0029 66  ASP   B CG  
4968 O OD1 . ASP   B 66  ? 0.2446 0.1800 0.1917 0.0051  -0.0516 0.0006  66  ASP   B OD1 
4969 O OD2 . ASP   B 66  ? 0.2327 0.2014 0.2647 0.0360  -0.0591 -0.0111 66  ASP   B OD2 
4974 N N   . ASP   B 67  ? 0.1774 0.1436 0.1668 -0.0065 -0.0322 -0.0204 67  ASP   B N   
4975 C CA  . ASP   B 67  ? 0.1910 0.1446 0.1782 -0.0091 -0.0387 -0.0132 67  ASP   B CA  
4976 C C   . ASP   B 67  ? 0.1829 0.1508 0.1774 -0.0003 -0.0315 -0.0171 67  ASP   B C   
4977 O O   . ASP   B 67  ? 0.1854 0.1578 0.1906 0.0047  -0.0249 -0.0262 67  ASP   B O   
4978 C CB  . ASP   B 67  ? 0.2148 0.1537 0.1957 -0.0152 -0.0502 -0.0031 67  ASP   B CB  
4979 C CG  . ASP   B 67  ? 0.2479 0.1635 0.1939 -0.0147 -0.0682 -0.0128 67  ASP   B CG  
4980 O OD1 . ASP   B 67  ? 0.2655 0.1696 0.1866 -0.0189 -0.0695 -0.0145 67  ASP   B OD1 
4981 O OD2 . ASP   B 67  ? 0.2614 0.1708 0.2045 -0.0009 -0.0739 -0.0103 67  ASP   B OD2 
4986 N N   . TYR   B 68  ? 0.1706 0.1464 0.1714 -0.0028 -0.0371 -0.0282 68  TYR   B N   
4987 C CA  . TYR   B 68  ? 0.1691 0.1627 0.1861 0.0046  -0.0370 -0.0373 68  TYR   B CA  
4988 C C   . TYR   B 68  ? 0.1616 0.1595 0.1820 0.0035  -0.0348 -0.0458 68  TYR   B C   
4989 O O   . TYR   B 68  ? 0.1722 0.1717 0.1861 0.0054  -0.0336 -0.0577 68  TYR   B O   
4990 C CB  . TYR   B 68  ? 0.1751 0.1867 0.1919 0.0087  -0.0434 -0.0504 68  TYR   B CB  
4991 C CG  . TYR   B 68  ? 0.1850 0.2055 0.2144 0.0127  -0.0355 -0.0706 68  TYR   B CG  
4992 C CD1 . TYR   B 68  ? 0.1860 0.2064 0.2426 -0.0076 -0.0392 -0.0869 68  TYR   B CD1 
4993 C CD2 . TYR   B 68  ? 0.1898 0.2233 0.2318 0.0213  -0.0443 -0.0693 68  TYR   B CD2 
4994 C CE1 . TYR   B 68  ? 0.1905 0.2226 0.2606 -0.0041 -0.0409 -0.0912 68  TYR   B CE1 
4995 C CE2 . TYR   B 68  ? 0.1901 0.2302 0.2410 0.0183  -0.0365 -0.0811 68  TYR   B CE2 
4996 C CZ  . TYR   B 68  ? 0.1859 0.2289 0.2494 0.0037  -0.0460 -0.0939 68  TYR   B CZ  
4997 O OH  . TYR   B 68  ? 0.1871 0.2483 0.2806 0.0038  -0.0385 -0.0690 68  TYR   B OH  
5007 N N   . ILE   B 69  ? 0.1683 0.1505 0.1927 0.0050  -0.0283 -0.0394 69  ILE   B N   
5008 C CA  . ILE   B 69  ? 0.1753 0.1573 0.2008 0.0015  -0.0243 -0.0450 69  ILE   B CA  
5009 C C   . ILE   B 69  ? 0.1756 0.1578 0.1898 0.0104  -0.0366 -0.0391 69  ILE   B C   
5010 O O   . ILE   B 69  ? 0.1816 0.1700 0.1921 0.0074  -0.0247 -0.0412 69  ILE   B O   
5011 C CB  . ILE   B 69  ? 0.1854 0.1587 0.2261 0.0002  0.0036  -0.0405 69  ILE   B CB  
5012 C CG1 . ILE   B 69  ? 0.1883 0.1573 0.2405 -0.0086 0.0046  -0.0419 69  ILE   B CG1 
5013 C CG2 . ILE   B 69  ? 0.2011 0.1707 0.2461 -0.0014 0.0014  -0.0302 69  ILE   B CG2 
5014 C CD1 . ILE   B 69  ? 0.1901 0.1616 0.2495 -0.0169 0.0106  -0.0445 69  ILE   B CD1 
5026 N N   . ALA   B 70  ? 0.1709 0.1552 0.1827 0.0088  -0.0407 -0.0307 70  ALA   B N   
5027 C CA  . ALA   B 70  ? 0.1743 0.1583 0.1680 0.0066  -0.0423 -0.0253 70  ALA   B CA  
5028 C C   . ALA   B 70  ? 0.1804 0.1585 0.1742 0.0060  -0.0528 -0.0344 70  ALA   B C   
5029 O O   . ALA   B 70  ? 0.1876 0.1597 0.1832 0.0091  -0.0435 -0.0366 70  ALA   B O   
5030 C CB  . ALA   B 70  ? 0.1729 0.1759 0.1703 -0.0022 -0.0408 -0.0260 70  ALA   B CB  
5036 N N   . THR   B 71  ? 0.1885 0.1624 0.1814 0.0135  -0.0554 -0.0350 71  THR   B N   
5037 C CA  . THR   B 71  ? 0.1983 0.1649 0.2051 0.0140  -0.0701 -0.0388 71  THR   B CA  
5038 C C   . THR   B 71  ? 0.1983 0.1734 0.2210 0.0274  -0.0665 -0.0530 71  THR   B C   
5039 O O   . THR   B 71  ? 0.2041 0.1815 0.2475 0.0294  -0.0582 -0.0685 71  THR   B O   
5040 C CB  . THR   B 71  ? 0.2238 0.1869 0.2319 0.0027  -0.0760 -0.0098 71  THR   B CB  
5041 O OG1 . THR   B 71  ? 0.2379 0.2102 0.2654 -0.0146 -0.0737 0.0078  71  THR   B OG1 
5042 C CG2 . THR   B 71  ? 0.2423 0.1825 0.2536 0.0054  -0.0644 0.0096  71  THR   B CG2 
5050 N N   . ASN   B 72  ? 0.1896 0.1791 0.2085 0.0212  -0.0634 -0.0712 72  ASN   B N   
5051 C CA  . ASN   B 72  ? 0.1915 0.1934 0.2200 0.0229  -0.0507 -0.0770 72  ASN   B CA  
5052 C C   . ASN   B 72  ? 0.1925 0.2021 0.2251 0.0068  -0.0307 -0.0736 72  ASN   B C   
5053 O O   . ASN   B 72  ? 0.1974 0.2183 0.2433 0.0145  -0.0141 -0.0755 72  ASN   B O   
5054 C CB  . ASN   B 72  ? 0.1931 0.2076 0.2303 0.0190  -0.0616 -0.0745 72  ASN   B CB  
5055 C CG  . ASN   B 72  ? 0.2082 0.2219 0.2399 0.0326  -0.0615 -0.0521 72  ASN   B CG  
5056 O OD1 . ASN   B 72  ? 0.2301 0.2426 0.2473 0.0210  -0.0439 -0.0558 72  ASN   B OD1 
5057 N ND2 . ASN   B 72  ? 0.2157 0.2282 0.2735 0.0422  -0.0579 -0.0245 72  ASN   B ND2 
5064 N N   . GLY   B 73  ? 0.1914 0.2037 0.1988 0.0020  -0.0359 -0.0697 73  GLY   B N   
5065 C CA  . GLY   B 73  ? 0.1886 0.2056 0.1865 0.0047  -0.0272 -0.0581 73  GLY   B CA  
5066 C C   . GLY   B 73  ? 0.1811 0.2032 0.1545 0.0056  -0.0278 -0.0522 73  GLY   B C   
5067 O O   . GLY   B 73  ? 0.1736 0.1892 0.1591 0.0051  -0.0189 -0.0466 73  GLY   B O   
5071 N N   . PRO   B 74  ? 0.1881 0.2089 0.1532 0.0031  -0.0335 -0.0455 74  PRO   B N   
5072 C CA  . PRO   B 74  ? 0.1778 0.2038 0.1394 0.0049  -0.0255 -0.0327 74  PRO   B CA  
5073 C C   . PRO   B 74  ? 0.1643 0.1915 0.1431 0.0072  -0.0211 -0.0249 74  PRO   B C   
5074 O O   . PRO   B 74  ? 0.1698 0.1968 0.1731 0.0117  -0.0124 -0.0363 74  PRO   B O   
5075 C CB  . PRO   B 74  ? 0.2009 0.2188 0.1386 0.0045  -0.0198 -0.0287 74  PRO   B CB  
5076 C CG  . PRO   B 74  ? 0.2140 0.2286 0.1708 0.0077  -0.0149 -0.0265 74  PRO   B CG  
5077 C CD  . PRO   B 74  ? 0.2085 0.2231 0.1668 0.0098  -0.0185 -0.0377 74  PRO   B CD  
5085 N N   . LEU   B 75  ? 0.1579 0.1781 0.1339 0.0055  -0.0258 -0.0245 75  LEU   B N   
5086 C CA  . LEU   B 75  ? 0.1642 0.1799 0.1306 0.0012  -0.0175 -0.0121 75  LEU   B CA  
5087 C C   . LEU   B 75  ? 0.1639 0.1928 0.1334 0.0036  -0.0047 -0.0179 75  LEU   B C   
5088 O O   . LEU   B 75  ? 0.1824 0.2068 0.1446 -0.0059 0.0003  -0.0089 75  LEU   B O   
5089 C CB  . LEU   B 75  ? 0.1738 0.1802 0.1212 -0.0067 -0.0189 0.0028  75  LEU   B CB  
5090 C CG  . LEU   B 75  ? 0.2018 0.1930 0.1457 -0.0289 -0.0097 -0.0106 75  LEU   B CG  
5091 C CD1 . LEU   B 75  ? 0.2308 0.2015 0.1545 -0.0365 0.0064  -0.0133 75  LEU   B CD1 
5092 C CD2 . LEU   B 75  ? 0.2265 0.2152 0.2173 -0.0232 0.0077  0.0008  75  LEU   B CD2 
5104 N N   . LYS   B 76  ? 0.1579 0.2080 0.1563 0.0046  0.0009  -0.0179 76  LYS   B N   
5105 C CA  . LYS   B 76  ? 0.1757 0.2136 0.1921 -0.0043 0.0181  -0.0132 76  LYS   B CA  
5106 C C   . LYS   B 76  ? 0.1628 0.1948 0.1488 0.0004  0.0067  0.0023  76  LYS   B C   
5107 O O   . LYS   B 76  ? 0.1605 0.1807 0.1501 0.0026  0.0032  0.0111  76  LYS   B O   
5108 C CB  . LYS   B 76  ? 0.1934 0.2304 0.2648 -0.0119 0.0431  -0.0458 76  LYS   B CB  
5109 C CG  . LYS   B 76  ? 0.2045 0.2506 0.3153 -0.0044 0.0331  -0.0557 76  LYS   B CG  
5110 C CD  . LYS   B 76  ? 0.2069 0.2649 0.3584 0.0004  0.0169  -0.0669 76  LYS   B CD  
5111 C CE  . LYS   B 76  ? 0.2161 0.2850 0.4130 0.0057  0.0019  -0.0720 76  LYS   B CE  
5112 N NZ  . LYS   B 76  ? 0.2171 0.2956 0.4309 0.0019  -0.0186 -0.0849 76  LYS   B NZ  
5126 N N   . VAL   B 77  ? 0.1722 0.2019 0.1450 0.0048  0.0140  0.0043  77  VAL   B N   
5127 C CA  . VAL   B 77  ? 0.1696 0.1894 0.1609 0.0128  0.0138  0.0198  77  VAL   B CA  
5128 C C   . VAL   B 77  ? 0.1583 0.1746 0.1498 0.0125  0.0160  0.0155  77  VAL   B C   
5129 O O   . VAL   B 77  ? 0.1638 0.1733 0.1534 0.0173  0.0265  0.0101  77  VAL   B O   
5130 C CB  . VAL   B 77  ? 0.1823 0.1998 0.1754 0.0124  0.0169  0.0292  77  VAL   B CB  
5131 C CG1 . VAL   B 77  ? 0.1867 0.1889 0.2055 0.0059  0.0227  0.0305  77  VAL   B CG1 
5132 C CG2 . VAL   B 77  ? 0.1923 0.2165 0.1879 0.0104  0.0111  0.0418  77  VAL   B CG2 
5142 N N   . GLY   B 78  ? 0.1565 0.1661 0.1583 0.0118  0.0183  0.0082  78  GLY   B N   
5143 C CA  . GLY   B 78  ? 0.1517 0.1649 0.1431 0.0044  0.0181  0.0039  78  GLY   B CA  
5144 C C   . GLY   B 78  ? 0.1450 0.1538 0.1374 0.0061  0.0163  -0.0019 78  GLY   B C   
5145 O O   . GLY   B 78  ? 0.1514 0.1532 0.1522 0.0157  0.0099  0.0052  78  GLY   B O   
5149 N N   . GLY   B 79  ? 0.1428 0.1539 0.1428 0.0054  0.0146  -0.0011 79  GLY   B N   
5150 C CA  . GLY   B 79  ? 0.1437 0.1446 0.1449 0.0073  0.0087  0.0022  79  GLY   B CA  
5151 C C   . GLY   B 79  ? 0.1350 0.1361 0.1368 0.0078  0.0031  -0.0058 79  GLY   B C   
5152 O O   . GLY   B 79  ? 0.1416 0.1407 0.1573 0.0091  0.0133  0.0016  79  GLY   B O   
5156 N N   . SER   B 80  ? 0.1332 0.1339 0.1581 0.0095  0.0150  -0.0074 80  SER   B N   
5157 C CA  . SER   B 80  ? 0.1296 0.1275 0.1654 0.0074  0.0073  -0.0043 80  SER   B CA  
5158 C C   . SER   B 80  ? 0.1338 0.1276 0.1686 0.0111  -0.0070 -0.0084 80  SER   B C   
5159 O O   . SER   B 80  ? 0.1458 0.1344 0.1850 0.0116  -0.0044 -0.0178 80  SER   B O   
5160 C CB  . SER   B 80  ? 0.1294 0.1327 0.1711 -0.0039 0.0022  -0.0072 80  SER   B CB  
5161 O OG  . SER   B 80  ? 0.1435 0.1502 0.1874 -0.0012 -0.0146 -0.0006 80  SER   B OG  
5167 N N   . CYS   B 81  ? 0.1313 0.1125 0.1671 -0.0003 -0.0082 -0.0141 81  CYS   B N   
5168 C CA  . CYS   B 81  ? 0.1418 0.1102 0.1582 0.0024  -0.0112 -0.0069 81  CYS   B CA  
5169 C C   . CYS   B 81  ? 0.1364 0.1087 0.1450 -0.0020 -0.0119 -0.0116 81  CYS   B C   
5170 O O   . CYS   B 81  ? 0.1579 0.1131 0.1588 0.0087  -0.0004 -0.0100 81  CYS   B O   
5171 C CB  . CYS   B 81  ? 0.1574 0.1246 0.1625 -0.0058 -0.0132 -0.0086 81  CYS   B CB  
5172 S SG  . CYS   B 81  ? 0.1545 0.1454 0.1682 -0.0046 -0.0291 -0.0177 81  CYS   B SG  
5178 N N   . VAL   B 82  ? 0.1393 0.1104 0.1562 -0.0006 -0.0154 -0.0158 82  VAL   B N   
5179 C CA  . VAL   B 82  ? 0.1442 0.1147 0.1515 -0.0020 -0.0128 -0.0046 82  VAL   B CA  
5180 C C   . VAL   B 82  ? 0.1493 0.1114 0.1660 -0.0048 -0.0112 -0.0020 82  VAL   B C   
5181 O O   . VAL   B 82  ? 0.1549 0.1157 0.1857 -0.0054 -0.0109 -0.0194 82  VAL   B O   
5182 C CB  . VAL   B 82  ? 0.1526 0.1379 0.1691 -0.0030 -0.0097 0.0035  82  VAL   B CB  
5183 C CG1 . VAL   B 82  ? 0.1703 0.1610 0.1892 -0.0019 -0.0096 0.0104  82  VAL   B CG1 
5184 C CG2 . VAL   B 82  ? 0.1636 0.1482 0.1802 -0.0047 -0.0285 0.0042  82  VAL   B CG2 
5194 N N   . LEU   B 83  ? 0.1405 0.1077 0.1641 -0.0136 -0.0183 -0.0075 83  LEU   B N   
5195 C CA  . LEU   B 83  ? 0.1422 0.1109 0.1577 -0.0125 -0.0197 -0.0076 83  LEU   B CA  
5196 C C   . LEU   B 83  ? 0.1377 0.1096 0.1499 -0.0145 -0.0214 -0.0031 83  LEU   B C   
5197 O O   . LEU   B 83  ? 0.1414 0.1222 0.1463 -0.0170 -0.0211 0.0037  83  LEU   B O   
5198 C CB  . LEU   B 83  ? 0.1497 0.1182 0.1479 -0.0083 -0.0217 -0.0104 83  LEU   B CB  
5199 C CG  . LEU   B 83  ? 0.1689 0.1438 0.1650 -0.0167 -0.0182 -0.0109 83  LEU   B CG  
5200 C CD1 . LEU   B 83  ? 0.1846 0.1528 0.1617 -0.0083 -0.0350 -0.0039 83  LEU   B CD1 
5201 C CD2 . LEU   B 83  ? 0.1803 0.1490 0.1701 -0.0072 -0.0147 -0.0221 83  LEU   B CD2 
5213 N N   . SER   B 84  ? 0.1468 0.1249 0.1807 -0.0153 -0.0230 0.0052  84  SER   B N   
5214 C CA  . SER   B 84  ? 0.1454 0.1406 0.1757 -0.0258 -0.0189 0.0152  84  SER   B CA  
5215 C C   . SER   B 84  ? 0.1359 0.1575 0.1272 -0.0227 -0.0179 0.0179  84  SER   B C   
5216 O O   . SER   B 84  ? 0.1440 0.1451 0.1275 -0.0209 -0.0117 0.0018  84  SER   B O   
5217 C CB  . SER   B 84  ? 0.1620 0.1471 0.2260 -0.0326 0.0076  0.0167  84  SER   B CB  
5218 O OG  . SER   B 84  ? 0.1621 0.1583 0.2800 -0.0310 0.0113  0.0276  84  SER   B OG  
5224 N N   . GLY   B 85  ? 0.1430 0.1809 0.1381 -0.0233 -0.0165 0.0155  85  GLY   B N   
5225 C CA  . GLY   B 85  ? 0.1437 0.1890 0.1447 -0.0353 -0.0097 -0.0033 85  GLY   B CA  
5226 C C   . GLY   B 85  ? 0.1411 0.1666 0.1484 -0.0389 -0.0080 0.0081  85  GLY   B C   
5227 O O   . GLY   B 85  ? 0.1487 0.1669 0.1529 -0.0522 0.0109  -0.0007 85  GLY   B O   
5231 N N   . HIS   B 86  ? 0.1399 0.1505 0.1638 -0.0273 -0.0222 0.0309  86  HIS   B N   
5232 C CA  . HIS   B 86  ? 0.1390 0.1522 0.1615 -0.0327 -0.0182 0.0321  86  HIS   B CA  
5233 C C   . HIS   B 86  ? 0.1402 0.1657 0.1500 -0.0381 -0.0135 0.0480  86  HIS   B C   
5234 O O   . HIS   B 86  ? 0.1548 0.1804 0.1615 -0.0304 -0.0020 0.0424  86  HIS   B O   
5235 C CB  . HIS   B 86  ? 0.1441 0.1496 0.1662 -0.0204 -0.0194 0.0158  86  HIS   B CB  
5236 C CG  . HIS   B 86  ? 0.1544 0.1537 0.1695 -0.0146 -0.0255 0.0193  86  HIS   B CG  
5237 N ND1 . HIS   B 86  ? 0.1641 0.1730 0.1906 -0.0237 -0.0294 0.0006  86  HIS   B ND1 
5238 C CD2 . HIS   B 86  ? 0.1587 0.1559 0.1690 -0.0100 -0.0244 0.0186  86  HIS   B CD2 
5239 C CE1 . HIS   B 86  ? 0.1694 0.1699 0.1845 -0.0185 -0.0240 -0.0174 86  HIS   B CE1 
5240 N NE2 . HIS   B 86  ? 0.1618 0.1668 0.1680 0.0009  -0.0212 0.0015  86  HIS   B NE2 
5248 N N   . ASN   B 87  ? 0.1400 0.1712 0.1643 -0.0348 -0.0109 0.0374  87  ASN   B N   
5249 C CA  . ASN   B 87  ? 0.1444 0.1869 0.1626 -0.0313 0.0132  0.0287  87  ASN   B CA  
5250 C C   . ASN   B 87  ? 0.1548 0.1749 0.1481 -0.0233 0.0199  0.0185  87  ASN   B C   
5251 O O   . ASN   B 87  ? 0.1801 0.1847 0.1763 -0.0211 0.0355  0.0187  87  ASN   B O   
5252 C CB  . ASN   B 87  ? 0.1506 0.2241 0.2024 -0.0266 0.0123  0.0156  87  ASN   B CB  
5253 C CG  . ASN   B 87  ? 0.1609 0.2417 0.2055 0.0027  0.0204  0.0279  87  ASN   B CG  
5254 O OD1 . ASN   B 87  ? 0.1524 0.2187 0.1907 0.0021  0.0409  0.0362  87  ASN   B OD1 
5255 N ND2 . ASN   B 87  ? 0.1964 0.2527 0.2325 0.0035  0.0233  0.0214  87  ASN   B ND2 
5262 N N   . LEU   B 88  ? 0.1430 0.1607 0.1435 -0.0310 0.0097  0.0106  88  LEU   B N   
5263 C CA  . LEU   B 88  ? 0.1575 0.1518 0.1458 -0.0235 0.0046  0.0093  88  LEU   B CA  
5264 C C   . LEU   B 88  ? 0.1589 0.1451 0.1360 -0.0300 0.0019  0.0041  88  LEU   B C   
5265 O O   . LEU   B 88  ? 0.1864 0.1520 0.1755 -0.0196 -0.0244 -0.0056 88  LEU   B O   
5266 C CB  . LEU   B 88  ? 0.1661 0.1598 0.1596 -0.0361 -0.0104 0.0285  88  LEU   B CB  
5267 C CG  . LEU   B 88  ? 0.2067 0.1842 0.1905 -0.0331 -0.0278 0.0409  88  LEU   B CG  
5268 C CD1 . LEU   B 88  ? 0.2186 0.2161 0.2179 -0.0423 -0.0213 0.0460  88  LEU   B CD1 
5269 C CD2 . LEU   B 88  ? 0.2421 0.2109 0.2433 0.0066  -0.0510 0.0227  88  LEU   B CD2 
5281 N N   . ALA   B 89  ? 0.1413 0.1411 0.1218 -0.0334 0.0138  0.0047  89  ALA   B N   
5282 C CA  . ALA   B 89  ? 0.1436 0.1341 0.1319 -0.0364 0.0045  0.0127  89  ALA   B CA  
5283 C C   . ALA   B 89  ? 0.1553 0.1379 0.1359 -0.0388 0.0104  0.0064  89  ALA   B C   
5284 O O   . ALA   B 89  ? 0.1450 0.1457 0.1645 -0.0388 0.0112  -0.0177 89  ALA   B O   
5285 C CB  . ALA   B 89  ? 0.1445 0.1379 0.1446 -0.0320 0.0010  0.0153  89  ALA   B CB  
5291 N N   . LYS   B 90  ? 0.1867 0.1278 0.1474 -0.0407 -0.0085 0.0155  90  LYS   B N   
5292 C CA  . LYS   B 90  ? 0.2040 0.1257 0.1375 -0.0373 -0.0059 0.0181  90  LYS   B CA  
5293 C C   . LYS   B 90  ? 0.1948 0.1201 0.1439 -0.0405 -0.0069 0.0018  90  LYS   B C   
5294 O O   . LYS   B 90  ? 0.2145 0.1399 0.1745 -0.0628 0.0027  -0.0053 90  LYS   B O   
5295 C CB  . LYS   B 90  ? 0.2218 0.1329 0.1734 -0.0298 0.0016  0.0238  90  LYS   B CB  
5296 C CG  . LYS   B 90  ? 0.2281 0.1454 0.1908 -0.0169 0.0324  0.0151  90  LYS   B CG  
5297 C CD  . LYS   B 90  ? 0.2561 0.1776 0.2321 -0.0096 0.0522  -0.0102 90  LYS   B CD  
5298 C CE  . LYS   B 90  ? 0.2717 0.1969 0.2823 -0.0205 0.0610  -0.0124 90  LYS   B CE  
5299 N NZ  . LYS   B 90  ? 0.2828 0.1920 0.2848 -0.0356 0.0716  -0.0152 90  LYS   B NZ  
5313 N N   . HIS   B 91  ? 0.1650 0.1050 0.1366 -0.0290 -0.0184 0.0070  91  HIS   B N   
5314 C CA  . HIS   B 91  ? 0.1526 0.1115 0.1466 -0.0206 -0.0164 0.0021  91  HIS   B CA  
5315 C C   . HIS   B 91  ? 0.1437 0.1161 0.1269 -0.0257 -0.0088 0.0040  91  HIS   B C   
5316 O O   . HIS   B 91  ? 0.1526 0.1185 0.1378 -0.0218 -0.0234 -0.0023 91  HIS   B O   
5317 C CB  . HIS   B 91  ? 0.1666 0.1197 0.1896 -0.0057 -0.0047 0.0148  91  HIS   B CB  
5318 C CG  . HIS   B 91  ? 0.2039 0.1346 0.2620 0.0046  0.0248  0.0267  91  HIS   B CG  
5319 N ND1 . HIS   B 91  ? 0.2372 0.1462 0.3145 -0.0017 0.0299  0.0127  91  HIS   B ND1 
5320 C CD2 . HIS   B 91  ? 0.2172 0.1673 0.3053 0.0173  0.0147  0.0577  91  HIS   B CD2 
5321 C CE1 . HIS   B 91  ? 0.2416 0.1603 0.3366 0.0165  0.0230  0.0216  91  HIS   B CE1 
5322 N NE2 . HIS   B 91  ? 0.2260 0.1727 0.3337 0.0300  0.0211  0.0624  91  HIS   B NE2 
5330 N N   . CYS   B 92  ? 0.1363 0.1150 0.1296 -0.0198 -0.0130 0.0017  92  CYS   B N   
5331 C CA  . CYS   B 92  ? 0.1327 0.1130 0.1274 -0.0205 -0.0097 0.0009  92  CYS   B CA  
5332 C C   . CYS   B 92  ? 0.1269 0.1082 0.1243 -0.0125 -0.0132 0.0029  92  CYS   B C   
5333 O O   . CYS   B 92  ? 0.1342 0.1151 0.1420 -0.0165 -0.0066 -0.0069 92  CYS   B O   
5334 C CB  . CYS   B 92  ? 0.1323 0.1239 0.1392 -0.0136 -0.0119 0.0006  92  CYS   B CB  
5335 S SG  . CYS   B 92  ? 0.1338 0.1246 0.1404 -0.0121 -0.0104 0.0045  92  CYS   B SG  
5341 N N   . LEU   B 93  ? 0.1197 0.1136 0.1195 -0.0101 -0.0055 -0.0058 93  LEU   B N   
5342 C CA  . LEU   B 93  ? 0.1216 0.1117 0.1235 -0.0017 -0.0073 0.0033  93  LEU   B CA  
5343 C C   . LEU   B 93  ? 0.1188 0.1083 0.1219 -0.0015 0.0012  0.0010  93  LEU   B C   
5344 O O   . LEU   B 93  ? 0.1261 0.1095 0.1345 -0.0082 -0.0036 -0.0037 93  LEU   B O   
5345 C CB  . LEU   B 93  ? 0.1272 0.1140 0.1442 0.0012  -0.0086 -0.0007 93  LEU   B CB  
5346 C CG  . LEU   B 93  ? 0.1221 0.1248 0.1544 -0.0036 -0.0044 0.0019  93  LEU   B CG  
5347 C CD1 . LEU   B 93  ? 0.1280 0.1385 0.1556 0.0024  -0.0054 -0.0083 93  LEU   B CD1 
5348 C CD2 . LEU   B 93  ? 0.1229 0.1257 0.1515 -0.0057 -0.0005 -0.0002 93  LEU   B CD2 
5360 N N   . HIS   B 94  ? 0.1245 0.1083 0.1124 -0.0032 -0.0103 -0.0022 94  HIS   B N   
5361 C CA  . HIS   B 94  ? 0.1271 0.1026 0.1234 -0.0007 -0.0032 -0.0039 94  HIS   B CA  
5362 C C   . HIS   B 94  ? 0.1258 0.1022 0.1397 -0.0031 0.0005  0.0012  94  HIS   B C   
5363 O O   . HIS   B 94  ? 0.1325 0.1153 0.1745 -0.0045 0.0098  -0.0128 94  HIS   B O   
5364 C CB  . HIS   B 94  ? 0.1231 0.1122 0.1406 -0.0005 -0.0069 0.0025  94  HIS   B CB  
5365 C CG  . HIS   B 94  ? 0.1245 0.1116 0.1386 -0.0055 -0.0216 -0.0065 94  HIS   B CG  
5366 N ND1 . HIS   B 94  ? 0.1315 0.1135 0.1384 -0.0087 -0.0169 -0.0056 94  HIS   B ND1 
5367 C CD2 . HIS   B 94  ? 0.1313 0.1142 0.1341 -0.0066 -0.0221 -0.0006 94  HIS   B CD2 
5368 C CE1 . HIS   B 94  ? 0.1343 0.1162 0.1370 -0.0167 -0.0149 0.0033  94  HIS   B CE1 
5369 N NE2 . HIS   B 94  ? 0.1265 0.1213 0.1426 -0.0187 -0.0145 0.0022  94  HIS   B NE2 
5377 N N   . VAL   B 95  ? 0.1240 0.1063 0.1418 0.0005  -0.0040 0.0018  95  VAL   B N   
5378 C CA  . VAL   B 95  ? 0.1202 0.1174 0.1429 0.0009  0.0040  0.0029  95  VAL   B CA  
5379 C C   . VAL   B 95  ? 0.1232 0.1159 0.1338 0.0001  0.0088  -0.0019 95  VAL   B C   
5380 O O   . VAL   B 95  ? 0.1304 0.1174 0.1500 0.0074  0.0063  0.0069  95  VAL   B O   
5381 C CB  . VAL   B 95  ? 0.1220 0.1149 0.1388 -0.0025 -0.0071 -0.0045 95  VAL   B CB  
5382 C CG1 . VAL   B 95  ? 0.1300 0.1379 0.1471 -0.0090 -0.0029 0.0085  95  VAL   B CG1 
5383 C CG2 . VAL   B 95  ? 0.1346 0.1136 0.1385 -0.0024 -0.0132 -0.0033 95  VAL   B CG2 
5393 N N   . VAL   B 96  ? 0.1313 0.1193 0.1402 0.0094  0.0077  0.0042  96  VAL   B N   
5394 C CA  . VAL   B 96  ? 0.1430 0.1335 0.1369 0.0072  0.0020  0.0027  96  VAL   B CA  
5395 C C   . VAL   B 96  ? 0.1409 0.1412 0.1416 0.0069  0.0040  0.0120  96  VAL   B C   
5396 O O   . VAL   B 96  ? 0.1472 0.1469 0.1599 0.0013  0.0165  -0.0017 96  VAL   B O   
5397 C CB  . VAL   B 96  ? 0.1522 0.1523 0.1417 0.0084  0.0022  -0.0025 96  VAL   B CB  
5398 C CG1 . VAL   B 96  ? 0.1536 0.1683 0.1497 0.0119  0.0111  0.0038  96  VAL   B CG1 
5399 C CG2 . VAL   B 96  ? 0.1607 0.1535 0.1507 -0.0022 0.0120  -0.0087 96  VAL   B CG2 
5409 N N   . GLY   B 97  ? 0.1450 0.1378 0.1427 -0.0014 0.0054  0.0131  97  GLY   B N   
5410 C CA  . GLY   B 97  ? 0.1546 0.1392 0.1374 -0.0034 0.0168  0.0068  97  GLY   B CA  
5411 C C   . GLY   B 97  ? 0.1619 0.1486 0.1453 0.0064  0.0169  0.0097  97  GLY   B C   
5412 O O   . GLY   B 97  ? 0.1721 0.1572 0.1491 0.0023  0.0151  0.0035  97  GLY   B O   
5416 N N   . PRO   B 98  ? 0.1755 0.1515 0.1519 0.0037  0.0245  0.0214  98  PRO   B N   
5417 C CA  . PRO   B 98  ? 0.1846 0.1660 0.1565 0.0084  0.0282  0.0199  98  PRO   B CA  
5418 C C   . PRO   B 98  ? 0.1956 0.1688 0.1317 0.0139  0.0233  0.0296  98  PRO   B C   
5419 O O   . PRO   B 98  ? 0.1906 0.1664 0.1554 0.0096  0.0180  0.0275  98  PRO   B O   
5420 C CB  . PRO   B 98  ? 0.1759 0.1656 0.1777 0.0060  0.0364  0.0154  98  PRO   B CB  
5421 C CG  . PRO   B 98  ? 0.1724 0.1594 0.1754 -0.0026 0.0293  0.0196  98  PRO   B CG  
5422 C CD  . PRO   B 98  ? 0.1595 0.1564 0.1689 -0.0005 0.0250  0.0220  98  PRO   B CD  
5430 N N   . ASN   B 99  ? 0.2040 0.1797 0.1383 0.0252  0.0217  0.0107  99  ASN   B N   
5431 C CA  . ASN   B 99  ? 0.2197 0.1822 0.1457 0.0278  0.0142  0.0254  99  ASN   B CA  
5432 C C   . ASN   B 99  ? 0.2493 0.2103 0.1552 0.0215  0.0386  0.0434  99  ASN   B C   
5433 O O   . ASN   B 99  ? 0.2624 0.2133 0.1710 0.0275  0.0314  0.0374  99  ASN   B O   
5434 C CB  . ASN   B 99  ? 0.2293 0.1849 0.1460 0.0307  0.0126  0.0219  99  ASN   B CB  
5435 C CG  . ASN   B 99  ? 0.2376 0.1950 0.1706 0.0291  -0.0000 0.0168  99  ASN   B CG  
5436 O OD1 . ASN   B 99  ? 0.2447 0.1935 0.1951 0.0325  -0.0034 0.0248  99  ASN   B OD1 
5437 N ND2 . ASN   B 99  ? 0.2387 0.1943 0.1887 0.0336  -0.0177 0.0193  99  ASN   B ND2 
5444 N N   A VAL   B 100 ? 0.2689 0.2253 0.1913 0.0123  0.0357  0.0582  100 VAL   B N   
5445 N N   B VAL   B 100 ? 0.2677 0.2237 0.1902 0.0099  0.0355  0.0592  100 VAL   B N   
5446 C CA  A VAL   B 100 ? 0.2956 0.2453 0.2382 0.0052  0.0411  0.0692  100 VAL   B CA  
5447 C CA  B VAL   B 100 ? 0.2940 0.2426 0.2370 0.0008  0.0418  0.0706  100 VAL   B CA  
5448 C C   A VAL   B 100 ? 0.3146 0.2497 0.2324 0.0128  0.0425  0.0855  100 VAL   B C   
5449 C C   B VAL   B 100 ? 0.3135 0.2464 0.2279 0.0090  0.0439  0.0870  100 VAL   B C   
5450 O O   A VAL   B 100 ? 0.3206 0.2562 0.2367 0.0157  0.0467  0.0849  100 VAL   B O   
5451 O O   B VAL   B 100 ? 0.3192 0.2502 0.2264 0.0097  0.0495  0.0874  100 VAL   B O   
5452 C CB  A VAL   B 100 ? 0.3035 0.2590 0.2997 -0.0098 0.0398  0.0683  100 VAL   B CB  
5453 C CB  B VAL   B 100 ? 0.3013 0.2559 0.3023 -0.0166 0.0403  0.0707  100 VAL   B CB  
5454 C CG1 A VAL   B 100 ? 0.3078 0.2653 0.3248 -0.0131 0.0407  0.0664  100 VAL   B CG1 
5455 C CG1 B VAL   B 100 ? 0.3059 0.2622 0.3298 -0.0201 0.0407  0.0691  100 VAL   B CG1 
5456 C CG2 A VAL   B 100 ? 0.3051 0.2640 0.3190 -0.0145 0.0407  0.0700  100 VAL   B CG2 
5457 C CG2 B VAL   B 100 ? 0.3023 0.2606 0.3233 -0.0226 0.0410  0.0721  100 VAL   B CG2 
5476 N N   . ASN   B 101 ? 0.3288 0.2525 0.2284 0.0224  0.0335  0.0953  101 ASN   B N   
5477 C CA  . ASN   B 101 ? 0.3674 0.2737 0.2545 0.0335  0.0146  0.1008  101 ASN   B CA  
5478 C C   . ASN   B 101 ? 0.4045 0.3187 0.2627 0.0320  -0.0040 0.0974  101 ASN   B C   
5479 O O   . ASN   B 101 ? 0.4127 0.3294 0.2881 0.0414  -0.0120 0.0789  101 ASN   B O   
5480 C CB  . ASN   B 101 ? 0.3716 0.2588 0.2779 0.0383  0.0242  0.0917  101 ASN   B CB  
5481 C CG  . ASN   B 101 ? 0.3755 0.2477 0.2852 0.0397  0.0362  0.0902  101 ASN   B CG  
5482 O OD1 . ASN   B 101 ? 0.3819 0.2480 0.3140 0.0386  0.0484  0.0815  101 ASN   B OD1 
5483 N ND2 . ASN   B 101 ? 0.3725 0.2458 0.2780 0.0398  0.0381  0.0851  101 ASN   B ND2 
5491 N N   A LYS   B 102 ? 0.4203 0.3394 0.2744 0.0259  -0.0045 0.0869  102 LYS   B N   
5492 N N   B LYS   B 102 ? 0.4173 0.3370 0.2728 0.0227  -0.0028 0.0915  102 LYS   B N   
5493 C CA  A LYS   B 102 ? 0.4353 0.3635 0.2960 0.0181  -0.0005 0.0707  102 LYS   B CA  
5494 C CA  B LYS   B 102 ? 0.4297 0.3596 0.2932 0.0119  0.0028  0.0784  102 LYS   B CA  
5495 C C   A LYS   B 102 ? 0.4342 0.3662 0.2809 0.0204  0.0090  0.0768  102 LYS   B C   
5496 C C   B LYS   B 102 ? 0.4276 0.3601 0.2807 0.0124  0.0118  0.0881  102 LYS   B C   
5497 O O   A LYS   B 102 ? 0.4409 0.3701 0.2798 0.0213  0.0031  0.0727  102 LYS   B O   
5498 O O   B LYS   B 102 ? 0.4338 0.3645 0.2856 0.0134  0.0058  0.0813  102 LYS   B O   
5499 C CB  A LYS   B 102 ? 0.4495 0.3829 0.3421 0.0084  0.0006  0.0440  102 LYS   B CB  
5500 C CB  B LYS   B 102 ? 0.4423 0.3799 0.3372 0.0011  0.0055  0.0494  102 LYS   B CB  
5501 C CG  A LYS   B 102 ? 0.4617 0.3998 0.3893 0.0008  0.0036  0.0192  102 LYS   B CG  
5502 C CG  B LYS   B 102 ? 0.4531 0.3978 0.3834 -0.0071 0.0095  0.0210  102 LYS   B CG  
5503 C CD  A LYS   B 102 ? 0.4720 0.4134 0.4350 -0.0050 0.0069  0.0003  102 LYS   B CD  
5504 C CD  B LYS   B 102 ? 0.4622 0.4123 0.4279 -0.0132 0.0131  -0.0002 102 LYS   B CD  
5505 C CE  A LYS   B 102 ? 0.4795 0.4229 0.4696 -0.0090 0.0099  -0.0142 102 LYS   B CE  
5506 C CE  B LYS   B 102 ? 0.4686 0.4223 0.4611 -0.0174 0.0165  -0.0165 102 LYS   B CE  
5507 N NZ  A LYS   B 102 ? 0.4837 0.4284 0.4898 -0.0110 0.0112  -0.0228 102 LYS   B NZ  
5508 N NZ  B LYS   B 102 ? 0.4721 0.4282 0.4801 -0.0192 0.0177  -0.0261 102 LYS   B NZ  
5535 N N   A GLY   B 103 ? 0.4236 0.3634 0.2806 0.0209  0.0246  0.0813  103 GLY   B N   
5536 N N   B GLY   B 103 ? 0.4165 0.3542 0.2766 0.0110  0.0277  0.0990  103 GLY   B N   
5537 C CA  A GLY   B 103 ? 0.4119 0.3594 0.2920 0.0213  0.0394  0.0742  103 GLY   B CA  
5538 C CA  B GLY   B 103 ? 0.4041 0.3476 0.2849 0.0085  0.0424  0.0937  103 GLY   B CA  
5539 C C   A GLY   B 103 ? 0.3976 0.3515 0.2927 0.0206  0.0534  0.0652  103 GLY   B C   
5540 C C   B GLY   B 103 ? 0.3888 0.3362 0.2796 0.0031  0.0579  0.0857  103 GLY   B C   
5541 O O   A GLY   B 103 ? 0.4006 0.3574 0.3065 0.0200  0.0511  0.0679  103 GLY   B O   
5542 O O   B GLY   B 103 ? 0.3921 0.3426 0.2972 0.0054  0.0545  0.0852  103 GLY   B O   
5549 N N   A GLU   B 104 ? 0.3781 0.3359 0.2741 0.0205  0.0667  0.0473  104 GLU   B N   
5550 N N   B GLU   B 104 ? 0.3674 0.3159 0.2481 -0.0052 0.0727  0.0704  104 GLU   B N   
5551 C CA  A GLU   B 104 ? 0.3583 0.3226 0.2607 0.0220  0.0710  0.0260  104 GLU   B CA  
5552 C CA  B GLU   B 104 ? 0.3457 0.2987 0.2254 -0.0110 0.0751  0.0478  104 GLU   B CA  
5553 C C   A GLU   B 104 ? 0.3602 0.3235 0.2753 0.0103  0.0909  0.0218  104 GLU   B C   
5554 C C   B GLU   B 104 ? 0.3436 0.2955 0.2350 -0.0208 0.0966  0.0410  104 GLU   B C   
5555 O O   A GLU   B 104 ? 0.3618 0.3261 0.2885 0.0086  0.0881  0.0170  104 GLU   B O   
5556 O O   B GLU   B 104 ? 0.3463 0.2991 0.2578 -0.0206 0.0900  0.0327  104 GLU   B O   
5557 C CB  A GLU   B 104 ? 0.3406 0.3074 0.2438 0.0348  0.0485  0.0036  104 GLU   B CB  
5558 C CB  B GLU   B 104 ? 0.3316 0.2824 0.2054 -0.0082 0.0452  0.0252  104 GLU   B CB  
5559 C CG  A GLU   B 104 ? 0.3268 0.2960 0.2276 0.0461  0.0246  -0.0206 104 GLU   B CG  
5560 C CG  B GLU   B 104 ? 0.3216 0.2704 0.1863 -0.0058 0.0148  0.0003  104 GLU   B CG  
5561 C CD  A GLU   B 104 ? 0.3152 0.2851 0.2130 0.0566  -0.0009 -0.0294 104 GLU   B CD  
5562 C CD  B GLU   B 104 ? 0.3141 0.2561 0.1638 -0.0083 -0.0142 -0.0002 104 GLU   B CD  
5563 O OE1 A GLU   B 104 ? 0.3027 0.2719 0.1905 0.0674  0.0062  -0.0310 104 GLU   B OE1 
5564 O OE1 B GLU   B 104 ? 0.3055 0.2403 0.1520 -0.0111 -0.0097 0.0048  104 GLU   B OE1 
5565 O OE2 A GLU   B 104 ? 0.3191 0.2938 0.2299 0.0540  -0.0272 -0.0319 104 GLU   B OE2 
5566 O OE2 B GLU   B 104 ? 0.3168 0.2632 0.1596 -0.0115 -0.0398 0.0002  104 GLU   B OE2 
5579 N N   A ASP   B 105 ? 0.3577 0.3232 0.2815 0.0004  0.1091  0.0230  105 ASP   B N   
5580 N N   B ASP   B 105 ? 0.3349 0.2903 0.2311 -0.0309 0.1199  0.0414  105 ASP   B N   
5581 C CA  A ASP   B 105 ? 0.3577 0.3226 0.2992 -0.0078 0.1222  0.0139  105 ASP   B CA  
5582 C CA  B ASP   B 105 ? 0.3307 0.2863 0.2484 -0.0378 0.1342  0.0277  105 ASP   B CA  
5583 C C   A ASP   B 105 ? 0.3462 0.3013 0.2774 -0.0156 0.1256  0.0092  105 ASP   B C   
5584 C C   B ASP   B 105 ? 0.3178 0.2578 0.2253 -0.0500 0.1306  0.0168  105 ASP   B C   
5585 O O   A ASP   B 105 ? 0.3419 0.2968 0.2716 -0.0133 0.1320  0.0065  105 ASP   B O   
5586 O O   B ASP   B 105 ? 0.3046 0.2446 0.2098 -0.0531 0.1335  0.0135  105 ASP   B O   
5587 C CB  A ASP   B 105 ? 0.3674 0.3398 0.3445 -0.0074 0.1260  0.0057  105 ASP   B CB  
5588 C CB  B ASP   B 105 ? 0.3381 0.3063 0.2946 -0.0338 0.1440  0.0206  105 ASP   B CB  
5589 C CG  A ASP   B 105 ? 0.3747 0.3517 0.3894 -0.0095 0.1268  0.0014  105 ASP   B CG  
5590 C CG  B ASP   B 105 ? 0.3420 0.3179 0.3331 -0.0363 0.1542  0.0229  105 ASP   B CG  
5591 O OD1 A ASP   B 105 ? 0.3758 0.3557 0.3967 -0.0129 0.1289  0.0037  105 ASP   B OD1 
5592 O OD1 B ASP   B 105 ? 0.3428 0.3224 0.3415 -0.0415 0.1535  0.0263  105 ASP   B OD1 
5593 O OD2 A ASP   B 105 ? 0.3789 0.3569 0.4186 -0.0074 0.1209  -0.0044 105 ASP   B OD2 
5594 O OD2 B ASP   B 105 ? 0.3401 0.3220 0.3420 -0.0377 0.1670  0.0274  105 ASP   B OD2 
5603 N N   A ILE   B 106 ? 0.3396 0.2844 0.2773 -0.0218 0.1143  0.0073  106 ILE   B N   
5604 N N   B ILE   B 106 ? 0.3177 0.2439 0.2380 -0.0527 0.1116  0.0073  106 ILE   B N   
5605 C CA  A ILE   B 106 ? 0.3263 0.2663 0.2740 -0.0286 0.1145  0.0073  106 ILE   B CA  
5606 C CA  B ILE   B 106 ? 0.3082 0.2284 0.2415 -0.0596 0.1101  0.0035  106 ILE   B CA  
5607 C C   A ILE   B 106 ? 0.3035 0.2627 0.2633 -0.0254 0.1110  -0.0083 106 ILE   B C   
5608 C C   B ILE   B 106 ? 0.2824 0.2279 0.2290 -0.0595 0.1035  -0.0237 106 ILE   B C   
5609 O O   A ILE   B 106 ? 0.2965 0.2509 0.2540 -0.0257 0.1106  -0.0102 106 ILE   B O   
5610 O O   B ILE   B 106 ? 0.2683 0.2061 0.2051 -0.0709 0.0969  -0.0361 106 ILE   B O   
5611 C CB  A ILE   B 106 ? 0.3375 0.2586 0.2873 -0.0348 0.1143  0.0143  106 ILE   B CB  
5612 C CB  B ILE   B 106 ? 0.3264 0.2253 0.2654 -0.0587 0.1092  0.0121  106 ILE   B CB  
5613 C CG1 A ILE   B 106 ? 0.3421 0.2537 0.2864 -0.0313 0.1124  0.0124  106 ILE   B CG1 
5614 C CG1 B ILE   B 106 ? 0.3359 0.2256 0.2737 -0.0470 0.1027  0.0060  106 ILE   B CG1 
5615 C CG2 A ILE   B 106 ? 0.3424 0.2614 0.3028 -0.0394 0.1137  0.0171  106 ILE   B CG2 
5616 C CG2 B ILE   B 106 ? 0.3326 0.2300 0.2814 -0.0632 0.1103  0.0155  106 ILE   B CG2 
5617 C CD1 A ILE   B 106 ? 0.3433 0.2525 0.2782 -0.0270 0.1136  0.0131  106 ILE   B CD1 
5618 C CD1 B ILE   B 106 ? 0.3395 0.2280 0.2713 -0.0382 0.1012  0.0054  106 ILE   B CD1 
5641 N N   A GLN   B 107 ? 0.2911 0.2721 0.2780 -0.0245 0.1024  -0.0138 107 GLN   B N   
5642 N N   B GLN   B 107 ? 0.2753 0.2502 0.2542 -0.0489 0.0986  -0.0274 107 GLN   B N   
5643 C CA  A GLN   B 107 ? 0.2800 0.2807 0.2954 -0.0212 0.0908  -0.0151 107 GLN   B CA  
5644 C CA  B GLN   B 107 ? 0.2705 0.2715 0.2816 -0.0353 0.0939  -0.0227 107 GLN   B CA  
5645 C C   A GLN   B 107 ? 0.2540 0.2600 0.2669 -0.0152 0.0718  -0.0253 107 GLN   B C   
5646 C C   B GLN   B 107 ? 0.2497 0.2578 0.2600 -0.0234 0.0737  -0.0293 107 GLN   B C   
5647 O O   A GLN   B 107 ? 0.2514 0.2597 0.2858 -0.0076 0.0574  -0.0350 107 GLN   B O   
5648 O O   B GLN   B 107 ? 0.2493 0.2627 0.2830 -0.0168 0.0575  -0.0400 107 GLN   B O   
5649 C CB  A GLN   B 107 ? 0.3026 0.3111 0.3607 -0.0197 0.0791  -0.0090 107 GLN   B CB  
5650 C CB  B GLN   B 107 ? 0.2969 0.3072 0.3517 -0.0290 0.0843  -0.0141 107 GLN   B CB  
5651 C CG  A GLN   B 107 ? 0.3268 0.3396 0.4290 -0.0145 0.0564  -0.0031 107 GLN   B CG  
5652 C CG  B GLN   B 107 ? 0.3261 0.3402 0.4249 -0.0191 0.0610  -0.0061 107 GLN   B CG  
5653 C CD  A GLN   B 107 ? 0.3440 0.3613 0.4828 -0.0135 0.0406  0.0019  107 GLN   B CD  
5654 C CD  B GLN   B 107 ? 0.3473 0.3652 0.4818 -0.0151 0.0443  0.0007  107 GLN   B CD  
5655 O OE1 A GLN   B 107 ? 0.3504 0.3705 0.5037 -0.0122 0.0384  0.0006  107 GLN   B OE1 
5656 O OE1 B GLN   B 107 ? 0.3556 0.3754 0.5031 -0.0136 0.0423  0.0006  107 GLN   B OE1 
5657 N NE2 A GLN   B 107 ? 0.3512 0.3685 0.5015 -0.0112 0.0333  0.0076  107 GLN   B NE2 
5658 N NE2 B GLN   B 107 ? 0.3563 0.3739 0.5016 -0.0112 0.0373  0.0063  107 GLN   B NE2 
5675 N N   . LEU   B 108 ? 0.2286 0.2397 0.2342 -0.0084 0.0650  -0.0279 108 LEU   B N   
5676 C CA  . LEU   B 108 ? 0.2129 0.2103 0.2007 0.0100  0.0477  -0.0131 108 LEU   B CA  
5677 C C   . LEU   B 108 ? 0.1864 0.1720 0.1957 0.0127  0.0348  0.0100  108 LEU   B C   
5678 O O   . LEU   B 108 ? 0.1896 0.1623 0.1880 0.0143  0.0261  0.0096  108 LEU   B O   
5679 C CB  . LEU   B 108 ? 0.2320 0.2306 0.1887 0.0069  0.0471  -0.0148 108 LEU   B CB  
5680 C CG  . LEU   B 108 ? 0.2508 0.2559 0.1945 0.0090  0.0413  -0.0295 108 LEU   B CG  
5681 C CD1 . LEU   B 108 ? 0.2556 0.2675 0.1796 -0.0013 0.0453  -0.0227 108 LEU   B CD1 
5682 C CD2 . LEU   B 108 ? 0.2672 0.2701 0.2298 0.0208  0.0327  -0.0399 108 LEU   B CD2 
5695 N N   . LEU   B 109 ? 0.1753 0.1557 0.1886 0.0101  0.0314  0.0116  109 LEU   B N   
5696 C CA  . LEU   B 109 ? 0.1595 0.1335 0.2080 0.0046  0.0309  0.0130  109 LEU   B CA  
5697 C C   . LEU   B 109 ? 0.1429 0.1203 0.2006 -0.0003 0.0306  0.0046  109 LEU   B C   
5698 O O   . LEU   B 109 ? 0.1408 0.1180 0.1975 -0.0010 0.0248  0.0134  109 LEU   B O   
5699 C CB  . LEU   B 109 ? 0.1630 0.1243 0.2094 0.0093  0.0239  0.0163  109 LEU   B CB  
5700 C CG  . LEU   B 109 ? 0.1619 0.1248 0.1912 0.0045  0.0167  0.0095  109 LEU   B CG  
5701 C CD1 . LEU   B 109 ? 0.1577 0.1396 0.1864 0.0052  0.0144  0.0113  109 LEU   B CD1 
5702 C CD2 . LEU   B 109 ? 0.1752 0.1349 0.2091 0.0061  0.0190  0.0050  109 LEU   B CD2 
5714 N N   . LYS   B 110 ? 0.1395 0.1295 0.2031 -0.0048 0.0352  0.0137  110 LYS   B N   
5715 C CA  . LYS   B 110 ? 0.1381 0.1250 0.2060 -0.0003 0.0283  0.0043  110 LYS   B CA  
5716 C C   . LYS   B 110 ? 0.1310 0.1247 0.1976 -0.0013 0.0257  -0.0031 110 LYS   B C   
5717 O O   . LYS   B 110 ? 0.1280 0.1281 0.1819 -0.0015 0.0183  -0.0069 110 LYS   B O   
5718 C CB  . LYS   B 110 ? 0.1391 0.1251 0.2279 -0.0031 0.0334  -0.0006 110 LYS   B CB  
5719 C CG  . LYS   B 110 ? 0.1377 0.1248 0.2447 -0.0066 0.0182  -0.0066 110 LYS   B CG  
5720 C CD  . LYS   B 110 ? 0.1434 0.1199 0.2587 -0.0076 0.0236  -0.0062 110 LYS   B CD  
5721 C CE  . LYS   B 110 ? 0.1447 0.1363 0.2589 -0.0060 0.0141  -0.0069 110 LYS   B CE  
5722 N NZ  . LYS   B 110 ? 0.1468 0.1513 0.2533 -0.0043 -0.0002 -0.0175 110 LYS   B NZ  
5736 N N   . SER   B 111 ? 0.1396 0.1273 0.1991 -0.0048 0.0291  0.0013  111 SER   B N   
5737 C CA  . SER   B 111 ? 0.1447 0.1298 0.1913 -0.0005 0.0237  0.0063  111 SER   B CA  
5738 C C   . SER   B 111 ? 0.1405 0.1245 0.1745 -0.0017 0.0138  -0.0048 111 SER   B C   
5739 O O   . SER   B 111 ? 0.1382 0.1252 0.1840 -0.0051 0.0082  -0.0032 111 SER   B O   
5740 C CB  . SER   B 111 ? 0.1649 0.1532 0.2049 0.0083  0.0340  0.0130  111 SER   B CB  
5741 O OG  . SER   B 111 ? 0.1839 0.1931 0.2104 0.0066  0.0380  0.0184  111 SER   B OG  
5747 N N   . ALA   B 112 ? 0.1360 0.1250 0.1807 0.0017  0.0172  0.0057  112 ALA   B N   
5748 C CA  . ALA   B 112 ? 0.1281 0.1302 0.1752 -0.0020 0.0121  0.0002  112 ALA   B CA  
5749 C C   . ALA   B 112 ? 0.1212 0.1226 0.1689 0.0025  0.0064  -0.0095 112 ALA   B C   
5750 O O   . ALA   B 112 ? 0.1256 0.1208 0.1740 -0.0082 0.0051  -0.0083 112 ALA   B O   
5751 C CB  . ALA   B 112 ? 0.1310 0.1407 0.1836 0.0062  0.0080  0.0085  112 ALA   B CB  
5757 N N   . TYR   B 113 ? 0.1224 0.1137 0.1767 -0.0028 0.0163  0.0018  113 TYR   B N   
5758 C CA  . TYR   B 113 ? 0.1182 0.1103 0.1678 -0.0017 0.0151  -0.0043 113 TYR   B CA  
5759 C C   . TYR   B 113 ? 0.1149 0.1092 0.1748 -0.0084 0.0052  0.0013  113 TYR   B C   
5760 O O   . TYR   B 113 ? 0.1224 0.1068 0.1695 -0.0047 0.0082  -0.0098 113 TYR   B O   
5761 C CB  . TYR   B 113 ? 0.1221 0.1100 0.1821 -0.0051 0.0157  -0.0038 113 TYR   B CB  
5762 C CG  . TYR   B 113 ? 0.1198 0.1107 0.1847 -0.0034 0.0063  0.0023  113 TYR   B CG  
5763 C CD1 . TYR   B 113 ? 0.1243 0.1136 0.1933 -0.0026 0.0070  0.0113  113 TYR   B CD1 
5764 C CD2 . TYR   B 113 ? 0.1348 0.1110 0.1798 -0.0069 0.0157  0.0038  113 TYR   B CD2 
5765 C CE1 . TYR   B 113 ? 0.1285 0.1189 0.1895 -0.0007 0.0191  0.0033  113 TYR   B CE1 
5766 C CE2 . TYR   B 113 ? 0.1316 0.1072 0.1903 0.0013  0.0139  0.0105  113 TYR   B CE2 
5767 C CZ  . TYR   B 113 ? 0.1249 0.1106 0.1915 0.0072  0.0101  0.0016  113 TYR   B CZ  
5768 O OH  . TYR   B 113 ? 0.1340 0.1109 0.2071 0.0056  0.0172  0.0054  113 TYR   B OH  
5778 N N   . GLU   B 114 ? 0.1124 0.1031 0.1840 -0.0020 0.0131  0.0004  114 GLU   B N   
5779 C CA  . GLU   B 114 ? 0.1126 0.1063 0.1802 -0.0004 0.0134  -0.0058 114 GLU   B CA  
5780 C C   . GLU   B 114 ? 0.1135 0.1093 0.1692 -0.0003 0.0114  -0.0123 114 GLU   B C   
5781 O O   . GLU   B 114 ? 0.1169 0.1062 0.1810 -0.0009 0.0031  -0.0035 114 GLU   B O   
5782 C CB  . GLU   B 114 ? 0.1194 0.1148 0.1913 -0.0026 0.0100  -0.0021 114 GLU   B CB  
5783 C CG  . GLU   B 114 ? 0.1239 0.1176 0.1938 -0.0070 0.0122  0.0000  114 GLU   B CG  
5784 C CD  . GLU   B 114 ? 0.1182 0.1225 0.1899 -0.0092 0.0125  -0.0080 114 GLU   B CD  
5785 O OE1 . GLU   B 114 ? 0.1233 0.1310 0.1933 -0.0097 0.0185  -0.0062 114 GLU   B OE1 
5786 O OE2 . GLU   B 114 ? 0.1190 0.1390 0.2068 -0.0163 0.0150  -0.0046 114 GLU   B OE2 
5793 N N   . ASN   B 115 ? 0.1180 0.1072 0.1680 -0.0024 0.0020  -0.0089 115 ASN   B N   
5794 C CA  . ASN   B 115 ? 0.1191 0.1114 0.1596 -0.0065 0.0013  -0.0059 115 ASN   B CA  
5795 C C   . ASN   B 115 ? 0.1152 0.1046 0.1694 -0.0093 -0.0018 -0.0070 115 ASN   B C   
5796 O O   . ASN   B 115 ? 0.1278 0.1065 0.1655 -0.0093 0.0022  -0.0061 115 ASN   B O   
5797 C CB  . ASN   B 115 ? 0.1298 0.1245 0.1727 -0.0093 0.0064  0.0000  115 ASN   B CB  
5798 C CG  . ASN   B 115 ? 0.1398 0.1267 0.1795 0.0005  0.0047  -0.0105 115 ASN   B CG  
5799 O OD1 . ASN   B 115 ? 0.1724 0.1378 0.1892 0.0013  0.0134  -0.0255 115 ASN   B OD1 
5800 N ND2 . ASN   B 115 ? 0.1384 0.1363 0.1638 -0.0042 0.0031  -0.0071 115 ASN   B ND2 
5807 N N   . PHE   B 116 ? 0.1120 0.1075 0.1500 -0.0043 -0.0015 0.0005  116 PHE   B N   
5808 C CA  . PHE   B 116 ? 0.1148 0.1076 0.1589 -0.0063 -0.0030 0.0003  116 PHE   B CA  
5809 C C   . PHE   B 116 ? 0.1229 0.0999 0.1534 -0.0088 -0.0050 -0.0011 116 PHE   B C   
5810 O O   . PHE   B 116 ? 0.1259 0.1079 0.1601 -0.0000 -0.0044 -0.0004 116 PHE   B O   
5811 C CB  . PHE   B 116 ? 0.1215 0.1072 0.1649 -0.0102 -0.0101 -0.0043 116 PHE   B CB  
5812 C CG  . PHE   B 116 ? 0.1122 0.1052 0.1584 -0.0073 -0.0062 -0.0001 116 PHE   B CG  
5813 C CD1 . PHE   B 116 ? 0.1221 0.1116 0.1665 -0.0054 -0.0072 0.0005  116 PHE   B CD1 
5814 C CD2 . PHE   B 116 ? 0.1181 0.1136 0.1612 0.0007  -0.0027 -0.0066 116 PHE   B CD2 
5815 C CE1 . PHE   B 116 ? 0.1216 0.1156 0.1672 -0.0057 -0.0134 -0.0011 116 PHE   B CE1 
5816 C CE2 . PHE   B 116 ? 0.1217 0.1116 0.1626 0.0016  0.0046  -0.0039 116 PHE   B CE2 
5817 C CZ  . PHE   B 116 ? 0.1151 0.1137 0.1600 -0.0041 -0.0035 -0.0030 116 PHE   B CZ  
5827 N N   . ASN   B 117 ? 0.1176 0.1100 0.1704 -0.0029 -0.0052 -0.0021 117 ASN   B N   
5828 C CA  . ASN   B 117 ? 0.1232 0.1076 0.1630 -0.0001 -0.0032 -0.0092 117 ASN   B CA  
5829 C C   . ASN   B 117 ? 0.1295 0.1093 0.1827 0.0041  -0.0051 -0.0092 117 ASN   B C   
5830 O O   . ASN   B 117 ? 0.1389 0.1131 0.2083 -0.0019 -0.0274 0.0022  117 ASN   B O   
5831 C CB  . ASN   B 117 ? 0.1255 0.1108 0.1695 -0.0002 -0.0044 -0.0141 117 ASN   B CB  
5832 C CG  . ASN   B 117 ? 0.1151 0.1157 0.1827 0.0008  -0.0067 -0.0161 117 ASN   B CG  
5833 O OD1 . ASN   B 117 ? 0.1396 0.1136 0.1924 -0.0127 0.0032  -0.0130 117 ASN   B OD1 
5834 N ND2 . ASN   B 117 ? 0.1190 0.1168 0.1743 0.0017  -0.0021 -0.0107 117 ASN   B ND2 
5841 N N   . GLN   B 118 ? 0.1265 0.1035 0.1761 -0.0054 -0.0112 -0.0064 118 GLN   B N   
5842 C CA  . GLN   B 118 ? 0.1334 0.1060 0.1829 0.0027  -0.0133 -0.0036 118 GLN   B CA  
5843 C C   . GLN   B 118 ? 0.1398 0.1060 0.1881 0.0016  -0.0086 -0.0036 118 GLN   B C   
5844 O O   . GLN   B 118 ? 0.1526 0.1049 0.2260 -0.0076 0.0078  -0.0033 118 GLN   B O   
5845 C CB  . GLN   B 118 ? 0.1378 0.1161 0.1964 0.0029  -0.0104 -0.0096 118 GLN   B CB  
5846 C CG  . GLN   B 118 ? 0.1452 0.1188 0.1964 0.0088  -0.0059 -0.0159 118 GLN   B CG  
5847 C CD  . GLN   B 118 ? 0.1480 0.1171 0.1940 0.0032  -0.0008 -0.0204 118 GLN   B CD  
5848 O OE1 . GLN   B 118 ? 0.1559 0.1121 0.2063 0.0030  0.0037  -0.0050 118 GLN   B OE1 
5849 N NE2 . GLN   B 118 ? 0.1503 0.1120 0.1932 0.0032  -0.0059 -0.0049 118 GLN   B NE2 
5858 N N   . HIS   B 119 ? 0.1376 0.1064 0.1543 -0.0071 -0.0056 -0.0003 119 HIS   B N   
5859 C CA  . HIS   B 119 ? 0.1428 0.1172 0.1542 -0.0019 -0.0136 0.0065  119 HIS   B CA  
5860 C C   . HIS   B 119 ? 0.1475 0.1201 0.1522 -0.0014 -0.0215 0.0017  119 HIS   B C   
5861 O O   . HIS   B 119 ? 0.1503 0.1210 0.1707 -0.0216 -0.0091 0.0066  119 HIS   B O   
5862 C CB  . HIS   B 119 ? 0.1448 0.1296 0.1685 0.0017  -0.0078 -0.0007 119 HIS   B CB  
5863 C CG  . HIS   B 119 ? 0.1472 0.1524 0.1825 0.0182  -0.0268 -0.0206 119 HIS   B CG  
5864 N ND1 . HIS   B 119 ? 0.1575 0.1659 0.2173 0.0083  -0.0452 -0.0374 119 HIS   B ND1 
5865 C CD2 . HIS   B 119 ? 0.1681 0.1772 0.1959 0.0345  -0.0364 -0.0298 119 HIS   B CD2 
5866 C CE1 . HIS   B 119 ? 0.1787 0.1847 0.2326 0.0248  -0.0479 -0.0552 119 HIS   B CE1 
5867 N NE2 . HIS   B 119 ? 0.1831 0.2005 0.2167 0.0335  -0.0460 -0.0454 119 HIS   B NE2 
5875 N N   . GLU   B 120 ? 0.1576 0.1235 0.1604 -0.0064 -0.0291 0.0092  120 GLU   B N   
5876 C CA  . GLU   B 120 ? 0.1842 0.1411 0.1688 0.0007  -0.0371 0.0244  120 GLU   B CA  
5877 C C   . GLU   B 120 ? 0.1654 0.1269 0.1616 -0.0084 -0.0274 0.0273  120 GLU   B C   
5878 O O   . GLU   B 120 ? 0.1628 0.1368 0.1567 -0.0132 -0.0313 0.0132  120 GLU   B O   
5879 C CB  . GLU   B 120 ? 0.2541 0.1775 0.2331 0.0229  -0.0688 0.0550  120 GLU   B CB  
5880 C CG  . GLU   B 120 ? 0.3149 0.2550 0.3367 0.0346  -0.0868 0.0768  120 GLU   B CG  
5881 C CD  . GLU   B 120 ? 0.3665 0.3296 0.4428 0.0371  -0.0926 0.0932  120 GLU   B CD  
5882 O OE1 . GLU   B 120 ? 0.3917 0.3566 0.4759 0.0326  -0.0891 0.1050  120 GLU   B OE1 
5883 O OE2 . GLU   B 120 ? 0.3892 0.3602 0.4977 0.0378  -0.0898 0.0871  120 GLU   B OE2 
5890 N N   . VAL   B 121 ? 0.1572 0.1202 0.1608 -0.0071 -0.0188 0.0116  121 VAL   B N   
5891 C CA  . VAL   B 121 ? 0.1544 0.1335 0.1505 -0.0094 -0.0138 0.0180  121 VAL   B CA  
5892 C C   . VAL   B 121 ? 0.1416 0.1281 0.1452 -0.0164 -0.0106 0.0163  121 VAL   B C   
5893 O O   . VAL   B 121 ? 0.1517 0.1221 0.1622 -0.0252 -0.0233 0.0080  121 VAL   B O   
5894 C CB  . VAL   B 121 ? 0.1707 0.1639 0.1516 -0.0007 -0.0193 0.0164  121 VAL   B CB  
5895 C CG1 . VAL   B 121 ? 0.1847 0.1753 0.1728 -0.0068 -0.0074 0.0192  121 VAL   B CG1 
5896 C CG2 . VAL   B 121 ? 0.1931 0.1886 0.1706 0.0026  -0.0145 0.0055  121 VAL   B CG2 
5906 N N   . LEU   B 122 ? 0.1394 0.1191 0.1345 -0.0120 -0.0133 0.0032  122 LEU   B N   
5907 C CA  . LEU   B 122 ? 0.1312 0.1306 0.1295 -0.0142 -0.0112 0.0051  122 LEU   B CA  
5908 C C   . LEU   B 122 ? 0.1298 0.1153 0.1324 -0.0196 -0.0146 0.0061  122 LEU   B C   
5909 O O   . LEU   B 122 ? 0.1406 0.1181 0.1596 -0.0227 -0.0306 0.0018  122 LEU   B O   
5910 C CB  . LEU   B 122 ? 0.1537 0.1365 0.1575 -0.0032 -0.0146 0.0156  122 LEU   B CB  
5911 C CG  . LEU   B 122 ? 0.1462 0.1384 0.1646 -0.0119 -0.0052 0.0151  122 LEU   B CG  
5912 C CD1 . LEU   B 122 ? 0.1502 0.1540 0.1834 -0.0108 -0.0187 0.0054  122 LEU   B CD1 
5913 C CD2 . LEU   B 122 ? 0.1488 0.1417 0.1407 -0.0032 -0.0002 -0.0002 122 LEU   B CD2 
5925 N N   . LEU   B 123 ? 0.1334 0.1112 0.1397 -0.0176 -0.0142 0.0068  123 LEU   B N   
5926 C CA  . LEU   B 123 ? 0.1345 0.1083 0.1350 -0.0200 -0.0244 0.0021  123 LEU   B CA  
5927 C C   . LEU   B 123 ? 0.1296 0.1026 0.1418 -0.0170 -0.0113 -0.0044 123 LEU   B C   
5928 O O   . LEU   B 123 ? 0.1423 0.1110 0.1346 -0.0262 -0.0103 -0.0030 123 LEU   B O   
5929 C CB  . LEU   B 123 ? 0.1401 0.1144 0.1443 -0.0205 -0.0091 -0.0071 123 LEU   B CB  
5930 C CG  . LEU   B 123 ? 0.1350 0.1199 0.1500 -0.0116 -0.0014 0.0055  123 LEU   B CG  
5931 C CD1 . LEU   B 123 ? 0.1400 0.1237 0.1664 -0.0115 0.0089  -0.0052 123 LEU   B CD1 
5932 C CD2 . LEU   B 123 ? 0.1440 0.1241 0.1626 -0.0114 -0.0002 0.0192  123 LEU   B CD2 
5944 N N   . ALA   B 124 ? 0.1273 0.1080 0.1274 -0.0168 -0.0035 -0.0054 124 ALA   B N   
5945 C CA  . ALA   B 124 ? 0.1190 0.1086 0.1416 -0.0171 -0.0074 -0.0098 124 ALA   B CA  
5946 C C   . ALA   B 124 ? 0.1124 0.1069 0.1424 -0.0169 -0.0094 -0.0038 124 ALA   B C   
5947 O O   . ALA   B 124 ? 0.1273 0.1116 0.1451 -0.0137 -0.0106 0.0021  124 ALA   B O   
5948 C CB  . ALA   B 124 ? 0.1331 0.1111 0.1399 -0.0090 0.0030  0.0024  124 ALA   B CB  
5954 N N   . PRO   B 125 ? 0.1279 0.1125 0.1358 -0.0124 -0.0148 0.0059  125 PRO   B N   
5955 C CA  . PRO   B 125 ? 0.1355 0.1103 0.1498 -0.0092 -0.0118 0.0123  125 PRO   B CA  
5956 C C   . PRO   B 125 ? 0.1280 0.1094 0.1704 -0.0133 -0.0085 0.0099  125 PRO   B C   
5957 O O   . PRO   B 125 ? 0.1329 0.1056 0.1758 -0.0073 -0.0011 0.0076  125 PRO   B O   
5958 C CB  . PRO   B 125 ? 0.1383 0.1373 0.1587 -0.0207 -0.0167 0.0254  125 PRO   B CB  
5959 C CG  . PRO   B 125 ? 0.1435 0.1412 0.1545 -0.0262 -0.0135 0.0153  125 PRO   B CG  
5960 C CD  . PRO   B 125 ? 0.1330 0.1259 0.1376 -0.0241 -0.0094 0.0022  125 PRO   B CD  
5968 N N   . LEU   B 126 ? 0.1310 0.1043 0.1847 -0.0127 0.0059  0.0098  126 LEU   B N   
5969 C CA  . LEU   B 126 ? 0.1392 0.1150 0.1750 -0.0141 0.0100  0.0085  126 LEU   B CA  
5970 C C   . LEU   B 126 ? 0.1381 0.1251 0.1770 -0.0051 0.0085  0.0163  126 LEU   B C   
5971 O O   . LEU   B 126 ? 0.1556 0.1520 0.1928 0.0119  -0.0036 -0.0112 126 LEU   B O   
5972 C CB  . LEU   B 126 ? 0.1542 0.1189 0.1982 -0.0167 0.0296  0.0044  126 LEU   B CB  
5973 C CG  . LEU   B 126 ? 0.1701 0.1295 0.2104 -0.0227 0.0244  -0.0156 126 LEU   B CG  
5974 C CD1 . LEU   B 126 ? 0.1798 0.1407 0.2544 -0.0236 0.0209  -0.0224 126 LEU   B CD1 
5975 C CD2 . LEU   B 126 ? 0.1671 0.1383 0.2140 -0.0292 0.0235  -0.0138 126 LEU   B CD2 
5987 N N   . LEU   B 127 ? 0.1330 0.1075 0.1896 -0.0020 0.0134  0.0075  127 LEU   B N   
5988 C CA  . LEU   B 127 ? 0.1384 0.1199 0.1927 -0.0110 0.0140  0.0146  127 LEU   B CA  
5989 C C   . LEU   B 127 ? 0.1311 0.1172 0.1922 -0.0099 0.0158  0.0111  127 LEU   B C   
5990 O O   . LEU   B 127 ? 0.1317 0.1275 0.1818 -0.0150 0.0086  0.0097  127 LEU   B O   
5991 C CB  . LEU   B 127 ? 0.1532 0.1227 0.1882 -0.0089 0.0177  0.0133  127 LEU   B CB  
5992 C CG  . LEU   B 127 ? 0.1586 0.1192 0.2010 -0.0013 0.0158  0.0120  127 LEU   B CG  
5993 C CD1 . LEU   B 127 ? 0.1698 0.1192 0.2147 0.0038  0.0038  0.0051  127 LEU   B CD1 
5994 C CD2 . LEU   B 127 ? 0.1574 0.1262 0.2162 -0.0070 0.0144  0.0181  127 LEU   B CD2 
6006 N N   . SER   B 128 ? 0.1315 0.1180 0.1852 -0.0052 -0.0015 0.0110  128 SER   B N   
6007 C CA  . SER   B 128 ? 0.1503 0.1291 0.1797 0.0027  -0.0052 0.0122  128 SER   B CA  
6008 C C   . SER   B 128 ? 0.1600 0.1283 0.1936 0.0026  -0.0154 0.0111  128 SER   B C   
6009 O O   . SER   B 128 ? 0.1740 0.1306 0.2312 -0.0004 -0.0037 0.0276  128 SER   B O   
6010 C CB  . SER   B 128 ? 0.1578 0.1298 0.1874 0.0019  0.0039  0.0199  128 SER   B CB  
6011 O OG  . SER   B 128 ? 0.1636 0.1416 0.1996 0.0085  0.0091  0.0234  128 SER   B OG  
6017 N N   . ALA   B 129 ? 0.1695 0.1337 0.1929 0.0178  -0.0105 0.0054  129 ALA   B N   
6018 C CA  . ALA   B 129 ? 0.1834 0.1435 0.2109 0.0208  -0.0123 -0.0051 129 ALA   B CA  
6019 C C   . ALA   B 129 ? 0.1713 0.1375 0.1938 0.0177  0.0071  -0.0028 129 ALA   B C   
6020 O O   . ALA   B 129 ? 0.1640 0.1408 0.1992 0.0209  -0.0042 0.0056  129 ALA   B O   
6021 C CB  . ALA   B 129 ? 0.2037 0.1643 0.2392 0.0264  -0.0124 -0.0071 129 ALA   B CB  
6027 N N   . GLY   B 130 ? 0.1679 0.1379 0.2132 0.0200  0.0073  -0.0024 130 GLY   B N   
6028 C CA  . GLY   B 130 ? 0.1722 0.1453 0.2265 0.0197  0.0194  -0.0007 130 GLY   B CA  
6029 C C   . GLY   B 130 ? 0.1754 0.1433 0.2250 0.0109  0.0112  -0.0006 130 GLY   B C   
6030 O O   . GLY   B 130 ? 0.1953 0.1499 0.2371 0.0102  0.0016  0.0131  130 GLY   B O   
6034 N N   . ILE   B 131 ? 0.1674 0.1540 0.2276 0.0247  0.0028  0.0053  131 ILE   B N   
6035 C CA  . ILE   B 131 ? 0.1883 0.1682 0.2271 0.0255  -0.0166 0.0162  131 ILE   B CA  
6036 C C   . ILE   B 131 ? 0.1998 0.1611 0.1965 0.0170  -0.0106 0.0128  131 ILE   B C   
6037 O O   . ILE   B 131 ? 0.2275 0.1799 0.2100 0.0211  -0.0318 0.0128  131 ILE   B O   
6038 C CB  . ILE   B 131 ? 0.1890 0.2064 0.2586 0.0216  -0.0240 0.0249  131 ILE   B CB  
6039 C CG1 . ILE   B 131 ? 0.1946 0.2264 0.2689 0.0005  -0.0178 0.0309  131 ILE   B CG1 
6040 C CG2 . ILE   B 131 ? 0.1883 0.2218 0.2804 0.0229  -0.0157 0.0146  131 ILE   B CG2 
6041 C CD1 . ILE   B 131 ? 0.2043 0.2421 0.2824 -0.0164 -0.0156 0.0447  131 ILE   B CD1 
6053 N N   . PHE   B 132 ? 0.1821 0.1426 0.1836 0.0151  0.0075  0.0210  132 PHE   B N   
6054 C CA  . PHE   B 132 ? 0.1929 0.1486 0.1868 0.0059  0.0246  0.0107  132 PHE   B CA  
6055 C C   . PHE   B 132 ? 0.2127 0.1611 0.1886 0.0052  0.0284  0.0125  132 PHE   B C   
6056 O O   . PHE   B 132 ? 0.2347 0.1849 0.2180 -0.0069 0.0406  0.0138  132 PHE   B O   
6057 C CB  . PHE   B 132 ? 0.1777 0.1521 0.1766 0.0073  0.0234  0.0115  132 PHE   B CB  
6058 C CG  . PHE   B 132 ? 0.1767 0.1491 0.1780 0.0107  0.0238  0.0133  132 PHE   B CG  
6059 C CD1 . PHE   B 132 ? 0.1794 0.1494 0.2048 0.0108  0.0302  0.0136  132 PHE   B CD1 
6060 C CD2 . PHE   B 132 ? 0.1736 0.1528 0.1580 0.0142  0.0194  0.0193  132 PHE   B CD2 
6061 C CE1 . PHE   B 132 ? 0.1819 0.1505 0.2243 0.0058  0.0248  0.0143  132 PHE   B CE1 
6062 C CE2 . PHE   B 132 ? 0.1796 0.1560 0.1758 0.0174  0.0101  0.0130  132 PHE   B CE2 
6063 C CZ  . PHE   B 132 ? 0.1844 0.1569 0.2105 0.0063  0.0082  0.0219  132 PHE   B CZ  
6073 N N   . GLY   B 133 ? 0.2150 0.1527 0.1910 -0.0046 0.0241  0.0359  133 GLY   B N   
6074 C CA  . GLY   B 133 ? 0.2232 0.1655 0.1986 -0.0192 0.0185  0.0365  133 GLY   B CA  
6075 C C   . GLY   B 133 ? 0.2297 0.1706 0.2043 -0.0278 0.0187  0.0393  133 GLY   B C   
6076 O O   . GLY   B 133 ? 0.2506 0.1816 0.2488 -0.0384 0.0153  0.0527  133 GLY   B O   
6080 N N   . ALA   B 134 ? 0.2118 0.1653 0.1896 -0.0306 0.0170  0.0247  134 ALA   B N   
6081 C CA  . ALA   B 134 ? 0.2085 0.1613 0.2008 -0.0263 0.0187  0.0087  134 ALA   B CA  
6082 C C   . ALA   B 134 ? 0.2067 0.1536 0.1979 -0.0146 0.0197  0.0154  134 ALA   B C   
6083 O O   . ALA   B 134 ? 0.2092 0.1751 0.2217 -0.0054 0.0191  0.0128  134 ALA   B O   
6084 C CB  . ALA   B 134 ? 0.2122 0.1619 0.2270 -0.0142 0.0130  0.0011  134 ALA   B CB  
6090 N N   . ASP   B 135 ? 0.2168 0.1526 0.2059 -0.0209 0.0084  0.0165  135 ASP   B N   
6091 C CA  . ASP   B 135 ? 0.2329 0.1485 0.2229 -0.0183 -0.0027 0.0183  135 ASP   B CA  
6092 C C   . ASP   B 135 ? 0.2122 0.1349 0.2115 -0.0047 -0.0035 0.0144  135 ASP   B C   
6093 O O   . ASP   B 135 ? 0.2003 0.1297 0.2129 -0.0052 0.0039  0.0199  135 ASP   B O   
6094 C CB  . ASP   B 135 ? 0.2621 0.1603 0.2458 -0.0388 -0.0034 0.0266  135 ASP   B CB  
6095 C CG  . ASP   B 135 ? 0.2927 0.1616 0.2884 -0.0586 -0.0010 0.0247  135 ASP   B CG  
6096 O OD1 . ASP   B 135 ? 0.3055 0.1530 0.2855 -0.0448 -0.0102 0.0171  135 ASP   B OD1 
6097 O OD2 . ASP   B 135 ? 0.3127 0.1932 0.3405 -0.0710 -0.0005 0.0066  135 ASP   B OD2 
6102 N N   . PRO   B 136 ? 0.2093 0.1404 0.2230 0.0145  -0.0095 0.0155  136 PRO   B N   
6103 C CA  . PRO   B 136 ? 0.1905 0.1315 0.2178 0.0143  -0.0136 0.0031  136 PRO   B CA  
6104 C C   . PRO   B 136 ? 0.1675 0.1220 0.2168 0.0070  -0.0044 -0.0031 136 PRO   B C   
6105 O O   . PRO   B 136 ? 0.1559 0.1184 0.2163 0.0053  -0.0004 0.0008  136 PRO   B O   
6106 C CB  . PRO   B 136 ? 0.1996 0.1541 0.2318 0.0245  -0.0225 -0.0049 136 PRO   B CB  
6107 C CG  . PRO   B 136 ? 0.2191 0.1600 0.2496 0.0314  -0.0160 -0.0029 136 PRO   B CG  
6108 C CD  . PRO   B 136 ? 0.2174 0.1537 0.2412 0.0357  -0.0060 0.0051  136 PRO   B CD  
6116 N N   . ILE   B 137 ? 0.1764 0.1161 0.2313 0.0101  -0.0121 -0.0054 137 ILE   B N   
6117 C CA  . ILE   B 137 ? 0.1844 0.1159 0.2408 -0.0031 -0.0081 -0.0068 137 ILE   B CA  
6118 C C   . ILE   B 137 ? 0.1749 0.1183 0.2297 -0.0117 0.0060  0.0088  137 ILE   B C   
6119 O O   . ILE   B 137 ? 0.1574 0.1233 0.2343 -0.0135 0.0079  0.0020  137 ILE   B O   
6120 C CB  . ILE   B 137 ? 0.2138 0.1243 0.2846 -0.0078 -0.0138 -0.0060 137 ILE   B CB  
6121 C CG1 . ILE   B 137 ? 0.2374 0.1379 0.3313 -0.0019 -0.0064 -0.0176 137 ILE   B CG1 
6122 C CG2 . ILE   B 137 ? 0.2199 0.1285 0.3008 -0.0343 -0.0127 -0.0024 137 ILE   B CG2 
6123 C CD1 . ILE   B 137 ? 0.2583 0.1595 0.3768 0.0176  -0.0065 -0.0048 137 ILE   B CD1 
6135 N N   . HIS   B 138 ? 0.1850 0.1233 0.2228 -0.0075 0.0138  0.0203  138 HIS   B N   
6136 C CA  . HIS   B 138 ? 0.1898 0.1292 0.2310 -0.0050 0.0274  0.0122  138 HIS   B CA  
6137 C C   . HIS   B 138 ? 0.1738 0.1261 0.2206 -0.0071 0.0284  0.0175  138 HIS   B C   
6138 O O   . HIS   B 138 ? 0.1671 0.1315 0.2421 -0.0008 0.0328  0.0282  138 HIS   B O   
6139 C CB  . HIS   B 138 ? 0.2084 0.1374 0.2553 -0.0106 0.0369  0.0109  138 HIS   B CB  
6140 C CG  . HIS   B 138 ? 0.2220 0.1576 0.2516 -0.0135 0.0501  0.0244  138 HIS   B CG  
6141 N ND1 . HIS   B 138 ? 0.2283 0.1787 0.2755 -0.0092 0.0658  0.0159  138 HIS   B ND1 
6142 C CD2 . HIS   B 138 ? 0.2327 0.1699 0.2471 -0.0159 0.0505  0.0210  138 HIS   B CD2 
6143 C CE1 . HIS   B 138 ? 0.2337 0.1806 0.2715 -0.0114 0.0726  0.0189  138 HIS   B CE1 
6144 N NE2 . HIS   B 138 ? 0.2401 0.1735 0.2550 -0.0051 0.0642  0.0167  138 HIS   B NE2 
6152 N N   . SER   B 139 ? 0.1689 0.1193 0.2163 0.0032  0.0227  0.0134  139 SER   B N   
6153 C CA  . SER   B 139 ? 0.1644 0.1094 0.1985 -0.0016 0.0207  -0.0035 139 SER   B CA  
6154 C C   . SER   B 139 ? 0.1413 0.1105 0.1967 -0.0059 0.0160  -0.0002 139 SER   B C   
6155 O O   . SER   B 139 ? 0.1405 0.1087 0.1963 0.0005  0.0064  -0.0024 139 SER   B O   
6156 C CB  . SER   B 139 ? 0.1692 0.1155 0.2042 -0.0036 0.0082  -0.0028 139 SER   B CB  
6157 O OG  . SER   B 139 ? 0.1686 0.1164 0.1995 -0.0047 -0.0106 0.0096  139 SER   B OG  
6163 N N   . LEU   B 140 ? 0.1407 0.0992 0.1942 -0.0069 0.0131  -0.0010 140 LEU   B N   
6164 C CA  . LEU   B 140 ? 0.1359 0.1082 0.1933 -0.0051 0.0082  -0.0006 140 LEU   B CA  
6165 C C   . LEU   B 140 ? 0.1308 0.1102 0.2125 -0.0087 0.0041  -0.0082 140 LEU   B C   
6166 O O   . LEU   B 140 ? 0.1345 0.1138 0.2199 -0.0044 -0.0046 -0.0046 140 LEU   B O   
6167 C CB  . LEU   B 140 ? 0.1305 0.1034 0.1955 -0.0082 0.0077  -0.0088 140 LEU   B CB  
6168 C CG  . LEU   B 140 ? 0.1409 0.1105 0.1892 -0.0123 -0.0041 -0.0023 140 LEU   B CG  
6169 C CD1 . LEU   B 140 ? 0.1504 0.1241 0.2081 -0.0123 0.0056  -0.0053 140 LEU   B CD1 
6170 C CD2 . LEU   B 140 ? 0.1645 0.1238 0.2031 -0.0056 -0.0096 -0.0103 140 LEU   B CD2 
6182 N N   . ARG   B 141 ? 0.1284 0.1107 0.2309 -0.0096 0.0084  -0.0112 141 ARG   B N   
6183 C CA  . ARG   B 141 ? 0.1303 0.1103 0.2649 -0.0112 0.0185  -0.0090 141 ARG   B CA  
6184 C C   . ARG   B 141 ? 0.1248 0.1164 0.2568 -0.0139 0.0112  -0.0057 141 ARG   B C   
6185 O O   . ARG   B 141 ? 0.1304 0.1108 0.2541 -0.0106 0.0056  -0.0179 141 ARG   B O   
6186 C CB  . ARG   B 141 ? 0.1529 0.1231 0.2977 -0.0157 0.0372  -0.0082 141 ARG   B CB  
6187 C CG  . ARG   B 141 ? 0.1802 0.1509 0.3197 -0.0175 0.0463  -0.0001 141 ARG   B CG  
6188 C CD  . ARG   B 141 ? 0.2251 0.1701 0.3277 -0.0107 0.0308  -0.0146 141 ARG   B CD  
6189 N NE  . ARG   B 141 ? 0.2488 0.1722 0.3387 -0.0333 0.0391  -0.0190 141 ARG   B NE  
6190 C CZ  . ARG   B 141 ? 0.2545 0.1541 0.3361 -0.0341 0.0578  -0.0306 141 ARG   B CZ  
6191 N NH1 . ARG   B 141 ? 0.2681 0.1465 0.3343 -0.0318 0.0542  -0.0315 141 ARG   B NH1 
6192 N NH2 . ARG   B 141 ? 0.2665 0.1737 0.3485 -0.0184 0.0435  -0.0287 141 ARG   B NH2 
6206 N N   . VAL   B 142 ? 0.1278 0.1125 0.2318 -0.0070 0.0206  -0.0092 142 VAL   B N   
6207 C CA  . VAL   B 142 ? 0.1273 0.1137 0.2335 -0.0063 0.0201  -0.0067 142 VAL   B CA  
6208 C C   . VAL   B 142 ? 0.1231 0.1114 0.2311 -0.0034 0.0093  -0.0084 142 VAL   B C   
6209 O O   . VAL   B 142 ? 0.1316 0.1078 0.2543 0.0016  0.0086  -0.0045 142 VAL   B O   
6210 C CB  . VAL   B 142 ? 0.1423 0.1194 0.2299 -0.0011 0.0175  0.0085  142 VAL   B CB  
6211 C CG1 . VAL   B 142 ? 0.1468 0.1141 0.2406 0.0089  0.0228  -0.0027 142 VAL   B CG1 
6212 C CG2 . VAL   B 142 ? 0.1591 0.1288 0.2310 -0.0025 0.0147  0.0058  142 VAL   B CG2 
6222 N N   . CYS   B 143 ? 0.1209 0.1100 0.2163 -0.0057 0.0075  0.0016  143 CYS   B N   
6223 C CA  . CYS   B 143 ? 0.1190 0.1111 0.2180 -0.0057 0.0064  -0.0083 143 CYS   B CA  
6224 C C   . CYS   B 143 ? 0.1138 0.1135 0.2220 -0.0019 0.0021  -0.0140 143 CYS   B C   
6225 O O   . CYS   B 143 ? 0.1201 0.1120 0.2188 -0.0023 0.0009  -0.0075 143 CYS   B O   
6226 C CB  . CYS   B 143 ? 0.1279 0.1161 0.2142 -0.0086 0.0048  -0.0126 143 CYS   B CB  
6227 S SG  . CYS   B 143 ? 0.1307 0.1315 0.2092 -0.0051 0.0074  -0.0001 143 CYS   B SG  
6233 N N   . VAL   B 144 ? 0.1222 0.1106 0.2306 -0.0046 0.0006  -0.0108 144 VAL   B N   
6234 C CA  . VAL   B 144 ? 0.1291 0.1180 0.2509 -0.0133 -0.0093 -0.0179 144 VAL   B CA  
6235 C C   . VAL   B 144 ? 0.1271 0.1254 0.2499 -0.0071 -0.0104 -0.0065 144 VAL   B C   
6236 O O   . VAL   B 144 ? 0.1376 0.1424 0.2779 0.0075  -0.0039 0.0107  144 VAL   B O   
6237 C CB  . VAL   B 144 ? 0.1531 0.1344 0.2957 -0.0073 -0.0147 -0.0334 144 VAL   B CB  
6238 C CG1 . VAL   B 144 ? 0.1784 0.1696 0.3215 0.0044  -0.0181 -0.0301 144 VAL   B CG1 
6239 C CG2 . VAL   B 144 ? 0.1650 0.1364 0.2975 0.0046  -0.0312 -0.0438 144 VAL   B CG2 
6249 N N   . ASP   B 145 ? 0.1270 0.1168 0.2579 -0.0035 -0.0041 -0.0184 145 ASP   B N   
6250 C CA  . ASP   B 145 ? 0.1288 0.1261 0.2707 -0.0078 -0.0008 -0.0077 145 ASP   B CA  
6251 C C   . ASP   B 145 ? 0.1268 0.1286 0.2642 -0.0037 -0.0011 -0.0115 145 ASP   B C   
6252 O O   . ASP   B 145 ? 0.1234 0.1390 0.3120 -0.0079 0.0089  -0.0295 145 ASP   B O   
6253 C CB  . ASP   B 145 ? 0.1409 0.1338 0.3014 -0.0157 0.0154  -0.0052 145 ASP   B CB  
6254 C CG  . ASP   B 145 ? 0.1514 0.1356 0.3410 -0.0240 0.0319  -0.0079 145 ASP   B CG  
6255 O OD1 . ASP   B 145 ? 0.1522 0.1383 0.3518 -0.0221 0.0035  -0.0197 145 ASP   B OD1 
6256 O OD2 . ASP   B 145 ? 0.1886 0.1514 0.3919 -0.0252 0.0564  -0.0021 145 ASP   B OD2 
6261 N N   . THR   B 146 ? 0.1209 0.1171 0.2294 -0.0069 0.0023  -0.0077 146 THR   B N   
6262 C CA  . THR   B 146 ? 0.1304 0.1115 0.2138 -0.0120 0.0087  -0.0092 146 THR   B CA  
6263 C C   . THR   B 146 ? 0.1257 0.1127 0.2029 -0.0032 0.0037  -0.0047 146 THR   B C   
6264 O O   . THR   B 146 ? 0.1340 0.1140 0.2207 -0.0035 0.0025  -0.0041 146 THR   B O   
6265 C CB  . THR   B 146 ? 0.1371 0.1108 0.2189 -0.0045 0.0186  -0.0112 146 THR   B CB  
6266 O OG1 . THR   B 146 ? 0.1382 0.1107 0.2211 -0.0064 0.0278  -0.0059 146 THR   B OG1 
6267 C CG2 . THR   B 146 ? 0.1418 0.1228 0.2090 -0.0043 0.0147  -0.0072 146 THR   B CG2 
6275 N N   . VAL   B 147 ? 0.1268 0.1162 0.1966 -0.0054 0.0103  -0.0079 147 VAL   B N   
6276 C CA  . VAL   B 147 ? 0.1290 0.1145 0.1906 -0.0058 -0.0045 -0.0079 147 VAL   B CA  
6277 C C   . VAL   B 147 ? 0.1247 0.1125 0.1989 -0.0126 -0.0084 -0.0114 147 VAL   B C   
6278 O O   . VAL   B 147 ? 0.1336 0.1246 0.2113 -0.0141 -0.0238 -0.0208 147 VAL   B O   
6279 C CB  . VAL   B 147 ? 0.1340 0.1214 0.1828 -0.0080 -0.0035 -0.0072 147 VAL   B CB  
6280 C CG1 . VAL   B 147 ? 0.1356 0.1352 0.1806 -0.0127 0.0033  -0.0024 147 VAL   B CG1 
6281 C CG2 . VAL   B 147 ? 0.1364 0.1250 0.1838 -0.0073 0.0020  -0.0041 147 VAL   B CG2 
6291 N N   . ARG   B 148 ? 0.1243 0.1134 0.1961 -0.0086 -0.0174 -0.0200 148 ARG   B N   
6292 C CA  . ARG   B 148 ? 0.1308 0.1223 0.1958 -0.0041 -0.0214 -0.0133 148 ARG   B CA  
6293 C C   . ARG   B 148 ? 0.1356 0.1299 0.1903 -0.0064 -0.0223 -0.0086 148 ARG   B C   
6294 O O   . ARG   B 148 ? 0.1542 0.1619 0.2070 -0.0196 -0.0292 -0.0086 148 ARG   B O   
6295 C CB  . ARG   B 148 ? 0.1322 0.1346 0.2052 -0.0037 -0.0295 -0.0233 148 ARG   B CB  
6296 C CG  . ARG   B 148 ? 0.1342 0.1456 0.2076 -0.0048 -0.0179 -0.0352 148 ARG   B CG  
6297 C CD  . ARG   B 148 ? 0.1395 0.1609 0.2159 0.0102  -0.0233 -0.0366 148 ARG   B CD  
6298 N NE  . ARG   B 148 ? 0.1489 0.1613 0.2042 0.0215  -0.0203 -0.0321 148 ARG   B NE  
6299 C CZ  . ARG   B 148 ? 0.1439 0.1511 0.1856 0.0176  -0.0140 -0.0247 148 ARG   B CZ  
6300 N NH1 . ARG   B 148 ? 0.1432 0.1484 0.1948 -0.0024 -0.0035 -0.0210 148 ARG   B NH1 
6301 N NH2 . ARG   B 148 ? 0.1631 0.1436 0.1804 0.0200  -0.0153 -0.0255 148 ARG   B NH2 
6315 N N   . THR   B 149 ? 0.1353 0.1282 0.1814 -0.0075 -0.0211 -0.0073 149 THR   B N   
6316 C CA  . THR   B 149 ? 0.1416 0.1344 0.1763 -0.0103 -0.0212 -0.0019 149 THR   B CA  
6317 C C   . THR   B 149 ? 0.1415 0.1254 0.1719 -0.0128 -0.0270 -0.0050 149 THR   B C   
6318 O O   . THR   B 149 ? 0.1461 0.1217 0.1863 -0.0120 -0.0180 -0.0011 149 THR   B O   
6319 C CB  . THR   B 149 ? 0.1443 0.1271 0.1719 -0.0111 -0.0204 0.0033  149 THR   B CB  
6320 O OG1 . THR   B 149 ? 0.1487 0.1306 0.1788 -0.0205 -0.0193 -0.0002 149 THR   B OG1 
6321 C CG2 . THR   B 149 ? 0.1534 0.1321 0.2040 -0.0052 -0.0119 0.0032  149 THR   B CG2 
6329 N N   . ASN   B 150 ? 0.1521 0.1216 0.1650 -0.0097 -0.0307 -0.0028 150 ASN   B N   
6330 C CA  . ASN   B 150 ? 0.1529 0.1306 0.1679 -0.0109 -0.0256 -0.0036 150 ASN   B CA  
6331 C C   . ASN   B 150 ? 0.1467 0.1271 0.1737 -0.0091 -0.0210 -0.0047 150 ASN   B C   
6332 O O   . ASN   B 150 ? 0.1540 0.1284 0.1895 -0.0244 -0.0372 -0.0052 150 ASN   B O   
6333 C CB  . ASN   B 150 ? 0.1725 0.1613 0.1672 -0.0126 -0.0235 0.0029  150 ASN   B CB  
6334 C CG  . ASN   B 150 ? 0.2018 0.2074 0.2046 -0.0151 -0.0334 0.0238  150 ASN   B CG  
6335 O OD1 . ASN   B 150 ? 0.2132 0.2320 0.2292 -0.0282 -0.0481 0.0175  150 ASN   B OD1 
6336 N ND2 . ASN   B 150 ? 0.2141 0.2227 0.2305 -0.0061 -0.0398 0.0554  150 ASN   B ND2 
6343 N N   . VAL   B 151 ? 0.1392 0.1250 0.1679 -0.0112 -0.0240 0.0010  151 VAL   B N   
6344 C CA  . VAL   B 151 ? 0.1397 0.1273 0.1649 -0.0159 -0.0183 -0.0017 151 VAL   B CA  
6345 C C   . VAL   B 151 ? 0.1390 0.1199 0.1719 -0.0229 -0.0237 -0.0038 151 VAL   B C   
6346 O O   . VAL   B 151 ? 0.1476 0.1272 0.1853 -0.0256 -0.0197 -0.0119 151 VAL   B O   
6347 C CB  . VAL   B 151 ? 0.1625 0.1468 0.1664 -0.0024 -0.0204 -0.0016 151 VAL   B CB  
6348 C CG1 . VAL   B 151 ? 0.1717 0.1484 0.1874 -0.0148 -0.0080 -0.0144 151 VAL   B CG1 
6349 C CG2 . VAL   B 151 ? 0.1728 0.1539 0.1686 0.0045  -0.0153 0.0111  151 VAL   B CG2 
6359 N N   . TYR   B 152 ? 0.1374 0.1117 0.1594 -0.0217 -0.0202 -0.0014 152 TYR   B N   
6360 C CA  . TYR   B 152 ? 0.1396 0.1225 0.1548 -0.0210 -0.0187 -0.0094 152 TYR   B CA  
6361 C C   . TYR   B 152 ? 0.1334 0.1128 0.1452 -0.0202 -0.0164 -0.0114 152 TYR   B C   
6362 O O   . TYR   B 152 ? 0.1462 0.1178 0.1497 -0.0221 -0.0133 0.0007  152 TYR   B O   
6363 C CB  . TYR   B 152 ? 0.1494 0.1361 0.1607 -0.0195 -0.0136 0.0063  152 TYR   B CB  
6364 C CG  . TYR   B 152 ? 0.1636 0.1439 0.1527 -0.0267 -0.0184 0.0059  152 TYR   B CG  
6365 C CD1 . TYR   B 152 ? 0.1739 0.1557 0.1449 -0.0216 -0.0264 0.0058  152 TYR   B CD1 
6366 C CD2 . TYR   B 152 ? 0.1875 0.1591 0.1524 -0.0283 -0.0109 0.0033  152 TYR   B CD2 
6367 C CE1 . TYR   B 152 ? 0.1925 0.1748 0.1532 -0.0169 -0.0276 0.0160  152 TYR   B CE1 
6368 C CE2 . TYR   B 152 ? 0.1981 0.1795 0.1493 -0.0284 -0.0221 -0.0043 152 TYR   B CE2 
6369 C CZ  . TYR   B 152 ? 0.2018 0.1934 0.1379 -0.0250 -0.0401 0.0153  152 TYR   B CZ  
6370 O OH  . TYR   B 152 ? 0.2255 0.2262 0.1785 -0.0120 -0.0407 0.0184  152 TYR   B OH  
6380 N N   . LEU   B 153 ? 0.1320 0.1142 0.1610 -0.0188 -0.0195 -0.0104 153 LEU   B N   
6381 C CA  . LEU   B 153 ? 0.1386 0.1079 0.1368 -0.0143 -0.0122 -0.0126 153 LEU   B CA  
6382 C C   . LEU   B 153 ? 0.1407 0.1050 0.1458 -0.0168 -0.0109 -0.0139 153 LEU   B C   
6383 O O   . LEU   B 153 ? 0.1462 0.1238 0.1611 -0.0117 -0.0100 -0.0247 153 LEU   B O   
6384 C CB  . LEU   B 153 ? 0.1453 0.1109 0.1595 -0.0166 -0.0032 -0.0097 153 LEU   B CB  
6385 C CG  . LEU   B 153 ? 0.1435 0.1195 0.1780 -0.0221 -0.0059 0.0024  153 LEU   B CG  
6386 C CD1 . LEU   B 153 ? 0.1474 0.1312 0.1842 -0.0270 0.0011  0.0082  153 LEU   B CD1 
6387 C CD2 . LEU   B 153 ? 0.1467 0.1369 0.1908 -0.0188 0.0039  0.0046  153 LEU   B CD2 
6399 N N   . ALA   B 154 ? 0.1359 0.1092 0.1536 -0.0050 -0.0123 -0.0104 154 ALA   B N   
6400 C CA  . ALA   B 154 ? 0.1483 0.1221 0.1709 0.0017  -0.0127 -0.0195 154 ALA   B CA  
6401 C C   . ALA   B 154 ? 0.1592 0.1238 0.1744 0.0014  -0.0249 -0.0228 154 ALA   B C   
6402 O O   . ALA   B 154 ? 0.1879 0.1238 0.1991 0.0014  -0.0132 -0.0112 154 ALA   B O   
6403 C CB  . ALA   B 154 ? 0.1424 0.1368 0.2052 -0.0007 -0.0103 -0.0257 154 ALA   B CB  
6409 N N   . VAL   B 155 ? 0.1334 0.1133 0.1833 -0.0026 -0.0068 -0.0101 155 VAL   B N   
6410 C CA  . VAL   B 155 ? 0.1235 0.1168 0.1965 -0.0036 -0.0121 -0.0042 155 VAL   B CA  
6411 C C   . VAL   B 155 ? 0.1268 0.1202 0.1865 -0.0028 -0.0189 -0.0122 155 VAL   B C   
6412 O O   . VAL   B 155 ? 0.1455 0.1383 0.2149 0.0033  -0.0134 -0.0298 155 VAL   B O   
6413 C CB  . VAL   B 155 ? 0.1307 0.1351 0.2373 -0.0090 -0.0182 0.0073  155 VAL   B CB  
6414 C CG1 . VAL   B 155 ? 0.1314 0.1271 0.2456 -0.0112 -0.0166 0.0046  155 VAL   B CG1 
6415 C CG2 . VAL   B 155 ? 0.1234 0.1417 0.2625 -0.0055 -0.0125 0.0397  155 VAL   B CG2 
6425 N N   . PHE   B 156 ? 0.1223 0.1273 0.1983 0.0037  -0.0152 -0.0097 156 PHE   B N   
6426 C CA  . PHE   B 156 ? 0.1226 0.1336 0.2358 0.0094  -0.0120 -0.0094 156 PHE   B CA  
6427 C C   . PHE   B 156 ? 0.1244 0.1351 0.2689 0.0126  -0.0162 -0.0238 156 PHE   B C   
6428 O O   . PHE   B 156 ? 0.1429 0.1557 0.2964 0.0281  -0.0056 -0.0346 156 PHE   B O   
6429 C CB  . PHE   B 156 ? 0.1322 0.1299 0.2344 0.0058  -0.0207 -0.0018 156 PHE   B CB  
6430 C CG  . PHE   B 156 ? 0.1312 0.1448 0.2424 -0.0006 -0.0164 0.0123  156 PHE   B CG  
6431 C CD1 . PHE   B 156 ? 0.1384 0.1735 0.2827 0.0028  -0.0133 0.0490  156 PHE   B CD1 
6432 C CD2 . PHE   B 156 ? 0.1345 0.1592 0.2287 0.0102  -0.0168 0.0140  156 PHE   B CD2 
6433 C CE1 . PHE   B 156 ? 0.1403 0.1904 0.2983 0.0003  -0.0031 0.0478  156 PHE   B CE1 
6434 C CE2 . PHE   B 156 ? 0.1437 0.1784 0.2579 0.0113  -0.0189 0.0187  156 PHE   B CE2 
6435 C CZ  . PHE   B 156 ? 0.1359 0.1897 0.2893 0.0153  -0.0174 0.0286  156 PHE   B CZ  
6445 N N   . ASP   B 157 ? 0.1253 0.1255 0.2843 0.0120  -0.0174 -0.0075 157 ASP   B N   
6446 C CA  . ASP   B 157 ? 0.1326 0.1329 0.3159 0.0070  -0.0285 -0.0113 157 ASP   B CA  
6447 C C   . ASP   B 157 ? 0.1361 0.1287 0.3226 0.0122  -0.0197 -0.0317 157 ASP   B C   
6448 O O   . ASP   B 157 ? 0.1294 0.1346 0.3009 0.0087  -0.0139 -0.0264 157 ASP   B O   
6449 C CB  . ASP   B 157 ? 0.1533 0.1560 0.3228 -0.0031 -0.0486 0.0007  157 ASP   B CB  
6450 C CG  . ASP   B 157 ? 0.1879 0.1706 0.3446 -0.0025 -0.0360 -0.0053 157 ASP   B CG  
6451 O OD1 . ASP   B 157 ? 0.2012 0.1621 0.3590 0.0072  -0.0276 -0.0064 157 ASP   B OD1 
6452 O OD2 . ASP   B 157 ? 0.2148 0.1889 0.3685 -0.0047 -0.0136 -0.0061 157 ASP   B OD2 
6457 N N   . LYS   B 158 ? 0.1328 0.1558 0.3319 0.0071  -0.0099 -0.0466 158 LYS   B N   
6458 C CA  . LYS   B 158 ? 0.1504 0.1711 0.3382 0.0041  -0.0012 -0.0708 158 LYS   B CA  
6459 C C   . LYS   B 158 ? 0.1487 0.1575 0.3329 0.0068  -0.0018 -0.0669 158 LYS   B C   
6460 O O   . LYS   B 158 ? 0.1520 0.1628 0.3381 -0.0054 -0.0053 -0.0701 158 LYS   B O   
6461 C CB  . LYS   B 158 ? 0.1732 0.2073 0.3503 0.0005  0.0132  -0.0872 158 LYS   B CB  
6462 C CG  . LYS   B 158 ? 0.2028 0.2422 0.3593 0.0039  0.0227  -0.0977 158 LYS   B CG  
6463 C CD  . LYS   B 158 ? 0.2293 0.2798 0.3757 0.0024  0.0313  -0.0981 158 LYS   B CD  
6464 C CE  . LYS   B 158 ? 0.2503 0.3069 0.3940 0.0061  0.0332  -0.0967 158 LYS   B CE  
6465 N NZ  . LYS   B 158 ? 0.2461 0.3125 0.3959 0.0005  0.0375  -0.0966 158 LYS   B NZ  
6479 N N   . ASN   B 159 ? 0.1533 0.1450 0.3371 0.0106  -0.0093 -0.0549 159 ASN   B N   
6480 C CA  . ASN   B 159 ? 0.1676 0.1417 0.3510 0.0130  -0.0298 -0.0374 159 ASN   B CA  
6481 C C   . ASN   B 159 ? 0.1552 0.1319 0.3419 0.0133  -0.0381 -0.0306 159 ASN   B C   
6482 O O   . ASN   B 159 ? 0.1577 0.1280 0.3530 -0.0014 -0.0377 -0.0263 159 ASN   B O   
6483 C CB  . ASN   B 159 ? 0.1859 0.1518 0.3858 0.0233  -0.0291 -0.0271 159 ASN   B CB  
6484 C CG  . ASN   B 159 ? 0.2127 0.1731 0.4201 0.0233  -0.0335 -0.0478 159 ASN   B CG  
6485 O OD1 . ASN   B 159 ? 0.2316 0.1831 0.4325 0.0272  -0.0333 -0.0671 159 ASN   B OD1 
6486 N ND2 . ASN   B 159 ? 0.2117 0.1859 0.4338 0.0254  -0.0341 -0.0395 159 ASN   B ND2 
6493 N N   . LEU   B 160 ? 0.1481 0.1304 0.3182 0.0040  -0.0376 -0.0264 160 LEU   B N   
6494 C CA  . LEU   B 160 ? 0.1421 0.1318 0.2911 0.0067  -0.0376 -0.0108 160 LEU   B CA  
6495 C C   . LEU   B 160 ? 0.1372 0.1250 0.2755 0.0039  -0.0237 -0.0215 160 LEU   B C   
6496 O O   . LEU   B 160 ? 0.1268 0.1312 0.2652 -0.0038 -0.0245 -0.0190 160 LEU   B O   
6497 C CB  . LEU   B 160 ? 0.1425 0.1406 0.2788 0.0021  -0.0367 -0.0047 160 LEU   B CB  
6498 C CG  . LEU   B 160 ? 0.1476 0.1517 0.2646 0.0095  -0.0315 -0.0001 160 LEU   B CG  
6499 C CD1 . LEU   B 160 ? 0.1548 0.1704 0.2719 0.0005  -0.0122 0.0023  160 LEU   B CD1 
6500 C CD2 . LEU   B 160 ? 0.1506 0.1549 0.2638 0.0112  -0.0339 -0.0127 160 LEU   B CD2 
6512 N N   . TYR   B 161 ? 0.1304 0.1319 0.2734 -0.0032 -0.0079 -0.0321 161 TYR   B N   
6513 C CA  . TYR   B 161 ? 0.1366 0.1303 0.2631 -0.0124 0.0070  -0.0306 161 TYR   B CA  
6514 C C   . TYR   B 161 ? 0.1454 0.1320 0.2597 -0.0102 0.0088  -0.0333 161 TYR   B C   
6515 O O   . TYR   B 161 ? 0.1495 0.1281 0.2539 -0.0121 -0.0030 -0.0355 161 TYR   B O   
6516 C CB  . TYR   B 161 ? 0.1530 0.1387 0.2627 -0.0184 0.0216  -0.0445 161 TYR   B CB  
6517 C CG  . TYR   B 161 ? 0.1791 0.1435 0.2555 -0.0201 0.0259  -0.0518 161 TYR   B CG  
6518 C CD1 . TYR   B 161 ? 0.1853 0.1424 0.2612 -0.0332 0.0315  -0.0472 161 TYR   B CD1 
6519 C CD2 . TYR   B 161 ? 0.1975 0.1493 0.2570 -0.0208 0.0161  -0.0468 161 TYR   B CD2 
6520 C CE1 . TYR   B 161 ? 0.2035 0.1573 0.2695 -0.0304 0.0294  -0.0419 161 TYR   B CE1 
6521 C CE2 . TYR   B 161 ? 0.2187 0.1649 0.2712 -0.0257 0.0218  -0.0423 161 TYR   B CE2 
6522 C CZ  . TYR   B 161 ? 0.2158 0.1669 0.2669 -0.0367 0.0248  -0.0316 161 TYR   B CZ  
6523 O OH  . TYR   B 161 ? 0.2444 0.1876 0.2924 -0.0358 0.0209  -0.0259 161 TYR   B OH  
6533 N N   . ASP   B 162 ? 0.1492 0.1297 0.2819 -0.0057 -0.0020 -0.0450 162 ASP   B N   
6534 C CA  . ASP   B 162 ? 0.1596 0.1341 0.2840 -0.0028 -0.0065 -0.0471 162 ASP   B CA  
6535 C C   . ASP   B 162 ? 0.1550 0.1259 0.2687 -0.0088 -0.0161 -0.0422 162 ASP   B C   
6536 O O   . ASP   B 162 ? 0.1604 0.1339 0.2660 -0.0110 -0.0242 -0.0388 162 ASP   B O   
6537 C CB  . ASP   B 162 ? 0.1726 0.1483 0.3074 0.0074  -0.0077 -0.0674 162 ASP   B CB  
6538 C CG  . ASP   B 162 ? 0.1757 0.1774 0.3283 0.0092  -0.0057 -0.0766 162 ASP   B CG  
6539 O OD1 . ASP   B 162 ? 0.1722 0.1972 0.3141 0.0028  0.0004  -0.0716 162 ASP   B OD1 
6540 O OD2 . ASP   B 162 ? 0.1886 0.2006 0.3637 0.0213  0.0012  -0.0760 162 ASP   B OD2 
6545 N N   A LYS   B 163 ? 0.1548 0.1261 0.2638 -0.0090 -0.0216 -0.0324 163 LYS   B N   
6546 N N   B LYS   B 163 ? 0.1518 0.1208 0.2610 -0.0086 -0.0231 -0.0312 163 LYS   B N   
6547 C CA  A LYS   B 163 ? 0.1630 0.1380 0.2712 -0.0130 -0.0211 -0.0168 163 LYS   B CA  
6548 C CA  B LYS   B 163 ? 0.1579 0.1290 0.2663 -0.0132 -0.0241 -0.0136 163 LYS   B CA  
6549 C C   A LYS   B 163 ? 0.1390 0.1277 0.2571 -0.0138 -0.0213 -0.0124 163 LYS   B C   
6550 C C   B LYS   B 163 ? 0.1357 0.1231 0.2558 -0.0136 -0.0226 -0.0081 163 LYS   B C   
6551 O O   A LYS   B 163 ? 0.1406 0.1334 0.2728 -0.0168 -0.0219 -0.0144 163 LYS   B O   
6552 O O   B LYS   B 163 ? 0.1370 0.1304 0.2764 -0.0152 -0.0226 -0.0055 163 LYS   B O   
6553 C CB  A LYS   B 163 ? 0.1969 0.1684 0.3063 -0.0086 -0.0240 -0.0017 163 LYS   B CB  
6554 C CB  B LYS   B 163 ? 0.1889 0.1544 0.2976 -0.0074 -0.0295 0.0043  163 LYS   B CB  
6555 C CG  A LYS   B 163 ? 0.2405 0.2160 0.3477 -0.0081 -0.0188 0.0027  163 LYS   B CG  
6556 C CG  B LYS   B 163 ? 0.2334 0.2037 0.3371 -0.0071 -0.0249 0.0079  163 LYS   B CG  
6557 C CD  A LYS   B 163 ? 0.2804 0.2558 0.3906 -0.0117 -0.0131 -0.0062 163 LYS   B CD  
6558 C CD  B LYS   B 163 ? 0.2759 0.2479 0.3833 -0.0114 -0.0184 -0.0019 163 LYS   B CD  
6559 C CE  A LYS   B 163 ? 0.3079 0.2835 0.4171 -0.0150 -0.0077 -0.0088 163 LYS   B CE  
6560 C CE  B LYS   B 163 ? 0.3064 0.2778 0.4144 -0.0165 -0.0114 -0.0070 163 LYS   B CE  
6561 N NZ  A LYS   B 163 ? 0.3209 0.2942 0.4370 -0.0176 -0.0060 -0.0128 163 LYS   B NZ  
6562 N NZ  B LYS   B 163 ? 0.3208 0.2891 0.4356 -0.0197 -0.0090 -0.0128 163 LYS   B NZ  
6589 N N   . LEU   B 164 ? 0.1218 0.1184 0.2499 -0.0139 -0.0217 -0.0059 164 LEU   B N   
6590 C CA  . LEU   B 164 ? 0.1288 0.1193 0.2318 -0.0071 -0.0223 -0.0089 164 LEU   B CA  
6591 C C   . LEU   B 164 ? 0.1352 0.1214 0.2273 -0.0110 -0.0283 -0.0060 164 LEU   B C   
6592 O O   . LEU   B 164 ? 0.1298 0.1459 0.2498 -0.0098 -0.0307 -0.0118 164 LEU   B O   
6593 C CB  . LEU   B 164 ? 0.1256 0.1183 0.2173 -0.0106 -0.0162 -0.0132 164 LEU   B CB  
6594 C CG  . LEU   B 164 ? 0.1326 0.1329 0.2271 -0.0130 -0.0103 -0.0027 164 LEU   B CG  
6595 C CD1 . LEU   B 164 ? 0.1430 0.1314 0.2340 -0.0137 -0.0246 -0.0140 164 LEU   B CD1 
6596 C CD2 . LEU   B 164 ? 0.1529 0.1713 0.2383 -0.0126 0.0039  -0.0193 164 LEU   B CD2 
6609 N N   . VAL   B 165 ? 0.1600 0.1253 0.2387 -0.0146 -0.0293 -0.0157 165 VAL   B N   
6610 C CA  . VAL   B 165 ? 0.1876 0.1380 0.2441 -0.0201 -0.0422 -0.0110 165 VAL   B CA  
6611 C C   . VAL   B 165 ? 0.2094 0.1483 0.2600 -0.0329 -0.0652 -0.0125 165 VAL   B C   
6612 O O   . VAL   B 165 ? 0.2224 0.1618 0.2654 -0.0385 -0.0680 -0.0026 165 VAL   B O   
6613 C CB  . VAL   B 165 ? 0.2104 0.1542 0.2353 -0.0019 -0.0158 -0.0192 165 VAL   B CB  
6614 C CG1 . VAL   B 165 ? 0.2295 0.1641 0.2624 -0.0055 -0.0139 -0.0143 165 VAL   B CG1 
6615 C CG2 . VAL   B 165 ? 0.2068 0.1506 0.2297 -0.0022 -0.0079 -0.0179 165 VAL   B CG2 
6625 N N   . SER   B 166 ? 0.2149 0.1420 0.2831 -0.0281 -0.0692 -0.0269 166 SER   B N   
6626 C CA  . SER   B 166 ? 0.2120 0.1435 0.3289 -0.0326 -0.0635 -0.0299 166 SER   B CA  
6627 C C   . SER   B 166 ? 0.2019 0.1476 0.3410 -0.0358 -0.0632 -0.0119 166 SER   B C   
6628 O O   . SER   B 166 ? 0.2046 0.1715 0.3693 -0.0462 -0.0721 -0.0305 166 SER   B O   
6629 C CB  . SER   B 166 ? 0.2131 0.1478 0.3464 -0.0263 -0.0562 -0.0410 166 SER   B CB  
6630 O OG  . SER   B 166 ? 0.1993 0.1408 0.3588 -0.0205 -0.0601 -0.0219 166 SER   B OG  
6636 N N   . SER   B 167 ? 0.1870 0.1470 0.3159 -0.0360 -0.0622 0.0264  167 SER   B N   
6637 C CA  . SER   B 167 ? 0.1781 0.1515 0.3034 -0.0362 -0.0447 0.0213  167 SER   B CA  
6638 C C   . SER   B 167 ? 0.1708 0.1588 0.2899 -0.0415 -0.0464 0.0336  167 SER   B C   
6639 O O   . SER   B 167 ? 0.1722 0.1627 0.2961 -0.0384 -0.0425 0.0314  167 SER   B O   
6640 C CB  . SER   B 167 ? 0.1716 0.1590 0.3032 -0.0321 -0.0243 0.0192  167 SER   B CB  
6641 O OG  . SER   B 167 ? 0.1677 0.1665 0.2899 -0.0187 -0.0162 0.0221  167 SER   B OG  
6647 N N   . PHE   B 168 ? 0.1729 0.1627 0.2836 -0.0318 -0.0431 0.0419  168 PHE   B N   
6648 C CA  . PHE   B 168 ? 0.1795 0.1572 0.2676 -0.0359 -0.0416 0.0265  168 PHE   B CA  
6649 C C   . PHE   B 168 ? 0.1539 0.1477 0.2210 -0.0131 -0.0133 0.0133  168 PHE   B C   
6650 O O   . PHE   B 168 ? 0.1803 0.1382 0.2324 0.0047  -0.0179 -0.0020 168 PHE   B O   
6651 C CB  . PHE   B 168 ? 0.2011 0.1597 0.2794 -0.0532 -0.0570 0.0393  168 PHE   B CB  
6652 C CG  . PHE   B 168 ? 0.2298 0.1461 0.2769 -0.0533 -0.0623 0.0190  168 PHE   B CG  
6653 C CD1 . PHE   B 168 ? 0.2644 0.1527 0.2850 -0.0448 -0.0719 0.0082  168 PHE   B CD1 
6654 C CD2 . PHE   B 168 ? 0.2180 0.1408 0.2801 -0.0468 -0.0685 0.0176  168 PHE   B CD2 
6655 C CE1 . PHE   B 168 ? 0.2799 0.1590 0.2859 -0.0330 -0.0637 0.0122  168 PHE   B CE1 
6656 C CE2 . PHE   B 168 ? 0.2496 0.1467 0.2716 -0.0319 -0.0715 0.0149  168 PHE   B CE2 
6657 C CZ  . PHE   B 168 ? 0.2709 0.1449 0.2771 -0.0236 -0.0727 0.0183  168 PHE   B CZ  
6667 N N   . LEU   B 169 ? 0.1563 0.1598 0.2198 0.0023  0.0030  -0.0015 169 LEU   B N   
6668 C CA  . LEU   B 169 ? 0.1763 0.1907 0.2579 -0.0060 0.0027  -0.0246 169 LEU   B CA  
6669 C C   . LEU   B 169 ? 0.2009 0.2132 0.3098 0.0047  -0.0034 -0.0464 169 LEU   B C   
6670 O O   . LEU   B 169 ? 0.2212 0.2354 0.3661 0.0017  -0.0116 -0.0730 169 LEU   B O   
6671 C CB  . LEU   B 169 ? 0.1922 0.2315 0.2768 -0.0165 -0.0056 -0.0026 169 LEU   B CB  
6672 C CG  . LEU   B 169 ? 0.2308 0.2721 0.3239 -0.0055 -0.0014 0.0050  169 LEU   B CG  
6673 C CD1 . LEU   B 169 ? 0.2467 0.2962 0.3307 -0.0059 -0.0039 0.0226  169 LEU   B CD1 
6674 C CD2 . LEU   B 169 ? 0.2208 0.2766 0.3261 0.0100  0.0235  -0.0109 169 LEU   B CD2 
6675 O OXT . LEU   B 169 ? 0.2225 0.2235 0.3015 0.0311  -0.0029 -0.0452 169 LEU   B OXT 
6687 S S   B DMS   C .   ? 0.2090 0.1739 0.2966 -0.0062 -0.0171 -0.0213 301 DMS   A S   
6688 O O   B DMS   C .   ? 0.1984 0.1452 0.2473 0.0050  -0.0228 -0.0271 301 DMS   A O   
6689 C C1  B DMS   C .   ? 0.2066 0.1696 0.2984 -0.0080 -0.0301 -0.0277 301 DMS   A C1  
6690 C C2  B DMS   C .   ? 0.2078 0.1771 0.2928 0.0006  -0.0194 -0.0183 301 DMS   A C2  
6697 S S   B DMS   D .   ? 0.3384 0.3427 0.4392 0.0402  -0.0539 -0.1107 302 DMS   A S   
6698 O O   B DMS   D .   ? 0.3375 0.3447 0.4360 0.0363  -0.0512 -0.1083 302 DMS   A O   
6699 C C1  B DMS   D .   ? 0.3410 0.3465 0.4359 0.0374  -0.0519 -0.1087 302 DMS   A C1  
6700 C C2  B DMS   D .   ? 0.3362 0.3380 0.4178 0.0386  -0.0515 -0.1157 302 DMS   A C2  
6707 N N2  B A1A9E E .   ? 0.1178 0.1090 0.1110 0.0059  0.0058  0.0028  303 A1A9E A N2  
6708 C C3  B A1A9E E .   ? 0.1923 0.1238 0.1309 0.0242  0.0001  0.0192  303 A1A9E A C3  
6709 C C6  B A1A9E E .   ? 0.1259 0.1090 0.1076 0.0072  0.0057  0.0137  303 A1A9E A C6  
6710 C C9  B A1A9E E .   ? 0.1168 0.1154 0.1003 0.0078  0.0192  0.0157  303 A1A9E A C9  
6711 C C12 B A1A9E E .   ? 0.1911 0.1012 0.1359 0.0159  0.0067  0.0147  303 A1A9E A C12 
6712 C C1  B A1A9E E .   ? 0.2337 0.1602 0.1454 0.0402  -0.0360 0.0088  303 A1A9E A C1  
6713 C C10 B A1A9E E .   ? 0.1313 0.1222 0.1216 0.0002  0.0208  0.0221  303 A1A9E A C10 
6714 C C11 B A1A9E E .   ? 0.1223 0.1165 0.1282 -0.0030 0.0198  0.0139  303 A1A9E A C11 
6715 C C2  B A1A9E E .   ? 0.2048 0.1229 0.1449 0.0265  0.0017  0.0168  303 A1A9E A C2  
6716 C C4  B A1A9E E .   ? 0.1701 0.1177 0.1254 0.0221  0.0035  0.0055  303 A1A9E A C4  
6717 C C5  B A1A9E E .   ? 0.1459 0.1373 0.1252 0.0282  0.0073  -0.0185 303 A1A9E A C5  
6718 C C7  B A1A9E E .   ? 0.1215 0.1183 0.1053 0.0105  0.0164  0.0091  303 A1A9E A C7  
6719 C C8  B A1A9E E .   ? 0.1224 0.1185 0.0985 0.0006  0.0203  0.0111  303 A1A9E A C8  
6720 N N1  B A1A9E E .   ? 0.1639 0.1002 0.1291 0.0100  -0.0022 0.0172  303 A1A9E A N1  
6721 N N3  B A1A9E E .   ? 0.1274 0.1224 0.1066 0.0044  0.0180  0.0169  303 A1A9E A N3  
6722 N N4  B A1A9E E .   ? 0.1271 0.1159 0.1245 -0.0043 0.0150  0.0161  303 A1A9E A N4  
6723 O O1  B A1A9E E .   ? 0.2224 0.1418 0.1371 0.0336  -0.0218 0.0145  303 A1A9E A O1  
6724 O O2  B A1A9E E .   ? 0.1408 0.1423 0.1449 0.0237  0.0077  0.0040  303 A1A9E A O2  
6741 O O   . HOH   F .   ? 0.3194 0.3053 0.4709 0.0327  -0.1321 0.0033  401 HOH   A O   
6742 O O   . HOH   F .   ? 0.4154 0.7859 0.5722 -0.1350 0.0670  0.1033  402 HOH   A O   
6743 O O   A HOH   F .   ? 0.2549 0.2841 0.2708 0.0336  0.0549  0.0142  403 HOH   A O   
6744 O O   . HOH   F .   ? 0.3192 0.3556 0.3557 -0.1036 0.0027  -0.0849 404 HOH   A O   
6745 O O   A HOH   F .   ? 0.2925 0.1136 0.3341 0.0104  -0.0725 0.0314  405 HOH   A O   
6746 O O   . HOH   F .   ? 0.1895 0.3673 0.3344 -0.0322 0.0354  -0.1363 406 HOH   A O   
6747 O O   . HOH   F .   ? 0.5787 0.5154 0.6114 -0.0005 0.0555  -0.0324 407 HOH   A O   
6748 O O   . HOH   F .   ? 0.6175 0.4207 0.3008 0.2132  -0.0826 0.0426  408 HOH   A O   
6749 O O   A HOH   F .   ? 0.2936 0.3297 0.4486 0.0593  -0.0670 -0.0703 409 HOH   A O   
6750 O O   . HOH   F .   ? 0.2808 0.3219 0.2842 0.0038  0.0070  -0.0768 410 HOH   A O   
6751 O O   . HOH   F .   ? 0.5117 0.1847 0.6036 0.0284  0.0910  -0.0196 411 HOH   A O   
6752 O O   . HOH   F .   ? 0.3710 0.5274 0.3454 0.1303  0.0843  -0.0922 412 HOH   A O   
6753 O O   . HOH   F .   ? 0.4499 0.3852 0.3880 -0.0521 0.0824  0.1226  413 HOH   A O   
6754 O O   B HOH   F .   ? 0.2825 0.1303 0.3257 -0.0025 -0.1707 0.0185  414 HOH   A O   
6755 O O   . HOH   F .   ? 0.6073 0.4608 0.3135 -0.0269 -0.0577 0.0696  415 HOH   A O   
6756 O O   . HOH   F .   ? 0.2035 0.1709 0.3808 -0.0451 0.0094  -0.0162 416 HOH   A O   
6757 O O   . HOH   F .   ? 0.3084 0.4117 0.3199 0.0318  0.0403  0.0325  417 HOH   A O   
6758 O O   A HOH   F .   ? 0.2057 0.2420 0.1044 -0.0210 0.0302  0.0263  418 HOH   A O   
6759 O O   . HOH   F .   ? 0.2450 0.2727 0.2725 -0.0400 0.0421  0.0639  419 HOH   A O   
6760 O O   . HOH   F .   ? 0.2107 0.1656 0.2442 0.0244  -0.0447 -0.0001 420 HOH   A O   
6761 O O   . HOH   F .   ? 0.6237 0.3759 0.3433 -0.0679 -0.0208 0.1133  421 HOH   A O   
6762 O O   . HOH   F .   ? 0.1602 0.1641 0.2581 -0.0222 0.0149  0.0245  422 HOH   A O   
6763 O O   A HOH   F .   ? 0.1385 0.1687 0.1847 0.0074  0.0273  0.0686  423 HOH   A O   
6764 O O   . HOH   F .   ? 0.1970 0.1770 0.2449 0.0272  -0.0207 0.0082  424 HOH   A O   
6765 O O   . HOH   F .   ? 0.4854 0.3669 0.5083 0.0674  0.2195  -0.0554 425 HOH   A O   
6766 O O   . HOH   F .   ? 0.1431 0.1395 0.2210 -0.0213 0.0093  -0.0162 426 HOH   A O   
6767 O O   B HOH   F .   ? 0.1794 0.1261 0.2023 0.0143  -0.0422 0.0174  427 HOH   A O   
6768 O O   . HOH   F .   ? 0.2425 0.2391 0.2467 -0.0654 -0.0222 -0.0242 428 HOH   A O   
6769 O O   . HOH   F .   ? 0.1682 0.3140 0.2947 0.0295  -0.0236 0.0023  429 HOH   A O   
6770 O O   . HOH   F .   ? 0.3924 0.3765 0.3467 -0.0199 0.1390  0.0535  430 HOH   A O   
6771 O O   . HOH   F .   ? 0.2438 0.2226 0.2652 0.0412  0.0223  0.0360  431 HOH   A O   
6772 O O   . HOH   F .   ? 0.2570 0.2516 0.2949 -0.0211 -0.0096 -0.0431 432 HOH   A O   
6773 O O   A HOH   F .   ? 0.2749 0.4300 0.2799 0.1419  -0.0364 -0.0894 433 HOH   A O   
6774 O O   . HOH   F .   ? 0.5023 0.1957 0.4060 0.0096  -0.1414 0.0455  434 HOH   A O   
6775 O O   . HOH   F .   ? 0.1812 0.2309 0.3202 -0.0040 0.0757  -0.0060 435 HOH   A O   
6776 O O   . HOH   F .   ? 0.2312 0.1867 0.2302 -0.0543 -0.0126 0.0467  436 HOH   A O   
6777 O O   A HOH   F .   ? 0.2885 0.2035 0.1952 0.0154  0.0165  -0.0437 437 HOH   A O   
6778 O O   . HOH   F .   ? 0.2214 0.4203 0.3543 0.1010  -0.0524 0.0207  438 HOH   A O   
6779 O O   . HOH   F .   ? 0.3290 0.3248 0.4368 -0.0813 -0.1223 -0.0216 439 HOH   A O   
6780 O O   A HOH   F .   ? 0.1519 0.3260 0.2083 0.0873  0.0624  0.1082  440 HOH   A O   
6781 O O   . HOH   F .   ? 0.3065 0.3197 0.2708 -0.0886 0.0931  0.0131  441 HOH   A O   
6782 O O   . HOH   F .   ? 0.5600 0.5034 0.3700 -0.0725 0.1442  0.1951  442 HOH   A O   
6783 O O   . HOH   F .   ? 0.6480 0.6804 0.4518 0.1181  -0.0845 0.0262  443 HOH   A O   
6784 O O   . HOH   F .   ? 0.1484 0.1755 0.2715 0.0162  -0.0460 -0.0699 444 HOH   A O   
6785 O O   B HOH   F .   ? 0.1958 0.1749 0.3062 -0.0040 -0.0920 0.0710  445 HOH   A O   
6786 O O   . HOH   F .   ? 0.4565 0.4540 0.4771 -0.0734 -0.1475 -0.0049 446 HOH   A O   
6787 O O   A HOH   F .   ? 0.3022 0.2778 0.2168 -0.0372 -0.0197 0.0045  447 HOH   A O   
6788 O O   . HOH   F .   ? 0.6646 0.3167 0.5341 -0.0824 -0.1383 -0.0197 448 HOH   A O   
6789 O O   . HOH   F .   ? 0.2086 0.4253 0.2691 0.0180  0.0002  -0.0748 449 HOH   A O   
6790 O O   . HOH   F .   ? 0.3848 0.7914 0.3508 0.1407  -0.0161 0.2151  450 HOH   A O   
6791 O O   . HOH   F .   ? 0.1405 0.2156 0.2220 0.0033  -0.0076 0.0420  451 HOH   A O   
6792 O O   B HOH   F .   ? 0.2376 0.3972 0.3021 -0.0647 -0.0648 0.0152  452 HOH   A O   
6793 O O   . HOH   F .   ? 0.4977 0.5088 0.3186 -0.1141 0.1428  0.0551  453 HOH   A O   
6794 O O   . HOH   F .   ? 0.3678 0.6671 0.4567 -0.0246 -0.1234 0.0126  454 HOH   A O   
6795 O O   . HOH   F .   ? 0.7104 0.5345 0.4679 -0.1876 -0.1049 0.2547  455 HOH   A O   
6796 O O   . HOH   F .   ? 0.3858 0.2685 0.4386 -0.1476 0.1331  -0.0559 456 HOH   A O   
6797 O O   . HOH   F .   ? 0.3782 0.3227 0.2252 -0.0684 -0.0218 -0.1029 457 HOH   A O   
6798 O O   A HOH   F .   ? 0.2518 0.2616 0.3993 0.0915  0.0823  0.1196  458 HOH   A O   
6799 O O   . HOH   F .   ? 0.2074 0.4386 0.3574 0.0042  -0.0458 0.1318  459 HOH   A O   
6800 O O   . HOH   F .   ? 0.2470 0.3647 0.2868 0.0218  0.0715  0.1384  460 HOH   A O   
6801 O O   . HOH   F .   ? 0.3151 0.3254 0.5551 -0.0792 -0.1298 -0.1152 461 HOH   A O   
6802 O O   . HOH   F .   ? 0.1860 0.1911 0.3699 0.0144  0.0862  -0.0252 462 HOH   A O   
6803 O O   B HOH   F .   ? 0.1940 0.1434 0.1850 0.0186  -0.0466 -0.0032 463 HOH   A O   
6804 O O   . HOH   F .   ? 0.3383 0.1804 0.2284 0.0904  0.0452  -0.0016 464 HOH   A O   
6805 O O   . HOH   F .   ? 0.2634 0.4662 0.3559 -0.0602 0.0802  -0.0584 465 HOH   A O   
6806 O O   . HOH   F .   ? 0.3824 0.2337 0.4690 -0.0889 -0.0137 -0.0073 466 HOH   A O   
6807 O O   . HOH   F .   ? 0.1482 0.1796 0.2476 0.0118  -0.0103 0.0010  467 HOH   A O   
6808 O O   . HOH   F .   ? 0.1323 0.1421 0.2039 -0.0005 -0.0159 -0.0018 468 HOH   A O   
6809 O O   . HOH   F .   ? 0.1224 0.1184 0.1307 -0.0024 0.0074  0.0035  469 HOH   A O   
6810 O O   . HOH   F .   ? 0.1799 0.3341 0.3690 0.0416  0.0308  -0.1451 470 HOH   A O   
6811 O O   . HOH   F .   ? 0.1423 0.1171 0.2137 -0.0057 0.0207  -0.0102 471 HOH   A O   
6812 O O   . HOH   F .   ? 0.3496 0.3501 0.3385 0.1514  0.0600  0.0475  472 HOH   A O   
6813 O O   . HOH   F .   ? 0.1826 0.1756 0.2210 -0.0322 0.0071  0.0286  473 HOH   A O   
6814 O O   . HOH   F .   ? 0.2529 0.1705 0.2794 -0.0118 0.0145  0.0340  474 HOH   A O   
6815 O O   . HOH   F .   ? 0.2897 0.5077 0.2136 0.0937  -0.0686 -0.0607 475 HOH   A O   
6816 O O   . HOH   F .   ? 0.1354 0.1473 0.1471 -0.0088 -0.0049 -0.0114 476 HOH   A O   
6817 O O   . HOH   F .   ? 0.3978 0.2160 0.4060 -0.1093 0.1017  0.0258  477 HOH   A O   
6818 O O   . HOH   F .   ? 0.2839 0.2893 0.1941 0.0218  0.0659  -0.0007 478 HOH   A O   
6819 O O   . HOH   F .   ? 0.2068 0.3411 0.2999 -0.0213 -0.0047 -0.0151 479 HOH   A O   
6820 O O   . HOH   F .   ? 0.2126 0.1991 0.3132 0.0049  0.0148  0.0418  480 HOH   A O   
6821 O O   . HOH   F .   ? 0.2593 0.1979 0.1873 -0.0701 0.0328  0.0189  481 HOH   A O   
6822 O O   A HOH   F .   ? 0.2515 0.5757 0.3478 -0.0298 -0.0234 0.1544  482 HOH   A O   
6823 O O   . HOH   F .   ? 0.5067 0.5319 0.5449 -0.1121 0.0878  -0.0039 483 HOH   A O   
6824 O O   . HOH   F .   ? 0.2031 0.2320 0.2165 -0.0379 -0.0217 0.0259  484 HOH   A O   
6825 O O   . HOH   F .   ? 0.4753 0.4976 0.5196 -0.1043 -0.0564 0.0980  485 HOH   A O   
6826 O O   . HOH   F .   ? 0.3362 0.2556 0.3179 -0.0113 -0.0186 0.0935  486 HOH   A O   
6827 O O   . HOH   F .   ? 0.5933 0.5028 0.3693 -0.1562 -0.0380 0.1797  487 HOH   A O   
6828 O O   . HOH   F .   ? 0.4229 0.3537 0.1585 -0.0687 0.0758  0.0355  488 HOH   A O   
6829 O O   B HOH   F .   ? 0.1438 0.1246 0.1445 -0.0064 0.0137  0.0097  489 HOH   A O   
6830 O O   . HOH   F .   ? 0.3256 0.5744 0.3513 0.0585  0.1299  -0.0891 490 HOH   A O   
6831 O O   . HOH   F .   ? 0.2382 0.3794 0.3119 -0.0374 0.0991  -0.0857 491 HOH   A O   
6832 O O   . HOH   F .   ? 0.4457 0.6500 0.5730 0.2118  -0.0736 0.1192  492 HOH   A O   
6833 O O   A HOH   F .   ? 0.2130 0.1903 0.3320 -0.0016 -0.1018 0.0859  493 HOH   A O   
6834 O O   A HOH   F .   ? 0.2450 0.3618 0.3491 -0.1207 0.0155  -0.0500 494 HOH   A O   
6835 O O   B HOH   F .   ? 0.1527 0.1427 0.1125 0.0229  0.0082  0.0286  495 HOH   A O   
6836 O O   . HOH   F .   ? 0.1757 0.1809 0.1830 0.0022  0.0073  -0.0029 496 HOH   A O   
6837 O O   B HOH   F .   ? 0.1255 0.1750 0.2432 -0.0307 -0.0165 0.0496  497 HOH   A O   
6838 O O   . HOH   F .   ? 0.1574 0.1265 0.1604 -0.0153 0.0069  -0.0068 498 HOH   A O   
6839 O O   . HOH   F .   ? 0.1836 0.1809 0.3581 0.0367  0.1091  0.0908  499 HOH   A O   
6840 O O   . HOH   F .   ? 0.4936 0.2817 0.2873 -0.1147 0.0672  0.0400  500 HOH   A O   
6841 O O   A HOH   F .   ? 0.1513 0.1413 0.2104 0.0051  -0.0445 0.0326  501 HOH   A O   
6842 O O   A HOH   F .   ? 0.3254 0.3791 0.4270 -0.0536 -0.0946 0.0021  502 HOH   A O   
6843 O O   B HOH   F .   ? 0.1912 0.1524 0.3072 0.0083  0.0394  0.0190  503 HOH   A O   
6844 O O   . HOH   F .   ? 0.4432 0.5005 0.3795 0.0123  -0.1086 -0.0158 504 HOH   A O   
6845 O O   . HOH   F .   ? 0.1892 0.2643 0.3498 -0.0151 -0.0023 0.0238  505 HOH   A O   
6846 O O   A HOH   F .   ? 0.1563 0.1903 0.3167 0.0009  0.0032  -0.0615 506 HOH   A O   
6847 O O   B HOH   F .   ? 0.2772 0.1864 0.1400 -0.0351 -0.0107 0.0185  507 HOH   A O   
6848 O O   . HOH   F .   ? 0.4677 0.5176 0.4766 0.0578  -0.1145 -0.0857 508 HOH   A O   
6849 O O   A HOH   F .   ? 0.1368 0.1197 0.0924 -0.0017 0.0117  0.0057  509 HOH   A O   
6850 O O   . HOH   F .   ? 0.1542 0.1627 0.2031 0.0048  -0.0335 -0.0071 510 HOH   A O   
6851 O O   . HOH   F .   ? 0.7358 0.8403 0.6958 -0.0038 -0.0743 -0.1037 511 HOH   A O   
6852 O O   A HOH   F .   ? 0.4041 0.3542 0.3828 0.0782  0.0751  0.0206  512 HOH   A O   
6853 O O   A HOH   F .   ? 0.1364 0.1891 0.1785 -0.0175 -0.0157 0.1006  513 HOH   A O   
6854 O O   . HOH   F .   ? 0.2023 0.1733 0.3152 -0.0035 -0.0170 -0.0190 514 HOH   A O   
6855 O O   . HOH   F .   ? 0.2554 0.2442 0.5264 -0.0634 0.1234  -0.0969 515 HOH   A O   
6856 O O   . HOH   F .   ? 0.5831 0.3660 0.4116 0.1616  -0.1128 0.0999  516 HOH   A O   
6857 O O   . HOH   F .   ? 0.6092 0.5520 0.5809 -0.1018 -0.0513 -0.0941 517 HOH   A O   
6858 O O   . HOH   F .   ? 0.1897 0.1632 0.1405 0.0042  0.0219  0.0162  518 HOH   A O   
6859 O O   . HOH   F .   ? 0.4493 0.5589 0.2739 -0.0858 -0.0554 0.0708  519 HOH   A O   
6860 O O   . HOH   F .   ? 0.1959 0.2950 0.2559 -0.0020 -0.0354 0.0409  520 HOH   A O   
6861 O O   . HOH   F .   ? 0.3277 0.1167 0.2179 0.0142  -0.0726 0.0069  521 HOH   A O   
6862 O O   B HOH   F .   ? 0.2453 0.2636 0.1874 -0.0098 0.0747  0.0340  522 HOH   A O   
6863 O O   . HOH   F .   ? 0.5396 0.6361 0.4281 0.0543  0.2687  -0.0446 523 HOH   A O   
6864 O O   . HOH   F .   ? 0.1479 0.1560 0.3082 -0.0021 0.0029  -0.0031 524 HOH   A O   
6865 O O   . HOH   F .   ? 0.6390 0.3723 0.5359 -0.0743 0.0946  -0.1271 525 HOH   A O   
6866 O O   A HOH   F .   ? 0.1331 0.1725 0.1087 -0.0269 -0.0117 0.0568  526 HOH   A O   
6867 O O   . HOH   F .   ? 0.1613 0.2079 0.2790 -0.0348 0.0317  -0.0202 527 HOH   A O   
6868 O O   A HOH   F .   ? 0.2385 0.2384 0.1705 -0.0007 0.0252  -0.0048 528 HOH   A O   
6869 O O   . HOH   F .   ? 0.3281 0.3573 0.6956 -0.0069 0.0799  -0.0254 529 HOH   A O   
6870 O O   . HOH   F .   ? 0.2693 0.2595 0.1971 -0.0682 -0.0349 0.0074  530 HOH   A O   
6871 O O   . HOH   F .   ? 0.4243 0.2504 0.3887 0.0377  -0.0262 -0.0417 531 HOH   A O   
6872 O O   . HOH   F .   ? 0.3149 0.5574 0.1738 -0.0879 0.0631  -0.0221 532 HOH   A O   
6873 O O   . HOH   F .   ? 0.2228 0.4377 0.2385 0.1639  -0.0085 -0.0009 533 HOH   A O   
6874 O O   A HOH   F .   ? 0.2470 0.3347 0.2825 0.0474  0.0499  -0.0345 534 HOH   A O   
6875 O O   B HOH   F .   ? 0.3448 0.2517 0.2893 0.0388  0.0794  -0.0267 535 HOH   A O   
6876 O O   A HOH   F .   ? 0.0985 0.1841 0.2351 0.0071  0.0538  0.0508  536 HOH   A O   
6877 O O   . HOH   F .   ? 0.7500 0.5941 0.3962 -0.0315 -0.0245 0.2070  537 HOH   A O   
6878 O O   . HOH   F .   ? 0.2836 0.3075 0.2207 -0.0280 -0.0262 0.0598  538 HOH   A O   
6879 O O   B HOH   F .   ? 0.2720 0.3331 0.3360 0.0661  0.0268  0.0988  539 HOH   A O   
6880 O O   B HOH   F .   ? 0.4114 0.1900 0.2569 -0.0758 -0.0379 -0.0202 540 HOH   A O   
6881 O O   . HOH   F .   ? 0.5537 0.6438 0.5689 -0.0449 0.1457  0.1155  541 HOH   A O   
6882 O O   A HOH   F .   ? 0.2734 0.3522 0.3020 -0.0264 0.1376  0.0487  542 HOH   A O   
6883 O O   . HOH   F .   ? 0.1588 0.1587 0.2502 0.0124  -0.0435 0.0241  543 HOH   A O   
6884 O O   . HOH   F .   ? 0.4810 0.6109 0.4662 0.0522  -0.0799 0.1025  544 HOH   A O   
6885 O O   . HOH   F .   ? 0.4063 0.2342 0.5054 -0.0965 -0.2243 0.1239  545 HOH   A O   
6886 O O   . HOH   F .   ? 0.6382 0.7249 0.6372 0.1214  -0.1184 0.0217  546 HOH   A O   
6887 O O   . HOH   F .   ? 0.3886 0.2551 0.1652 -0.0774 0.0708  0.0458  547 HOH   A O   
6888 O O   . HOH   F .   ? 0.5143 0.4717 0.4844 -0.0532 -0.1261 -0.1309 548 HOH   A O   
6889 O O   . HOH   F .   ? 0.2260 0.1565 0.3026 -0.0071 0.0174  -0.0055 549 HOH   A O   
6890 O O   A HOH   F .   ? 0.1179 0.1218 0.1351 -0.0156 -0.0622 -0.0137 550 HOH   A O   
6891 O O   A HOH   F .   ? 0.7245 0.5343 0.5023 0.1909  0.0810  0.1085  551 HOH   A O   
6892 O O   . HOH   F .   ? 0.3732 0.5220 0.5783 0.0899  0.1769  -0.1568 552 HOH   A O   
6893 O O   . HOH   F .   ? 0.4261 0.4243 0.3830 0.2493  -0.0177 -0.0570 553 HOH   A O   
6894 O O   B HOH   F .   ? 0.1737 0.2070 0.2215 -0.0011 0.0052  0.0388  554 HOH   A O   
6895 O O   . HOH   F .   ? 0.2019 0.2439 0.2553 -0.0035 -0.0072 -0.0543 555 HOH   A O   
6896 O O   B HOH   F .   ? 0.1395 0.1121 0.2099 0.0287  -0.0693 -0.0231 556 HOH   A O   
6897 O O   B HOH   F .   ? 0.3150 0.2425 0.2649 0.0333  -0.1335 -0.0301 557 HOH   A O   
6898 O O   A HOH   F .   ? 0.0839 0.1090 0.1217 0.0209  -0.0259 0.0016  558 HOH   A O   
6899 O O   B HOH   F .   ? 0.5554 0.2175 0.3029 0.0627  -0.0839 -0.0215 559 HOH   A O   
6900 O O   . HOH   F .   ? 0.2329 0.1970 0.2817 0.0113  0.0093  0.0168  560 HOH   A O   
6901 O O   . HOH   F .   ? 0.5360 0.5267 0.7451 0.0792  -0.1147 0.1631  561 HOH   A O   
6902 O O   . HOH   F .   ? 0.5845 0.5430 0.6543 -0.1521 -0.0911 -0.1410 562 HOH   A O   
6903 O O   . HOH   F .   ? 0.6429 0.6937 0.4045 0.0778  0.0002  -0.0271 563 HOH   A O   
6904 O O   . HOH   F .   ? 0.6004 0.2744 0.4524 -0.0185 0.0341  0.0443  564 HOH   A O   
6905 O O   B HOH   F .   ? 0.1825 0.1146 0.2302 0.0483  -0.1155 -0.0591 565 HOH   A O   
6906 O O   . HOH   F .   ? 0.1840 0.2260 0.5139 -0.0335 -0.1045 0.0864  566 HOH   A O   
6907 O O   A HOH   F .   ? 0.5105 0.5357 0.4550 -0.0512 0.0977  0.1048  567 HOH   A O   
6908 O O   . HOH   F .   ? 0.2755 0.4285 0.5411 0.0770  -0.0634 0.2032  568 HOH   A O   
6909 O O   . HOH   F .   ? 0.6231 0.7181 0.6016 0.0728  -0.1416 0.1536  569 HOH   A O   
6910 O O   . HOH   F .   ? 0.2554 0.2673 0.4486 -0.0563 0.0764  -0.0931 570 HOH   A O   
6911 O O   . HOH   F .   ? 0.3937 0.4339 0.4545 0.0338  0.0112  0.0780  571 HOH   A O   
6912 O O   . HOH   F .   ? 0.4841 0.4225 0.5094 0.0519  0.0818  0.0097  572 HOH   A O   
6913 O O   . HOH   F .   ? 0.6595 0.5759 0.4322 -0.1019 0.1096  0.0903  573 HOH   A O   
6914 O O   B HOH   F .   ? 0.4841 0.2630 0.2806 -0.0801 -0.0392 0.0466  574 HOH   A O   
6915 O O   . HOH   F .   ? 0.3288 0.4537 0.4441 -0.0061 -0.0570 -0.0300 575 HOH   A O   
6916 O O   . HOH   F .   ? 0.4498 0.6126 0.3846 -0.1176 -0.1248 0.2238  576 HOH   A O   
6917 O O   . HOH   F .   ? 0.5846 0.3350 0.6873 0.0811  0.1042  0.1571  577 HOH   A O   
6918 O O   . HOH   F .   ? 0.2889 0.4659 0.4923 -0.1340 0.0417  -0.1615 578 HOH   A O   
6919 O O   . HOH   F .   ? 0.3581 0.4961 0.4520 0.0352  -0.0790 0.0923  579 HOH   A O   
6920 O O   . HOH   F .   ? 0.3139 0.2639 0.6313 0.0845  -0.1834 -0.0487 580 HOH   A O   
6921 O O   . HOH   F .   ? 0.4900 0.6986 0.6085 0.0858  0.1612  -0.1291 581 HOH   A O   
6922 O O   . HOH   F .   ? 0.3950 0.4821 0.3619 0.0253  -0.0436 -0.0846 582 HOH   A O   
6923 O O   . HOH   F .   ? 0.5055 0.4958 0.2821 0.0320  0.0294  -0.0379 583 HOH   A O   
6924 O O   . HOH   F .   ? 0.2826 0.4364 0.5470 0.0564  0.0471  -0.2076 584 HOH   A O   
6925 O O   . HOH   F .   ? 0.2696 0.2889 0.3960 -0.1174 0.0478  -0.0559 585 HOH   A O   
6926 O O   . HOH   F .   ? 0.4718 0.5731 0.4920 0.0761  0.0774  -0.0463 586 HOH   A O   
6927 O O   . HOH   F .   ? 0.4994 0.5989 0.5274 0.0094  0.1331  0.2564  587 HOH   A O   
6928 O O   . HOH   F .   ? 0.3012 0.1780 0.2714 0.0329  -0.0825 -0.0368 588 HOH   A O   
6929 O O   . HOH   F .   ? 0.3766 0.3037 0.3795 0.0855  0.0717  0.0273  589 HOH   A O   
6930 O O   . HOH   F .   ? 0.4021 0.4480 0.5166 -0.2204 -0.0116 -0.0145 590 HOH   A O   
6931 O O   . HOH   F .   ? 0.5212 0.5026 0.4679 0.0643  0.1646  0.0600  591 HOH   A O   
6932 O O   . HOH   F .   ? 0.4857 0.4510 0.3299 0.0389  -0.0830 -0.0949 592 HOH   A O   
6933 O O   . HOH   F .   ? 0.4533 0.6336 0.5700 -0.1622 -0.1347 0.0232  593 HOH   A O   
6934 O O   . HOH   F .   ? 0.5455 0.2705 0.3564 -0.0578 -0.0312 0.0405  594 HOH   A O   
6935 O O   . HOH   F .   ? 0.6413 0.5379 0.4610 -0.1257 -0.0714 -0.0068 595 HOH   A O   
6936 O O   . HOH   F .   ? 0.5963 0.4252 0.3005 0.0498  0.1303  -0.0144 596 HOH   A O   
6937 O O   . HOH   F .   ? 0.8127 0.3595 0.2940 -0.0031 -0.1111 0.0084  597 HOH   A O   
6938 O O   . HOH   F .   ? 0.6607 0.6254 0.7174 -0.0270 0.0691  -0.0836 598 HOH   A O   
6939 O O   . HOH   F .   ? 0.5922 0.4079 0.4538 -0.0552 0.0322  -0.1108 599 HOH   A O   
6940 O O   . HOH   F .   ? 0.2335 0.2371 0.2463 0.0322  -0.0071 -0.0138 600 HOH   A O   
6941 O O   B HOH   F .   ? 0.2370 0.2208 0.2501 0.0091  -0.1214 0.0422  601 HOH   A O   
6942 O O   . HOH   F .   ? 0.3640 0.3595 0.4445 -0.0365 0.1377  0.0918  602 HOH   A O   
6943 O O   . HOH   F .   ? 0.2712 0.5395 0.3293 0.1082  0.0869  0.2242  603 HOH   A O   
6944 O O   . HOH   F .   ? 0.2598 0.2641 0.7149 -0.0172 -0.1492 0.0473  604 HOH   A O   
6945 O O   . HOH   F .   ? 0.6201 0.6184 0.4161 0.0217  0.1031  0.1507  605 HOH   A O   
6946 O O   . HOH   F .   ? 0.5096 0.3433 0.4512 -0.0621 0.1865  0.0527  606 HOH   A O   
6947 O O   . HOH   F .   ? 0.4321 0.2923 0.4285 -0.1353 -0.0328 0.1149  607 HOH   A O   
6948 O O   . HOH   F .   ? 0.5234 0.3590 0.2338 -0.1010 0.1195  -0.0396 608 HOH   A O   
6949 O O   . HOH   F .   ? 0.4992 0.4299 0.5737 0.0368  -0.0467 -0.0240 609 HOH   A O   
6950 O O   . HOH   F .   ? 0.2826 0.3156 0.4405 0.0137  0.0990  -0.0147 610 HOH   A O   
6951 O O   . HOH   F .   ? 0.3014 0.2115 0.5347 -0.0086 0.0812  0.0515  611 HOH   A O   
6952 O O   . HOH   F .   ? 0.5069 0.8231 0.4827 -0.0662 -0.0600 0.2370  612 HOH   A O   
6953 O O   . HOH   F .   ? 0.2286 0.3173 0.3403 0.0468  -0.0445 0.0590  613 HOH   A O   
6954 O O   B HOH   F .   ? 0.3446 0.2564 0.2402 0.0186  -0.0925 0.1148  614 HOH   A O   
6955 O O   . HOH   F .   ? 0.4823 0.2446 0.4504 -0.1389 0.0142  0.0268  615 HOH   A O   
6956 O O   . HOH   F .   ? 0.6016 0.2458 0.3423 -0.0699 0.0217  0.0524  616 HOH   A O   
6957 O O   . HOH   F .   ? 0.2310 0.3814 0.4194 0.0440  -0.0309 -0.0069 617 HOH   A O   
6958 O O   . HOH   F .   ? 0.6079 0.4281 0.6101 0.1257  0.0775  -0.0871 618 HOH   A O   
6959 O O   B HOH   F .   ? 0.2534 0.2955 0.2944 0.1046  0.0833  0.0490  619 HOH   A O   
6960 O O   . HOH   F .   ? 0.2892 0.4149 0.3484 0.0058  -0.0325 -0.1133 620 HOH   A O   
6961 O O   B HOH   F .   ? 0.3593 0.2669 0.2169 0.0854  -0.0553 0.0561  621 HOH   A O   
6962 O O   . HOH   F .   ? 0.5841 0.7140 0.5704 0.2081  -0.1117 -0.0113 622 HOH   A O   
6963 O O   . HOH   F .   ? 0.3169 0.2279 0.4558 0.0129  0.0700  0.0532  623 HOH   A O   
6964 O O   . HOH   F .   ? 0.5026 0.6568 0.4612 0.2858  -0.0782 0.0995  624 HOH   A O   
6965 O O   . HOH   F .   ? 0.5437 0.5203 0.4348 -0.0327 -0.0944 -0.1248 625 HOH   A O   
6966 O O   . HOH   F .   ? 0.3836 0.6663 0.4622 0.0404  0.0409  -0.1058 626 HOH   A O   
6967 O O   A HOH   F .   ? 0.3707 0.6240 0.3728 0.0600  0.0298  -0.1093 627 HOH   A O   
6968 O O   . HOH   F .   ? 0.4679 0.6839 0.5799 -0.0549 -0.0891 0.0126  628 HOH   A O   
6969 O O   . HOH   F .   ? 0.5294 0.4598 0.4964 0.0133  0.0422  0.0861  629 HOH   A O   
6970 O O   . HOH   F .   ? 0.3709 0.4555 0.6261 0.0666  -0.1222 0.2308  630 HOH   A O   
6971 O O   . HOH   G .   ? 0.2318 0.2241 0.3156 0.0062  0.0851  0.0206  201 HOH   B O   
6972 O O   . HOH   G .   ? 0.6111 0.4985 0.3997 0.1302  -0.1048 -0.1497 202 HOH   B O   
6973 O O   . HOH   G .   ? 0.4389 0.3940 0.5313 -0.1088 0.0597  -0.1113 203 HOH   B O   
6974 O O   . HOH   G .   ? 0.6014 0.5417 0.6293 0.1217  0.1196  -0.0016 204 HOH   B O   
6975 O O   . HOH   G .   ? 0.4148 0.4043 0.5753 0.0030  -0.1165 0.2546  205 HOH   B O   
6976 O O   . HOH   G .   ? 0.5746 0.5510 0.3322 0.1804  -0.1228 -0.1048 206 HOH   B O   
6977 O O   . HOH   G .   ? 0.2686 0.4845 0.4592 -0.0249 0.1448  -0.1807 207 HOH   B O   
6978 O O   . HOH   G .   ? 0.4360 0.2695 0.3715 -0.0482 -0.0086 -0.1102 208 HOH   B O   
6979 O O   . HOH   G .   ? 0.7203 0.2601 0.3975 0.0650  0.0542  -0.0206 209 HOH   B O   
6980 O O   . HOH   G .   ? 0.3384 0.5814 0.3082 0.0523  0.0160  0.1797  210 HOH   B O   
6981 O O   . HOH   G .   ? 0.2982 0.4655 0.6020 -0.0469 0.0148  -0.0780 211 HOH   B O   
6982 O O   . HOH   G .   ? 0.4028 0.4294 0.4166 0.0052  0.0557  -0.1482 212 HOH   B O   
6983 O O   . HOH   G .   ? 0.2810 0.2754 0.6713 0.0702  -0.1149 0.0576  213 HOH   B O   
6984 O O   . HOH   G .   ? 0.2658 0.2613 0.4437 -0.0031 0.0402  0.0679  214 HOH   B O   
6985 O O   . HOH   G .   ? 0.1511 0.1779 0.2319 -0.0164 -0.0015 -0.0014 215 HOH   B O   
6986 O O   . HOH   G .   ? 0.1930 0.2130 0.2811 0.0001  0.0309  -0.0035 216 HOH   B O   
6987 O O   . HOH   G .   ? 0.3843 0.4178 0.4126 0.1655  -0.0779 0.0222  217 HOH   B O   
6988 O O   . HOH   G .   ? 0.6157 0.2985 0.3950 -0.1727 0.0730  0.0196  218 HOH   B O   
6989 O O   . HOH   G .   ? 0.4616 0.3939 0.3809 -0.0302 -0.1345 0.1294  219 HOH   B O   
6990 O O   . HOH   G .   ? 0.2878 0.5127 0.4174 0.1964  0.0059  -0.0634 220 HOH   B O   
6991 O O   . HOH   G .   ? 0.4893 0.4627 0.5720 -0.0320 -0.1314 -0.1059 221 HOH   B O   
6992 O O   . HOH   G .   ? 0.3122 0.2084 0.5510 0.0349  0.2017  0.0982  222 HOH   B O   
6993 O O   . HOH   G .   ? 0.2374 0.1788 0.2705 -0.0325 0.1001  0.0020  223 HOH   B O   
6994 O O   . HOH   G .   ? 0.3120 0.1932 0.4255 -0.0157 0.1567  -0.0089 224 HOH   B O   
6995 O O   . HOH   G .   ? 0.4464 0.1946 0.2897 -0.0136 -0.0847 0.0187  225 HOH   B O   
6996 O O   . HOH   G .   ? 0.3035 0.3185 0.5036 0.0726  -0.1095 0.0064  226 HOH   B O   
6997 O O   . HOH   G .   ? 0.4592 0.3063 0.3041 -0.1064 0.0212  -0.0327 227 HOH   B O   
6998 O O   . HOH   G .   ? 0.1617 0.1837 0.2730 -0.0150 0.0059  -0.0004 228 HOH   B O   
6999 O O   . HOH   G .   ? 0.2121 0.1901 0.3621 -0.0398 -0.0112 -0.0464 229 HOH   B O   
7000 O O   . HOH   G .   ? 0.3719 0.2154 0.3923 0.0701  -0.0313 -0.0457 230 HOH   B O   
7001 O O   . HOH   G .   ? 0.3580 0.4313 0.4718 -0.1659 0.0080  0.0268  231 HOH   B O   
7002 O O   . HOH   G .   ? 0.4242 0.3155 0.2772 0.0442  0.1321  0.0439  232 HOH   B O   
7003 O O   . HOH   G .   ? 0.3958 0.6522 0.3648 0.2295  0.0564  0.0908  233 HOH   B O   
7004 O O   . HOH   G .   ? 0.2858 0.2658 0.3237 0.0395  0.0015  -0.1043 234 HOH   B O   
7005 O O   . HOH   G .   ? 0.3156 0.3916 0.2958 -0.1135 -0.0398 -0.0348 235 HOH   B O   
7006 O O   . HOH   G .   ? 0.4475 0.2780 0.3966 -0.1987 -0.0178 0.0177  236 HOH   B O   
7007 O O   . HOH   G .   ? 0.4913 0.5807 0.2965 0.1132  0.0570  0.0894  237 HOH   B O   
7008 O O   . HOH   G .   ? 0.3722 0.1690 0.2052 0.0158  -0.0804 -0.0191 238 HOH   B O   
7009 O O   . HOH   G .   ? 0.3033 0.4325 0.2870 -0.1197 0.0548  -0.1062 239 HOH   B O   
7010 O O   . HOH   G .   ? 0.2113 0.1213 0.3792 0.0190  -0.0916 -0.0297 240 HOH   B O   
7011 O O   . HOH   G .   ? 0.1463 0.1322 0.1593 -0.0140 -0.0114 -0.0025 241 HOH   B O   
7012 O O   . HOH   G .   ? 0.2186 0.4413 0.3110 -0.0392 -0.0546 -0.0949 242 HOH   B O   
7013 O O   . HOH   G .   ? 0.1403 0.1221 0.1555 -0.0011 -0.0051 0.0040  243 HOH   B O   
7014 O O   . HOH   G .   ? 0.2130 0.2036 0.1752 -0.0006 -0.0136 0.0003  244 HOH   B O   
7015 O O   . HOH   G .   ? 0.1509 0.1369 0.2355 -0.0096 0.0103  -0.0147 245 HOH   B O   
7016 O O   . HOH   G .   ? 0.3248 0.4212 0.3389 -0.0422 -0.1012 0.0672  246 HOH   B O   
7017 O O   . HOH   G .   ? 0.2836 0.1746 0.5906 -0.0133 -0.1486 -0.0303 247 HOH   B O   
7018 O O   . HOH   G .   ? 0.3603 0.3453 0.3878 0.0563  -0.0878 -0.1760 248 HOH   B O   
7019 O O   . HOH   G .   ? 0.2876 0.2199 0.2796 -0.0253 0.0131  -0.0406 249 HOH   B O   
7020 O O   . HOH   G .   ? 0.2659 0.2285 0.2827 0.0887  0.0703  0.0289  250 HOH   B O   
7021 O O   . HOH   G .   ? 0.2140 0.1894 0.2245 -0.0357 -0.0461 0.0101  251 HOH   B O   
7022 O O   . HOH   G .   ? 0.2221 0.1990 0.2571 0.0686  -0.0678 -0.0691 252 HOH   B O   
7023 O O   . HOH   G .   ? 0.1995 0.4257 0.2287 -0.0514 -0.0242 0.0547  253 HOH   B O   
7024 O O   . HOH   G .   ? 0.6130 0.4232 0.5483 0.1282  0.0052  -0.1358 254 HOH   B O   
7025 O O   . HOH   G .   ? 0.1941 0.1894 0.2584 -0.0414 0.0166  -0.0235 255 HOH   B O   
7026 O O   . HOH   G .   ? 0.1674 0.2565 0.2651 0.0410  0.0423  0.0851  256 HOH   B O   
7027 O O   . HOH   G .   ? 0.1394 0.1505 0.1928 -0.0111 0.0091  -0.0093 257 HOH   B O   
7028 O O   . HOH   G .   ? 0.5254 0.3376 0.2461 -0.0202 -0.0137 0.0191  258 HOH   B O   
7029 O O   . HOH   G .   ? 0.1537 0.1577 0.2511 -0.0185 -0.0138 0.0031  259 HOH   B O   
7030 O O   . HOH   G .   ? 0.3358 0.3236 0.2047 0.0219  0.0696  -0.0026 260 HOH   B O   
7031 O O   . HOH   G .   ? 0.2174 0.3040 0.2510 -0.0452 0.0233  0.0681  261 HOH   B O   
7032 O O   . HOH   G .   ? 0.2111 0.3052 0.5006 0.0486  -0.0643 -0.0954 262 HOH   B O   
7033 O O   . HOH   G .   ? 0.1810 0.1410 0.2129 -0.0256 -0.0158 0.0169  263 HOH   B O   
7034 O O   . HOH   G .   ? 0.2291 0.3777 0.3373 0.0055  0.0876  0.0216  264 HOH   B O   
7035 O O   . HOH   G .   ? 0.1967 0.1390 0.2059 -0.0238 -0.0295 0.0182  265 HOH   B O   
7036 O O   . HOH   G .   ? 0.2045 0.1907 0.4476 0.0092  -0.0873 -0.0986 266 HOH   B O   
7037 O O   . HOH   G .   ? 0.2584 0.1859 0.2960 -0.0636 0.0129  -0.0065 267 HOH   B O   
7038 O O   . HOH   G .   ? 0.4651 0.5034 0.2489 0.1634  -0.0265 -0.0256 268 HOH   B O   
7039 O O   . HOH   G .   ? 0.2615 0.2785 0.2602 -0.0410 -0.0812 0.0146  269 HOH   B O   
7040 O O   . HOH   G .   ? 0.4568 0.2866 0.2353 0.0695  -0.0192 -0.0524 270 HOH   B O   
7041 O O   . HOH   G .   ? 0.1696 0.1630 0.1644 -0.0381 -0.0339 0.0058  271 HOH   B O   
7042 O O   . HOH   G .   ? 0.2404 0.2475 0.2647 -0.0285 -0.0855 -0.0352 272 HOH   B O   
7043 O O   . HOH   G .   ? 0.2340 0.2047 0.1850 0.0039  -0.0129 -0.0039 273 HOH   B O   
7044 O O   . HOH   G .   ? 0.1631 0.1279 0.4652 -0.0110 -0.0280 -0.0140 274 HOH   B O   
7045 O O   . HOH   G .   ? 0.4791 0.6275 0.2542 0.1273  0.0272  0.1379  275 HOH   B O   
7046 O O   . HOH   G .   ? 0.2266 0.4886 0.4540 -0.0904 -0.0980 0.1131  276 HOH   B O   
7047 O O   . HOH   G .   ? 0.2395 0.3125 0.3204 -0.0535 0.0733  -0.1177 277 HOH   B O   
7048 O O   . HOH   G .   ? 0.4155 0.2761 0.3836 -0.0077 -0.0959 -0.0493 278 HOH   B O   
7049 O O   . HOH   G .   ? 0.5537 0.3518 0.2812 0.2453  0.0654  0.0612  279 HOH   B O   
7050 O O   . HOH   G .   ? 0.2345 0.2426 0.2860 0.0166  -0.0813 -0.0029 280 HOH   B O   
7051 O O   . HOH   G .   ? 0.2553 0.3635 0.4816 0.0239  0.0334  -0.0591 281 HOH   B O   
7052 O O   . HOH   G .   ? 0.1555 0.1516 0.3369 -0.0181 0.0056  -0.0135 282 HOH   B O   
7053 O O   . HOH   G .   ? 0.2520 0.2849 0.4571 0.0103  -0.0142 -0.1389 283 HOH   B O   
7054 O O   . HOH   G .   ? 0.2331 0.2519 0.2089 0.0884  -0.0526 -0.0425 284 HOH   B O   
7055 O O   . HOH   G .   ? 0.1936 0.4352 0.4683 -0.0531 -0.0496 -0.1050 285 HOH   B O   
7056 O O   . HOH   G .   ? 0.2277 0.7261 0.2563 0.0760  -0.0311 -0.0630 286 HOH   B O   
7057 O O   . HOH   G .   ? 0.2623 0.2107 0.4834 0.0103  0.0788  0.0433  287 HOH   B O   
7058 O O   . HOH   G .   ? 0.3713 0.3956 0.4270 0.1409  -0.0872 -0.1295 288 HOH   B O   
7059 O O   . HOH   G .   ? 0.1547 0.1413 0.1595 0.0020  -0.0019 -0.0003 289 HOH   B O   
7060 O O   . HOH   G .   ? 0.3295 0.6331 0.7791 0.1809  -0.0015 -0.0988 290 HOH   B O   
7061 O O   . HOH   G .   ? 0.3723 0.2748 0.2183 0.0522  -0.0964 -0.0279 291 HOH   B O   
7062 O O   . HOH   G .   ? 0.1546 0.1745 0.2495 0.0185  -0.0088 0.0052  292 HOH   B O   
7063 O O   . HOH   G .   ? 0.3217 0.6404 0.4525 0.0939  -0.1240 0.1507  293 HOH   B O   
7064 O O   . HOH   G .   ? 0.6340 0.4618 0.3946 -0.1103 0.0329  0.0187  294 HOH   B O   
7065 O O   . HOH   G .   ? 0.5262 0.2879 0.2691 -0.1915 0.1060  -0.0182 295 HOH   B O   
7066 O O   . HOH   G .   ? 0.1619 0.3244 0.4132 0.0362  -0.0052 -0.1301 296 HOH   B O   
7067 O O   . HOH   G .   ? 0.2967 0.2706 0.2315 -0.0161 0.0007  -0.1159 297 HOH   B O   
7068 O O   . HOH   G .   ? 0.1563 0.2008 0.1520 -0.0150 -0.0221 0.0019  298 HOH   B O   
7069 O O   . HOH   G .   ? 0.2022 0.2537 0.5493 0.0545  -0.0578 -0.1136 299 HOH   B O   
7070 O O   . HOH   G .   ? 0.4324 0.2898 0.4839 -0.0922 0.0320  0.0578  300 HOH   B O   
7071 O O   . HOH   G .   ? 0.4256 0.3711 0.2741 0.1090  -0.0826 0.0511  301 HOH   B O   
7072 O O   . HOH   G .   ? 0.1608 0.1442 0.2156 -0.0041 -0.0007 0.0106  302 HOH   B O   
7073 O O   . HOH   G .   ? 0.3804 0.2089 0.3896 -0.0954 -0.2044 0.0630  303 HOH   B O   
7074 O O   . HOH   G .   ? 0.3794 0.5624 0.5732 0.0017  -0.1475 0.0382  304 HOH   B O   
7075 O O   . HOH   G .   ? 0.3543 0.1798 0.3401 0.0714  0.1323  0.0587  305 HOH   B O   
7076 O O   . HOH   G .   ? 0.3902 0.3744 0.1835 -0.0100 0.0231  0.0220  306 HOH   B O   
7077 O O   . HOH   G .   ? 0.2154 0.1420 0.2545 -0.0161 -0.0177 -0.0105 307 HOH   B O   
7078 O O   . HOH   G .   ? 0.1981 0.1513 0.2981 0.0266  -0.0987 0.0024  308 HOH   B O   
7079 O O   . HOH   G .   ? 0.2069 0.3011 0.5503 -0.0203 -0.0525 0.0075  309 HOH   B O   
7080 O O   . HOH   G .   ? 0.4358 0.2347 0.2761 0.1610  0.1054  0.0409  310 HOH   B O   
7081 O O   . HOH   G .   ? 0.2317 0.1352 0.2577 -0.0129 -0.0195 0.0318  311 HOH   B O   
7082 O O   . HOH   G .   ? 0.4282 0.2317 0.2871 0.0350  0.0431  0.0756  312 HOH   B O   
7083 O O   . HOH   G .   ? 0.1512 0.1434 0.2874 0.0072  -0.0046 -0.0146 313 HOH   B O   
7084 O O   . HOH   G .   ? 0.2715 0.3150 0.4042 -0.0930 0.1054  -0.0754 314 HOH   B O   
7085 O O   . HOH   G .   ? 0.2805 0.2684 0.4760 -0.0288 -0.0774 0.0921  315 HOH   B O   
7086 O O   . HOH   G .   ? 0.2144 0.1953 0.1753 -0.0141 0.0277  0.0085  316 HOH   B O   
7087 O O   . HOH   G .   ? 0.1519 0.1752 0.2583 -0.0207 -0.0041 -0.0033 317 HOH   B O   
7088 O O   . HOH   G .   ? 0.2631 0.3316 0.5241 -0.0687 -0.1791 0.1387  318 HOH   B O   
7089 O O   . HOH   G .   ? 0.2529 0.2869 0.3224 -0.0455 0.0872  -0.0790 319 HOH   B O   
7090 O O   . HOH   G .   ? 0.1664 0.2689 0.2499 -0.0136 -0.0207 0.0604  320 HOH   B O   
7091 O O   . HOH   G .   ? 0.1492 0.1598 0.2855 -0.0098 -0.0096 -0.0180 321 HOH   B O   
7092 O O   . HOH   G .   ? 0.5862 0.3814 0.5555 0.1306  0.1515  0.0088  322 HOH   B O   
7093 O O   . HOH   G .   ? 0.4471 0.4049 0.1936 0.0521  -0.0380 -0.0160 323 HOH   B O   
7094 O O   . HOH   G .   ? 0.4316 0.3389 0.5697 0.0865  -0.0244 0.0868  324 HOH   B O   
7095 O O   . HOH   G .   ? 0.6452 0.1786 0.2839 -0.0151 -0.0876 -0.0071 325 HOH   B O   
7096 O O   . HOH   G .   ? 0.2593 0.2126 0.2207 0.0102  -0.0164 0.0204  326 HOH   B O   
7097 O O   . HOH   G .   ? 0.5525 0.4493 0.6444 0.0852  -0.0579 0.1398  327 HOH   B O   
7098 O O   . HOH   G .   ? 0.4033 0.3404 0.4951 0.1066  0.1966  0.1903  328 HOH   B O   
7099 O O   . HOH   G .   ? 0.1949 0.1731 0.2881 0.0292  0.0617  0.0194  329 HOH   B O   
7100 O O   . HOH   G .   ? 0.2998 0.3176 0.7057 0.0033  -0.0481 0.1731  330 HOH   B O   
7101 O O   . HOH   G .   ? 0.2349 0.5951 0.4471 -0.0927 -0.0140 -0.0495 331 HOH   B O   
7102 O O   . HOH   G .   ? 0.5676 0.3486 0.3820 -0.0046 0.1464  0.1142  332 HOH   B O   
7103 O O   . HOH   G .   ? 0.2564 0.1965 0.4302 -0.0022 -0.0090 0.0081  333 HOH   B O   
7104 O O   . HOH   G .   ? 0.2088 0.2150 0.5464 -0.0365 0.0138  0.1248  334 HOH   B O   
7105 O O   . HOH   G .   ? 0.4711 0.5976 0.3413 0.0450  -0.0892 -0.0241 335 HOH   B O   
7106 O O   . HOH   G .   ? 0.6554 0.5966 0.5287 0.3068  -0.0101 -0.0696 336 HOH   B O   
7107 O O   . HOH   G .   ? 0.1643 0.1382 0.2109 0.0035  -0.0245 0.0078  337 HOH   B O   
7108 O O   . HOH   G .   ? 0.4417 0.4254 0.5092 -0.0058 -0.0284 -0.1209 338 HOH   B O   
7109 O O   . HOH   G .   ? 0.1634 0.2542 0.2502 0.0239  -0.0142 -0.0611 339 HOH   B O   
7110 O O   . HOH   G .   ? 0.5052 0.3418 0.3969 0.0426  0.0426  -0.1691 340 HOH   B O   
7111 O O   . HOH   G .   ? 0.3735 0.6588 0.3453 -0.0243 -0.0472 0.1195  341 HOH   B O   
7112 O O   . HOH   G .   ? 0.4708 0.3855 0.3206 0.0827  -0.1143 -0.1191 342 HOH   B O   
7113 O O   . HOH   G .   ? 0.6292 0.5266 0.2927 -0.0033 -0.0684 0.1140  343 HOH   B O   
7114 O O   . HOH   G .   ? 0.1980 0.1903 0.3213 -0.0055 0.0558  -0.0276 344 HOH   B O   
7115 O O   . HOH   G .   ? 0.2594 0.5024 0.5794 -0.0309 0.1078  -0.0272 345 HOH   B O   
7116 O O   . HOH   G .   ? 0.4778 0.5972 0.4472 -0.1400 0.0716  0.1057  346 HOH   B O   
7117 O O   . HOH   G .   ? 0.3904 0.3858 0.5304 0.0142  -0.0538 0.0533  347 HOH   B O   
7118 O O   . HOH   G .   ? 0.3969 0.6236 0.3893 -0.1187 -0.1323 -0.0766 348 HOH   B O   
7119 O O   . HOH   G .   ? 0.2683 0.2139 0.4623 -0.0103 -0.0898 -0.0316 349 HOH   B O   
7120 O O   . HOH   G .   ? 0.3105 0.1937 0.3766 0.0442  -0.1052 -0.0636 350 HOH   B O   
7121 O O   . HOH   G .   ? 0.4979 0.6248 0.5551 0.0406  -0.0362 -0.0050 351 HOH   B O   
7122 O O   . HOH   G .   ? 0.2246 0.3286 0.5824 0.0308  0.0413  -0.0155 352 HOH   B O   
7123 O O   . HOH   G .   ? 0.4415 0.3592 0.3633 0.1133  0.0735  -0.0347 353 HOH   B O   
7124 O O   . HOH   G .   ? 0.2218 0.5366 0.3562 0.1105  -0.0320 -0.1360 354 HOH   B O   
7125 O O   . HOH   G .   ? 0.4827 0.3025 0.5660 -0.1352 0.1356  0.0127  355 HOH   B O   
7126 O O   . HOH   G .   ? 0.4238 0.2256 0.3779 -0.1033 0.0804  -0.1277 356 HOH   B O   
7127 O O   . HOH   G .   ? 0.3195 0.4028 0.5075 -0.1188 0.0118  -0.0077 357 HOH   B O   
7128 O O   . HOH   G .   ? 0.4979 0.5071 0.4764 0.1930  -0.1231 0.1233  358 HOH   B O   
7129 O O   . HOH   G .   ? 0.3518 0.3093 0.3560 -0.0967 -0.0274 -0.0190 359 HOH   B O   
7130 O O   . HOH   G .   ? 0.4473 0.3178 0.5229 0.0283  -0.1720 -0.0017 360 HOH   B O   
7131 O O   . HOH   G .   ? 0.4629 0.4942 0.4462 -0.0152 -0.0360 0.0405  361 HOH   B O   
7132 O O   . HOH   G .   ? 0.5080 0.6632 0.3408 0.1793  -0.0394 0.0520  362 HOH   B O   
7133 O O   . HOH   G .   ? 0.4596 0.4051 0.6416 0.0128  0.1050  0.1434  363 HOH   B O   
7134 O O   . HOH   G .   ? 0.2155 0.3777 0.5755 -0.0777 -0.0476 -0.0882 364 HOH   B O   
7135 O O   . HOH   G .   ? 0.6530 0.4840 0.4554 0.1621  0.1477  0.0688  365 HOH   B O   
7136 O O   . HOH   G .   ? 0.4693 0.3858 0.5013 0.1117  -0.1395 0.0215  366 HOH   B O   
7137 O O   . HOH   G .   ? 0.5064 0.5276 0.4542 -0.0818 -0.1094 -0.1060 367 HOH   B O   
7138 O O   . HOH   G .   ? 0.5291 0.2030 0.3996 0.0130  0.0266  0.0538  368 HOH   B O   
7139 O O   . HOH   G .   ? 0.4647 0.3062 0.5414 -0.1479 -0.0636 0.0171  369 HOH   B O   
7140 O O   . HOH   G .   ? 0.5987 0.5159 0.3880 0.0586  -0.1574 0.0987  370 HOH   B O   
7141 O O   . HOH   G .   ? 0.7576 0.6671 0.5074 0.2344  -0.1230 0.0953  371 HOH   B O   
7142 O O   . HOH   G .   ? 0.5112 0.3097 0.4148 0.0610  -0.1265 -0.0302 372 HOH   B O   
7143 O O   . HOH   G .   ? 0.4241 0.5461 0.6032 0.2121  0.0784  0.1298  373 HOH   B O   
7144 O O   . HOH   G .   ? 0.2702 0.4550 0.3802 0.0240  -0.0436 -0.1068 374 HOH   B O   
7145 O O   . HOH   G .   ? 0.6313 0.3868 0.3214 -0.0730 -0.1194 -0.0921 375 HOH   B O   
7146 O O   . HOH   G .   ? 0.3747 0.4931 0.5062 -0.1417 -0.0778 0.0477  376 HOH   B O   
7147 O O   . HOH   G .   ? 0.3784 0.5033 0.5082 0.0116  -0.0626 0.0295  377 HOH   B O   
7148 O O   . HOH   G .   ? 0.7471 0.3689 0.5261 -0.1128 -0.0353 -0.0582 378 HOH   B O   
7149 O O   . HOH   G .   ? 0.3826 0.3807 0.2098 0.0647  0.0783  0.0087  379 HOH   B O   
7150 O O   . HOH   G .   ? 0.5318 0.6666 0.6567 -0.0917 0.2054  0.0905  380 HOH   B O   
7151 O O   . HOH   G .   ? 0.5535 0.6731 0.6727 0.2144  0.0364  0.2796  381 HOH   B O   
7152 O O   . HOH   G .   ? 0.5365 0.6248 0.3720 -0.1405 0.0667  -0.1370 382 HOH   B O   
7153 O O   . HOH   G .   ? 0.2912 0.2276 0.3326 -0.0092 0.0235  0.0260  383 HOH   B O   
7154 O O   . HOH   G .   ? 0.3100 0.6451 0.4815 0.1374  0.1055  0.1025  384 HOH   B O   
7155 O O   . HOH   G .   ? 0.5753 0.4271 0.4428 -0.0037 -0.0012 -0.1372 385 HOH   B O   
7156 O O   . HOH   G .   ? 0.4042 0.3723 0.3747 0.0470  0.0079  -0.0645 386 HOH   B O   
7157 O O   . HOH   G .   ? 0.2572 0.4184 0.3555 -0.0845 -0.0967 -0.0246 387 HOH   B O   
7158 O O   . HOH   G .   ? 0.7159 0.5631 0.4055 0.0970  0.0215  0.0564  388 HOH   B O   
7159 O O   . HOH   G .   ? 0.5335 0.4736 0.5669 -0.0999 -0.0055 0.0078  389 HOH   B O   
7160 O O   . HOH   G .   ? 0.5721 0.5023 0.4538 0.0595  -0.1320 -0.0538 390 HOH   B O   
7161 O O   . HOH   G .   ? 0.3214 0.2227 0.3267 0.0526  -0.0326 0.0003  391 HOH   B O   
7162 O O   . HOH   G .   ? 0.4358 0.4162 0.3587 0.0037  0.0205  0.0708  392 HOH   B O   
7163 O O   . HOH   G .   ? 0.2310 0.3551 0.6019 -0.0884 -0.0703 0.0492  393 HOH   B O   
7164 O O   . HOH   G .   ? 0.4095 0.2118 0.5162 -0.0221 0.1050  0.0426  394 HOH   B O   
7165 O O   . HOH   G .   ? 0.6256 0.6954 0.7280 0.1933  -0.0277 0.2206  395 HOH   B O   
7166 O O   . HOH   G .   ? 0.4297 0.4670 0.3484 -0.0900 0.0986  0.0618  396 HOH   B O   
7167 O O   . HOH   G .   ? 0.4302 0.5936 0.3251 0.1624  -0.0542 -0.1035 397 HOH   B O   
7168 O O   . HOH   G .   ? 0.2135 0.2471 0.5034 -0.0517 -0.1099 0.0385  398 HOH   B O   
7169 O O   . HOH   G .   ? 0.3168 0.3411 0.3458 0.0390  0.0150  -0.0224 399 HOH   B O   
7170 O O   . HOH   G .   ? 0.5451 0.3679 0.2908 -0.1878 -0.0303 0.0995  400 HOH   B O   
7171 O O   . HOH   G .   ? 0.6069 0.6040 0.3908 0.2200  -0.0001 0.0000  401 HOH   B O   
# 
