data_7HE9
# 
_entry.id   7HE9 
# 
_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   7HE9         pdb_00007he9 10.2210/pdb7he9/pdb 
WWPDB D_1001407363 ?            ?                   
# 
_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                        7HE9 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                        18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                                            114.023   2   ? ? ? ? 
3 non-polymer syn '(2S)-3-[(3S)-oxolan-3-yl]-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 262.308   1   ? ? ? ? 
4 water       nat water                                                                             18.015    432 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                                            TFA   
3 '(2S)-3-[(3S)-oxolan-3-yl]-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1A9L 
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 
A1A9L non-polymer         . '(2S)-3-[(3S)-oxolan-3-yl]-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C13 H18 N4 O2'  
262.308 
ALA   'L-peptide linking' y ALANINE                                                                           ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                          ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                        ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                   ? 'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                          ? 'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                         ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                   ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                           ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                         ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                             ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                        ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                           ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                            ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                        ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                     ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                           ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                            ? 'C3 H7 N O3'     
105.093 
TFA   non-polymer         . 'trifluoroacetic acid'                                                            ? 'C2 H F3 O2'     
114.023 
THR   'L-peptide linking' y THREONINE                                                                         ? 'C4 H9 N O3'     
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                          ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                            ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 2 TFA   1   202 301  TFA   TFA A . 
E 3 A1A9L 1   203 201  A1A9L LA1 A . 
F 4 HOH   1   301 153  HOH   HOH A . 
F 4 HOH   2   302 109  HOH   HOH A . 
F 4 HOH   3   303 229  HOH   HOH A . 
F 4 HOH   4   304 292  HOH   HOH A . 
F 4 HOH   5   305 196  HOH   HOH A . 
F 4 HOH   6   306 493  HOH   HOH A . 
F 4 HOH   7   307 625  HOH   HOH A . 
F 4 HOH   8   308 1309 HOH   HOH A . 
F 4 HOH   9   309 4    HOH   HOH A . 
F 4 HOH   10  310 1301 HOH   HOH A . 
F 4 HOH   11  311 1290 HOH   HOH A . 
F 4 HOH   12  312 209  HOH   HOH A . 
F 4 HOH   13  313 76   HOH   HOH A . 
F 4 HOH   14  314 18   HOH   HOH A . 
F 4 HOH   15  315 247  HOH   HOH A . 
F 4 HOH   16  316 136  HOH   HOH A . 
F 4 HOH   17  317 405  HOH   HOH A . 
F 4 HOH   18  318 236  HOH   HOH A . 
F 4 HOH   19  319 661  HOH   HOH A . 
F 4 HOH   20  320 1283 HOH   HOH A . 
F 4 HOH   21  321 1275 HOH   HOH A . 
F 4 HOH   22  322 56   HOH   HOH A . 
F 4 HOH   23  323 192  HOH   HOH A . 
F 4 HOH   24  324 39   HOH   HOH A . 
F 4 HOH   25  325 26   HOH   HOH A . 
F 4 HOH   26  326 469  HOH   HOH A . 
F 4 HOH   27  327 124  HOH   HOH A . 
F 4 HOH   28  328 964  HOH   HOH A . 
F 4 HOH   29  329 155  HOH   HOH A . 
F 4 HOH   30  330 151  HOH   HOH A . 
F 4 HOH   31  331 1295 HOH   HOH A . 
F 4 HOH   32  332 225  HOH   HOH A . 
F 4 HOH   33  333 3    HOH   HOH A . 
F 4 HOH   34  334 105  HOH   HOH A . 
F 4 HOH   35  335 662  HOH   HOH A . 
F 4 HOH   36  336 15   HOH   HOH A . 
F 4 HOH   37  337 337  HOH   HOH A . 
F 4 HOH   38  338 164  HOH   HOH A . 
F 4 HOH   39  339 21   HOH   HOH A . 
F 4 HOH   40  340 1300 HOH   HOH A . 
F 4 HOH   41  341 140  HOH   HOH A . 
F 4 HOH   42  342 630  HOH   HOH A . 
F 4 HOH   43  343 393  HOH   HOH A . 
F 4 HOH   44  344 8    HOH   HOH A . 
F 4 HOH   45  345 57   HOH   HOH A . 
F 4 HOH   46  346 18   HOH   HOH A . 
F 4 HOH   47  347 241  HOH   HOH A . 
F 4 HOH   48  348 409  HOH   HOH A . 
F 4 HOH   49  349 92   HOH   HOH A . 
F 4 HOH   50  350 396  HOH   HOH A . 
F 4 HOH   51  351 165  HOH   HOH A . 
F 4 HOH   52  352 139  HOH   HOH A . 
F 4 HOH   53  353 93   HOH   HOH A . 
F 4 HOH   54  354 12   HOH   HOH A . 
F 4 HOH   55  355 2    HOH   HOH A . 
F 4 HOH   56  356 320  HOH   HOH A . 
F 4 HOH   57  357 22   HOH   HOH A . 
F 4 HOH   58  358 354  HOH   HOH A . 
F 4 HOH   59  359 17   HOH   HOH A . 
F 4 HOH   60  360 169  HOH   HOH A . 
F 4 HOH   61  361 102  HOH   HOH A . 
F 4 HOH   62  362 33   HOH   HOH A . 
F 4 HOH   63  363 42   HOH   HOH A . 
F 4 HOH   64  364 66   HOH   HOH A . 
F 4 HOH   65  365 939  HOH   HOH A . 
F 4 HOH   66  366 19   HOH   HOH A . 
F 4 HOH   67  367 5    HOH   HOH A . 
F 4 HOH   68  368 333  HOH   HOH A . 
F 4 HOH   69  369 1308 HOH   HOH A . 
F 4 HOH   70  370 138  HOH   HOH A . 
F 4 HOH   71  371 36   HOH   HOH A . 
F 4 HOH   72  372 81   HOH   HOH A . 
F 4 HOH   73  373 46   HOH   HOH A . 
F 4 HOH   74  374 49   HOH   HOH A . 
F 4 HOH   75  375 45   HOH   HOH A . 
F 4 HOH   76  376 23   HOH   HOH A . 
F 4 HOH   77  377 24   HOH   HOH A . 
F 4 HOH   78  378 162  HOH   HOH A . 
F 4 HOH   79  379 186  HOH   HOH A . 
F 4 HOH   80  380 461  HOH   HOH A . 
F 4 HOH   81  381 74   HOH   HOH A . 
F 4 HOH   82  382 148  HOH   HOH A . 
F 4 HOH   83  383 86   HOH   HOH A . 
F 4 HOH   84  384 16   HOH   HOH A . 
F 4 HOH   85  385 27   HOH   HOH A . 
F 4 HOH   86  386 218  HOH   HOH A . 
F 4 HOH   87  387 134  HOH   HOH A . 
F 4 HOH   88  388 115  HOH   HOH A . 
F 4 HOH   89  389 159  HOH   HOH A . 
F 4 HOH   90  390 35   HOH   HOH A . 
F 4 HOH   91  391 140  HOH   HOH A . 
F 4 HOH   92  392 154  HOH   HOH A . 
F 4 HOH   93  393 34   HOH   HOH A . 
F 4 HOH   94  394 366  HOH   HOH A . 
F 4 HOH   95  395 15   HOH   HOH A . 
F 4 HOH   96  396 1310 HOH   HOH A . 
F 4 HOH   97  397 116  HOH   HOH A . 
F 4 HOH   98  398 96   HOH   HOH A . 
F 4 HOH   99  399 281  HOH   HOH A . 
F 4 HOH   100 400 1    HOH   HOH A . 
F 4 HOH   101 401 67   HOH   HOH A . 
F 4 HOH   102 402 25   HOH   HOH A . 
F 4 HOH   103 403 195  HOH   HOH A . 
F 4 HOH   104 404 296  HOH   HOH A . 
F 4 HOH   105 405 83   HOH   HOH A . 
F 4 HOH   106 406 1315 HOH   HOH A . 
F 4 HOH   107 407 2    HOH   HOH A . 
F 4 HOH   108 408 58   HOH   HOH A . 
F 4 HOH   109 409 121  HOH   HOH A . 
F 4 HOH   110 410 85   HOH   HOH A . 
F 4 HOH   111 411 199  HOH   HOH A . 
F 4 HOH   112 412 1068 HOH   HOH A . 
F 4 HOH   113 413 3    HOH   HOH A . 
F 4 HOH   114 414 125  HOH   HOH A . 
F 4 HOH   115 415 303  HOH   HOH A . 
F 4 HOH   116 416 4    HOH   HOH A . 
F 4 HOH   117 417 68   HOH   HOH A . 
F 4 HOH   118 418 1289 HOH   HOH A . 
F 4 HOH   119 419 278  HOH   HOH A . 
F 4 HOH   120 420 6    HOH   HOH A . 
F 4 HOH   121 421 78   HOH   HOH A . 
F 4 HOH   122 422 351  HOH   HOH A . 
F 4 HOH   123 423 123  HOH   HOH A . 
F 4 HOH   124 424 51   HOH   HOH A . 
F 4 HOH   125 425 8    HOH   HOH A . 
F 4 HOH   126 426 53   HOH   HOH A . 
F 4 HOH   127 427 7    HOH   HOH A . 
F 4 HOH   128 428 1279 HOH   HOH A . 
F 4 HOH   129 429 122  HOH   HOH A . 
F 4 HOH   130 430 95   HOH   HOH A . 
F 4 HOH   131 431 582  HOH   HOH A . 
F 4 HOH   132 432 156  HOH   HOH A . 
F 4 HOH   133 433 397  HOH   HOH A . 
F 4 HOH   134 434 1313 HOH   HOH A . 
F 4 HOH   135 435 132  HOH   HOH A . 
F 4 HOH   136 436 1222 HOH   HOH A . 
F 4 HOH   137 437 7    HOH   HOH A . 
F 4 HOH   138 438 1189 HOH   HOH A . 
F 4 HOH   139 439 70   HOH   HOH A . 
F 4 HOH   140 440 14   HOH   HOH A . 
F 4 HOH   141 441 40   HOH   HOH A . 
F 4 HOH   142 442 73   HOH   HOH A . 
F 4 HOH   143 443 71   HOH   HOH A . 
F 4 HOH   144 444 952  HOH   HOH A . 
F 4 HOH   145 445 1286 HOH   HOH A . 
F 4 HOH   146 446 944  HOH   HOH A . 
F 4 HOH   147 447 576  HOH   HOH A . 
F 4 HOH   148 448 1238 HOH   HOH A . 
F 4 HOH   149 449 80   HOH   HOH A . 
F 4 HOH   150 450 94   HOH   HOH A . 
F 4 HOH   151 451 212  HOH   HOH A . 
F 4 HOH   152 452 381  HOH   HOH A . 
F 4 HOH   153 453 97   HOH   HOH A . 
F 4 HOH   154 454 79   HOH   HOH A . 
F 4 HOH   155 455 1296 HOH   HOH A . 
F 4 HOH   156 456 21   HOH   HOH A . 
F 4 HOH   157 457 16   HOH   HOH A . 
F 4 HOH   158 458 104  HOH   HOH A . 
F 4 HOH   159 459 12   HOH   HOH A . 
F 4 HOH   160 460 188  HOH   HOH A . 
F 4 HOH   161 461 1094 HOH   HOH A . 
F 4 HOH   162 462 330  HOH   HOH A . 
F 4 HOH   163 463 17   HOH   HOH A . 
F 4 HOH   164 464 1119 HOH   HOH A . 
F 4 HOH   165 465 509  HOH   HOH A . 
F 4 HOH   166 466 107  HOH   HOH A . 
F 4 HOH   167 467 1134 HOH   HOH A . 
F 4 HOH   168 468 726  HOH   HOH A . 
F 4 HOH   169 469 163  HOH   HOH A . 
F 4 HOH   170 470 5    HOH   HOH A . 
F 4 HOH   171 471 408  HOH   HOH A . 
F 4 HOH   172 472 756  HOH   HOH A . 
F 4 HOH   173 473 361  HOH   HOH A . 
F 4 HOH   174 474 319  HOH   HOH A . 
F 4 HOH   175 475 126  HOH   HOH A . 
F 4 HOH   176 476 556  HOH   HOH A . 
F 4 HOH   177 477 63   HOH   HOH A . 
F 4 HOH   178 478 280  HOH   HOH A . 
F 4 HOH   179 479 801  HOH   HOH A . 
F 4 HOH   180 480 1307 HOH   HOH A . 
F 4 HOH   181 481 1276 HOH   HOH A . 
F 4 HOH   182 482 6    HOH   HOH A . 
F 4 HOH   183 483 13   HOH   HOH A . 
F 4 HOH   184 484 267  HOH   HOH A . 
F 4 HOH   185 485 224  HOH   HOH A . 
F 4 HOH   186 486 342  HOH   HOH A . 
F 4 HOH   187 487 370  HOH   HOH A . 
F 4 HOH   188 488 250  HOH   HOH A . 
F 4 HOH   189 489 135  HOH   HOH A . 
F 4 HOH   190 490 1306 HOH   HOH A . 
F 4 HOH   191 491 202  HOH   HOH A . 
F 4 HOH   192 492 1287 HOH   HOH A . 
F 4 HOH   193 493 695  HOH   HOH A . 
F 4 HOH   194 494 919  HOH   HOH A . 
F 4 HOH   195 495 315  HOH   HOH A . 
F 4 HOH   196 496 674  HOH   HOH A . 
F 4 HOH   197 497 318  HOH   HOH A . 
F 4 HOH   198 498 1299 HOH   HOH A . 
F 4 HOH   199 499 309  HOH   HOH A . 
F 4 HOH   200 500 1314 HOH   HOH A . 
F 4 HOH   201 501 521  HOH   HOH A . 
F 4 HOH   202 502 20   HOH   HOH A . 
F 4 HOH   203 503 331  HOH   HOH A . 
F 4 HOH   204 504 805  HOH   HOH A . 
F 4 HOH   205 505 711  HOH   HOH A . 
F 4 HOH   206 506 263  HOH   HOH A . 
F 4 HOH   207 507 152  HOH   HOH A . 
F 4 HOH   208 508 941  HOH   HOH A . 
F 4 HOH   209 509 208  HOH   HOH A . 
F 4 HOH   210 510 1071 HOH   HOH A . 
F 4 HOH   211 511 180  HOH   HOH A . 
F 4 HOH   212 512 350  HOH   HOH A . 
F 4 HOH   213 513 363  HOH   HOH A . 
F 4 HOH   214 514 356  HOH   HOH A . 
F 4 HOH   215 515 313  HOH   HOH A . 
F 4 HOH   216 516 371  HOH   HOH A . 
F 4 HOH   217 517 19   HOH   HOH A . 
F 4 HOH   218 518 1284 HOH   HOH A . 
F 4 HOH   219 519 326  HOH   HOH A . 
F 4 HOH   220 520 429  HOH   HOH A . 
F 4 HOH   221 521 1074 HOH   HOH A . 
F 4 HOH   222 522 185  HOH   HOH A . 
F 4 HOH   223 523 9    HOH   HOH A . 
F 4 HOH   224 524 10   HOH   HOH A . 
F 4 HOH   225 525 376  HOH   HOH A . 
F 4 HOH   226 526 70   HOH   HOH A . 
F 4 HOH   227 527 772  HOH   HOH A . 
F 4 HOH   228 528 11   HOH   HOH A . 
F 4 HOH   229 529 346  HOH   HOH A . 
F 4 HOH   230 530 1292 HOH   HOH A . 
F 4 HOH   231 531 1078 HOH   HOH A . 
G 4 HOH   1   201 64   HOH   HOH B . 
G 4 HOH   2   202 549  HOH   HOH B . 
G 4 HOH   3   203 654  HOH   HOH B . 
G 4 HOH   4   204 900  HOH   HOH B . 
G 4 HOH   5   205 531  HOH   HOH B . 
G 4 HOH   6   206 240  HOH   HOH B . 
G 4 HOH   7   207 1249 HOH   HOH B . 
G 4 HOH   8   208 398  HOH   HOH B . 
G 4 HOH   9   209 364  HOH   HOH B . 
G 4 HOH   10  210 758  HOH   HOH B . 
G 4 HOH   11  211 452  HOH   HOH B . 
G 4 HOH   12  212 743  HOH   HOH B . 
G 4 HOH   13  213 358  HOH   HOH B . 
G 4 HOH   14  214 120  HOH   HOH B . 
G 4 HOH   15  215 332  HOH   HOH B . 
G 4 HOH   16  216 282  HOH   HOH B . 
G 4 HOH   17  217 50   HOH   HOH B . 
G 4 HOH   18  218 264  HOH   HOH B . 
G 4 HOH   19  219 353  HOH   HOH B . 
G 4 HOH   20  220 131  HOH   HOH B . 
G 4 HOH   21  221 232  HOH   HOH B . 
G 4 HOH   22  222 272  HOH   HOH B . 
G 4 HOH   23  223 444  HOH   HOH B . 
G 4 HOH   24  224 276  HOH   HOH B . 
G 4 HOH   25  225 1278 HOH   HOH B . 
G 4 HOH   26  226 75   HOH   HOH B . 
G 4 HOH   27  227 1140 HOH   HOH B . 
G 4 HOH   28  228 127  HOH   HOH B . 
G 4 HOH   29  229 723  HOH   HOH B . 
G 4 HOH   30  230 82   HOH   HOH B . 
G 4 HOH   31  231 60   HOH   HOH B . 
G 4 HOH   32  232 252  HOH   HOH B . 
G 4 HOH   33  233 343  HOH   HOH B . 
G 4 HOH   34  234 54   HOH   HOH B . 
G 4 HOH   35  235 205  HOH   HOH B . 
G 4 HOH   36  236 1312 HOH   HOH B . 
G 4 HOH   37  237 181  HOH   HOH B . 
G 4 HOH   38  238 14   HOH   HOH B . 
G 4 HOH   39  239 1    HOH   HOH B . 
G 4 HOH   40  240 110  HOH   HOH B . 
G 4 HOH   41  241 133  HOH   HOH B . 
G 4 HOH   42  242 325  HOH   HOH B . 
G 4 HOH   43  243 166  HOH   HOH B . 
G 4 HOH   44  244 30   HOH   HOH B . 
G 4 HOH   45  245 172  HOH   HOH B . 
G 4 HOH   46  246 9    HOH   HOH B . 
G 4 HOH   47  247 69   HOH   HOH B . 
G 4 HOH   48  248 128  HOH   HOH B . 
G 4 HOH   49  249 391  HOH   HOH B . 
G 4 HOH   50  250 52   HOH   HOH B . 
G 4 HOH   51  251 129  HOH   HOH B . 
G 4 HOH   52  252 72   HOH   HOH B . 
G 4 HOH   53  253 300  HOH   HOH B . 
G 4 HOH   54  254 144  HOH   HOH B . 
G 4 HOH   55  255 47   HOH   HOH B . 
G 4 HOH   56  256 31   HOH   HOH B . 
G 4 HOH   57  257 10   HOH   HOH B . 
G 4 HOH   58  258 231  HOH   HOH B . 
G 4 HOH   59  259 41   HOH   HOH B . 
G 4 HOH   60  260 59   HOH   HOH B . 
G 4 HOH   61  261 143  HOH   HOH B . 
G 4 HOH   62  262 302  HOH   HOH B . 
G 4 HOH   63  263 103  HOH   HOH B . 
G 4 HOH   64  264 62   HOH   HOH B . 
G 4 HOH   65  265 347  HOH   HOH B . 
G 4 HOH   66  266 61   HOH   HOH B . 
G 4 HOH   67  267 150  HOH   HOH B . 
G 4 HOH   68  268 221  HOH   HOH B . 
G 4 HOH   69  269 20   HOH   HOH B . 
G 4 HOH   70  270 11   HOH   HOH B . 
G 4 HOH   71  271 117  HOH   HOH B . 
G 4 HOH   72  272 1277 HOH   HOH B . 
G 4 HOH   73  273 175  HOH   HOH B . 
G 4 HOH   74  274 242  HOH   HOH B . 
G 4 HOH   75  275 271  HOH   HOH B . 
G 4 HOH   76  276 114  HOH   HOH B . 
G 4 HOH   77  277 84   HOH   HOH B . 
G 4 HOH   78  278 77   HOH   HOH B . 
G 4 HOH   79  279 147  HOH   HOH B . 
G 4 HOH   80  280 22   HOH   HOH B . 
G 4 HOH   81  281 216  HOH   HOH B . 
G 4 HOH   82  282 220  HOH   HOH B . 
G 4 HOH   83  283 287  HOH   HOH B . 
G 4 HOH   84  284 43   HOH   HOH B . 
G 4 HOH   85  285 243  HOH   HOH B . 
G 4 HOH   86  286 137  HOH   HOH B . 
G 4 HOH   87  287 106  HOH   HOH B . 
G 4 HOH   88  288 235  HOH   HOH B . 
G 4 HOH   89  289 88   HOH   HOH B . 
G 4 HOH   90  290 13   HOH   HOH B . 
G 4 HOH   91  291 1305 HOH   HOH B . 
G 4 HOH   92  292 1066 HOH   HOH B . 
G 4 HOH   93  293 311  HOH   HOH B . 
G 4 HOH   94  294 99   HOH   HOH B . 
G 4 HOH   95  295 112  HOH   HOH B . 
G 4 HOH   96  296 160  HOH   HOH B . 
G 4 HOH   97  297 299  HOH   HOH B . 
G 4 HOH   98  298 89   HOH   HOH B . 
G 4 HOH   99  299 142  HOH   HOH B . 
G 4 HOH   100 300 416  HOH   HOH B . 
G 4 HOH   101 301 32   HOH   HOH B . 
G 4 HOH   102 302 1106 HOH   HOH B . 
G 4 HOH   103 303 316  HOH   HOH B . 
G 4 HOH   104 304 297  HOH   HOH B . 
G 4 HOH   105 305 38   HOH   HOH B . 
G 4 HOH   106 306 37   HOH   HOH B . 
G 4 HOH   107 307 207  HOH   HOH B . 
G 4 HOH   108 308 48   HOH   HOH B . 
G 4 HOH   109 309 387  HOH   HOH B . 
G 4 HOH   110 310 118  HOH   HOH B . 
G 4 HOH   111 311 215  HOH   HOH B . 
G 4 HOH   112 312 101  HOH   HOH B . 
G 4 HOH   113 313 161  HOH   HOH B . 
G 4 HOH   114 314 635  HOH   HOH B . 
G 4 HOH   115 315 91   HOH   HOH B . 
G 4 HOH   116 316 1274 HOH   HOH B . 
G 4 HOH   117 317 1126 HOH   HOH B . 
G 4 HOH   118 318 1285 HOH   HOH B . 
G 4 HOH   119 319 197  HOH   HOH B . 
G 4 HOH   120 320 704  HOH   HOH B . 
G 4 HOH   121 321 170  HOH   HOH B . 
G 4 HOH   122 322 23   HOH   HOH B . 
G 4 HOH   123 323 44   HOH   HOH B . 
G 4 HOH   124 324 182  HOH   HOH B . 
G 4 HOH   125 325 28   HOH   HOH B . 
G 4 HOH   126 326 177  HOH   HOH B . 
G 4 HOH   127 327 334  HOH   HOH B . 
G 4 HOH   128 328 100  HOH   HOH B . 
G 4 HOH   129 329 29   HOH   HOH B . 
G 4 HOH   130 330 141  HOH   HOH B . 
G 4 HOH   131 331 1294 HOH   HOH B . 
G 4 HOH   132 332 1291 HOH   HOH B . 
G 4 HOH   133 333 339  HOH   HOH B . 
G 4 HOH   134 334 98   HOH   HOH B . 
G 4 HOH   135 335 717  HOH   HOH B . 
G 4 HOH   136 336 55   HOH   HOH B . 
G 4 HOH   137 337 341  HOH   HOH B . 
G 4 HOH   138 338 65   HOH   HOH B . 
G 4 HOH   139 339 234  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 90   HOH   HOH B . 
G 4 HOH   144 344 178  HOH   HOH B . 
G 4 HOH   145 345 960  HOH   HOH B . 
G 4 HOH   146 346 362  HOH   HOH B . 
G 4 HOH   147 347 1304 HOH   HOH B . 
G 4 HOH   148 348 463  HOH   HOH B . 
G 4 HOH   149 349 623  HOH   HOH B . 
G 4 HOH   150 350 191  HOH   HOH B . 
G 4 HOH   151 351 335  HOH   HOH B . 
G 4 HOH   152 352 1046 HOH   HOH B . 
G 4 HOH   153 353 203  HOH   HOH B . 
G 4 HOH   154 354 1280 HOH   HOH B . 
G 4 HOH   155 355 304  HOH   HOH B . 
G 4 HOH   156 356 541  HOH   HOH B . 
G 4 HOH   157 357 87   HOH   HOH B . 
G 4 HOH   158 358 290  HOH   HOH B . 
G 4 HOH   159 359 1077 HOH   HOH B . 
G 4 HOH   160 360 389  HOH   HOH B . 
G 4 HOH   161 361 718  HOH   HOH B . 
G 4 HOH   162 362 283  HOH   HOH B . 
G 4 HOH   163 363 1072 HOH   HOH B . 
G 4 HOH   164 364 479  HOH   HOH B . 
G 4 HOH   165 365 291  HOH   HOH B . 
G 4 HOH   166 366 898  HOH   HOH B . 
G 4 HOH   167 367 615  HOH   HOH B . 
G 4 HOH   168 368 667  HOH   HOH B . 
G 4 HOH   169 369 373  HOH   HOH B . 
G 4 HOH   170 370 340  HOH   HOH B . 
G 4 HOH   171 371 1316 HOH   HOH B . 
G 4 HOH   172 372 190  HOH   HOH B . 
G 4 HOH   173 373 1303 HOH   HOH B . 
G 4 HOH   174 374 149  HOH   HOH B . 
G 4 HOH   175 375 431  HOH   HOH B . 
G 4 HOH   176 376 310  HOH   HOH B . 
G 4 HOH   177 377 183  HOH   HOH B . 
G 4 HOH   178 378 1173 HOH   HOH B . 
G 4 HOH   179 379 1163 HOH   HOH B . 
G 4 HOH   180 380 1000 HOH   HOH B . 
G 4 HOH   181 381 418  HOH   HOH B . 
G 4 HOH   182 382 1311 HOH   HOH B . 
G 4 HOH   183 383 176  HOH   HOH B . 
G 4 HOH   184 384 424  HOH   HOH B . 
G 4 HOH   185 385 981  HOH   HOH B . 
G 4 HOH   186 386 248  HOH   HOH B . 
G 4 HOH   187 387 265  HOH   HOH B . 
G 4 HOH   188 388 491  HOH   HOH B . 
G 4 HOH   189 389 470  HOH   HOH B . 
G 4 HOH   190 390 1298 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   195 395 274  HOH   HOH B . 
G 4 HOH   196 396 566  HOH   HOH B . 
G 4 HOH   197 397 314  HOH   HOH B . 
G 4 HOH   198 398 157  HOH   HOH B . 
G 4 HOH   199 399 792  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           7HE9 
_cell.length_a           88.785 
_cell.length_b           88.785 
_cell.length_c           39.577 
_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                         7HE9 
_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          7HE9 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.77 
_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                     7HE9 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.390 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165703 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.043 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.400 
_reflns.B_iso_Wilson_estimate        12.330 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.047 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1049678 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 33763 7612 ? 1.766 ? ? ? 4.400 ? 0.600  ? ? ? ? ? ? 92.400 2.000 0.916 0.417 
1 2 5.480 44.390 ? 7417  1097 ? 0.025 ? ? ? 6.800 ? 62.000 ? ? ? ? ? ? 99.900 0.027 0.010 0.999 
# 
_refine.entry_id                                 7HE9 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.3900 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4900 
_refine.ls_number_reflns_obs                     165520 
_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                          0.1461 
_refine.ls_R_factor_R_work                       0.1454 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1609 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7983 
_refine.ls_number_reflns_R_work                  157537 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.9071 
_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                                60.260 
_refine.B_iso_min                                8.750 
_refine.pdbx_overall_phase_error                 18.2200 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        44.3900 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             432 
_refine_hist.number_atoms_total               3025 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           14.67 
_refine_hist.pdbx_B_iso_mean_solvent          30.02 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 88.0000  4631 . 0.4107 0.3730 . 246 0.0000 4877 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 98.0000  5221 . 0.3568 0.3732 . 233 0.0000 5454 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5228 . 0.3179 0.3042 . 244 0.0000 5472 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5196 . 0.2819 0.2833 . 285 0.0000 5481 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5194 . 0.2536 0.2745 . 314 0.0000 5508 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5276 . 0.2254 0.2417 . 255 0.0000 5531 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5297 . 0.2053 0.2192 . 262 0.0000 5559 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5224 . 0.1841 0.1972 . 255 0.0000 5479 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5226 . 0.1776 0.1951 . 282 0.0000 5508 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5269 . 0.1589 0.1931 . 241 0.0000 5510 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5282 . 0.1541 0.1783 . 254 0.0000 5536 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5275 . 0.1421 0.1743 . 273 0.0000 5548 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5192 . 0.1339 0.1658 . 286 0.0000 5478 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5316 . 0.1269 0.1486 . 242 0.0000 5558 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5211 . 0.1292 0.1477 . 262 0.0000 5473 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5311 . 0.1271 0.1525 . 273 0.0000 5584 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5256 . 0.1272 0.1457 . 284 0.0000 5540 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5222 . 0.1306 0.1467 . 275 0.0000 5497 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5269 . 0.1321 0.1628 . 251 0.0000 5520 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5274 . 0.1288 0.1608 . 266 0.0000 5540 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5315 . 0.1246 0.1333 . 253 0.0000 5568 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5227 . 0.1181 0.1314 . 278 0.0000 5505 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5283 . 0.1175 0.1333 . 262 0.0000 5545 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5336 . 0.1245 0.1484 . 270 0.0000 5606 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5267 . 0.1331 0.1503 . 252 0.0000 5519 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5287 . 0.1343 0.1388 . 281 0.0000 5568 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5315 . 0.1369 0.1388 . 283 0.0000 5598 . 'X-RAY DIFFRACTION' 
2.1600 2.4700  30 100.0000 5305 . 0.1363 0.1466 . 292 0.0000 5597 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5341 . 0.1482 0.1670 . 260 0.0000 5601 . 'X-RAY DIFFRACTION' 
3.1100 44.3900 30 100.0000 5491 . 0.1486 0.1690 . 269 0.0000 5760 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HE9 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003665' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HE9 
_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 7HE9 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HE9 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 7HE9 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HE9 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HE9 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HE9 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O 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                   7HE9 
_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   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    205 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    319 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.14 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.12 -133.21 
2 1 SER A 128 ? B 66.15 -4.00   
3 1 HIS B 86  ? ? 57.37 -128.01 
# 
_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 529 ? 5.88 . 
2 1 O ? A HOH 530 ? 5.98 . 
3 1 O ? A HOH 531 ? 7.49 . 
4 1 O ? B HOH 401 ? 6.52 . 
# 
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 
A1A9L N2   N Y N 1   
A1A9L C3   C N N 2   
A1A9L C6   C N N 3   
A1A9L C9   C Y N 4   
A1A9L C12  C Y N 5   
A1A9L C1   C N N 6   
A1A9L C10  C Y N 7   
A1A9L C11  C Y N 8   
A1A9L C13  C Y N 9   
A1A9L C2   C N S 10  
A1A9L C4   C N S 11  
A1A9L C5   C N N 12  
A1A9L C7   C N N 13  
A1A9L C8   C Y N 14  
A1A9L N1   N N N 15  
A1A9L N3   N Y N 16  
A1A9L N4   N Y N 17  
A1A9L O1   O N N 18  
A1A9L O2   O N N 19  
A1A9L H6   H N N 20  
A1A9L H7   H N N 21  
A1A9L H11  H N N 22  
A1A9L H10  H N N 23  
A1A9L H15  H N N 24  
A1A9L H16  H N N 25  
A1A9L H5   H N N 26  
A1A9L H4   H N N 27  
A1A9L H17  H N N 28  
A1A9L H1   H N N 29  
A1A9L H2   H N N 30  
A1A9L H9   H N N 31  
A1A9L H8   H N N 32  
A1A9L H13  H N N 33  
A1A9L H12  H N N 34  
A1A9L H14  H N N 35  
A1A9L H18  H N N 36  
A1A9L H3   H N N 37  
ALA   N    N N N 38  
ALA   CA   C N S 39  
ALA   C    C N N 40  
ALA   O    O N N 41  
ALA   CB   C N N 42  
ALA   OXT  O N N 43  
ALA   H    H N N 44  
ALA   H2   H N N 45  
ALA   HA   H N N 46  
ALA   HB1  H N N 47  
ALA   HB2  H N N 48  
ALA   HB3  H N N 49  
ALA   HXT  H N N 50  
ARG   N    N N N 51  
ARG   CA   C N S 52  
ARG   C    C N N 53  
ARG   O    O N N 54  
ARG   CB   C N N 55  
ARG   CG   C N N 56  
ARG   CD   C N N 57  
ARG   NE   N N N 58  
ARG   CZ   C N N 59  
ARG   NH1  N N N 60  
ARG   NH2  N N N 61  
ARG   OXT  O N N 62  
ARG   H    H N N 63  
ARG   H2   H N N 64  
ARG   HA   H N N 65  
ARG   HB2  H N N 66  
ARG   HB3  H N N 67  
ARG   HG2  H N N 68  
ARG   HG3  H N N 69  
ARG   HD2  H N N 70  
ARG   HD3  H N N 71  
ARG   HE   H N N 72  
ARG   HH11 H N N 73  
ARG   HH12 H N N 74  
ARG   HH21 H N N 75  
ARG   HH22 H N N 76  
ARG   HXT  H N N 77  
ASN   N    N N N 78  
ASN   CA   C N S 79  
ASN   C    C N N 80  
ASN   O    O N N 81  
ASN   CB   C N N 82  
ASN   CG   C N N 83  
ASN   OD1  O N N 84  
ASN   ND2  N N N 85  
ASN   OXT  O N N 86  
ASN   H    H N N 87  
ASN   H2   H N N 88  
ASN   HA   H N N 89  
ASN   HB2  H N N 90  
ASN   HB3  H N N 91  
ASN   HD21 H N N 92  
ASN   HD22 H N N 93  
ASN   HXT  H N N 94  
ASP   N    N N N 95  
ASP   CA   C N S 96  
ASP   C    C N N 97  
ASP   O    O N N 98  
ASP   CB   C N N 99  
ASP   CG   C N N 100 
ASP   OD1  O N N 101 
ASP   OD2  O N N 102 
ASP   OXT  O N N 103 
ASP   H    H N N 104 
ASP   H2   H N N 105 
ASP   HA   H N N 106 
ASP   HB2  H N N 107 
ASP   HB3  H N N 108 
ASP   HD2  H N N 109 
ASP   HXT  H N N 110 
CYS   N    N N N 111 
CYS   CA   C N R 112 
CYS   C    C N N 113 
CYS   O    O N N 114 
CYS   CB   C N N 115 
CYS   SG   S N N 116 
CYS   OXT  O N N 117 
CYS   H    H N N 118 
CYS   H2   H N N 119 
CYS   HA   H N N 120 
CYS   HB2  H N N 121 
CYS   HB3  H N N 122 
CYS   HG   H N N 123 
CYS   HXT  H N N 124 
GLN   N    N N N 125 
GLN   CA   C N S 126 
GLN   C    C N N 127 
GLN   O    O N N 128 
GLN   CB   C N N 129 
GLN   CG   C N N 130 
GLN   CD   C N N 131 
GLN   OE1  O N N 132 
GLN   NE2  N N N 133 
GLN   OXT  O N N 134 
GLN   H    H N N 135 
GLN   H2   H N N 136 
GLN   HA   H N N 137 
GLN   HB2  H N N 138 
GLN   HB3  H N N 139 
GLN   HG2  H N N 140 
GLN   HG3  H N N 141 
GLN   HE21 H N N 142 
GLN   HE22 H N N 143 
GLN   HXT  H N N 144 
GLU   N    N N N 145 
GLU   CA   C N S 146 
GLU   C    C N N 147 
GLU   O    O N N 148 
GLU   CB   C N N 149 
GLU   CG   C N N 150 
GLU   CD   C N N 151 
GLU   OE1  O N N 152 
GLU   OE2  O N N 153 
GLU   OXT  O N N 154 
GLU   H    H N N 155 
GLU   H2   H N N 156 
GLU   HA   H N N 157 
GLU   HB2  H N N 158 
GLU   HB3  H N N 159 
GLU   HG2  H N N 160 
GLU   HG3  H N N 161 
GLU   HE2  H N N 162 
GLU   HXT  H N N 163 
GLY   N    N N N 164 
GLY   CA   C N N 165 
GLY   C    C N N 166 
GLY   O    O N N 167 
GLY   OXT  O N N 168 
GLY   H    H N N 169 
GLY   H2   H N N 170 
GLY   HA2  H N N 171 
GLY   HA3  H N N 172 
GLY   HXT  H N N 173 
HIS   N    N N N 174 
HIS   CA   C N S 175 
HIS   C    C N N 176 
HIS   O    O N N 177 
HIS   CB   C N N 178 
HIS   CG   C Y N 179 
HIS   ND1  N Y N 180 
HIS   CD2  C Y N 181 
HIS   CE1  C Y N 182 
HIS   NE2  N Y N 183 
HIS   OXT  O N N 184 
HIS   H    H N N 185 
HIS   H2   H N N 186 
HIS   HA   H N N 187 
HIS   HB2  H N N 188 
HIS   HB3  H N N 189 
HIS   HD1  H N N 190 
HIS   HD2  H N N 191 
HIS   HE1  H N N 192 
HIS   HE2  H N N 193 
HIS   HXT  H N N 194 
HOH   O    O N N 195 
HOH   H1   H N N 196 
HOH   H2   H N N 197 
ILE   N    N N N 198 
ILE   CA   C N S 199 
ILE   C    C N N 200 
ILE   O    O N N 201 
ILE   CB   C N S 202 
ILE   CG1  C N N 203 
ILE   CG2  C N N 204 
ILE   CD1  C N N 205 
ILE   OXT  O N N 206 
ILE   H    H N N 207 
ILE   H2   H N N 208 
ILE   HA   H N N 209 
ILE   HB   H N N 210 
ILE   HG12 H N N 211 
ILE   HG13 H N N 212 
ILE   HG21 H N N 213 
ILE   HG22 H N N 214 
ILE   HG23 H N N 215 
ILE   HD11 H N N 216 
ILE   HD12 H N N 217 
ILE   HD13 H N N 218 
ILE   HXT  H N N 219 
LEU   N    N N N 220 
LEU   CA   C N S 221 
LEU   C    C N N 222 
LEU   O    O N N 223 
LEU   CB   C N N 224 
LEU   CG   C N N 225 
LEU   CD1  C N N 226 
LEU   CD2  C N N 227 
LEU   OXT  O N N 228 
LEU   H    H N N 229 
LEU   H2   H N N 230 
LEU   HA   H N N 231 
LEU   HB2  H N N 232 
LEU   HB3  H N N 233 
LEU   HG   H N N 234 
LEU   HD11 H N N 235 
LEU   HD12 H N N 236 
LEU   HD13 H N N 237 
LEU   HD21 H N N 238 
LEU   HD22 H N N 239 
LEU   HD23 H N N 240 
LEU   HXT  H N N 241 
LYS   N    N N N 242 
LYS   CA   C N S 243 
LYS   C    C N N 244 
LYS   O    O N N 245 
LYS   CB   C N N 246 
LYS   CG   C N N 247 
LYS   CD   C N N 248 
LYS   CE   C N N 249 
LYS   NZ   N N N 250 
LYS   OXT  O N N 251 
LYS   H    H N N 252 
LYS   H2   H N N 253 
LYS   HA   H N N 254 
LYS   HB2  H N N 255 
LYS   HB3  H N N 256 
LYS   HG2  H N N 257 
LYS   HG3  H N N 258 
LYS   HD2  H N N 259 
LYS   HD3  H N N 260 
LYS   HE2  H N N 261 
LYS   HE3  H N N 262 
LYS   HZ1  H N N 263 
LYS   HZ2  H N N 264 
LYS   HZ3  H N N 265 
LYS   HXT  H N N 266 
MET   N    N N N 267 
MET   CA   C N S 268 
MET   C    C N N 269 
MET   O    O N N 270 
MET   CB   C N N 271 
MET   CG   C N N 272 
MET   SD   S N N 273 
MET   CE   C N N 274 
MET   OXT  O N N 275 
MET   H    H N N 276 
MET   H2   H N N 277 
MET   HA   H N N 278 
MET   HB2  H N N 279 
MET   HB3  H N N 280 
MET   HG2  H N N 281 
MET   HG3  H N N 282 
MET   HE1  H N N 283 
MET   HE2  H N N 284 
MET   HE3  H N N 285 
MET   HXT  H N N 286 
PHE   N    N N N 287 
PHE   CA   C N S 288 
PHE   C    C N N 289 
PHE   O    O N N 290 
PHE   CB   C N N 291 
PHE   CG   C Y N 292 
PHE   CD1  C Y N 293 
PHE   CD2  C Y N 294 
PHE   CE1  C Y N 295 
PHE   CE2  C Y N 296 
PHE   CZ   C Y N 297 
PHE   OXT  O N N 298 
PHE   H    H N N 299 
PHE   H2   H N N 300 
PHE   HA   H N N 301 
PHE   HB2  H N N 302 
PHE   HB3  H N N 303 
PHE   HD1  H N N 304 
PHE   HD2  H N N 305 
PHE   HE1  H N N 306 
PHE   HE2  H N N 307 
PHE   HZ   H N N 308 
PHE   HXT  H N N 309 
PRO   N    N N N 310 
PRO   CA   C N S 311 
PRO   C    C N N 312 
PRO   O    O N N 313 
PRO   CB   C N N 314 
PRO   CG   C N N 315 
PRO   CD   C N N 316 
PRO   OXT  O N N 317 
PRO   H    H N N 318 
PRO   HA   H N N 319 
PRO   HB2  H N N 320 
PRO   HB3  H N N 321 
PRO   HG2  H N N 322 
PRO   HG3  H N N 323 
PRO   HD2  H N N 324 
PRO   HD3  H N N 325 
PRO   HXT  H N N 326 
SER   N    N N N 327 
SER   CA   C N S 328 
SER   C    C N N 329 
SER   O    O N N 330 
SER   CB   C N N 331 
SER   OG   O N N 332 
SER   OXT  O N N 333 
SER   H    H N N 334 
SER   H2   H N N 335 
SER   HA   H N N 336 
SER   HB2  H N N 337 
SER   HB3  H N N 338 
SER   HG   H N N 339 
SER   HXT  H N N 340 
TFA   C1   C N N 341 
TFA   C2   C N N 342 
TFA   O    O N N 343 
TFA   F1   F N N 344 
TFA   F2   F N N 345 
TFA   F3   F N N 346 
TFA   OXT  O N N 347 
TFA   HXT  H N N 348 
THR   N    N N N 349 
THR   CA   C N S 350 
THR   C    C N N 351 
THR   O    O N N 352 
THR   CB   C N R 353 
THR   OG1  O N N 354 
THR   CG2  C N N 355 
THR   OXT  O N N 356 
THR   H    H N N 357 
THR   H2   H N N 358 
THR   HA   H N N 359 
THR   HB   H N N 360 
THR   HG1  H N N 361 
THR   HG21 H N N 362 
THR   HG22 H N N 363 
THR   HG23 H N N 364 
THR   HXT  H N N 365 
TYR   N    N N N 366 
TYR   CA   C N S 367 
TYR   C    C N N 368 
TYR   O    O N N 369 
TYR   CB   C N N 370 
TYR   CG   C Y N 371 
TYR   CD1  C Y N 372 
TYR   CD2  C Y N 373 
TYR   CE1  C Y N 374 
TYR   CE2  C Y N 375 
TYR   CZ   C Y N 376 
TYR   OH   O N N 377 
TYR   OXT  O N N 378 
TYR   H    H N N 379 
TYR   H2   H N N 380 
TYR   HA   H N N 381 
TYR   HB2  H N N 382 
TYR   HB3  H N N 383 
TYR   HD1  H N N 384 
TYR   HD2  H N N 385 
TYR   HE1  H N N 386 
TYR   HE2  H N N 387 
TYR   HH   H N N 388 
TYR   HXT  H N N 389 
VAL   N    N N N 390 
VAL   CA   C N S 391 
VAL   C    C N N 392 
VAL   O    O N N 393 
VAL   CB   C N N 394 
VAL   CG1  C N N 395 
VAL   CG2  C N N 396 
VAL   OXT  O N N 397 
VAL   H    H N N 398 
VAL   H2   H N N 399 
VAL   HA   H N N 400 
VAL   HB   H N N 401 
VAL   HG11 H N N 402 
VAL   HG12 H N N 403 
VAL   HG13 H N N 404 
VAL   HG21 H N N 405 
VAL   HG22 H N N 406 
VAL   HG23 H N N 407 
VAL   HXT  H N N 408 
# 
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 
A1A9L C5  C6   sing N N 1   
A1A9L C5  C4   sing N N 2   
A1A9L O1  C1   sing N N 3   
A1A9L C3  C4   sing N N 4   
A1A9L C3  C2   sing N N 5   
A1A9L C1  C2   sing N N 6   
A1A9L C6  O2   sing N N 7   
A1A9L C4  C7   sing N N 8   
A1A9L C2  N1   sing N N 9   
A1A9L C7  O2   sing N N 10  
A1A9L N1  C8   sing N N 11  
A1A9L C8  C11  doub Y N 12  
A1A9L C8  N2   sing Y N 13  
A1A9L C12 C11  sing Y N 14  
A1A9L C12 C13  doub Y N 15  
A1A9L C11 C10  sing Y N 16  
A1A9L N2  C9   doub Y N 17  
A1A9L C13 N4   sing Y N 18  
A1A9L C9  N3   sing Y N 19  
A1A9L C10 N4   sing Y N 20  
A1A9L C10 N3   doub Y N 21  
A1A9L C3  H6   sing N N 22  
A1A9L C3  H7   sing N N 23  
A1A9L C6  H11  sing N N 24  
A1A9L C6  H10  sing N N 25  
A1A9L C9  H15  sing N N 26  
A1A9L C12 H16  sing N N 27  
A1A9L C1  H5   sing N N 28  
A1A9L C1  H4   sing N N 29  
A1A9L C13 H17  sing N N 30  
A1A9L C2  H1   sing N N 31  
A1A9L C4  H2   sing N N 32  
A1A9L C5  H9   sing N N 33  
A1A9L C5  H8   sing N N 34  
A1A9L C7  H13  sing N N 35  
A1A9L C7  H12  sing N N 36  
A1A9L N1  H14  sing N N 37  
A1A9L N4  H18  sing N N 38  
A1A9L O1  H3   sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
TFA   C1  C2   sing N N 329 
TFA   C1  O    doub N N 330 
TFA   C1  OXT  sing N N 331 
TFA   C2  F1   sing N N 332 
TFA   C2  F2   sing N N 333 
TFA   C2  F3   sing N N 334 
TFA   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TYR   N   CA   sing N N 352 
TYR   N   H    sing N N 353 
TYR   N   H2   sing N N 354 
TYR   CA  C    sing N N 355 
TYR   CA  CB   sing N N 356 
TYR   CA  HA   sing N N 357 
TYR   C   O    doub N N 358 
TYR   C   OXT  sing N N 359 
TYR   CB  CG   sing N N 360 
TYR   CB  HB2  sing N N 361 
TYR   CB  HB3  sing N N 362 
TYR   CG  CD1  doub Y N 363 
TYR   CG  CD2  sing Y N 364 
TYR   CD1 CE1  sing Y N 365 
TYR   CD1 HD1  sing N N 366 
TYR   CD2 CE2  doub Y N 367 
TYR   CD2 HD2  sing N N 368 
TYR   CE1 CZ   doub Y N 369 
TYR   CE1 HE1  sing N N 370 
TYR   CE2 CZ   sing Y N 371 
TYR   CE2 HE2  sing N N 372 
TYR   CZ  OH   sing N N 373 
TYR   OH  HH   sing N N 374 
TYR   OXT HXT  sing N N 375 
VAL   N   CA   sing N N 376 
VAL   N   H    sing N N 377 
VAL   N   H2   sing N N 378 
VAL   CA  C    sing N N 379 
VAL   CA  CB   sing N N 380 
VAL   CA  HA   sing N N 381 
VAL   C   O    doub N N 382 
VAL   C   OXT  sing N N 383 
VAL   CB  CG1  sing N N 384 
VAL   CB  CG2  sing N N 385 
VAL   CB  HB   sing N N 386 
VAL   CG1 HG11 sing N N 387 
VAL   CG1 HG12 sing N N 388 
VAL   CG1 HG13 sing N N 389 
VAL   CG2 HG21 sing N N 390 
VAL   CG2 HG22 sing N N 391 
VAL   CG2 HG23 sing N N 392 
VAL   OXT HXT  sing N N 393 
# 
_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                    7HE9 
_atom_sites.fract_transf_matrix[1][1]   0.011263 
_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]   0.011263 
_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]   0.025267 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
F 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.656 -16.257 22.292  0.66 49.67 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.610 -16.248 22.346  0.34 48.89 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.679 -15.184 22.434  0.66 49.33 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.673 -15.145 22.513  0.34 48.60 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.333 -13.835 22.149  0.66 47.88 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.342 -13.824 22.152  0.34 47.48 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.447 -13.567 22.599  0.66 48.24 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.478 -13.566 22.550  0.34 47.84 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.017 -15.210 23.828  0.66 50.12 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.106 -15.104 23.947  0.34 49.19 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 16.993 -14.091 23.956  0.66 50.24 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.102 -13.967 24.093  0.34 49.28 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.366 -16.562 24.083  0.66 50.24 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.465 -16.436 24.306  0.34 49.28 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.977 -15.312 21.779  0.66 59.17 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.927 -15.271 21.909  0.34 58.30 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.697 -15.073 24.505  0.66 60.12 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.831 -14.944 24.570  0.34 59.01 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.470 -14.234 24.761  0.66 60.26 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.638 -14.064 24.939  0.34 59.11 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.455 -13.241 24.009  0.66 60.26 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.575 -13.120 24.072  0.34 59.11 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.411 -14.106 23.180  0.66 60.26 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.466 -14.011 23.362  0.34 59.11 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.898 -16.532 24.932  0.66 60.26 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.054 -16.361 25.182  0.34 59.11 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.739 -16.750 23.367  0.66 60.26 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.792 -16.650 23.642  0.34 59.11 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.054 -17.245 24.109  0.66 60.26 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.149 -17.123 24.319  0.34 59.11 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.634 -12.994 21.389  1.00 45.81 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.090 -11.649 21.053  1.00 41.68 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 17.943 -10.668 21.278  1.00 38.23 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.827 -11.056 21.638  1.00 37.65 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.656 -11.568 19.627  1.00 40.52 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.643 -11.942 18.569  1.00 39.22 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.542 -11.393 18.524  1.00 38.87 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.013 -12.882 17.704  1.00 38.89 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.870 -13.190 21.047  0.66 54.95 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.868 -13.193 21.052  0.34 54.95 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.806 -11.408 21.655  1.00 49.99 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 19.944 -10.656 19.453  1.00 48.60 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.409 -12.172 19.549  1.00 48.60 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.477 -13.132 17.079  1.00 46.64 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.793 -13.242 17.768  1.00 46.64 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.222 -9.382  21.060  1.00 35.09 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.310 -8.309  21.436  1.00 32.00 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.427 -7.825  20.288  1.00 28.60 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.716 -6.828  20.451  1.00 28.49 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.089 -7.136  22.035  1.00 33.07 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 18.988 -6.583  21.091  1.00 33.53 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 18.948 -9.107  20.687  1.00 42.08 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.722 -8.640  22.128  1.00 38.37 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.463 -6.447  22.309  1.00 39.66 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.591 -7.449  22.806  1.00 39.66 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.414 -5.942  21.438  1.00 40.21 ?  5   SER   A HG   1 
ATOM   57   N N    . PHE   A 1 6   ? 16.442 -8.500  19.143  1.00 24.01 ?  6   PHE   A N    1 
ATOM   58   C CA   . PHE   A 1 6   ? 15.541 -8.133  18.057  1.00 20.39 ?  6   PHE   A CA   1 
ATOM   59   C C    . PHE   A 1 6   ? 14.110 -8.501  18.437  1.00 21.00 ?  6   PHE   A C    1 
ATOM   60   O O    . PHE   A 1 6   ? 13.849 -9.619  18.889  1.00 22.71 ?  6   PHE   A O    1 
ATOM   61   C CB   . PHE   A 1 6   ? 15.954 -8.854  16.780  1.00 18.57 ?  6   PHE   A CB   1 
ATOM   62   C CG   . PHE   A 1 6   ? 17.237 -8.338  16.184  1.00 17.58 ?  6   PHE   A CG   1 
ATOM   63   C CD1  . PHE   A 1 6   ? 17.254 -7.145  15.488  1.00 17.59 ?  6   PHE   A CD1  1 
ATOM   64   C CD2  . PHE   A 1 6   ? 18.414 -9.051  16.311  1.00 18.00 ?  6   PHE   A CD2  1 
ATOM   65   C CE1  . PHE   A 1 6   ? 18.429 -6.664  14.935  1.00 17.87 ?  6   PHE   A CE1  1 
ATOM   66   C CE2  . PHE   A 1 6   ? 19.588 -8.580  15.760  1.00 18.66 ?  6   PHE   A CE2  1 
ATOM   67   C CZ   . PHE   A 1 6   ? 19.595 -7.384  15.069  1.00 18.50 ?  6   PHE   A CZ   1 
ATOM   68   H H    . PHE   A 1 6   ? 16.949 -9.176  18.976  1.00 28.79 ?  6   PHE   A H    1 
ATOM   69   H HA   . PHE   A 1 6   ? 15.585 -7.180  17.907  1.00 24.44 ?  6   PHE   A HA   1 
ATOM   70   H HB2  . PHE   A 1 6   ? 16.076 -9.799  16.978  1.00 22.26 ?  6   PHE   A HB2  1 
ATOM   71   H HB3  . PHE   A 1 6   ? 15.253 -8.749  16.119  1.00 22.26 ?  6   PHE   A HB3  1 
ATOM   72   H HD1  . PHE   A 1 6   ? 16.466 -6.657  15.395  1.00 21.08 ?  6   PHE   A HD1  1 
ATOM   73   H HD2  . PHE   A 1 6   ? 18.415 -9.858  16.777  1.00 21.57 ?  6   PHE   A HD2  1 
ATOM   74   H HE1  . PHE   A 1 6   ? 18.431 -5.858  14.469  1.00 21.42 ?  6   PHE   A HE1  1 
ATOM   75   H HE2  . PHE   A 1 6   ? 20.375 -9.067  15.857  1.00 22.36 ?  6   PHE   A HE2  1 
ATOM   76   H HZ   . PHE   A 1 6   ? 20.387 -7.063  14.700  1.00 22.17 ?  6   PHE   A HZ   1 
ATOM   77   N N    A SER   A 1 7   ? 13.177 -7.572  18.212  0.66 20.74 ?  7   SER   A N    1 
ATOM   78   N N    B SER   A 1 7   ? 13.184 -7.557  18.277  0.34 20.94 ?  7   SER   A N    1 
ATOM   79   C CA   A SER   A 1 7   ? 11.804 -7.701  18.686  0.66 21.14 ?  7   SER   A CA   1 
ATOM   80   C CA   B SER   A 1 7   ? 11.834 -7.707  18.802  0.34 21.13 ?  7   SER   A CA   1 
ATOM   81   C C    A SER   A 1 7   ? 10.811 -7.481  17.551  0.66 19.29 ?  7   SER   A C    1 
ATOM   82   C C    B SER   A 1 7   ? 10.810 -7.392  17.724  0.34 19.69 ?  7   SER   A C    1 
ATOM   83   O O    A SER   A 1 7   ? 11.008 -6.609  16.700  0.66 19.18 ?  7   SER   A O    1 
ATOM   84   O O    B SER   A 1 7   ? 11.022 -6.506  16.890  0.34 19.64 ?  7   SER   A O    1 
ATOM   85   C CB   A SER   A 1 7   ? 11.535 -6.680  19.802  0.66 23.35 ?  7   SER   A CB   1 
ATOM   86   C CB   B SER   A 1 7   ? 11.613 -6.774  19.999  0.34 22.67 ?  7   SER   A CB   1 
ATOM   87   O OG   A SER   A 1 7   ? 10.176 -6.695  20.197  0.66 25.52 ?  7   SER   A OG   1 
ATOM   88   O OG   B SER   A 1 7   ? 10.351 -6.999  20.599  0.34 24.14 ?  7   SER   A OG   1 
ATOM   89   H H    A SER   A 1 7   ? 13.323 -6.847  17.773  0.66 24.86 ?  7   SER   A H    1 
ATOM   90   H H    B SER   A 1 7   ? 13.315 -6.817  17.857  0.34 25.10 ?  7   SER   A H    1 
ATOM   91   H HA   A SER   A 1 7   ? 11.667 -8.591  19.043  0.66 25.35 ?  7   SER   A HA   1 
ATOM   92   H HA   B SER   A 1 7   ? 11.695 -8.621  19.095  0.34 25.33 ?  7   SER   A HA   1 
ATOM   93   H HB2  A SER   A 1 7   ? 12.095 -6.899  20.565  0.66 28.00 ?  7   SER   A HB2  1 
ATOM   94   H HB2  B SER   A 1 7   ? 12.304 -6.941  20.658  0.34 27.18 ?  7   SER   A HB2  1 
ATOM   95   H HB3  A SER   A 1 7   ? 11.754 -5.794  19.477  0.66 28.00 ?  7   SER   A HB3  1 
ATOM   96   H HB3  B SER   A 1 7   ? 11.662 -5.854  19.693  0.34 27.18 ?  7   SER   A HB3  1 
ATOM   97   H HG   A SER   A 1 7   ? 10.051 -6.141  20.816  0.66 30.60 ?  7   SER   A HG   1 
ATOM   98   H HG   B SER   A 1 7   ? 10.244 -6.475  21.247  0.34 28.94 ?  7   SER   A HG   1 
ATOM   99   N N    A GLY   A 1 8   ? 9.737  -8.274  17.550  0.66 17.55 ?  8   GLY   A N    1 
ATOM   100  N N    B GLY   A 1 8   ? 9.696  -8.124  17.745  0.34 18.20 ?  8   GLY   A N    1 
ATOM   101  C CA   A GLY   A 1 8   ? 8.639  -8.053  16.630  0.66 16.88 ?  8   GLY   A CA   1 
ATOM   102  C CA   B GLY   A 1 8   ? 8.607  -7.853  16.833  0.34 17.31 ?  8   GLY   A CA   1 
ATOM   103  C C    A GLY   A 1 8   ? 8.852  -8.549  15.219  0.66 15.76 ?  8   GLY   A C    1 
ATOM   104  C C    B GLY   A 1 8   ? 8.798  -8.377  15.431  0.34 15.78 ?  8   GLY   A C    1 
ATOM   105  O O    A GLY   A 1 8   ? 8.120  -8.130  14.316  0.66 16.42 ?  8   GLY   A O    1 
ATOM   106  O O    B GLY   A 1 8   ? 8.026  -8.005  14.541  0.34 15.99 ?  8   GLY   A O    1 
ATOM   107  H H    A GLY   A 1 8   ? 9.631  -8.945  18.075  0.66 21.04 ?  8   GLY   A H    1 
ATOM   108  H H    B GLY   A 1 8   ? 9.558  -8.791  18.276  0.34 21.81 ?  8   GLY   A H    1 
ATOM   109  H HA2  A GLY   A 1 8   ? 7.846  -8.486  16.987  0.66 20.22 ?  8   GLY   A HA2  1 
ATOM   110  H HA2  B GLY   A 1 8   ? 7.795  -8.247  17.183  0.34 20.74 ?  8   GLY   A HA2  1 
ATOM   111  H HA3  A GLY   A 1 8   ? 8.460  -7.102  16.581  0.66 20.22 ?  8   GLY   A HA3  1 
ATOM   112  H HA3  B GLY   A 1 8   ? 8.478  -6.893  16.778  0.34 20.74 ?  8   GLY   A HA3  1 
ATOM   113  N N    A TYR   A 1 9   ? 9.825  -9.429  14.995  0.66 14.54 ?  9   TYR   A N    1 
ATOM   114  N N    B TYR   A 1 9   ? 9.795  -9.227  15.204  0.34 14.50 ?  9   TYR   A N    1 
ATOM   115  C CA   A TYR   A 1 9   ? 10.093 -9.960  13.666  0.66 13.54 ?  9   TYR   A CA   1 
ATOM   116  C CA   B TYR   A 1 9   ? 10.038 -9.769  13.877  0.34 13.75 ?  9   TYR   A CA   1 
ATOM   117  C C    A TYR   A 1 9   ? 9.244  -11.192 13.386  0.66 13.02 ?  9   TYR   A C    1 
ATOM   118  C C    B TYR   A 1 9   ? 9.147  -10.974 13.606  0.34 13.29 ?  9   TYR   A C    1 
ATOM   119  O O    A TYR   A 1 9   ? 8.996  -12.016 14.274  0.66 13.81 ?  9   TYR   A O    1 
ATOM   120  O O    B TYR   A 1 9   ? 8.809  -11.747 14.508  0.34 14.08 ?  9   TYR   A O    1 
ATOM   121  C CB   A TYR   A 1 9   ? 11.576 -10.317 13.502  0.66 13.57 ?  9   TYR   A CB   1 
ATOM   122  C CB   B TYR   A 1 9   ? 11.497 -10.207 13.730  0.34 14.24 ?  9   TYR   A CB   1 
ATOM   123  C CG   A TYR   A 1 9   ? 12.463 -9.103  13.350  0.66 13.77 ?  9   TYR   A CG   1 
ATOM   124  C CG   B TYR   A 1 9   ? 12.460 -9.067  13.521  0.34 14.24 ?  9   TYR   A CG   1 
ATOM   125  C CD1  A TYR   A 1 9   ? 12.780 -8.317  14.445  0.66 14.38 ?  9   TYR   A CD1  1 
ATOM   126  C CD1  B TYR   A 1 9   ? 12.817 -8.239  14.571  0.34 14.77 ?  9   TYR   A CD1  1 
ATOM   127  C CD2  A TYR   A 1 9   ? 12.960 -8.729  12.107  0.66 14.01 ?  9   TYR   A CD2  1 
ATOM   128  C CD2  B TYR   A 1 9   ? 13.009 -8.816  12.270  0.34 14.08 ?  9   TYR   A CD2  1 
ATOM   129  C CE1  A TYR   A 1 9   ? 13.575 -7.191  14.313  0.66 15.25 ?  9   TYR   A CE1  1 
ATOM   130  C CE1  B TYR   A 1 9   ? 13.693 -7.192  14.386  0.34 15.10 ?  9   TYR   A CE1  1 
ATOM   131  C CE2  A TYR   A 1 9   ? 13.758 -7.605  11.962  0.66 14.12 ?  9   TYR   A CE2  1 
ATOM   132  C CE2  B TYR   A 1 9   ? 13.883 -7.769  12.073  0.34 14.38 ?  9   TYR   A CE2  1 
ATOM   133  C CZ   A TYR   A 1 9   ? 14.059 -6.839  13.066  0.66 14.80 ?  9   TYR   A CZ   1 
ATOM   134  C CZ   B TYR   A 1 9   ? 14.222 -6.960  13.134  0.34 15.09 ?  9   TYR   A CZ   1 
ATOM   135  O OH   A TYR   A 1 9   ? 14.843 -5.721  12.920  0.66 15.90 ?  9   TYR   A OH   1 
ATOM   136  O OH   B TYR   A 1 9   ? 15.095 -5.919  12.944  0.34 15.91 ?  9   TYR   A OH   1 
ATOM   137  H H    A TYR   A 1 9   ? 10.348 -9.738  15.605  0.66 17.42 ?  9   TYR   A H    1 
ATOM   138  H H    B TYR   A 1 9   ? 10.346 -9.505  15.807  0.34 17.38 ?  9   TYR   A H    1 
ATOM   139  H HA   A TYR   A 1 9   ? 9.874  -9.289  13.003  0.66 16.22 ?  9   TYR   A HA   1 
ATOM   140  H HA   B TYR   A 1 9   ? 9.856  -9.087  13.210  0.34 16.47 ?  9   TYR   A HA   1 
ATOM   141  H HB2  A TYR   A 1 9   ? 11.875 -10.817 14.279  0.66 16.26 ?  9   TYR   A HB2  1 
ATOM   142  H HB2  B TYR   A 1 9   ? 11.769 -10.678 14.533  0.34 17.06 ?  9   TYR   A HB2  1 
ATOM   143  H HB3  A TYR   A 1 9   ? 11.671 -10.860 12.704  0.66 16.26 ?  9   TYR   A HB3  1 
ATOM   144  H HB3  B TYR   A 1 9   ? 11.570 -10.797 12.963  0.34 17.06 ?  9   TYR   A HB3  1 
ATOM   145  H HD1  A TYR   A 1 9   ? 12.447 -8.550  15.286  0.66 17.23 ?  9   TYR   A HD1  1 
ATOM   146  H HD1  B TYR   A 1 9   ? 12.457 -8.393  15.416  0.34 17.69 ?  9   TYR   A HD1  1 
ATOM   147  H HD2  A TYR   A 1 9   ? 12.753 -9.242  11.360  0.66 16.78 ?  9   TYR   A HD2  1 
ATOM   148  H HD2  B TYR   A 1 9   ? 12.782 -9.362  11.551  0.34 16.87 ?  9   TYR   A HD2  1 
ATOM   149  H HE1  A TYR   A 1 9   ? 13.778 -6.675  15.060  0.66 18.27 ?  9   TYR   A HE1  1 
ATOM   150  H HE1  B TYR   A 1 9   ? 13.918 -6.644  15.102  0.34 18.09 ?  9   TYR   A HE1  1 
ATOM   151  H HE2  A TYR   A 1 9   ? 14.085 -7.369  11.124  0.66 16.92 ?  9   TYR   A HE2  1 
ATOM   152  H HE2  B TYR   A 1 9   ? 14.244 -7.613  11.231  0.34 17.23 ?  9   TYR   A HE2  1 
ATOM   153  H HH   A TYR   A 1 9   ? 14.963 -5.354  13.668  0.66 19.06 ?  9   TYR   A HH   1 
ATOM   154  H HH   B TYR   A 1 9   ? 15.205 -5.514  13.671  0.34 19.07 ?  9   TYR   A HH   1 
ATOM   155  N N    A LEU   A 1 10  ? 8.827  -11.322 12.132  0.66 12.88 ?  10  LEU   A N    1 
ATOM   156  N N    B LEU   A 1 10  ? 8.761  -11.119 12.343  0.34 12.83 ?  10  LEU   A N    1 
ATOM   157  C CA   A LEU   A 1 10  ? 8.210  -12.540 11.632  0.66 12.76 ?  10  LEU   A CA   1 
ATOM   158  C CA   B LEU   A 1 10  ? 8.218  -12.374 11.852  0.34 12.96 ?  10  LEU   A CA   1 
ATOM   159  C C    A LEU   A 1 10  ? 9.326  -13.471 11.176  0.66 12.49 ?  10  LEU   A C    1 
ATOM   160  C C    B LEU   A 1 10  ? 9.361  -13.298 11.450  0.34 12.74 ?  10  LEU   A C    1 
ATOM   161  O O    A LEU   A 1 10  ? 10.257 -13.039 10.488  0.66 12.02 ?  10  LEU   A O    1 
ATOM   162  O O    B LEU   A 1 10  ? 10.406 -12.854 10.969  0.34 11.99 ?  10  LEU   A O    1 
ATOM   163  C CB   A LEU   A 1 10  ? 7.297  -12.200 10.456  0.66 14.25 ?  10  LEU   A CB   1 
ATOM   164  C CB   B LEU   A 1 10  ? 7.324  -12.126 10.640  0.34 13.29 ?  10  LEU   A CB   1 
ATOM   165  C CG   A LEU   A 1 10  ? 6.588  -13.377 9.797   0.66 16.99 ?  10  LEU   A CG   1 
ATOM   166  C CG   B LEU   A 1 10  ? 5.939  -11.553 10.923  0.34 15.02 ?  10  LEU   A CG   1 
ATOM   167  C CD1  A LEU   A 1 10  ? 5.517  -13.931 10.721  0.66 18.68 ?  10  LEU   A CD1  1 
ATOM   168  C CD1  B LEU   A 1 10  ? 5.164  -11.384 9.627   0.34 15.61 ?  10  LEU   A CD1  1 
ATOM   169  C CD2  A LEU   A 1 10  ? 6.008  -12.964 8.452   0.66 18.73 ?  10  LEU   A CD2  1 
ATOM   170  C CD2  B LEU   A 1 10  ? 5.187  -12.456 11.889  0.34 15.24 ?  10  LEU   A CD2  1 
ATOM   171  H H    A LEU   A 1 10  ? 8.912  -10.714 11.524  0.66 15.43 ?  10  LEU   A H    1 
ATOM   172  H H    B LEU   A 1 10  ? 8.802  -10.493 11.750  0.34 15.37 ?  10  LEU   A H    1 
ATOM   173  H HA   A LEU   A 1 10  ? 7.694  -12.972 12.331  0.66 15.28 ?  10  LEU   A HA   1 
ATOM   174  H HA   B LEU   A 1 10  ? 7.702  -12.802 12.555  0.34 15.52 ?  10  LEU   A HA   1 
ATOM   175  H HB2  A LEU   A 1 10  ? 6.610  -11.590 10.768  0.66 17.07 ?  10  LEU   A HB2  1 
ATOM   176  H HB2  B LEU   A 1 10  ? 7.776  -11.504 10.049  0.34 15.92 ?  10  LEU   A HB2  1 
ATOM   177  H HB3  A LEU   A 1 10  ? 7.827  -11.765 9.770   0.66 17.07 ?  10  LEU   A HB3  1 
ATOM   178  H HB3  B LEU   A 1 10  ? 7.194  -12.969 10.182  0.34 15.92 ?  10  LEU   A HB3  1 
ATOM   179  H HG   A LEU   A 1 10  ? 7.231  -14.085 9.636   0.66 20.36 ?  10  LEU   A HG   1 
ATOM   180  H HG   B LEU   A 1 10  ? 6.033  -10.677 11.332  0.34 18.00 ?  10  LEU   A HG   1 
ATOM   181  H HD11 A LEU   A 1 10  ? 5.080  -14.682 10.287  0.66 22.39 ?  10  LEU   A HD11 1 
ATOM   182  H HD11 B LEU   A 1 10  ? 4.285  -11.025 9.828   0.34 18.71 ?  10  LEU   A HD11 1 
ATOM   183  H HD12 A LEU   A 1 10  ? 5.930  -14.226 11.549  0.66 22.39 ?  10  LEU   A HD12 1 
ATOM   184  H HD12 B LEU   A 1 10  ? 5.645  -10.776 9.045   0.34 18.71 ?  10  LEU   A HD12 1 
ATOM   185  H HD13 A LEU   A 1 10  ? 4.866  -13.236 10.907  0.66 22.39 ?  10  LEU   A HD13 1 
ATOM   186  H HD13 B LEU   A 1 10  ? 5.076  -12.251 9.198   0.34 18.71 ?  10  LEU   A HD13 1 
ATOM   187  H HD21 A LEU   A 1 10  ? 5.558  -13.727 8.057   0.66 22.45 ?  10  LEU   A HD21 1 
ATOM   188  H HD21 B LEU   A 1 10  ? 4.245  -12.236 11.858  0.34 18.27 ?  10  LEU   A HD21 1 
ATOM   189  H HD22 A LEU   A 1 10  ? 5.378  -12.241 8.590   0.66 22.45 ?  10  LEU   A HD22 1 
ATOM   190  H HD22 B LEU   A 1 10  ? 5.325  -13.379 11.625  0.34 18.27 ?  10  LEU   A HD22 1 
ATOM   191  H HD23 A LEU   A 1 10  ? 6.731  -12.671 7.876   0.66 22.45 ?  10  LEU   A HD23 1 
ATOM   192  H HD23 B LEU   A 1 10  ? 5.533  -12.314 12.785  0.34 18.27 ?  10  LEU   A HD23 1 
ATOM   193  N N    A LYS   A 1 11  ? 9.248  -14.734 11.583  0.66 13.24 ?  11  LYS   A N    1 
ATOM   194  N N    B LYS   A 1 11  ? 9.155  -14.595 11.653  0.34 13.35 ?  11  LYS   A N    1 
ATOM   195  C CA   A LYS   A 1 11  ? 10.232 -15.729 11.184  0.66 13.42 ?  11  LYS   A CA   1 
ATOM   196  C CA   B LYS   A 1 11  ? 10.184 -15.605 11.419  0.34 13.36 ?  11  LYS   A CA   1 
ATOM   197  C C    A LYS   A 1 11  ? 9.842  -16.271 9.817   0.66 13.07 ?  11  LYS   A C    1 
ATOM   198  C C    B LYS   A 1 11  ? 9.905  -16.281 10.081  0.34 13.15 ?  11  LYS   A C    1 
ATOM   199  O O    A LYS   A 1 11  ? 8.711  -16.736 9.634   0.66 13.84 ?  11  LYS   A O    1 
ATOM   200  O O    B LYS   A 1 11  ? 9.053  -17.169 9.984   0.34 13.48 ?  11  LYS   A O    1 
ATOM   201  C CB   A LYS   A 1 11  ? 10.269 -16.839 12.234  0.66 12.79 ?  11  LYS   A CB   1 
ATOM   202  C CB   B LYS   A 1 11  ? 10.206 -16.607 12.568  0.34 12.92 ?  11  LYS   A CB   1 
ATOM   203  C CG   A LYS   A 1 11  ? 11.288 -17.947 12.005  0.66 12.93 ?  11  LYS   A CG   1 
ATOM   204  C CG   B LYS   A 1 11  ? 11.219 -17.721 12.406  0.34 12.89 ?  11  LYS   A CG   1 
ATOM   205  C CD   A LYS   A 1 11  ? 11.369 -18.826 13.256  0.66 13.40 ?  11  LYS   A CD   1 
ATOM   206  C CD   B LYS   A 1 11  ? 11.334 -18.539 13.684  0.34 13.12 ?  11  LYS   A CD   1 
ATOM   207  C CE   A LYS   A 1 11  ? 12.371 -19.966 13.135  0.66 13.62 ?  11  LYS   A CE   1 
ATOM   208  C CE   B LYS   A 1 11  ? 12.279 -19.721 13.517  0.34 13.17 ?  11  LYS   A CE   1 
ATOM   209  N NZ   A LYS   A 1 11  ? 13.759 -19.496 12.893  0.66 14.22 ?  11  LYS   A NZ   1 
ATOM   210  N NZ   B LYS   A 1 11  ? 13.667 -19.282 13.210  0.34 13.20 ?  11  LYS   A NZ   1 
ATOM   211  H H    A LYS   A 1 11  ? 8.622  -15.042 12.093  0.66 15.86 ?  11  LYS   A H    1 
ATOM   212  H H    B LYS   A 1 11  ? 8.408  -14.917 11.928  0.34 16.00 ?  11  LYS   A H    1 
ATOM   213  H HA   A LYS   A 1 11  ? 11.106 -15.320 11.120  0.66 16.08 ?  11  LYS   A HA   1 
ATOM   214  H HA   B LYS   A 1 11  ? 11.050 -15.174 11.371  0.34 16.01 ?  11  LYS   A HA   1 
ATOM   215  H HB2  A LYS   A 1 11  ? 10.474 -16.437 13.093  0.66 15.32 ?  11  LYS   A HB2  1 
ATOM   216  H HB2  B LYS   A 1 11  ? 10.422 -16.128 13.384  0.34 15.47 ?  11  LYS   A HB2  1 
ATOM   217  H HB3  A LYS   A 1 11  ? 9.396  -17.255 12.273  0.66 15.32 ?  11  LYS   A HB3  1 
ATOM   218  H HB3  B LYS   A 1 11  ? 9.327  -17.007 12.649  0.34 15.47 ?  11  LYS   A HB3  1 
ATOM   219  H HG2  A LYS   A 1 11  ? 11.010 -18.502 11.257  0.66 15.49 ?  11  LYS   A HG2  1 
ATOM   220  H HG2  B LYS   A 1 11  ? 10.933 -18.310 11.690  0.34 15.44 ?  11  LYS   A HG2  1 
ATOM   221  H HG3  A LYS   A 1 11  ? 12.163 -17.566 11.841  0.66 15.49 ?  11  LYS   A HG3  1 
ATOM   222  H HG3  B LYS   A 1 11  ? 12.087 -17.339 12.205  0.34 15.44 ?  11  LYS   A HG3  1 
ATOM   223  H HD2  A LYS   A 1 11  ? 11.633 -18.278 14.009  0.66 16.05 ?  11  LYS   A HD2  1 
ATOM   224  H HD2  B LYS   A 1 11  ? 11.677 -17.972 14.394  0.34 15.72 ?  11  LYS   A HD2  1 
ATOM   225  H HD3  A LYS   A 1 11  ? 10.496 -19.218 13.421  0.66 16.05 ?  11  LYS   A HD3  1 
ATOM   226  H HD3  B LYS   A 1 11  ? 10.458 -18.880 13.924  0.34 15.72 ?  11  LYS   A HD3  1 
ATOM   227  H HE2  A LYS   A 1 11  ? 12.369 -20.480 13.960  0.66 16.32 ?  11  LYS   A HE2  1 
ATOM   228  H HE2  B LYS   A 1 11  ? 12.300 -20.233 14.341  0.34 15.78 ?  11  LYS   A HE2  1 
ATOM   229  H HE3  A LYS   A 1 11  ? 12.117 -20.535 12.393  0.66 16.32 ?  11  LYS   A HE3  1 
ATOM   230  H HE3  B LYS   A 1 11  ? 11.970 -20.278 12.785  0.34 15.78 ?  11  LYS   A HE3  1 
ATOM   231  H HZ1  A LYS   A 1 11  ? 14.308 -20.194 12.821  0.66 17.04 ?  11  LYS   A HZ1  1 
ATOM   232  H HZ1  B LYS   A 1 11  ? 14.198 -19.990 13.126  0.34 15.81 ?  11  LYS   A HZ1  1 
ATOM   233  H HZ2  A LYS   A 1 11  ? 13.792 -19.021 12.143  0.66 17.04 ?  11  LYS   A HZ2  1 
ATOM   234  H HZ2  B LYS   A 1 11  ? 13.677 -18.820 12.450  0.34 15.81 ?  11  LYS   A HZ2  1 
ATOM   235  H HZ3  A LYS   A 1 11  ? 14.029 -18.987 13.572  0.66 17.04 ?  11  LYS   A HZ3  1 
ATOM   236  H HZ3  B LYS   A 1 11  ? 13.974 -18.766 13.867  0.34 15.81 ?  11  LYS   A HZ3  1 
ATOM   237  N N    A LEU   A 1 12  ? 10.758 -16.193 8.851   0.66 12.03 ?  12  LEU   A N    1 
ATOM   238  N N    B LEU   A 1 12  ? 10.634 -15.863 9.044   0.34 12.90 ?  12  LEU   A N    1 
ATOM   239  C CA   A LEU   A 1 12  ? 10.521 -16.774 7.531   0.66 12.18 ?  12  LEU   A CA   1 
ATOM   240  C CA   B LEU   A 1 12  ? 10.393 -16.402 7.709   0.34 12.60 ?  12  LEU   A CA   1 
ATOM   241  C C    A LEU   A 1 12  ? 11.115 -18.166 7.380   0.66 12.21 ?  12  LEU   A C    1 
ATOM   242  C C    B LEU   A 1 12  ? 10.941 -17.817 7.564   0.34 12.59 ?  12  LEU   A C    1 
ATOM   243  O O    A LEU   A 1 12  ? 10.493 -19.034 6.763   0.66 12.80 ?  12  LEU   A O    1 
ATOM   244  O O    B LEU   A 1 12  ? 10.262 -18.702 7.033   0.34 12.50 ?  12  LEU   A O    1 
ATOM   245  C CB   A LEU   A 1 12  ? 11.079 -15.875 6.421   0.66 12.85 ?  12  LEU   A CB   1 
ATOM   246  C CB   B LEU   A 1 12  ? 10.991 -15.481 6.644   0.34 13.13 ?  12  LEU   A CB   1 
ATOM   247  C CG   A LEU   A 1 12  ? 10.439 -14.501 6.245   0.66 13.94 ?  12  LEU   A CG   1 
ATOM   248  C CG   B LEU   A 1 12  ? 10.281 -14.143 6.437   0.34 13.74 ?  12  LEU   A CG   1 
ATOM   249  C CD1  A LEU   A 1 12  ? 11.198 -13.719 5.189   0.66 14.41 ?  12  LEU   A CD1  1 
ATOM   250  C CD1  B LEU   A 1 12  ? 10.884 -13.388 5.261   0.34 13.94 ?  12  LEU   A CD1  1 
ATOM   251  C CD2  A LEU   A 1 12  ? 8.969  -14.635 5.865   0.66 14.93 ?  12  LEU   A CD2  1 
ATOM   252  C CD2  B LEU   A 1 12  ? 8.794  -14.361 6.226   0.34 14.00 ?  12  LEU   A CD2  1 
ATOM   253  H H    A LEU   A 1 12  ? 11.526 -15.814 8.939   0.66 14.41 ?  12  LEU   A H    1 
ATOM   254  H H    B LEU   A 1 12  ? 11.256 -15.266 9.086   0.34 15.45 ?  12  LEU   A H    1 
ATOM   255  H HA   A LEU   A 1 12  ? 9.567  -16.854 7.399   0.66 14.59 ?  12  LEU   A HA   1 
ATOM   256  H HA   B LEU   A 1 12  ? 9.437  -16.450 7.569   0.34 15.09 ?  12  LEU   A HA   1 
ATOM   257  H HB2  A LEU   A 1 12  ? 12.020 -15.733 6.593   0.66 15.40 ?  12  LEU   A HB2  1 
ATOM   258  H HB2  B LEU   A 1 12  ? 11.909 -15.287 6.889   0.34 15.73 ?  12  LEU   A HB2  1 
ATOM   259  H HB3  A LEU   A 1 12  ? 10.975 -16.346 5.578   0.66 15.40 ?  12  LEU   A HB3  1 
ATOM   260  H HB3  B LEU   A 1 12  ? 10.976 -15.950 5.795   0.34 15.73 ?  12  LEU   A HB3  1 
ATOM   261  H HG   A LEU   A 1 12  ? 10.494 -14.014 7.082   0.66 16.70 ?  12  LEU   A HG   1 
ATOM   262  H HG   B LEU   A 1 12  ? 10.395 -13.597 7.231   0.34 16.46 ?  12  LEU   A HG   1 
ATOM   263  H HD11 A LEU   A 1 12  ? 10.786 -12.849 5.081   0.66 17.26 ?  12  LEU   A HD11 1 
ATOM   264  H HD11 B LEU   A 1 12  ? 10.423 -12.539 5.160   0.34 16.70 ?  12  LEU   A HD11 1 
ATOM   265  H HD12 A LEU   A 1 12  ? 12.121 -13.616 5.476   0.66 17.26 ?  12  LEU   A HD12 1 
ATOM   266  H HD12 B LEU   A 1 12  ? 11.826 -13.234 5.433   0.34 16.70 ?  12  LEU   A HD12 1 
ATOM   267  H HD13 A LEU   A 1 12  ? 11.167 -14.208 4.351   0.66 17.26 ?  12  LEU   A HD13 1 
ATOM   268  H HD13 B LEU   A 1 12  ? 10.777 -13.919 4.456   0.34 16.70 ?  12  LEU   A HD13 1 
ATOM   269  H HD21 A LEU   A 1 12  ? 8.610  -13.756 5.668   0.66 17.89 ?  12  LEU   A HD21 1 
ATOM   270  H HD21 B LEU   A 1 12  ? 8.412  -13.566 5.827   0.34 16.77 ?  12  LEU   A HD21 1 
ATOM   271  H HD22 A LEU   A 1 12  ? 8.894  -15.204 5.083   0.66 17.89 ?  12  LEU   A HD22 1 
ATOM   272  H HD22 B LEU   A 1 12  ? 8.670  -15.122 5.637   0.34 16.77 ?  12  LEU   A HD22 1 
ATOM   273  H HD23 A LEU   A 1 12  ? 8.482  -15.030 6.607   0.66 17.89 ?  12  LEU   A HD23 1 
ATOM   274  H HD23 B LEU   A 1 12  ? 8.378  -14.536 7.085   0.34 16.77 ?  12  LEU   A HD23 1 
ATOM   275  N N    A THR   A 1 13  ? 12.318 -18.380 7.905   0.66 12.44 ?  13  THR   A N    1 
ATOM   276  N N    B THR   A 1 13  ? 12.177 -18.039 8.001   0.34 12.75 ?  13  THR   A N    1 
ATOM   277  C CA   A THR   A 1 13  ? 13.020 -19.655 7.815   0.66 12.66 ?  13  THR   A CA   1 
ATOM   278  C CA   B THR   A 1 13  ? 12.812 -19.347 7.918   0.34 12.66 ?  13  THR   A CA   1 
ATOM   279  C C    A THR   A 1 13  ? 13.798 -19.862 9.108   0.66 13.01 ?  13  THR   A C    1 
ATOM   280  C C    B THR   A 1 13  ? 13.582 -19.589 9.210   0.34 13.09 ?  13  THR   A C    1 
ATOM   281  O O    A THR   A 1 13  ? 13.705 -19.075 10.055  0.66 13.03 ?  13  THR   A O    1 
ATOM   282  O O    B THR   A 1 13  ? 13.493 -18.821 10.173  0.34 13.50 ?  13  THR   A O    1 
ATOM   283  C CB   A THR   A 1 13  ? 14.002 -19.693 6.634   0.66 13.81 ?  13  THR   A CB   1 
ATOM   284  C CB   B THR   A 1 13  ? 13.750 -19.439 6.706   0.34 12.79 ?  13  THR   A CB   1 
ATOM   285  O OG1  A THR   A 1 13  ? 15.080 -18.787 6.888   0.66 13.72 ?  13  THR   A OG1  1 
ATOM   286  O OG1  B THR   A 1 13  ? 14.826 -18.511 6.870   0.34 12.63 ?  13  THR   A OG1  1 
ATOM   287  C CG2  A THR   A 1 13  ? 13.338 -19.326 5.318   0.66 14.70 ?  13  THR   A CG2  1 
ATOM   288  C CG2  B THR   A 1 13  ? 13.013 -19.142 5.401   0.34 13.42 ?  13  THR   A CG2  1 
ATOM   289  H H    A THR   A 1 13  ? 12.768 -17.782 8.324   0.66 14.90 ?  13  THR   A H    1 
ATOM   290  H H    B THR   A 1 13  ? 12.677 -17.430 8.345   0.34 15.27 ?  13  THR   A H    1 
ATOM   291  H HA   A THR   A 1 13  ? 12.381 -20.380 7.713   0.66 15.16 ?  13  THR   A HA   1 
ATOM   292  H HA   B THR   A 1 13  ? 12.131 -20.031 7.830   0.34 15.17 ?  13  THR   A HA   1 
ATOM   293  H HB   A THR   A 1 13  ? 14.359 -20.593 6.546   0.66 16.54 ?  13  THR   A HB   1 
ATOM   294  H HB   B THR   A 1 13  ? 14.113 -20.338 6.649   0.34 15.32 ?  13  THR   A HB   1 
ATOM   295  H HG1  A THR   A 1 13  ? 15.624 -18.801 6.242   0.66 16.44 ?  13  THR   A HG1  1 
ATOM   296  H HG1  B THR   A 1 13  ? 15.343 -18.552 6.207   0.34 15.13 ?  13  THR   A HG1  1 
ATOM   297  H HG21 A THR   A 1 13  ? 13.962 -19.462 4.585   0.66 17.61 ?  13  THR   A HG21 1 
ATOM   298  H HG21 B THR   A 1 13  ? 13.616 -19.260 4.647   0.34 16.08 ?  13  THR   A HG21 1 
ATOM   299  H HG22 A THR   A 1 13  ? 12.559 -19.885 5.173   0.66 17.61 ?  13  THR   A HG22 1 
ATOM   300  H HG22 B THR   A 1 13  ? 12.263 -19.749 5.298   0.34 16.08 ?  13  THR   A HG22 1 
ATOM   301  H HG23 A THR   A 1 13  ? 13.065 -18.398 5.332   0.66 17.61 ?  13  THR   A HG23 1 
ATOM   302  H HG23 B THR   A 1 13  ? 12.687 -18.231 5.402   0.34 16.08 ?  13  THR   A HG23 1 
ATOM   303  N N    A ASP   A 1 14  ? 14.614 -20.916 9.129   0.66 13.70 ?  14  ASP   A N    1 
ATOM   304  N N    B ASP   A 1 14  ? 14.362 -20.670 9.210   0.34 13.17 ?  14  ASP   A N    1 
ATOM   305  C CA   A ASP   A 1 14  ? 15.453 -21.175 10.292  0.66 14.45 ?  14  ASP   A CA   1 
ATOM   306  C CA   B ASP   A 1 14  ? 15.215 -20.983 10.348  0.34 14.00 ?  14  ASP   A CA   1 
ATOM   307  C C    A ASP   A 1 14  ? 16.287 -19.962 10.692  0.66 14.03 ?  14  ASP   A C    1 
ATOM   308  C C    B ASP   A 1 14  ? 16.093 -19.796 10.725  0.34 13.66 ?  14  ASP   A C    1 
ATOM   309  O O    A ASP   A 1 14  ? 16.585 -19.782 11.878  0.66 14.55 ?  14  ASP   A O    1 
ATOM   310  O O    B ASP   A 1 14  ? 16.244 -19.477 11.911  0.34 13.84 ?  14  ASP   A O    1 
ATOM   311  C CB   A ASP   A 1 14  ? 16.385 -22.350 10.007  0.66 17.23 ?  14  ASP   A CB   1 
ATOM   312  C CB   B ASP   A 1 14  ? 16.085 -22.189 9.997   0.34 15.85 ?  14  ASP   A CB   1 
ATOM   313  C CG   A ASP   A 1 14  ? 17.359 -22.586 11.132  0.66 20.86 ?  14  ASP   A CG   1 
ATOM   314  C CG   B ASP   A 1 14  ? 16.947 -22.643 11.153  0.34 17.66 ?  14  ASP   A CG   1 
ATOM   315  O OD1  A ASP   A 1 14  ? 16.913 -22.981 12.229  0.66 22.15 ?  14  ASP   A OD1  1 
ATOM   316  O OD1  B ASP   A 1 14  ? 16.393 -23.076 12.186  0.34 17.79 ?  14  ASP   A OD1  1 
ATOM   317  O OD2  A ASP   A 1 14  ? 18.567 -22.347 10.920  0.66 23.40 -1 14  ASP   A OD2  1 
ATOM   318  O OD2  B ASP   A 1 14  ? 18.182 -22.577 11.023  0.34 19.40 -1 14  ASP   A OD2  1 
ATOM   319  H H    A ASP   A 1 14  ? 14.709 -21.487 8.487   0.66 16.41 ?  14  ASP   A H    1 
ATOM   320  H H    B ASP   A 1 14  ? 14.420 -21.223 8.562   0.34 15.78 ?  14  ASP   A H    1 
ATOM   321  H HA   A ASP   A 1 14  ? 14.891 -21.415 11.045  0.66 17.32 ?  14  ASP   A HA   1 
ATOM   322  H HA   B ASP   A 1 14  ? 14.665 -21.214 11.114  0.34 16.78 ?  14  ASP   A HA   1 
ATOM   323  H HB2  A ASP   A 1 14  ? 15.843 -23.157 9.868   0.66 20.65 ?  14  ASP   A HB2  1 
ATOM   324  H HB2  B ASP   A 1 14  ? 15.510 -22.929 9.740   0.34 18.99 ?  14  ASP   A HB2  1 
ATOM   325  H HB3  A ASP   A 1 14  ? 16.906 -22.169 9.218   0.66 20.65 ?  14  ASP   A HB3  1 
ATOM   326  H HB3  B ASP   A 1 14  ? 16.669 -21.955 9.259   0.34 18.99 ?  14  ASP   A HB3  1 
ATOM   327  N N    . ASN   A 1 15  ? 16.675 -19.122 9.729   1.00 13.42 ?  15  ASN   A N    1 
ATOM   328  C CA   . ASN   A 1 15  ? 17.667 -18.081 9.978   1.00 13.92 ?  15  ASN   A CA   1 
ATOM   329  C C    . ASN   A 1 15  ? 17.297 -16.689 9.484   1.00 14.11 ?  15  ASN   A C    1 
ATOM   330  O O    . ASN   A 1 15  ? 18.070 -15.761 9.732   1.00 15.28 ?  15  ASN   A O    1 
ATOM   331  C CB   . ASN   A 1 15  ? 19.034 -18.485 9.390   1.00 13.48 ?  15  ASN   A CB   1 
ATOM   332  C CG   . ASN   A 1 15  ? 19.018 -18.556 7.880   1.00 13.85 ?  15  ASN   A CG   1 
ATOM   333  O OD1  . ASN   A 1 15  ? 18.288 -19.363 7.288   1.00 15.19 ?  15  ASN   A OD1  1 
ATOM   334  N ND2  . ASN   A 1 15  ? 19.814 -17.701 7.240   1.00 14.05 ?  15  ASN   A ND2  1 
ATOM   335  H H    A ASN   A 1 15  ? 16.366 -19.133 8.931   0.66 16.08 ?  15  ASN   A H    1 
ATOM   336  H H    B ASN   A 1 15  ? 16.509 -19.259 8.900   0.34 16.08 ?  15  ASN   A H    1 
ATOM   337  H HA   . ASN   A 1 15  ? 17.793 -18.004 10.932  1.00 16.68 ?  15  ASN   A HA   1 
ATOM   338  H HB2  . ASN   A 1 15  ? 19.701 -17.828 9.658   1.00 16.15 ?  15  ASN   A HB2  1 
ATOM   339  H HB3  . ASN   A 1 15  ? 19.282 -19.361 9.731   1.00 16.15 ?  15  ASN   A HB3  1 
ATOM   340  H HD21 . ASN   A 1 15  ? 19.839 -17.693 6.381   1.00 16.84 ?  15  ASN   A HD21 1 
ATOM   341  H HD22 . ASN   A 1 15  ? 20.304 -17.144 7.685   1.00 16.84 ?  15  ASN   A HD22 1 
ATOM   342  N N    A VAL   A 1 16  ? 16.177 -16.516 8.781   0.66 13.24 ?  16  VAL   A N    1 
ATOM   343  N N    B VAL   A 1 16  ? 16.142 -16.499 8.849   0.34 13.68 ?  16  VAL   A N    1 
ATOM   344  C CA   A VAL   A 1 16  ? 15.792 -15.231 8.208   0.66 13.37 ?  16  VAL   A CA   1 
ATOM   345  C CA   B VAL   A 1 16  ? 15.755 -15.210 8.284   0.34 13.36 ?  16  VAL   A CA   1 
ATOM   346  C C    A VAL   A 1 16  ? 14.508 -14.747 8.864   0.66 12.41 ?  16  VAL   A C    1 
ATOM   347  C C    B VAL   A 1 16  ? 14.520 -14.688 9.014   0.34 13.01 ?  16  VAL   A C    1 
ATOM   348  O O    A VAL   A 1 16  ? 13.494 -15.460 8.886   0.66 12.43 ?  16  VAL   A O    1 
ATOM   349  O O    B VAL   A 1 16  ? 13.543 -15.423 9.202   0.34 13.07 ?  16  VAL   A O    1 
ATOM   350  C CB   A VAL   A 1 16  ? 15.629 -15.298 6.680   0.66 13.60 ?  16  VAL   A CB   1 
ATOM   351  C CB   B VAL   A 1 16  ? 15.523 -15.308 6.764   0.34 13.07 ?  16  VAL   A CB   1 
ATOM   352  C CG1  A VAL   A 1 16  ? 15.212 -13.932 6.129   0.66 14.27 ?  16  VAL   A CG1  1 
ATOM   353  C CG1  B VAL   A 1 16  ? 15.075 -13.969 6.192   0.34 13.28 ?  16  VAL   A CG1  1 
ATOM   354  C CG2  A VAL   A 1 16  ? 16.914 -15.778 6.022   0.66 14.38 ?  16  VAL   A CG2  1 
ATOM   355  C CG2  B VAL   A 1 16  ? 16.793 -15.796 6.062   0.34 13.65 ?  16  VAL   A CG2  1 
ATOM   356  H H    A VAL   A 1 16  ? 15.611 -17.147 8.627   0.66 15.86 ?  16  VAL   A H    1 
ATOM   357  H H    B VAL   A 1 16  ? 15.551 -17.115 8.735   0.34 16.39 ?  16  VAL   A H    1 
ATOM   358  H HA   A VAL   A 1 16  ? 16.488 -14.584 8.402   0.66 16.01 ?  16  VAL   A HA   1 
ATOM   359  H HA   B VAL   A 1 16  ? 16.472 -14.575 8.427   0.34 16.01 ?  16  VAL   A HA   1 
ATOM   360  H HB   A VAL   A 1 16  ? 14.929 -15.937 6.469   0.66 16.29 ?  16  VAL   A HB   1 
ATOM   361  H HB   B VAL   A 1 16  ? 14.826 -15.959 6.591   0.34 15.66 ?  16  VAL   A HB   1 
ATOM   362  H HG11 A VAL   A 1 16  ? 15.307 -13.942 5.165   0.66 17.09 ?  16  VAL   A HG11 1 
ATOM   363  H HG11 B VAL   A 1 16  ? 15.129 -14.009 5.223   0.34 15.91 ?  16  VAL   A HG11 1 
ATOM   364  H HG12 A VAL   A 1 16  ? 14.288 -13.762 6.368   0.66 17.09 ?  16  VAL   A HG12 1 
ATOM   365  H HG12 B VAL   A 1 16  ? 14.163 -13.799 6.465   0.34 15.91 ?  16  VAL   A HG12 1 
ATOM   366  H HG13 A VAL   A 1 16  ? 15.786 -13.250 6.511   0.66 17.09 ?  16  VAL   A HG13 1 
ATOM   367  H HG13 B VAL   A 1 16  ? 15.661 -13.273 6.526   0.34 15.91 ?  16  VAL   A HG13 1 
ATOM   368  H HG21 A VAL   A 1 16  ? 16.808 -15.734 5.060   0.66 17.23 ?  16  VAL   A HG21 1 
ATOM   369  H HG21 B VAL   A 1 16  ? 16.645 -15.804 5.104   0.34 16.36 ?  16  VAL   A HG21 1 
ATOM   370  H HG22 A VAL   A 1 16  ? 17.644 -15.208 6.303   0.66 17.23 ?  16  VAL   A HG22 1 
ATOM   371  H HG22 B VAL   A 1 16  ? 17.525 -15.196 6.277   0.34 16.36 ?  16  VAL   A HG22 1 
ATOM   372  H HG23 A VAL   A 1 16  ? 17.085 -16.694 6.295   0.66 17.23 ?  16  VAL   A HG23 1 
ATOM   373  H HG23 B VAL   A 1 16  ? 17.004 -16.693 6.371   0.34 16.36 ?  16  VAL   A HG23 1 
ATOM   374  N N    A TYR   A 1 17  ? 14.552 -13.509 9.348   0.66 12.44 ?  17  TYR   A N    1 
ATOM   375  N N    B TYR   A 1 17  ? 14.574 -13.414 9.418   0.34 12.91 ?  17  TYR   A N    1 
ATOM   376  C CA   A TYR   A 1 17  ? 13.463 -12.826 10.023  0.66 12.44 ?  17  TYR   A CA   1 
ATOM   377  C CA   B TYR   A 1 17  ? 13.513 -12.738 10.155  0.34 12.28 ?  17  TYR   A CA   1 
ATOM   378  C C    A TYR   A 1 17  ? 13.175 -11.521 9.289   0.66 12.43 ?  17  TYR   A C    1 
ATOM   379  C C    B TYR   A 1 17  ? 13.245 -11.381 9.515   0.34 12.06 ?  17  TYR   A C    1 
ATOM   380  O O    A TYR   A 1 17  ? 14.055 -10.973 8.624   0.66 12.16 ?  17  TYR   A O    1 
ATOM   381  O O    B TYR   A 1 17  ? 14.155 -10.769 8.952   0.34 12.17 ?  17  TYR   A O    1 
ATOM   382  C CB   A TYR   A 1 17  ? 13.868 -12.540 11.472  0.66 13.27 ?  17  TYR   A CB   1 
ATOM   383  C CB   B TYR   A 1 17  ? 13.931 -12.520 11.618  0.34 12.66 ?  17  TYR   A CB   1 
ATOM   384  C CG   A TYR   A 1 17  ? 14.037 -13.800 12.295  0.66 14.62 ?  17  TYR   A CG   1 
ATOM   385  C CG   B TYR   A 1 17  ? 14.229 -13.795 12.381  0.34 13.19 ?  17  TYR   A CG   1 
ATOM   386  C CD1  A TYR   A 1 17  ? 15.196 -14.571 12.217  0.66 15.41 ?  17  TYR   A CD1  1 
ATOM   387  C CD1  B TYR   A 1 17  ? 15.448 -14.450 12.243  0.34 13.62 ?  17  TYR   A CD1  1 
ATOM   388  C CD2  A TYR   A 1 17  ? 13.022 -14.236 13.137  0.66 14.77 ?  17  TYR   A CD2  1 
ATOM   389  C CD2  B TYR   A 1 17  ? 13.290 -14.340 13.247  0.34 13.41 ?  17  TYR   A CD2  1 
ATOM   390  C CE1  A TYR   A 1 17  ? 15.339 -15.743 12.963  0.66 15.56 ?  17  TYR   A CE1  1 
ATOM   391  C CE1  B TYR   A 1 17  ? 15.718 -15.620 12.940  0.34 14.33 ?  17  TYR   A CE1  1 
ATOM   392  C CE2  A TYR   A 1 17  ? 13.153 -15.402 13.884  0.66 15.13 ?  17  TYR   A CE2  1 
ATOM   393  C CE2  B TYR   A 1 17  ? 13.551 -15.506 13.949  0.34 14.05 ?  17  TYR   A CE2  1 
ATOM   394  C CZ   A TYR   A 1 17  ? 14.312 -16.151 13.797  0.66 15.27 ?  17  TYR   A CZ   1 
ATOM   395  C CZ   B TYR   A 1 17  ? 14.765 -16.142 13.792  0.34 14.58 ?  17  TYR   A CZ   1 
ATOM   396  O OH   A TYR   A 1 17  ? 14.438 -17.304 14.544  0.66 15.45 ?  17  TYR   A OH   1 
ATOM   397  O OH   B TYR   A 1 17  ? 15.021 -17.301 14.492  0.34 15.40 ?  17  TYR   A OH   1 
ATOM   398  H H    A TYR   A 1 17  ? 15.257 -13.014 9.283   0.66 14.90 ?  17  TYR   A H    1 
ATOM   399  H H    B TYR   A 1 17  ? 15.251 -12.903 9.269   0.34 15.46 ?  17  TYR   A H    1 
ATOM   400  H HA   A TYR   A 1 17  ? 12.667 -13.388 10.012  0.66 14.90 ?  17  TYR   A HA   1 
ATOM   401  H HA   B TYR   A 1 17  ? 12.699 -13.263 10.128  0.34 14.71 ?  17  TYR   A HA   1 
ATOM   402  H HB2  A TYR   A 1 17  ? 14.713 -12.067 11.471  0.66 15.89 ?  17  TYR   A HB2  1 
ATOM   403  H HB2  B TYR   A 1 17  ? 14.731 -11.975 11.630  0.34 15.17 ?  17  TYR   A HB2  1 
ATOM   404  H HB3  A TYR   A 1 17  ? 13.183 -12.002 11.885  0.66 15.89 ?  17  TYR   A HB3  1 
ATOM   405  H HB3  B TYR   A 1 17  ? 13.212 -12.060 12.078  0.34 15.17 ?  17  TYR   A HB3  1 
ATOM   406  H HD1  A TYR   A 1 17  ? 15.888 -14.303 11.654  0.66 18.47 ?  17  TYR   A HD1  1 
ATOM   407  H HD1  B TYR   A 1 17  ? 16.090 -14.104 11.668  0.34 16.31 ?  17  TYR   A HD1  1 
ATOM   408  H HD2  A TYR   A 1 17  ? 12.235 -13.745 13.201  0.66 17.69 ?  17  TYR   A HD2  1 
ATOM   409  H HD2  B TYR   A 1 17  ? 12.468 -13.918 13.356  0.34 16.07 ?  17  TYR   A HD2  1 
ATOM   410  H HE1  A TYR   A 1 17  ? 16.124 -16.248 12.902  0.66 18.64 ?  17  TYR   A HE1  1 
ATOM   411  H HE1  B TYR   A 1 17  ? 16.539 -16.049 12.839  0.34 17.16 ?  17  TYR   A HE1  1 
ATOM   412  H HE2  A TYR   A 1 17  ? 12.463 -15.678 14.445  0.66 18.13 ?  17  TYR   A HE2  1 
ATOM   413  H HE2  B TYR   A 1 17  ? 12.912 -15.860 14.527  0.34 16.84 ?  17  TYR   A HE2  1 
ATOM   414  H HH   A TYR   A 1 17  ? 13.692 -17.525 14.860  0.66 18.52 ?  17  TYR   A HH   1 
ATOM   415  H HH   B TYR   A 1 17  ? 15.740 -17.649 14.225  0.34 18.45 ?  17  TYR   A HH   1 
ATOM   416  N N    A ILE   A 1 18  ? 11.946 -11.005 9.400   0.66 12.27 ?  18  ILE   A N    1 
ATOM   417  N N    B ILE   A 1 18  ? 12.001 -10.891 9.613   0.34 11.36 ?  18  ILE   A N    1 
ATOM   418  C CA   A ILE   A 1 18  ? 11.556 -9.827  8.624   0.66 11.93 ?  18  ILE   A CA   1 
ATOM   419  C CA   B ILE   A 1 18  ? 11.608 -9.666  8.918   0.34 10.68 ?  18  ILE   A CA   1 
ATOM   420  C C    A ILE   A 1 18  ? 10.575 -8.962  9.410   0.66 12.53 ?  18  ILE   A C    1 
ATOM   421  C C    B ILE   A 1 18  ? 10.690 -8.812  9.785   0.34 10.39 ?  18  ILE   A C    1 
ATOM   422  O O    A ILE   A 1 18  ? 9.738  -9.466  10.163  0.66 12.47 ?  18  ILE   A O    1 
ATOM   423  O O    B ILE   A 1 18  ? 9.892  -9.322  10.579  0.34 10.96 ?  18  ILE   A O    1 
ATOM   424  C CB   A ILE   A 1 18  ? 11.024 -10.249 7.233   0.66 11.93 ?  18  ILE   A CB   1 
ATOM   425  C CB   B ILE   A 1 18  ? 10.948 -9.983  7.559   0.34 9.87  ?  18  ILE   A CB   1 
ATOM   426  C CG1  A ILE   A 1 18  ? 10.973 -9.056  6.283   0.66 12.26 ?  18  ILE   A CG1  1 
ATOM   427  C CG1  B ILE   A 1 18  ? 10.874 -8.743  6.667   0.34 11.35 ?  18  ILE   A CG1  1 
ATOM   428  C CG2  A ILE   A 1 18  ? 9.677  -10.989 7.354   0.66 12.05 ?  18  ILE   A CG2  1 
ATOM   429  C CG2  B ILE   A 1 18  ? 9.569  -10.605 7.764   0.34 10.52 ?  18  ILE   A CG2  1 
ATOM   430  C CD1  A ILE   A 1 18  ? 10.746 -9.456  4.853   0.66 13.06 ?  18  ILE   A CD1  1 
ATOM   431  C CD1  B ILE   A 1 18  ? 10.442 -9.070  5.255   0.34 12.17 ?  18  ILE   A CD1  1 
ATOM   432  H H    A ILE   A 1 18  ? 11.332 -11.329 9.909   0.66 14.70 ?  18  ILE   A H    1 
ATOM   433  H H    B ILE   A 1 18  ? 11.369 -11.253 10.076  0.34 13.61 ?  18  ILE   A H    1 
ATOM   434  H HA   A ILE   A 1 18  ? 12.351 -9.301  8.473   0.66 14.29 ?  18  ILE   A HA   1 
ATOM   435  H HA   B ILE   A 1 18  ? 12.407 -9.144  8.743   0.34 12.78 ?  18  ILE   A HA   1 
ATOM   436  H HB   A ILE   A 1 18  ? 11.656 -10.885 6.858   0.66 14.29 ?  18  ILE   A HB   1 
ATOM   437  H HB   B ILE   A 1 18  ? 11.503 -10.631 7.114   0.34 11.81 ?  18  ILE   A HB   1 
ATOM   438  H HG12 A ILE   A 1 18  ? 10.252 -8.469  6.551   0.66 14.68 ?  18  ILE   A HG12 1 
ATOM   439  H HG12 B ILE   A 1 18  ? 10.233 -8.115  7.037   0.34 13.60 ?  18  ILE   A HG12 1 
ATOM   440  H HG13 A ILE   A 1 18  ? 11.822 -8.585  6.329   0.66 14.68 ?  18  ILE   A HG13 1 
ATOM   441  H HG13 B ILE   A 1 18  ? 11.753 -8.329  6.622   0.34 13.60 ?  18  ILE   A HG13 1 
ATOM   442  H HG21 A ILE   A 1 18  ? 9.435  -11.359 6.486   0.66 14.43 ?  18  ILE   A HG21 1 
ATOM   443  H HG21 B ILE   A 1 18  ? 9.275  -10.996 6.924   0.34 12.60 ?  18  ILE   A HG21 1 
ATOM   444  H HG22 A ILE   A 1 18  ? 9.765  -11.708 8.000   0.66 14.43 ?  18  ILE   A HG22 1 
ATOM   445  H HG22 B ILE   A 1 18  ? 9.632  -11.293 8.443   0.34 12.60 ?  18  ILE   A HG22 1 
ATOM   446  H HG23 A ILE   A 1 18  ? 8.995  -10.365 7.645   0.66 14.43 ?  18  ILE   A HG23 1 
ATOM   447  H HG23 B ILE   A 1 18  ? 8.944  -9.918  8.044   0.34 12.60 ?  18  ILE   A HG23 1 
ATOM   448  H HD11 A ILE   A 1 18  ? 10.788 -8.664  4.293   0.66 15.64 ?  18  ILE   A HD11 1 
ATOM   449  H HD11 B ILE   A 1 18  ? 10.502 -8.271  4.710   0.34 14.57 ?  18  ILE   A HD11 1 
ATOM   450  H HD12 A ILE   A 1 18  ? 11.432 -10.087 4.586   0.66 15.64 ?  18  ILE   A HD12 1 
ATOM   451  H HD12 B ILE   A 1 18  ? 11.029 -9.757  4.898   0.34 14.57 ?  18  ILE   A HD12 1 
ATOM   452  H HD13 A ILE   A 1 18  ? 9.870  -9.868  4.776   0.66 15.64 ?  18  ILE   A HD13 1 
ATOM   453  H HD13 B ILE   A 1 18  ? 9.528  -9.393  5.270   0.34 14.57 ?  18  ILE   A HD13 1 
ATOM   454  N N    A LYS   A 1 19  ? 10.670 -7.644  9.209   0.66 12.57 ?  19  LYS   A N    1 
ATOM   455  N N    B LYS   A 1 19  ? 10.792 -7.493  9.603   0.34 10.35 ?  19  LYS   A N    1 
ATOM   456  C CA   A LYS   A 1 19  ? 9.855  -6.677  9.937   0.66 13.13 ?  19  LYS   A CA   1 
ATOM   457  C CA   B LYS   A 1 19  ? 10.018 -6.543  10.387  0.34 11.20 ?  19  LYS   A CA   1 
ATOM   458  C C    A LYS   A 1 19  ? 9.682  -5.423  9.087   0.66 13.04 ?  19  LYS   A C    1 
ATOM   459  C C    B LYS   A 1 19  ? 9.831  -5.281  9.562   0.34 11.14 ?  19  LYS   A C    1 
ATOM   460  O O    A LYS   A 1 19  ? 10.571 -5.058  8.316   0.66 12.50 ?  19  LYS   A O    1 
ATOM   461  O O    B LYS   A 1 19  ? 10.752 -4.854  8.864   0.34 11.38 ?  19  LYS   A O    1 
ATOM   462  C CB   A LYS   A 1 19  ? 10.554 -6.306  11.251  0.66 14.20 ?  19  LYS   A CB   1 
ATOM   463  C CB   B LYS   A 1 19  ? 10.771 -6.215  11.683  0.34 12.04 ?  19  LYS   A CB   1 
ATOM   464  C CG   A LYS   A 1 19  ? 9.803  -5.356  12.174  0.66 15.99 ?  19  LYS   A CG   1 
ATOM   465  C CG   B LYS   A 1 19  ? 10.103 -5.224  12.613  0.34 13.07 ?  19  LYS   A CG   1 
ATOM   466  C CD   A LYS   A 1 19  ? 10.648 -5.103  13.420  0.66 17.84 ?  19  LYS   A CD   1 
ATOM   467  C CD   B LYS   A 1 19  ? 11.034 -4.926  13.778  0.34 14.15 ?  19  LYS   A CD   1 
ATOM   468  C CE   A LYS   A 1 19  ? 10.004 -4.132  14.393  0.66 19.36 ?  19  LYS   A CE   1 
ATOM   469  C CE   B LYS   A 1 19  ? 10.393 -4.022  14.807  0.34 15.17 ?  19  LYS   A CE   1 
ATOM   470  N NZ   A LYS   A 1 19  ? 10.895 -3.848  15.557  0.66 19.58 ?  19  LYS   A NZ   1 
ATOM   471  N NZ   B LYS   A 1 19  ? 11.294 -3.856  15.979  0.34 15.39 ?  19  LYS   A NZ   1 
ATOM   472  H H    A LYS   A 1 19  ? 11.213 -7.294  8.648   0.66 15.06 ?  19  LYS   A H    1 
ATOM   473  H H    B LYS   A 1 19  ? 11.318 -7.111  9.026   0.34 12.40 ?  19  LYS   A H    1 
ATOM   474  H HA   A LYS   A 1 19  ? 8.985  -7.064  10.134  0.66 15.73 ?  19  LYS   A HA   1 
ATOM   475  H HA   B LYS   A 1 19  ? 9.151  -6.913  10.608  0.34 13.41 ?  19  LYS   A HA   1 
ATOM   476  H HB2  A LYS   A 1 19  ? 10.714 -7.125  11.751  0.66 17.01 ?  19  LYS   A HB2  1 
ATOM   477  H HB2  B LYS   A 1 19  ? 10.888 -7.038  12.185  0.34 14.42 ?  19  LYS   A HB2  1 
ATOM   478  H HB3  A LYS   A 1 19  ? 11.403 -5.893  11.034  0.66 17.01 ?  19  LYS   A HB3  1 
ATOM   479  H HB3  B LYS   A 1 19  ? 11.640 -5.852  11.453  0.34 14.42 ?  19  LYS   A HB3  1 
ATOM   480  H HG2  A LYS   A 1 19  ? 9.653  -4.511  11.722  0.66 19.16 ?  19  LYS   A HG2  1 
ATOM   481  H HG2  B LYS   A 1 19  ? 9.928  -4.396  12.140  0.34 15.66 ?  19  LYS   A HG2  1 
ATOM   482  H HG3  A LYS   A 1 19  ? 8.961  -5.755  12.444  0.66 19.16 ?  19  LYS   A HG3  1 
ATOM   483  H HG3  B LYS   A 1 19  ? 9.281  -5.603  12.960  0.34 15.66 ?  19  LYS   A HG3  1 
ATOM   484  H HD2  A LYS   A 1 19  ? 10.786 -5.944  13.885  0.66 21.39 ?  19  LYS   A HD2  1 
ATOM   485  H HD2  B LYS   A 1 19  ? 11.269 -5.761  14.215  0.34 16.95 ?  19  LYS   A HD2  1 
ATOM   486  H HD3  A LYS   A 1 19  ? 11.505 -4.732  13.151  0.66 21.39 ?  19  LYS   A HD3  1 
ATOM   487  H HD3  B LYS   A 1 19  ? 11.832 -4.488  13.444  0.34 16.95 ?  19  LYS   A HD3  1 
ATOM   488  H HE2  A LYS   A 1 19  ? 9.826  -3.294  13.939  0.66 23.21 ?  19  LYS   A HE2  1 
ATOM   489  H HE2  B LYS   A 1 19  ? 10.231 -3.150  14.413  0.34 18.18 ?  19  LYS   A HE2  1 
ATOM   490  H HE3  A LYS   A 1 19  ? 9.181  -4.514  14.731  0.66 23.21 ?  19  LYS   A HE3  1 
ATOM   491  H HE3  B LYS   A 1 19  ? 9.558  -4.417  15.108  0.34 18.18 ?  19  LYS   A HE3  1 
ATOM   492  H HZ1  A LYS   A 1 19  ? 10.500 -3.278  16.115  0.66 23.47 ?  19  LYS   A HZ1  1 
ATOM   493  H HZ1  B LYS   A 1 19  ? 10.909 -3.330  16.583  0.34 18.44 ?  19  LYS   A HZ1  1 
ATOM   494  H HZ2  A LYS   A 1 19  ? 11.075 -4.603  15.996  0.66 23.47 ?  19  LYS   A HZ2  1 
ATOM   495  H HZ2  B LYS   A 1 19  ? 11.457 -4.650  16.347  0.34 18.44 ?  19  LYS   A HZ2  1 
ATOM   496  H HZ3  A LYS   A 1 19  ? 11.662 -3.491  15.277  0.66 23.47 ?  19  LYS   A HZ3  1 
ATOM   497  H HZ3  B LYS   A 1 19  ? 12.062 -3.492  15.720  0.34 18.44 ?  19  LYS   A HZ3  1 
ATOM   498  N N    A ASN   A 1 20  ? 8.528  -4.769  9.227   0.66 14.29 ?  20  ASN   A N    1 
ATOM   499  N N    B ASN   A 1 20  ? 8.638  -4.696  9.624   0.34 11.97 ?  20  ASN   A N    1 
ATOM   500  C CA   A ASN   A 1 20  ? 8.298  -3.457  8.616   0.66 15.48 ?  20  ASN   A CA   1 
ATOM   501  C CA   B ASN   A 1 20  ? 8.437  -3.363  9.069   0.34 12.57 ?  20  ASN   A CA   1 
ATOM   502  C C    A ASN   A 1 20  ? 8.885  -2.410  9.556   0.66 16.67 ?  20  ASN   A C    1 
ATOM   503  C C    B ASN   A 1 20  ? 9.137  -2.375  9.985   0.34 12.50 ?  20  ASN   A C    1 
ATOM   504  O O    A ASN   A 1 20  ? 8.293  -2.089  10.590  0.66 17.14 ?  20  ASN   A O    1 
ATOM   505  O O    B ASN   A 1 20  ? 8.710  -2.160  11.124  0.34 12.64 ?  20  ASN   A O    1 
ATOM   506  C CB   A ASN   A 1 20  ? 6.805  -3.238  8.375   0.66 16.17 ?  20  ASN   A CB   1 
ATOM   507  C CB   B ASN   A 1 20  ? 6.951  -3.042  8.952   0.34 13.42 ?  20  ASN   A CB   1 
ATOM   508  C CG   A ASN   A 1 20  ? 6.468  -1.808  7.958   0.66 16.84 ?  20  ASN   A CG   1 
ATOM   509  C CG   B ASN   A 1 20  ? 6.686  -1.568  8.671   0.34 14.20 ?  20  ASN   A CG   1 
ATOM   510  O OD1  A ASN   A 1 20  ? 5.485  -1.226  8.432   0.66 18.73 ?  20  ASN   A OD1  1 
ATOM   511  O OD1  B ASN   A 1 20  ? 5.838  -0.952  9.315   0.34 15.11 ?  20  ASN   A OD1  1 
ATOM   512  N ND2  A ASN   A 1 20  ? 7.274  -1.243  7.064   0.66 17.28 ?  20  ASN   A ND2  1 
ATOM   513  N ND2  B ASN   A 1 20  ? 7.417  -0.996  7.718   0.34 14.24 ?  20  ASN   A ND2  1 
ATOM   514  H H    A ASN   A 1 20  ? 7.855  -5.080  9.668   0.66 17.12 ?  20  ASN   A H    1 
ATOM   515  H H    B ASN   A 1 20  ? 7.942  -5.049  9.977   0.34 14.33 ?  20  ASN   A H    1 
ATOM   516  H HA   A ASN   A 1 20  ? 8.762  -3.418  7.768   0.66 18.55 ?  20  ASN   A HA   1 
ATOM   517  H HA   B ASN   A 1 20  ? 8.841  -3.307  8.189   0.34 15.06 ?  20  ASN   A HA   1 
ATOM   518  H HB2  A ASN   A 1 20  ? 6.511  -3.831  7.666   0.66 19.37 ?  20  ASN   A HB2  1 
ATOM   519  H HB2  B ASN   A 1 20  ? 6.579  -3.556  8.222   0.34 16.08 ?  20  ASN   A HB2  1 
ATOM   520  H HB3  A ASN   A 1 20  ? 6.323  -3.438  9.193   0.66 19.37 ?  20  ASN   A HB3  1 
ATOM   521  H HB3  B ASN   A 1 20  ? 6.516  -3.277  9.784   0.34 16.08 ?  20  ASN   A HB3  1 
ATOM   522  H HD21 A ASN   A 1 20  ? 7.124  -0.441  6.803   0.66 20.71 ?  20  ASN   A HD21 1 
ATOM   523  H HD21 B ASN   A 1 20  ? 7.297  -0.165  7.527   0.34 17.06 ?  20  ASN   A HD21 1 
ATOM   524  H HD22 A ASN   A 1 20  ? 7.942  -1.684  6.745   0.66 20.71 ?  20  ASN   A HD22 1 
ATOM   525  H HD22 B ASN   A 1 20  ? 8.004  -1.455  7.291   0.34 17.06 ?  20  ASN   A HD22 1 
ATOM   526  N N    A ALA   A 1 21  ? 10.060 -1.876  9.212   0.66 17.15 ?  21  ALA   A N    1 
ATOM   527  N N    B ALA   A 1 21  ? 10.238 -1.808  9.507   0.34 12.97 ?  21  ALA   A N    1 
ATOM   528  C CA   A ALA   A 1 21  ? 10.738 -0.954  10.117  0.66 17.44 ?  21  ALA   A CA   1 
ATOM   529  C CA   B ALA   A 1 21  ? 10.989 -0.849  10.294  0.34 13.67 ?  21  ALA   A CA   1 
ATOM   530  C C    A ALA   A 1 21  ? 11.730 -0.080  9.363   0.66 16.57 ?  21  ALA   A C    1 
ATOM   531  C C    B ALA   A 1 21  ? 11.949 -0.125  9.373   0.34 14.16 ?  21  ALA   A C    1 
ATOM   532  O O    A ALA   A 1 21  ? 12.192 -0.423  8.270   0.66 16.11 ?  21  ALA   A O    1 
ATOM   533  O O    B ALA   A 1 21  ? 12.484 -0.721  8.437   0.34 14.51 ?  21  ALA   A O    1 
ATOM   534  C CB   A ALA   A 1 21  ? 11.457 -1.700  11.245  0.66 19.32 ?  21  ALA   A CB   1 
ATOM   535  C CB   B ALA   A 1 21  ? 11.779 -1.554  11.402  0.34 14.60 ?  21  ALA   A CB   1 
ATOM   536  H H    A ALA   A 1 21  ? 10.472 -2.027  8.472   0.66 20.55 ?  21  ALA   A H    1 
ATOM   537  H H    B ALA   A 1 21  ? 10.572 -1.967  8.732   0.34 15.53 ?  21  ALA   A H    1 
ATOM   538  H HA   A ALA   A 1 21  ? 10.076 -0.371  10.519  0.66 20.90 ?  21  ALA   A HA   1 
ATOM   539  H HA   B ALA   A 1 21  ? 10.385 -0.203  10.697  0.34 16.38 ?  21  ALA   A HA   1 
ATOM   540  H HB1  A ALA   A 1 21  ? 11.889 -1.052  11.823  0.66 23.16 ?  21  ALA   A HB1  1 
ATOM   541  H HB1  B ALA   A 1 21  ? 12.201 -0.879  11.957  0.34 17.49 ?  21  ALA   A HB1  1 
ATOM   542  H HB2  A ALA   A 1 21  ? 10.803 -2.210  11.750  0.66 23.16 ?  21  ALA   A HB2  1 
ATOM   543  H HB2  B ALA   A 1 21  ? 11.169 -2.086  11.939  0.34 17.49 ?  21  ALA   A HB2  1 
ATOM   544  H HB3  A ALA   A 1 21  ? 12.116 -2.295  10.860  0.66 23.16 ?  21  ALA   A HB3  1 
ATOM   545  H HB3  B ALA   A 1 21  ? 12.449 -2.127  10.999  0.34 17.49 ?  21  ALA   A HB3  1 
ATOM   546  N N    A ASP   A 1 22  ? 12.054 1.058   9.985   0.66 16.14 ?  22  ASP   A N    1 
ATOM   547  N N    B ASP   A 1 22  ? 12.123 1.167   9.620   0.34 14.24 ?  22  ASP   A N    1 
ATOM   548  C CA   A ASP   A 1 22  ? 13.092 1.972   9.522   0.66 16.09 ?  22  ASP   A CA   1 
ATOM   549  C CA   B ASP   A 1 22  ? 13.269 1.888   9.088   0.34 14.70 ?  22  ASP   A CA   1 
ATOM   550  C C    A ASP   A 1 22  ? 14.419 1.512   10.112  0.66 15.15 ?  22  ASP   A C    1 
ATOM   551  C C    B ASP   A 1 22  ? 14.526 1.309   9.731   0.34 14.17 ?  22  ASP   A C    1 
ATOM   552  O O    A ASP   A 1 22  ? 14.593 1.518   11.335  0.66 16.08 ?  22  ASP   A O    1 
ATOM   553  O O    B ASP   A 1 22  ? 14.643 1.290   10.960  0.34 14.73 ?  22  ASP   A O    1 
ATOM   554  C CB   A ASP   A 1 22  ? 12.758 3.391   9.986   0.66 17.85 ?  22  ASP   A CB   1 
ATOM   555  C CB   B ASP   A 1 22  ? 13.113 3.365   9.445   0.34 16.04 ?  22  ASP   A CB   1 
ATOM   556  C CG   A ASP   A 1 22  ? 13.789 4.430   9.546   0.66 19.83 ?  22  ASP   A CG   1 
ATOM   557  C CG   B ASP   A 1 22  ? 14.203 4.239   8.870   0.34 16.96 ?  22  ASP   A CG   1 
ATOM   558  O OD1  A ASP   A 1 22  ? 14.849 4.066   8.996   0.66 20.68 ?  22  ASP   A OD1  1 
ATOM   559  O OD1  B ASP   A 1 22  ? 15.187 3.699   8.331   0.34 16.53 ?  22  ASP   A OD1  1 
ATOM   560  O OD2  A ASP   A 1 22  ? 13.525 5.634   9.753   0.66 21.64 -1 22  ASP   A OD2  1 
ATOM   561  O OD2  B ASP   A 1 22  ? 14.073 5.479   8.970   0.34 18.39 -1 22  ASP   A OD2  1 
ATOM   562  H H    A ASP   A 1 22  ? 11.668 1.327   10.705  0.66 19.34 ?  22  ASP   A H    1 
ATOM   563  H H    B ASP   A 1 22  ? 11.575 1.651   10.081  0.34 17.07 ?  22  ASP   A H    1 
ATOM   564  H HA   A ASP   A 1 22  ? 13.152 1.955   8.557   0.66 19.28 ?  22  ASP   A HA   1 
ATOM   565  H HA   B ASP   A 1 22  ? 13.310 1.778   8.121   0.34 17.62 ?  22  ASP   A HA   1 
ATOM   566  H HB2  A ASP   A 1 22  ? 11.901 3.648   9.613   0.66 21.39 ?  22  ASP   A HB2  1 
ATOM   567  H HB2  B ASP   A 1 22  ? 12.262 3.681   9.113   0.34 19.22 ?  22  ASP   A HB2  1 
ATOM   568  H HB3  A ASP   A 1 22  ? 12.710 3.401   10.957  0.66 21.39 ?  22  ASP   A HB3  1 
ATOM   569  H HB3  B ASP   A 1 22  ? 13.160 3.458   10.404  0.34 19.22 ?  22  ASP   A HB3  1 
ATOM   570  N N    A ILE   A 1 23  ? 15.345 1.106   9.240   0.66 14.79 ?  23  ILE   A N    1 
ATOM   571  N N    B ILE   A 1 23  ? 15.455 0.809   8.908   0.34 13.79 ?  23  ILE   A N    1 
ATOM   572  C CA   A ILE   A 1 23  ? 16.594 0.497   9.690   0.66 14.29 ?  23  ILE   A CA   1 
ATOM   573  C CA   B ILE   A 1 23  ? 16.671 0.201   9.447   0.34 13.15 ?  23  ILE   A CA   1 
ATOM   574  C C    A ILE   A 1 23  ? 17.389 1.447   10.576  0.66 14.33 ?  23  ILE   A C    1 
ATOM   575  C C    B ILE   A 1 23  ? 17.420 1.194   10.321  0.34 13.69 ?  23  ILE   A C    1 
ATOM   576  O O    A ILE   A 1 23  ? 18.110 1.004   11.480  0.66 14.86 ?  23  ILE   A O    1 
ATOM   577  O O    B ILE   A 1 23  ? 18.084 0.805   11.290  0.34 13.68 ?  23  ILE   A O    1 
ATOM   578  C CB   A ILE   A 1 23  ? 17.402 -0.016  8.478   0.66 13.60 ?  23  ILE   A CB   1 
ATOM   579  C CB   B ILE   A 1 23  ? 17.568 -0.387  8.333   0.34 12.55 ?  23  ILE   A CB   1 
ATOM   580  C CG1  A ILE   A 1 23  ? 18.525 -0.949  8.933   0.66 14.08 ?  23  ILE   A CG1  1 
ATOM   581  C CG1  B ILE   A 1 23  ? 18.604 -1.336  8.952   0.34 12.29 ?  23  ILE   A CG1  1 
ATOM   582  C CG2  A ILE   A 1 23  ? 17.937 1.145   7.640   0.66 13.83 ?  23  ILE   A CG2  1 
ATOM   583  C CG2  B ILE   A 1 23  ? 18.246 0.722   7.522   0.34 12.45 ?  23  ILE   A CG2  1 
ATOM   584  C CD1  A ILE   A 1 23  ? 19.223 -1.648  7.793   0.66 14.24 ?  23  ILE   A CD1  1 
ATOM   585  C CD1  B ILE   A 1 23  ? 19.559 -1.959  7.966   0.34 12.41 ?  23  ILE   A CD1  1 
ATOM   586  H H    A ILE   A 1 23  ? 15.270 1.168   8.390   0.66 17.72 ?  23  ILE   A H    1 
ATOM   587  H H    B ILE   A 1 23  ? 15.409 0.807   8.060   0.34 16.52 ?  23  ILE   A H    1 
ATOM   588  H HA   A ILE   A 1 23  ? 16.379 -0.276  10.234  0.66 17.13 ?  23  ILE   A HA   1 
ATOM   589  H HA   B ILE   A 1 23  ? 16.411 -0.539  10.012  0.34 15.76 ?  23  ILE   A HA   1 
ATOM   590  H HB   A ILE   A 1 23  ? 16.799 -0.528  7.919   0.66 16.29 ?  23  ILE   A HB   1 
ATOM   591  H HB   B ILE   A 1 23  ? 17.011 -0.904  7.731   0.34 15.03 ?  23  ILE   A HB   1 
ATOM   592  H HG12 A ILE   A 1 23  ? 19.188 -0.432  9.416   0.66 16.87 ?  23  ILE   A HG12 1 
ATOM   593  H HG12 B ILE   A 1 23  ? 19.133 -0.846  9.598   0.34 14.72 ?  23  ILE   A HG12 1 
ATOM   594  H HG13 A ILE   A 1 23  ? 18.149 -1.629  9.514   0.66 16.87 ?  23  ILE   A HG13 1 
ATOM   595  H HG13 B ILE   A 1 23  ? 18.135 -2.062  9.395   0.34 14.72 ?  23  ILE   A HG13 1 
ATOM   596  H HG21 A ILE   A 1 23  ? 18.280 0.798   6.801   0.66 16.56 ?  23  ILE   A HG21 1 
ATOM   597  H HG21 B ILE   A 1 23  ? 18.623 0.337   6.711   0.34 14.91 ?  23  ILE   A HG21 1 
ATOM   598  H HG22 A ILE   A 1 23  ? 17.212 1.768   7.466   0.66 16.56 ?  23  ILE   A HG22 1 
ATOM   599  H HG22 B ILE   A 1 23  ? 17.587 1.391   7.292   0.34 14.91 ?  23  ILE   A HG22 1 
ATOM   600  H HG23 A ILE   A 1 23  ? 18.645 1.592   8.129   0.66 16.56 ?  23  ILE   A HG23 1 
ATOM   601  H HG23 B ILE   A 1 23  ? 18.953 1.119   8.054   0.34 14.91 ?  23  ILE   A HG23 1 
ATOM   602  H HD11 A ILE   A 1 23  ? 19.858 -2.282  8.156   0.66 17.06 ?  23  ILE   A HD11 1 
ATOM   603  H HD11 B ILE   A 1 23  ? 20.115 -2.608  8.430   0.34 14.86 ?  23  ILE   A HD11 1 
ATOM   604  H HD12 A ILE   A 1 23  ? 18.560 -2.111  7.257   0.66 17.06 ?  23  ILE   A HD12 1 
ATOM   605  H HD12 B ILE   A 1 23  ? 19.048 -2.399  7.273   0.34 14.86 ?  23  ILE   A HD12 1 
ATOM   606  H HD13 A ILE   A 1 23  ? 19.683 -0.987  7.253   0.66 17.06 ?  23  ILE   A HD13 1 
ATOM   607  H HD13 B ILE   A 1 23  ? 20.118 -1.265  7.580   0.34 14.86 ?  23  ILE   A HD13 1 
ATOM   608  N N    A VAL   A 1 24  ? 17.269 2.758   10.349  0.66 14.96 ?  24  VAL   A N    1 
ATOM   609  N N    B VAL   A 1 24  ? 17.323 2.485   10.001  0.34 14.54 ?  24  VAL   A N    1 
ATOM   610  C CA   A VAL   A 1 24  ? 17.958 3.722   11.205  0.66 15.87 ?  24  VAL   A CA   1 
ATOM   611  C CA   B VAL   A 1 24  ? 17.942 3.511   10.835  0.34 15.63 ?  24  VAL   A CA   1 
ATOM   612  C C    A VAL   A 1 24  ? 17.441 3.625   12.634  0.66 16.46 ?  24  VAL   A C    1 
ATOM   613  C C    B VAL   A 1 24  ? 17.316 3.505   12.224  0.34 16.52 ?  24  VAL   A C    1 
ATOM   614  O O    A VAL   A 1 24  ? 18.218 3.527   13.593  0.66 16.59 ?  24  VAL   A O    1 
ATOM   615  O O    B VAL   A 1 24  ? 18.015 3.543   13.243  0.34 17.20 ?  24  VAL   A O    1 
ATOM   616  C CB   A VAL   A 1 24  ? 17.808 5.146   10.640  0.66 16.69 ?  24  VAL   A CB   1 
ATOM   617  C CB   B VAL   A 1 24  ? 17.828 4.888   10.156  0.34 15.86 ?  24  VAL   A CB   1 
ATOM   618  C CG1  A VAL   A 1 24  ? 18.281 6.178   11.656  0.66 18.06 ?  24  VAL   A CG1  1 
ATOM   619  C CG1  B VAL   A 1 24  ? 18.514 5.954   10.992  0.34 16.68 ?  24  VAL   A CG1  1 
ATOM   620  C CG2  A VAL   A 1 24  ? 18.581 5.282   9.336   0.66 17.65 ?  24  VAL   A CG2  1 
ATOM   621  C CG2  B VAL   A 1 24  ? 18.417 4.834   8.751   0.34 15.55 ?  24  VAL   A CG2  1 
ATOM   622  H H    A VAL   A 1 24  ? 16.806 3.106   9.713   0.66 17.92 ?  24  VAL   A H    1 
ATOM   623  H H    B VAL   A 1 24  ? 16.903 2.789   9.318   0.34 17.42 ?  24  VAL   A H    1 
ATOM   624  H HA   A VAL   A 1 24  ? 18.905 3.511   11.214  0.66 19.02 ?  24  VAL   A HA   1 
ATOM   625  H HA   B VAL   A 1 24  ? 18.885 3.310   10.934  0.34 18.73 ?  24  VAL   A HA   1 
ATOM   626  H HB   A VAL   A 1 24  ? 16.872 5.317   10.447  0.66 20.00 ?  24  VAL   A HB   1 
ATOM   627  H HB   B VAL   A 1 24  ? 16.891 5.125   10.075  0.34 19.01 ?  24  VAL   A HB   1 
ATOM   628  H HG11 A VAL   A 1 24  ? 18.441 7.017   11.198  0.66 21.65 ?  24  VAL   A HG11 1 
ATOM   629  H HG11 B VAL   A 1 24  ? 18.572 6.770   10.473  0.34 19.99 ?  24  VAL   A HG11 1 
ATOM   630  H HG12 A VAL   A 1 24  ? 17.595 6.294   12.330  0.66 21.65 ?  24  VAL   A HG12 1 
ATOM   631  H HG12 B VAL   A 1 24  ? 17.991 6.110   11.795  0.34 19.99 ?  24  VAL   A HG12 1 
ATOM   632  H HG13 A VAL   A 1 24  ? 19.102 5.861   12.063  0.66 21.65 ?  24  VAL   A HG13 1 
ATOM   633  H HG13 B VAL   A 1 24  ? 19.402 5.646   11.227  0.34 19.99 ?  24  VAL   A HG13 1 
ATOM   634  H HG21 A VAL   A 1 24  ? 18.482 6.187   8.998   0.66 21.16 ?  24  VAL   A HG21 1 
ATOM   635  H HG21 B VAL   A 1 24  ? 18.421 5.728   8.376   0.34 18.64 ?  24  VAL   A HG21 1 
ATOM   636  H HG22 A VAL   A 1 24  ? 19.520 5.095   9.503   0.66 21.16 ?  24  VAL   A HG22 1 
ATOM   637  H HG22 B VAL   A 1 24  ? 19.324 4.497   8.803   0.34 18.64 ?  24  VAL   A HG22 1 
ATOM   638  H HG23 A VAL   A 1 24  ? 18.232 4.648   8.689   0.66 21.16 ?  24  VAL   A HG23 1 
ATOM   639  H HG23 B VAL   A 1 24  ? 17.879 4.246   8.199   0.34 18.64 ?  24  VAL   A HG23 1 
ATOM   640  N N    A GLU   A 1 25  ? 16.117 3.655   12.795  0.66 17.09 ?  25  GLU   A N    1 
ATOM   641  N N    B GLU   A 1 25  ? 15.984 3.445   12.284  0.34 17.05 ?  25  GLU   A N    1 
ATOM   642  C CA   A GLU   A 1 25  ? 15.534 3.592   14.131  0.66 18.40 ?  25  GLU   A CA   1 
ATOM   643  C CA   B GLU   A 1 25  ? 15.308 3.380   13.576  0.34 18.05 ?  25  GLU   A CA   1 
ATOM   644  C C    A GLU   A 1 25  ? 15.765 2.230   14.774  0.66 17.30 ?  25  GLU   A C    1 
ATOM   645  C C    B GLU   A 1 25  ? 15.555 2.042   14.264  0.34 18.08 ?  25  GLU   A C    1 
ATOM   646  O O    A GLU   A 1 25  ? 15.996 2.144   15.986  0.66 17.85 ?  25  GLU   A O    1 
ATOM   647  O O    B GLU   A 1 25  ? 15.746 1.995   15.485  0.34 18.55 ?  25  GLU   A O    1 
ATOM   648  C CB   A GLU   A 1 25  ? 14.046 3.942   14.070  0.66 21.02 ?  25  GLU   A CB   1 
ATOM   649  C CB   B GLU   A 1 25  ? 13.812 3.648   13.402  0.34 19.61 ?  25  GLU   A CB   1 
ATOM   650  C CG   A GLU   A 1 25  ? 13.789 5.395   13.691  0.66 24.24 ?  25  GLU   A CG   1 
ATOM   651  C CG   B GLU   A 1 25  ? 13.502 5.063   12.941  0.34 21.95 ?  25  GLU   A CG   1 
ATOM   652  C CD   A GLU   A 1 25  ? 14.587 6.375   14.543  0.66 27.09 ?  25  GLU   A CD   1 
ATOM   653  C CD   B GLU   A 1 25  ? 14.029 6.112   13.894  0.34 23.98 ?  25  GLU   A CD   1 
ATOM   654  O OE1  A GLU   A 1 25  ? 14.582 6.232   15.785  0.66 28.01 ?  25  GLU   A OE1  1 
ATOM   655  O OE1  B GLU   A 1 25  ? 13.912 5.910   15.122  0.34 24.98 ?  25  GLU   A OE1  1 
ATOM   656  O OE2  A GLU   A 1 25  ? 15.240 7.272   13.968  0.66 28.09 -1 25  GLU   A OE2  1 
ATOM   657  O OE2  B GLU   A 1 25  ? 14.567 7.131   13.416  0.34 24.76 -1 25  GLU   A OE2  1 
ATOM   658  H H    A GLU   A 1 25  ? 15.546 3.720   12.155  0.66 20.48 ?  25  GLU   A H    1 
ATOM   659  H H    B GLU   A 1 25  ? 15.460 3.448   11.601  0.34 20.43 ?  25  GLU   A H    1 
ATOM   660  H HA   A GLU   A 1 25  ? 15.975 4.245   14.692  0.66 22.05 ?  25  GLU   A HA   1 
ATOM   661  H HA   B GLU   A 1 25  ? 15.669 4.074   14.148  0.34 21.63 ?  25  GLU   A HA   1 
ATOM   662  H HB2  A GLU   A 1 25  ? 13.613 3.381   13.403  0.66 25.20 ?  25  GLU   A HB2  1 
ATOM   663  H HB2  B GLU   A 1 25  ? 13.457 3.037   12.737  0.34 23.51 ?  25  GLU   A HB2  1 
ATOM   664  H HB3  A GLU   A 1 25  ? 13.645 3.786   14.939  0.66 25.20 ?  25  GLU   A HB3  1 
ATOM   665  H HB3  B GLU   A 1 25  ? 13.366 3.508   14.251  0.34 23.51 ?  25  GLU   A HB3  1 
ATOM   666  H HG2  A GLU   A 1 25  ? 14.054 5.532   12.770  0.66 29.06 ?  25  GLU   A HG2  1 
ATOM   667  H HG2  B GLU   A 1 25  ? 13.906 5.210   12.071  0.34 26.32 ?  25  GLU   A HG2  1 
ATOM   668  H HG3  A GLU   A 1 25  ? 12.842 5.586   13.799  0.66 29.06 ?  25  GLU   A HG3  1 
ATOM   669  H HG3  B GLU   A 1 25  ? 12.543 5.181   12.890  0.34 26.32 ?  25  GLU   A HG3  1 
ATOM   670  N N    A GLU   A 1 26  ? 15.729 1.158   13.979  0.66 17.18 ?  26  GLU   A N    1 
ATOM   671  N N    B GLU   A 1 26  ? 15.555 0.944   13.503  0.34 17.52 ?  26  GLU   A N    1 
ATOM   672  C CA   A GLU   A 1 26  ? 16.012 -0.170  14.515  0.66 16.77 ?  26  GLU   A CA   1 
ATOM   673  C CA   B GLU   A 1 26  ? 15.901 -0.352  14.083  0.34 17.58 ?  26  GLU   A CA   1 
ATOM   674  C C    A GLU   A 1 26  ? 17.439 -0.251  15.041  0.66 16.51 ?  26  GLU   A C    1 
ATOM   675  C C    B GLU   A 1 26  ? 17.296 -0.325  14.694  0.34 17.18 ?  26  GLU   A C    1 
ATOM   676  O O    A GLU   A 1 26  ? 17.685 -0.771  16.135  0.66 17.03 ?  26  GLU   A O    1 
ATOM   677  O O    B GLU   A 1 26  ? 17.509 -0.835  15.799  0.34 17.22 ?  26  GLU   A O    1 
ATOM   678  C CB   A GLU   A 1 26  ? 15.793 -1.229  13.434  0.66 18.35 ?  26  GLU   A CB   1 
ATOM   679  C CB   B GLU   A 1 26  ? 15.837 -1.452  13.020  0.34 18.14 ?  26  GLU   A CB   1 
ATOM   680  C CG   A GLU   A 1 26  ? 14.357 -1.635  13.203  0.66 21.41 ?  26  GLU   A CG   1 
ATOM   681  C CG   B GLU   A 1 26  ? 14.638 -2.416  13.091  0.34 18.02 ?  26  GLU   A CG   1 
ATOM   682  C CD   A GLU   A 1 26  ? 13.791 -2.437  14.347  0.66 22.61 ?  26  GLU   A CD   1 
ATOM   683  C CD   B GLU   A 1 26  ? 14.314 -2.986  14.481  0.34 16.82 ?  26  GLU   A CD   1 
ATOM   684  O OE1  A GLU   A 1 26  ? 14.395 -3.453  14.751  0.66 23.26 ?  26  GLU   A OE1  1 
ATOM   685  O OE1  B GLU   A 1 26  ? 13.719 -2.253  15.289  0.34 16.37 ?  26  GLU   A OE1  1 
ATOM   686  O OE2  A GLU   A 1 26  ? 12.739 -2.024  14.852  0.66 23.68 -1 26  GLU   A OE2  1 
ATOM   687  O OE2  B GLU   A 1 26  ? 14.592 -4.180  14.758  0.34 16.71 -1 26  GLU   A OE2  1 
ATOM   688  H H    A GLU   A 1 26  ? 15.562 1.177   13.138  0.66 20.58 ?  26  GLU   A H    1 
ATOM   689  H H    B GLU   A 1 26  ? 15.358 0.927   12.668  0.34 21.00 ?  26  GLU   A H    1 
ATOM   690  H HA   A GLU   A 1 26  ? 15.414 -0.353  15.249  0.66 20.10 ?  26  GLU   A HA   1 
ATOM   691  H HA   B GLU   A 1 26  ? 15.271 -0.557  14.784  0.34 21.07 ?  26  GLU   A HA   1 
ATOM   692  H HB2  A GLU   A 1 26  ? 16.135 -0.886  12.593  0.66 22.00 ?  26  GLU   A HB2  1 
ATOM   693  H HB2  B GLU   A 1 26  ? 15.813 -1.025  12.141  0.34 21.74 ?  26  GLU   A HB2  1 
ATOM   694  H HB3  A GLU   A 1 26  ? 16.289 -2.026  13.681  0.66 22.00 ?  26  GLU   A HB3  1 
ATOM   695  H HB3  B GLU   A 1 26  ? 16.643 -1.986  13.084  0.34 21.74 ?  26  GLU   A HB3  1 
ATOM   696  H HG2  A GLU   A 1 26  ? 13.806 -0.844  13.130  0.66 25.67 ?  26  GLU   A HG2  1 
ATOM   697  H HG2  B GLU   A 1 26  ? 13.862 -1.934  12.785  0.34 21.60 ?  26  GLU   A HG2  1 
ATOM   698  H HG3  A GLU   A 1 26  ? 14.298 -2.157  12.386  0.66 25.67 ?  26  GLU   A HG3  1 
ATOM   699  H HG3  B GLU   A 1 26  ? 14.814 -3.169  12.511  0.34 21.60 ?  26  GLU   A HG3  1 
ATOM   700  N N    A ALA   A 1 27  ? 18.402 0.249   14.265  0.66 15.92 ?  27  ALA   A N    1 
ATOM   701  N N    B ALA   A 1 27  ? 18.264 0.261   13.985  0.34 16.72 ?  27  ALA   A N    1 
ATOM   702  C CA   A ALA   A 1 27  ? 19.792 0.210   14.707  0.66 15.88 ?  27  ALA   A CA   1 
ATOM   703  C CA   B ALA   A 1 27  ? 19.643 0.234   14.463  0.34 16.95 ?  27  ALA   A CA   1 
ATOM   704  C C    A ALA   A 1 27  ? 19.983 1.023   15.980  0.66 17.10 ?  27  ALA   A C    1 
ATOM   705  C C    B ALA   A 1 27  ? 19.803 1.040   15.746  0.34 18.34 ?  27  ALA   A C    1 
ATOM   706  O O    A ALA   A 1 27  ? 20.654 0.576   16.918  0.66 17.08 ?  27  ALA   A O    1 
ATOM   707  O O    B ALA   A 1 27  ? 20.498 0.610   16.673  0.34 18.81 ?  27  ALA   A O    1 
ATOM   708  C CB   A ALA   A 1 27  ? 20.714 0.716   13.595  0.66 15.46 ?  27  ALA   A CB   1 
ATOM   709  C CB   B ALA   A 1 27  ? 20.588 0.752   13.378  0.34 16.29 ?  27  ALA   A CB   1 
ATOM   710  H H    A ALA   A 1 27  ? 18.285 0.616   13.499  0.66 19.07 ?  27  ALA   A H    1 
ATOM   711  H H    B ALA   A 1 27  ? 18.148 0.674   13.239  0.34 20.04 ?  27  ALA   A H    1 
ATOM   712  H HA   A ALA   A 1 27  ? 20.041 -0.704  14.901  0.66 19.03 ?  27  ALA   A HA   1 
ATOM   713  H HA   B ALA   A 1 27  ? 19.888 -0.683  14.655  0.34 20.31 ?  27  ALA   A HA   1 
ATOM   714  H HB1  A ALA   A 1 27  ? 21.639 0.684   13.904  0.66 18.52 ?  27  ALA   A HB1  1 
ATOM   715  H HB1  B ALA   A 1 27  ? 21.499 0.724   13.715  0.34 19.52 ?  27  ALA   A HB1  1 
ATOM   716  H HB2  A ALA   A 1 27  ? 20.614 0.147   12.815  0.66 18.52 ?  27  ALA   A HB2  1 
ATOM   717  H HB2  B ALA   A 1 27  ? 20.510 0.187   12.593  0.34 19.52 ?  27  ALA   A HB2  1 
ATOM   718  H HB3  A ALA   A 1 27  ? 20.479 1.630   13.371  0.66 18.52 ?  27  ALA   A HB3  1 
ATOM   719  H HB3  B ALA   A 1 27  ? 20.347 1.664   13.156  0.34 19.52 ?  27  ALA   A HB3  1 
ATOM   720  N N    A LYS   A 1 28  ? 19.398 2.220   16.037  0.66 19.03 ?  28  LYS   A N    1 
ATOM   721  N N    B LYS   A 1 28  ? 19.166 2.211   15.822  0.34 20.00 ?  28  LYS   A N    1 
ATOM   722  C CA   A LYS   A 1 28  ? 19.530 3.039   17.239  0.66 22.08 ?  28  LYS   A CA   1 
ATOM   723  C CA   B LYS   A 1 28  ? 19.338 3.066   16.993  0.34 22.35 ?  28  LYS   A CA   1 
ATOM   724  C C    A LYS   A 1 28  ? 18.968 2.319   18.459  0.66 23.34 ?  28  LYS   A C    1 
ATOM   725  C C    B LYS   A 1 28  ? 18.836 2.400   18.268  0.34 23.88 ?  28  LYS   A C    1 
ATOM   726  O O    A LYS   A 1 28  ? 19.541 2.396   19.551  0.66 25.18 ?  28  LYS   A O    1 
ATOM   727  O O    B LYS   A 1 28  ? 19.356 2.675   19.355  0.34 24.52 ?  28  LYS   A O    1 
ATOM   728  C CB   A LYS   A 1 28  ? 18.872 4.406   17.028  0.66 24.22 ?  28  LYS   A CB   1 
ATOM   729  C CB   B LYS   A 1 28  ? 18.638 4.408   16.777  0.34 23.64 ?  28  LYS   A CB   1 
ATOM   730  C CG   A LYS   A 1 28  ? 19.701 5.342   16.161  0.66 26.73 ?  28  LYS   A CG   1 
ATOM   731  C CG   B LYS   A 1 28  ? 19.314 5.271   15.725  0.34 25.28 ?  28  LYS   A CG   1 
ATOM   732  C CD   A LYS   A 1 28  ? 19.227 6.781   16.252  0.66 29.72 ?  28  LYS   A CD   1 
ATOM   733  C CD   B LYS   A 1 28  ? 18.861 6.721   15.780  0.34 27.34 ?  28  LYS   A CD   1 
ATOM   734  C CE   A LYS   A 1 28  ? 17.918 6.978   15.521  0.66 31.50 ?  28  LYS   A CE   1 
ATOM   735  C CE   B LYS   A 1 28  ? 17.542 6.934   15.060  0.34 28.82 ?  28  LYS   A CE   1 
ATOM   736  N NZ   A LYS   A 1 28  ? 17.538 8.415   15.471  0.66 32.96 ?  28  LYS   A NZ   1 
ATOM   737  N NZ   B LYS   A 1 28  ? 17.280 8.384   14.831  0.34 29.64 ?  28  LYS   A NZ   1 
ATOM   738  H H    A LYS   A 1 28  ? 18.936 2.574   15.411  0.66 22.81 ?  28  LYS   A H    1 
ATOM   739  H H    B LYS   A 1 28  ? 18.644 2.526   15.219  0.34 23.98 ?  28  LYS   A H    1 
ATOM   740  H HA   A LYS   A 1 28  ? 20.468 3.197   17.417  0.66 26.47 ?  28  LYS   A HA   1 
ATOM   741  H HA   B LYS   A 1 28  ? 20.283 3.246   17.106  0.34 26.79 ?  28  LYS   A HA   1 
ATOM   742  H HB2  A LYS   A 1 28  ? 18.016 4.288   16.590  0.66 29.04 ?  28  LYS   A HB2  1 
ATOM   743  H HB2  B LYS   A 1 28  ? 17.726 4.242   16.492  0.34 28.34 ?  28  LYS   A HB2  1 
ATOM   744  H HB3  A LYS   A 1 28  ? 18.747 4.842   17.886  0.66 29.04 ?  28  LYS   A HB3  1 
ATOM   745  H HB3  B LYS   A 1 28  ? 18.639 4.896   17.615  0.34 28.34 ?  28  LYS   A HB3  1 
ATOM   746  H HG2  A LYS   A 1 28  ? 20.625 5.313   16.453  0.66 32.05 ?  28  LYS   A HG2  1 
ATOM   747  H HG2  B LYS   A 1 28  ? 20.272 5.249   15.868  0.34 30.31 ?  28  LYS   A HG2  1 
ATOM   748  H HG3  A LYS   A 1 28  ? 19.634 5.063   15.235  0.66 32.05 ?  28  LYS   A HG3  1 
ATOM   749  H HG3  B LYS   A 1 28  ? 19.102 4.922   14.846  0.34 30.31 ?  28  LYS   A HG3  1 
ATOM   750  H HD2  A LYS   A 1 28  ? 19.093 7.017   17.184  0.66 35.64 ?  28  LYS   A HD2  1 
ATOM   751  H HD2  B LYS   A 1 28  ? 18.745 6.985   16.707  0.34 32.78 ?  28  LYS   A HD2  1 
ATOM   752  H HD3  A LYS   A 1 28  ? 19.890 7.365   15.851  0.66 35.64 ?  28  LYS   A HD3  1 
ATOM   753  H HD3  B LYS   A 1 28  ? 19.531 7.279   15.356  0.34 32.78 ?  28  LYS   A HD3  1 
ATOM   754  H HE2  A LYS   A 1 28  ? 18.009 6.653   14.611  0.66 37.78 ?  28  LYS   A HE2  1 
ATOM   755  H HE2  B LYS   A 1 28  ? 17.571 6.489   14.198  0.34 34.56 ?  28  LYS   A HE2  1 
ATOM   756  H HE3  A LYS   A 1 28  ? 17.217 6.492   15.983  0.66 37.78 ?  28  LYS   A HE3  1 
ATOM   757  H HE3  B LYS   A 1 28  ? 16.820 6.575   15.599  0.34 34.56 ?  28  LYS   A HE3  1 
ATOM   758  H HZ1  A LYS   A 1 28  ? 16.768 8.510   15.036  0.66 39.53 ?  28  LYS   A HZ1  1 
ATOM   759  H HZ1  B LYS   A 1 28  ? 16.505 8.491   14.408  0.34 35.54 ?  28  LYS   A HZ1  1 
ATOM   760  H HZ2  A LYS   A 1 28  ? 17.448 8.735   16.296  0.66 39.53 ?  28  LYS   A HZ2  1 
ATOM   761  H HZ2  B LYS   A 1 28  ? 17.247 8.814   15.610  0.34 35.54 ?  28  LYS   A HZ2  1 
ATOM   762  H HZ3  A LYS   A 1 28  ? 18.168 8.881   15.047  0.66 39.53 ?  28  LYS   A HZ3  1 
ATOM   763  H HZ3  B LYS   A 1 28  ? 17.931 8.736   14.335  0.34 35.54 ?  28  LYS   A HZ3  1 
ATOM   764  N N    A LYS   A 1 29  ? 17.864 1.589   18.286  0.66 23.88 ?  29  LYS   A N    1 
ATOM   765  N N    B LYS   A 1 29  ? 17.833 1.528   18.160  0.34 25.08 ?  29  LYS   A N    1 
ATOM   766  C CA   A LYS   A 1 29  ? 17.263 0.865   19.404  0.66 25.55 ?  29  LYS   A CA   1 
ATOM   767  C CA   B LYS   A 1 29  ? 17.272 0.880   19.343  0.34 26.60 ?  29  LYS   A CA   1 
ATOM   768  C C    A LYS   A 1 29  ? 18.082 -0.368  19.775  0.66 25.28 ?  29  LYS   A C    1 
ATOM   769  C C    B LYS   A 1 29  ? 18.086 -0.344  19.753  0.34 25.70 ?  29  LYS   A C    1 
ATOM   770  O O    A LYS   A 1 29  ? 18.381 -0.595  20.954  0.66 26.52 ?  29  LYS   A O    1 
ATOM   771  O O    B LYS   A 1 29  ? 18.389 -0.531  20.936  0.34 26.48 ?  29  LYS   A O    1 
ATOM   772  C CB   A LYS   A 1 29  ? 15.829 0.460   19.052  0.66 28.13 ?  29  LYS   A CB   1 
ATOM   773  C CB   B LYS   A 1 29  ? 15.821 0.481   19.066  0.34 28.86 ?  29  LYS   A CB   1 
ATOM   774  C CG   A LYS   A 1 29  ? 15.085 -0.252  20.175  0.66 31.12 ?  29  LYS   A CG   1 
ATOM   775  C CG   B LYS   A 1 29  ? 15.104 -0.178  20.236  0.34 31.09 ?  29  LYS   A CG   1 
ATOM   776  C CD   A LYS   A 1 29  ? 14.755 0.698   21.316  0.66 34.08 ?  29  LYS   A CD   1 
ATOM   777  C CD   B LYS   A 1 29  ? 14.716 0.837   21.299  0.34 33.07 ?  29  LYS   A CD   1 
ATOM   778  C CE   A LYS   A 1 29  ? 13.878 0.025   22.362  0.66 35.73 ?  29  LYS   A CE   1 
ATOM   779  C CE   B LYS   A 1 29  ? 13.838 0.209   22.371  0.34 34.22 ?  29  LYS   A CE   1 
ATOM   780  N NZ   A LYS   A 1 29  ? 13.439 0.979   23.419  0.66 36.99 ?  29  LYS   A NZ   1 
ATOM   781  N NZ   B LYS   A 1 29  ? 13.383 1.210   23.376  0.34 35.03 ?  29  LYS   A NZ   1 
ATOM   782  H H    A LYS   A 1 29  ? 17.444 1.505   17.543  0.66 28.63 ?  29  LYS   A H    1 
ATOM   783  H H    B LYS   A 1 29  ? 17.454 1.304   17.420  0.34 30.07 ?  29  LYS   A H    1 
ATOM   784  H HA   A LYS   A 1 29  ? 17.226 1.445   20.181  0.66 30.64 ?  29  LYS   A HA   1 
ATOM   785  H HA   B LYS   A 1 29  ? 17.279 1.507   20.080  0.34 31.89 ?  29  LYS   A HA   1 
ATOM   786  H HB2  A LYS   A 1 29  ? 15.323 1.257   18.828  0.66 33.73 ?  29  LYS   A HB2  1 
ATOM   787  H HB2  B LYS   A 1 29  ? 15.323 1.279   18.830  0.34 34.60 ?  29  LYS   A HB2  1 
ATOM   788  H HB3  A LYS   A 1 29  ? 15.850 -0.139  18.290  0.66 33.73 ?  29  LYS   A HB3  1 
ATOM   789  H HB3  B LYS   A 1 29  ? 15.808 -0.143  18.325  0.34 34.60 ?  29  LYS   A HB3  1 
ATOM   790  H HG2  A LYS   A 1 29  ? 14.251 -0.610  19.831  0.66 37.32 ?  29  LYS   A HG2  1 
ATOM   791  H HG2  B LYS   A 1 29  ? 14.295 -0.600  19.911  0.34 37.29 ?  29  LYS   A HG2  1 
ATOM   792  H HG3  A LYS   A 1 29  ? 15.633 -0.972  20.529  0.66 37.32 ?  29  LYS   A HG3  1 
ATOM   793  H HG3  B LYS   A 1 29  ? 15.683 -0.841  20.645  0.34 37.29 ?  29  LYS   A HG3  1 
ATOM   794  H HD2  A LYS   A 1 29  ? 15.577 0.983   21.745  0.66 40.87 ?  29  LYS   A HD2  1 
ATOM   795  H HD2  B LYS   A 1 29  ? 15.518 1.180   21.723  0.34 39.66 ?  29  LYS   A HD2  1 
ATOM   796  H HD3  A LYS   A 1 29  ? 14.276 1.466   20.965  0.66 40.87 ?  29  LYS   A HD3  1 
ATOM   797  H HD3  B LYS   A 1 29  ? 14.219 1.560   20.884  0.34 39.66 ?  29  LYS   A HD3  1 
ATOM   798  H HE2  A LYS   A 1 29  ? 13.087 -0.334  21.931  0.66 42.84 ?  29  LYS   A HE2  1 
ATOM   799  H HE2  B LYS   A 1 29  ? 13.053 -0.180  21.954  0.34 41.04 ?  29  LYS   A HE2  1 
ATOM   800  H HE3  A LYS   A 1 29  ? 14.380 -0.688  22.787  0.66 42.84 ?  29  LYS   A HE3  1 
ATOM   801  H HE3  B LYS   A 1 29  ? 14.343 -0.478  22.835  0.34 41.04 ?  29  LYS   A HE3  1 
ATOM   802  H HZ1  A LYS   A 1 29  ? 12.929 0.559   24.015  0.66 44.36 ?  29  LYS   A HZ1  1 
ATOM   803  H HZ1  B LYS   A 1 29  ? 12.873 0.815   23.989  0.34 42.01 ?  29  LYS   A HZ1  1 
ATOM   804  H HZ2  A LYS   A 1 29  ? 14.148 1.320   23.834  0.66 44.36 ?  29  LYS   A HZ2  1 
ATOM   805  H HZ2  B LYS   A 1 29  ? 14.086 1.578   23.778  0.34 42.01 ?  29  LYS   A HZ2  1 
ATOM   806  H HZ3  A LYS   A 1 29  ? 12.971 1.642   23.054  0.66 44.36 ?  29  LYS   A HZ3  1 
ATOM   807  H HZ3  B LYS   A 1 29  ? 12.911 1.850   22.975  0.34 42.01 ?  29  LYS   A HZ3  1 
ATOM   808  N N    . VAL   A 1 30  ? 18.436 -1.189  18.785  1.00 24.09 ?  30  VAL   A N    1 
ATOM   809  C CA   . VAL   A 1 30  ? 19.077 -2.467  19.086  1.00 23.08 ?  30  VAL   A CA   1 
ATOM   810  C C    . VAL   A 1 30  ? 20.575 -2.314  19.333  1.00 21.86 ?  30  VAL   A C    1 
ATOM   811  O O    . VAL   A 1 30  ? 21.147 -3.031  20.162  1.00 22.77 ?  30  VAL   A O    1 
ATOM   812  C CB   . VAL   A 1 30  ? 18.785 -3.457  17.942  1.00 23.84 ?  30  VAL   A CB   1 
ATOM   813  C CG1  . VAL   A 1 30  ? 19.512 -4.777  18.163  1.00 24.09 ?  30  VAL   A CG1  1 
ATOM   814  C CG2  . VAL   A 1 30  ? 17.281 -3.684  17.801  1.00 24.28 ?  30  VAL   A CG2  1 
ATOM   815  H H    A VAL   A 1 30  ? 18.320 -1.035  17.948  0.66 28.88 ?  30  VAL   A H    1 
ATOM   816  H H    B VAL   A 1 30  ? 18.312 -1.048  17.947  0.34 28.88 ?  30  VAL   A H    1 
ATOM   817  H HA   . VAL   A 1 30  ? 18.675 -2.830  19.888  1.00 27.67 ?  30  VAL   A HA   1 
ATOM   818  H HB   . VAL   A 1 30  ? 19.107 -3.082  17.106  1.00 28.58 ?  30  VAL   A HB   1 
ATOM   819  H HG11 . VAL   A 1 30  ? 19.154 -5.442  17.551  1.00 28.88 ?  30  VAL   A HG11 1 
ATOM   820  H HG12 . VAL   A 1 30  ? 20.458 -4.653  17.997  1.00 28.88 ?  30  VAL   A HG12 1 
ATOM   821  H HG13 . VAL   A 1 30  ? 19.369 -5.066  19.079  1.00 28.88 ?  30  VAL   A HG13 1 
ATOM   822  H HG21 . VAL   A 1 30  ? 17.125 -4.357  17.119  1.00 29.11 ?  30  VAL   A HG21 1 
ATOM   823  H HG22 . VAL   A 1 30  ? 16.928 -3.985  18.651  1.00 29.11 ?  30  VAL   A HG22 1 
ATOM   824  H HG23 . VAL   A 1 30  ? 16.860 -2.849  17.543  1.00 29.11 ?  30  VAL   A HG23 1 
ATOM   825  N N    . LYS   A 1 31  ? 21.228 -1.389  18.642  1.00 20.62 ?  31  LYS   A N    1 
ATOM   826  C CA   . LYS   A 1 31  ? 22.683 -1.296  18.613  1.00 21.53 ?  31  LYS   A CA   1 
ATOM   827  C C    . LYS   A 1 31  ? 23.272 -2.668  18.277  1.00 19.59 ?  31  LYS   A C    1 
ATOM   828  O O    . LYS   A 1 31  ? 24.028 -3.240  19.071  1.00 21.21 ?  31  LYS   A O    1 
ATOM   829  C CB   . LYS   A 1 31  ? 23.249 -0.754  19.918  1.00 26.63 ?  31  LYS   A CB   1 
ATOM   830  C CG   . LYS   A 1 31  ? 22.588 0.537   20.382  1.00 33.11 ?  31  LYS   A CG   1 
ATOM   831  C CD   . LYS   A 1 31  ? 23.618 1.577   20.804  1.00 37.58 ?  31  LYS   A CD   1 
ATOM   832  C CE   . LYS   A 1 31  ? 23.000 2.653   21.689  1.00 40.26 ?  31  LYS   A CE   1 
ATOM   833  N NZ   . LYS   A 1 31  ? 21.846 3.346   21.052  1.00 42.34 ?  31  LYS   A NZ   1 
ATOM   834  H H    . LYS   A 1 31  ? 20.837 -0.787  18.170  1.00 24.72 ?  31  LYS   A H    1 
ATOM   835  H HA   . LYS   A 1 31  ? 22.931 -0.682  17.909  1.00 25.80 ?  31  LYS   A HA   1 
ATOM   836  H HB2  . LYS   A 1 31  ? 23.129 -1.417  20.612  1.00 31.93 ?  31  LYS   A HB2  1 
ATOM   837  H HB3  . LYS   A 1 31  ? 24.195 -0.574  19.793  1.00 31.93 ?  31  LYS   A HB3  1 
ATOM   838  H HG2  . LYS   A 1 31  ? 22.063 0.909   19.655  1.00 39.71 ?  31  LYS   A HG2  1 
ATOM   839  H HG3  . LYS   A 1 31  ? 22.019 0.349   21.144  1.00 39.71 ?  31  LYS   A HG3  1 
ATOM   840  H HD2  . LYS   A 1 31  ? 24.326 1.142   21.304  1.00 45.07 ?  31  LYS   A HD2  1 
ATOM   841  H HD3  . LYS   A 1 31  ? 23.981 2.006   20.012  1.00 45.07 ?  31  LYS   A HD3  1 
ATOM   842  H HE2  . LYS   A 1 31  ? 22.686 2.242   22.510  1.00 48.28 ?  31  LYS   A HE2  1 
ATOM   843  H HE3  . LYS   A 1 31  ? 23.675 3.320   21.890  1.00 48.28 ?  31  LYS   A HE3  1 
ATOM   844  H HZ1  . LYS   A 1 31  ? 21.524 3.968   21.602  1.00 50.78 ?  31  LYS   A HZ1  1 
ATOM   845  H HZ2  . LYS   A 1 31  ? 22.103 3.735   20.295  1.00 50.78 ?  31  LYS   A HZ2  1 
ATOM   846  H HZ3  . LYS   A 1 31  ? 21.200 2.760   20.872  1.00 50.78 ?  31  LYS   A HZ3  1 
ATOM   847  N N    . PRO   A 1 32  ? 22.929 -3.222  17.119  1.00 17.16 ?  32  PRO   A N    1 
ATOM   848  C CA   . PRO   A 1 32  ? 23.393 -4.564  16.774  1.00 17.43 ?  32  PRO   A CA   1 
ATOM   849  C C    . PRO   A 1 32  ? 24.893 -4.584  16.569  1.00 16.97 ?  32  PRO   A C    1 
ATOM   850  O O    . PRO   A 1 32  ? 25.541 -3.556  16.366  1.00 17.11 ?  32  PRO   A O    1 
ATOM   851  C CB   . PRO   A 1 32  ? 22.667 -4.848  15.457  1.00 17.70 ?  32  PRO   A CB   1 
ATOM   852  C CG   . PRO   A 1 32  ? 22.519 -3.490  14.839  1.00 16.07 ?  32  PRO   A CG   1 
ATOM   853  C CD   . PRO   A 1 32  ? 22.215 -2.588  15.999  1.00 16.25 ?  32  PRO   A CD   1 
ATOM   854  H HA   . PRO   A 1 32  ? 23.138 -5.208  17.451  1.00 20.89 ?  32  PRO   A HA   1 
ATOM   855  H HB2  . PRO   A 1 32  ? 23.209 -5.434  14.900  1.00 21.21 ?  32  PRO   A HB2  1 
ATOM   856  H HB3  . PRO   A 1 32  ? 21.802 -5.251  15.639  1.00 21.21 ?  32  PRO   A HB3  1 
ATOM   857  H HG2  . PRO   A 1 32  ? 23.347 -3.243  14.403  1.00 19.25 ?  32  PRO   A HG2  1 
ATOM   858  H HG3  . PRO   A 1 32  ? 21.784 -3.507  14.203  1.00 19.25 ?  32  PRO   A HG3  1 
ATOM   859  H HD2  . PRO   A 1 32  ? 22.566 -1.701  15.820  1.00 19.48 ?  32  PRO   A HD2  1 
ATOM   860  H HD3  . PRO   A 1 32  ? 21.263 -2.571  16.167  1.00 19.48 ?  32  PRO   A HD3  1 
ATOM   861  N N    . THR   A 1 33  ? 25.443 -5.793  16.602  1.00 16.67 ?  33  THR   A N    1 
ATOM   862  C CA   . THR   A 1 33  ? 26.856 -5.956  16.295  1.00 16.86 ?  33  THR   A CA   1 
ATOM   863  C C    . THR   A 1 33  ? 27.162 -5.497  14.876  1.00 15.26 ?  33  THR   A C    1 
ATOM   864  O O    . THR   A 1 33  ? 28.197 -4.861  14.633  1.00 16.16 ?  33  THR   A O    1 
ATOM   865  C CB   . THR   A 1 33  ? 27.255 -7.415  16.499  1.00 18.94 ?  33  THR   A CB   1 
ATOM   866  O OG1  . THR   A 1 33  ? 26.918 -7.813  17.833  1.00 20.81 ?  33  THR   A OG1  1 
ATOM   867  C CG2  . THR   A 1 33  ? 28.748 -7.602  16.277  1.00 20.09 ?  33  THR   A CG2  1 
ATOM   868  H H    . THR   A 1 33  ? 25.028 -6.523  16.798  1.00 19.97 ?  33  THR   A H    1 
ATOM   869  H HA   . THR   A 1 33  ? 27.381 -5.419  16.911  1.00 20.20 ?  33  THR   A HA   1 
ATOM   870  H HB   . THR   A 1 33  ? 26.779 -7.980  15.867  1.00 22.70 ?  33  THR   A HB   1 
ATOM   871  H HG1  . THR   A 1 33  ? 27.339 -7.342  18.390  1.00 24.95 ?  33  THR   A HG1  1 
ATOM   872  H HG21 . THR   A 1 33  ? 29.018 -8.492  16.560  1.00 24.08 ?  33  THR   A HG21 1 
ATOM   873  H HG22 . THR   A 1 33  ? 28.961 -7.494  15.338  1.00 24.08 ?  33  THR   A HG22 1 
ATOM   874  H HG23 . THR   A 1 33  ? 29.243 -6.948  16.793  1.00 24.08 ?  33  THR   A HG23 1 
ATOM   875  N N    . VAL   A 1 34  ? 26.277 -5.806  13.930  1.00 13.89 ?  34  VAL   A N    1 
ATOM   876  C CA   . VAL   A 1 34  ? 26.482 -5.475  12.525  1.00 12.82 ?  34  VAL   A CA   1 
ATOM   877  C C    . VAL   A 1 34  ? 25.189 -4.908  11.950  1.00 12.03 ?  34  VAL   A C    1 
ATOM   878  O O    . VAL   A 1 34  ? 24.147 -5.577  11.980  1.00 12.95 ?  34  VAL   A O    1 
ATOM   879  C CB   . VAL   A 1 34  ? 26.916 -6.688  11.686  1.00 13.61 ?  34  VAL   A CB   1 
ATOM   880  C CG1  . VAL   A 1 34  ? 27.075 -6.281  10.231  1.00 13.75 ?  34  VAL   A CG1  1 
ATOM   881  C CG2  . VAL   A 1 34  ? 28.202 -7.299  12.237  1.00 15.02 ?  34  VAL   A CG2  1 
ATOM   882  H H    . VAL   A 1 34  ? 25.533 -6.217  14.086  1.00 16.65 ?  34  VAL   A H    1 
ATOM   883  H HA   . VAL   A 1 34  ? 27.168 -4.792  12.454  1.00 15.36 ?  34  VAL   A HA   1 
ATOM   884  H HB   . VAL   A 1 34  ? 26.220 -7.364  11.740  1.00 16.31 ?  34  VAL   A HB   1 
ATOM   885  H HG11 . VAL   A 1 34  ? 27.592 -6.960  9.774   1.00 16.47 ?  34  VAL   A HG11 1 
ATOM   886  H HG12 . VAL   A 1 34  ? 26.196 -6.207  9.825   1.00 16.47 ?  34  VAL   A HG12 1 
ATOM   887  H HG13 . VAL   A 1 34  ? 27.535 -5.430  10.191  1.00 16.47 ?  34  VAL   A HG13 1 
ATOM   888  H HG21 . VAL   A 1 34  ? 28.461 -8.046  11.674  1.00 18.00 ?  34  VAL   A HG21 1 
ATOM   889  H HG22 . VAL   A 1 34  ? 28.898 -6.626  12.236  1.00 18.00 ?  34  VAL   A HG22 1 
ATOM   890  H HG23 . VAL   A 1 34  ? 28.045 -7.611  13.145  1.00 18.00 ?  34  VAL   A HG23 1 
ATOM   891  N N    . VAL   A 1 35  ? 25.257 -3.694  11.404  1.00 11.48 ?  35  VAL   A N    1 
ATOM   892  C CA   . VAL   A 1 35  ? 24.227 -3.175  10.512  1.00 11.06 ?  35  VAL   A CA   1 
ATOM   893  C C    . VAL   A 1 35  ? 24.781 -3.176  9.094   1.00 10.97 ?  35  VAL   A C    1 
ATOM   894  O O    . VAL   A 1 35  ? 25.931 -2.781  8.870   1.00 11.21 ?  35  VAL   A O    1 
ATOM   895  C CB   . VAL   A 1 35  ? 23.700 -1.782  10.923  1.00 12.06 ?  35  VAL   A CB   1 
ATOM   896  C CG1  . VAL   A 1 35  ? 24.767 -0.691  10.794  1.00 12.67 ?  35  VAL   A CG1  1 
ATOM   897  C CG2  . VAL   A 1 35  ? 22.470 -1.436  10.093  1.00 12.54 ?  35  VAL   A CG2  1 
ATOM   898  H H    . VAL   A 1 35  ? 25.901 -3.139  11.533  1.00 13.75 ?  35  VAL   A H    1 
ATOM   899  H HA   . VAL   A 1 35  ? 23.468 -3.784  10.527  1.00 13.24 ?  35  VAL   A HA   1 
ATOM   900  H HB   . VAL   A 1 35  ? 23.416 -1.816  11.847  1.00 14.45 ?  35  VAL   A HB   1 
ATOM   901  H HG11 . VAL   A 1 35  ? 24.419 0.138   11.164  1.00 15.17 ?  35  VAL   A HG11 1 
ATOM   902  H HG12 . VAL   A 1 35  ? 25.555 -0.965  11.281  1.00 15.17 ?  35  VAL   A HG12 1 
ATOM   903  H HG13 . VAL   A 1 35  ? 24.982 -0.563  9.855   1.00 15.17 ?  35  VAL   A HG13 1 
ATOM   904  H HG21 . VAL   A 1 35  ? 22.099 -0.597  10.405  1.00 15.02 ?  35  VAL   A HG21 1 
ATOM   905  H HG22 . VAL   A 1 35  ? 22.727 -1.354  9.158   1.00 15.02 ?  35  VAL   A HG22 1 
ATOM   906  H HG23 . VAL   A 1 35  ? 21.810 -2.144  10.188  1.00 15.02 ?  35  VAL   A HG23 1 
ATOM   907  N N    . VAL   A 1 36  ? 23.961 -3.616  8.137   1.00 10.29 ?  36  VAL   A N    1 
ATOM   908  C CA   . VAL   A 1 36  ? 24.345 -3.631  6.732   1.00 9.56  ?  36  VAL   A CA   1 
ATOM   909  C C    . VAL   A 1 36  ? 23.891 -2.341  6.068   1.00 9.82  ?  36  VAL   A C    1 
ATOM   910  O O    . VAL   A 1 36  ? 22.730 -1.932  6.201   1.00 10.67 ?  36  VAL   A O    1 
ATOM   911  C CB   . VAL   A 1 36  ? 23.743 -4.846  6.007   1.00 10.10 ?  36  VAL   A CB   1 
ATOM   912  C CG1  . VAL   A 1 36  ? 24.007 -4.762  4.511   1.00 10.52 ?  36  VAL   A CG1  1 
ATOM   913  C CG2  . VAL   A 1 36  ? 24.304 -6.139  6.579   1.00 11.07 ?  36  VAL   A CG2  1 
ATOM   914  H H    . VAL   A 1 36  ? 23.165 -3.920  8.281   1.00 12.33 ?  36  VAL   A H    1 
ATOM   915  H HA   . VAL   A 1 36  ? 25.313 -3.694  6.664   1.00 11.45 ?  36  VAL   A HA   1 
ATOM   916  H HB   . VAL   A 1 36  ? 22.780 -4.848  6.138   1.00 12.09 ?  36  VAL   A HB   1 
ATOM   917  H HG11 . VAL   A 1 36  ? 23.875 -5.636  4.117   1.00 12.60 ?  36  VAL   A HG11 1 
ATOM   918  H HG12 . VAL   A 1 36  ? 23.392 -4.124  4.112   1.00 12.60 ?  36  VAL   A HG12 1 
ATOM   919  H HG13 . VAL   A 1 36  ? 24.922 -4.470  4.369   1.00 12.60 ?  36  VAL   A HG13 1 
ATOM   920  H HG21 . VAL   A 1 36  ? 23.921 -6.893  6.100   1.00 13.26 ?  36  VAL   A HG21 1 
ATOM   921  H HG22 . VAL   A 1 36  ? 25.270 -6.140  6.470   1.00 13.26 ?  36  VAL   A HG22 1 
ATOM   922  H HG23 . VAL   A 1 36  ? 24.078 -6.197  7.519   1.00 13.26 ?  36  VAL   A HG23 1 
ATOM   923  N N    . ASN   A 1 37  ? 24.815 -1.705  5.347   1.00 9.83  ?  37  ASN   A N    1 
ATOM   924  C CA   . ASN   A 1 37  ? 24.493 -0.584  4.478   1.00 9.46  ?  37  ASN   A CA   1 
ATOM   925  C C    . ASN   A 1 37  ? 24.371 -1.048  3.036   1.00 9.58  ?  37  ASN   A C    1 
ATOM   926  O O    . ASN   A 1 37  ? 25.158 -1.880  2.563   1.00 10.24 ?  37  ASN   A O    1 
ATOM   927  C CB   . ASN   A 1 37  ? 25.567 0.497   4.569   1.00 9.97  ?  37  ASN   A CB   1 
ATOM   928  C CG   . ASN   A 1 37  ? 25.248 1.693   3.713   1.00 10.09 ?  37  ASN   A CG   1 
ATOM   929  O OD1  . ASN   A 1 37  ? 24.081 2.037   3.518   1.00 10.41 ?  37  ASN   A OD1  1 
ATOM   930  N ND2  . ASN   A 1 37  ? 26.291 2.337   3.194   1.00 10.53 ?  37  ASN   A ND2  1 
ATOM   931  H H    . ASN   A 1 37  ? 25.653 -1.907  5.351   1.00 11.77 ?  37  ASN   A H    1 
ATOM   932  H HA   . ASN   A 1 37  ? 23.650 -0.197  4.752   1.00 11.32 ?  37  ASN   A HA   1 
ATOM   933  H HB2  . ASN   A 1 37  ? 25.635 0.799   5.492   1.00 11.94 ?  37  ASN   A HB2  1 
ATOM   934  H HB3  . ASN   A 1 37  ? 26.417 0.130   4.279   1.00 11.94 ?  37  ASN   A HB3  1 
ATOM   935  H HD21 . ASN   A 1 37  ? 26.164 3.023   2.692   1.00 12.61 ?  37  ASN   A HD21 1 
ATOM   936  H HD22 . ASN   A 1 37  ? 27.086 2.069   3.354   1.00 12.61 ?  37  ASN   A HD22 1 
ATOM   937  N N    A ALA   A 1 38  ? 23.368 -0.504  2.346   0.66 9.97  ?  38  ALA   A N    1 
ATOM   938  N N    B ALA   A 1 38  ? 23.380 -0.499  2.333   0.34 10.08 ?  38  ALA   A N    1 
ATOM   939  C CA   A ALA   A 1 38  ? 23.178 -0.679  0.908   0.66 10.17 ?  38  ALA   A CA   1 
ATOM   940  C CA   B ALA   A 1 38  ? 23.240 -0.696  0.891   0.34 10.52 ?  38  ALA   A CA   1 
ATOM   941  C C    A ALA   A 1 38  ? 24.082 0.323   0.191   0.66 10.42 ?  38  ALA   A C    1 
ATOM   942  C C    B ALA   A 1 38  ? 24.133 0.326   0.193   0.34 10.69 ?  38  ALA   A C    1 
ATOM   943  O O    A ALA   A 1 38  ? 23.664 1.409   -0.221  0.66 10.43 ?  38  ALA   A O    1 
ATOM   944  O O    B ALA   A 1 38  ? 23.697 1.396   -0.242  0.34 10.77 ?  38  ALA   A O    1 
ATOM   945  C CB   A ALA   A 1 38  ? 21.712 -0.464  0.545   0.66 11.79 ?  38  ALA   A CB   1 
ATOM   946  C CB   B ALA   A 1 38  ? 21.784 -0.557  0.464   0.34 11.51 ?  38  ALA   A CB   1 
ATOM   947  H H    A ALA   A 1 38  ? 22.769 -0.002  2.707   0.66 11.94 ?  38  ALA   A H    1 
ATOM   948  H H    B ALA   A 1 38  ? 22.770 0.005   2.676   0.34 12.07 ?  38  ALA   A H    1 
ATOM   949  H HA   A ALA   A 1 38  ? 23.435 -1.577  0.650   0.66 12.18 ?  38  ALA   A HA   1 
ATOM   950  H HA   B ALA   A 1 38  ? 23.548 -1.581  0.654   0.34 12.59 ?  38  ALA   A HA   1 
ATOM   951  H HB1  A ALA   A 1 38  ? 21.600 -0.585  -0.411  0.66 14.12 ?  38  ALA   A HB1  1 
ATOM   952  H HB1  B ALA   A 1 38  ? 21.719 -0.722  -0.490  0.34 13.78 ?  38  ALA   A HB1  1 
ATOM   953  H HB2  A ALA   A 1 38  ? 21.167 -1.108  1.025   0.66 14.12 ?  38  ALA   A HB2  1 
ATOM   954  H HB2  B ALA   A 1 38  ? 21.250 -1.204  0.949   0.34 13.78 ?  38  ALA   A HB2  1 
ATOM   955  H HB3  A ALA   A 1 38  ? 21.451 0.438   0.796   0.66 14.12 ?  38  ALA   A HB3  1 
ATOM   956  H HB3  B ALA   A 1 38  ? 21.480 0.342   0.664   0.34 13.78 ?  38  ALA   A HB3  1 
ATOM   957  N N    A ALA   A 1 39  ? 25.348 -0.055  0.045   0.66 10.22 ?  39  ALA   A N    1 
ATOM   958  N N    B ALA   A 1 39  ? 25.411 -0.019  0.087   0.34 10.61 ?  39  ALA   A N    1 
ATOM   959  C CA   A ALA   A 1 39  ? 26.393 0.833   -0.436  0.66 9.98  ?  39  ALA   A CA   1 
ATOM   960  C CA   B ALA   A 1 39  ? 26.427 0.896   -0.402  0.34 10.96 ?  39  ALA   A CA   1 
ATOM   961  C C    A ALA   A 1 39  ? 26.506 0.808   -1.959  0.66 10.24 ?  39  ALA   A C    1 
ATOM   962  C C    B ALA   A 1 39  ? 26.600 0.776   -1.912  0.34 10.63 ?  39  ALA   A C    1 
ATOM   963  O O    A ALA   A 1 39  ? 25.990 -0.080  -2.641  0.66 10.47 ?  39  ALA   A O    1 
ATOM   964  O O    B ALA   A 1 39  ? 26.196 -0.206  -2.538  0.34 9.80  ?  39  ALA   A O    1 
ATOM   965  C CB   A ALA   A 1 39  ? 27.726 0.424   0.192   0.66 10.63 ?  39  ALA   A CB   1 
ATOM   966  C CB   B ALA   A 1 39  ? 27.760 0.607   0.288   0.34 11.92 ?  39  ALA   A CB   1 
ATOM   967  H H    A ALA   A 1 39  ? 25.627 -0.852  0.229   0.66 12.24 ?  39  ALA   A H    1 
ATOM   968  H H    B ALA   A 1 39  ? 25.716 -0.800  0.296   0.34 12.70 ?  39  ALA   A H    1 
ATOM   969  H HA   A ALA   A 1 39  ? 26.186 1.737   -0.152  0.66 11.94 ?  39  ALA   A HA   1 
ATOM   970  H HA   B ALA   A 1 39  ? 26.165 1.803   -0.195  0.34 13.12 ?  39  ALA   A HA   1 
ATOM   971  H HB1  A ALA   A 1 39  ? 28.417 1.023   -0.127  0.66 12.73 ?  39  ALA   A HB1  1 
ATOM   972  H HB1  B ALA   A 1 39  ? 28.428 1.224   -0.047  0.34 14.27 ?  39  ALA   A HB1  1 
ATOM   973  H HB2  A ALA   A 1 39  ? 27.655 0.491   1.161   0.66 12.73 ?  39  ALA   A HB2  1 
ATOM   974  H HB2  B ALA   A 1 39  ? 27.651 0.724   1.246   0.34 14.27 ?  39  ALA   A HB2  1 
ATOM   975  H HB3  A ALA   A 1 39  ? 27.929 -0.488  -0.060  0.66 12.73 ?  39  ALA   A HB3  1 
ATOM   976  H HB3  B ALA   A 1 39  ? 28.026 -0.307  0.096   0.34 14.27 ?  39  ALA   A HB3  1 
ATOM   977  N N    . ASN   A 1 40  ? 27.218 1.803   -2.490  1.00 10.96 ?  40  ASN   A N    1 
ATOM   978  C CA   . ASN   A 1 40  ? 27.743 1.762   -3.849  1.00 11.15 ?  40  ASN   A CA   1 
ATOM   979  C C    . ASN   A 1 40  ? 29.268 1.648   -3.788  1.00 10.53 ?  40  ASN   A C    1 
ATOM   980  O O    . ASN   A 1 40  ? 29.875 1.738   -2.716  1.00 10.61 ?  40  ASN   A O    1 
ATOM   981  C CB   . ASN   A 1 40  ? 27.269 2.954   -4.695  1.00 11.79 ?  40  ASN   A CB   1 
ATOM   982  C CG   . ASN   A 1 40  ? 27.650 4.296   -4.106  1.00 12.83 ?  40  ASN   A CG   1 
ATOM   983  O OD1  . ASN   A 1 40  ? 28.822 4.558   -3.799  1.00 13.57 ?  40  ASN   A OD1  1 
ATOM   984  N ND2  . ASN   A 1 40  ? 26.651 5.164   -3.948  1.00 13.70 ?  40  ASN   A ND2  1 
ATOM   985  H H    A ASN   A 1 40  ? 27.417 2.524   -2.067  0.66 13.13 ?  40  ASN   A H    1 
ATOM   986  H H    B ASN   A 1 40  ? 27.352 2.554   -2.095  0.34 13.13 ?  40  ASN   A H    1 
ATOM   987  H HA   . ASN   A 1 40  ? 27.411 0.957   -4.280  1.00 13.35 ?  40  ASN   A HA   1 
ATOM   988  H HB2  . ASN   A 1 40  ? 27.664 2.886   -5.579  1.00 14.12 ?  40  ASN   A HB2  1 
ATOM   989  H HB3  . ASN   A 1 40  ? 26.301 2.921   -4.766  1.00 14.12 ?  40  ASN   A HB3  1 
ATOM   990  H HD21 . ASN   A 1 40  ? 26.811 5.949   -3.628  1.00 16.41 ?  40  ASN   A HD21 1 
ATOM   991  H HD22 . ASN   A 1 40  ? 25.853 4.950   -4.178  1.00 16.41 ?  40  ASN   A HD22 1 
ATOM   992  N N    . VAL   A 1 41  ? 29.887 1.399   -4.945  1.00 10.85 ?  41  VAL   A N    1 
ATOM   993  C CA   . VAL   A 1 41  ? 31.316 1.088   -4.969  1.00 11.47 ?  41  VAL   A CA   1 
ATOM   994  C C    . VAL   A 1 41  ? 32.180 2.236   -4.491  1.00 11.34 ?  41  VAL   A C    1 
ATOM   995  O O    . VAL   A 1 41  ? 33.321 2.010   -4.077  1.00 12.15 ?  41  VAL   A O    1 
ATOM   996  C CB   . VAL   A 1 41  ? 31.801 0.609   -6.356  1.00 12.95 ?  41  VAL   A CB   1 
ATOM   997  C CG1  . VAL   A 1 41  ? 31.114 -0.702  -6.746  1.00 13.59 ?  41  VAL   A CG1  1 
ATOM   998  C CG2  . VAL   A 1 41  ? 31.628 1.680   -7.424  1.00 13.78 ?  41  VAL   A CG2  1 
ATOM   999  H H    . VAL   A 1 41  ? 29.509 1.395   -5.718  1.00 12.99 ?  41  VAL   A H    1 
ATOM   1000 H HA   . VAL   A 1 41  ? 31.470 0.348   -4.352  1.00 13.73 ?  41  VAL   A HA   1 
ATOM   1001 H HB   . VAL   A 1 41  ? 32.750 0.415   -6.293  1.00 15.51 ?  41  VAL   A HB   1 
ATOM   1002 H HG11 . VAL   A 1 41  ? 31.455 -0.996  -7.606  1.00 16.29 ?  41  VAL   A HG11 1 
ATOM   1003 H HG12 . VAL   A 1 41  ? 31.304 -1.375  -6.070  1.00 16.29 ?  41  VAL   A HG12 1 
ATOM   1004 H HG13 . VAL   A 1 41  ? 30.158 -0.554  -6.803  1.00 16.29 ?  41  VAL   A HG13 1 
ATOM   1005 H HG21 . VAL   A 1 41  ? 31.868 1.305   -8.288  1.00 16.51 ?  41  VAL   A HG21 1 
ATOM   1006 H HG22 . VAL   A 1 41  ? 30.707 1.973   -7.434  1.00 16.51 ?  41  VAL   A HG22 1 
ATOM   1007 H HG23 . VAL   A 1 41  ? 32.213 2.426   -7.217  1.00 16.51 ?  41  VAL   A HG23 1 
ATOM   1008 N N    . TYR   A 1 42  ? 31.676 3.467   -4.559  1.00 11.50 ?  42  TYR   A N    1 
ATOM   1009 C CA   . TYR   A 1 42  ? 32.415 4.650   -4.138  1.00 11.47 ?  42  TYR   A CA   1 
ATOM   1010 C C    . TYR   A 1 42  ? 32.155 5.020   -2.688  1.00 11.09 ?  42  TYR   A C    1 
ATOM   1011 O O    . TYR   A 1 42  ? 32.718 6.008   -2.200  1.00 11.71 ?  42  TYR   A O    1 
ATOM   1012 C CB   . TYR   A 1 42  ? 32.067 5.840   -5.048  1.00 12.42 ?  42  TYR   A CB   1 
ATOM   1013 C CG   . TYR   A 1 42  ? 32.248 5.531   -6.515  1.00 13.30 ?  42  TYR   A CG   1 
ATOM   1014 C CD1  . TYR   A 1 42  ? 33.510 5.331   -7.048  1.00 13.94 ?  42  TYR   A CD1  1 
ATOM   1015 C CD2  . TYR   A 1 42  ? 31.157 5.407   -7.361  1.00 14.58 ?  42  TYR   A CD2  1 
ATOM   1016 C CE1  . TYR   A 1 42  ? 33.682 5.027   -8.387  1.00 14.76 ?  42  TYR   A CE1  1 
ATOM   1017 C CE2  . TYR   A 1 42  ? 31.320 5.110   -8.702  1.00 15.58 ?  42  TYR   A CE2  1 
ATOM   1018 C CZ   . TYR   A 1 42  ? 32.587 4.921   -9.209  1.00 15.58 ?  42  TYR   A CZ   1 
ATOM   1019 O OH   . TYR   A 1 42  ? 32.748 4.616   -10.542 1.00 17.34 ?  42  TYR   A OH   1 
ATOM   1020 H H    . TYR   A 1 42  ? 30.887 3.643   -4.861  1.00 13.78 ?  42  TYR   A H    1 
ATOM   1021 H HA   . TYR   A 1 42  ? 33.363 4.479   -4.237  1.00 13.73 ?  42  TYR   A HA   1 
ATOM   1022 H HB2  . TYR   A 1 42  ? 31.136 6.086   -4.907  1.00 14.87 ?  42  TYR   A HB2  1 
ATOM   1023 H HB3  . TYR   A 1 42  ? 32.642 6.589   -4.827  1.00 14.87 ?  42  TYR   A HB3  1 
ATOM   1024 H HD1  . TYR   A 1 42  ? 34.255 5.398   -6.497  1.00 16.70 ?  42  TYR   A HD1  1 
ATOM   1025 H HD2  . TYR   A 1 42  ? 30.301 5.538   -7.022  1.00 17.47 ?  42  TYR   A HD2  1 
ATOM   1026 H HE1  . TYR   A 1 42  ? 34.536 4.897   -8.733  1.00 17.68 ?  42  TYR   A HE1  1 
ATOM   1027 H HE2  . TYR   A 1 42  ? 30.577 5.036   -9.260  1.00 18.67 ?  42  TYR   A HE2  1 
ATOM   1028 H HH   . TYR   A 1 42  ? 33.567 4.519   -10.720 1.00 20.78 ?  42  TYR   A HH   1 
ATOM   1029 N N    . LEU   A 1 43  ? 31.297 4.263   -2.005  1.00 10.91 ?  43  LEU   A N    1 
ATOM   1030 C CA   . LEU   A 1 43  ? 30.839 4.599   -0.661  1.00 10.62 ?  43  LEU   A CA   1 
ATOM   1031 C C    . LEU   A 1 43  ? 30.355 6.046   -0.573  1.00 10.85 ?  43  LEU   A C    1 
ATOM   1032 O O    . LEU   A 1 43  ? 30.620 6.753   0.402   1.00 11.82 ?  43  LEU   A O    1 
ATOM   1033 C CB   . LEU   A 1 43  ? 31.887 4.297   0.409   1.00 11.19 ?  43  LEU   A CB   1 
ATOM   1034 C CG   . LEU   A 1 43  ? 32.377 2.845   0.505   1.00 11.66 ?  43  LEU   A CG   1 
ATOM   1035 C CD1  . LEU   A 1 43  ? 33.411 2.731   1.609   1.00 12.46 ?  43  LEU   A CD1  1 
ATOM   1036 C CD2  . LEU   A 1 43  ? 31.242 1.867   0.739   1.00 12.02 ?  43  LEU   A CD2  1 
ATOM   1037 H H    . LEU   A 1 43  ? 30.958 3.524   -2.305  1.00 13.06 ?  43  LEU   A H    1 
ATOM   1038 H HA   . LEU   A 1 43  ? 30.074 4.035   -0.460  1.00 12.72 ?  43  LEU   A HA   1 
ATOM   1039 H HB2  . LEU   A 1 43  ? 32.663 4.855   0.243   1.00 13.41 ?  43  LEU   A HB2  1 
ATOM   1040 H HB3  . LEU   A 1 43  ? 31.508 4.526   1.275   1.00 13.41 ?  43  LEU   A HB3  1 
ATOM   1041 H HG   . LEU   A 1 43  ? 32.813 2.606   -0.328  1.00 13.96 ?  43  LEU   A HG   1 
ATOM   1042 H HD11 . LEU   A 1 43  ? 33.720 1.810   1.662   1.00 14.93 ?  43  LEU   A HD11 1 
ATOM   1043 H HD12 . LEU   A 1 43  ? 34.158 3.317   1.411   1.00 14.93 ?  43  LEU   A HD12 1 
ATOM   1044 H HD13 . LEU   A 1 43  ? 33.005 2.988   2.453   1.00 14.93 ?  43  LEU   A HD13 1 
ATOM   1045 H HD21 . LEU   A 1 43  ? 31.617 0.984   0.894   1.00 14.39 ?  43  LEU   A HD21 1 
ATOM   1046 H HD22 . LEU   A 1 43  ? 30.738 2.152   1.516   1.00 14.39 ?  43  LEU   A HD22 1 
ATOM   1047 H HD23 . LEU   A 1 43  ? 30.674 1.854   -0.043  1.00 14.39 ?  43  LEU   A HD23 1 
ATOM   1048 N N    A LYS   A 1 44  ? 29.636 6.489   -1.606  0.66 10.73 ?  44  LYS   A N    1 
ATOM   1049 N N    B LYS   A 1 44  ? 29.638 6.486   -1.610  0.34 11.35 ?  44  LYS   A N    1 
ATOM   1050 C CA   A LYS   A 1 44  ? 29.001 7.805   -1.605  0.66 11.24 ?  44  LYS   A CA   1 
ATOM   1051 C CA   B LYS   A 1 44  ? 28.993 7.798   -1.625  0.34 12.39 ?  44  LYS   A CA   1 
ATOM   1052 C C    A LYS   A 1 44  ? 27.573 7.622   -1.114  0.66 10.59 ?  44  LYS   A C    1 
ATOM   1053 C C    B LYS   A 1 44  ? 27.573 7.601   -1.109  0.34 11.43 ?  44  LYS   A C    1 
ATOM   1054 O O    A LYS   A 1 44  ? 26.706 7.127   -1.840  0.66 11.65 ?  44  LYS   A O    1 
ATOM   1055 O O    B LYS   A 1 44  ? 26.707 7.080   -1.816  0.34 11.76 ?  44  LYS   A O    1 
ATOM   1056 C CB   A LYS   A 1 44  ? 29.053 8.436   -2.989  0.66 12.86 ?  44  LYS   A CB   1 
ATOM   1057 C CB   B LYS   A 1 44  ? 28.995 8.377   -3.035  0.34 14.70 ?  44  LYS   A CB   1 
ATOM   1058 C CG   A LYS   A 1 44  ? 30.432 8.916   -3.390  0.66 16.18 ?  44  LYS   A CG   1 
ATOM   1059 C CG   B LYS   A 1 44  ? 30.365 8.771   -3.554  0.34 17.76 ?  44  LYS   A CG   1 
ATOM   1060 C CD   A LYS   A 1 44  ? 31.084 9.789   -2.322  0.66 21.17 ?  44  LYS   A CD   1 
ATOM   1061 C CD   B LYS   A 1 44  ? 31.032 9.809   -2.669  0.34 20.94 ?  44  LYS   A CD   1 
ATOM   1062 C CE   A LYS   A 1 44  ? 32.412 10.337  -2.801  0.66 23.88 ?  44  LYS   A CE   1 
ATOM   1063 C CE   B LYS   A 1 44  ? 32.284 10.353  -3.331  0.34 22.87 ?  44  LYS   A CE   1 
ATOM   1064 N NZ   A LYS   A 1 44  ? 33.229 10.871  -1.680  0.66 24.70 ?  44  LYS   A NZ   1 
ATOM   1065 N NZ   B LYS   A 1 44  ? 33.090 11.192  -2.407  0.34 23.86 ?  44  LYS   A NZ   1 
ATOM   1066 H H    A LYS   A 1 44  ? 29.494 6.034   -2.323  0.66 12.85 ?  44  LYS   A H    1 
ATOM   1067 H H    B LYS   A 1 44  ? 29.504 6.026   -2.327  0.34 13.60 ?  44  LYS   A H    1 
ATOM   1068 H HA   A LYS   A 1 44  ? 29.448 8.375   -0.964  0.66 13.46 ?  44  LYS   A HA   1 
ATOM   1069 H HA   B LYS   A 1 44  ? 29.462 8.403   -1.029  0.34 14.84 ?  44  LYS   A HA   1 
ATOM   1070 H HB2  A LYS   A 1 44  ? 28.766 7.780   -3.642  0.66 15.40 ?  44  LYS   A HB2  1 
ATOM   1071 H HB2  B LYS   A 1 44  ? 28.633 7.715   -3.643  0.34 17.61 ?  44  LYS   A HB2  1 
ATOM   1072 H HB3  A LYS   A 1 44  ? 28.457 9.200   -3.004  0.66 15.40 ?  44  LYS   A HB3  1 
ATOM   1073 H HB3  B LYS   A 1 44  ? 28.440 9.171   -3.046  0.34 17.61 ?  44  LYS   A HB3  1 
ATOM   1074 H HG2  A LYS   A 1 44  ? 31.004 8.147   -3.540  0.66 19.39 ?  44  LYS   A HG2  1 
ATOM   1075 H HG2  B LYS   A 1 44  ? 30.935 7.986   -3.582  0.34 21.29 ?  44  LYS   A HG2  1 
ATOM   1076 H HG3  A LYS   A 1 44  ? 30.359 9.441   -4.202  0.66 19.39 ?  44  LYS   A HG3  1 
ATOM   1077 H HG3  B LYS   A 1 44  ? 30.274 9.148   -4.444  0.34 21.29 ?  44  LYS   A HG3  1 
ATOM   1078 H HD2  A LYS   A 1 44  ? 30.493 10.529  -2.108  0.66 25.38 ?  44  LYS   A HD2  1 
ATOM   1079 H HD2  B LYS   A 1 44  ? 30.418 10.544  -2.514  0.34 25.10 ?  44  LYS   A HD2  1 
ATOM   1080 H HD3  A LYS   A 1 44  ? 31.256 9.255   -1.529  0.66 25.38 ?  44  LYS   A HD3  1 
ATOM   1081 H HD3  B LYS   A 1 44  ? 31.286 9.398   -1.826  0.34 25.10 ?  44  LYS   A HD3  1 
ATOM   1082 H HE2  A LYS   A 1 44  ? 32.914 9.624   -3.228  0.66 28.63 ?  44  LYS   A HE2  1 
ATOM   1083 H HE2  B LYS   A 1 44  ? 32.835 9.609   -3.624  0.34 27.42 ?  44  LYS   A HE2  1 
ATOM   1084 H HE3  A LYS   A 1 44  ? 32.250 11.055  -3.431  0.66 28.63 ?  44  LYS   A HE3  1 
ATOM   1085 H HE3  B LYS   A 1 44  ? 32.028 10.898  -4.091  0.34 27.42 ?  44  LYS   A HE3  1 
ATOM   1086 H HZ1  A LYS   A 1 44  ? 34.000 11.188  -1.990  0.66 29.62 ?  44  LYS   A HZ1  1 
ATOM   1087 H HZ1  B LYS   A 1 44  ? 33.816 11.492  -2.825  0.34 28.61 ?  44  LYS   A HZ1  1 
ATOM   1088 H HZ2  A LYS   A 1 44  ? 32.788 11.532  -1.274  0.66 29.62 ?  44  LYS   A HZ2  1 
ATOM   1089 H HZ2  B LYS   A 1 44  ? 32.608 11.885  -2.128  0.34 28.61 ?  44  LYS   A HZ2  1 
ATOM   1090 H HZ3  A LYS   A 1 44  ? 33.393 10.229  -1.089  0.66 29.62 ?  44  LYS   A HZ3  1 
ATOM   1091 H HZ3  B LYS   A 1 44  ? 33.341 10.711  -1.701  0.34 28.61 ?  44  LYS   A HZ3  1 
ATOM   1092 N N    . HIS   A 1 45  ? 27.335 8.002   0.138   1.00 10.66 ?  45  HIS   A N    1 
ATOM   1093 C CA   . HIS   A 1 45  ? 26.089 7.670   0.826   1.00 10.67 ?  45  HIS   A CA   1 
ATOM   1094 C C    . HIS   A 1 45  ? 25.076 8.801   0.650   1.00 11.82 ?  45  HIS   A C    1 
ATOM   1095 O O    . HIS   A 1 45  ? 24.781 9.570   1.565   1.00 13.51 ?  45  HIS   A O    1 
ATOM   1096 C CB   . HIS   A 1 45  ? 26.376 7.410   2.294   1.00 10.39 ?  45  HIS   A CB   1 
ATOM   1097 C CG   . HIS   A 1 45  ? 27.488 6.440   2.528   1.00 10.14 ?  45  HIS   A CG   1 
ATOM   1098 N ND1  . HIS   A 1 45  ? 27.479 5.153   2.027   1.00 10.58 ?  45  HIS   A ND1  1 
ATOM   1099 C CD2  . HIS   A 1 45  ? 28.651 6.584   3.208   1.00 10.84 ?  45  HIS   A CD2  1 
ATOM   1100 C CE1  . HIS   A 1 45  ? 28.594 4.549   2.402   1.00 10.40 ?  45  HIS   A CE1  1 
ATOM   1101 N NE2  . HIS   A 1 45  ? 29.320 5.392   3.120   1.00 10.80 ?  45  HIS   A NE2  1 
ATOM   1102 H H    A HIS   A 1 45  ? 27.884 8.462   0.614   0.66 12.77 ?  45  HIS   A H    1 
ATOM   1103 H H    B HIS   A 1 45  ? 27.886 8.459   0.615   0.34 12.77 ?  45  HIS   A H    1 
ATOM   1104 H HA   . HIS   A 1 45  ? 25.711 6.865   0.441   1.00 12.78 ?  45  HIS   A HA   1 
ATOM   1105 H HB2  . HIS   A 1 45  ? 26.607 8.248   2.722   1.00 12.44 ?  45  HIS   A HB2  1 
ATOM   1106 H HB3  . HIS   A 1 45  ? 25.567 7.050   2.709   1.00 12.44 ?  45  HIS   A HB3  1 
ATOM   1107 H HD2  . HIS   A 1 45  ? 28.934 7.351   3.654   1.00 12.98 ?  45  HIS   A HD2  1 
ATOM   1108 H HE1  . HIS   A 1 45  ? 28.826 3.671   2.205   1.00 12.45 ?  45  HIS   A HE1  1 
ATOM   1109 H HE2  . HIS   A 1 45  ? 30.086 5.224   3.469   1.00 12.93 ?  45  HIS   A HE2  1 
ATOM   1110 N N    A GLY   A 1 46  ? 24.452 8.824   -0.523  0.66 12.31 ?  46  GLY   A N    1 
ATOM   1111 N N    B GLY   A 1 46  ? 24.595 8.941   -0.579  0.34 12.43 ?  46  GLY   A N    1 
ATOM   1112 C CA   A GLY   A 1 46  ? 23.604 9.947   -0.882  0.66 12.87 ?  46  GLY   A CA   1 
ATOM   1113 C CA   B GLY   A 1 46  ? 23.858 10.139  -0.941  0.34 12.96 ?  46  GLY   A CA   1 
ATOM   1114 C C    A GLY   A 1 46  ? 22.128 9.801   -0.580  0.66 12.95 ?  46  GLY   A C    1 
ATOM   1115 C C    B GLY   A 1 46  ? 22.370 10.064  -0.670  0.34 12.43 ?  46  GLY   A C    1 
ATOM   1116 O O    A GLY   A 1 46  ? 21.470 10.780  -0.207  0.66 14.13 ?  46  GLY   A O    1 
ATOM   1117 O O    B GLY   A 1 46  ? 21.723 11.085  -0.416  0.34 12.92 ?  46  GLY   A O    1 
ATOM   1118 H H    A GLY   A 1 46  ? 24.494 8.206   -1.117  0.66 14.74 ?  46  GLY   A H    1 
ATOM   1119 H H    B GLY   A 1 46  ? 24.674 8.364   -1.210  0.34 14.89 ?  46  GLY   A H    1 
ATOM   1120 H HA2  A GLY   A 1 46  ? 23.910 10.736  -0.413  0.66 15.42 ?  46  GLY   A HA2  1 
ATOM   1121 H HA2  B GLY   A 1 46  ? 24.221 10.894  -0.446  0.34 15.52 ?  46  GLY   A HA2  1 
ATOM   1122 H HA3  A GLY   A 1 46  ? 23.690 10.112  -1.832  0.66 15.42 ?  46  GLY   A HA3  1 
ATOM   1123 H HA3  B GLY   A 1 46  ? 23.983 10.314  -1.885  0.34 15.52 ?  46  GLY   A HA3  1 
ATOM   1124 N N    A GLY   A 1 47  ? 21.587 8.599   -0.752  0.66 12.99 ?  47  GLY   A N    1 
ATOM   1125 N N    B GLY   A 1 47  ? 21.814 8.864   -0.739  0.34 11.67 ?  47  GLY   A N    1 
ATOM   1126 C CA   A GLY   A 1 47  ? 20.154 8.403   -0.705  0.66 13.08 ?  47  GLY   A CA   1 
ATOM   1127 C CA   B GLY   A 1 47  ? 20.393 8.675   -0.568  0.34 11.89 ?  47  GLY   A CA   1 
ATOM   1128 C C    A GLY   A 1 47  ? 19.819 6.986   -0.295  0.66 12.23 ?  47  GLY   A C    1 
ATOM   1129 C C    B GLY   A 1 47  ? 20.104 7.227   -0.238  0.34 11.66 ?  47  GLY   A C    1 
ATOM   1130 O O    A GLY   A 1 47  ? 20.702 6.158   -0.057  0.66 11.91 ?  47  GLY   A O    1 
ATOM   1131 O O    B GLY   A 1 47  ? 21.016 6.417   -0.050  0.34 11.93 ?  47  GLY   A O    1 
ATOM   1132 H H    A GLY   A 1 47  ? 22.033 7.872   -0.880  0.66 15.56 ?  47  GLY   A H    1 
ATOM   1133 H H    B GLY   A 1 47  ? 22.248 8.138   -0.882  0.34 13.97 ?  47  GLY   A H    1 
ATOM   1134 H HA2  A GLY   A 1 47  ? 19.751 9.012   -0.067  0.66 15.67 ?  47  GLY   A HA2  1 
ATOM   1135 H HA2  B GLY   A 1 47  ? 20.061 9.242   0.154   0.34 14.24 ?  47  GLY   A HA2  1 
ATOM   1136 H HA3  A GLY   A 1 47  ? 19.767 8.569   -1.581  0.66 15.67 ?  47  GLY   A HA3  1 
ATOM   1137 H HA3  B GLY   A 1 47  ? 19.928 8.923   -1.388  0.34 14.24 ?  47  GLY   A HA3  1 
ATOM   1138 N N    A GLY   A 1 48  ? 18.521 6.703   -0.235  0.66 12.14 ?  48  GLY   A N    1 
ATOM   1139 N N    B GLY   A 1 48  ? 18.819 6.905   -0.171  0.34 11.99 ?  48  GLY   A N    1 
ATOM   1140 C CA   A GLY   A 1 48  ? 18.082 5.400   0.208   0.66 12.11 ?  48  GLY   A CA   1 
ATOM   1141 C CA   B GLY   A 1 48  ? 18.430 5.548   0.154   0.34 12.17 ?  48  GLY   A CA   1 
ATOM   1142 C C    A GLY   A 1 48  ? 18.589 5.097   1.604   0.66 11.25 ?  48  GLY   A C    1 
ATOM   1143 C C    B GLY   A 1 48  ? 18.882 5.154   1.550   0.34 11.91 ?  48  GLY   A C    1 
ATOM   1144 O O    A GLY   A 1 48  ? 18.735 5.987   2.453   0.66 12.01 ?  48  GLY   A O    1 
ATOM   1145 O O    B GLY   A 1 48  ? 19.048 5.994   2.445   0.34 12.72 ?  48  GLY   A O    1 
ATOM   1146 H H    A GLY   A 1 48  ? 17.881 7.245   -0.434  0.66 14.54 ?  48  GLY   A H    1 
ATOM   1147 H H    B GLY   A 1 48  ? 18.169 7.449   -0.304  0.34 14.36 ?  48  GLY   A H    1 
ATOM   1148 H HA2  A GLY   A 1 48  ? 17.112 5.357   0.215   0.66 14.50 ?  48  GLY   A HA2  1 
ATOM   1149 H HA2  B GLY   A 1 48  ? 17.467 5.466   0.090   0.34 14.57 ?  48  GLY   A HA2  1 
ATOM   1150 H HA3  A GLY   A 1 48  ? 18.418 4.716   -0.393  0.66 14.50 ?  48  GLY   A HA3  1 
ATOM   1151 H HA3  B GLY   A 1 48  ? 18.836 4.933   -0.478  0.34 14.57 ?  48  GLY   A HA3  1 
ATOM   1152 N N    A VAL   A 1 49  ? 18.855 3.813   1.850   0.66 10.66 ?  49  VAL   A N    1 
ATOM   1153 N N    B VAL   A 1 49  ? 19.091 3.845   1.735   0.34 11.59 ?  49  VAL   A N    1 
ATOM   1154 C CA   A VAL   A 1 49  ? 19.365 3.392   3.153   0.66 11.47 ?  49  VAL   A CA   1 
ATOM   1155 C CA   B VAL   A 1 49  ? 19.603 3.327   3.006   0.34 11.25 ?  49  VAL   A CA   1 
ATOM   1156 C C    A VAL   A 1 49  ? 20.678 4.098   3.468   0.66 10.12 ?  49  VAL   A C    1 
ATOM   1157 C C    B VAL   A 1 49  ? 20.857 4.084   3.420   0.34 10.10 ?  49  VAL   A C    1 
ATOM   1158 O O    A VAL   A 1 49  ? 20.902 4.541   4.599   0.66 10.83 ?  49  VAL   A O    1 
ATOM   1159 O O    B VAL   A 1 49  ? 21.020 4.468   4.583   0.34 10.23 ?  49  VAL   A O    1 
ATOM   1160 C CB   A VAL   A 1 49  ? 19.518 1.856   3.193   0.66 12.41 ?  49  VAL   A CB   1 
ATOM   1161 C CB   B VAL   A 1 49  ? 19.886 1.815   2.897   0.34 10.92 ?  49  VAL   A CB   1 
ATOM   1162 C CG1  A VAL   A 1 49  ? 20.343 1.413   4.407   0.66 12.55 ?  49  VAL   A CG1  1 
ATOM   1163 C CG1  B VAL   A 1 49  ? 20.740 1.346   4.073   0.34 10.95 ?  49  VAL   A CG1  1 
ATOM   1164 C CG2  A VAL   A 1 49  ? 18.148 1.174   3.185   0.66 14.48 ?  49  VAL   A CG2  1 
ATOM   1165 C CG2  B VAL   A 1 49  ? 18.596 1.022   2.836   0.34 11.15 ?  49  VAL   A CG2  1 
ATOM   1166 H H    A VAL   A 1 49  ? 18.755 3.168   1.286   0.66 12.76 ?  49  VAL   A H    1 
ATOM   1167 H H    B VAL   A 1 49  ? 18.954 3.242   1.141   0.34 13.88 ?  49  VAL   A H    1 
ATOM   1168 H HA   A VAL   A 1 49  ? 18.726 3.638   3.835   0.66 13.74 ?  49  VAL   A HA   1 
ATOM   1169 H HA   B VAL   A 1 49  ? 18.933 3.453   3.698   0.34 13.47 ?  49  VAL   A HA   1 
ATOM   1170 H HB   A VAL   A 1 49  ? 19.995 1.569   2.400   0.66 14.87 ?  49  VAL   A HB   1 
ATOM   1171 H HB   B VAL   A 1 49  ? 20.379 1.643   2.079   0.34 13.07 ?  49  VAL   A HB   1 
ATOM   1172 H HG11 A VAL   A 1 49  ? 20.196 0.468   4.558   0.66 15.04 ?  49  VAL   A HG11 1 
ATOM   1173 H HG11 B VAL   A 1 49  ? 20.658 0.384   4.158   0.34 13.12 ?  49  VAL   A HG11 1 
ATOM   1174 H HG12 A VAL   A 1 49  ? 21.282 1.579   4.231   0.66 15.04 ?  49  VAL   A HG12 1 
ATOM   1175 H HG12 B VAL   A 1 49  ? 21.666 1.580   3.907   0.34 13.12 ?  49  VAL   A HG12 1 
ATOM   1176 H HG13 A VAL   A 1 49  ? 20.055 1.920   5.184   0.66 15.04 ?  49  VAL   A HG13 1 
ATOM   1177 H HG13 B VAL   A 1 49  ? 20.425 1.775   4.882   0.34 13.12 ?  49  VAL   A HG13 1 
ATOM   1178 H HG21 A VAL   A 1 49  ? 18.275 0.215   3.208   0.66 17.34 ?  49  VAL   A HG21 1 
ATOM   1179 H HG21 B VAL   A 1 49  ? 18.810 0.081   2.716   0.34 13.35 ?  49  VAL   A HG21 1 
ATOM   1180 H HG22 A VAL   A 1 49  ? 17.650 1.465   3.964   0.66 17.34 ?  49  VAL   A HG22 1 
ATOM   1181 H HG22 B VAL   A 1 49  ? 18.112 1.144   3.667   0.34 13.35 ?  49  VAL   A HG22 1 
ATOM   1182 H HG23 A VAL   A 1 49  ? 17.680 1.431   2.376   0.66 17.34 ?  49  VAL   A HG23 1 
ATOM   1183 H HG23 B VAL   A 1 49  ? 18.065 1.340   2.091   0.34 13.35 ?  49  VAL   A HG23 1 
ATOM   1184 N N    A ALA   A 1 50  ? 21.582 4.167   2.489   0.66 9.60  ?  50  ALA   A N    1 
ATOM   1185 N N    B ALA   A 1 50  ? 21.782 4.268   2.478   0.34 9.87  ?  50  ALA   A N    1 
ATOM   1186 C CA   A ALA   A 1 50  ? 22.907 4.726   2.739   0.66 9.71  ?  50  ALA   A CA   1 
ATOM   1187 C CA   B ALA   A 1 50  ? 23.088 4.820   2.823   0.34 9.85  ?  50  ALA   A CA   1 
ATOM   1188 C C    A ALA   A 1 50  ? 22.814 6.182   3.167   0.66 9.62  ?  50  ALA   A C    1 
ATOM   1189 C C    B ALA   A 1 50  ? 22.977 6.281   3.232   0.34 9.56  ?  50  ALA   A C    1 
ATOM   1190 O O    A ALA   A 1 50  ? 23.455 6.595   4.139   0.66 10.26 ?  50  ALA   A O    1 
ATOM   1191 O O    B ALA   A 1 50  ? 23.571 6.703   4.231   0.34 10.00 ?  50  ALA   A O    1 
ATOM   1192 C CB   A ALA   A 1 50  ? 23.772 4.596   1.487   0.66 9.42  ?  50  ALA   A CB   1 
ATOM   1193 C CB   B ALA   A 1 50  ? 24.050 4.662   1.646   0.34 10.09 ?  50  ALA   A CB   1 
ATOM   1194 H H    A ALA   A 1 50  ? 21.457 3.898   1.684   0.66 11.50 ?  50  ALA   A H    1 
ATOM   1195 H H    B ALA   A 1 50  ? 21.676 4.082   1.646   0.34 11.81 ?  50  ALA   A H    1 
ATOM   1196 H HA   A ALA   A 1 50  ? 23.335 4.234   3.459   0.66 11.63 ?  50  ALA   A HA   1 
ATOM   1197 H HA   B ALA   A 1 50  ? 23.447 4.328   3.576   0.34 11.79 ?  50  ALA   A HA   1 
ATOM   1198 H HB1  A ALA   A 1 50  ? 24.648 4.974   1.672   0.66 11.28 ?  50  ALA   A HB1  1 
ATOM   1199 H HB1  B ALA   A 1 50  ? 24.911 5.028   1.896   0.34 12.08 ?  50  ALA   A HB1  1 
ATOM   1200 H HB2  A ALA   A 1 50  ? 23.857 3.658   1.261   0.66 11.28 ?  50  ALA   A HB2  1 
ATOM   1201 H HB2  B ALA   A 1 50  ? 24.137 3.720   1.436   0.34 12.08 ?  50  ALA   A HB2  1 
ATOM   1202 H HB3  A ALA   A 1 50  ? 23.349 5.079   0.764   0.66 11.28 ?  50  ALA   A HB3  1 
ATOM   1203 H HB3  B ALA   A 1 50  ? 23.694 5.142   0.882   0.34 12.08 ?  50  ALA   A HB3  1 
ATOM   1204 N N    A GLY   A 1 51  ? 22.019 6.977   2.451   0.66 10.06 ?  51  GLY   A N    1 
ATOM   1205 N N    B GLY   A 1 51  ? 22.223 7.071   2.468   0.34 9.70  ?  51  GLY   A N    1 
ATOM   1206 C CA   A GLY   A 1 51  ? 21.834 8.360   2.854   0.66 10.72 ?  51  GLY   A CA   1 
ATOM   1207 C CA   B GLY   A 1 51  ? 22.072 8.473   2.810   0.34 9.32  ?  51  GLY   A CA   1 
ATOM   1208 C C    A GLY   A 1 51  ? 21.257 8.471   4.252   0.66 10.90 ?  51  GLY   A C    1 
ATOM   1209 C C    B GLY   A 1 51  ? 21.380 8.670   4.142   0.34 9.21  ?  51  GLY   A C    1 
ATOM   1210 O O    A GLY   A 1 51  ? 21.659 9.335   5.035   0.66 11.61 ?  51  GLY   A O    1 
ATOM   1211 O O    B GLY   A 1 51  ? 21.733 9.570   4.908   0.34 9.54  ?  51  GLY   A O    1 
ATOM   1212 H H    A GLY   A 1 51  ? 21.593 6.742   1.738   0.66 12.04 ?  51  GLY   A H    1 
ATOM   1213 H H    B GLY   A 1 51  ? 21.803 6.821   1.761   0.34 11.62 ?  51  GLY   A H    1 
ATOM   1214 H HA2  A GLY   A 1 51  ? 22.689 8.822   2.829   0.66 12.84 ?  51  GLY   A HA2  1 
ATOM   1215 H HA2  B GLY   A 1 51  ? 22.947 8.889   2.857   0.34 11.15 ?  51  GLY   A HA2  1 
ATOM   1216 H HA3  A GLY   A 1 51  ? 21.233 8.801   2.228   0.66 12.84 ?  51  GLY   A HA3  1 
ATOM   1217 H HA3  B GLY   A 1 51  ? 21.555 8.920   2.122   0.34 11.15 ?  51  GLY   A HA3  1 
ATOM   1218 N N    A ALA   A 1 52  ? 20.314 7.586   4.586   0.66 10.70 ?  52  ALA   A N    1 
ATOM   1219 N N    B ALA   A 1 52  ? 20.378 7.836   4.435   0.34 9.25  ?  52  ALA   A N    1 
ATOM   1220 C CA   A ALA   A 1 52  ? 19.678 7.621   5.899   0.66 10.85 ?  52  ALA   A CA   1 
ATOM   1221 C CA   B ALA   A 1 52  ? 19.677 7.948   5.710   0.34 9.59  ?  52  ALA   A CA   1 
ATOM   1222 C C    A ALA   A 1 52  ? 20.651 7.221   7.007   0.66 10.40 ?  52  ALA   A C    1 
ATOM   1223 C C    B ALA   A 1 52  ? 20.556 7.499   6.873   0.34 9.78  ?  52  ALA   A C    1 
ATOM   1224 O O    A ALA   A 1 52  ? 20.725 7.880   8.051   0.66 11.13 ?  52  ALA   A O    1 
ATOM   1225 O O    B ALA   A 1 52  ? 20.599 8.162   7.915   0.34 11.03 ?  52  ALA   A O    1 
ATOM   1226 C CB   A ALA   A 1 52  ? 18.453 6.707   5.892   0.66 12.09 ?  52  ALA   A CB   1 
ATOM   1227 C CB   B ALA   A 1 52  ? 18.370 7.155   5.667   0.34 9.89  ?  52  ALA   A CB   1 
ATOM   1228 H H    A ALA   A 1 52  ? 20.036 6.956   4.067   0.66 12.81 ?  52  ALA   A H    1 
ATOM   1229 H H    B ALA   A 1 52  ? 20.093 7.210   3.919   0.34 11.07 ?  52  ALA   A H    1 
ATOM   1230 H HA   A ALA   A 1 52  ? 19.379 8.523   6.074   0.66 12.99 ?  52  ALA   A HA   1 
ATOM   1231 H HA   B ALA   A 1 52  ? 19.449 8.877   5.856   0.34 11.48 ?  52  ALA   A HA   1 
ATOM   1232 H HB1  A ALA   A 1 52  ? 18.032 6.740   6.764   0.66 14.48 ?  52  ALA   A HB1  1 
ATOM   1233 H HB1  B ALA   A 1 52  ? 17.918 7.242   6.523   0.34 11.84 ?  52  ALA   A HB1  1 
ATOM   1234 H HB2  A ALA   A 1 52  ? 17.831 7.020   5.213   0.66 14.48 ?  52  ALA   A HB2  1 
ATOM   1235 H HB2  B ALA   A 1 52  ? 17.806 7.512   4.961   0.34 11.84 ?  52  ALA   A HB2  1 
ATOM   1236 H HB3  A ALA   A 1 52  ? 18.732 5.801   5.689   0.66 14.48 ?  52  ALA   A HB3  1 
ATOM   1237 H HB3  B ALA   A 1 52  ? 18.568 6.222   5.491   0.34 11.84 ?  52  ALA   A HB3  1 
ATOM   1238 N N    A LEU   A 1 53  ? 21.390 6.126   6.818   0.66 10.25 ?  53  LEU   A N    1 
ATOM   1239 N N    B LEU   A 1 53  ? 21.264 6.376   6.721   0.34 9.62  ?  53  LEU   A N    1 
ATOM   1240 C CA   A LEU   A 1 53  ? 22.369 5.732   7.829   0.66 10.42 ?  53  LEU   A CA   1 
ATOM   1241 C CA   B LEU   A 1 53  ? 22.180 5.938   7.771   0.34 10.47 ?  53  LEU   A CA   1 
ATOM   1242 C C    A LEU   A 1 53  ? 23.405 6.827   8.023   0.66 10.37 ?  53  LEU   A C    1 
ATOM   1243 C C    B LEU   A 1 53  ? 23.266 6.978   8.005   0.34 10.39 ?  53  LEU   A C    1 
ATOM   1244 O O    A LEU   A 1 53  ? 23.759 7.169   9.157   0.66 11.17 ?  53  LEU   A O    1 
ATOM   1245 O O    B LEU   A 1 53  ? 23.531 7.376   9.146   0.34 10.51 ?  53  LEU   A O    1 
ATOM   1246 C CB   A LEU   A 1 53  ? 23.060 4.425   7.434   0.66 10.76 ?  53  LEU   A CB   1 
ATOM   1247 C CB   B LEU   A 1 53  ? 22.805 4.588   7.405   0.34 11.02 ?  53  LEU   A CB   1 
ATOM   1248 C CG   A LEU   A 1 53  ? 22.239 3.133   7.496   0.66 11.31 ?  53  LEU   A CG   1 
ATOM   1249 C CG   B LEU   A 1 53  ? 21.944 3.325   7.514   0.34 10.99 ?  53  LEU   A CG   1 
ATOM   1250 C CD1  A LEU   A 1 53  ? 23.033 1.992   6.880   0.66 12.51 ?  53  LEU   A CD1  1 
ATOM   1251 C CD1  B LEU   A 1 53  ? 22.711 2.142   6.961   0.34 10.88 ?  53  LEU   A CD1  1 
ATOM   1252 C CD2  A LEU   A 1 53  ? 21.850 2.786   8.924   0.66 12.10 ?  53  LEU   A CD2  1 
ATOM   1253 C CD2  B LEU   A 1 53  ? 21.529 3.048   8.951   0.34 12.05 ?  53  LEU   A CD2  1 
ATOM   1254 H H    A LEU   A 1 53  ? 21.349 5.606   6.131   0.66 12.27 ?  53  LEU   A H    1 
ATOM   1255 H H    B LEU   A 1 53  ? 21.233 5.861   6.034   0.34 11.52 ?  53  LEU   A H    1 
ATOM   1256 H HA   A LEU   A 1 53  ? 21.914 5.588   8.675   0.66 12.47 ?  53  LEU   A HA   1 
ATOM   1257 H HA   B LEU   A 1 53  ? 21.688 5.833   8.597   0.34 12.54 ?  53  LEU   A HA   1 
ATOM   1258 H HB2  A LEU   A 1 53  ? 23.375 4.516   6.523   0.66 12.89 ?  53  LEU   A HB2  1 
ATOM   1259 H HB2  B LEU   A 1 53  ? 23.106 4.640   6.484   0.34 13.20 ?  53  LEU   A HB2  1 
ATOM   1260 H HB3  A LEU   A 1 53  ? 23.824 4.301   8.022   0.66 12.89 ?  53  LEU   A HB3  1 
ATOM   1261 H HB3  B LEU   A 1 53  ? 23.573 4.448   7.979   0.34 13.20 ?  53  LEU   A HB3  1 
ATOM   1262 H HG   A LEU   A 1 53  ? 21.429 3.245   6.979   0.66 13.55 ?  53  LEU   A HG   1 
ATOM   1263 H HG   B LEU   A 1 53  ? 21.140 3.435   6.980   0.34 13.16 ?  53  LEU   A HG   1 
ATOM   1264 H HD11 A LEU   A 1 53  ? 22.507 1.180   6.927   0.66 14.99 ?  53  LEU   A HD11 1 
ATOM   1265 H HD11 B LEU   A 1 53  ? 22.167 1.345   7.039   0.34 13.03 ?  53  LEU   A HD11 1 
ATOM   1266 H HD12 A LEU   A 1 53  ? 23.228 2.209   5.954   0.66 14.99 ?  53  LEU   A HD12 1 
ATOM   1267 H HD12 B LEU   A 1 53  ? 22.924 2.309   6.029   0.34 13.03 ?  53  LEU   A HD12 1 
ATOM   1268 H HD13 A LEU   A 1 53  ? 23.861 1.881   7.374   0.66 14.99 ?  53  LEU   A HD13 1 
ATOM   1269 H HD13 B LEU   A 1 53  ? 23.532 2.034   7.471   0.34 13.03 ?  53  LEU   A HD13 1 
ATOM   1270 H HD21 A LEU   A 1 53  ? 21.379 1.937   8.928   0.66 14.49 ?  53  LEU   A HD21 1 
ATOM   1271 H HD21 B LEU   A 1 53  ? 20.730 2.501   8.947   0.34 14.43 ?  53  LEU   A HD21 1 
ATOM   1272 H HD22 A LEU   A 1 53  ? 22.651 2.722   9.467   0.66 14.49 ?  53  LEU   A HD22 1 
ATOM   1273 H HD22 B LEU   A 1 53  ? 22.250 2.576   9.398   0.34 14.43 ?  53  LEU   A HD22 1 
ATOM   1274 H HD23 A LEU   A 1 53  ? 21.270 3.484   9.272   0.66 14.49 ?  53  LEU   A HD23 1 
ATOM   1275 H HD23 B LEU   A 1 53  ? 21.355 3.885   9.404   0.34 14.43 ?  53  LEU   A HD23 1 
ATOM   1276 N N    A ASN   A 1 54  ? 23.901 7.396   6.927   0.66 9.93  ?  54  ASN   A N    1 
ATOM   1277 N N    B ASN   A 1 54  ? 23.903 7.438   6.929   0.34 10.34 ?  54  ASN   A N    1 
ATOM   1278 C CA   A ASN   A 1 54  ? 24.948 8.400   7.058   0.66 10.40 ?  54  ASN   A CA   1 
ATOM   1279 C CA   B ASN   A 1 54  ? 24.970 8.419   7.074   0.34 10.65 ?  54  ASN   A CA   1 
ATOM   1280 C C    A ASN   A 1 54  ? 24.435 9.636   7.792   0.66 10.54 ?  54  ASN   A C    1 
ATOM   1281 C C    B ASN   A 1 54  ? 24.465 9.689   7.751   0.34 10.94 ?  54  ASN   A C    1 
ATOM   1282 O O    A ASN   A 1 54  ? 25.107 10.160  8.688   0.66 10.54 ?  54  ASN   A O    1 
ATOM   1283 O O    B ASN   A 1 54  ? 25.179 10.300  8.554   0.34 11.20 ?  54  ASN   A O    1 
ATOM   1284 C CB   A ASN   A 1 54  ? 25.502 8.781   5.693   0.66 10.43 ?  54  ASN   A CB   1 
ATOM   1285 C CB   B ASN   A 1 54  ? 25.564 8.749   5.712   0.34 10.62 ?  54  ASN   A CB   1 
ATOM   1286 C CG   A ASN   A 1 54  ? 26.529 9.878   5.801   0.66 10.62 ?  54  ASN   A CG   1 
ATOM   1287 C CG   B ASN   A 1 54  ? 26.608 9.830   5.798   0.34 10.51 ?  54  ASN   A CG   1 
ATOM   1288 O OD1  A ASN   A 1 54  ? 27.584 9.676   6.409   0.66 10.95 ?  54  ASN   A OD1  1 
ATOM   1289 O OD1  B ASN   A 1 54  ? 27.496 9.781   6.655   0.34 9.39  ?  54  ASN   A OD1  1 
ATOM   1290 N ND2  A ASN   A 1 54  ? 26.227 11.049  5.246   0.66 10.16 ?  54  ASN   A ND2  1 
ATOM   1291 N ND2  B ASN   A 1 54  ? 26.500 10.828  4.931   0.34 11.33 ?  54  ASN   A ND2  1 
ATOM   1292 H H    A ASN   A 1 54  ? 23.651 7.219   6.123   0.66 11.89 ?  54  ASN   A H    1 
ATOM   1293 H H    B ASN   A 1 54  ? 23.740 7.197   6.120   0.34 12.38 ?  54  ASN   A H    1 
ATOM   1294 H HA   A ASN   A 1 54  ? 25.669 8.023   7.583   0.66 12.45 ?  54  ASN   A HA   1 
ATOM   1295 H HA   B ASN   A 1 54  ? 25.672 8.045   7.628   0.34 12.75 ?  54  ASN   A HA   1 
ATOM   1296 H HB2  A ASN   A 1 54  ? 25.929 8.001   5.299   0.66 12.48 ?  54  ASN   A HB2  1 
ATOM   1297 H HB2  B ASN   A 1 54  ? 25.981 7.950   5.349   0.34 12.72 ?  54  ASN   A HB2  1 
ATOM   1298 H HB3  A ASN   A 1 54  ? 24.780 9.089   5.131   0.66 12.48 ?  54  ASN   A HB3  1 
ATOM   1299 H HB3  B ASN   A 1 54  ? 24.857 9.052   5.122   0.34 12.72 ?  54  ASN   A HB3  1 
ATOM   1300 H HD21 A ASN   A 1 54  ? 26.783 11.703  5.290   0.66 12.16 ?  54  ASN   A HD21 1 
ATOM   1301 H HD21 B ASN   A 1 54  ? 27.069 11.469  4.943   0.34 13.56 ?  54  ASN   A HD21 1 
ATOM   1302 H HD22 A ASN   A 1 54  ? 25.480 11.146  4.831   0.66 12.16 ?  54  ASN   A HD22 1 
ATOM   1303 H HD22 B ASN   A 1 54  ? 25.860 10.827  4.354   0.34 13.56 ?  54  ASN   A HD22 1 
ATOM   1304 N N    . LYS   A 1 55  ? 23.239 10.111  7.428   1.00 10.97 ?  55  LYS   A N    1 
ATOM   1305 C CA   . LYS   A 1 55  ? 22.655 11.264  8.099   1.00 11.78 ?  55  LYS   A CA   1 
ATOM   1306 C C    . LYS   A 1 55  ? 22.557 11.027  9.601   1.00 12.04 ?  55  LYS   A C    1 
ATOM   1307 O O    . LYS   A 1 55  ? 22.831 11.931  10.400  1.00 12.54 ?  55  LYS   A O    1 
ATOM   1308 C CB   . LYS   A 1 55  ? 21.283 11.560  7.483   1.00 12.89 ?  55  LYS   A CB   1 
ATOM   1309 C CG   . LYS   A 1 55  ? 20.538 12.742  8.087   1.00 14.84 ?  55  LYS   A CG   1 
ATOM   1310 C CD   . LYS   A 1 55  ? 19.207 12.959  7.358   1.00 16.30 ?  55  LYS   A CD   1 
ATOM   1311 C CE   . LYS   A 1 55  ? 18.343 14.024  8.020   1.00 18.41 ?  55  LYS   A CE   1 
ATOM   1312 N NZ   . LYS   A 1 55  ? 17.003 14.150  7.363   1.00 18.82 ?  55  LYS   A NZ   1 
ATOM   1313 H H    A LYS   A 1 55  ? 22.746 9.776   6.803   0.66 13.13 ?  55  LYS   A H    1 
ATOM   1314 H H    B LYS   A 1 55  ? 22.732 9.745   6.832   0.34 13.13 ?  55  LYS   A H    1 
ATOM   1315 H HA   . LYS   A 1 55  ? 23.219 12.032  7.955   1.00 14.11 ?  55  LYS   A HA   1 
ATOM   1316 H HB2  . LYS   A 1 55  ? 21.401 11.746  6.539   1.00 15.45 ?  55  LYS   A HB2  1 
ATOM   1317 H HB3  . LYS   A 1 55  ? 20.716 10.777  7.589   1.00 15.45 ?  55  LYS   A HB3  1 
ATOM   1318 H HG2  . LYS   A 1 55  ? 20.347 12.561  9.022   1.00 17.79 ?  55  LYS   A HG2  1 
ATOM   1319 H HG3  . LYS   A 1 55  ? 21.075 13.542  7.998   1.00 17.79 ?  55  LYS   A HG3  1 
ATOM   1320 H HD2  . LYS   A 1 55  ? 19.391 13.244  6.448   1.00 19.54 ?  55  LYS   A HD2  1 
ATOM   1321 H HD3  . LYS   A 1 55  ? 18.710 12.127  7.351   1.00 19.54 ?  55  LYS   A HD3  1 
ATOM   1322 H HE2  . LYS   A 1 55  ? 18.204 13.786  8.951   1.00 22.06 ?  55  LYS   A HE2  1 
ATOM   1323 H HE3  . LYS   A 1 55  ? 18.794 14.882  7.960   1.00 22.06 ?  55  LYS   A HE3  1 
ATOM   1324 H HZ1  . LYS   A 1 55  ? 16.451 14.613  7.885   1.00 22.55 ?  55  LYS   A HZ1  1 
ATOM   1325 H HZ2  . LYS   A 1 55  ? 17.084 14.573  6.584   1.00 22.55 ?  55  LYS   A HZ2  1 
ATOM   1326 H HZ3  . LYS   A 1 55  ? 16.656 13.343  7.220   1.00 22.55 ?  55  LYS   A HZ3  1 
ATOM   1327 N N    . ALA   A 1 56  ? 22.168 9.814   10.004  1.00 12.21 ?  56  ALA   A N    1 
ATOM   1328 C CA   . ALA   A 1 56  ? 22.039 9.487   11.419  1.00 12.77 ?  56  ALA   A CA   1 
ATOM   1329 C C    . ALA   A 1 56  ? 23.376 9.511   12.149  1.00 12.65 ?  56  ALA   A C    1 
ATOM   1330 O O    . ALA   A 1 56  ? 23.393 9.696   13.368  1.00 13.82 ?  56  ALA   A O    1 
ATOM   1331 C CB   . ALA   A 1 56  ? 21.350 8.131   11.587  1.00 13.40 ?  56  ALA   A CB   1 
ATOM   1332 H H    . ALA   A 1 56  ? 21.968 9.164   9.473   1.00 14.63 ?  56  ALA   A H    1 
ATOM   1333 H HA   . ALA   A 1 56  ? 21.480 10.146  11.840  1.00 15.29 ?  56  ALA   A HA   1 
ATOM   1334 H HB1  . ALA   A 1 56  ? 21.276 7.924   12.535  1.00 16.05 ?  56  ALA   A HB1  1 
ATOM   1335 H HB2  . ALA   A 1 56  ? 20.464 8.176   11.193  1.00 16.05 ?  56  ALA   A HB2  1 
ATOM   1336 H HB3  . ALA   A 1 56  ? 21.873 7.443   11.143  1.00 16.05 ?  56  ALA   A HB3  1 
ATOM   1337 N N    . THR   A 1 57  ? 24.490 9.316   11.439  1.00 11.72 ?  57  THR   A N    1 
ATOM   1338 C CA   . THR   A 1 57  ? 25.832 9.442   12.015  1.00 11.75 ?  57  THR   A CA   1 
ATOM   1339 C C    . THR   A 1 57  ? 26.386 10.859  11.940  1.00 12.16 ?  57  THR   A C    1 
ATOM   1340 O O    . THR   A 1 57  ? 27.572 11.069  12.227  1.00 12.82 ?  57  THR   A O    1 
ATOM   1341 C CB   . THR   A 1 57  ? 26.843 8.497   11.333  1.00 11.91 ?  57  THR   A CB   1 
ATOM   1342 O OG1  . THR   A 1 57  ? 27.224 9.007   10.044  1.00 11.51 ?  57  THR   A OG1  1 
ATOM   1343 C CG2  . THR   A 1 57  ? 26.304 7.078   11.216  1.00 11.84 ?  57  THR   A CG2  1 
ATOM   1344 H H    . THR   A 1 57  ? 24.496 9.082   10.611  1.00 14.03 ?  57  THR   A H    1 
ATOM   1345 H HA   . THR   A 1 57  ? 25.787 9.182   12.955  1.00 14.07 ?  57  THR   A HA   1 
ATOM   1346 H HB   . THR   A 1 57  ? 27.636 8.446   11.890  1.00 14.26 ?  57  THR   A HB   1 
ATOM   1347 H HG1  . THR   A 1 57  ? 26.545 9.079   9.556   1.00 13.78 ?  57  THR   A HG1  1 
ATOM   1348 H HG21 . THR   A 1 57  ? 26.973 6.494   10.822  1.00 14.18 ?  57  THR   A HG21 1 
ATOM   1349 H HG22 . THR   A 1 57  ? 26.067 6.733   12.093  1.00 14.18 ?  57  THR   A HG22 1 
ATOM   1350 H HG23 . THR   A 1 57  ? 25.513 7.064   10.655  1.00 14.18 ?  57  THR   A HG23 1 
ATOM   1351 N N    . ASN   A 1 58  ? 25.573 11.833  11.536  1.00 12.53 ?  58  ASN   A N    1 
ATOM   1352 C CA   . ASN   A 1 58  ? 26.039 13.215  11.433  1.00 13.63 ?  58  ASN   A CA   1 
ATOM   1353 C C    . ASN   A 1 58  ? 27.197 13.342  10.436  1.00 12.71 ?  58  ASN   A C    1 
ATOM   1354 O O    . ASN   A 1 58  ? 28.098 14.174  10.605  1.00 13.25 ?  58  ASN   A O    1 
ATOM   1355 C CB   . ASN   A 1 58  ? 26.400 13.753  12.828  1.00 16.39 ?  58  ASN   A CB   1 
ATOM   1356 C CG   . ASN   A 1 58  ? 26.775 15.217  12.829  1.00 20.82 ?  58  ASN   A CG   1 
ATOM   1357 O OD1  . ASN   A 1 58  ? 26.152 16.028  12.152  1.00 22.49 ?  58  ASN   A OD1  1 
ATOM   1358 N ND2  . ASN   A 1 58  ? 27.799 15.566  13.606  1.00 23.12 ?  58  ASN   A ND2  1 
ATOM   1359 H H    . ASN   A 1 58  ? 24.746 11.708  11.306  1.00 15.00 ?  58  ASN   A H    1 
ATOM   1360 H HA   . ASN   A 1 58  ? 25.302 13.744  11.098  1.00 16.33 ?  58  ASN   A HA   1 
ATOM   1361 H HB2  . ASN   A 1 58  ? 25.631 13.637  13.419  1.00 19.64 ?  58  ASN   A HB2  1 
ATOM   1362 H HB3  . ASN   A 1 58  ? 27.153 13.257  13.177  1.00 19.64 ?  58  ASN   A HB3  1 
ATOM   1363 H HD21 . ASN   A 1 58  ? 28.043 16.390  13.645  1.00 27.72 ?  58  ASN   A HD21 1 
ATOM   1364 H HD22 . ASN   A 1 58  ? 28.203 14.971  14.069  1.00 27.72 ?  58  ASN   A HD22 1 
ATOM   1365 N N    . ASN   A 1 59  ? 27.177 12.518  9.383   1.00 11.68 ?  59  ASN   A N    1 
ATOM   1366 C CA   . ASN   A 1 59  ? 28.158 12.493  8.292   1.00 11.35 ?  59  ASN   A CA   1 
ATOM   1367 C C    . ASN   A 1 59  ? 29.469 11.812  8.689   1.00 10.91 ?  59  ASN   A C    1 
ATOM   1368 O O    . ASN   A 1 59  ? 30.390 11.771  7.869   1.00 11.23 ?  59  ASN   A O    1 
ATOM   1369 C CB   . ASN   A 1 59  ? 28.446 13.885  7.694   1.00 11.59 ?  59  ASN   A CB   1 
ATOM   1370 C CG   . ASN   A 1 59  ? 28.803 13.827  6.224   1.00 12.11 ?  59  ASN   A CG   1 
ATOM   1371 O OD1  . ASN   A 1 59  ? 28.099 13.207  5.425   1.00 12.35 ?  59  ASN   A OD1  1 
ATOM   1372 N ND2  . ASN   A 1 59  ? 29.897 14.482  5.852   1.00 12.47 ?  59  ASN   A ND2  1 
ATOM   1373 H H    . ASN   A 1 59  ? 26.561 11.928  9.266   1.00 13.99 ?  59  ASN   A H    1 
ATOM   1374 H HA   . ASN   A 1 59  ? 27.783 11.962  7.577   1.00 13.60 ?  59  ASN   A HA   1 
ATOM   1375 H HB2  . ASN   A 1 59  ? 27.656 14.440  7.780   1.00 13.88 ?  59  ASN   A HB2  1 
ATOM   1376 H HB3  . ASN   A 1 59  ? 29.192 14.289  8.160   1.00 13.88 ?  59  ASN   A HB3  1 
ATOM   1377 H HD21 . ASN   A 1 59  ? 30.147 14.482  5.025   1.00 14.93 ?  59  ASN   A HD21 1 
ATOM   1378 H HD22 . ASN   A 1 59  ? 30.371 14.906  6.436   1.00 14.93 ?  59  ASN   A HD22 1 
ATOM   1379 N N    . ALA   A 1 60  ? 29.587 11.266  9.900   1.00 11.23 ?  60  ALA   A N    1 
ATOM   1380 C CA   . ALA   A 1 60  ? 30.820 10.574  10.260  1.00 11.36 ?  60  ALA   A CA   1 
ATOM   1381 C C    . ALA   A 1 60  ? 31.044 9.342   9.390   1.00 11.17 ?  60  ALA   A C    1 
ATOM   1382 O O    . ALA   A 1 60  ? 32.189 9.008   9.068   1.00 11.65 ?  60  ALA   A O    1 
ATOM   1383 C CB   . ALA   A 1 60  ? 30.805 10.189  11.739  1.00 12.18 ?  60  ALA   A CB   1 
ATOM   1384 H H    . ALA   A 1 60  ? 28.984 11.272  10.512  1.00 13.45 ?  60  ALA   A H    1 
ATOM   1385 H HA   . ALA   A 1 60  ? 31.569 11.175  10.122  1.00 13.60 ?  60  ALA   A HA   1 
ATOM   1386 H HB1  . ALA   A 1 60  ? 31.633 9.736   11.961  1.00 14.59 ?  60  ALA   A HB1  1 
ATOM   1387 H HB2  . ALA   A 1 60  ? 30.721 10.998  12.275  1.00 14.59 ?  60  ALA   A HB2  1 
ATOM   1388 H HB3  . ALA   A 1 60  ? 30.050 9.606   11.909  1.00 14.59 ?  60  ALA   A HB3  1 
ATOM   1389 N N    . MET   A 1 61  ? 29.969 8.655   8.997   1.00 10.86 ?  61  MET   A N    1 
ATOM   1390 C CA   . MET   A 1 61  ? 30.114 7.520   8.091   1.00 10.95 ?  61  MET   A CA   1 
ATOM   1391 C C    . MET   A 1 61  ? 30.752 7.942   6.768   1.00 10.73 ?  61  MET   A C    1 
ATOM   1392 O O    . MET   A 1 61  ? 31.654 7.264   6.260   1.00 10.93 ?  61  MET   A O    1 
ATOM   1393 C CB   . MET   A 1 61  ? 28.756 6.848   7.879   1.00 10.61 ?  61  MET   A CB   1 
ATOM   1394 C CG   . MET   A 1 61  ? 28.760 5.698   6.897   1.00 11.30 ?  61  MET   A CG   1 
ATOM   1395 S SD   . MET   A 1 61  ? 27.139 4.958   6.671   1.00 12.38 ?  61  MET   A SD   1 
ATOM   1396 C CE   . MET   A 1 61  ? 26.967 4.057   8.215   1.00 13.48 ?  61  MET   A CE   1 
ATOM   1397 H H    . MET   A 1 61  ? 29.161 8.830   9.230   1.00 13.00 ?  61  MET   A H    1 
ATOM   1398 H HA   . MET   A 1 61  ? 30.697 6.867   8.514   1.00 13.11 ?  61  MET   A HA   1 
ATOM   1399 H HB2  . MET   A 1 61  ? 28.448 6.503   8.731   1.00 12.71 ?  61  MET   A HB2  1 
ATOM   1400 H HB3  . MET   A 1 61  ? 28.133 7.509   7.549   1.00 12.71 ?  61  MET   A HB3  1 
ATOM   1401 H HG2  . MET   A 1 61  ? 29.055 6.011   6.032   1.00 13.54 ?  61  MET   A HG2  1 
ATOM   1402 H HG3  . MET   A 1 61  ? 29.356 5.003   7.222   1.00 13.54 ?  61  MET   A HG3  1 
ATOM   1403 H HE1  . MET   A 1 61  ? 26.116 3.584   8.212   1.00 16.15 ?  61  MET   A HE1  1 
ATOM   1404 H HE2  . MET   A 1 61  ? 27.695 3.423   8.295   1.00 16.15 ?  61  MET   A HE2  1 
ATOM   1405 H HE3  . MET   A 1 61  ? 26.990 4.685   8.954   1.00 16.15 ?  61  MET   A HE3  1 
ATOM   1406 N N    . GLN   A 1 62  ? 30.317 9.076   6.209   1.00 10.79 ?  62  GLN   A N    1 
ATOM   1407 C CA   . GLN   A 1 62  ? 30.884 9.551   4.950   1.00 10.57 ?  62  GLN   A CA   1 
ATOM   1408 C C    . GLN   A 1 62  ? 32.356 9.925   5.106   1.00 10.77 ?  62  GLN   A C    1 
ATOM   1409 O O    . GLN   A 1 62  ? 33.173 9.607   4.236   1.00 11.06 ?  62  GLN   A O    1 
ATOM   1410 C CB   . GLN   A 1 62  ? 30.082 10.735  4.415   1.00 10.77 ?  62  GLN   A CB   1 
ATOM   1411 C CG   . GLN   A 1 62  ? 30.466 11.099  2.999   1.00 10.89 ?  62  GLN   A CG   1 
ATOM   1412 C CD   . GLN   A 1 62  ? 30.149 9.973   2.044   1.00 11.17 ?  62  GLN   A CD   1 
ATOM   1413 O OE1  . GLN   A 1 62  ? 28.973 9.668   1.824   1.00 11.73 ?  62  GLN   A OE1  1 
ATOM   1414 N NE2  . GLN   A 1 62  ? 31.174 9.311   1.516   1.00 11.64 ?  62  GLN   A NE2  1 
ATOM   1415 H H    . GLN   A 1 62  ? 29.697 9.572   6.535   1.00 12.92 ?  62  GLN   A H    1 
ATOM   1416 H HA   . GLN   A 1 62  ? 30.834 8.828   4.302   1.00 12.65 ?  62  GLN   A HA   1 
ATOM   1417 H HB2  . GLN   A 1 62  ? 29.140 10.509  4.425   1.00 12.90 ?  62  GLN   A HB2  1 
ATOM   1418 H HB3  . GLN   A 1 62  ? 30.248 11.506  4.978   1.00 12.90 ?  62  GLN   A HB3  1 
ATOM   1419 H HG2  . GLN   A 1 62  ? 29.960 11.879  2.720   1.00 13.04 ?  62  GLN   A HG2  1 
ATOM   1420 H HG3  . GLN   A 1 62  ? 31.416 11.280  2.950   1.00 13.04 ?  62  GLN   A HG3  1 
ATOM   1421 H HE21 . GLN   A 1 62  ? 31.979 9.547   1.705   1.00 13.94 ?  62  GLN   A HE21 1 
ATOM   1422 H HE22 . GLN   A 1 62  ? 31.033 8.660   0.972   1.00 13.94 ?  62  GLN   A HE22 1 
ATOM   1423 N N    . VAL   A 1 63  ? 32.710 10.600  6.202   1.00 11.32 ?  63  VAL   A N    1 
ATOM   1424 C CA   . VAL   A 1 63  ? 34.102 10.991  6.434   1.00 11.83 ?  63  VAL   A CA   1 
ATOM   1425 C C    . VAL   A 1 63  ? 34.997 9.755   6.497   1.00 11.43 ?  63  VAL   A C    1 
ATOM   1426 O O    . VAL   A 1 63  ? 36.050 9.686   5.845   1.00 11.99 ?  63  VAL   A O    1 
ATOM   1427 C CB   . VAL   A 1 63  ? 34.195 11.859  7.702   1.00 13.76 ?  63  VAL   A CB   1 
ATOM   1428 C CG1  . VAL   A 1 63  ? 35.640 12.087  8.106   1.00 15.35 ?  63  VAL   A CG1  1 
ATOM   1429 C CG2  . VAL   A 1 63  ? 33.477 13.188  7.471   1.00 13.89 ?  63  VAL   A CG2  1 
ATOM   1430 H H    . VAL   A 1 63  ? 32.161 10.847  6.821   1.00 13.55 ?  63  VAL   A H    1 
ATOM   1431 H HA   . VAL   A 1 63  ? 34.394 11.535  5.687   1.00 14.16 ?  63  VAL   A HA   1 
ATOM   1432 H HB   . VAL   A 1 63  ? 33.744 11.403  8.433   1.00 16.48 ?  63  VAL   A HB   1 
ATOM   1433 H HG11 . VAL   A 1 63  ? 35.673 12.814  8.748   1.00 18.39 ?  63  VAL   A HG11 1 
ATOM   1434 H HG12 . VAL   A 1 63  ? 35.989 11.278  8.503   1.00 18.39 ?  63  VAL   A HG12 1 
ATOM   1435 H HG13 . VAL   A 1 63  ? 36.150 12.322  7.316   1.00 18.39 ?  63  VAL   A HG13 1 
ATOM   1436 H HG21 . VAL   A 1 63  ? 33.556 13.734  8.268   1.00 16.64 ?  63  VAL   A HG21 1 
ATOM   1437 H HG22 . VAL   A 1 63  ? 33.893 13.641  6.718   1.00 16.64 ?  63  VAL   A HG22 1 
ATOM   1438 H HG23 . VAL   A 1 63  ? 32.543 13.016  7.276   1.00 16.64 ?  63  VAL   A HG23 1 
ATOM   1439 N N    . GLU   A 1 64  ? 34.570 8.745   7.259   1.00 11.41 ?  64  GLU   A N    1 
ATOM   1440 C CA   . GLU   A 1 64  ? 35.330 7.505   7.348   1.00 11.47 ?  64  GLU   A CA   1 
ATOM   1441 C C    . GLU   A 1 64  ? 35.419 6.818   5.991   1.00 11.29 ?  64  GLU   A C    1 
ATOM   1442 O O    . GLU   A 1 64  ? 36.469 6.276   5.613   1.00 11.96 ?  64  GLU   A O    1 
ATOM   1443 C CB   . GLU   A 1 64  ? 34.642 6.594   8.364   1.00 12.02 ?  64  GLU   A CB   1 
ATOM   1444 C CG   . GLU   A 1 64  ? 35.293 5.243   8.514   1.00 12.85 ?  64  GLU   A CG   1 
ATOM   1445 C CD   . GLU   A 1 64  ? 34.408 4.244   9.233   1.00 13.45 ?  64  GLU   A CD   1 
ATOM   1446 O OE1  . GLU   A 1 64  ? 33.167 4.327   9.101   1.00 13.72 ?  64  GLU   A OE1  1 
ATOM   1447 O OE2  . GLU   A 1 64  ? 34.950 3.344   9.911   1.00 13.73 -1 64  GLU   A OE2  1 
ATOM   1448 H H    . GLU   A 1 64  ? 33.845 8.756   7.721   1.00 13.66 ?  64  GLU   A H    1 
ATOM   1449 H HA   . GLU   A 1 64  ? 36.228 7.702   7.664   1.00 13.73 ?  64  GLU   A HA   1 
ATOM   1450 H HB2  . GLU   A 1 64  ? 34.663 7.033   9.238   1.00 14.40 ?  64  GLU   A HB2  1 
ATOM   1451 H HB3  . GLU   A 1 64  ? 33.724 6.465   8.091   1.00 14.40 ?  64  GLU   A HB3  1 
ATOM   1452 H HG2  . GLU   A 1 64  ? 35.496 4.876   7.638   1.00 15.40 ?  64  GLU   A HG2  1 
ATOM   1453 H HG3  . GLU   A 1 64  ? 36.112 5.339   9.025   1.00 15.40 ?  64  GLU   A HG3  1 
ATOM   1454 N N    . SER   A 1 65  ? 34.308 6.820   5.250   1.00 10.80 ?  65  SER   A N    1 
ATOM   1455 C CA   . SER   A 1 65  ? 34.265 6.163   3.949   1.00 10.78 ?  65  SER   A CA   1 
ATOM   1456 C C    . SER   A 1 65  ? 35.190 6.837   2.942   1.00 11.10 ?  65  SER   A C    1 
ATOM   1457 O O    . SER   A 1 65  ? 35.830 6.163   2.126   1.00 12.14 ?  65  SER   A O    1 
ATOM   1458 C CB   . SER   A 1 65  ? 32.831 6.174   3.417   1.00 10.82 ?  65  SER   A CB   1 
ATOM   1459 O OG   . SER   A 1 65  ? 31.970 5.358   4.203   1.00 11.26 ?  65  SER   A OG   1 
ATOM   1460 H H    . SER   A 1 65  ? 33.572 7.202   5.481   1.00 12.93 ?  65  SER   A H    1 
ATOM   1461 H HA   . SER   A 1 65  ? 34.547 5.242   4.049   1.00 12.91 ?  65  SER   A HA   1 
ATOM   1462 H HB2  . SER   A 1 65  ? 32.492 7.079   3.431   1.00 12.96 ?  65  SER   A HB2  1 
ATOM   1463 H HB3  . SER   A 1 65  ? 32.831 5.832   2.510   1.00 12.96 ?  65  SER   A HB3  1 
ATOM   1464 H HG   . SER   A 1 65  ? 31.958 5.639   4.999   1.00 13.48 ?  65  SER   A HG   1 
ATOM   1465 N N    . ASP   A 1 66  ? 35.265 8.168   2.971   1.00 11.28 ?  66  ASP   A N    1 
ATOM   1466 C CA   . ASP   A 1 66  ? 36.128 8.869   2.029   1.00 12.15 ?  66  ASP   A CA   1 
ATOM   1467 C C    . ASP   A 1 66  ? 37.591 8.515   2.270   1.00 11.88 ?  66  ASP   A C    1 
ATOM   1468 O O    . ASP   A 1 66  ? 38.364 8.351   1.319   1.00 12.88 ?  66  ASP   A O    1 
ATOM   1469 C CB   . ASP   A 1 66  ? 35.901 10.376  2.140   1.00 13.64 ?  66  ASP   A CB   1 
ATOM   1470 C CG   . ASP   A 1 66  ? 34.571 10.839  1.522   1.00 16.04 ?  66  ASP   A CG   1 
ATOM   1471 O OD1  . ASP   A 1 66  ? 33.862 10.043  0.869   1.00 16.11 ?  66  ASP   A OD1  1 
ATOM   1472 O OD2  . ASP   A 1 66  ? 34.266 12.039  1.673   1.00 19.56 -1 66  ASP   A OD2  1 
ATOM   1473 H H    . ASP   A 1 66  ? 34.824 8.677   3.513   1.00 13.50 ?  66  ASP   A H    1 
ATOM   1474 H HA   . ASP   A 1 66  ? 35.898 8.595   1.130   1.00 14.55 ?  66  ASP   A HA   1 
ATOM   1475 H HB2  . ASP   A 1 66  ? 35.883 10.627  3.075   1.00 16.34 ?  66  ASP   A HB2  1 
ATOM   1476 H HB3  . ASP   A 1 66  ? 36.625 10.835  1.685   1.00 16.34 ?  66  ASP   A HB3  1 
ATOM   1477 N N    . ASP   A 1 67  ? 37.987 8.379   3.536   1.00 12.07 ?  67  ASP   A N    1 
ATOM   1478 C CA   . ASP   A 1 67  ? 39.339 7.928   3.842   1.00 13.15 ?  67  ASP   A CA   1 
ATOM   1479 C C    . ASP   A 1 67  ? 39.561 6.495   3.369   1.00 12.80 ?  67  ASP   A C    1 
ATOM   1480 O O    . ASP   A 1 67  ? 40.618 6.175   2.813   1.00 13.52 ?  67  ASP   A O    1 
ATOM   1481 C CB   . ASP   A 1 67  ? 39.604 8.061   5.340   1.00 14.43 ?  67  ASP   A CB   1 
ATOM   1482 C CG   . ASP   A 1 67  ? 40.896 7.400   5.764   1.00 15.66 ?  67  ASP   A CG   1 
ATOM   1483 O OD1  . ASP   A 1 67  ? 41.967 8.041   5.653   1.00 18.31 ?  67  ASP   A OD1  1 
ATOM   1484 O OD2  . ASP   A 1 67  ? 40.842 6.233   6.208   1.00 15.20 -1 67  ASP   A OD2  1 
ATOM   1485 H H    . ASP   A 1 67  ? 37.499 8.540   4.226   1.00 14.46 ?  67  ASP   A H    1 
ATOM   1486 H HA   . ASP   A 1 67  ? 39.972 8.494   3.377   1.00 15.75 ?  67  ASP   A HA   1 
ATOM   1487 H HB2  . ASP   A 1 67  ? 39.662 8.998   5.567   1.00 17.29 ?  67  ASP   A HB2  1 
ATOM   1488 H HB3  . ASP   A 1 67  ? 38.876 7.641   5.827   1.00 17.29 ?  67  ASP   A HB3  1 
ATOM   1489 N N    . TYR   A 1 68  ? 38.566 5.619   3.557   1.00 12.47 ?  68  TYR   A N    1 
ATOM   1490 C CA   . TYR   A 1 68  ? 38.686 4.240   3.081   1.00 12.54 ?  68  TYR   A CA   1 
ATOM   1491 C C    . TYR   A 1 68  ? 38.931 4.191   1.571   1.00 12.34 ?  68  TYR   A C    1 
ATOM   1492 O O    . TYR   A 1 68  ? 39.807 3.457   1.095   1.00 13.05 ?  68  TYR   A O    1 
ATOM   1493 C CB   . TYR   A 1 68  ? 37.434 3.425   3.461   1.00 12.58 ?  68  TYR   A CB   1 
ATOM   1494 C CG   . TYR   A 1 68  ? 37.454 2.039   2.831   1.00 14.42 ?  68  TYR   A CG   1 
ATOM   1495 C CD1  . TYR   A 1 68  ? 36.999 1.848   1.531   1.00 16.27 ?  68  TYR   A CD1  1 
ATOM   1496 C CD2  . TYR   A 1 68  ? 37.984 0.951   3.501   1.00 16.39 ?  68  TYR   A CD2  1 
ATOM   1497 C CE1  . TYR   A 1 68  ? 37.057 0.630   0.916   1.00 17.66 ?  68  TYR   A CE1  1 
ATOM   1498 C CE2  . TYR   A 1 68  ? 38.040 -0.309  2.885   1.00 17.51 ?  68  TYR   A CE2  1 
ATOM   1499 C CZ   . TYR   A 1 68  ? 37.579 -0.446  1.595   1.00 18.11 ?  68  TYR   A CZ   1 
ATOM   1500 O OH   . TYR   A 1 68  ? 37.649 -1.662  0.968   1.00 19.58 ?  68  TYR   A OH   1 
ATOM   1501 H H    . TYR   A 1 68  ? 37.820 5.799   3.946   1.00 14.93 ?  68  TYR   A H    1 
ATOM   1502 H HA   . TYR   A 1 68  ? 39.446 3.828   3.516   1.00 15.02 ?  68  TYR   A HA   1 
ATOM   1503 H HB2  . TYR   A 1 68  ? 37.405 3.318   4.426   1.00 15.07 ?  68  TYR   A HB2  1 
ATOM   1504 H HB3  . TYR   A 1 68  ? 36.642 3.889   3.151   1.00 15.07 ?  68  TYR   A HB3  1 
ATOM   1505 H HD1  . TYR   A 1 68  ? 36.656 2.581   1.064   1.00 19.50 ?  68  TYR   A HD1  1 
ATOM   1506 H HD2  . TYR   A 1 68  ? 38.310 1.053   4.364   1.00 19.65 ?  68  TYR   A HD2  1 
ATOM   1507 H HE1  . TYR   A 1 68  ? 36.734 0.533   0.049   1.00 21.17 ?  68  TYR   A HE1  1 
ATOM   1508 H HE2  . TYR   A 1 68  ? 38.390 -1.041  3.330   1.00 20.98 ?  68  TYR   A HE2  1 
ATOM   1509 H HH   . TYR   A 1 68  ? 37.965 -2.236  1.493   1.00 23.47 ?  68  TYR   A HH   1 
ATOM   1510 N N    . ILE   A 1 69  ? 38.150 4.955   0.798   1.00 12.14 ?  69  ILE   A N    1 
ATOM   1511 C CA   . ILE   A 1 69  ? 38.286 4.941   -0.660  1.00 12.44 ?  69  ILE   A CA   1 
ATOM   1512 C C    . ILE   A 1 69  ? 39.620 5.547   -1.090  1.00 12.46 ?  69  ILE   A C    1 
ATOM   1513 O O    . ILE   A 1 69  ? 40.267 5.062   -2.026  1.00 12.87 ?  69  ILE   A O    1 
ATOM   1514 C CB   . ILE   A 1 69  ? 37.094 5.663   -1.320  1.00 13.33 ?  69  ILE   A CB   1 
ATOM   1515 C CG1  . ILE   A 1 69  ? 35.779 4.925   -1.050  1.00 13.66 ?  69  ILE   A CG1  1 
ATOM   1516 C CG2  . ILE   A 1 69  ? 37.339 5.867   -2.823  1.00 15.33 ?  69  ILE   A CG2  1 
ATOM   1517 C CD1  . ILE   A 1 69  ? 35.624 3.627   -1.814  1.00 14.24 ?  69  ILE   A CD1  1 
ATOM   1518 H H    . ILE   A 1 69  ? 37.548 5.490   1.094   1.00 14.54 ?  69  ILE   A H    1 
ATOM   1519 H HA   . ILE   A 1 69  ? 38.276 4.020   -0.959  1.00 14.91 ?  69  ILE   A HA   1 
ATOM   1520 H HB   . ILE   A 1 69  ? 37.023 6.541   -0.915  1.00 15.97 ?  69  ILE   A HB   1 
ATOM   1521 H HG12 . ILE   A 1 69  ? 35.730 4.719   -0.101  1.00 16.36 ?  69  ILE   A HG12 1 
ATOM   1522 H HG13 . ILE   A 1 69  ? 35.043 5.505   -1.295  1.00 16.36 ?  69  ILE   A HG13 1 
ATOM   1523 H HG21 . ILE   A 1 69  ? 36.494 6.075   -3.255  1.00 18.37 ?  69  ILE   A HG21 1 
ATOM   1524 H HG22 . ILE   A 1 69  ? 37.956 6.612   -2.946  1.00 18.37 ?  69  ILE   A HG22 1 
ATOM   1525 H HG23 . ILE   A 1 69  ? 37.714 5.061   -3.199  1.00 18.37 ?  69  ILE   A HG23 1 
ATOM   1526 H HD11 . ILE   A 1 69  ? 34.810 3.192   -1.526  1.00 17.06 ?  69  ILE   A HD11 1 
ATOM   1527 H HD12 . ILE   A 1 69  ? 35.580 3.824   -2.762  1.00 17.06 ?  69  ILE   A HD12 1 
ATOM   1528 H HD13 . ILE   A 1 69  ? 36.388 3.059   -1.629  1.00 17.06 ?  69  ILE   A HD13 1 
ATOM   1529 N N    . ALA   A 1 70  ? 40.042 6.625   -0.433  1.00 13.16 ?  70  ALA   A N    1 
ATOM   1530 C CA   . ALA   A 1 70  ? 41.322 7.228   -0.790  1.00 14.33 ?  70  ALA   A CA   1 
ATOM   1531 C C    . ALA   A 1 70  ? 42.465 6.238   -0.618  1.00 14.81 ?  70  ALA   A C    1 
ATOM   1532 O O    . ALA   A 1 70  ? 43.435 6.272   -1.377  1.00 16.41 ?  70  ALA   A O    1 
ATOM   1533 C CB   . ALA   A 1 70  ? 41.569 8.481   0.051   1.00 14.74 ?  70  ALA   A CB   1 
ATOM   1534 H H    . ALA   A 1 70  ? 39.618 7.016   0.203   1.00 15.77 ?  70  ALA   A H    1 
ATOM   1535 H HA   . ALA   A 1 70  ? 41.295 7.497   -1.723  1.00 17.16 ?  70  ALA   A HA   1 
ATOM   1536 H HB1  . ALA   A 1 70  ? 42.428 8.864   -0.203  1.00 17.66 ?  70  ALA   A HB1  1 
ATOM   1537 H HB2  . ALA   A 1 70  ? 40.862 9.120   -0.114  1.00 17.66 ?  70  ALA   A HB2  1 
ATOM   1538 H HB3  . ALA   A 1 70  ? 41.585 8.233   0.988   1.00 17.66 ?  70  ALA   A HB3  1 
ATOM   1539 N N    . THR   A 1 71  ? 42.361 5.346   0.363   1.00 14.13 ?  71  THR   A N    1 
ATOM   1540 C CA   . THR   A 1 71  ? 43.413 4.365   0.614   1.00 15.23 ?  71  THR   A CA   1 
ATOM   1541 C C    . THR   A 1 71  ? 43.289 3.136   -0.277  1.00 15.52 ?  71  THR   A C    1 
ATOM   1542 O O    . THR   A 1 71  ? 44.299 2.608   -0.761  1.00 17.49 ?  71  THR   A O    1 
ATOM   1543 C CB   . THR   A 1 71  ? 43.342 3.919   2.070   1.00 17.44 ?  71  THR   A CB   1 
ATOM   1544 O OG1  . THR   A 1 71  ? 43.569 5.048   2.920   1.00 18.87 ?  71  THR   A OG1  1 
ATOM   1545 C CG2  . THR   A 1 71  ? 44.371 2.833   2.360   1.00 19.29 ?  71  THR   A CG2  1 
ATOM   1546 H H    . THR   A 1 71  ? 41.688 5.280   0.888   1.00 16.93 ?  71  THR   A H    1 
ATOM   1547 H HA   . THR   A 1 71  ? 44.279 4.767   0.454   1.00 18.25 ?  71  THR   A HA   1 
ATOM   1548 H HB   . THR   A 1 71  ? 42.460 3.546   2.242   1.00 20.90 ?  71  THR   A HB   1 
ATOM   1549 H HG1  . THR   A 1 71  ? 43.521 4.802   3.722   1.00 22.62 ?  71  THR   A HG1  1 
ATOM   1550 H HG21 . THR   A 1 71  ? 44.505 2.751   3.319   1.00 23.12 ?  71  THR   A HG21 1 
ATOM   1551 H HG22 . THR   A 1 71  ? 44.076 1.976   2.013   1.00 23.12 ?  71  THR   A HG22 1 
ATOM   1552 H HG23 . THR   A 1 71  ? 45.223 3.061   1.949   1.00 23.12 ?  71  THR   A HG23 1 
ATOM   1553 N N    . ASN   A 1 72  ? 42.065 2.638   -0.467  1.00 14.39 ?  72  ASN   A N    1 
ATOM   1554 C CA   . ASN   A 1 72  ? 41.849 1.314   -1.035  1.00 14.29 ?  72  ASN   A CA   1 
ATOM   1555 C C    . ASN   A 1 72  ? 41.238 1.311   -2.422  1.00 14.52 ?  72  ASN   A C    1 
ATOM   1556 O O    . ASN   A 1 72  ? 41.251 0.262   -3.076  1.00 15.99 ?  72  ASN   A O    1 
ATOM   1557 C CB   . ASN   A 1 72  ? 40.953 0.492   -0.105  1.00 15.09 ?  72  ASN   A CB   1 
ATOM   1558 C CG   . ASN   A 1 72  ? 41.556 0.336   1.265   1.00 16.38 ?  72  ASN   A CG   1 
ATOM   1559 O OD1  . ASN   A 1 72  ? 41.104 0.948   2.231   1.00 17.84 ?  72  ASN   A OD1  1 
ATOM   1560 N ND2  . ASN   A 1 72  ? 42.601 -0.460  1.354   1.00 16.84 ?  72  ASN   A ND2  1 
ATOM   1561 H H    . ASN   A 1 72  ? 41.335 3.051   -0.263  1.00 17.24 ?  72  ASN   A H    1 
ATOM   1562 H HA   . ASN   A 1 72  ? 42.700 0.861   -1.094  1.00 17.12 ?  72  ASN   A HA   1 
ATOM   1563 H HB2  . ASN   A 1 72  ? 40.096 0.932   -0.008  1.00 18.08 ?  72  ASN   A HB2  1 
ATOM   1564 H HB3  . ASN   A 1 72  ? 40.831 -0.396  -0.482  1.00 18.08 ?  72  ASN   A HB3  1 
ATOM   1565 H HD21 . ASN   A 1 72  ? 42.990 -0.579  2.114   1.00 20.18 ?  72  ASN   A HD21 1 
ATOM   1566 H HD22 . ASN   A 1 72  ? 42.901 -0.862  0.654   1.00 20.18 ?  72  ASN   A HD22 1 
ATOM   1567 N N    . GLY   A 1 73  ? 40.694 2.428   -2.882  1.00 13.92 ?  73  GLY   A N    1 
ATOM   1568 C CA   . GLY   A 1 73  ? 39.962 2.445   -4.122  1.00 14.02 ?  73  GLY   A CA   1 
ATOM   1569 C C    . GLY   A 1 73  ? 38.568 1.868   -3.959  1.00 13.18 ?  73  GLY   A C    1 
ATOM   1570 O O    . GLY   A 1 73  ? 38.173 1.414   -2.880  1.00 13.68 ?  73  GLY   A O    1 
ATOM   1571 H H    . GLY   A 1 73  ? 40.728 3.198   -2.485  1.00 16.68 ?  73  GLY   A H    1 
ATOM   1572 H HA2  . GLY   A 1 73  ? 39.884 3.359   -4.439  1.00 16.80 ?  73  GLY   A HA2  1 
ATOM   1573 H HA3  . GLY   A 1 73  ? 40.437 1.924   -4.785  1.00 16.80 ?  73  GLY   A HA3  1 
ATOM   1574 N N    . PRO   A 1 74  ? 37.798 1.882   -5.044  1.00 13.69 ?  74  PRO   A N    1 
ATOM   1575 C CA   . PRO   A 1 74  ? 36.399 1.452   -4.969  1.00 13.77 ?  74  PRO   A CA   1 
ATOM   1576 C C    . PRO   A 1 74  ? 36.243 -0.032  -4.658  1.00 13.13 ?  74  PRO   A C    1 
ATOM   1577 O O    . PRO   A 1 74  ? 37.112 -0.862  -4.948  1.00 13.87 ?  74  PRO   A O    1 
ATOM   1578 C CB   . PRO   A 1 74  ? 35.857 1.761   -6.370  1.00 15.56 ?  74  PRO   A CB   1 
ATOM   1579 C CG   . PRO   A 1 74  ? 36.819 2.737   -6.969  1.00 18.65 ?  74  PRO   A CG   1 
ATOM   1580 C CD   . PRO   A 1 74  ? 38.149 2.394   -6.380  1.00 15.93 ?  74  PRO   A CD   1 
ATOM   1581 H HA   . PRO   A 1 74  ? 35.913 1.980   -4.312  1.00 16.50 ?  74  PRO   A HA   1 
ATOM   1582 H HB2  . PRO   A 1 74  ? 35.825 0.946   -6.894  1.00 18.65 ?  74  PRO   A HB2  1 
ATOM   1583 H HB3  . PRO   A 1 74  ? 34.972 2.156   -6.300  1.00 18.65 ?  74  PRO   A HB3  1 
ATOM   1584 H HG2  . PRO   A 1 74  ? 36.836 2.631   -7.934  1.00 22.36 ?  74  PRO   A HG2  1 
ATOM   1585 H HG3  . PRO   A 1 74  ? 36.564 3.640   -6.728  1.00 22.36 ?  74  PRO   A HG3  1 
ATOM   1586 H HD2  . PRO   A 1 74  ? 38.589 1.702   -6.906  1.00 19.08 ?  74  PRO   A HD2  1 
ATOM   1587 H HD3  . PRO   A 1 74  ? 38.703 3.190   -6.317  1.00 19.08 ?  74  PRO   A HD3  1 
ATOM   1588 N N    . LEU   A 1 75  ? 35.095 -0.358  -4.072  1.00 12.05 ?  75  LEU   A N    1 
ATOM   1589 C CA   . LEU   A 1 75  ? 34.687 -1.746  -3.935  1.00 11.79 ?  75  LEU   A CA   1 
ATOM   1590 C C    . LEU   A 1 75  ? 34.303 -2.310  -5.299  1.00 12.37 ?  75  LEU   A C    1 
ATOM   1591 O O    . LEU   A 1 75  ? 34.197 -1.593  -6.296  1.00 13.57 ?  75  LEU   A O    1 
ATOM   1592 C CB   . LEU   A 1 75  ? 33.495 -1.871  -2.991  1.00 12.01 ?  75  LEU   A CB   1 
ATOM   1593 C CG   . LEU   A 1 75  ? 33.701 -1.452  -1.539  1.00 13.76 ?  75  LEU   A CG   1 
ATOM   1594 C CD1  . LEU   A 1 75  ? 32.408 -1.651  -0.752  1.00 16.28 ?  75  LEU   A CD1  1 
ATOM   1595 C CD2  . LEU   A 1 75  ? 34.828 -2.186  -0.879  1.00 17.45 ?  75  LEU   A CD2  1 
ATOM   1596 H H    . LEU   A 1 75  ? 34.540 0.212   -3.739  1.00 14.44 ?  75  LEU   A H    1 
ATOM   1597 H HA   . LEU   A 1 75  ? 35.423 -2.264  -3.583  1.00 14.12 ?  75  LEU   A HA   1 
ATOM   1598 H HB2  . LEU   A 1 75  ? 32.771 -1.332  -3.344  1.00 14.39 ?  75  LEU   A HB2  1 
ATOM   1599 H HB3  . LEU   A 1 75  ? 33.221 -2.803  -2.981  1.00 14.39 ?  75  LEU   A HB3  1 
ATOM   1600 H HG   . LEU   A 1 75  ? 33.917 -0.505  -1.520  1.00 16.49 ?  75  LEU   A HG   1 
ATOM   1601 H HD11 . LEU   A 1 75  ? 32.553 -1.373  0.167   1.00 19.51 ?  75  LEU   A HD11 1 
ATOM   1602 H HD12 . LEU   A 1 75  ? 31.710 -1.105  -1.153  1.00 19.51 ?  75  LEU   A HD12 1 
ATOM   1603 H HD13 . LEU   A 1 75  ? 32.159 -2.584  -0.783  1.00 19.51 ?  75  LEU   A HD13 1 
ATOM   1604 H HD21 . LEU   A 1 75  ? 34.871 -1.926  0.054   1.00 20.91 ?  75  LEU   A HD21 1 
ATOM   1605 H HD22 . LEU   A 1 75  ? 34.672 -3.138  -0.954  1.00 20.91 ?  75  LEU   A HD22 1 
ATOM   1606 H HD23 . LEU   A 1 75  ? 35.662 -1.951  -1.323  1.00 20.91 ?  75  LEU   A HD23 1 
ATOM   1607 N N    . LYS   A 1 76  ? 34.105 -3.625  -5.327  1.00 12.34 ?  76  LYS   A N    1 
ATOM   1608 C CA   . LYS   A 1 76  ? 33.507 -4.327  -6.454  1.00 12.56 ?  76  LYS   A CA   1 
ATOM   1609 C C    . LYS   A 1 76  ? 31.998 -4.419  -6.257  1.00 11.47 ?  76  LYS   A C    1 
ATOM   1610 O O    . LYS   A 1 76  ? 31.518 -4.556  -5.132  1.00 11.84 ?  76  LYS   A O    1 
ATOM   1611 C CB   . LYS   A 1 76  ? 34.047 -5.766  -6.525  1.00 15.00 ?  76  LYS   A CB   1 
ATOM   1612 C CG   . LYS   A 1 76  ? 35.560 -5.886  -6.695  1.00 16.48 ?  76  LYS   A CG   1 
ATOM   1613 C CD   . LYS   A 1 76  ? 36.055 -7.308  -6.541  1.00 17.92 ?  76  LYS   A CD   1 
ATOM   1614 C CE   . LYS   A 1 76  ? 37.557 -7.376  -6.719  1.00 20.64 ?  76  LYS   A CE   1 
ATOM   1615 N NZ   . LYS   A 1 76  ? 38.067 -8.749  -6.548  1.00 21.77 ?  76  LYS   A NZ   1 
ATOM   1616 H H    . LYS   A 1 76  ? 34.316 -4.147  -4.677  1.00 14.78 ?  76  LYS   A H    1 
ATOM   1617 H HA   . LYS   A 1 76  ? 33.703 -3.864  -7.286  1.00 15.04 ?  76  LYS   A HA   1 
ATOM   1618 H HB2  . LYS   A 1 76  ? 33.809 -6.220  -5.703  1.00 17.98 ?  76  LYS   A HB2  1 
ATOM   1619 H HB3  . LYS   A 1 76  ? 33.633 -6.209  -7.278  1.00 17.98 ?  76  LYS   A HB3  1 
ATOM   1620 H HG2  . LYS   A 1 76  ? 35.804 -5.574  -7.581  1.00 19.75 ?  76  LYS   A HG2  1 
ATOM   1621 H HG3  . LYS   A 1 76  ? 35.999 -5.340  -6.021  1.00 19.75 ?  76  LYS   A HG3  1 
ATOM   1622 H HD2  . LYS   A 1 76  ? 35.834 -7.631  -5.653  1.00 21.48 ?  76  LYS   A HD2  1 
ATOM   1623 H HD3  . LYS   A 1 76  ? 35.639 -7.866  -7.217  1.00 21.48 ?  76  LYS   A HD3  1 
ATOM   1624 H HE2  . LYS   A 1 76  ? 37.785 -7.073  -7.611  1.00 24.74 ?  76  LYS   A HE2  1 
ATOM   1625 H HE3  . LYS   A 1 76  ? 37.980 -6.809  -6.054  1.00 24.74 ?  76  LYS   A HE3  1 
ATOM   1626 H HZ1  . LYS   A 1 76  ? 38.949 -8.765  -6.658  1.00 26.09 ?  76  LYS   A HZ1  1 
ATOM   1627 H HZ2  . LYS   A 1 76  ? 37.871 -9.052  -5.734  1.00 26.09 ?  76  LYS   A HZ2  1 
ATOM   1628 H HZ3  . LYS   A 1 76  ? 37.693 -9.291  -7.152  1.00 26.09 ?  76  LYS   A HZ3  1 
ATOM   1629 N N    . VAL   A 1 77  ? 31.247 -4.379  -7.360  1.00 11.92 ?  77  VAL   A N    1 
ATOM   1630 C CA   . VAL   A 1 77  ? 29.840 -4.765  -7.272  1.00 12.20 ?  77  VAL   A CA   1 
ATOM   1631 C C    . VAL   A 1 77  ? 29.773 -6.219  -6.836  1.00 11.82 ?  77  VAL   A C    1 
ATOM   1632 O O    . VAL   A 1 77  ? 30.435 -7.087  -7.418  1.00 12.09 ?  77  VAL   A O    1 
ATOM   1633 C CB   . VAL   A 1 77  ? 29.109 -4.542  -8.603  1.00 13.39 ?  77  VAL   A CB   1 
ATOM   1634 C CG1  . VAL   A 1 77  ? 27.644 -4.963  -8.476  1.00 14.08 ?  77  VAL   A CG1  1 
ATOM   1635 C CG2  . VAL   A 1 77  ? 29.203 -3.089  -9.032  1.00 14.69 ?  77  VAL   A CG2  1 
ATOM   1636 H H    . VAL   A 1 77  ? 31.520 -4.135  -8.137  1.00 14.27 ?  77  VAL   A H    1 
ATOM   1637 H HA   . VAL   A 1 77  ? 29.405 -4.224  -6.594  1.00 14.61 ?  77  VAL   A HA   1 
ATOM   1638 H HB   . VAL   A 1 77  ? 29.526 -5.089  -9.289  1.00 16.04 ?  77  VAL   A HB   1 
ATOM   1639 H HG11 . VAL   A 1 77  ? 27.163 -4.660  -9.259  1.00 16.87 ?  77  VAL   A HG11 1 
ATOM   1640 H HG12 . VAL   A 1 77  ? 27.596 -5.929  -8.408  1.00 16.87 ?  77  VAL   A HG12 1 
ATOM   1641 H HG13 . VAL   A 1 77  ? 27.270 -4.556  -7.678  1.00 16.87 ?  77  VAL   A HG13 1 
ATOM   1642 H HG21 . VAL   A 1 77  ? 28.686 -2.969  -9.840  1.00 17.60 ?  77  VAL   A HG21 1 
ATOM   1643 H HG22 . VAL   A 1 77  ? 28.849 -2.532  -8.321  1.00 17.60 ?  77  VAL   A HG22 1 
ATOM   1644 H HG23 . VAL   A 1 77  ? 30.133 -2.868  -9.193  1.00 17.60 ?  77  VAL   A HG23 1 
ATOM   1645 N N    . GLY   A 1 78  ? 28.980 -6.491  -5.797  1.00 11.55 ?  78  GLY   A N    1 
ATOM   1646 C CA   . GLY   A 1 78  ? 28.954 -7.782  -5.144  1.00 11.84 ?  78  GLY   A CA   1 
ATOM   1647 C C    . GLY   A 1 78  ? 29.864 -7.890  -3.940  1.00 11.31 ?  78  GLY   A C    1 
ATOM   1648 O O    . GLY   A 1 78  ? 29.805 -8.901  -3.224  1.00 12.05 ?  78  GLY   A O    1 
ATOM   1649 H H    . GLY   A 1 78  ? 28.428 -5.920  -5.457  1.00 13.84 ?  78  GLY   A H    1 
ATOM   1650 H HA2  . GLY   A 1 78  ? 28.049 -7.968  -4.856  1.00 14.18 ?  78  GLY   A HA2  1 
ATOM   1651 H HA3  . GLY   A 1 78  ? 29.214 -8.461  -5.786  1.00 14.18 ?  78  GLY   A HA3  1 
ATOM   1652 N N    . GLY   A 1 79  ? 30.725 -6.894  -3.712  1.00 11.38 ?  79  GLY   A N    1 
ATOM   1653 C CA   . GLY   A 1 79  ? 31.683 -6.926  -2.630  1.00 11.70 ?  79  GLY   A CA   1 
ATOM   1654 C C    . GLY   A 1 79  ? 31.236 -6.125  -1.420  1.00 10.84 ?  79  GLY   A C    1 
ATOM   1655 O O    . GLY   A 1 79  ? 30.121 -5.602  -1.349  1.00 11.15 ?  79  GLY   A O    1 
ATOM   1656 H H    . GLY   A 1 79  ? 30.778 -6.180  -4.191  1.00 13.63 ?  79  GLY   A H    1 
ATOM   1657 H HA2  . GLY   A 1 79  ? 31.825 -7.852  -2.356  1.00 14.01 ?  79  GLY   A HA2  1 
ATOM   1658 H HA3  . GLY   A 1 79  ? 32.532 -6.574  -2.938  1.00 14.01 ?  79  GLY   A HA3  1 
ATOM   1659 N N    . SER   A 1 80  ? 32.135 -6.038  -0.443  1.00 11.55 ?  80  SER   A N    1 
ATOM   1660 C CA   . SER   A 1 80  ? 31.816 -5.402  0.825   1.00 11.12 ?  80  SER   A CA   1 
ATOM   1661 C C    . SER   A 1 80  ? 33.085 -4.958  1.532   1.00 10.89 ?  80  SER   A C    1 
ATOM   1662 O O    . SER   A 1 80  ? 34.198 -5.388  1.206   1.00 12.42 ?  80  SER   A O    1 
ATOM   1663 C CB   . SER   A 1 80  ? 31.047 -6.358  1.745   1.00 11.97 ?  80  SER   A CB   1 
ATOM   1664 O OG   . SER   A 1 80  ? 31.870 -7.414  2.216   1.00 13.84 ?  80  SER   A OG   1 
ATOM   1665 H H    . SER   A 1 80  ? 32.944 -6.331  -0.497  1.00 13.83 ?  80  SER   A H    1 
ATOM   1666 H HA   . SER   A 1 80  ? 31.266 -4.621  0.648   1.00 13.31 ?  80  SER   A HA   1 
ATOM   1667 H HB2  . SER   A 1 80  ? 30.719 -5.856  2.506   1.00 14.34 ?  80  SER   A HB2  1 
ATOM   1668 H HB3  . SER   A 1 80  ? 30.304 -6.734  1.251   1.00 14.34 ?  80  SER   A HB3  1 
ATOM   1669 H HG   . SER   A 1 80  ? 32.165 -7.856  1.560   1.00 16.58 ?  80  SER   A HG   1 
ATOM   1670 N N    . CYS   A 1 81  ? 32.894 -4.111  2.541   1.00 10.74 ?  81  CYS   A N    1 
ATOM   1671 C CA   . CYS   A 1 81  ? 33.940 -3.822  3.507   1.00 10.95 ?  81  CYS   A CA   1 
ATOM   1672 C C    . CYS   A 1 81  ? 33.293 -3.592  4.864   1.00 10.98 ?  81  CYS   A C    1 
ATOM   1673 O O    . CYS   A 1 81  ? 32.130 -3.189  4.950   1.00 12.13 ?  81  CYS   A O    1 
ATOM   1674 C CB   . CYS   A 1 81  ? 34.809 -2.629  3.094   1.00 11.73 ?  81  CYS   A CB   1 
ATOM   1675 S SG   . CYS   A 1 81  ? 33.926 -1.055  3.107   1.00 12.34 ?  81  CYS   A SG   1 
ATOM   1676 H H    . CYS   A 1 81  ? 32.154 -3.695  2.693   1.00 12.86 ?  81  CYS   A H    1 
ATOM   1677 H HA   . CYS   A 1 81  ? 34.521 -4.596  3.580   1.00 13.11 ?  81  CYS   A HA   1 
ATOM   1678 H HB2  . CYS   A 1 81  ? 35.558 -2.558  3.710   1.00 14.05 ?  81  CYS   A HB2  1 
ATOM   1679 H HB3  . CYS   A 1 81  ? 35.144 -2.780  2.194   1.00 14.05 ?  81  CYS   A HB3  1 
ATOM   1680 H HG   . CYS   A 1 81  ? 34.686 -0.180  2.769   1.00 14.78 ?  81  CYS   A HG   1 
ATOM   1681 N N    . VAL   A 1 82  ? 34.054 -3.859  5.920   1.00 11.08 ?  82  VAL   A N    1 
ATOM   1682 C CA   . VAL   A 1 82  ? 33.623 -3.616  7.291   1.00 11.71 ?  82  VAL   A CA   1 
ATOM   1683 C C    . VAL   A 1 82  ? 34.225 -2.299  7.762   1.00 11.71 ?  82  VAL   A C    1 
ATOM   1684 O O    . VAL   A 1 82  ? 35.450 -2.124  7.740   1.00 12.65 ?  82  VAL   A O    1 
ATOM   1685 C CB   . VAL   A 1 82  ? 34.044 -4.759  8.226   1.00 13.27 ?  82  VAL   A CB   1 
ATOM   1686 C CG1  . VAL   A 1 82  ? 33.586 -4.466  9.643   1.00 14.44 ?  82  VAL   A CG1  1 
ATOM   1687 C CG2  . VAL   A 1 82  ? 33.482 -6.083  7.747   1.00 14.45 ?  82  VAL   A CG2  1 
ATOM   1688 H H    . VAL   A 1 82  ? 34.849 -4.197  5.863   1.00 13.26 ?  82  VAL   A H    1 
ATOM   1689 H HA   . VAL   A 1 82  ? 32.656 -3.535  7.309   1.00 14.02 ?  82  VAL   A HA   1 
ATOM   1690 H HB   . VAL   A 1 82  ? 35.010 -4.820  8.230   1.00 15.89 ?  82  VAL   A HB   1 
ATOM   1691 H HG11 . VAL   A 1 82  ? 33.673 -5.273  10.174  1.00 17.30 ?  82  VAL   A HG11 1 
ATOM   1692 H HG12 . VAL   A 1 82  ? 34.135 -3.762  10.022  1.00 17.30 ?  82  VAL   A HG12 1 
ATOM   1693 H HG13 . VAL   A 1 82  ? 32.654 -4.185  9.625   1.00 17.30 ?  82  VAL   A HG13 1 
ATOM   1694 H HG21 . VAL   A 1 82  ? 33.726 -6.775  8.381   1.00 17.31 ?  82  VAL   A HG21 1 
ATOM   1695 H HG22 . VAL   A 1 82  ? 32.515 -6.015  7.689   1.00 17.31 ?  82  VAL   A HG22 1 
ATOM   1696 H HG23 . VAL   A 1 82  ? 33.852 -6.287  6.874   1.00 17.31 ?  82  VAL   A HG23 1 
ATOM   1697 N N    . LEU   A 1 83  ? 33.373 -1.373  8.187   1.00 11.38 ?  83  LEU   A N    1 
ATOM   1698 C CA   . LEU   A 1 83  ? 33.793 -0.109  8.771   1.00 11.60 ?  83  LEU   A CA   1 
ATOM   1699 C C    . LEU   A 1 83  ? 33.078 0.069   10.107  1.00 11.68 ?  83  LEU   A C    1 
ATOM   1700 O O    . LEU   A 1 83  ? 32.360 -0.823  10.572  1.00 12.09 ?  83  LEU   A O    1 
ATOM   1701 C CB   . LEU   A 1 83  ? 33.549 1.052   7.795   1.00 12.28 ?  83  LEU   A CB   1 
ATOM   1702 C CG   . LEU   A 1 83  ? 34.459 1.044   6.559   1.00 12.76 ?  83  LEU   A CG   1 
ATOM   1703 C CD1  . LEU   A 1 83  ? 34.045 2.091   5.545   1.00 13.34 ?  83  LEU   A CD1  1 
ATOM   1704 C CD2  . LEU   A 1 83  ? 35.931 1.246   6.947   1.00 13.65 ?  83  LEU   A CD2  1 
ATOM   1705 H H    . LEU   A 1 83  ? 32.518 -1.457  8.140   1.00 13.62 ?  83  LEU   A H    1 
ATOM   1706 H HA   . LEU   A 1 83  ? 34.743 -0.143  8.951   1.00 13.89 ?  83  LEU   A HA   1 
ATOM   1707 H HB2  . LEU   A 1 83  ? 32.631 1.015   7.482   1.00 14.71 ?  83  LEU   A HB2  1 
ATOM   1708 H HB3  . LEU   A 1 83  ? 33.697 1.892   8.260   1.00 14.71 ?  83  LEU   A HB3  1 
ATOM   1709 H HG   . LEU   A 1 83  ? 34.387 0.176   6.132   1.00 15.29 ?  83  LEU   A HG   1 
ATOM   1710 H HD11 . LEU   A 1 83  ? 34.644 2.037   4.778   1.00 15.98 ?  83  LEU   A HD11 1 
ATOM   1711 H HD12 . LEU   A 1 83  ? 33.136 1.916   5.263   1.00 15.98 ?  83  LEU   A HD12 1 
ATOM   1712 H HD13 . LEU   A 1 83  ? 34.110 2.967   5.950   1.00 15.98 ?  83  LEU   A HD13 1 
ATOM   1713 H HD21 . LEU   A 1 83  ? 36.454 1.398   6.142   1.00 16.35 ?  83  LEU   A HD21 1 
ATOM   1714 H HD22 . LEU   A 1 83  ? 36.002 2.014   7.535   1.00 16.35 ?  83  LEU   A HD22 1 
ATOM   1715 H HD23 . LEU   A 1 83  ? 36.254 0.452   7.402   1.00 16.35 ?  83  LEU   A HD23 1 
ATOM   1716 N N    . SER   A 1 84  ? 33.287 1.219   10.739  1.00 12.04 ?  84  SER   A N    1 
ATOM   1717 C CA   . SER   A 1 84  ? 32.641 1.475   12.014  1.00 12.33 ?  84  SER   A CA   1 
ATOM   1718 C C    . SER   A 1 84  ? 31.123 1.557   11.865  1.00 12.14 ?  84  SER   A C    1 
ATOM   1719 O O    . SER   A 1 84  ? 30.597 2.014   10.849  1.00 12.29 ?  84  SER   A O    1 
ATOM   1720 C CB   . SER   A 1 84  ? 33.132 2.803   12.579  1.00 13.25 ?  84  SER   A CB   1 
ATOM   1721 O OG   . SER   A 1 84  ? 32.498 3.075   13.812  1.00 14.12 ?  84  SER   A OG   1 
ATOM   1722 H H    . SER   A 1 84  ? 33.790 1.860   10.447  1.00 14.42 ?  84  SER   A H    1 
ATOM   1723 H HA   . SER   A 1 84  ? 32.865 0.771   12.638  1.00 14.76 ?  84  SER   A HA   1 
ATOM   1724 H HB2  . SER   A 1 84  ? 34.092 2.760   12.711  1.00 15.87 ?  84  SER   A HB2  1 
ATOM   1725 H HB3  . SER   A 1 84  ? 32.919 3.515   11.948  1.00 15.87 ?  84  SER   A HB3  1 
ATOM   1726 H HG   . SER   A 1 84  ? 32.775 3.810   14.119  1.00 16.92 ?  84  SER   A HG   1 
ATOM   1727 N N    . GLY   A 1 85  ? 30.417 1.151   12.917  1.00 13.02 ?  85  GLY   A N    1 
ATOM   1728 C CA   . GLY   A 1 85  ? 28.993 1.386   12.998  1.00 13.32 ?  85  GLY   A CA   1 
ATOM   1729 C C    . GLY   A 1 85  ? 28.624 2.703   13.640  1.00 12.90 ?  85  GLY   A C    1 
ATOM   1730 O O    . GLY   A 1 85  ? 27.435 3.020   13.749  1.00 13.93 ?  85  GLY   A O    1 
ATOM   1731 H H    . GLY   A 1 85  ? 30.753 0.740   13.596  1.00 15.59 ?  85  GLY   A H    1 
ATOM   1732 H HA2  . GLY   A 1 85  ? 28.623 1.368   12.101  1.00 15.96 ?  85  GLY   A HA2  1 
ATOM   1733 H HA3  . GLY   A 1 85  ? 28.588 0.678   13.510  1.00 15.96 ?  85  GLY   A HA3  1 
ATOM   1734 N N    . HIS   A 1 86  ? 29.611 3.478   14.080  1.00 13.07 ?  86  HIS   A N    1 
ATOM   1735 C CA   . HIS   A 1 86  ? 29.387 4.815   14.652  1.00 13.33 ?  86  HIS   A CA   1 
ATOM   1736 C C    . HIS   A 1 86  ? 28.396 4.694   15.802  1.00 14.27 ?  86  HIS   A C    1 
ATOM   1737 O O    . HIS   A 1 86  ? 28.568 3.807   16.655  1.00 15.90 ?  86  HIS   A O    1 
ATOM   1738 C CB   . HIS   A 1 86  ? 29.022 5.802   13.549  1.00 13.54 ?  86  HIS   A CB   1 
ATOM   1739 C CG   . HIS   A 1 86  ? 30.082 5.897   12.514  1.00 13.26 ?  86  HIS   A CG   1 
ATOM   1740 N ND1  . HIS   A 1 86  ? 31.176 6.723   12.655  1.00 14.59 ?  86  HIS   A ND1  1 
ATOM   1741 C CD2  . HIS   A 1 86  ? 30.266 5.211   11.364  1.00 13.06 ?  86  HIS   A CD2  1 
ATOM   1742 C CE1  . HIS   A 1 86  ? 31.974 6.561   11.615  1.00 14.44 ?  86  HIS   A CE1  1 
ATOM   1743 N NE2  . HIS   A 1 86  ? 31.452 5.640   10.826  1.00 13.24 ?  86  HIS   A NE2  1 
ATOM   1744 H H    . HIS   A 1 86  ? 30.437 3.257   14.065  1.00 15.65 ?  86  HIS   A H    1 
ATOM   1745 H HA   . HIS   A 1 86  ? 30.222 5.125   15.032  1.00 15.97 ?  86  HIS   A HA   1 
ATOM   1746 H HB2  . HIS   A 1 86  ? 28.202 5.524   13.117  1.00 16.23 ?  86  HIS   A HB2  1 
ATOM   1747 H HB3  . HIS   A 1 86  ? 28.906 6.692   13.935  1.00 16.23 ?  86  HIS   A HB3  1 
ATOM   1748 H HD2  . HIS   A 1 86  ? 29.705 4.558   11.009  1.00 15.65 ?  86  HIS   A HD2  1 
ATOM   1749 H HE1  . HIS   A 1 86  ? 32.775 7.012   11.458  1.00 17.30 ?  86  HIS   A HE1  1 
ATOM   1750 H HE2  . HIS   A 1 86  ? 31.794 5.364   10.076  1.00 15.86 ?  86  HIS   A HE2  1 
ATOM   1751 N N    . ASN   A 1 87  ? 27.384 5.550   15.872  1.00 15.21 ?  87  ASN   A N    1 
ATOM   1752 C CA   . ASN   A 1 87  ? 26.398 5.537   16.935  1.00 15.97 ?  87  ASN   A CA   1 
ATOM   1753 C C    . ASN   A 1 87  ? 25.274 4.543   16.691  1.00 17.55 ?  87  ASN   A C    1 
ATOM   1754 O O    . ASN   A 1 87  ? 24.357 4.467   17.511  1.00 20.20 ?  87  ASN   A O    1 
ATOM   1755 C CB   . ASN   A 1 87  ? 25.802 6.944   17.097  1.00 17.10 ?  87  ASN   A CB   1 
ATOM   1756 C CG   . ASN   A 1 87  ? 25.300 7.527   15.780  1.00 18.42 ?  87  ASN   A CG   1 
ATOM   1757 O OD1  . ASN   A 1 87  ? 25.939 7.395   14.738  1.00 19.16 ?  87  ASN   A OD1  1 
ATOM   1758 N ND2  . ASN   A 1 87  ? 24.153 8.182   15.828  1.00 19.60 ?  87  ASN   A ND2  1 
ATOM   1759 H H    . ASN   A 1 87  ? 27.245 6.168   15.297  1.00 18.23 ?  87  ASN   A H    1 
ATOM   1760 H HA   . ASN   A 1 87  ? 26.821 5.297   17.776  1.00 19.14 ?  87  ASN   A HA   1 
ATOM   1761 H HB2  . ASN   A 1 87  ? 25.050 6.906   17.718  1.00 20.49 ?  87  ASN   A HB2  1 
ATOM   1762 H HB3  . ASN   A 1 87  ? 26.484 7.538   17.451  1.00 20.49 ?  87  ASN   A HB3  1 
ATOM   1763 H HD21 . ASN   A 1 87  ? 23.831 8.526   15.112  1.00 23.49 ?  87  ASN   A HD21 1 
ATOM   1764 H HD22 . ASN   A 1 87  ? 23.732 8.263   16.575  1.00 23.49 ?  87  ASN   A HD22 1 
ATOM   1765 N N    . LEU   A 1 88  ? 25.323 3.774   15.608  1.00 16.06 ?  88  LEU   A N    1 
ATOM   1766 C CA   . LEU   A 1 88  ? 24.217 2.906   15.221  1.00 16.29 ?  88  LEU   A CA   1 
ATOM   1767 C C    . LEU   A 1 88  ? 24.439 1.429   15.520  1.00 15.77 ?  88  LEU   A C    1 
ATOM   1768 O O    . LEU   A 1 88  ? 23.460 0.696   15.684  1.00 17.17 ?  88  LEU   A O    1 
ATOM   1769 C CB   . LEU   A 1 88  ? 23.952 3.055   13.722  1.00 16.71 ?  88  LEU   A CB   1 
ATOM   1770 C CG   . LEU   A 1 88  ? 23.685 4.479   13.237  1.00 18.71 ?  88  LEU   A CG   1 
ATOM   1771 C CD1  . LEU   A 1 88  ? 23.557 4.488   11.725  1.00 19.07 ?  88  LEU   A CD1  1 
ATOM   1772 C CD2  . LEU   A 1 88  ? 22.436 5.062   13.889  1.00 20.74 ?  88  LEU   A CD2  1 
ATOM   1773 H H    . LEU   A 1 88  ? 25.990 3.750   15.074  1.00 19.24 ?  88  LEU   A H    1 
ATOM   1774 H HA   . LEU   A 1 88  ? 23.416 3.188   15.691  1.00 19.52 ?  88  LEU   A HA   1 
ATOM   1775 H HB2  . LEU   A 1 88  ? 24.720 2.723   13.235  1.00 20.03 ?  88  LEU   A HB2  1 
ATOM   1776 H HB3  . LEU   A 1 88  ? 23.170 2.524   13.494  1.00 20.03 ?  88  LEU   A HB3  1 
ATOM   1777 H HG   . LEU   A 1 88  ? 24.438 5.040   13.474  1.00 22.42 ?  88  LEU   A HG   1 
ATOM   1778 H HD11 . LEU   A 1 88  ? 23.402 5.398   11.426  1.00 22.85 ?  88  LEU   A HD11 1 
ATOM   1779 H HD12 . LEU   A 1 88  ? 24.379 4.148   11.336  1.00 22.85 ?  88  LEU   A HD12 1 
ATOM   1780 H HD13 . LEU   A 1 88  ? 22.811 3.923   11.467  1.00 22.85 ?  88  LEU   A HD13 1 
ATOM   1781 H HD21 . LEU   A 1 88  ? 22.249 5.927   13.490  1.00 24.86 ?  88  LEU   A HD21 1 
ATOM   1782 H HD22 . LEU   A 1 88  ? 21.693 4.459   13.738  1.00 24.86 ?  88  LEU   A HD22 1 
ATOM   1783 H HD23 . LEU   A 1 88  ? 22.597 5.163   14.838  1.00 24.86 ?  88  LEU   A HD23 1 
ATOM   1784 N N    . ALA   A 1 89  ? 25.688 0.976   15.570  1.00 14.94 ?  89  ALA   A N    1 
ATOM   1785 C CA   . ALA   A 1 89  ? 26.016 -0.439  15.663  1.00 14.46 ?  89  ALA   A CA   1 
ATOM   1786 C C    . ALA   A 1 89  ? 27.498 -0.518  15.984  1.00 14.75 ?  89  ALA   A C    1 
ATOM   1787 O O    . ALA   A 1 89  ? 28.220 0.474   15.869  1.00 15.76 ?  89  ALA   A O    1 
ATOM   1788 C CB   . ALA   A 1 89  ? 25.733 -1.143  14.337  1.00 14.15 ?  89  ALA   A CB   1 
ATOM   1789 H H    . ALA   A 1 89  ? 26.379 1.490   15.545  1.00 17.90 ?  89  ALA   A H    1 
ATOM   1790 H HA   . ALA   A 1 89  ? 25.504 -0.853  16.376  1.00 17.33 ?  89  ALA   A HA   1 
ATOM   1791 H HB1  . ALA   A 1 89  ? 25.967 -2.079  14.424  1.00 16.95 ?  89  ALA   A HB1  1 
ATOM   1792 H HB2  . ALA   A 1 89  ? 24.787 -1.057  14.129  1.00 16.95 ?  89  ALA   A HB2  1 
ATOM   1793 H HB3  . ALA   A 1 89  ? 26.263 -0.729  13.640  1.00 16.95 ?  89  ALA   A HB3  1 
ATOM   1794 N N    . LYS   A 1 90  ? 27.964 -1.701  16.378  1.00 15.38 ?  90  LYS   A N    1 
ATOM   1795 C CA   . LYS   A 1 90  ? 29.406 -1.857  16.535  1.00 16.28 ?  90  LYS   A CA   1 
ATOM   1796 C C    . LYS   A 1 90  ? 30.112 -1.669  15.194  1.00 15.57 ?  90  LYS   A C    1 
ATOM   1797 O O    . LYS   A 1 90  ? 31.051 -0.865  15.071  1.00 16.83 ?  90  LYS   A O    1 
ATOM   1798 C CB   . LYS   A 1 90  ? 29.738 -3.215  17.154  1.00 18.93 ?  90  LYS   A CB   1 
ATOM   1799 C CG   . LYS   A 1 90  ? 31.212 -3.363  17.507  1.00 24.35 ?  90  LYS   A CG   1 
ATOM   1800 C CD   . LYS   A 1 90  ? 31.447 -4.598  18.360  1.00 29.24 ?  90  LYS   A CD   1 
ATOM   1801 C CE   . LYS   A 1 90  ? 32.840 -4.607  18.968  1.00 32.85 ?  90  LYS   A CE   1 
ATOM   1802 N NZ   . LYS   A 1 90  ? 33.905 -4.813  17.951  1.00 36.57 ?  90  LYS   A NZ   1 
ATOM   1803 H H    . LYS   A 1 90  ? 27.484 -2.389  16.553  1.00 18.43 ?  90  LYS   A H    1 
ATOM   1804 H HA   . LYS   A 1 90  ? 29.727 -1.169  17.135  1.00 19.51 ?  90  LYS   A HA   1 
ATOM   1805 H HB2  . LYS   A 1 90  ? 29.219 -3.322  17.969  1.00 22.69 ?  90  LYS   A HB2  1 
ATOM   1806 H HB3  . LYS   A 1 90  ? 29.506 -3.914  16.523  1.00 22.69 ?  90  LYS   A HB3  1 
ATOM   1807 H HG2  . LYS   A 1 90  ? 31.730 -3.450  16.692  1.00 29.20 ?  90  LYS   A HG2  1 
ATOM   1808 H HG3  . LYS   A 1 90  ? 31.501 -2.584  18.009  1.00 29.20 ?  90  LYS   A HG3  1 
ATOM   1809 H HD2  . LYS   A 1 90  ? 30.800 -4.616  19.084  1.00 35.06 ?  90  LYS   A HD2  1 
ATOM   1810 H HD3  . LYS   A 1 90  ? 31.352 -5.391  17.809  1.00 35.06 ?  90  LYS   A HD3  1 
ATOM   1811 H HE2  . LYS   A 1 90  ? 33.002 -3.754  19.403  1.00 39.39 ?  90  LYS   A HE2  1 
ATOM   1812 H HE3  . LYS   A 1 90  ? 32.900 -5.326  19.617  1.00 39.39 ?  90  LYS   A HE3  1 
ATOM   1813 H HZ1  . LYS   A 1 90  ? 34.705 -4.811  18.343  1.00 43.86 ?  90  LYS   A HZ1  1 
ATOM   1814 H HZ2  . LYS   A 1 90  ? 33.787 -5.594  17.541  1.00 43.86 ?  90  LYS   A HZ2  1 
ATOM   1815 H HZ3  . LYS   A 1 90  ? 33.879 -4.161  17.346  1.00 43.86 ?  90  LYS   A HZ3  1 
ATOM   1816 N N    . HIS   A 1 91  ? 29.644 -2.380  14.169  1.00 13.72 ?  91  HIS   A N    1 
ATOM   1817 C CA   . HIS   A 1 91  ? 30.227 -2.364  12.843  1.00 13.04 ?  91  HIS   A CA   1 
ATOM   1818 C C    . HIS   A 1 91  ? 29.151 -2.084  11.812  1.00 11.51 ?  91  HIS   A C    1 
ATOM   1819 O O    . HIS   A 1 91  ? 27.985 -2.443  11.996  1.00 12.22 ?  91  HIS   A O    1 
ATOM   1820 C CB   . HIS   A 1 91  ? 30.819 -3.735  12.490  1.00 15.74 ?  91  HIS   A CB   1 
ATOM   1821 C CG   . HIS   A 1 91  ? 31.794 -4.255  13.497  1.00 20.11 ?  91  HIS   A CG   1 
ATOM   1822 N ND1  . HIS   A 1 91  ? 33.072 -3.757  13.620  1.00 22.41 ?  91  HIS   A ND1  1 
ATOM   1823 C CD2  . HIS   A 1 91  ? 31.683 -5.238  14.422  1.00 22.15 ?  91  HIS   A CD2  1 
ATOM   1824 C CE1  . HIS   A 1 91  ? 33.707 -4.408  14.579  1.00 23.30 ?  91  HIS   A CE1  1 
ATOM   1825 N NE2  . HIS   A 1 91  ? 32.885 -5.313  15.081  1.00 23.37 ?  91  HIS   A NE2  1 
ATOM   1826 H H    . HIS   A 1 91  ? 28.961 -2.910  14.232  1.00 16.44 ?  91  HIS   A H    1 
ATOM   1827 H HA   . HIS   A 1 91  ? 30.918 -1.692  12.783  1.00 15.62 ?  91  HIS   A HA   1 
ATOM   1828 H HB2  . HIS   A 1 91  ? 30.096 -4.383  12.422  1.00 18.86 ?  91  HIS   A HB2  1 
ATOM   1829 H HB3  . HIS   A 1 91  ? 31.279 -3.670  11.640  1.00 18.86 ?  91  HIS   A HB3  1 
ATOM   1830 H HD1  . HIS   A 1 91  ? 33.405 -3.121  13.144  1.00 26.87 ?  91  HIS   A HD1  1 
ATOM   1831 H HD2  . HIS   A 1 91  ? 30.939 -5.766  14.583  1.00 26.55 ?  91  HIS   A HD2  1 
ATOM   1832 H HE1  . HIS   A 1 91  ? 34.585 -4.250  14.852  1.00 27.93 ?  91  HIS   A HE1  1 
ATOM   1833 N N    . CYS   A 1 92  ? 29.565 -1.487  10.701  1.00 11.48 ?  92  CYS   A N    1 
ATOM   1834 C CA   . CYS   A 1 92  ? 28.735 -1.402  9.508   1.00 11.29 ?  92  CYS   A CA   1 
ATOM   1835 C C    . CYS   A 1 92  ? 29.387 -2.221  8.403   1.00 11.00 ?  92  CYS   A C    1 
ATOM   1836 O O    . CYS   A 1 92  ? 30.546 -1.972  8.038   1.00 11.54 ?  92  CYS   A O    1 
ATOM   1837 C CB   . CYS   A 1 92  ? 28.532 0.045   9.047   1.00 11.49 ?  92  CYS   A CB   1 
ATOM   1838 S SG   . CYS   A 1 92  ? 27.522 0.157   7.535   1.00 11.35 ?  92  CYS   A SG   1 
ATOM   1839 H H    . CYS   A 1 92  ? 30.337 -1.111  10.614  1.00 13.75 ?  92  CYS   A H    1 
ATOM   1840 H HA   . CYS   A 1 92  ? 27.864 -1.780  9.697   1.00 13.52 ?  92  CYS   A HA   1 
ATOM   1841 H HB2  . CYS   A 1 92  ? 28.081 0.545   9.745   1.00 13.76 ?  92  CYS   A HB2  1 
ATOM   1842 H HB3  . CYS   A 1 92  ? 29.396 0.446   8.857   1.00 13.76 ?  92  CYS   A HB3  1 
ATOM   1843 H HG   . CYS   A 1 92  ? 27.393 1.308   7.239   1.00 13.59 ?  92  CYS   A HG   1 
ATOM   1844 N N    . LEU   A 1 93  ? 28.647 -3.200  7.888   1.00 10.62 ?  93  LEU   A N    1 
ATOM   1845 C CA   . LEU   A 1 93  ? 29.053 -3.953  6.708   1.00 10.56 ?  93  LEU   A CA   1 
ATOM   1846 C C    . LEU   A 1 93  ? 28.463 -3.259  5.486   1.00 9.88  ?  93  LEU   A C    1 
ATOM   1847 O O    . LEU   A 1 93  ? 27.247 -3.309  5.256   1.00 9.98  ?  93  LEU   A O    1 
ATOM   1848 C CB   . LEU   A 1 93  ? 28.574 -5.401  6.810   1.00 11.07 ?  93  LEU   A CB   1 
ATOM   1849 C CG   . LEU   A 1 93  ? 28.954 -6.306  5.638   1.00 11.28 ?  93  LEU   A CG   1 
ATOM   1850 C CD1  . LEU   A 1 93  ? 30.460 -6.568  5.616   1.00 12.48 ?  93  LEU   A CD1  1 
ATOM   1851 C CD2  . LEU   A 1 93  ? 28.175 -7.625  5.675   1.00 11.95 ?  93  LEU   A CD2  1 
ATOM   1852 H H    . LEU   A 1 93  ? 27.891 -3.448  8.217   1.00 12.72 ?  93  LEU   A H    1 
ATOM   1853 H HA   . LEU   A 1 93  ? 30.016 -3.943  6.636   1.00 12.64 ?  93  LEU   A HA   1 
ATOM   1854 H HB2  . LEU   A 1 93  ? 28.959 -5.790  7.615   1.00 13.25 ?  93  LEU   A HB2  1 
ATOM   1855 H HB3  . LEU   A 1 93  ? 27.611 -5.405  6.878   1.00 13.25 ?  93  LEU   A HB3  1 
ATOM   1856 H HG   . LEU   A 1 93  ? 28.735 -5.857  4.813   1.00 13.51 ?  93  LEU   A HG   1 
ATOM   1857 H HD11 . LEU   A 1 93  ? 30.669 -7.175  4.890   1.00 14.95 ?  93  LEU   A HD11 1 
ATOM   1858 H HD12 . LEU   A 1 93  ? 30.931 -5.729  5.493   1.00 14.95 ?  93  LEU   A HD12 1 
ATOM   1859 H HD13 . LEU   A 1 93  ? 30.727 -6.970  6.464   1.00 14.95 ?  93  LEU   A HD13 1 
ATOM   1860 H HD21 . LEU   A 1 93  ? 28.447 -8.172  4.918   1.00 14.31 ?  93  LEU   A HD21 1 
ATOM   1861 H HD22 . LEU   A 1 93  ? 28.372 -8.089  6.503   1.00 14.31 ?  93  LEU   A HD22 1 
ATOM   1862 H HD23 . LEU   A 1 93  ? 27.229 -7.430  5.618   1.00 14.31 ?  93  LEU   A HD23 1 
ATOM   1863 N N    . HIS   A 1 94  ? 29.318 -2.570  4.728   1.00 9.66  ?  94  HIS   A N    1 
ATOM   1864 C CA   . HIS   A 1 94  ? 28.903 -1.892  3.504   1.00 10.14 ?  94  HIS   A CA   1 
ATOM   1865 C C    . HIS   A 1 94  ? 28.914 -2.919  2.388   1.00 9.83  ?  94  HIS   A C    1 
ATOM   1866 O O    . HIS   A 1 94  ? 29.978 -3.434  2.043   1.00 11.13 ?  94  HIS   A O    1 
ATOM   1867 C CB   . HIS   A 1 94  ? 29.869 -0.752  3.181   1.00 10.12 ?  94  HIS   A CB   1 
ATOM   1868 C CG   . HIS   A 1 94  ? 29.853 0.342   4.196   1.00 9.79  ?  94  HIS   A CG   1 
ATOM   1869 N ND1  . HIS   A 1 94  ? 28.984 1.411   4.129   1.00 10.28 ?  94  HIS   A ND1  1 
ATOM   1870 C CD2  . HIS   A 1 94  ? 30.581 0.505   5.325   1.00 10.84 ?  94  HIS   A CD2  1 
ATOM   1871 C CE1  . HIS   A 1 94  ? 29.192 2.187   5.176   1.00 10.50 ?  94  HIS   A CE1  1 
ATOM   1872 N NE2  . HIS   A 1 94  ? 30.154 1.661   5.915   1.00 10.61 ?  94  HIS   A NE2  1 
ATOM   1873 H H    . HIS   A 1 94  ? 30.157 -2.483  4.898   1.00 11.56 ?  94  HIS   A H    1 
ATOM   1874 H HA   . HIS   A 1 94  ? 28.002 -1.538  3.601   1.00 12.15 ?  94  HIS   A HA   1 
ATOM   1875 H HB2  . HIS   A 1 94  ? 30.762 -1.102  3.133   1.00 12.11 ?  94  HIS   A HB2  1 
ATOM   1876 H HB3  . HIS   A 1 94  ? 29.613 -0.360  2.326   1.00 12.11 ?  94  HIS   A HB3  1 
ATOM   1877 H HD2  . HIS   A 1 94  ? 31.246 -0.057  5.638   1.00 12.98 ?  94  HIS   A HD2  1 
ATOM   1878 H HE1  . HIS   A 1 94  ? 28.731 2.978   5.365   1.00 12.58 ?  94  HIS   A HE1  1 
ATOM   1879 H HE2  . HIS   A 1 94  ? 30.462 2.002   6.644   1.00 12.71 ?  94  HIS   A HE2  1 
ATOM   1880 N N    . VAL   A 1 95  ? 27.745 -3.244  1.838   1.00 9.41  ?  95  VAL   A N    1 
ATOM   1881 C CA   . VAL   A 1 95  ? 27.605 -4.275  0.813   1.00 9.57  ?  95  VAL   A CA   1 
ATOM   1882 C C    . VAL   A 1 95  ? 27.065 -3.635  -0.454  1.00 9.36  ?  95  VAL   A C    1 
ATOM   1883 O O    . VAL   A 1 95  ? 26.068 -2.903  -0.405  1.00 10.27 ?  95  VAL   A O    1 
ATOM   1884 C CB   . VAL   A 1 95  ? 26.676 -5.421  1.259   1.00 10.25 ?  95  VAL   A CB   1 
ATOM   1885 C CG1  . VAL   A 1 95  ? 26.561 -6.457  0.150   1.00 10.79 ?  95  VAL   A CG1  1 
ATOM   1886 C CG2  . VAL   A 1 95  ? 27.177 -6.048  2.541   1.00 10.76 ?  95  VAL   A CG2  1 
ATOM   1887 H H    . VAL   A 1 95  ? 26.996 -2.875  2.049   1.00 11.27 ?  95  VAL   A H    1 
ATOM   1888 H HA   . VAL   A 1 95  ? 28.473 -4.654  0.612   1.00 11.45 ?  95  VAL   A HA   1 
ATOM   1889 H HB   . VAL   A 1 95  ? 25.790 -5.068  1.425   1.00 12.28 ?  95  VAL   A HB   1 
ATOM   1890 H HG11 . VAL   A 1 95  ? 26.164 -7.272  0.511   1.00 12.92 ?  95  VAL   A HG11 1 
ATOM   1891 H HG12 . VAL   A 1 95  ? 26.000 -6.114  -0.563  1.00 12.92 ?  95  VAL   A HG12 1 
ATOM   1892 H HG13 . VAL   A 1 95  ? 27.447 -6.660  -0.197  1.00 12.92 ?  95  VAL   A HG13 1 
ATOM   1893 H HG21 . VAL   A 1 95  ? 26.617 -6.812  2.760   1.00 12.89 ?  95  VAL   A HG21 1 
ATOM   1894 H HG22 . VAL   A 1 95  ? 28.094 -6.338  2.415   1.00 12.89 ?  95  VAL   A HG22 1 
ATOM   1895 H HG23 . VAL   A 1 95  ? 27.130 -5.391  3.251   1.00 12.89 ?  95  VAL   A HG23 1 
ATOM   1896 N N    . VAL   A 1 96  ? 27.703 -3.921  -1.587  1.00 9.58  ?  96  VAL   A N    1 
ATOM   1897 C CA   . VAL   A 1 96  ? 27.302 -3.363  -2.873  1.00 10.33 ?  96  VAL   A CA   1 
ATOM   1898 C C    . VAL   A 1 96  ? 26.488 -4.406  -3.631  1.00 10.52 ?  96  VAL   A C    1 
ATOM   1899 O O    . VAL   A 1 96  ? 27.041 -5.344  -4.211  1.00 11.34 ?  96  VAL   A O    1 
ATOM   1900 C CB   . VAL   A 1 96  ? 28.500 -2.891  -3.701  1.00 10.85 ?  96  VAL   A CB   1 
ATOM   1901 C CG1  . VAL   A 1 96  ? 27.998 -2.245  -4.979  1.00 10.86 ?  96  VAL   A CG1  1 
ATOM   1902 C CG2  . VAL   A 1 96  ? 29.380 -1.934  -2.908  1.00 11.11 ?  96  VAL   A CG2  1 
ATOM   1903 H H    . VAL   A 1 96  ? 28.391 -4.441  -1.635  1.00 11.47 ?  96  VAL   A H    1 
ATOM   1904 H HA   . VAL   A 1 96  ? 26.732 -2.597  -2.717  1.00 12.37 ?  96  VAL   A HA   1 
ATOM   1905 H HB   . VAL   A 1 96  ? 29.039 -3.655  -3.945  1.00 13.00 ?  96  VAL   A HB   1 
ATOM   1906 H HG11 . VAL   A 1 96  ? 28.739 -1.778  -5.402  1.00 13.01 ?  96  VAL   A HG11 1 
ATOM   1907 H HG12 . VAL   A 1 96  ? 27.658 -2.930  -5.568  1.00 13.01 ?  96  VAL   A HG12 1 
ATOM   1908 H HG13 . VAL   A 1 96  ? 27.298 -1.611  -4.757  1.00 13.01 ?  96  VAL   A HG13 1 
ATOM   1909 H HG21 . VAL   A 1 96  ? 30.087 -1.602  -3.479  1.00 13.30 ?  96  VAL   A HG21 1 
ATOM   1910 H HG22 . VAL   A 1 96  ? 28.836 -1.192  -2.589  1.00 13.30 ?  96  VAL   A HG22 1 
ATOM   1911 H HG23 . VAL   A 1 96  ? 29.761 -2.407  -2.149  1.00 13.30 ?  96  VAL   A HG23 1 
ATOM   1912 N N    . GLY   A 1 97  ? 25.171 -4.241  -3.656  1.00 10.64 ?  97  GLY   A N    1 
ATOM   1913 C CA   . GLY   A 1 97  ? 24.352 -4.987  -4.577  1.00 11.04 ?  97  GLY   A CA   1 
ATOM   1914 C C    . GLY   A 1 97  ? 24.366 -4.330  -5.945  1.00 11.26 ?  97  GLY   A C    1 
ATOM   1915 O O    . GLY   A 1 97  ? 24.643 -3.132  -6.078  1.00 12.07 ?  97  GLY   A O    1 
ATOM   1916 H H    . GLY   A 1 97  ? 24.730 -3.697  -3.145  1.00 12.74 ?  97  GLY   A H    1 
ATOM   1917 H HA2  . GLY   A 1 97  ? 24.698 -5.893  -4.648  1.00 13.22 ?  97  GLY   A HA2  1 
ATOM   1918 H HA3  . GLY   A 1 97  ? 23.439 -5.032  -4.242  1.00 13.22 ?  97  GLY   A HA3  1 
ATOM   1919 N N    . PRO   A 1 98  ? 24.048 -5.086  -6.990  1.00 11.15 ?  98  PRO   A N    1 
ATOM   1920 C CA   . PRO   A 1 98  ? 23.945 -4.476  -8.316  1.00 12.46 ?  98  PRO   A CA   1 
ATOM   1921 C C    . PRO   A 1 98  ? 22.827 -3.445  -8.374  1.00 13.09 ?  98  PRO   A C    1 
ATOM   1922 O O    . PRO   A 1 98  ? 21.746 -3.628  -7.806  1.00 12.80 ?  98  PRO   A O    1 
ATOM   1923 C CB   . PRO   A 1 98  ? 23.656 -5.669  -9.234  1.00 12.66 ?  98  PRO   A CB   1 
ATOM   1924 C CG   . PRO   A 1 98  ? 23.013 -6.681  -8.347  1.00 12.85 ?  98  PRO   A CG   1 
ATOM   1925 C CD   . PRO   A 1 98  ? 23.736 -6.526  -7.023  1.00 11.95 ?  98  PRO   A CD   1 
ATOM   1926 H HA   . PRO   A 1 98  ? 24.790 -4.063  -8.560  1.00 14.92 ?  98  PRO   A HA   1 
ATOM   1927 H HB2  . PRO   A 1 98  ? 23.051 -5.389  -9.940  1.00 15.16 ?  98  PRO   A HB2  1 
ATOM   1928 H HB3  . PRO   A 1 98  ? 24.486 -6.005  -9.601  1.00 15.16 ?  98  PRO   A HB3  1 
ATOM   1929 H HG2  . PRO   A 1 98  ? 22.068 -6.474  -8.250  1.00 15.39 ?  98  PRO   A HG2  1 
ATOM   1930 H HG3  . PRO   A 1 98  ? 23.141 -7.564  -8.714  1.00 15.39 ?  98  PRO   A HG3  1 
ATOM   1931 H HD2  . PRO   A 1 98  ? 23.152 -6.773  -6.286  1.00 14.32 ?  98  PRO   A HD2  1 
ATOM   1932 H HD3  . PRO   A 1 98  ? 24.552 -7.052  -7.018  1.00 14.32 ?  98  PRO   A HD3  1 
ATOM   1933 N N    A ASN   A 1 99  ? 23.100 -2.332  -9.063  0.66 13.95 ?  99  ASN   A N    1 
ATOM   1934 N N    B ASN   A 1 99  ? 23.111 -2.356  -9.074  0.34 13.89 ?  99  ASN   A N    1 
ATOM   1935 C CA   A ASN   A 1 99  ? 22.122 -1.261  -9.269  0.66 15.02 ?  99  ASN   A CA   1 
ATOM   1936 C CA   B ASN   A 1 99  ? 22.139 -1.315  -9.353  0.34 15.04 ?  99  ASN   A CA   1 
ATOM   1937 C C    A ASN   A 1 99  ? 21.563 -1.399  -10.682 0.66 16.10 ?  99  ASN   A C    1 
ATOM   1938 C C    B ASN   A 1 99  ? 21.603 -1.573  -10.755 0.34 16.15 ?  99  ASN   A C    1 
ATOM   1939 O O    A ASN   A 1 99  ? 22.208 -1.014  -11.664 0.66 17.42 ?  99  ASN   A O    1 
ATOM   1940 O O    B ASN   A 1 99  ? 22.361 -1.535  -11.732 0.34 16.12 ?  99  ASN   A O    1 
ATOM   1941 C CB   A ASN   A 1 99  ? 22.756 0.111   -9.050  0.66 15.97 ?  99  ASN   A CB   1 
ATOM   1942 C CB   B ASN   A 1 99  ? 22.805 0.058   -9.255  0.34 16.17 ?  99  ASN   A CB   1 
ATOM   1943 C CG   A ASN   A 1 99  ? 21.727 1.245   -9.034  0.66 17.21 ?  99  ASN   A CG   1 
ATOM   1944 C CG   B ASN   A 1 99  ? 21.809 1.199   -9.299  0.34 17.09 ?  99  ASN   A CG   1 
ATOM   1945 O OD1  A ASN   A 1 99  ? 20.730 1.199   -9.753  0.66 18.14 ?  99  ASN   A OD1  1 
ATOM   1946 O OD1  B ASN   A 1 99  ? 20.825 1.147   -10.034 0.34 17.06 ?  99  ASN   A OD1  1 
ATOM   1947 N ND2  A ASN   A 1 99  ? 21.977 2.270   -8.217  0.66 17.61 ?  99  ASN   A ND2  1 
ATOM   1948 N ND2  B ASN   A 1 99  ? 22.064 2.244   -8.509  0.34 17.54 ?  99  ASN   A ND2  1 
ATOM   1949 H H    A ASN   A 1 99  ? 23.869 -2.167  -9.410  0.66 16.71 ?  99  ASN   A H    1 
ATOM   1950 H H    B ASN   A 1 99  ? 23.884 -2.198  -9.416  0.34 16.64 ?  99  ASN   A H    1 
ATOM   1951 H HA   A ASN   A 1 99  ? 21.394 -1.367  -8.629  0.66 18.00 ?  99  ASN   A HA   1 
ATOM   1952 H HA   B ASN   A 1 99  ? 21.408 -1.356  -8.714  0.34 18.02 ?  99  ASN   A HA   1 
ATOM   1953 H HB2  A ASN   A 1 99  ? 23.226 0.120   -8.205  0.66 19.13 ?  99  ASN   A HB2  1 
ATOM   1954 H HB2  B ASN   A 1 99  ? 23.292 0.115   -8.414  0.34 19.38 ?  99  ASN   A HB2  1 
ATOM   1955 H HB3  A ASN   A 1 99  ? 23.379 0.283   -9.778  0.66 19.13 ?  99  ASN   A HB3  1 
ATOM   1956 H HB3  B ASN   A 1 99  ? 23.417 0.167   -9.997  0.34 19.38 ?  99  ASN   A HB3  1 
ATOM   1957 H HD21 A ASN   A 1 99  ? 21.430 2.934   -8.174  0.66 21.10 ?  99  ASN   A HD21 1 
ATOM   1958 H HD21 B ASN   A 1 99  ? 21.531 2.917   -8.494  0.34 21.02 ?  99  ASN   A HD21 1 
ATOM   1959 H HD22 A ASN   A 1 99  ? 22.687 2.267   -7.731  0.66 21.10 ?  99  ASN   A HD22 1 
ATOM   1960 H HD22 B ASN   A 1 99  ? 22.768 2.244   -8.009  0.34 21.02 ?  99  ASN   A HD22 1 
ATOM   1961 N N    A VAL   A 1 100 ? 20.343 -1.940  -10.770 0.66 17.41 ?  100 VAL   A N    1 
ATOM   1962 N N    B VAL   A 1 100 ? 20.311 -1.891  -10.843 0.34 17.57 ?  100 VAL   A N    1 
ATOM   1963 C CA   A VAL   A 1 100 ? 19.706 -2.178  -12.061 0.66 19.86 ?  100 VAL   A CA   1 
ATOM   1964 C CA   B VAL   A 1 100 ? 19.699 -2.125  -12.146 0.34 19.83 ?  100 VAL   A CA   1 
ATOM   1965 C C    A VAL   A 1 100 ? 19.561 -0.881  -12.845 0.66 20.34 ?  100 VAL   A C    1 
ATOM   1966 C C    B VAL   A 1 100 ? 19.675 -0.842  -12.960 0.34 21.19 ?  100 VAL   A C    1 
ATOM   1967 O O    A VAL   A 1 100 ? 19.622 -0.882  -14.081 0.66 21.59 ?  100 VAL   A O    1 
ATOM   1968 O O    B VAL   A 1 100 ? 19.819 -0.869  -14.188 0.34 22.08 ?  100 VAL   A O    1 
ATOM   1969 C CB   A VAL   A 1 100 ? 18.359 -2.905  -11.860 0.66 21.32 ?  100 VAL   A CB   1 
ATOM   1970 C CB   B VAL   A 1 100 ? 18.289 -2.717  -11.968 0.34 20.64 ?  100 VAL   A CB   1 
ATOM   1971 C CG1  A VAL   A 1 100 ? 17.648 -3.114  -13.190 0.66 22.31 ?  100 VAL   A CG1  1 
ATOM   1972 C CG1  B VAL   A 1 100 ? 17.568 -2.792  -13.308 0.34 21.38 ?  100 VAL   A CG1  1 
ATOM   1973 C CG2  A VAL   A 1 100 ? 18.586 -4.240  -11.165 0.66 22.17 ?  100 VAL   A CG2  1 
ATOM   1974 C CG2  B VAL   A 1 100 ? 18.379 -4.086  -11.322 0.34 21.06 ?  100 VAL   A CG2  1 
ATOM   1975 H H    A VAL   A 1 100 ? 19.858 -2.169  -10.090 0.66 20.86 ?  100 VAL   A H    1 
ATOM   1976 H H    B VAL   A 1 100 ? 19.777 -1.973  -10.172 0.34 21.06 ?  100 VAL   A H    1 
ATOM   1977 H HA   A VAL   A 1 100 ? 20.273 -2.764  -12.578 0.66 23.80 ?  100 VAL   A HA   1 
ATOM   1978 H HA   B VAL   A 1 100 ? 20.234 -2.776  -12.626 0.34 23.77 ?  100 VAL   A HA   1 
ATOM   1979 H HB   A VAL   A 1 100 ? 17.782 -2.367  -11.295 0.66 25.56 ?  100 VAL   A HB   1 
ATOM   1980 H HB   B VAL   A 1 100 ? 17.771 -2.143  -11.381 0.34 24.74 ?  100 VAL   A HB   1 
ATOM   1981 H HG11 A VAL   A 1 100 ? 16.903 -3.723  -13.057 0.66 26.75 ?  100 VAL   A HG11 1 
ATOM   1982 H HG11 B VAL   A 1 100 ? 16.799 -3.376  -13.221 0.34 25.63 ?  100 VAL   A HG11 1 
ATOM   1983 H HG12 A VAL   A 1 100 ? 17.321 -2.261  -13.514 0.66 26.75 ?  100 VAL   A HG12 1 
ATOM   1984 H HG12 B VAL   A 1 100 ? 17.278 -1.902  -13.564 0.34 25.63 ?  100 VAL   A HG12 1 
ATOM   1985 H HG13 A VAL   A 1 100 ? 18.274 -3.495  -13.826 0.66 26.75 ?  100 VAL   A HG13 1 
ATOM   1986 H HG13 B VAL   A 1 100 ? 18.179 -3.147  -13.973 0.34 25.63 ?  100 VAL   A HG13 1 
ATOM   1987 H HG21 A VAL   A 1 100 ? 17.744 -4.723  -11.122 0.66 26.58 ?  100 VAL   A HG21 1 
ATOM   1988 H HG21 B VAL   A 1 100 ? 17.487 -4.458  -11.242 0.34 25.24 ?  100 VAL   A HG21 1 
ATOM   1989 H HG22 A VAL   A 1 100 ? 19.234 -4.753  -11.672 0.66 26.58 ?  100 VAL   A HG22 1 
ATOM   1990 H HG22 B VAL   A 1 100 ? 18.929 -4.658  -11.879 0.34 25.24 ?  100 VAL   A HG22 1 
ATOM   1991 H HG23 A VAL   A 1 100 ? 18.919 -4.078  -10.269 0.66 26.58 ?  100 VAL   A HG23 1 
ATOM   1992 H HG23 B VAL   A 1 100 ? 18.780 -3.994  -10.443 0.34 25.24 ?  100 VAL   A HG23 1 
ATOM   1993 N N    A ASN   A 1 101 ? 19.367 0.243   -12.155 0.66 21.57 ?  101 ASN   A N    1 
ATOM   1994 N N    B ASN   A 1 101 ? 19.494 0.298   -12.296 0.34 22.16 ?  101 ASN   A N    1 
ATOM   1995 C CA   A ASN   A 1 101 ? 19.300 1.527   -12.844 0.66 23.05 ?  101 ASN   A CA   1 
ATOM   1996 C CA   B ASN   A 1 101 ? 19.415 1.569   -13.003 0.34 23.25 ?  101 ASN   A CA   1 
ATOM   1997 C C    A ASN   A 1 101 ? 20.651 1.968   -13.408 0.66 25.15 ?  101 ASN   A C    1 
ATOM   1998 C C    B ASN   A 1 101 ? 20.766 2.022   -13.540 0.34 24.48 ?  101 ASN   A C    1 
ATOM   1999 O O    A ASN   A 1 101 ? 20.716 3.025   -14.049 0.66 27.43 ?  101 ASN   A O    1 
ATOM   2000 O O    B ASN   A 1 101 ? 20.806 2.895   -14.414 0.34 25.14 ?  101 ASN   A O    1 
ATOM   2001 C CB   A ASN   A 1 101 ? 18.694 2.583   -11.915 0.66 22.12 ?  101 ASN   A CB   1 
ATOM   2002 C CB   B ASN   A 1 101 ? 18.810 2.626   -12.083 0.34 23.23 ?  101 ASN   A CB   1 
ATOM   2003 C CG   A ASN   A 1 101 ? 17.301 2.197   -11.428 0.66 21.09 ?  101 ASN   A CG   1 
ATOM   2004 C CG   B ASN   A 1 101 ? 17.476 2.192   -11.505 0.34 22.87 ?  101 ASN   A CG   1 
ATOM   2005 O OD1  A ASN   A 1 101 ? 16.481 1.682   -12.194 0.66 21.20 ?  101 ASN   A OD1  1 
ATOM   2006 O OD1  B ASN   A 1 101 ? 16.647 1.598   -12.198 0.34 22.74 ?  101 ASN   A OD1  1 
ATOM   2007 N ND2  A ASN   A 1 101 ? 17.034 2.427   -10.146 0.66 21.01 ?  101 ASN   A ND2  1 
ATOM   2008 N ND2  B ASN   A 1 101 ? 17.267 2.472   -10.228 0.34 23.13 ?  101 ASN   A ND2  1 
ATOM   2009 H H    A ASN   A 1 101 ? 19.257 0.285   -11.301 0.66 25.86 ?  101 ASN   A H    1 
ATOM   2010 H H    B ASN   A 1 101 ? 19.410 0.353   -11.444 0.34 26.57 ?  101 ASN   A H    1 
ATOM   2011 H HA   A ASN   A 1 101 ? 18.695 1.433   -13.592 0.66 27.63 ?  101 ASN   A HA   1 
ATOM   2012 H HA   B ASN   A 1 101 ? 18.826 1.462   -13.761 0.34 27.87 ?  101 ASN   A HA   1 
ATOM   2013 H HB2  A ASN   A 1 101 ? 19.264 2.697   -11.140 0.66 26.52 ?  101 ASN   A HB2  1 
ATOM   2014 H HB2  B ASN   A 1 101 ? 19.419 2.792   -11.347 0.34 27.84 ?  101 ASN   A HB2  1 
ATOM   2015 H HB3  A ASN   A 1 101 ? 18.623 3.425   -12.399 0.66 26.52 ?  101 ASN   A HB3  1 
ATOM   2016 H HB3  B ASN   A 1 101 ? 18.670 3.439   -12.591 0.34 27.84 ?  101 ASN   A HB3  1 
ATOM   2017 H HD21 A ASN   A 1 101 ? 16.261 2.229   -9.824  0.66 25.19 ?  101 ASN   A HD21 1 
ATOM   2018 H HD21 B ASN   A 1 101 ? 16.528 2.244   -9.854  0.34 27.73 ?  101 ASN   A HD21 1 
ATOM   2019 H HD22 A ASN   A 1 101 ? 17.632 2.781   -9.637  0.66 25.19 ?  101 ASN   A HD22 1 
ATOM   2020 H HD22 B ASN   A 1 101 ? 17.870 2.885   -9.776  0.34 27.73 ?  101 ASN   A HD22 1 
ATOM   2021 N N    A LYS   A 1 102 ? 21.714 1.182   -13.197 0.66 26.09 ?  102 LYS   A N    1 
ATOM   2022 N N    B LYS   A 1 102 ? 21.866 1.452   -13.048 0.34 24.89 ?  102 LYS   A N    1 
ATOM   2023 C CA   A LYS   A 1 102 ? 23.002 1.364   -13.857 0.66 26.57 ?  102 LYS   A CA   1 
ATOM   2024 C CA   B LYS   A 1 102 ? 23.188 1.714   -13.600 0.34 25.39 ?  102 LYS   A CA   1 
ATOM   2025 C C    A LYS   A 1 102 ? 23.304 0.255   -14.859 0.66 26.48 ?  102 LYS   A C    1 
ATOM   2026 C C    B LYS   A 1 102 ? 23.635 0.651   -14.596 0.34 25.84 ?  102 LYS   A C    1 
ATOM   2027 O O    A LYS   A 1 102 ? 24.390 0.250   -15.447 0.66 27.00 ?  102 LYS   A O    1 
ATOM   2028 O O    B LYS   A 1 102 ? 24.728 0.771   -15.156 0.34 26.02 ?  102 LYS   A O    1 
ATOM   2029 C CB   A LYS   A 1 102 ? 24.134 1.405   -12.821 0.66 27.66 ?  102 LYS   A CB   1 
ATOM   2030 C CB   B LYS   A 1 102 ? 24.226 1.864   -12.479 0.34 25.83 ?  102 LYS   A CB   1 
ATOM   2031 C CG   A LYS   A 1 102 ? 24.058 2.543   -11.819 0.66 28.50 ?  102 LYS   A CG   1 
ATOM   2032 C CG   B LYS   A 1 102 ? 23.971 3.050   -11.557 0.34 26.39 ?  102 LYS   A CG   1 
ATOM   2033 C CD   A LYS   A 1 102 ? 25.211 2.463   -10.821 0.66 29.75 ?  102 LYS   A CD   1 
ATOM   2034 C CD   B LYS   A 1 102 ? 24.977 3.101   -10.414 0.34 27.14 ?  102 LYS   A CD   1 
ATOM   2035 C CE   A LYS   A 1 102 ? 25.161 3.595   -9.803  0.66 31.02 ?  102 LYS   A CE   1 
ATOM   2036 C CE   B LYS   A 1 102 ? 24.719 4.293   -9.503  0.34 27.76 ?  102 LYS   A CE   1 
ATOM   2037 N NZ   A LYS   A 1 102 ? 26.262 3.500   -8.797  0.66 31.37 ?  102 LYS   A NZ   1 
ATOM   2038 N NZ   B LYS   A 1 102 ? 25.654 4.336   -8.344  0.34 28.12 ?  102 LYS   A NZ   1 
ATOM   2039 H H    A LYS   A 1 102 ? 21.708 0.508   -12.659 0.66 31.28 ?  102 LYS   A H    1 
ATOM   2040 H H    B LYS   A 1 102 ? 21.871 0.903   -12.384 0.34 29.84 ?  102 LYS   A H    1 
ATOM   2041 H HA   A LYS   A 1 102 ? 22.997 2.211   -14.327 0.66 31.86 ?  102 LYS   A HA   1 
ATOM   2042 H HA   B LYS   A 1 102 ? 23.163 2.549   -14.080 0.34 30.44 ?  102 LYS   A HA   1 
ATOM   2043 H HB2  A LYS   A 1 102 ? 24.122 0.575   -12.319 0.66 33.17 ?  102 LYS   A HB2  1 
ATOM   2044 H HB2  B LYS   A 1 102 ? 24.225 1.063   -11.935 0.34 30.97 ?  102 LYS   A HB2  1 
ATOM   2045 H HB3  A LYS   A 1 102 ? 24.978 1.487   -13.290 0.66 33.17 ?  102 LYS   A HB3  1 
ATOM   2046 H HB3  B LYS   A 1 102 ? 25.103 1.989   -12.878 0.34 30.97 ?  102 LYS   A HB3  1 
ATOM   2047 H HG2  A LYS   A 1 102 ? 24.118 3.389   -12.288 0.66 34.18 ?  102 LYS   A HG2  1 
ATOM   2048 H HG2  B LYS   A 1 102 ? 24.049 3.874   -12.065 0.34 31.64 ?  102 LYS   A HG2  1 
ATOM   2049 H HG3  A LYS   A 1 102 ? 23.224 2.485   -11.328 0.66 34.18 ?  102 LYS   A HG3  1 
ATOM   2050 H HG3  B LYS   A 1 102 ? 23.083 2.974   -11.176 0.34 31.64 ?  102 LYS   A HG3  1 
ATOM   2051 H HD2  A LYS   A 1 102 ? 25.160 1.621   -10.341 0.66 35.68 ?  102 LYS   A HD2  1 
ATOM   2052 H HD2  B LYS   A 1 102 ? 24.903 2.291   -9.885  0.34 32.54 ?  102 LYS   A HD2  1 
ATOM   2053 H HD3  A LYS   A 1 102 ? 26.052 2.523   -11.300 0.66 35.68 ?  102 LYS   A HD3  1 
ATOM   2054 H HD3  B LYS   A 1 102 ? 25.873 3.184   -10.778 0.34 32.54 ?  102 LYS   A HD3  1 
ATOM   2055 H HE2  A LYS   A 1 102 ? 25.247 4.443   -10.268 0.66 37.20 ?  102 LYS   A HE2  1 
ATOM   2056 H HE2  B LYS   A 1 102 ? 24.832 5.111   -10.012 0.34 33.28 ?  102 LYS   A HE2  1 
ATOM   2057 H HE3  A LYS   A 1 102 ? 24.314 3.559   -9.330  0.66 37.20 ?  102 LYS   A HE3  1 
ATOM   2058 H HE3  B LYS   A 1 102 ? 23.814 4.238   -9.158  0.34 33.28 ?  102 LYS   A HE3  1 
ATOM   2059 H HZ1  A LYS   A 1 102 ? 26.204 4.174   -8.219  0.66 37.62 ?  102 LYS   A HZ1  1 
ATOM   2060 H HZ1  B LYS   A 1 102 ? 25.474 5.044   -7.835  0.34 33.71 ?  102 LYS   A HZ1  1 
ATOM   2061 H HZ2  A LYS   A 1 102 ? 26.202 2.732   -8.352  0.66 37.62 ?  102 LYS   A HZ2  1 
ATOM   2062 H HZ2  B LYS   A 1 102 ? 25.567 3.599   -7.855  0.34 33.71 ?  102 LYS   A HZ2  1 
ATOM   2063 H HZ3  A LYS   A 1 102 ? 27.052 3.536   -9.206  0.66 37.62 ?  102 LYS   A HZ3  1 
ATOM   2064 H HZ3  B LYS   A 1 102 ? 26.494 4.395   -8.633  0.34 33.71 ?  102 LYS   A HZ3  1 
ATOM   2065 N N    A GLY   A 1 103 ? 22.388 -0.693  -15.049 0.66 26.83 ?  103 GLY   A N    1 
ATOM   2066 N N    B GLY   A 1 103 ? 22.819 -0.374  -14.836 0.34 25.95 ?  103 GLY   A N    1 
ATOM   2067 C CA   A GLY   A 1 103 ? 22.598 -1.809  -15.954 0.66 26.67 ?  103 GLY   A CA   1 
ATOM   2068 C CA   B GLY   A 1 103 ? 23.146 -1.383  -15.822 0.34 25.67 ?  103 GLY   A CA   1 
ATOM   2069 C C    A GLY   A 1 103 ? 23.424 -2.952  -15.403 0.66 26.37 ?  103 GLY   A C    1 
ATOM   2070 C C    B GLY   A 1 103 ? 23.995 -2.525  -15.317 0.34 25.68 ?  103 GLY   A C    1 
ATOM   2071 O O    A GLY   A 1 103 ? 23.905 -3.783  -16.179 0.66 27.37 ?  103 GLY   A O    1 
ATOM   2072 O O    B GLY   A 1 103 ? 24.700 -3.156  -16.113 0.34 25.83 ?  103 GLY   A O    1 
ATOM   2073 H H    A GLY   A 1 103 ? 21.626 -0.704  -14.665 0.66 32.17 ?  103 GLY   A H    1 
ATOM   2074 H H    B GLY   A 1 103 ? 22.069 -0.508  -14.435 0.34 31.11 ?  103 GLY   A H    1 
ATOM   2075 H HA2  A GLY   A 1 103 ? 21.728 -2.164  -16.209 0.66 31.98 ?  103 GLY   A HA2  1 
ATOM   2076 H HA2  B GLY   A 1 103 ? 22.327 -1.757  -16.179 0.34 30.78 ?  103 GLY   A HA2  1 
ATOM   2077 H HA3  A GLY   A 1 103 ? 23.029 -1.482  -16.759 0.66 31.98 ?  103 GLY   A HA3  1 
ATOM   2078 H HA3  B GLY   A 1 103 ? 23.630 -0.967  -16.552 0.34 30.78 ?  103 GLY   A HA3  1 
ATOM   2079 N N    A GLU   A 1 104 ? 23.593 -3.037  -14.088 0.66 24.29 ?  104 GLU   A N    1 
ATOM   2080 N N    B GLU   A 1 104 ? 23.946 -2.820  -14.023 0.34 24.70 ?  104 GLU   A N    1 
ATOM   2081 C CA   A GLU   A 1 104 ? 24.480 -4.031  -13.501 0.66 22.76 ?  104 GLU   A CA   1 
ATOM   2082 C CA   B GLU   A 1 104 ? 24.788 -3.840  -13.419 0.34 24.47 ?  104 GLU   A CA   1 
ATOM   2083 C C    A GLU   A 1 104 ? 23.801 -5.396  -13.396 0.66 22.72 ?  104 GLU   A C    1 
ATOM   2084 C C    B GLU   A 1 104 ? 24.027 -5.156  -13.314 0.34 25.47 ?  104 GLU   A C    1 
ATOM   2085 O O    A GLU   A 1 104 ? 22.576 -5.504  -13.276 0.66 23.22 ?  104 GLU   A O    1 
ATOM   2086 O O    B GLU   A 1 104 ? 22.835 -5.176  -12.989 0.34 25.98 ?  104 GLU   A O    1 
ATOM   2087 C CB   A GLU   A 1 104 ? 24.990 -3.543  -12.142 0.66 20.98 ?  104 GLU   A CB   1 
ATOM   2088 C CB   B GLU   A 1 104 ? 25.264 -3.362  -12.046 0.34 23.30 ?  104 GLU   A CB   1 
ATOM   2089 C CG   A GLU   A 1 104 ? 25.956 -2.368  -12.305 0.66 20.04 ?  104 GLU   A CG   1 
ATOM   2090 C CG   B GLU   A 1 104 ? 25.891 -1.967  -12.120 0.34 22.46 ?  104 GLU   A CG   1 
ATOM   2091 C CD   A GLU   A 1 104 ? 26.261 -1.588  -11.035 0.66 19.32 ?  104 GLU   A CD   1 
ATOM   2092 C CD   B GLU   A 1 104 ? 26.337 -1.421  -10.774 0.34 21.54 ?  104 GLU   A CD   1 
ATOM   2093 O OE1  A GLU   A 1 104 ? 25.707 -1.899  -9.959  0.66 18.64 ?  104 GLU   A OE1  1 
ATOM   2094 O OE1  B GLU   A 1 104 ? 25.697 -1.737  -9.750  0.34 20.35 ?  104 GLU   A OE1  1 
ATOM   2095 O OE2  A GLU   A 1 104 ? 27.066 -0.631  -11.141 0.66 20.20 -1 104 GLU   A OE2  1 
ATOM   2096 O OE2  B GLU   A 1 104 ? 27.331 -0.664  -10.745 0.34 22.43 -1 104 GLU   A OE2  1 
ATOM   2097 H H    A GLU   A 1 104 ? 23.202 -2.530  -13.517 0.66 29.12 ?  104 GLU   A H    1 
ATOM   2098 H H    B GLU   A 1 104 ? 23.424 -2.430  -13.458 0.34 29.61 ?  104 GLU   A H    1 
ATOM   2099 H HA   A GLU   A 1 104 ? 25.247 -4.133  -14.084 0.66 27.28 ?  104 GLU   A HA   1 
ATOM   2100 H HA   B GLU   A 1 104 ? 25.567 -3.989  -13.977 0.34 29.34 ?  104 GLU   A HA   1 
ATOM   2101 H HB2  A GLU   A 1 104 ? 24.237 -3.253  -11.606 0.66 25.15 ?  104 GLU   A HB2  1 
ATOM   2102 H HB2  B GLU   A 1 104 ? 24.508 -3.325  -11.440 0.34 27.94 ?  104 GLU   A HB2  1 
ATOM   2103 H HB3  A GLU   A 1 104 ? 25.459 -4.269  -11.704 0.66 25.15 ?  104 GLU   A HB3  1 
ATOM   2104 H HB3  B GLU   A 1 104 ? 25.934 -3.978  -11.707 0.34 27.94 ?  104 GLU   A HB3  1 
ATOM   2105 H HG2  A GLU   A 1 104 ? 26.793 -2.708  -12.651 0.66 24.02 ?  104 GLU   A HG2  1 
ATOM   2106 H HG2  B GLU   A 1 104 ? 26.669 -2.008  -12.698 0.34 26.92 ?  104 GLU   A HG2  1 
ATOM   2107 H HG3  A GLU   A 1 104 ? 25.569 -1.739  -12.931 0.66 24.02 ?  104 GLU   A HG3  1 
ATOM   2108 H HG3  B GLU   A 1 104 ? 25.240 -1.350  -12.494 0.34 26.92 ?  104 GLU   A HG3  1 
ATOM   2109 N N    A ASP   A 1 105 ? 24.623 -6.443  -13.439 0.66 23.71 ?  105 ASP   A N    1 
ATOM   2110 N N    B ASP   A 1 105 ? 24.727 -6.253  -13.597 0.34 26.33 ?  105 ASP   A N    1 
ATOM   2111 C CA   A ASP   A 1 105 ? 24.136 -7.811  -13.579 0.66 25.47 ?  105 ASP   A CA   1 
ATOM   2112 C CA   B ASP   A 1 105 ? 24.085 -7.556  -13.713 0.34 27.38 ?  105 ASP   A CA   1 
ATOM   2113 C C    A ASP   A 1 105 ? 23.433 -8.262  -12.302 0.66 22.81 ?  105 ASP   A C    1 
ATOM   2114 C C    B ASP   A 1 105 ? 23.432 -7.959  -12.397 0.34 26.53 ?  105 ASP   A C    1 
ATOM   2115 O O    A ASP   A 1 105 ? 24.062 -8.378  -11.247 0.66 20.25 ?  105 ASP   A O    1 
ATOM   2116 O O    B ASP   A 1 105 ? 24.052 -7.893  -11.332 0.34 26.06 ?  105 ASP   A O    1 
ATOM   2117 C CB   A ASP   A 1 105 ? 25.321 -8.724  -13.889 0.66 28.76 ?  105 ASP   A CB   1 
ATOM   2118 C CB   B ASP   A 1 105 ? 25.117 -8.601  -14.140 0.34 28.94 ?  105 ASP   A CB   1 
ATOM   2119 C CG   A ASP   A 1 105 ? 24.907 -10.142 -14.211 0.66 31.70 ?  105 ASP   A CG   1 
ATOM   2120 C CG   B ASP   A 1 105 ? 24.623 -10.015 -13.940 0.34 30.39 ?  105 ASP   A CG   1 
ATOM   2121 O OD1  A ASP   A 1 105 ? 23.690 -10.405 -14.283 0.66 32.66 ?  105 ASP   A OD1  1 
ATOM   2122 O OD1  B ASP   A 1 105 ? 23.480 -10.303 -14.350 0.34 30.84 ?  105 ASP   A OD1  1 
ATOM   2123 O OD2  A ASP   A 1 105 ? 25.806 -10.993 -14.396 0.66 32.92 -1 105 ASP   A OD2  1 
ATOM   2124 O OD2  B ASP   A 1 105 ? 25.377 -10.837 -13.379 0.34 31.13 -1 105 ASP   A OD2  1 
ATOM   2125 H H    A ASP   A 1 105 ? 25.482 -6.382  -13.386 0.66 28.43 ?  105 ASP   A H    1 
ATOM   2126 H H    B ASP   A 1 105 ? 25.575 -6.272  -13.720 0.34 31.57 ?  105 ASP   A H    1 
ATOM   2127 H HA   A ASP   A 1 105 ? 23.506 -7.859  -14.314 0.66 30.54 ?  105 ASP   A HA   1 
ATOM   2128 H HA   B ASP   A 1 105 ? 23.396 -7.523  -14.391 0.34 32.83 ?  105 ASP   A HA   1 
ATOM   2129 H HB2  A ASP   A 1 105 ? 25.797 -8.375  -14.659 0.66 34.49 ?  105 ASP   A HB2  1 
ATOM   2130 H HB2  B ASP   A 1 105 ? 25.310 -8.492  -15.087 0.34 34.71 ?  105 ASP   A HB2  1 
ATOM   2131 H HB3  A ASP   A 1 105 ? 25.908 -8.753  -13.119 0.66 34.49 ?  105 ASP   A HB3  1 
ATOM   2132 H HB3  B ASP   A 1 105 ? 25.931 -8.480  -13.624 0.34 34.71 ?  105 ASP   A HB3  1 
ATOM   2133 N N    A ILE   A 1 106 ? 22.129 -8.532  -12.401 0.66 23.25 ?  106 ILE   A N    1 
ATOM   2134 N N    B ILE   A 1 106 ? 22.168 -8.383  -12.480 0.34 26.01 ?  106 ILE   A N    1 
ATOM   2135 C CA   A ILE   A 1 106 ? 21.362 -8.965  -11.240 0.66 22.89 ?  106 ILE   A CA   1 
ATOM   2136 C CA   B ILE   A 1 106 ? 21.410 -8.734  -11.285 0.34 25.27 ?  106 ILE   A CA   1 
ATOM   2137 C C    A ILE   A 1 106 ? 21.904 -10.260 -10.663 0.66 21.76 ?  106 ILE   A C    1 
ATOM   2138 C C    B ILE   A 1 106 ? 21.869 -10.056 -10.680 0.34 24.12 ?  106 ILE   A C    1 
ATOM   2139 O O    A ILE   A 1 106 ? 21.707 -10.531 -9.475  0.66 20.46 ?  106 ILE   A O    1 
ATOM   2140 O O    B ILE   A 1 106 ? 21.607 -10.311 -9.499  0.34 23.18 ?  106 ILE   A O    1 
ATOM   2141 C CB   A ILE   A 1 106 ? 19.857 -9.068  -11.583 0.66 24.25 ?  106 ILE   A CB   1 
ATOM   2142 C CB   B ILE   A 1 106 ? 19.897 -8.716  -11.587 0.34 25.77 ?  106 ILE   A CB   1 
ATOM   2143 C CG1  A ILE   A 1 106 ? 19.010 -9.158  -10.310 0.66 24.66 ?  106 ILE   A CG1  1 
ATOM   2144 C CG1  B ILE   A 1 106 ? 19.074 -8.834  -10.300 0.34 26.01 ?  106 ILE   A CG1  1 
ATOM   2145 C CG2  A ILE   A 1 106 ? 19.586 -10.276 -12.464 0.66 25.29 ?  106 ILE   A CG2  1 
ATOM   2146 C CG2  B ILE   A 1 106 ? 19.529 -9.836  -12.545 0.34 26.27 ?  106 ILE   A CG2  1 
ATOM   2147 C CD1  A ILE   A 1 106 ? 19.111 -7.939  -9.421  0.66 24.86 ?  106 ILE   A CD1  1 
ATOM   2148 C CD1  B ILE   A 1 106 ? 19.367 -7.756  -9.280  0.34 26.09 ?  106 ILE   A CD1  1 
ATOM   2149 H H    A ILE   A 1 106 ? 21.673 -8.468  -13.123 0.66 27.87 ?  106 ILE   A H    1 
ATOM   2150 H H    B ILE   A 1 106 ? 21.728 -8.462  -13.213 0.34 31.19 ?  106 ILE   A H    1 
ATOM   2151 H HA   A ILE   A 1 106 ? 21.461 -8.301  -10.550 0.66 27.44 ?  106 ILE   A HA   1 
ATOM   2152 H HA   B ILE   A 1 106 ? 21.581 -8.053  -10.624 0.34 30.29 ?  106 ILE   A HA   1 
ATOM   2153 H HB   A ILE   A 1 106 ? 19.600 -8.270  -12.067 0.66 29.08 ?  106 ILE   A HB   1 
ATOM   2154 H HB   B ILE   A 1 106 ? 19.681 -7.872  -12.010 0.34 30.90 ?  106 ILE   A HB   1 
ATOM   2155 H HG12 A ILE   A 1 106 ? 18.079 -9.261  -10.562 0.66 29.57 ?  106 ILE   A HG12 1 
ATOM   2156 H HG12 B ILE   A 1 106 ? 18.131 -8.772  -10.527 0.34 31.19 ?  106 ILE   A HG12 1 
ATOM   2157 H HG13 A ILE   A 1 106 ? 19.297 -9.926  -9.794  0.66 29.57 ?  106 ILE   A HG13 1 
ATOM   2158 H HG13 B ILE   A 1 106 ? 19.254 -9.691  -9.887  0.34 31.19 ?  106 ILE   A HG13 1 
ATOM   2159 H HG21 A ILE   A 1 106 ? 18.698 -10.192 -12.845 0.66 30.32 ?  106 ILE   A HG21 1 
ATOM   2160 H HG21 B ILE   A 1 106 ? 18.602 -9.729  -12.811 0.34 31.49 ?  106 ILE   A HG21 1 
ATOM   2161 H HG22 A ILE   A 1 106 ? 20.249 -10.302 -13.170 0.66 30.32 ?  106 ILE   A HG22 1 
ATOM   2162 H HG22 B ILE   A 1 106 ? 20.104 -9.787  -13.323 0.34 31.49 ?  106 ILE   A HG22 1 
ATOM   2163 H HG23 A ILE   A 1 106 ? 19.641 -11.080 -11.926 0.66 30.32 ?  106 ILE   A HG23 1 
ATOM   2164 H HG23 B ILE   A 1 106 ? 19.648 -10.688 -12.098 0.34 31.49 ?  106 ILE   A HG23 1 
ATOM   2165 H HD11 A ILE   A 1 106 ? 18.376 -7.947  -8.791  0.66 29.81 ?  106 ILE   A HD11 1 
ATOM   2166 H HD11 B ILE   A 1 106 ? 18.657 -7.746  -8.621  0.34 31.28 ?  106 ILE   A HD11 1 
ATOM   2167 H HD12 A ILE   A 1 106 ? 19.956 -7.963  -8.942  0.66 29.81 ?  106 ILE   A HD12 1 
ATOM   2168 H HD12 B ILE   A 1 106 ? 20.215 -7.952  -8.850  0.34 31.28 ?  106 ILE   A HD12 1 
ATOM   2169 H HD13 A ILE   A 1 106 ? 19.066 -7.141  -9.972  0.66 29.81 ?  106 ILE   A HD13 1 
ATOM   2170 H HD13 B ILE   A 1 106 ? 19.413 -6.899  -9.732  0.34 31.28 ?  106 ILE   A HD13 1 
ATOM   2171 N N    A GLN   A 1 107 ? 22.594 -11.069 -11.477 0.66 22.52 ?  107 GLN   A N    1 
ATOM   2172 N N    B GLN   A 1 107 ? 22.555 -10.907 -11.451 0.34 24.34 ?  107 GLN   A N    1 
ATOM   2173 C CA   A GLN   A 1 107 ? 23.236 -12.274 -10.967 0.66 25.18 ?  107 GLN   A CA   1 
ATOM   2174 C CA   B GLN   A 1 107 ? 23.072 -12.154 -10.897 0.34 24.66 ?  107 GLN   A CA   1 
ATOM   2175 C C    A GLN   A 1 107 ? 24.215 -11.960 -9.848  0.66 23.12 ?  107 GLN   A C    1 
ATOM   2176 C C    B GLN   A 1 107 ? 24.098 -11.905 -9.800  0.34 22.46 ?  107 GLN   A C    1 
ATOM   2177 O O    A GLN   A 1 107 ? 24.495 -12.831 -9.018  0.66 25.19 ?  107 GLN   A O    1 
ATOM   2178 O O    B GLN   A 1 107 ? 24.307 -12.777 -8.950  0.34 23.36 ?  107 GLN   A O    1 
ATOM   2179 C CB   A GLN   A 1 107 ? 23.955 -13.013 -12.105 0.66 29.58 ?  107 GLN   A CB   1 
ATOM   2180 C CB   B GLN   A 1 107 ? 23.674 -13.029 -12.004 0.34 27.32 ?  107 GLN   A CB   1 
ATOM   2181 C CG   A GLN   A 1 107 ? 23.077 -13.293 -13.319 0.66 33.86 ?  107 GLN   A CG   1 
ATOM   2182 C CG   B GLN   A 1 107 ? 22.765 -13.223 -13.212 0.34 29.96 ?  107 GLN   A CG   1 
ATOM   2183 C CD   A GLN   A 1 107 ? 21.851 -14.111 -12.975 0.66 37.20 ?  107 GLN   A CD   1 
ATOM   2184 C CD   B GLN   A 1 107 ? 21.353 -13.624 -12.832 0.34 31.97 ?  107 GLN   A CD   1 
ATOM   2185 O OE1  A GLN   A 1 107 ? 21.950 -15.165 -12.346 0.66 38.70 ?  107 GLN   A OE1  1 
ATOM   2186 O OE1  B GLN   A 1 107 ? 21.145 -14.488 -11.979 0.34 32.79 ?  107 GLN   A OE1  1 
ATOM   2187 N NE2  A GLN   A 1 107 ? 20.681 -13.625 -13.382 0.66 38.39 ?  107 GLN   A NE2  1 
ATOM   2188 N NE2  B GLN   A 1 107 ? 20.370 -12.990 -13.463 0.34 32.39 ?  107 GLN   A NE2  1 
ATOM   2189 H H    A GLN   A 1 107 ? 22.707 -10.940 -12.318 0.66 27.00 ?  107 GLN   A H    1 
ATOM   2190 H H    B GLN   A 1 107 ? 22.734 -10.785 -12.281 0.34 29.18 ?  107 GLN   A H    1 
ATOM   2191 H HA   A GLN   A 1 107 ? 22.567 -12.874 -10.609 0.66 30.18 ?  107 GLN   A HA   1 
ATOM   2192 H HA   B GLN   A 1 107 ? 22.345 -12.648 -10.498 0.34 29.57 ?  107 GLN   A HA   1 
ATOM   2193 H HB2  A GLN   A 1 107 ? 24.707 -12.479 -12.405 0.66 35.47 ?  107 GLN   A HB2  1 
ATOM   2194 H HB2  B GLN   A 1 107 ? 24.497 -12.624 -12.318 0.34 32.75 ?  107 GLN   A HB2  1 
ATOM   2195 H HB3  A GLN   A 1 107 ? 24.275 -13.870 -11.776 0.66 35.47 ?  107 GLN   A HB3  1 
ATOM   2196 H HB3  B GLN   A 1 107 ? 23.863 -13.909 -11.640 0.34 32.75 ?  107 GLN   A HB3  1 
ATOM   2197 H HG2  A GLN   A 1 107 ? 22.777 -12.453 -13.699 0.66 40.60 ?  107 GLN   A HG2  1 
ATOM   2198 H HG2  B GLN   A 1 107 ? 22.713 -12.395 -13.710 0.34 35.93 ?  107 GLN   A HG2  1 
ATOM   2199 H HG3  A GLN   A 1 107 ? 23.592 -13.787 -13.977 0.66 40.60 ?  107 GLN   A HG3  1 
ATOM   2200 H HG3  B GLN   A 1 107 ? 23.134 -13.923 -13.775 0.34 35.93 ?  107 GLN   A HG3  1 
ATOM   2201 H HE21 A GLN   A 1 107 ? 20.651 -12.884 -13.819 0.66 46.04 ?  107 GLN   A HE21 1 
ATOM   2202 H HE21 B GLN   A 1 107 ? 20.554 -12.391 -14.052 0.34 38.84 ?  107 GLN   A HE21 1 
ATOM   2203 H HE22 A GLN   A 1 107 ? 19.955 -14.052 -13.209 0.66 46.04 ?  107 GLN   A HE22 1 
ATOM   2204 H HE22 B GLN   A 1 107 ? 19.552 -13.180 -13.283 0.34 38.84 ?  107 GLN   A HE22 1 
ATOM   2205 N N    . LEU   A 1 108 ? 24.726 -10.727 -9.788  1.00 19.22 ?  108 LEU   A N    1 
ATOM   2206 C CA   . LEU   A 1 108 ? 25.652 -10.357 -8.729  1.00 16.24 ?  108 LEU   A CA   1 
ATOM   2207 C C    . LEU   A 1 108 ? 24.962 -10.206 -7.382  1.00 14.70 ?  108 LEU   A C    1 
ATOM   2208 O O    . LEU   A 1 108 ? 25.650 -10.066 -6.371  1.00 14.36 ?  108 LEU   A O    1 
ATOM   2209 C CB   . LEU   A 1 108 ? 26.393 -9.064  -9.099  1.00 15.63 ?  108 LEU   A CB   1 
ATOM   2210 C CG   . LEU   A 1 108 ? 27.412 -9.243  -10.229 1.00 17.69 ?  108 LEU   A CG   1 
ATOM   2211 C CD1  . LEU   A 1 108 ? 27.904 -7.905  -10.757 1.00 18.48 ?  108 LEU   A CD1  1 
ATOM   2212 C CD2  . LEU   A 1 108 ? 28.593 -10.085 -9.761  1.00 19.71 ?  108 LEU   A CD2  1 
ATOM   2213 H H    A LEU   A 1 108 ? 24.548 -10.098 -10.341 0.66 23.03 ?  108 LEU   A H    1 
ATOM   2214 H H    B LEU   A 1 108 ? 24.625 -10.123 -10.387 0.34 23.03 ?  108 LEU   A H    1 
ATOM   2215 H HA   . LEU   A 1 108 ? 26.314 -11.056 -8.634  1.00 19.46 ?  108 LEU   A HA   1 
ATOM   2216 H HB2  . LEU   A 1 108 ? 25.742 -8.401  -9.390  1.00 18.73 ?  108 LEU   A HB2  1 
ATOM   2217 H HB3  . LEU   A 1 108 ? 26.866 -8.736  -8.319  1.00 18.73 ?  108 LEU   A HB3  1 
ATOM   2218 H HG   . LEU   A 1 108 ? 26.986 -9.714  -10.962 1.00 21.20 ?  108 LEU   A HG   1 
ATOM   2219 H HD11 . LEU   A 1 108 ? 28.527 -8.062  -11.487 1.00 22.15 ?  108 LEU   A HD11 1 
ATOM   2220 H HD12 . LEU   A 1 108 ? 27.146 -7.391  -11.075 1.00 22.15 ?  108 LEU   A HD12 1 
ATOM   2221 H HD13 . LEU   A 1 108 ? 28.352 -7.426  -10.041 1.00 22.15 ?  108 LEU   A HD13 1 
ATOM   2222 H HD21 . LEU   A 1 108 ? 29.295 -10.037 -10.424 1.00 23.62 ?  108 LEU   A HD21 1 
ATOM   2223 H HD22 . LEU   A 1 108 ? 28.909 -9.736  -8.913  1.00 23.62 ?  108 LEU   A HD22 1 
ATOM   2224 H HD23 . LEU   A 1 108 ? 28.301 -11.004 -9.651  1.00 23.62 ?  108 LEU   A HD23 1 
ATOM   2225 N N    . LEU   A 1 109 ? 23.630 -10.259 -7.333  1.00 13.56 ?  109 LEU   A N    1 
ATOM   2226 C CA   . LEU   A 1 109 ? 22.943 -10.132 -6.055  1.00 12.36 ?  109 LEU   A CA   1 
ATOM   2227 C C    . LEU   A 1 109 ? 23.291 -11.284 -5.118  1.00 11.75 ?  109 LEU   A C    1 
ATOM   2228 O O    . LEU   A 1 109 ? 23.430 -11.085 -3.907  1.00 12.32 ?  109 LEU   A O    1 
ATOM   2229 C CB   . LEU   A 1 109 ? 21.439 -10.054 -6.296  1.00 13.35 ?  109 LEU   A CB   1 
ATOM   2230 C CG   . LEU   A 1 109 ? 20.555 -9.759  -5.090  1.00 13.52 ?  109 LEU   A CG   1 
ATOM   2231 C CD1  . LEU   A 1 109 ? 21.014 -8.498  -4.377  1.00 13.49 ?  109 LEU   A CD1  1 
ATOM   2232 C CD2  . LEU   A 1 109 ? 19.107 -9.618  -5.535  1.00 14.32 ?  109 LEU   A CD2  1 
ATOM   2233 H H    . LEU   A 1 109 ? 23.110 -10.370 -8.007  1.00 16.24 ?  109 LEU   A H    1 
ATOM   2234 H HA   . LEU   A 1 109 ? 23.227 -9.307  -5.629  1.00 14.80 ?  109 LEU   A HA   1 
ATOM   2235 H HB2  . LEU   A 1 109 ? 21.276 -9.348  -6.943  1.00 16.00 ?  109 LEU   A HB2  1 
ATOM   2236 H HB3  . LEU   A 1 109 ? 21.146 -10.899 -6.661  1.00 16.00 ?  109 LEU   A HB3  1 
ATOM   2237 H HG   . LEU   A 1 109 ? 20.607 -10.496 -4.463  1.00 16.20 ?  109 LEU   A HG   1 
ATOM   2238 H HD11 . LEU   A 1 109 ? 20.331 -8.218  -3.749  1.00 16.16 ?  109 LEU   A HD11 1 
ATOM   2239 H HD12 . LEU   A 1 109 ? 21.843 -8.680  -3.909  1.00 16.16 ?  109 LEU   A HD12 1 
ATOM   2240 H HD13 . LEU   A 1 109 ? 21.157 -7.797  -5.038  1.00 16.16 ?  109 LEU   A HD13 1 
ATOM   2241 H HD21 . LEU   A 1 109 ? 18.572 -9.316  -4.783  1.00 17.16 ?  109 LEU   A HD21 1 
ATOM   2242 H HD22 . LEU   A 1 109 ? 19.059 -8.966  -6.254  1.00 17.16 ?  109 LEU   A HD22 1 
ATOM   2243 H HD23 . LEU   A 1 109 ? 18.785 -10.477 -5.847  1.00 17.16 ?  109 LEU   A HD23 1 
ATOM   2244 N N    . LYS   A 1 110 ? 23.429 -12.498 -5.652  1.00 11.60 ?  110 LYS   A N    1 
ATOM   2245 C CA   . LYS   A 1 110 ? 23.802 -13.618 -4.796  1.00 11.64 ?  110 LYS   A CA   1 
ATOM   2246 C C    . LYS   A 1 110 ? 25.183 -13.397 -4.189  1.00 11.36 ?  110 LYS   A C    1 
ATOM   2247 O O    . LYS   A 1 110 ? 25.380 -13.593 -2.988  1.00 11.38 ?  110 LYS   A O    1 
ATOM   2248 C CB   . LYS   A 1 110 ? 23.724 -14.940 -5.559  1.00 13.02 ?  110 LYS   A CB   1 
ATOM   2249 C CG   . LYS   A 1 110 ? 23.934 -16.155 -4.654  1.00 12.91 ?  110 LYS   A CG   1 
ATOM   2250 C CD   . LYS   A 1 110 ? 23.694 -17.481 -5.363  1.00 13.62 ?  110 LYS   A CD   1 
ATOM   2251 C CE   . LYS   A 1 110 ? 23.807 -18.661 -4.399  1.00 14.39 ?  110 LYS   A CE   1 
ATOM   2252 N NZ   . LYS   A 1 110 ? 22.629 -18.795 -3.501  1.00 14.66 ?  110 LYS   A NZ   1 
ATOM   2253 H H    . LYS   A 1 110 ? 23.324 -12.690 -6.482  1.00 13.89 ?  110 LYS   A H    1 
ATOM   2254 H HA   . LYS   A 1 110 ? 23.163 -13.664 -4.063  1.00 13.94 ?  110 LYS   A HA   1 
ATOM   2255 H HB2  . LYS   A 1 110 ? 22.848 -15.019 -5.965  1.00 15.60 ?  110 LYS   A HB2  1 
ATOM   2256 H HB3  . LYS   A 1 110 ? 24.412 -14.951 -6.238  1.00 15.60 ?  110 LYS   A HB3  1 
ATOM   2257 H HG2  . LYS   A 1 110 ? 24.849 -16.152 -4.327  1.00 15.47 ?  110 LYS   A HG2  1 
ATOM   2258 H HG3  . LYS   A 1 110 ? 23.319 -16.102 -3.905  1.00 15.47 ?  110 LYS   A HG3  1 
ATOM   2259 H HD2  . LYS   A 1 110 ? 22.805 -17.487 -5.742  1.00 16.32 ?  110 LYS   A HD2  1 
ATOM   2260 H HD3  . LYS   A 1 110 ? 24.361 -17.597 -6.059  1.00 16.32 ?  110 LYS   A HD3  1 
ATOM   2261 H HE2  . LYS   A 1 110 ? 23.890 -19.484 -4.907  1.00 17.24 ?  110 LYS   A HE2  1 
ATOM   2262 H HE3  . LYS   A 1 110 ? 24.595 -18.542 -3.838  1.00 17.24 ?  110 LYS   A HE3  1 
ATOM   2263 H HZ1  . LYS   A 1 110 ? 22.732 -19.490 -2.957  1.00 17.56 ?  110 LYS   A HZ1  1 
ATOM   2264 H HZ2  . LYS   A 1 110 ? 22.533 -18.056 -3.012  1.00 17.56 ?  110 LYS   A HZ2  1 
ATOM   2265 H HZ3  . LYS   A 1 110 ? 21.891 -18.915 -3.987  1.00 17.56 ?  110 LYS   A HZ3  1 
ATOM   2266 N N    . SER   A 1 111 ? 26.150 -12.965 -5.007  1.00 11.60 ?  111 SER   A N    1 
ATOM   2267 C CA   . SER   A 1 111 ? 27.481 -12.658 -4.488  1.00 11.73 ?  111 SER   A CA   1 
ATOM   2268 C C    . SER   A 1 111 ? 27.412 -11.611 -3.381  1.00 11.26 ?  111 SER   A C    1 
ATOM   2269 O O    . SER   A 1 111 ? 28.102 -11.717 -2.362  1.00 11.64 ?  111 SER   A O    1 
ATOM   2270 C CB   . SER   A 1 111 ? 28.374 -12.162 -5.624  1.00 13.20 ?  111 SER   A CB   1 
ATOM   2271 O OG   . SER   A 1 111 ? 28.490 -13.155 -6.626  1.00 14.81 ?  111 SER   A OG   1 
ATOM   2272 H H    . SER   A 1 111 ? 26.056 -12.842 -5.850  1.00 13.89 ?  111 SER   A H    1 
ATOM   2273 H HA   . SER   A 1 111 ? 27.874 -13.463 -4.120  1.00 14.05 ?  111 SER   A HA   1 
ATOM   2274 H HB2  . SER   A 1 111 ? 27.973 -11.372 -6.020  1.00 15.82 ?  111 SER   A HB2  1 
ATOM   2275 H HB3  . SER   A 1 111 ? 29.249 -11.950 -5.269  1.00 15.82 ?  111 SER   A HB3  1 
ATOM   2276 H HG   . SER   A 1 111 ? 29.000 -12.880 -7.244  1.00 17.75 ?  111 SER   A HG   1 
ATOM   2277 N N    . ALA   A 1 112 ? 26.567 -10.596 -3.561  1.00 11.29 ?  112 ALA   A N    1 
ATOM   2278 C CA   . ALA   A 1 112 ? 26.428 -9.560  -2.541  1.00 11.06 ?  112 ALA   A CA   1 
ATOM   2279 C C    . ALA   A 1 112 ? 25.947 -10.160 -1.222  1.00 11.19 ?  112 ALA   A C    1 
ATOM   2280 O O    . ALA   A 1 112 ? 26.492 -9.863  -0.154  1.00 11.33 ?  112 ALA   A O    1 
ATOM   2281 C CB   . ALA   A 1 112 ? 25.472 -8.469  -3.025  1.00 11.36 ?  112 ALA   A CB   1 
ATOM   2282 H H    . ALA   A 1 112 ? 26.074 -10.477 -4.252  1.00 13.52 ?  112 ALA   A H    1 
ATOM   2283 H HA   . ALA   A 1 112 ? 27.292 -9.147  -2.381  1.00 13.24 ?  112 ALA   A HA   1 
ATOM   2284 H HB1  . ALA   A 1 112 ? 25.406 -7.776  -2.339  1.00 13.61 ?  112 ALA   A HB1  1 
ATOM   2285 H HB2  . ALA   A 1 112 ? 25.817 -8.082  -3.843  1.00 13.61 ?  112 ALA   A HB2  1 
ATOM   2286 H HB3  . ALA   A 1 112 ? 24.597 -8.855  -3.180  1.00 13.61 ?  112 ALA   A HB3  1 
ATOM   2287 N N    . TYR   A 1 113 ? 24.904 -10.997 -1.274  1.00 11.00 ?  113 TYR   A N    1 
ATOM   2288 C CA   . TYR   A 1 113 ? 24.388 -11.602 -0.048  1.00 10.96 ?  113 TYR   A CA   1 
ATOM   2289 C C    . TYR   A 1 113 ? 25.386 -12.556 0.604   1.00 10.64 ?  113 TYR   A C    1 
ATOM   2290 O O    . TYR   A 1 113 ? 25.343 -12.741 1.824   1.00 11.23 ?  113 TYR   A O    1 
ATOM   2291 C CB   . TYR   A 1 113 ? 23.066 -12.319 -0.317  1.00 11.22 ?  113 TYR   A CB   1 
ATOM   2292 C CG   . TYR   A 1 113 ? 21.859 -11.415 -0.227  1.00 11.07 ?  113 TYR   A CG   1 
ATOM   2293 C CD1  . TYR   A 1 113 ? 21.495 -10.828 0.979   1.00 11.23 ?  113 TYR   A CD1  1 
ATOM   2294 C CD2  . TYR   A 1 113 ? 21.057 -11.182 -1.338  1.00 11.29 ?  113 TYR   A CD2  1 
ATOM   2295 C CE1  . TYR   A 1 113 ? 20.370 -10.024 1.073   1.00 11.34 ?  113 TYR   A CE1  1 
ATOM   2296 C CE2  . TYR   A 1 113 ? 19.913 -10.379 -1.249  1.00 11.45 ?  113 TYR   A CE2  1 
ATOM   2297 C CZ   . TYR   A 1 113 ? 19.577 -9.814  -0.040  1.00 11.45 ?  113 TYR   A CZ   1 
ATOM   2298 O OH   . TYR   A 1 113 ? 18.459 -9.013  0.094   1.00 12.11 ?  113 TYR   A OH   1 
ATOM   2299 H H    . TYR   A 1 113 ? 24.493 -11.227 -1.994  1.00 13.17 ?  113 TYR   A H    1 
ATOM   2300 H HA   . TYR   A 1 113 ? 24.213 -10.890 0.588   1.00 13.13 ?  113 TYR   A HA   1 
ATOM   2301 H HB2  . TYR   A 1 113 ? 23.081 -12.690 -1.208  1.00 13.44 ?  113 TYR   A HB2  1 
ATOM   2302 H HB3  . TYR   A 1 113 ? 22.952 -13.022 0.339   1.00 13.44 ?  113 TYR   A HB3  1 
ATOM   2303 H HD1  . TYR   A 1 113 ? 22.018 -10.979 1.737   1.00 13.45 ?  113 TYR   A HD1  1 
ATOM   2304 H HD2  . TYR   A 1 113 ? 21.272 -11.579 -2.146  1.00 13.52 ?  113 TYR   A HD2  1 
ATOM   2305 H HE1  . TYR   A 1 113 ? 20.141 -9.637  1.892   1.00 13.58 ?  113 TYR   A HE1  1 
ATOM   2306 H HE2  . TYR   A 1 113 ? 19.380 -10.230 -1.995  1.00 13.71 ?  113 TYR   A HE2  1 
ATOM   2307 H HH   . TYR   A 1 113 ? 18.002 -9.048  -0.616  1.00 14.51 ?  113 TYR   A HH   1 
ATOM   2308 N N    . GLU   A 1 114 ? 26.287 -13.169 -0.177  1.00 11.08 ?  114 GLU   A N    1 
ATOM   2309 C CA   . GLU   A 1 114 ? 27.281 -14.066 0.416   1.00 11.09 ?  114 GLU   A CA   1 
ATOM   2310 C C    . GLU   A 1 114 ? 28.127 -13.361 1.469   1.00 10.87 ?  114 GLU   A C    1 
ATOM   2311 O O    . GLU   A 1 114 ? 28.595 -13.998 2.420   1.00 11.23 ?  114 GLU   A O    1 
ATOM   2312 C CB   . GLU   A 1 114 ? 28.149 -14.705 -0.675  1.00 11.34 ?  114 GLU   A CB   1 
ATOM   2313 C CG   . GLU   A 1 114 ? 27.381 -15.750 -1.465  1.00 11.74 ?  114 GLU   A CG   1 
ATOM   2314 C CD   . GLU   A 1 114 ? 28.092 -16.289 -2.696  1.00 11.92 ?  114 GLU   A CD   1 
ATOM   2315 O OE1  . GLU   A 1 114 ? 29.056 -15.671 -3.196  1.00 12.16 ?  114 GLU   A OE1  1 
ATOM   2316 O OE2  . GLU   A 1 114 ? 27.643 -17.350 -3.182  1.00 13.31 -1 114 GLU   A OE2  1 
ATOM   2317 H H    . GLU   A 1 114 ? 26.341 -13.073 -1.037  1.00 13.27 ?  114 GLU   A H    1 
ATOM   2318 H HA   . GLU   A 1 114 ? 26.805 -14.780 0.854   1.00 13.28 ?  114 GLU   A HA   1 
ATOM   2319 H HB2  . GLU   A 1 114 ? 28.448 -14.020 -1.298  1.00 13.58 ?  114 GLU   A HB2  1 
ATOM   2320 H HB3  . GLU   A 1 114 ? 28.910 -15.139 -0.265  1.00 13.58 ?  114 GLU   A HB3  1 
ATOM   2321 H HG2  . GLU   A 1 114 ? 27.200 -16.506 -0.887  1.00 14.06 ?  114 GLU   A HG2  1 
ATOM   2322 H HG3  . GLU   A 1 114 ? 26.539 -15.363 -1.761  1.00 14.06 ?  114 GLU   A HG3  1 
ATOM   2323 N N    . ASN   A 1 115 ? 28.313 -12.046 1.344   1.00 10.69 ?  115 ASN   A N    1 
ATOM   2324 C CA   . ASN   A 1 115 ? 29.079 -11.325 2.354   1.00 11.39 ?  115 ASN   A CA   1 
ATOM   2325 C C    . ASN   A 1 115 ? 28.460 -11.459 3.740   1.00 11.03 ?  115 ASN   A C    1 
ATOM   2326 O O    . ASN   A 1 115 ? 29.170 -11.391 4.749   1.00 11.65 ?  115 ASN   A O    1 
ATOM   2327 C CB   . ASN   A 1 115 ? 29.178 -9.846  1.986   1.00 11.37 ?  115 ASN   A CB   1 
ATOM   2328 C CG   . ASN   A 1 115 ? 29.990 -9.606  0.737   1.00 12.18 ?  115 ASN   A CG   1 
ATOM   2329 O OD1  . ASN   A 1 115 ? 31.209 -9.679  0.767   1.00 15.71 ?  115 ASN   A OD1  1 
ATOM   2330 N ND2  . ASN   A 1 115 ? 29.320 -9.320  -0.365  1.00 11.68 ?  115 ASN   A ND2  1 
ATOM   2331 H H    . ASN   A 1 115 ? 28.004 -11.554 0.704   1.00 12.80 ?  115 ASN   A H    1 
ATOM   2332 H HA   . ASN   A 1 115 ? 29.972 -11.685 2.389   1.00 13.64 ?  115 ASN   A HA   1 
ATOM   2333 H HB2  . ASN   A 1 115 ? 28.279 -9.495  1.846   1.00 13.62 ?  115 ASN   A HB2  1 
ATOM   2334 H HB3  . ASN   A 1 115 ? 29.599 -9.368  2.722   1.00 13.62 ?  115 ASN   A HB3  1 
ATOM   2335 H HD21 . ASN   A 1 115 ? 29.742 -9.171  -1.098  1.00 13.99 ?  115 ASN   A HD21 1 
ATOM   2336 H HD22 . ASN   A 1 115 ? 28.459 -9.292  -0.352  1.00 13.99 ?  115 ASN   A HD22 1 
ATOM   2337 N N    . PHE   A 1 116 ? 27.135 -11.625 3.815   1.00 11.11 ?  116 PHE   A N    1 
ATOM   2338 C CA   . PHE   A 1 116 ? 26.479 -11.724 5.115   1.00 10.96 ?  116 PHE   A CA   1 
ATOM   2339 C C    . PHE   A 1 116 ? 26.950 -12.959 5.881   1.00 11.11 ?  116 PHE   A C    1 
ATOM   2340 O O    . PHE   A 1 116 ? 26.871 -12.985 7.110   1.00 11.54 ?  116 PHE   A O    1 
ATOM   2341 C CB   . PHE   A 1 116 ? 24.952 -11.852 4.973   1.00 11.29 ?  116 PHE   A CB   1 
ATOM   2342 C CG   . PHE   A 1 116 ? 24.203 -10.605 4.515   1.00 10.68 ?  116 PHE   A CG   1 
ATOM   2343 C CD1  . PHE   A 1 116 ? 24.780 -9.584  3.766   1.00 10.85 ?  116 PHE   A CD1  1 
ATOM   2344 C CD2  . PHE   A 1 116 ? 22.851 -10.500 4.829   1.00 11.48 ?  116 PHE   A CD2  1 
ATOM   2345 C CE1  . PHE   A 1 116 ? 24.015 -8.486  3.354   1.00 11.22 ?  116 PHE   A CE1  1 
ATOM   2346 C CE2  . PHE   A 1 116 ? 22.090 -9.420  4.422   1.00 11.42 ?  116 PHE   A CE2  1 
ATOM   2347 C CZ   . PHE   A 1 116 ? 22.667 -8.412  3.684   1.00 11.19 ?  116 PHE   A CZ   1 
ATOM   2348 H H    . PHE   A 1 116 ? 26.598 -11.676 3.139   1.00 13.31 ?  116 PHE   A H    1 
ATOM   2349 H HA   . PHE   A 1 116 ? 26.674 -10.935 5.644   1.00 13.13 ?  116 PHE   A HA   1 
ATOM   2350 H HB2  . PHE   A 1 116 ? 24.765 -12.553 4.328   1.00 13.52 ?  116 PHE   A HB2  1 
ATOM   2351 H HB3  . PHE   A 1 116 ? 24.587 -12.109 5.836   1.00 13.52 ?  116 PHE   A HB3  1 
ATOM   2352 H HD1  . PHE   A 1 116 ? 25.677 -9.642  3.534   1.00 12.99 ?  116 PHE   A HD1  1 
ATOM   2353 H HD2  . PHE   A 1 116 ? 22.447 -11.184 5.324   1.00 13.74 ?  116 PHE   A HD2  1 
ATOM   2354 H HE1  . PHE   A 1 116 ? 24.408 -7.810  2.855   1.00 13.44 ?  116 PHE   A HE1  1 
ATOM   2355 H HE2  . PHE   A 1 116 ? 21.191 -9.379  4.655   1.00 13.68 ?  116 PHE   A HE2  1 
ATOM   2356 H HZ   . PHE   A 1 116 ? 22.162 -7.681  3.418   1.00 13.40 ?  116 PHE   A HZ   1 
ATOM   2357 N N    . ASN   A 1 117 ? 27.390 -14.008 5.173   1.00 11.47 ?  117 ASN   A N    1 
ATOM   2358 C CA   . ASN   A 1 117 ? 27.757 -15.256 5.838   1.00 11.57 ?  117 ASN   A CA   1 
ATOM   2359 C C    . ASN   A 1 117 ? 29.019 -15.141 6.672   1.00 12.23 ?  117 ASN   A C    1 
ATOM   2360 O O    . ASN   A 1 117 ? 29.326 -16.065 7.433   1.00 13.27 ?  117 ASN   A O    1 
ATOM   2361 C CB   . ASN   A 1 117 ? 27.876 -16.376 4.812   1.00 12.08 ?  117 ASN   A CB   1 
ATOM   2362 C CG   . ASN   A 1 117 ? 26.523 -16.764 4.275   1.00 11.77 ?  117 ASN   A CG   1 
ATOM   2363 O OD1  . ASN   A 1 117 ? 25.551 -16.787 5.027   1.00 12.64 ?  117 ASN   A OD1  1 
ATOM   2364 N ND2  . ASN   A 1 117 ? 26.434 -17.015 2.988   1.00 11.79 ?  117 ASN   A ND2  1 
ATOM   2365 H H    . ASN   A 1 117 ? 27.468 -14.022 4.311   1.00 13.74 ?  117 ASN   A H    1 
ATOM   2366 H HA   . ASN   A 1 117 ? 27.033 -15.494 6.439   1.00 13.86 ?  117 ASN   A HA   1 
ATOM   2367 H HB2  . ASN   A 1 117 ? 28.422 -16.074 4.068   1.00 14.46 ?  117 ASN   A HB2  1 
ATOM   2368 H HB3  . ASN   A 1 117 ? 28.271 -17.152 5.231   1.00 14.46 ?  117 ASN   A HB3  1 
ATOM   2369 H HD21 . ASN   A 1 117 ? 25.676 -17.232 2.650   1.00 14.12 ?  117 ASN   A HD21 1 
ATOM   2370 H HD22 . ASN   A 1 117 ? 27.135 -16.975 2.494   1.00 14.12 ?  117 ASN   A HD22 1 
ATOM   2371 N N    . GLN   A 1 118 ? 29.744 -14.028 6.556   1.00 11.98 ?  118 GLN   A N    1 
ATOM   2372 C CA   . GLN   A 1 118 ? 30.923 -13.788 7.380   1.00 12.63 ?  118 GLN   A CA   1 
ATOM   2373 C C    . GLN   A 1 118 ? 30.584 -13.215 8.752   1.00 12.43 ?  118 GLN   A C    1 
ATOM   2374 O O    . GLN   A 1 118 ? 31.500 -12.939 9.537   1.00 14.08 ?  118 GLN   A O    1 
ATOM   2375 C CB   . GLN   A 1 118 ? 31.918 -12.886 6.643   1.00 12.95 ?  118 GLN   A CB   1 
ATOM   2376 C CG   . GLN   A 1 118 ? 32.392 -13.475 5.324   1.00 13.09 ?  118 GLN   A CG   1 
ATOM   2377 C CD   . GLN   A 1 118 ? 33.223 -14.736 5.509   1.00 13.54 ?  118 GLN   A CD   1 
ATOM   2378 O OE1  . GLN   A 1 118 ? 34.085 -14.808 6.397   1.00 14.13 ?  118 GLN   A OE1  1 
ATOM   2379 N NE2  . GLN   A 1 118 ? 32.981 -15.735 4.660   1.00 13.73 ?  118 GLN   A NE2  1 
ATOM   2380 H H    . GLN   A 1 118 ? 29.565 -13.388 5.998   1.00 14.35 ?  118 GLN   A H    1 
ATOM   2381 H HA   . GLN   A 1 118 ? 31.354 -14.642 7.521   1.00 15.13 ?  118 GLN   A HA   1 
ATOM   2382 H HB2  . GLN   A 1 118 ? 31.492 -12.035 6.457   1.00 15.52 ?  118 GLN   A HB2  1 
ATOM   2383 H HB3  . GLN   A 1 118 ? 32.692 -12.755 7.210   1.00 15.52 ?  118 GLN   A HB3  1 
ATOM   2384 H HG2  . GLN   A 1 118 ? 31.622 -13.696 4.773   1.00 15.68 ?  118 GLN   A HG2  1 
ATOM   2385 H HG3  . GLN   A 1 118 ? 32.947 -12.823 4.866   1.00 15.68 ?  118 GLN   A HG3  1 
ATOM   2386 H HE21 . GLN   A 1 118 ? 32.374 -15.650 4.048   1.00 16.44 ?  118 GLN   A HE21 1 
ATOM   2387 H HE22 . GLN   A 1 118 ? 33.417 -16.474 4.720   1.00 16.44 ?  118 GLN   A HE22 1 
ATOM   2388 N N    . HIS   A 1 119 ? 29.296 -13.063 9.070   1.00 12.21 ?  119 HIS   A N    1 
ATOM   2389 C CA   . HIS   A 1 119 ? 28.844 -12.468 10.323  1.00 12.79 ?  119 HIS   A CA   1 
ATOM   2390 C C    . HIS   A 1 119 ? 27.705 -13.297 10.892  1.00 12.91 ?  119 HIS   A C    1 
ATOM   2391 O O    . HIS   A 1 119 ? 26.756 -13.626 10.174  1.00 13.45 ?  119 HIS   A O    1 
ATOM   2392 C CB   . HIS   A 1 119 ? 28.385 -11.032 10.068  1.00 13.44 ?  119 HIS   A CB   1 
ATOM   2393 C CG   . HIS   A 1 119 ? 29.466 -10.211 9.469   1.00 14.84 ?  119 HIS   A CG   1 
ATOM   2394 N ND1  . HIS   A 1 119 ? 30.436 -9.610  10.235  1.00 17.42 ?  119 HIS   A ND1  1 
ATOM   2395 C CD2  . HIS   A 1 119 ? 29.818 -10.010 8.179   1.00 15.82 ?  119 HIS   A CD2  1 
ATOM   2396 C CE1  . HIS   A 1 119 ? 31.306 -9.014  9.441   1.00 17.66 ?  119 HIS   A CE1  1 
ATOM   2397 N NE2  . HIS   A 1 119 ? 30.964 -9.255  8.188   1.00 17.69 ?  119 HIS   A NE2  1 
ATOM   2398 H H    . HIS   A 1 119 ? 28.642 -13.316 8.560   1.00 14.62 ?  119 HIS   A H    1 
ATOM   2399 H HA   . HIS   A 1 119 ? 29.576 -12.462 10.959  1.00 15.32 ?  119 HIS   A HA   1 
ATOM   2400 H HB2  . HIS   A 1 119 ? 27.633 -11.045 9.457   1.00 16.10 ?  119 HIS   A HB2  1 
ATOM   2401 H HB3  . HIS   A 1 119 ? 28.128 -10.632 10.912  1.00 16.10 ?  119 HIS   A HB3  1 
ATOM   2402 H HD1  . HIS   A 1 119 ? 30.458 -9.600  11.093  1.00 20.88 ?  119 HIS   A HD1  1 
ATOM   2403 H HD2  . HIS   A 1 119 ? 29.363 -10.314 7.426   1.00 18.95 ?  119 HIS   A HD2  1 
ATOM   2404 H HE1  . HIS   A 1 119 ? 32.040 -8.511  9.715   1.00 21.16 ?  119 HIS   A HE1  1 
ATOM   2405 N N    . GLU   A 1 120 ? 27.795 -13.629 12.180  1.00 13.94 ?  120 GLU   A N    1 
ATOM   2406 C CA   . GLU   A 1 120 ? 26.835 -14.565 12.761  1.00 16.40 ?  120 GLU   A CA   1 
ATOM   2407 C C    . GLU   A 1 120 ? 25.422 -13.994 12.829  1.00 14.58 ?  120 GLU   A C    1 
ATOM   2408 O O    . GLU   A 1 120 ? 24.446 -14.751 12.712  1.00 14.85 ?  120 GLU   A O    1 
ATOM   2409 C CB   . GLU   A 1 120 ? 27.297 -14.992 14.153  1.00 21.41 ?  120 GLU   A CB   1 
ATOM   2410 C CG   . GLU   A 1 120 ? 28.494 -15.928 14.145  1.00 29.67 ?  120 GLU   A CG   1 
ATOM   2411 C CD   . GLU   A 1 120 ? 28.679 -16.646 15.466  1.00 38.79 ?  120 GLU   A CD   1 
ATOM   2412 O OE1  . GLU   A 1 120 ? 28.146 -16.163 16.489  1.00 40.28 ?  120 GLU   A OE1  1 
ATOM   2413 O OE2  . GLU   A 1 120 ? 29.355 -17.696 15.482  1.00 44.32 -1 120 GLU   A OE2  1 
ATOM   2414 H H    . GLU   A 1 120 ? 28.401 -13.340 12.726  1.00 16.70 ?  120 GLU   A H    1 
ATOM   2415 H HA   . GLU   A 1 120 ? 26.809 -15.360 12.213  1.00 19.66 ?  120 GLU   A HA   1 
ATOM   2416 H HB2  . GLU   A 1 120 ? 27.549 -14.210 14.664  1.00 25.67 ?  120 GLU   A HB2  1 
ATOM   2417 H HB3  . GLU   A 1 120 ? 26.571 -15.457 14.599  1.00 25.67 ?  120 GLU   A HB3  1 
ATOM   2418 H HG2  . GLU   A 1 120 ? 28.377 -16.594 13.448  1.00 35.58 ?  120 GLU   A HG2  1 
ATOM   2419 H HG3  . GLU   A 1 120 ? 29.302 -15.419 13.988  1.00 35.58 ?  120 GLU   A HG3  1 
ATOM   2420 N N    . VAL   A 1 121 ? 25.293 -12.687 13.062  1.00 13.92 ?  121 VAL   A N    1 
ATOM   2421 C CA   . VAL   A 1 121 ? 24.001 -12.019 13.189  1.00 13.99 ?  121 VAL   A CA   1 
ATOM   2422 C C    . VAL   A 1 121 ? 24.114 -10.632 12.562  1.00 12.72 ?  121 VAL   A C    1 
ATOM   2423 O O    . VAL   A 1 121 ? 25.080 -9.907  12.819  1.00 13.38 ?  121 VAL   A O    1 
ATOM   2424 C CB   . VAL   A 1 121 ? 23.578 -11.883 14.670  1.00 16.91 ?  121 VAL   A CB   1 
ATOM   2425 C CG1  . VAL   A 1 121 ? 22.193 -11.254 14.776  1.00 17.25 ?  121 VAL   A CG1  1 
ATOM   2426 C CG2  . VAL   A 1 121 ? 23.611 -13.218 15.397  1.00 19.31 ?  121 VAL   A CG2  1 
ATOM   2427 H H    . VAL   A 1 121 ? 25.964 -12.149 13.146  1.00 16.68 ?  121 VAL   A H    1 
ATOM   2428 H HA   . VAL   A 1 121 ? 23.325 -12.530 12.717  1.00 16.76 ?  121 VAL   A HA   1 
ATOM   2429 H HB   . VAL   A 1 121 ? 24.202 -11.296 15.120  1.00 20.26 ?  121 VAL   A HB   1 
ATOM   2430 H HG11 . VAL   A 1 121 ? 21.882 -11.321 15.693  1.00 20.68 ?  121 VAL   A HG11 1 
ATOM   2431 H HG12 . VAL   A 1 121 ? 22.247 -10.322 14.515  1.00 20.68 ?  121 VAL   A HG12 1 
ATOM   2432 H HG13 . VAL   A 1 121 ? 21.583 -11.728 14.188  1.00 20.68 ?  121 VAL   A HG13 1 
ATOM   2433 H HG21 . VAL   A 1 121 ? 23.266 -13.097 16.301  1.00 23.15 ?  121 VAL   A HG21 1 
ATOM   2434 H HG22 . VAL   A 1 121 ? 23.052 -13.855 14.921  1.00 23.15 ?  121 VAL   A HG22 1 
ATOM   2435 H HG23 . VAL   A 1 121 ? 24.522 -13.541 15.435  1.00 23.15 ?  121 VAL   A HG23 1 
ATOM   2436 N N    . LEU   A 1 122 ? 23.109 -10.239 11.775  1.00 12.29 ?  122 LEU   A N    1 
ATOM   2437 C CA   . LEU   A 1 122 ? 23.108 -8.938  11.109  1.00 12.43 ?  122 LEU   A CA   1 
ATOM   2438 C C    . LEU   A 1 122 ? 21.709 -8.348  11.073  1.00 11.98 ?  122 LEU   A C    1 
ATOM   2439 O O    . LEU   A 1 122 ? 20.722 -9.070  10.924  1.00 12.96 ?  122 LEU   A O    1 
ATOM   2440 C CB   . LEU   A 1 122 ? 23.529 -9.032  9.635   1.00 13.93 ?  122 LEU   A CB   1 
ATOM   2441 C CG   . LEU   A 1 122 ? 24.734 -9.883  9.269   1.00 13.79 ?  122 LEU   A CG   1 
ATOM   2442 C CD1  . LEU   A 1 122 ? 24.318 -11.324 9.029   1.00 14.85 ?  122 LEU   A CD1  1 
ATOM   2443 C CD2  . LEU   A 1 122 ? 25.426 -9.311  8.044   1.00 13.44 ?  122 LEU   A CD2  1 
ATOM   2444 H H    . LEU   A 1 122 ? 22.409 -10.715 11.608  1.00 14.73 ?  122 LEU   A H    1 
ATOM   2445 H HA   . LEU   A 1 122 ? 23.701 -8.327  11.568  1.00 14.89 ?  122 LEU   A HA   1 
ATOM   2446 H HB2  . LEU   A 1 122 ? 22.784 -9.388  9.133   1.00 16.68 ?  122 LEU   A HB2  1 
ATOM   2447 H HB3  . LEU   A 1 122 ? 23.727 -8.139  9.324   1.00 16.68 ?  122 LEU   A HB3  1 
ATOM   2448 H HG   . LEU   A 1 122 ? 25.376 -9.880  9.998   1.00 16.52 ?  122 LEU   A HG   1 
ATOM   2449 H HD11 . LEU   A 1 122 ? 25.094 -11.848 8.765   1.00 17.80 ?  122 LEU   A HD11 1 
ATOM   2450 H HD12 . LEU   A 1 122 ? 23.943 -11.689 9.847   1.00 17.80 ?  122 LEU   A HD12 1 
ATOM   2451 H HD13 . LEU   A 1 122 ? 23.652 -11.351 8.322   1.00 17.80 ?  122 LEU   A HD13 1 
ATOM   2452 H HD21 . LEU   A 1 122 ? 26.175 -9.889  7.795   1.00 16.10 ?  122 LEU   A HD21 1 
ATOM   2453 H HD22 . LEU   A 1 122 ? 24.796 -9.267  7.310   1.00 16.10 ?  122 LEU   A HD22 1 
ATOM   2454 H HD23 . LEU   A 1 122 ? 25.761 -8.424  8.250   1.00 16.10 ?  122 LEU   A HD23 1 
ATOM   2455 N N    . LEU   A 1 123 ? 21.645 -7.018  11.173  1.00 11.73 ?  123 LEU   A N    1 
ATOM   2456 C CA   . LEU   A 1 123 ? 20.473 -6.225  10.804  1.00 11.43 ?  123 LEU   A CA   1 
ATOM   2457 C C    . LEU   A 1 123 ? 20.723 -5.689  9.401   1.00 10.89 ?  123 LEU   A C    1 
ATOM   2458 O O    . LEU   A 1 123 ? 21.771 -5.088  9.158   1.00 11.39 ?  123 LEU   A O    1 
ATOM   2459 C CB   . LEU   A 1 123 ? 20.340 -5.050  11.774  1.00 11.99 ?  123 LEU   A CB   1 
ATOM   2460 C CG   . LEU   A 1 123 ? 19.285 -3.999  11.433  1.00 12.82 ?  123 LEU   A CG   1 
ATOM   2461 C CD1  . LEU   A 1 123 ? 17.887 -4.593  11.425  1.00 13.63 ?  123 LEU   A CD1  1 
ATOM   2462 C CD2  . LEU   A 1 123 ? 19.374 -2.837  12.418  1.00 13.59 ?  123 LEU   A CD2  1 
ATOM   2463 H H    . LEU   A 1 123 ? 22.300 -6.532  11.452  1.00 14.05 ?  123 LEU   A H    1 
ATOM   2464 H HA   . LEU   A 1 123 ? 19.668 -6.764  10.816  1.00 13.69 ?  123 LEU   A HA   1 
ATOM   2465 H HB2  . LEU   A 1 123 ? 20.112 -5.404  12.649  1.00 14.37 ?  123 LEU   A HB2  1 
ATOM   2466 H HB3  . LEU   A 1 123 ? 21.192 -4.595  11.822  1.00 14.37 ?  123 LEU   A HB3  1 
ATOM   2467 H HG   . LEU   A 1 123 ? 19.461 -3.641  10.547  1.00 15.36 ?  123 LEU   A HG   1 
ATOM   2468 H HD11 . LEU   A 1 123 ? 17.242 -3.893  11.248  1.00 16.33 ?  123 LEU   A HD11 1 
ATOM   2469 H HD12 . LEU   A 1 123 ? 17.836 -5.274  10.734  1.00 16.33 ?  123 LEU   A HD12 1 
ATOM   2470 H HD13 . LEU   A 1 123 ? 17.710 -4.994  12.293  1.00 16.33 ?  123 LEU   A HD13 1 
ATOM   2471 H HD21 . LEU   A 1 123 ? 18.744 -2.150  12.154  1.00 16.28 ?  123 LEU   A HD21 1 
ATOM   2472 H HD22 . LEU   A 1 123 ? 19.152 -3.165  13.306  1.00 16.28 ?  123 LEU   A HD22 1 
ATOM   2473 H HD23 . LEU   A 1 123 ? 20.275 -2.486  12.410  1.00 16.28 ?  123 LEU   A HD23 1 
ATOM   2474 N N    A ALA   A 1 124 ? 19.769 -5.873  8.487   0.66 10.74 ?  124 ALA   A N    1 
ATOM   2475 N N    B ALA   A 1 124 ? 19.783 -5.912  8.483   0.34 10.50 ?  124 ALA   A N    1 
ATOM   2476 C CA   A ALA   A 1 124 ? 20.065 -5.598  7.087   0.66 10.94 ?  124 ALA   A CA   1 
ATOM   2477 C CA   B ALA   A 1 124 ? 20.050 -5.598  7.087   0.34 10.52 ?  124 ALA   A CA   1 
ATOM   2478 C C    A ALA   A 1 124 ? 18.829 -5.123  6.337   0.66 10.97 ?  124 ALA   A C    1 
ATOM   2479 C C    B ALA   A 1 124 ? 18.797 -5.122  6.371   0.34 10.57 ?  124 ALA   A C    1 
ATOM   2480 O O    A ALA   A 1 124 ? 17.693 -5.423  6.734   0.66 11.86 ?  124 ALA   A O    1 
ATOM   2481 O O    B ALA   A 1 124 ? 17.689 -5.578  6.683   0.34 10.51 ?  124 ALA   A O    1 
ATOM   2482 C CB   A ALA   A 1 124 ? 20.630 -6.842  6.391   0.66 11.84 ?  124 ALA   A CB   1 
ATOM   2483 C CB   B ALA   A 1 124 ? 20.620 -6.818  6.348   0.34 10.84 ?  124 ALA   A CB   1 
ATOM   2484 H H    A ALA   A 1 124 ? 18.971 -6.151  8.644   0.66 12.86 ?  124 ALA   A H    1 
ATOM   2485 H H    B ALA   A 1 124 ? 19.005 -6.240  8.638   0.34 12.57 ?  124 ALA   A H    1 
ATOM   2486 H HA   A ALA   A 1 124 ? 20.742 -4.907  7.047   0.66 13.10 ?  124 ALA   A HA   1 
ATOM   2487 H HA   B ALA   A 1 124 ? 20.711 -4.896  7.051   0.34 12.60 ?  124 ALA   A HA   1 
ATOM   2488 H HB1  A ALA   A 1 124 ? 20.823 -6.633  5.463   0.66 14.18 ?  124 ALA   A HB1  1 
ATOM   2489 H HB1  B ALA   A 1 124 ? 20.791 -6.583  5.422   0.34 12.98 ?  124 ALA   A HB1  1 
ATOM   2490 H HB2  A ALA   A 1 124 ? 21.453 -7.115  6.839   0.66 14.18 ?  124 ALA   A HB2  1 
ATOM   2491 H HB2  B ALA   A 1 124 ? 21.454 -7.089  6.774   0.34 12.98 ?  124 ALA   A HB2  1 
ATOM   2492 H HB3  A ALA   A 1 124 ? 19.981 -7.561  6.439   0.66 14.18 ?  124 ALA   A HB3  1 
ATOM   2493 H HB3  B ALA   A 1 124 ? 19.983 -7.549  6.391   0.34 12.98 ?  124 ALA   A HB3  1 
ATOM   2494 N N    A PRO   A 1 125 ? 19.027 -4.424  5.217   0.66 10.06 ?  125 PRO   A N    1 
ATOM   2495 N N    B PRO   A 1 125 ? 18.945 -4.234  5.390   0.34 10.96 ?  125 PRO   A N    1 
ATOM   2496 C CA   A PRO   A 1 125 ? 17.960 -4.160  4.253   0.66 10.07 ?  125 PRO   A CA   1 
ATOM   2497 C CA   B PRO   A 1 125 ? 17.851 -3.928  4.470   0.34 11.28 ?  125 PRO   A CA   1 
ATOM   2498 C C    A PRO   A 1 125 ? 17.998 -5.215  3.152   0.66 10.41 ?  125 PRO   A C    1 
ATOM   2499 C C    B PRO   A 1 125 ? 17.885 -4.925  3.315   0.34 11.38 ?  125 PRO   A C    1 
ATOM   2500 O O    A PRO   A 1 125 ? 18.949 -5.988  3.036   0.66 10.89 ?  125 PRO   A O    1 
ATOM   2501 O O    B PRO   A 1 125 ? 18.805 -5.738  3.194   0.34 11.48 ?  125 PRO   A O    1 
ATOM   2502 C CB   A PRO   A 1 125 ? 18.399 -2.808  3.674   0.66 9.58  ?  125 PRO   A CB   1 
ATOM   2503 C CB   B PRO   A 1 125 ? 18.234 -2.529  3.974   0.34 11.41 ?  125 PRO   A CB   1 
ATOM   2504 C CG   A PRO   A 1 125 ? 19.921 -2.950  3.585   0.66 9.70  ?  125 PRO   A CG   1 
ATOM   2505 C CG   B PRO   A 1 125 ? 19.733 -2.596  3.888   0.34 11.89 ?  125 PRO   A CG   1 
ATOM   2506 C CD   A PRO   A 1 125 ? 20.305 -3.813  4.783   0.66 9.94  ?  125 PRO   A CD   1 
ATOM   2507 C CD   B PRO   A 1 125 ? 20.182 -3.514  5.012   0.34 11.32 ?  125 PRO   A CD   1 
ATOM   2508 H HA   A PRO   A 1 125 ? 17.087 -4.115  4.669   0.66 12.05 ?  125 PRO   A HA   1 
ATOM   2509 H HA   B PRO   A 1 125 ? 16.997 -3.914  4.925   0.34 13.51 ?  125 PRO   A HA   1 
ATOM   2510 H HB2  A PRO   A 1 125 ? 18.003 -2.685  2.793   0.66 11.47 ?  125 PRO   A HB2  1 
ATOM   2511 H HB2  B PRO   A 1 125 ? 17.838 -2.364  3.103   0.34 13.67 ?  125 PRO   A HB2  1 
ATOM   2512 H HB3  A PRO   A 1 125 ? 18.140 -2.097  4.276   0.66 11.47 ?  125 PRO   A HB3  1 
ATOM   2513 H HB3  B PRO   A 1 125 ? 17.950 -1.855  4.617   0.34 13.67 ?  125 PRO   A HB3  1 
ATOM   2514 H HG2  A PRO   A 1 125 ? 20.164 -3.385  2.754   0.66 11.61 ?  125 PRO   A HG2  1 
ATOM   2515 H HG2  B PRO   A 1 125 ? 19.992 -2.961  3.027   0.34 14.24 ?  125 PRO   A HG2  1 
ATOM   2516 H HG3  A PRO   A 1 125 ? 20.332 -2.072  3.647   0.66 11.61 ?  125 PRO   A HG3  1 
ATOM   2517 H HG3  B PRO   A 1 125 ? 20.107 -1.709  4.004   0.34 14.24 ?  125 PRO   A HG3  1 
ATOM   2518 H HD2  A PRO   A 1 125 ? 20.942 -4.498  4.515   0.66 11.90 ?  125 PRO   A HD2  1 
ATOM   2519 H HD2  B PRO   A 1 125 ? 20.857 -4.135  4.686   0.34 13.56 ?  125 PRO   A HD2  1 
ATOM   2520 H HD3  A PRO   A 1 125 ? 20.667 -3.259  5.494   0.66 11.90 ?  125 PRO   A HD3  1 
ATOM   2521 H HD3  B PRO   A 1 125 ? 20.526 -2.994  5.756   0.34 13.56 ?  125 PRO   A HD3  1 
ATOM   2522 N N    A LEU   A 1 126 ? 16.949 -5.226  2.335   0.66 10.31 ?  126 LEU   A N    1 
ATOM   2523 N N    B LEU   A 1 126 ? 16.866 -4.850  2.461   0.34 12.01 ?  126 LEU   A N    1 
ATOM   2524 C CA   A LEU   A 1 126 ? 16.951 -6.040  1.126   0.66 10.54 ?  126 LEU   A CA   1 
ATOM   2525 C CA   B LEU   A 1 126 ? 16.877 -5.648  1.240   0.34 11.71 ?  126 LEU   A CA   1 
ATOM   2526 C C    A LEU   A 1 126 ? 17.876 -5.423  0.081   0.66 10.72 ?  126 LEU   A C    1 
ATOM   2527 C C    B LEU   A 1 126 ? 17.906 -5.070  0.274   0.34 11.48 ?  126 LEU   A C    1 
ATOM   2528 O O    A LEU   A 1 126 ? 17.634 -4.315  -0.411  0.66 11.41 ?  126 LEU   A O    1 
ATOM   2529 O O    B LEU   A 1 126 ? 17.842 -3.888  -0.075  0.34 12.31 ?  126 LEU   A O    1 
ATOM   2530 C CB   A LEU   A 1 126 ? 15.541 -6.165  0.573   0.66 10.92 ?  126 LEU   A CB   1 
ATOM   2531 C CB   B LEU   A 1 126 ? 15.497 -5.632  0.588   0.34 12.53 ?  126 LEU   A CB   1 
ATOM   2532 C CG   A LEU   A 1 126 ? 14.628 -7.094  1.368   0.66 12.18 ?  126 LEU   A CG   1 
ATOM   2533 C CG   B LEU   A 1 126 ? 14.397 -6.466  1.243   0.34 12.91 ?  126 LEU   A CG   1 
ATOM   2534 C CD1  A LEU   A 1 126 ? 13.201 -6.949  0.883   0.66 13.71 ?  126 LEU   A CD1  1 
ATOM   2535 C CD1  B LEU   A 1 126 ? 13.073 -6.247  0.528   0.34 13.14 ?  126 LEU   A CD1  1 
ATOM   2536 C CD2  A LEU   A 1 126 ? 15.104 -8.544  1.237   0.66 11.97 ?  126 LEU   A CD2  1 
ATOM   2537 C CD2  B LEU   A 1 126 ? 14.760 -7.937  1.236   0.34 13.31 ?  126 LEU   A CD2  1 
ATOM   2538 H H    A LEU   A 1 126 ? 16.233 -4.771  2.455   0.66 12.35 ?  126 LEU   A H    1 
ATOM   2539 H H    B LEU   A 1 126 ? 16.158 -4.362  2.559   0.34 14.39 ?  126 LEU   A H    1 
ATOM   2540 H HA   A LEU   A 1 126 ? 17.281 -6.927  1.332   0.66 12.62 ?  126 LEU   A HA   1 
ATOM   2541 H HA   B LEU   A 1 126 ? 17.119 -6.567  1.451   0.34 14.02 ?  126 LEU   A HA   1 
ATOM   2542 H HB2  A LEU   A 1 126 ? 15.127 -5.287  0.569   0.66 13.08 ?  126 LEU   A HB2  1 
ATOM   2543 H HB2  B LEU   A 1 126 ? 15.184 -4.715  0.570   0.34 15.01 ?  126 LEU   A HB2  1 
ATOM   2544 H HB3  A LEU   A 1 126 ? 15.585 -6.510  -0.331  0.66 13.08 ?  126 LEU   A HB3  1 
ATOM   2545 H HB3  B LEU   A 1 126 ? 15.592 -5.956  -0.321  0.34 15.01 ?  126 LEU   A HB3  1 
ATOM   2546 H HG   A LEU   A 1 126 ? 14.650 -6.847  2.308   0.66 14.59 ?  126 LEU   A HG   1 
ATOM   2547 H HG   B LEU   A 1 126 ? 14.286 -6.184  2.164   0.34 15.46 ?  126 LEU   A HG   1 
ATOM   2548 H HD11 A LEU   A 1 126 ? 12.628 -7.545  1.390   0.66 16.42 ?  126 LEU   A HD11 1 
ATOM   2549 H HD11 B LEU   A 1 126 ? 12.396 -6.814  0.934   0.34 15.74 ?  126 LEU   A HD11 1 
ATOM   2550 H HD12 A LEU   A 1 126 ? 12.914 -6.030  1.007   0.66 16.42 ?  126 LEU   A HD12 1 
ATOM   2551 H HD12 B LEU   A 1 126 ? 12.815 -5.316  0.610   0.34 15.74 ?  126 LEU   A HD12 1 
ATOM   2552 H HD13 A LEU   A 1 126 ? 13.164 -7.181  -0.060  0.66 16.42 ?  126 LEU   A HD13 1 
ATOM   2553 H HD13 B LEU   A 1 126 ? 13.176 -6.480  -0.409  0.34 15.74 ?  126 LEU   A HD13 1 
ATOM   2554 H HD21 A LEU   A 1 126 ? 14.421 -9.135  1.584   0.66 14.33 ?  126 LEU   A HD21 1 
ATOM   2555 H HD21 B LEU   A 1 126 ? 13.991 -8.455  1.514   0.34 15.95 ?  126 LEU   A HD21 1 
ATOM   2556 H HD22 A LEU   A 1 126 ? 15.266 -8.736  0.300   0.66 14.33 ?  126 LEU   A HD22 1 
ATOM   2557 H HD22 B LEU   A 1 126 ? 15.024 -8.189  0.337   0.34 15.95 ?  126 LEU   A HD22 1 
ATOM   2558 H HD23 A LEU   A 1 126 ? 15.925 -8.651  1.743   0.66 14.33 ?  126 LEU   A HD23 1 
ATOM   2559 H HD23 B LEU   A 1 126 ? 15.497 -8.080  1.849   0.34 15.95 ?  126 LEU   A HD23 1 
ATOM   2560 N N    A LEU   A 1 127 ? 18.927 -6.155  -0.273  0.66 10.60 ?  127 LEU   A N    1 
ATOM   2561 N N    B LEU   A 1 127 ? 18.861 -5.884  -0.160  0.34 10.72 ?  127 LEU   A N    1 
ATOM   2562 C CA   A LEU   A 1 127 ? 19.925 -5.650  -1.203  0.66 10.43 ?  127 LEU   A CA   1 
ATOM   2563 C CA   B LEU   A 1 127 ? 19.856 -5.396  -1.103  0.34 10.58 ?  127 LEU   A CA   1 
ATOM   2564 C C    A LEU   A 1 127 ? 19.318 -5.443  -2.581  0.66 10.53 ?  127 LEU   A C    1 
ATOM   2565 C C    B LEU   A 1 127 ? 19.272 -5.319  -2.509  0.34 10.76 ?  127 LEU   A C    1 
ATOM   2566 O O    A LEU   A 1 127 ? 18.496 -6.237  -3.049  0.66 10.18 ?  127 LEU   A O    1 
ATOM   2567 O O    B LEU   A 1 127 ? 18.380 -6.087  -2.884  0.34 11.32 ?  127 LEU   A O    1 
ATOM   2568 C CB   A LEU   A 1 127 ? 21.085 -6.636  -1.301  0.66 11.37 ?  127 LEU   A CB   1 
ATOM   2569 C CB   B LEU   A 1 127 ? 21.086 -6.301  -1.116  0.34 10.89 ?  127 LEU   A CB   1 
ATOM   2570 C CG   A LEU   A 1 127 ? 21.889 -6.882  -0.027  0.66 12.00 ?  127 LEU   A CG   1 
ATOM   2571 C CG   B LEU   A 1 127 ? 21.864 -6.410  0.198   0.34 11.39 ?  127 LEU   A CG   1 
ATOM   2572 C CD1  A LEU   A 1 127 ? 22.976 -7.888  -0.329  0.66 12.12 ?  127 LEU   A CD1  1 
ATOM   2573 C CD1  B LEU   A 1 127 ? 23.057 -7.338  0.028   0.34 12.01 ?  127 LEU   A CD1  1 
ATOM   2574 C CD2  A LEU   A 1 127 ? 22.495 -5.603  0.506   0.66 12.49 ?  127 LEU   A CD2  1 
ATOM   2575 C CD2  B LEU   A 1 127 ? 22.309 -5.037  0.703   0.34 11.58 ?  127 LEU   A CD2  1 
ATOM   2576 H H    A LEU   A 1 127 ? 19.073 -6.954  0.013   0.66 12.69 ?  127 LEU   A H    1 
ATOM   2577 H H    B LEU   A 1 127 ? 18.955 -6.707  0.081   0.34 12.84 ?  127 LEU   A H    1 
ATOM   2578 H HA   A LEU   A 1 127 ? 20.261 -4.803  -0.880  0.66 12.49 ?  127 LEU   A HA   1 
ATOM   2579 H HA   B LEU   A 1 127 ? 20.131 -4.505  -0.833  0.34 12.67 ?  127 LEU   A HA   1 
ATOM   2580 H HB2  A LEU   A 1 127 ? 20.728 -7.494  -1.585  0.66 13.62 ?  127 LEU   A HB2  1 
ATOM   2581 H HB2  B LEU   A 1 127 ? 20.798 -7.194  -1.361  0.34 13.04 ?  127 LEU   A HB2  1 
ATOM   2582 H HB3  A LEU   A 1 127 ? 21.702 -6.308  -1.967  0.66 13.62 ?  127 LEU   A HB3  1 
ATOM   2583 H HB3  B LEU   A 1 127 ? 21.695 -5.962  -1.790  0.34 13.04 ?  127 LEU   A HB3  1 
ATOM   2584 H HG   A LEU   A 1 127 ? 21.305 -7.259  0.658   0.66 14.37 ?  127 LEU   A HG   1 
ATOM   2585 H HG   B LEU   A 1 127 ? 21.283 -6.799  0.869   0.34 13.64 ?  127 LEU   A HG   1 
ATOM   2586 H HD11 A LEU   A 1 127 ? 23.461 -8.085  0.487   0.66 14.52 ?  127 LEU   A HD11 1 
ATOM   2587 H HD11 B LEU   A 1 127 ? 23.580 -7.327  0.844   0.34 14.38 ?  127 LEU   A HD11 1 
ATOM   2588 H HD12 A LEU   A 1 127 ? 22.567 -8.702  -0.673  0.66 14.52 ?  127 LEU   A HD12 1 
ATOM   2589 H HD12 B LEU   A 1 127 ? 22.735 -8.236  -0.147  0.34 14.38 ?  127 LEU   A HD12 1 
ATOM   2590 H HD13 A LEU   A 1 127 ? 23.572 -7.514  -0.992  0.66 14.52 ?  127 LEU   A HD13 1 
ATOM   2591 H HD13 B LEU   A 1 127 ? 23.595 -7.027  -0.715  0.34 14.38 ?  127 LEU   A HD13 1 
ATOM   2592 H HD21 A LEU   A 1 127 ? 23.088 -5.817  1.242   0.66 14.96 ?  127 LEU   A HD21 1 
ATOM   2593 H HD21 B LEU   A 1 127 ? 22.902 -5.158  1.460   0.34 13.86 ?  127 LEU   A HD21 1 
ATOM   2594 H HD22 A LEU   A 1 127 ? 22.995 -5.176  -0.209  0.66 14.96 ?  127 LEU   A HD22 1 
ATOM   2595 H HD22 B LEU   A 1 127 ? 22.770 -4.573  -0.011  0.34 13.86 ?  127 LEU   A HD22 1 
ATOM   2596 H HD23 A LEU   A 1 127 ? 21.785 -5.018  0.809   0.66 14.96 ?  127 LEU   A HD23 1 
ATOM   2597 H HD23 B LEU   A 1 127 ? 21.525 -4.533  0.974   0.34 13.86 ?  127 LEU   A HD23 1 
ATOM   2598 N N    A SER   A 1 128 ? 19.741 -4.365  -3.231  0.66 10.79 ?  128 SER   A N    1 
ATOM   2599 N N    B SER   A 1 128 ? 19.792 -4.372  -3.286  0.34 10.87 ?  128 SER   A N    1 
ATOM   2600 C CA   A SER   A 1 128 ? 19.346 -3.965  -4.573  0.66 10.76 ?  128 SER   A CA   1 
ATOM   2601 C CA   B SER   A 1 128 ? 19.439 -4.095  -4.677  0.34 10.58 ?  128 SER   A CA   1 
ATOM   2602 C C    A SER   A 1 128 ? 17.888 -3.526  -4.668  0.66 11.31 ?  128 SER   A C    1 
ATOM   2603 C C    B SER   A 1 128 ? 18.013 -3.582  -4.874  0.34 10.57 ?  128 SER   A C    1 
ATOM   2604 O O    A SER   A 1 128 ? 17.435 -3.201  -5.766  0.66 12.32 ?  128 SER   A O    1 
ATOM   2605 O O    B SER   A 1 128 ? 17.659 -3.227  -6.003  0.34 10.28 ?  128 SER   A O    1 
ATOM   2606 C CB   A SER   A 1 128 ? 19.692 -5.010  -5.643  0.66 10.90 ?  128 SER   A CB   1 
ATOM   2607 C CB   B SER   A 1 128 ? 19.727 -5.268  -5.625  0.34 11.02 ?  128 SER   A CB   1 
ATOM   2608 O OG   A SER   A 1 128 ? 21.099 -5.214  -5.699  0.66 11.04 ?  128 SER   A OG   1 
ATOM   2609 O OG   B SER   A 1 128 ? 21.125 -5.489  -5.745  0.34 10.92 ?  128 SER   A OG   1 
ATOM   2610 H H    A SER   A 1 128 ? 20.308 -3.814  -2.883  0.66 12.92 ?  128 SER   A H    1 
ATOM   2611 H H    B SER   A 1 128 ? 20.414 -3.844  -3.004  0.34 13.02 ?  128 SER   A H    1 
ATOM   2612 H HA   A SER   A 1 128 ? 19.873 -3.186  -4.791  0.66 12.89 ?  128 SER   A HA   1 
ATOM   2613 H HA   B SER   A 1 128 ? 20.017 -3.378  -4.964  0.34 12.67 ?  128 SER   A HA   1 
ATOM   2614 H HB2  A SER   A 1 128 ? 19.252 -5.848  -5.424  0.66 13.05 ?  128 SER   A HB2  1 
ATOM   2615 H HB2  B SER   A 1 128 ? 19.306 -6.068  -5.279  0.34 13.20 ?  128 SER   A HB2  1 
ATOM   2616 H HB3  A SER   A 1 128 ? 19.382 -4.689  -6.506  0.66 13.05 ?  128 SER   A HB3  1 
ATOM   2617 H HB3  B SER   A 1 128 ? 19.364 -5.055  -6.502  0.34 13.20 ?  128 SER   A HB3  1 
ATOM   2618 H HG   A SER   A 1 128 ? 21.482 -4.488  -5.875  0.66 13.22 ?  128 SER   A HG   1 
ATOM   2619 H HG   B SER   A 1 128 ? 21.495 -4.791  -6.038  0.34 13.08 ?  128 SER   A HG   1 
ATOM   2620 N N    A ALA   A 1 129 ? 17.161 -3.465  -3.554  0.66 11.91 ?  129 ALA   A N    1 
ATOM   2621 N N    B ALA   A 1 129 ? 17.199 -3.505  -3.825  0.34 10.74 ?  129 ALA   A N    1 
ATOM   2622 C CA   A ALA   A 1 129 ? 15.790 -2.978  -3.552  0.66 12.08 ?  129 ALA   A CA   1 
ATOM   2623 C CA   B ALA   A 1 129 ? 15.852 -2.961  -3.938  0.34 11.07 ?  129 ALA   A CA   1 
ATOM   2624 C C    A ALA   A 1 129 ? 15.771 -1.450  -3.514  0.66 11.22 ?  129 ALA   A C    1 
ATOM   2625 C C    B ALA   A 1 129 ? 15.908 -1.435  -3.838  0.34 11.43 ?  129 ALA   A C    1 
ATOM   2626 O O    A ALA   A 1 129 ? 16.808 -0.784  -3.575  0.66 11.26 ?  129 ALA   A O    1 
ATOM   2627 O O    B ALA   A 1 129 ? 16.981 -0.827  -3.861  0.34 12.05 ?  129 ALA   A O    1 
ATOM   2628 C CB   A ALA   A 1 129 ? 15.017 -3.576  -2.376  0.66 13.48 ?  129 ALA   A CB   1 
ATOM   2629 C CB   B ALA   A 1 129 ? 14.931 -3.609  -2.905  0.34 11.27 ?  129 ALA   A CB   1 
ATOM   2630 H H    A ALA   A 1 129 ? 17.447 -3.699  -2.777  0.66 14.26 ?  129 ALA   A H    1 
ATOM   2631 H H    B ALA   A 1 129 ? 17.403 -3.760  -3.030  0.34 12.86 ?  129 ALA   A H    1 
ATOM   2632 H HA   A ALA   A 1 129 ? 15.356 -3.259  -4.369  0.66 14.47 ?  129 ALA   A HA   1 
ATOM   2633 H HA   B ALA   A 1 129 ? 15.504 -3.173  -4.813  0.34 13.26 ?  129 ALA   A HA   1 
ATOM   2634 H HB1  A ALA   A 1 129 ? 14.102 -3.250  -2.402  0.66 16.15 ?  129 ALA   A HB1  1 
ATOM   2635 H HB1  B ALA   A 1 129 ? 14.040 -3.238  -3.001  0.34 13.50 ?  129 ALA   A HB1  1 
ATOM   2636 H HB2  A ALA   A 1 129 ? 15.027 -4.540  -2.450  0.66 16.15 ?  129 ALA   A HB2  1 
ATOM   2637 H HB2  B ALA   A 1 129 ? 14.910 -4.565  -3.059  0.34 13.50 ?  129 ALA   A HB2  1 
ATOM   2638 H HB3  A ALA   A 1 129 ? 15.440 -3.301  -1.546  0.66 16.15 ?  129 ALA   A HB3  1 
ATOM   2639 H HB3  B ALA   A 1 129 ? 15.272 -3.424  -2.015  0.34 13.50 ?  129 ALA   A HB3  1 
ATOM   2640 N N    A GLY   A 1 130 ? 14.572 -0.884  -3.413  0.66 11.71 ?  130 GLY   A N    1 
ATOM   2641 N N    B GLY   A 1 130 ? 14.746 -0.793  -3.745  0.34 11.60 ?  130 GLY   A N    1 
ATOM   2642 C CA   A GLY   A 1 130 ? 14.455 0.565   -3.362  0.66 11.84 ?  130 GLY   A CA   1 
ATOM   2643 C CA   B GLY   A 1 130 ? 14.732 0.659   -3.668  0.34 11.59 ?  130 GLY   A CA   1 
ATOM   2644 C C    A GLY   A 1 130 ? 15.068 1.206   -4.589  0.66 10.97 ?  130 GLY   A C    1 
ATOM   2645 C C    B GLY   A 1 130 ? 15.355 1.277   -4.903  0.34 11.87 ?  130 GLY   A C    1 
ATOM   2646 O O    A GLY   A 1 130 ? 14.833 0.778   -5.722  0.66 11.10 ?  130 GLY   A O    1 
ATOM   2647 O O    B GLY   A 1 130 ? 15.128 0.833   -6.034  0.34 12.33 ?  130 GLY   A O    1 
ATOM   2648 H H    A GLY   A 1 130 ? 13.826 -1.311  -3.380  0.66 14.03 ?  130 GLY   A H    1 
ATOM   2649 H H    B GLY   A 1 130 ? 13.970 -1.166  -3.733  0.34 13.90 ?  130 GLY   A H    1 
ATOM   2650 H HA2  A GLY   A 1 130 ? 13.515 0.814   -3.317  0.66 14.18 ?  130 GLY   A HA2  1 
ATOM   2651 H HA2  B GLY   A 1 130 ? 13.816 0.976   -3.587  0.34 13.89 ?  130 GLY   A HA2  1 
ATOM   2652 H HA3  A GLY   A 1 130 ? 14.904 0.904   -2.578  0.66 14.18 ?  130 GLY   A HA3  1 
ATOM   2653 H HA3  B GLY   A 1 130 ? 15.230 0.953   -2.889  0.34 13.89 ?  130 GLY   A HA3  1 
ATOM   2654 N N    A ILE   A 1 131 ? 15.869 2.255   -4.367  0.66 11.43 ?  131 ILE   A N    1 
ATOM   2655 N N    B ILE   A 1 131 ? 16.176 2.309   -4.684  0.34 11.91 ?  131 ILE   A N    1 
ATOM   2656 C CA   A ILE   A 1 131 ? 16.424 3.030   -5.473  0.66 11.34 ?  131 ILE   A CA   1 
ATOM   2657 C CA   B ILE   A 1 131 ? 16.783 3.047   -5.789  0.34 11.99 ?  131 ILE   A CA   1 
ATOM   2658 C C    A ILE   A 1 131 ? 17.452 2.268   -6.298  0.66 11.48 ?  131 ILE   A C    1 
ATOM   2659 C C    B ILE   A 1 131 ? 17.793 2.228   -6.578  0.34 11.73 ?  131 ILE   A C    1 
ATOM   2660 O O    A ILE   A 1 131 ? 17.854 2.766   -7.357  0.66 12.15 ?  131 ILE   A O    1 
ATOM   2661 O O    B ILE   A 1 131 ? 18.279 2.703   -7.612  0.34 11.89 ?  131 ILE   A O    1 
ATOM   2662 C CB   A ILE   A 1 131 ? 16.988 4.391   -5.008  0.66 12.85 ?  131 ILE   A CB   1 
ATOM   2663 C CB   B ILE   A 1 131 ? 17.405 4.384   -5.329  0.34 12.83 ?  131 ILE   A CB   1 
ATOM   2664 C CG1  A ILE   A 1 131 ? 18.214 4.211   -4.107  0.66 14.51 ?  131 ILE   A CG1  1 
ATOM   2665 C CG1  B ILE   A 1 131 ? 18.644 4.152   -4.455  0.34 13.66 ?  131 ILE   A CG1  1 
ATOM   2666 C CG2  A ILE   A 1 131 ? 15.908 5.191   -4.292  0.66 13.65 ?  131 ILE   A CG2  1 
ATOM   2667 C CG2  B ILE   A 1 131 ? 16.368 5.226   -4.593  0.34 13.23 ?  131 ILE   A CG2  1 
ATOM   2668 C CD1  A ILE   A 1 131 ? 18.863 5.528   -3.698  0.66 16.36 ?  131 ILE   A CD1  1 
ATOM   2669 C CD1  B ILE   A 1 131 ? 19.330 5.442   -3.998  0.34 14.39 ?  131 ILE   A CD1  1 
ATOM   2670 H H    A ILE   A 1 131 ? 16.094 2.538   -3.587  0.66 13.69 ?  131 ILE   A H    1 
ATOM   2671 H H    B ILE   A 1 131 ? 16.393 2.597   -3.905  0.34 14.27 ?  131 ILE   A H    1 
ATOM   2672 H HA   A ILE   A 1 131 ? 15.695 3.234   -6.074  0.66 13.58 ?  131 ILE   A HA   1 
ATOM   2673 H HA   B ILE   A 1 131 ? 16.081 3.271   -6.409  0.34 14.36 ?  131 ILE   A HA   1 
ATOM   2674 H HB   A ILE   A 1 131 ? 17.261 4.889   -5.793  0.66 15.39 ?  131 ILE   A HB   1 
ATOM   2675 H HB   B ILE   A 1 131 ? 17.681 4.875   -6.118  0.34 15.36 ?  131 ILE   A HB   1 
ATOM   2676 H HG12 A ILE   A 1 131 ? 17.944 3.748   -3.298  0.66 17.38 ?  131 ILE   A HG12 1 
ATOM   2677 H HG12 B ILE   A 1 131 ? 18.382 3.660   -3.663  0.34 16.37 ?  131 ILE   A HG12 1 
ATOM   2678 H HG13 A ILE   A 1 131 ? 18.881 3.688   -4.578  0.66 17.38 ?  131 ILE   A HG13 1 
ATOM   2679 H HG13 B ILE   A 1 131 ? 19.298 3.644   -4.958  0.34 16.37 ?  131 ILE   A HG13 1 
ATOM   2680 H HG21 A ILE   A 1 131 ? 16.220 6.099   -4.164  0.66 16.36 ?  131 ILE   A HG21 1 
ATOM   2681 H HG21 B ILE   A 1 131 ? 16.716 6.123   -4.469  0.34 15.84 ?  131 ILE   A HG21 1 
ATOM   2682 H HG22 A ILE   A 1 131 ? 15.106 5.188   -4.835  0.66 16.36 ?  131 ILE   A HG22 1 
ATOM   2683 H HG22 B ILE   A 1 131 ? 15.557 5.258   -5.125  0.34 15.84 ?  131 ILE   A HG22 1 
ATOM   2684 H HG23 A ILE   A 1 131 ? 15.729 4.776   -3.433  0.66 16.36 ?  131 ILE   A HG23 1 
ATOM   2685 H HG23 B ILE   A 1 131 ? 16.183 4.819   -3.733  0.34 15.84 ?  131 ILE   A HG23 1 
ATOM   2686 H HD11 A ILE   A 1 131 ? 19.701 5.340   -3.243  0.66 19.60 ?  131 ILE   A HD11 1 
ATOM   2687 H HD11 B ILE   A 1 131 ? 20.166 5.218   -3.558  0.34 17.25 ?  131 ILE   A HD11 1 
ATOM   2688 H HD12 A ILE   A 1 131 ? 19.034 6.057   -4.494  0.66 19.60 ?  131 ILE   A HD12 1 
ATOM   2689 H HD12 B ILE   A 1 131 ? 19.504 6.002   -4.771  0.34 17.25 ?  131 ILE   A HD12 1 
ATOM   2690 H HD13 A ILE   A 1 131 ? 18.266 6.008   -3.104  0.66 19.60 ?  131 ILE   A HD13 1 
ATOM   2691 H HD13 B ILE   A 1 131 ? 18.748 5.910   -3.376  0.34 17.25 ?  131 ILE   A HD13 1 
ATOM   2692 N N    A PHE   A 1 132 ? 17.889 1.080   -5.858  0.66 11.13 ?  132 PHE   A N    1 
ATOM   2693 N N    B PHE   A 1 132 ? 18.132 1.017   -6.125  0.34 11.88 ?  132 PHE   A N    1 
ATOM   2694 C CA   A PHE   A 1 132 ? 18.755 0.246   -6.686  0.66 11.38 ?  132 PHE   A CA   1 
ATOM   2695 C CA   B PHE   A 1 132 ? 19.018 0.153   -6.897  0.34 12.27 ?  132 PHE   A CA   1 
ATOM   2696 C C    A PHE   A 1 132 ? 17.984 -0.510  -7.772  0.66 11.55 ?  132 PHE   A C    1 
ATOM   2697 C C    B PHE   A 1 132 ? 18.292 -0.598  -8.013  0.34 13.00 ?  132 PHE   A C    1 
ATOM   2698 O O    A PHE   A 1 132 ? 18.604 -1.146  -8.629  0.66 12.87 ?  132 PHE   A O    1 
ATOM   2699 O O    B PHE   A 1 132 ? 18.954 -1.241  -8.837  0.34 14.18 ?  132 PHE   A O    1 
ATOM   2700 C CB   A PHE   A 1 132 ? 19.556 -0.733  -5.817  0.66 11.27 ?  132 PHE   A CB   1 
ATOM   2701 C CB   B PHE   A 1 132 ? 19.760 -0.826  -5.980  0.34 11.74 ?  132 PHE   A CB   1 
ATOM   2702 C CG   A PHE   A 1 132 ? 20.806 -0.145  -5.173  0.66 11.31 ?  132 PHE   A CG   1 
ATOM   2703 C CG   B PHE   A 1 132 ? 20.912 -0.209  -5.215  0.34 11.66 ?  132 PHE   A CG   1 
ATOM   2704 C CD1  A PHE   A 1 132 ? 20.732 0.906   -4.273  0.66 12.45 ?  132 PHE   A CD1  1 
ATOM   2705 C CD1  B PHE   A 1 132 ? 20.694 0.775   -4.264  0.34 12.29 ?  132 PHE   A CD1  1 
ATOM   2706 C CD2  A PHE   A 1 132 ? 22.050 -0.707  -5.428  0.66 12.40 ?  132 PHE   A CD2  1 
ATOM   2707 C CD2  B PHE   A 1 132 ? 22.210 -0.646  -5.428  0.34 11.76 ?  132 PHE   A CD2  1 
ATOM   2708 C CE1  A PHE   A 1 132 ? 21.875 1.410   -3.674  0.66 12.71 ?  132 PHE   A CE1  1 
ATOM   2709 C CE1  B PHE   A 1 132 ? 21.749 1.324   -3.557  0.34 12.18 ?  132 PHE   A CE1  1 
ATOM   2710 C CE2  A PHE   A 1 132 ? 23.197 -0.215  -4.825  0.66 13.03 ?  132 PHE   A CE2  1 
ATOM   2711 C CE2  B PHE   A 1 132 ? 23.269 -0.104  -4.721  0.34 11.79 ?  132 PHE   A CE2  1 
ATOM   2712 C CZ   A PHE   A 1 132 ? 23.105 0.848   -3.948  0.66 12.91 ?  132 PHE   A CZ   1 
ATOM   2713 C CZ   B PHE   A 1 132 ? 23.036 0.884   -3.785  0.34 11.70 ?  132 PHE   A CZ   1 
ATOM   2714 H H    A PHE   A 1 132 ? 17.696 0.740   -5.090  0.66 13.32 ?  132 PHE   A H    1 
ATOM   2715 H H    B PHE   A 1 132 ? 17.865 0.680   -5.374  0.34 14.22 ?  132 PHE   A H    1 
ATOM   2716 H HA   A PHE   A 1 132 ? 19.396 0.821   -7.129  0.66 13.63 ?  132 PHE   A HA   1 
ATOM   2717 H HA   B PHE   A 1 132 ? 19.690 0.713   -7.309  0.34 14.70 ?  132 PHE   A HA   1 
ATOM   2718 H HB2  A PHE   A 1 132 ? 18.986 -1.054  -5.100  0.66 13.50 ?  132 PHE   A HB2  1 
ATOM   2719 H HB2  B PHE   A 1 132 ? 19.137 -1.181  -5.329  0.34 14.07 ?  132 PHE   A HB2  1 
ATOM   2720 H HB3  A PHE   A 1 132 ? 19.836 -1.483  -6.369  0.66 13.50 ?  132 PHE   A HB3  1 
ATOM   2721 H HB3  B PHE   A 1 132 ? 20.119 -1.549  -6.520  0.34 14.07 ?  132 PHE   A HB3  1 
ATOM   2722 H HD1  A PHE   A 1 132 ? 19.905 1.283   -4.081  0.66 14.91 ?  132 PHE   A HD1  1 
ATOM   2723 H HD1  B PHE   A 1 132 ? 19.829 1.076   -4.105  0.34 14.72 ?  132 PHE   A HD1  1 
ATOM   2724 H HD2  A PHE   A 1 132 ? 22.123 -1.427  -6.018  0.66 14.86 ?  132 PHE   A HD2  1 
ATOM   2725 H HD2  B PHE   A 1 132 ? 22.373 -1.314  -6.057  0.34 14.08 ?  132 PHE   A HD2  1 
ATOM   2726 H HE1  A PHE   A 1 132 ? 21.812 2.120   -3.078  0.66 15.22 ?  132 PHE   A HE1  1 
ATOM   2727 H HE1  B PHE   A 1 132 ? 21.592 1.989   -2.926  0.34 14.59 ?  132 PHE   A HE1  1 
ATOM   2728 H HE2  A PHE   A 1 132 ? 24.029 -0.593  -5.017  0.66 15.61 ?  132 PHE   A HE2  1 
ATOM   2729 H HE2  B PHE   A 1 132 ? 24.135 -0.404  -4.880  0.34 14.12 ?  132 PHE   A HE2  1 
ATOM   2730 H HZ   A PHE   A 1 132 ? 23.872 1.186   -3.546  0.66 15.46 ?  132 PHE   A HZ   1 
ATOM   2731 H HZ   B PHE   A 1 132 ? 23.746 1.251   -3.312  0.34 14.02 ?  132 PHE   A HZ   1 
ATOM   2732 N N    A GLY   A 1 133 ? 16.654 -0.469  -7.756  0.66 11.65 ?  133 GLY   A N    1 
ATOM   2733 N N    B GLY   A 1 133 ? 16.957 -0.547  -8.055  0.34 12.53 ?  133 GLY   A N    1 
ATOM   2734 C CA   A GLY   A 1 133 ? 15.863 -0.833  -8.918  0.66 12.47 ?  133 GLY   A CA   1 
ATOM   2735 C CA   B GLY   A 1 133 ? 16.198 -0.919  -9.230  0.34 12.31 ?  133 GLY   A CA   1 
ATOM   2736 C C    A GLY   A 1 133 ? 15.586 -2.305  -9.147  0.66 13.79 ?  133 GLY   A C    1 
ATOM   2737 C C    B GLY   A 1 133 ? 15.565 -2.298  -9.207  0.34 12.77 ?  133 GLY   A C    1 
ATOM   2738 O O    A GLY   A 1 133 ? 15.056 -2.646  -10.211 0.66 14.85 ?  133 GLY   A O    1 
ATOM   2739 O O    B GLY   A 1 133 ? 14.613 -2.532  -9.963  0.34 12.70 ?  133 GLY   A O    1 
ATOM   2740 H H    A GLY   A 1 133 ? 16.186 -0.220  -7.082  0.66 13.95 ?  133 GLY   A H    1 
ATOM   2741 H H    B GLY   A 1 133 ? 16.467 -0.290  -7.395  0.34 15.01 ?  133 GLY   A H    1 
ATOM   2742 H HA2  A GLY   A 1 133 ? 15.003 -0.392  -8.852  0.66 14.93 ?  133 GLY   A HA2  1 
ATOM   2743 H HA2  B GLY   A 1 133 ? 15.485 -0.278  -9.356  0.34 14.75 ?  133 GLY   A HA2  1 
ATOM   2744 H HA3  A GLY   A 1 133 ? 16.306 -0.497  -9.712  0.66 14.93 ?  133 GLY   A HA3  1 
ATOM   2745 H HA3  B GLY   A 1 133 ? 16.779 -0.863  -10.004 0.34 14.75 ?  133 GLY   A HA3  1 
ATOM   2746 N N    A ALA   A 1 134 ? 15.922 -3.189  -8.210  0.66 13.52 ?  134 ALA   A N    1 
ATOM   2747 N N    B ALA   A 1 134 ? 16.057 -3.214  -8.378  0.34 12.95 ?  134 ALA   A N    1 
ATOM   2748 C CA   A ALA   A 1 134 ? 15.617 -4.600  -8.392  0.66 14.23 ?  134 ALA   A CA   1 
ATOM   2749 C CA   B ALA   A 1 134 ? 15.586 -4.588  -8.456  0.34 13.09 ?  134 ALA   A CA   1 
ATOM   2750 C C    A ALA   A 1 134 ? 14.252 -4.939  -7.790  0.66 14.52 ?  134 ALA   A C    1 
ATOM   2751 C C    B ALA   A 1 134 ? 14.274 -4.777  -7.695  0.34 13.09 ?  134 ALA   A C    1 
ATOM   2752 O O    A ALA   A 1 134 ? 13.661 -4.165  -7.035  0.66 15.47 ?  134 ALA   A O    1 
ATOM   2753 O O    B ALA   A 1 134 ? 13.873 -3.958  -6.862  0.34 13.75 ?  134 ALA   A O    1 
ATOM   2754 C CB   A ALA   A 1 134 ? 16.707 -5.483  -7.787  0.66 15.71 ?  134 ALA   A CB   1 
ATOM   2755 C CB   B ALA   A 1 134 ? 16.639 -5.556  -7.921  0.34 13.67 ?  134 ALA   A CB   1 
ATOM   2756 H H    A ALA   A 1 134 ? 16.332 -2.998  -7.475  0.66 16.20 ?  134 ALA   A H    1 
ATOM   2757 H H    B ALA   A 1 134 ? 16.656 -3.066  -7.776  0.34 15.51 ?  134 ALA   A H    1 
ATOM   2758 H HA   A ALA   A 1 134 ? 15.578 -4.790  -9.344  0.66 17.04 ?  134 ALA   A HA   1 
ATOM   2759 H HA   B ALA   A 1 134 ? 15.425 -4.804  -9.387  0.34 15.68 ?  134 ALA   A HA   1 
ATOM   2760 H HB1  A ALA   A 1 134 ? 16.483 -6.411  -7.951  0.66 18.82 ?  134 ALA   A HB1  1 
ATOM   2761 H HB1  B ALA   A 1 134 ? 16.298 -6.460  -7.999  0.34 16.38 ?  134 ALA   A HB1  1 
ATOM   2762 H HB2  A ALA   A 1 134 ? 17.556 -5.267  -8.208  0.66 18.82 ?  134 ALA   A HB2  1 
ATOM   2763 H HB2  B ALA   A 1 134 ? 17.448 -5.458  -8.447  0.34 16.38 ?  134 ALA   A HB2  1 
ATOM   2764 H HB3  A ALA   A 1 134 ? 16.757 -5.313  -6.836  0.66 18.82 ?  134 ALA   A HB3  1 
ATOM   2765 H HB3  B ALA   A 1 134 ? 16.817 -5.345  -6.993  0.34 16.38 ?  134 ALA   A HB3  1 
ATOM   2766 N N    A ASP   A 1 135 ? 13.749 -6.117  -8.147  0.66 14.92 ?  135 ASP   A N    1 
ATOM   2767 N N    B ASP   A 1 135 ? 13.609 -5.889  -7.999  0.34 13.37 ?  135 ASP   A N    1 
ATOM   2768 C CA   A ASP   A 1 135 ? 12.487 -6.614  -7.602  0.66 15.37 ?  135 ASP   A CA   1 
ATOM   2769 C CA   B ASP   A 1 135 ? 12.341 -6.239  -7.369  0.34 13.97 ?  135 ASP   A CA   1 
ATOM   2770 C C    A ASP   A 1 135 ? 12.711 -7.068  -6.167  0.66 14.42 ?  135 ASP   A C    1 
ATOM   2771 C C    B ASP   A 1 135 ? 12.598 -6.708  -5.942  0.34 13.23 ?  135 ASP   A C    1 
ATOM   2772 O O    A ASP   A 1 135 ? 13.494 -7.999  -5.940  0.66 14.42 ?  135 ASP   A O    1 
ATOM   2773 O O    B ASP   A 1 135 ? 13.334 -7.684  -5.744  0.34 12.97 ?  135 ASP   A O    1 
ATOM   2774 C CB   A ASP   A 1 135 ? 12.019 -7.797  -8.444  0.66 17.32 ?  135 ASP   A CB   1 
ATOM   2775 C CB   B ASP   A 1 135 ? 11.685 -7.361  -8.168  0.34 15.23 ?  135 ASP   A CB   1 
ATOM   2776 C CG   A ASP   A 1 135 ? 10.721 -8.428  -7.939  0.66 19.28 ?  135 ASP   A CG   1 
ATOM   2777 C CG   B ASP   A 1 135 ? 10.275 -7.683  -7.691  0.34 16.86 ?  135 ASP   A CG   1 
ATOM   2778 O OD1  A ASP   A 1 135 ? 10.155 -7.971  -6.926  0.66 19.43 ?  135 ASP   A OD1  1 
ATOM   2779 O OD1  B ASP   A 1 135 ? 9.924  -7.328  -6.544  0.34 17.37 ?  135 ASP   A OD1  1 
ATOM   2780 O OD2  A ASP   A 1 135 ? 10.263 -9.399  -8.578  0.66 21.87 -1 135 ASP   A OD2  1 
ATOM   2781 O OD2  B ASP   A 1 135 ? 9.519  -8.309  -8.467  0.34 18.08 -1 135 ASP   A OD2  1 
ATOM   2782 H H    A ASP   A 1 135 ? 14.123 -6.648  -8.709  0.66 17.87 ?  135 ASP   A H    1 
ATOM   2783 H H    B ASP   A 1 135 ? 13.873 -6.464  -8.577  0.34 16.02 ?  135 ASP   A H    1 
ATOM   2784 H HA   A ASP   A 1 135 ? 11.821 -5.911  -7.635  0.66 18.42 ?  135 ASP   A HA   1 
ATOM   2785 H HA   B ASP   A 1 135 ? 11.747 -5.470  -7.375  0.34 16.74 ?  135 ASP   A HA   1 
ATOM   2786 H HB2  A ASP   A 1 135 ? 11.864 -7.496  -9.346  0.66 20.75 ?  135 ASP   A HB2  1 
ATOM   2787 H HB2  B ASP   A 1 135 ? 11.647 -7.102  -9.102  0.34 18.24 ?  135 ASP   A HB2  1 
ATOM   2788 H HB3  A ASP   A 1 135 ? 12.703 -8.481  -8.425  0.66 20.75 ?  135 ASP   A HB3  1 
ATOM   2789 H HB3  B ASP   A 1 135 ? 12.212 -8.167  -8.068  0.34 18.24 ?  135 ASP   A HB3  1 
ATOM   2790 N N    A PRO   A 1 136 ? 12.060 -6.454  -5.177  0.66 14.03 ?  136 PRO   A N    1 
ATOM   2791 N N    B PRO   A 1 136 ? 12.021 -6.061  -4.928  0.34 13.12 ?  136 PRO   A N    1 
ATOM   2792 C CA   A PRO   A 1 136 ? 12.298 -6.867  -3.782  0.66 14.18 ?  136 PRO   A CA   1 
ATOM   2793 C CA   B PRO   A 1 136 ? 12.257 -6.507  -3.545  0.34 13.07 ?  136 PRO   A CA   1 
ATOM   2794 C C    A PRO   A 1 136 ? 11.879 -8.296  -3.474  0.66 13.65 ?  136 PRO   A C    1 
ATOM   2795 C C    B PRO   A 1 136 ? 11.829 -7.939  -3.278  0.34 12.69 ?  136 PRO   A C    1 
ATOM   2796 O O    A PRO   A 1 136 ? 12.485 -8.930  -2.601  0.66 13.49 ?  136 PRO   A O    1 
ATOM   2797 O O    B PRO   A 1 136 ? 12.414 -8.598  -2.409  0.34 11.67 ?  136 PRO   A O    1 
ATOM   2798 C CB   A PRO   A 1 136 ? 11.503 -5.836  -2.968  0.66 15.19 ?  136 PRO   A CB   1 
ATOM   2799 C CB   B PRO   A 1 136 ? 11.457 -5.494  -2.711  0.34 13.78 ?  136 PRO   A CB   1 
ATOM   2800 C CG   A PRO   A 1 136 ? 10.461 -5.329  -3.917  0.66 15.87 ?  136 PRO   A CG   1 
ATOM   2801 C CG   B PRO   A 1 136 ? 10.454 -4.922  -3.667  0.34 14.54 ?  136 PRO   A CG   1 
ATOM   2802 C CD   A PRO   A 1 136 ? 11.077 -5.361  -5.277  0.66 15.03 ?  136 PRO   A CD   1 
ATOM   2803 C CD   B PRO   A 1 136 ? 11.158 -4.871  -4.977  0.34 13.94 ?  136 PRO   A CD   1 
ATOM   2804 H HA   A PRO   A 1 136 ? 13.239 -6.769  -3.562  0.66 16.99 ?  136 PRO   A HA   1 
ATOM   2805 H HA   B PRO   A 1 136 ? 13.196 -6.414  -3.324  0.34 15.66 ?  136 PRO   A HA   1 
ATOM   2806 H HB2  A PRO   A 1 136 ? 11.089 -6.264  -2.202  0.66 18.20 ?  136 PRO   A HB2  1 
ATOM   2807 H HB2  B PRO   A 1 136 ? 11.013 -5.944  -1.978  0.34 16.51 ?  136 PRO   A HB2  1 
ATOM   2808 H HB3  A PRO   A 1 136 ? 12.090 -5.116  -2.682  0.66 18.20 ?  136 PRO   A HB3  1 
ATOM   2809 H HB3  B PRO   A 1 136 ? 12.049 -4.796  -2.382  0.34 16.51 ?  136 PRO   A HB3  1 
ATOM   2810 H HG2  A PRO   A 1 136 ? 9.685  -5.904  -3.886  0.66 19.02 ?  136 PRO   A HG2  1 
ATOM   2811 H HG2  B PRO   A 1 136 ? 9.682  -5.508  -3.723  0.34 17.42 ?  136 PRO   A HG2  1 
ATOM   2812 H HG3  A PRO   A 1 136 ? 10.221 -4.418  -3.680  0.66 19.02 ?  136 PRO   A HG3  1 
ATOM   2813 H HG3  B PRO   A 1 136 ? 10.194 -4.033  -3.387  0.34 17.42 ?  136 PRO   A HG3  1 
ATOM   2814 H HD2  A PRO   A 1 136 ? 10.402 -5.573  -5.945  0.66 18.01 ?  136 PRO   A HD2  1 
ATOM   2815 H HD2  B PRO   A 1 136 ? 10.519 -4.939  -5.706  0.34 16.70 ?  136 PRO   A HD2  1 
ATOM   2816 H HD3  A PRO   A 1 136 ? 11.518 -4.520  -5.474  0.66 18.01 ?  136 PRO   A HD3  1 
ATOM   2817 H HD3  B PRO   A 1 136 ? 11.695 -4.064  -5.049  0.34 16.70 ?  136 PRO   A HD3  1 
ATOM   2818 N N    A ILE   A 1 137 ? 10.847 -8.819  -4.141  0.66 13.40 ?  137 ILE   A N    1 
ATOM   2819 N N    B ILE   A 1 137 ? 10.814 -8.438  -3.989  0.34 12.86 ?  137 ILE   A N    1 
ATOM   2820 C CA   A ILE   A 1 137 ? 10.479 -10.216 -3.927  0.66 13.94 ?  137 ILE   A CA   1 
ATOM   2821 C CA   B ILE   A 1 137 ? 10.424 -9.839  -3.843  0.34 13.01 ?  137 ILE   A CA   1 
ATOM   2822 C C    A ILE   A 1 137 ? 11.636 -11.123 -4.320  0.66 13.72 ?  137 ILE   A C    1 
ATOM   2823 C C    B ILE   A 1 137 ? 11.574 -10.751 -4.253  0.34 12.63 ?  137 ILE   A C    1 
ATOM   2824 O O    A ILE   A 1 137 ? 11.965 -12.085 -3.614  0.66 13.95 ?  137 ILE   A O    1 
ATOM   2825 O O    B ILE   A 1 137 ? 11.843 -11.772 -3.607  0.34 12.61 ?  137 ILE   A O    1 
ATOM   2826 C CB   A ILE   A 1 137 ? 9.188  -10.560 -4.695  0.66 15.29 ?  137 ILE   A CB   1 
ATOM   2827 C CB   B ILE   A 1 137 ? 9.146  -10.118 -4.658  0.34 14.45 ?  137 ILE   A CB   1 
ATOM   2828 C CG1  A ILE   A 1 137 ? 8.014  -9.720  -4.182  0.66 17.57 ?  137 ILE   A CG1  1 
ATOM   2829 C CG1  B ILE   A 1 137 ? 7.990  -9.248  -4.143  0.34 15.67 ?  137 ILE   A CG1  1 
ATOM   2830 C CG2  A ILE   A 1 137 ? 8.879  -12.046 -4.565  0.66 16.25 ?  137 ILE   A CG2  1 
ATOM   2831 C CG2  B ILE   A 1 137 ? 8.800  -11.607 -4.624  0.34 14.89 ?  137 ILE   A CG2  1 
ATOM   2832 C CD1  A ILE   A 1 137 ? 6.730  -9.912  -4.963  0.66 19.13 ?  137 ILE   A CD1  1 
ATOM   2833 C CD1  B ILE   A 1 137 ? 6.754  -9.278  -5.016  0.34 16.46 ?  137 ILE   A CD1  1 
ATOM   2834 H H    A ILE   A 1 137 ? 10.359 -8.396  -4.706  0.66 16.05 ?  137 ILE   A H    1 
ATOM   2835 H H    B ILE   A 1 137 ? 10.339 -7.987  -4.549  0.34 15.41 ?  137 ILE   A H    1 
ATOM   2836 H HA   A ILE   A 1 137 ? 10.304 -10.354 -2.985  0.66 16.70 ?  137 ILE   A HA   1 
ATOM   2837 H HA   B ILE   A 1 137 ? 10.222 -10.009 -2.910  0.34 15.58 ?  137 ILE   A HA   1 
ATOM   2838 H HB   A ILE   A 1 137 ? 9.322  -10.357 -5.632  0.66 18.32 ?  137 ILE   A HB   1 
ATOM   2839 H HB   B ILE   A 1 137 ? 9.316  -9.871  -5.578  0.34 17.32 ?  137 ILE   A HB   1 
ATOM   2840 H HG12 A ILE   A 1 137 ? 7.840  -9.955  -3.258  0.66 21.06 ?  137 ILE   A HG12 1 
ATOM   2841 H HG12 B ILE   A 1 137 ? 7.735  -9.555  -3.261  0.34 18.78 ?  137 ILE   A HG12 1 
ATOM   2842 H HG13 A ILE   A 1 137 ? 8.257  -8.779  -4.240  0.66 21.06 ?  137 ILE   A HG13 1 
ATOM   2843 H HG13 B ILE   A 1 137 ? 8.287  -8.325  -4.096  0.34 18.78 ?  137 ILE   A HG13 1 
ATOM   2844 H HG21 A ILE   A 1 137 ? 7.982  -12.225 -4.889  0.66 19.48 ?  137 ILE   A HG21 1 
ATOM   2845 H HG21 B ILE   A 1 137 ? 7.903  -11.734 -4.970  0.34 17.84 ?  137 ILE   A HG21 1 
ATOM   2846 H HG22 A ILE   A 1 137 ? 9.519  -12.547 -5.091  0.66 19.48 ?  137 ILE   A HG22 1 
ATOM   2847 H HG22 B ILE   A 1 137 ? 9.435  -12.092 -5.176  0.34 17.84 ?  137 ILE   A HG22 1 
ATOM   2848 H HG23 A ILE   A 1 137 ? 8.944  -12.297 -3.632  0.66 19.48 ?  137 ILE   A HG23 1 
ATOM   2849 H HG23 B ILE   A 1 137 ? 8.847  -11.923 -3.709  0.34 17.84 ?  137 ILE   A HG23 1 
ATOM   2850 H HD11 A ILE   A 1 137 ? 6.036  -10.216 -4.359  0.66 22.93 ?  137 ILE   A HD11 1 
ATOM   2851 H HD11 B ILE   A 1 137 ? 6.505  -8.368  -5.245  0.34 19.73 ?  137 ILE   A HD11 1 
ATOM   2852 H HD12 A ILE   A 1 137 ? 6.484  -9.063  -5.357  0.66 22.93 ?  137 ILE   A HD12 1 
ATOM   2853 H HD12 B ILE   A 1 137 ? 6.947  -9.780  -5.823  0.34 19.73 ?  137 ILE   A HD12 1 
ATOM   2854 H HD13 A ILE   A 1 137 ? 6.874  -10.565 -5.664  0.66 22.93 ?  137 ILE   A HD13 1 
ATOM   2855 H HD13 B ILE   A 1 137 ? 6.032  -9.705  -4.526  0.34 19.73 ?  137 ILE   A HD13 1 
ATOM   2856 N N    A HIS   A 1 138 ? 12.271 -10.827 -5.453  0.66 13.18 ?  138 HIS   A N    1 
ATOM   2857 N N    B HIS   A 1 138 ? 12.266 -10.396 -5.337  0.34 12.59 ?  138 HIS   A N    1 
ATOM   2858 C CA   A HIS   A 1 138 ? 13.441 -11.589 -5.868  0.66 13.31 ?  138 HIS   A CA   1 
ATOM   2859 C CA   B HIS   A 1 138 ? 13.427 -11.166 -5.774  0.34 11.93 ?  138 HIS   A CA   1 
ATOM   2860 C C    A HIS   A 1 138 ? 14.581 -11.438 -4.870  0.66 12.77 ?  138 HIS   A C    1 
ATOM   2861 C C    B HIS   A 1 138 ? 14.574 -11.054 -4.774  0.34 11.71 ?  138 HIS   A C    1 
ATOM   2862 O O    A HIS   A 1 138 ? 15.240 -12.424 -4.514  0.66 13.13 ?  138 HIS   A O    1 
ATOM   2863 O O    B HIS   A 1 138 ? 15.259 -12.045 -4.490  0.34 12.10 ?  138 HIS   A O    1 
ATOM   2864 C CB   A HIS   A 1 138 ? 13.875 -11.151 -7.262  0.66 14.33 ?  138 HIS   A CB   1 
ATOM   2865 C CB   B HIS   A 1 138 ? 13.852 -10.682 -7.161  0.34 12.39 ?  138 HIS   A CB   1 
ATOM   2866 C CG   A HIS   A 1 138 ? 15.151 -11.785 -7.711  0.66 15.44 ?  138 HIS   A CG   1 
ATOM   2867 C CG   B HIS   A 1 138 ? 15.102 -11.325 -7.674  0.34 13.04 ?  138 HIS   A CG   1 
ATOM   2868 N ND1  A HIS   A 1 138 ? 15.266 -13.140 -7.940  0.66 16.91 ?  138 HIS   A ND1  1 
ATOM   2869 N ND1  B HIS   A 1 138 ? 15.184 -12.670 -7.962  0.34 13.80 ?  138 HIS   A ND1  1 
ATOM   2870 C CD2  A HIS   A 1 138 ? 16.373 -11.256 -7.949  0.66 15.66 ?  138 HIS   A CD2  1 
ATOM   2871 C CD2  B HIS   A 1 138 ? 16.320 -10.805 -7.954  0.34 13.57 ?  138 HIS   A CD2  1 
ATOM   2872 C CE1  A HIS   A 1 138 ? 16.502 -13.415 -8.312  0.66 17.60 ?  138 HIS   A CE1  1 
ATOM   2873 C CE1  B HIS   A 1 138 ? 16.401 -12.952 -8.394  0.34 14.17 ?  138 HIS   A CE1  1 
ATOM   2874 N NE2  A HIS   A 1 138 ? 17.194 -12.290 -8.327  0.66 16.70 ?  138 HIS   A NE2  1 
ATOM   2875 N NE2  B HIS   A 1 138 ? 17.110 -11.837 -8.398  0.34 14.06 ?  138 HIS   A NE2  1 
ATOM   2876 H H    A HIS   A 1 138 ? 12.044 -10.194 -5.992  0.66 15.79 ?  138 HIS   A H    1 
ATOM   2877 H H    B HIS   A 1 138 ? 12.076 -9.721  -5.836  0.34 15.08 ?  138 HIS   A H    1 
ATOM   2878 H HA   A HIS   A 1 138 ? 13.202 -12.526 -5.912  0.66 15.95 ?  138 HIS   A HA   1 
ATOM   2879 H HA   B HIS   A 1 138 ? 13.176 -12.096 -5.844  0.34 14.28 ?  138 HIS   A HA   1 
ATOM   2880 H HB2  A HIS   A 1 138 ? 13.177 -11.391 -7.895  0.66 17.17 ?  138 HIS   A HB2  1 
ATOM   2881 H HB2  B HIS   A 1 138 ? 13.139 -10.876 -7.791  0.34 14.84 ?  138 HIS   A HB2  1 
ATOM   2882 H HB3  A HIS   A 1 138 ? 13.999 -10.188 -7.263  0.66 17.17 ?  138 HIS   A HB3  1 
ATOM   2883 H HB3  B HIS   A 1 138 ? 14.005 -9.724  -7.127  0.34 14.84 ?  138 HIS   A HB3  1 
ATOM   2884 H HD1  A HIS   A 1 138 ? 14.627 -13.712 -7.859  0.66 20.27 ?  138 HIS   A HD1  1 
ATOM   2885 H HD2  A HIS   A 1 138 ? 16.604 -10.357 -7.873  0.66 18.77 ?  138 HIS   A HD2  1 
ATOM   2886 H HD2  B HIS   A 1 138 ? 16.575 -9.916  -7.862  0.34 16.26 ?  138 HIS   A HD2  1 
ATOM   2887 H HE1  A HIS   A 1 138 ? 16.827 -14.254 -8.527  0.66 21.10 ?  138 HIS   A HE1  1 
ATOM   2888 H HE1  B HIS   A 1 138 ? 16.704 -13.793 -8.650  0.34 16.98 ?  138 HIS   A HE1  1 
ATOM   2889 H HE2  B HIS   A 1 138 ? 17.932 -11.771 -8.642  0.34 16.84 ?  138 HIS   A HE2  1 
ATOM   2890 N N    A SER   A 1 139 ? 14.834 -10.214 -4.407  0.66 12.19 ?  139 SER   A N    1 
ATOM   2891 N N    B SER   A 1 139 ? 14.792 -9.858  -4.222  0.34 11.77 ?  139 SER   A N    1 
ATOM   2892 C CA   A SER   A 1 139 ? 15.911 -10.011 -3.448  0.66 12.15 ?  139 SER   A CA   1 
ATOM   2893 C CA   B SER   A 1 139 ? 15.845 -9.679  -3.229  0.34 11.35 ?  139 SER   A CA   1 
ATOM   2894 C C    A SER   A 1 139 ? 15.691 -10.822 -2.176  0.66 12.27 ?  139 SER   A C    1 
ATOM   2895 C C    B SER   A 1 139 ? 15.632 -10.586 -2.022  0.34 11.24 ?  139 SER   A C    1 
ATOM   2896 O O    A SER   A 1 139 ? 16.630 -11.442 -1.665  0.66 11.68 ?  139 SER   A O    1 
ATOM   2897 O O    B SER   A 1 139 ? 16.597 -11.109 -1.451  0.34 11.25 ?  139 SER   A O    1 
ATOM   2898 C CB   A SER   A 1 139 ? 16.064 -8.530  -3.119  0.66 11.68 ?  139 SER   A CB   1 
ATOM   2899 C CB   B SER   A 1 139 ? 15.917 -8.210  -2.810  0.34 10.78 ?  139 SER   A CB   1 
ATOM   2900 O OG   A SER   A 1 139 ? 17.146 -8.357  -2.219  0.66 11.41 ?  139 SER   A OG   1 
ATOM   2901 O OG   B SER   A 1 139 ? 16.942 -8.022  -1.849  0.34 10.86 ?  139 SER   A OG   1 
ATOM   2902 H H    A SER   A 1 139 ? 14.409 -9.500  -4.630  0.66 14.60 ?  139 SER   A H    1 
ATOM   2903 H H    B SER   A 1 139 ? 14.354 -9.142  -4.401  0.34 14.10 ?  139 SER   A H    1 
ATOM   2904 H HA   A SER   A 1 139 ? 16.744 -10.308 -3.850  0.66 14.56 ?  139 SER   A HA   1 
ATOM   2905 H HA   B SER   A 1 139 ? 16.701 -9.914  -3.619  0.34 13.59 ?  139 SER   A HA   1 
ATOM   2906 H HB2  A SER   A 1 139 ? 16.251 -8.036  -3.936  0.66 13.99 ?  139 SER   A HB2  1 
ATOM   2907 H HB2  B SER   A 1 139 ? 16.102 -7.663  -3.597  0.34 12.91 ?  139 SER   A HB2  1 
ATOM   2908 H HB3  A SER   A 1 139 ? 15.248 -8.205  -2.711  0.66 13.99 ?  139 SER   A HB3  1 
ATOM   2909 H HB3  B SER   A 1 139 ? 15.069 -7.942  -2.423  0.34 12.91 ?  139 SER   A HB3  1 
ATOM   2910 H HG   A SER   A 1 139 ? 17.236 -7.542  -2.027  0.66 13.67 ?  139 SER   A HG   1 
ATOM   2911 H HG   B SER   A 1 139 ? 17.696 -8.071  -2.218  0.34 13.00 ?  139 SER   A HG   1 
ATOM   2912 N N    A LEU   A 1 140 ? 14.466 -10.819 -1.640  0.66 12.55 ?  140 LEU   A N    1 
ATOM   2913 N N    B LEU   A 1 140 ? 14.374 -10.794 -1.622  0.34 11.64 ?  140 LEU   A N    1 
ATOM   2914 C CA   A LEU   A 1 140 ? 14.184 -11.631 -0.459  0.66 12.46 ?  140 LEU   A CA   1 
ATOM   2915 C CA   B LEU   A 1 140 ? 14.102 -11.627 -0.453  0.34 11.72 ?  140 LEU   A CA   1 
ATOM   2916 C C    A LEU   A 1 140 ? 14.431 -13.105 -0.747  0.66 12.72 ?  140 LEU   A C    1 
ATOM   2917 C C    B LEU   A 1 140 ? 14.401 -13.095 -0.741  0.34 12.38 ?  140 LEU   A C    1 
ATOM   2918 O O    A LEU   A 1 140 ? 14.986 -13.828 0.091   0.66 13.31 ?  140 LEU   A O    1 
ATOM   2919 O O    B LEU   A 1 140 ? 14.966 -13.800 0.104   0.34 12.61 ?  140 LEU   A O    1 
ATOM   2920 C CB   A LEU   A 1 140 ? 12.747 -11.403 0.011   0.66 12.78 ?  140 LEU   A CB   1 
ATOM   2921 C CB   B LEU   A 1 140 ? 12.648 -11.442 -0.018  0.34 11.92 ?  140 LEU   A CB   1 
ATOM   2922 C CG   A LEU   A 1 140 ? 12.276 -12.326 1.141   0.66 13.29 ?  140 LEU   A CG   1 
ATOM   2923 C CG   B LEU   A 1 140 ? 12.192 -12.175 1.245   0.34 12.31 ?  140 LEU   A CG   1 
ATOM   2924 C CD1  A LEU   A 1 140 ? 13.175 -12.230 2.366   0.66 12.67 ?  140 LEU   A CD1  1 
ATOM   2925 C CD1  B LEU   A 1 140 ? 13.037 -11.798 2.450   0.34 12.02 ?  140 LEU   A CD1  1 
ATOM   2926 C CD2  A LEU   A 1 140 ? 10.822 -12.036 1.517   0.66 14.17 ?  140 LEU   A CD2  1 
ATOM   2927 C CD2  B LEU   A 1 140 ? 10.721 -11.882 1.509   0.34 12.92 ?  140 LEU   A CD2  1 
ATOM   2928 H H    A LEU   A 1 140 ? 13.801 -10.362 -1.933  0.66 15.03 ?  140 LEU   A H    1 
ATOM   2929 H H    B LEU   A 1 140 ? 13.675 -10.470 -2.006  0.34 13.94 ?  140 LEU   A H    1 
ATOM   2930 H HA   A LEU   A 1 140 ? 14.777 -11.363 0.260   0.66 14.92 ?  140 LEU   A HA   1 
ATOM   2931 H HA   B LEU   A 1 140 ? 14.670 -11.338 0.278   0.34 14.04 ?  140 LEU   A HA   1 
ATOM   2932 H HB2  A LEU   A 1 140 ? 12.665 -10.493 0.330   0.66 15.30 ?  140 LEU   A HB2  1 
ATOM   2933 H HB2  B LEU   A 1 140 ? 12.494 -10.498 0.133   0.34 14.28 ?  140 LEU   A HB2  1 
ATOM   2934 H HB3  A LEU   A 1 140 ? 12.151 -11.540 -0.742  0.66 15.30 ?  140 LEU   A HB3  1 
ATOM   2935 H HB3  B LEU   A 1 140 ? 12.078 -11.746 -0.742  0.34 14.28 ?  140 LEU   A HB3  1 
ATOM   2936 H HG   A LEU   A 1 140 ? 12.301 -13.244 0.827   0.66 15.92 ?  140 LEU   A HG   1 
ATOM   2937 H HG   B LEU   A 1 140 ? 12.281 -13.130 1.105   0.34 14.74 ?  140 LEU   A HG   1 
ATOM   2938 H HD11 A LEU   A 1 140 ? 12.791 -12.767 3.079   0.66 15.18 ?  140 LEU   A HD11 1 
ATOM   2939 H HD11 B LEU   A 1 140 ? 12.655 -12.207 3.241   0.34 14.39 ?  140 LEU   A HD11 1 
ATOM   2940 H HD12 A LEU   A 1 140 ? 14.053 -12.571 2.135   0.66 15.18 ?  140 LEU   A HD12 1 
ATOM   2941 H HD12 B LEU   A 1 140 ? 13.940 -12.118 2.312   0.34 14.39 ?  140 LEU   A HD12 1 
ATOM   2942 H HD13 A LEU   A 1 140 ? 13.235 -11.306 2.642   0.66 15.18 ?  140 LEU   A HD13 1 
ATOM   2943 H HD13 B LEU   A 1 140 ? 13.035 -10.832 2.543   0.34 14.39 ?  140 LEU   A HD13 1 
ATOM   2944 H HD21 A LEU   A 1 140 ? 10.550 -12.637 2.232   0.66 16.98 ?  140 LEU   A HD21 1 
ATOM   2945 H HD21 B LEU   A 1 140 ? 10.430 -12.394 2.281   0.34 15.48 ?  140 LEU   A HD21 1 
ATOM   2946 H HD22 A LEU   A 1 140 ? 10.745 -11.117 1.816   0.66 16.98 ?  140 LEU   A HD22 1 
ATOM   2947 H HD22 B LEU   A 1 140 ? 10.614 -10.934 1.681   0.34 15.48 ?  140 LEU   A HD22 1 
ATOM   2948 H HD23 A LEU   A 1 140 ? 10.254 -12.178 0.740   0.66 16.98 ?  140 LEU   A HD23 1 
ATOM   2949 H HD23 B LEU   A 1 140 ? 10.201 -12.139 0.730   0.34 15.48 ?  140 LEU   A HD23 1 
ATOM   2950 N N    . ARG   A 1 141 ? 14.036 -13.566 -1.935  1.00 13.08 ?  141 ARG   A N    1 
ATOM   2951 C CA   . ARG   A 1 141 ? 14.271 -14.955 -2.309  1.00 14.18 ?  141 ARG   A CA   1 
ATOM   2952 C C    . ARG   A 1 141 ? 15.767 -15.269 -2.327  1.00 13.17 ?  141 ARG   A C    1 
ATOM   2953 O O    . ARG   A 1 141 ? 16.212 -16.288 -1.783  1.00 13.36 ?  141 ARG   A O    1 
ATOM   2954 C CB   . ARG   A 1 141 ? 13.639 -15.187 -3.683  1.00 16.15 ?  141 ARG   A CB   1 
ATOM   2955 C CG   . ARG   A 1 141 ? 13.613 -16.621 -4.152  1.00 18.65 ?  141 ARG   A CG   1 
ATOM   2956 C CD   . ARG   A 1 141 ? 12.590 -17.397 -3.379  1.00 20.25 ?  141 ARG   A CD   1 
ATOM   2957 N NE   . ARG   A 1 141 ? 13.211 -18.156 -2.308  1.00 20.09 ?  141 ARG   A NE   1 
ATOM   2958 C CZ   . ARG   A 1 141 ? 12.536 -18.754 -1.335  1.00 20.70 ?  141 ARG   A CZ   1 
ATOM   2959 N NH1  . ARG   A 1 141 ? 11.235 -18.570 -1.181  1.00 20.67 ?  141 ARG   A NH1  1 
ATOM   2960 N NH2  . ARG   A 1 141 ? 13.182 -19.552 -0.491  1.00 21.60 ?  141 ARG   A NH2  1 
ATOM   2961 H H    A ARG   A 1 141 ? 13.633 -13.096 -2.532  0.66 15.67 ?  141 ARG   A H    1 
ATOM   2962 H H    B ARG   A 1 141 ? 13.644 -13.098 -2.541  0.34 15.67 ?  141 ARG   A H    1 
ATOM   2963 H HA   . ARG   A 1 141 ? 13.846 -15.540 -1.667  1.00 16.99 ?  141 ARG   A HA   1 
ATOM   2964 H HB2  . ARG   A 1 141 ? 12.723 -14.865 -3.659  1.00 19.35 ?  141 ARG   A HB2  1 
ATOM   2965 H HB3  . ARG   A 1 141 ? 14.139 -14.677 -4.340  1.00 19.35 ?  141 ARG   A HB3  1 
ATOM   2966 H HG2  . ARG   A 1 141 ? 13.377 -16.651 -5.094  1.00 22.36 ?  141 ARG   A HG2  1 
ATOM   2967 H HG3  . ARG   A 1 141 ? 14.483 -17.028 -4.010  1.00 22.36 ?  141 ARG   A HG3  1 
ATOM   2968 H HD2  . ARG   A 1 141 ? 11.948 -16.787 -2.981  1.00 24.27 ?  141 ARG   A HD2  1 
ATOM   2969 H HD3  . ARG   A 1 141 ? 12.135 -18.015 -3.976  1.00 24.27 ?  141 ARG   A HD3  1 
ATOM   2970 H HE   . ARG   A 1 141 ? 14.054 -18.307 -2.359  1.00 24.08 ?  141 ARG   A HE   1 
ATOM   2971 H HH11 . ARG   A 1 141 ? 10.800 -18.069 -1.727  1.00 24.78 ?  141 ARG   A HH11 1 
ATOM   2972 H HH12 . ARG   A 1 141 ? 10.816 -18.967 -0.541  1.00 24.78 ?  141 ARG   A HH12 1 
ATOM   2973 H HH21 . ARG   A 1 141 ? 14.030 -19.674 -0.576  1.00 25.90 ?  141 ARG   A HH21 1 
ATOM   2974 H HH22 . ARG   A 1 141 ? 12.758 -19.934 0.154   1.00 25.90 ?  141 ARG   A HH22 1 
ATOM   2975 N N    . VAL   A 1 142 ? 16.562 -14.400 -2.955  1.00 12.64 ?  142 VAL   A N    1 
ATOM   2976 C CA   . VAL   A 1 142 ? 18.003 -14.620 -2.987  1.00 12.80 ?  142 VAL   A CA   1 
ATOM   2977 C C    . VAL   A 1 142 ? 18.572 -14.602 -1.577  1.00 12.37 ?  142 VAL   A C    1 
ATOM   2978 O O    . VAL   A 1 142 ? 19.434 -15.421 -1.236  1.00 12.56 ?  142 VAL   A O    1 
ATOM   2979 C CB   . VAL   A 1 142 ? 18.708 -13.605 -3.905  1.00 13.00 ?  142 VAL   A CB   1 
ATOM   2980 C CG1  . VAL   A 1 142 ? 20.223 -13.818 -3.847  1.00 13.11 ?  142 VAL   A CG1  1 
ATOM   2981 C CG2  . VAL   A 1 142 ? 18.224 -13.736 -5.336  1.00 14.04 ?  142 VAL   A CG2  1 
ATOM   2982 H H    . VAL   A 1 142 ? 16.299 -13.684 -3.363  1.00 15.14 ?  142 VAL   A H    1 
ATOM   2983 H HA   . VAL   A 1 142 ? 18.173 -15.497 -3.354  1.00 15.33 ?  142 VAL   A HA   1 
ATOM   2984 H HB   . VAL   A 1 142 ? 18.524 -12.699 -3.602  1.00 15.57 ?  142 VAL   A HB   1 
ATOM   2985 H HG11 . VAL   A 1 142 ? 20.642 -13.346 -4.585  1.00 15.70 ?  142 VAL   A HG11 1 
ATOM   2986 H HG12 . VAL   A 1 142 ? 20.565 -13.472 -3.004  1.00 15.70 ?  142 VAL   A HG12 1 
ATOM   2987 H HG13 . VAL   A 1 142 ? 20.412 -14.767 -3.914  1.00 15.70 ?  142 VAL   A HG13 1 
ATOM   2988 H HG21 . VAL   A 1 142 ? 18.698 -13.094 -5.890  1.00 16.82 ?  142 VAL   A HG21 1 
ATOM   2989 H HG22 . VAL   A 1 142 ? 18.415 -14.638 -5.644  1.00 16.82 ?  142 VAL   A HG22 1 
ATOM   2990 H HG23 . VAL   A 1 142 ? 17.277 -13.568 -5.361  1.00 16.82 ?  142 VAL   A HG23 1 
ATOM   2991 N N    . CYS   A 1 143 ? 18.107 -13.677 -0.737  1.00 12.01 ?  143 CYS   A N    1 
ATOM   2992 C CA   . CYS   A 1 143 ? 18.574 -13.635 0.646   1.00 12.45 ?  143 CYS   A CA   1 
ATOM   2993 C C    . CYS   A 1 143 ? 18.344 -14.978 1.336   1.00 12.48 ?  143 CYS   A C    1 
ATOM   2994 O O    . CYS   A 1 143 ? 19.266 -15.571 1.906   1.00 12.31 ?  143 CYS   A O    1 
ATOM   2995 C CB   . CYS   A 1 143 ? 17.846 -12.517 1.395   1.00 12.63 ?  143 CYS   A CB   1 
ATOM   2996 S SG   . CYS   A 1 143 ? 18.342 -12.362 3.124   1.00 13.01 ?  143 CYS   A SG   1 
ATOM   2997 H H    . CYS   A 1 143 ? 17.528 -13.074 -0.939  1.00 14.38 ?  143 CYS   A H    1 
ATOM   2998 H HA   . CYS   A 1 143 ? 19.522 -13.449 0.658   1.00 14.92 ?  143 CYS   A HA   1 
ATOM   2999 H HB2  . CYS   A 1 143 ? 18.019 -11.676 0.952   1.00 15.13 ?  143 CYS   A HB2  1 
ATOM   3000 H HB3  . CYS   A 1 143 ? 16.893 -12.704 1.379   1.00 15.13 ?  143 CYS   A HB3  1 
ATOM   3001 H HG   . CYS   A 1 143 ? 17.793 -11.405 3.595   1.00 15.59 ?  143 CYS   A HG   1 
ATOM   3002 N N    . VAL   A 1 144 ? 17.109 -15.474 1.285   1.00 12.97 ?  144 VAL   A N    1 
ATOM   3003 C CA   . VAL   A 1 144 ? 16.766 -16.713 1.975   1.00 14.24 ?  144 VAL   A CA   1 
ATOM   3004 C C    . VAL   A 1 144 ? 17.582 -17.882 1.442   1.00 13.85 ?  144 VAL   A C    1 
ATOM   3005 O O    . VAL   A 1 144 ? 17.959 -18.791 2.196   1.00 14.38 ?  144 VAL   A O    1 
ATOM   3006 C CB   . VAL   A 1 144 ? 15.249 -16.956 1.852   1.00 16.66 ?  144 VAL   A CB   1 
ATOM   3007 C CG1  . VAL   A 1 144 ? 14.886 -18.389 2.187   1.00 18.80 ?  144 VAL   A CG1  1 
ATOM   3008 C CG2  . VAL   A 1 144 ? 14.498 -15.958 2.733   1.00 16.52 ?  144 VAL   A CG2  1 
ATOM   3009 H H    . VAL   A 1 144 ? 16.451 -15.110 0.858   1.00 15.54 ?  144 VAL   A H    1 
ATOM   3010 H HA   . VAL   A 1 144 ? 16.972 -16.614 2.913   1.00 17.06 ?  144 VAL   A HA   1 
ATOM   3011 H HB   . VAL   A 1 144 ? 14.979 -16.788 0.932   1.00 19.97 ?  144 VAL   A HB   1 
ATOM   3012 H HG11 . VAL   A 1 144 ? 13.933 -18.437 2.371   1.00 22.53 ?  144 VAL   A HG11 1 
ATOM   3013 H HG12 . VAL   A 1 144 ? 15.102 -18.956 1.431   1.00 22.53 ?  144 VAL   A HG12 1 
ATOM   3014 H HG13 . VAL   A 1 144 ? 15.386 -18.665 2.968   1.00 22.53 ?  144 VAL   A HG13 1 
ATOM   3015 H HG21 . VAL   A 1 144 ? 13.546 -16.138 2.680   1.00 19.79 ?  144 VAL   A HG21 1 
ATOM   3016 H HG22 . VAL   A 1 144 ? 14.801 -16.052 3.648   1.00 19.79 ?  144 VAL   A HG22 1 
ATOM   3017 H HG23 . VAL   A 1 144 ? 14.677 -15.055 2.418   1.00 19.79 ?  144 VAL   A HG23 1 
ATOM   3018 N N    . ASP   A 1 145 ? 17.844 -17.896 0.139   1.00 14.28 ?  145 ASP   A N    1 
ATOM   3019 C CA   . ASP   A 1 145 ? 18.551 -19.002 -0.494  1.00 14.57 ?  145 ASP   A CA   1 
ATOM   3020 C C    . ASP   A 1 145 ? 20.071 -18.859 -0.454  1.00 13.78 ?  145 ASP   A C    1 
ATOM   3021 O O    . ASP   A 1 145 ? 20.772 -19.746 -0.951  1.00 15.89 ?  145 ASP   A O    1 
ATOM   3022 C CB   . ASP   A 1 145 ? 18.096 -19.152 -1.946  1.00 16.54 ?  145 ASP   A CB   1 
ATOM   3023 C CG   . ASP   A 1 145 ? 16.635 -19.551 -2.063  1.00 18.83 ?  145 ASP   A CG   1 
ATOM   3024 O OD1  . ASP   A 1 145 ? 16.076 -20.097 -1.087  1.00 18.95 ?  145 ASP   A OD1  1 
ATOM   3025 O OD2  . ASP   A 1 145 ? 16.045 -19.315 -3.134  1.00 20.35 -1 145 ASP   A OD2  1 
ATOM   3026 H H    . ASP   A 1 145 ? 17.609 -17.274 -0.412  1.00 17.11 ?  145 ASP   A H    1 
ATOM   3027 H HA   . ASP   A 1 145 ? 18.321 -19.821 -0.030  1.00 17.46 ?  145 ASP   A HA   1 
ATOM   3028 H HB2  . ASP   A 1 145 ? 18.220 -18.307 -2.406  1.00 19.82 ?  145 ASP   A HB2  1 
ATOM   3029 H HB3  . ASP   A 1 145 ? 18.621 -19.845 -2.373  1.00 19.82 ?  145 ASP   A HB3  1 
ATOM   3030 N N    . THR   A 1 146 ? 20.601 -17.779 0.116   1.00 12.78 ?  146 THR   A N    1 
ATOM   3031 C CA   . THR   A 1 146 ? 22.042 -17.530 0.131   1.00 12.40 ?  146 THR   A CA   1 
ATOM   3032 C C    . THR   A 1 146 ? 22.598 -17.357 1.533   1.00 12.13 ?  146 THR   A C    1 
ATOM   3033 O O    . THR   A 1 146 ? 23.676 -17.888 1.840   1.00 13.02 ?  146 THR   A O    1 
ATOM   3034 C CB   . THR   A 1 146 ? 22.370 -16.276 -0.703  1.00 12.48 ?  146 THR   A CB   1 
ATOM   3035 O OG1  . THR   A 1 146 ? 21.840 -16.427 -2.018  1.00 12.63 ?  146 THR   A OG1  1 
ATOM   3036 C CG2  . THR   A 1 146 ? 23.874 -16.053 -0.798  1.00 13.13 ?  146 THR   A CG2  1 
ATOM   3037 H H    . THR   A 1 146 ? 20.136 -17.158 0.498   1.00 15.31 ?  146 THR   A H    1 
ATOM   3038 H HA   . THR   A 1 146 ? 22.497 -18.284 -0.265  1.00 14.85 ?  146 THR   A HA   1 
ATOM   3039 H HB   . THR   A 1 146 ? 21.983 -15.496 -0.277  1.00 14.95 ?  146 THR   A HB   1 
ATOM   3040 H HG1  . THR   A 1 146 ? 21.001 -16.489 -1.973  1.00 15.12 ?  146 THR   A HG1  1 
ATOM   3041 H HG21 . THR   A 1 146 ? 24.065 -15.374 -1.465  1.00 15.73 ?  146 THR   A HG21 1 
ATOM   3042 H HG22 . THR   A 1 146 ? 24.227 -15.757 0.058   1.00 15.73 ?  146 THR   A HG22 1 
ATOM   3043 H HG23 . THR   A 1 146 ? 24.318 -16.877 -1.053  1.00 15.73 ?  146 THR   A HG23 1 
ATOM   3044 N N    . VAL   A 1 147 ? 21.922 -16.576 2.371   1.00 11.96 ?  147 VAL   A N    1 
ATOM   3045 C CA   . VAL   A 1 147 ? 22.399 -16.287 3.713   1.00 12.22 ?  147 VAL   A CA   1 
ATOM   3046 C C    . VAL   A 1 147 ? 22.073 -17.461 4.623   1.00 12.57 ?  147 VAL   A C    1 
ATOM   3047 O O    . VAL   A 1 147 ? 20.930 -17.936 4.668   1.00 12.83 ?  147 VAL   A O    1 
ATOM   3048 C CB   . VAL   A 1 147 ? 21.780 -14.980 4.235   1.00 12.12 ?  147 VAL   A CB   1 
ATOM   3049 C CG1  . VAL   A 1 147 ? 22.320 -14.672 5.614   1.00 13.50 ?  147 VAL   A CG1  1 
ATOM   3050 C CG2  . VAL   A 1 147 ? 22.058 -13.838 3.269   1.00 12.21 ?  147 VAL   A CG2  1 
ATOM   3051 H H    . VAL   A 1 147 ? 21.168 -16.199 2.184   1.00 14.32 ?  147 VAL   A H    1 
ATOM   3052 H HA   . VAL   A 1 147 ? 23.363 -16.176 3.692   1.00 14.64 ?  147 VAL   A HA   1 
ATOM   3053 H HB   . VAL   A 1 147 ? 20.820 -15.089 4.306   1.00 14.52 ?  147 VAL   A HB   1 
ATOM   3054 H HG11 . VAL   A 1 147 ? 22.072 -13.769 5.857   1.00 16.17 ?  147 VAL   A HG11 1 
ATOM   3055 H HG12 . VAL   A 1 147 ? 21.940 -15.301 6.252   1.00 16.17 ?  147 VAL   A HG12 1 
ATOM   3056 H HG13 . VAL   A 1 147 ? 23.286 -14.760 5.603   1.00 16.17 ?  147 VAL   A HG13 1 
ATOM   3057 H HG21 . VAL   A 1 147 ? 21.747 -13.008 3.664   1.00 14.62 ?  147 VAL   A HG21 1 
ATOM   3058 H HG22 . VAL   A 1 147 ? 23.014 -13.789 3.107   1.00 14.62 ?  147 VAL   A HG22 1 
ATOM   3059 H HG23 . VAL   A 1 147 ? 21.590 -14.006 2.438   1.00 14.62 ?  147 VAL   A HG23 1 
ATOM   3060 N N    . ARG   A 1 148 ? 23.090 -17.940 5.336   1.00 12.58 ?  148 ARG   A N    1 
ATOM   3061 C CA   . ARG   A 1 148 ? 22.961 -19.023 6.296   1.00 12.64 ?  148 ARG   A CA   1 
ATOM   3062 C C    . ARG   A 1 148 ? 23.092 -18.557 7.734   1.00 13.29 ?  148 ARG   A C    1 
ATOM   3063 O O    . ARG   A 1 148 ? 22.672 -19.278 8.646   1.00 14.70 ?  148 ARG   A O    1 
ATOM   3064 C CB   . ARG   A 1 148 ? 24.003 -20.112 6.004   1.00 13.02 ?  148 ARG   A CB   1 
ATOM   3065 C CG   . ARG   A 1 148 ? 23.817 -20.759 4.636   1.00 14.63 ?  148 ARG   A CG   1 
ATOM   3066 C CD   . ARG   A 1 148 ? 24.894 -21.798 4.321   1.00 15.70 ?  148 ARG   A CD   1 
ATOM   3067 N NE   . ARG   A 1 148 ? 26.239 -21.231 4.347   1.00 15.96 ?  148 ARG   A NE   1 
ATOM   3068 C CZ   . ARG   A 1 148 ? 26.752 -20.477 3.383   1.00 15.11 ?  148 ARG   A CZ   1 
ATOM   3069 N NH1  . ARG   A 1 148 ? 26.080 -20.222 2.270   1.00 15.70 ?  148 ARG   A NH1  1 
ATOM   3070 N NH2  . ARG   A 1 148 ? 27.967 -19.951 3.544   1.00 15.56 ?  148 ARG   A NH2  1 
ATOM   3071 H H    . ARG   A 1 148 ? 23.894 -17.643 5.263   1.00 15.07 ?  148 ARG   A H    1 
ATOM   3072 H HA   . ARG   A 1 148 ? 22.087 -19.423 6.195   1.00 15.14 ?  148 ARG   A HA   1 
ATOM   3073 H HB2  . ARG   A 1 148 ? 24.889 -19.725 6.030   1.00 15.60 ?  148 ARG   A HB2  1 
ATOM   3074 H HB3  . ARG   A 1 148 ? 23.924 -20.813 6.670   1.00 15.60 ?  148 ARG   A HB3  1 
ATOM   3075 H HG2  . ARG   A 1 148 ? 22.952 -21.195 4.610   1.00 17.53 ?  148 ARG   A HG2  1 
ATOM   3076 H HG3  . ARG   A 1 148 ? 23.857 -20.063 3.956   1.00 17.53 ?  148 ARG   A HG3  1 
ATOM   3077 H HD2  . ARG   A 1 148 ? 24.851 -22.503 4.982   1.00 18.81 ?  148 ARG   A HD2  1 
ATOM   3078 H HD3  . ARG   A 1 148 ? 24.733 -22.157 3.434   1.00 18.81 ?  148 ARG   A HD3  1 
ATOM   3079 H HE   . ARG   A 1 148 ? 26.724 -21.384 5.034   1.00 19.13 ?  148 ARG   A HE   1 
ATOM   3080 H HH11 . ARG   A 1 148 ? 25.294 -20.545 2.153   1.00 18.81 ?  148 ARG   A HH11 1 
ATOM   3081 H HH12 . ARG   A 1 148 ? 26.433 -19.723 1.659   1.00 18.81 ?  148 ARG   A HH12 1 
ATOM   3082 H HH21 . ARG   A 1 148 ? 28.404 -20.094 4.266   1.00 18.64 ?  148 ARG   A HH21 1 
ATOM   3083 H HH22 . ARG   A 1 148 ? 28.306 -19.450 2.927   1.00 18.64 ?  148 ARG   A HH22 1 
ATOM   3084 N N    . THR   A 1 149 ? 23.653 -17.373 7.953   1.00 13.40 ?  149 THR   A N    1 
ATOM   3085 C CA   . THR   A 1 149 ? 23.726 -16.779 9.273   1.00 13.42 ?  149 THR   A CA   1 
ATOM   3086 C C    . THR   A 1 149 ? 22.399 -16.085 9.586   1.00 12.85 ?  149 THR   A C    1 
ATOM   3087 O O    . THR   A 1 149 ? 21.462 -16.079 8.778   1.00 13.59 ?  149 THR   A O    1 
ATOM   3088 C CB   . THR   A 1 149 ? 24.928 -15.843 9.338   1.00 13.69 ?  149 THR   A CB   1 
ATOM   3089 O OG1  . THR   A 1 149 ? 24.804 -14.900 8.271   1.00 13.60 ?  149 THR   A OG1  1 
ATOM   3090 C CG2  . THR   A 1 149 ? 26.238 -16.639 9.203   1.00 14.11 ?  149 THR   A CG2  1 
ATOM   3091 H H    . THR   A 1 149 ? 24.011 -16.886 7.337   1.00 16.05 ?  149 THR   A H    1 
ATOM   3092 H HA   . THR   A 1 149 ? 23.855 -17.486 9.926   1.00 16.07 ?  149 THR   A HA   1 
ATOM   3093 H HB   . THR   A 1 149 ? 24.927 -15.378 10.188  1.00 16.41 ?  149 THR   A HB   1 
ATOM   3094 H HG1  . THR   A 1 149 ? 25.458 -14.373 8.278   1.00 16.29 ?  149 THR   A HG1  1 
ATOM   3095 H HG21 . THR   A 1 149 ? 26.998 -16.044 9.267   1.00 16.90 ?  149 THR   A HG21 1 
ATOM   3096 H HG22 . THR   A 1 149 ? 26.299 -17.305 9.910   1.00 16.90 ?  149 THR   A HG22 1 
ATOM   3097 H HG23 . THR   A 1 149 ? 26.266 -17.096 8.345   1.00 16.90 ?  149 THR   A HG23 1 
ATOM   3098 N N    . ASN   A 1 150 ? 22.282 -15.545 10.791  1.00 13.03 ?  150 ASN   A N    1 
ATOM   3099 C CA   . ASN   A 1 150 ? 21.001 -15.034 11.278  1.00 13.55 ?  150 ASN   A CA   1 
ATOM   3100 C C    . ASN   A 1 150 ? 20.823 -13.594 10.826  1.00 12.97 ?  150 ASN   A C    1 
ATOM   3101 O O    . ASN   A 1 150 ? 21.558 -12.701 11.263  1.00 14.42 ?  150 ASN   A O    1 
ATOM   3102 C CB   . ASN   A 1 150 ? 20.933 -15.155 12.794  1.00 16.05 ?  150 ASN   A CB   1 
ATOM   3103 C CG   . ASN   A 1 150 ? 20.841 -16.589 13.244  1.00 19.99 ?  150 ASN   A CG   1 
ATOM   3104 O OD1  . ASN   A 1 150 ? 20.236 -17.416 12.566  1.00 21.77 ?  150 ASN   A OD1  1 
ATOM   3105 N ND2  . ASN   A 1 150 ? 21.457 -16.901 14.380  1.00 22.75 ?  150 ASN   A ND2  1 
ATOM   3106 H H    . ASN   A 1 150 ? 22.927 -15.466 11.354  1.00 15.61 ?  150 ASN   A H    1 
ATOM   3107 H HA   . ASN   A 1 150 ? 20.279 -15.568 10.905  1.00 16.23 ?  150 ASN   A HA   1 
ATOM   3108 H HB2  . ASN   A 1 150 ? 21.734 -14.771 13.183  1.00 19.23 ?  150 ASN   A HB2  1 
ATOM   3109 H HB3  . ASN   A 1 150 ? 20.147 -14.691 13.120  1.00 19.23 ?  150 ASN   A HB3  1 
ATOM   3110 H HD21 . ASN   A 1 150 ? 21.436 -17.710 14.681  1.00 27.27 ?  150 ASN   A HD21 1 
ATOM   3111 H HD22 . ASN   A 1 150 ? 21.875 -16.294 14.826  1.00 27.27 ?  150 ASN   A HD22 1 
ATOM   3112 N N    . VAL   A 1 151 ? 19.849 -13.365 9.953   1.00 12.55 ?  151 VAL   A N    1 
ATOM   3113 C CA   . VAL   A 1 151 ? 19.635 -12.053 9.360   1.00 12.80 ?  151 VAL   A CA   1 
ATOM   3114 C C    . VAL   A 1 151 ? 18.249 -11.541 9.723   1.00 12.48 ?  151 VAL   A C    1 
ATOM   3115 O O    . VAL   A 1 151 ? 17.242 -12.251 9.566   1.00 13.76 ?  151 VAL   A O    1 
ATOM   3116 C CB   . VAL   A 1 151 ? 19.922 -12.040 7.843   1.00 13.55 ?  151 VAL   A CB   1 
ATOM   3117 C CG1  . VAL   A 1 151 ? 19.117 -13.087 7.093   1.00 15.10 ?  151 VAL   A CG1  1 
ATOM   3118 C CG2  . VAL   A 1 151 ? 19.709 -10.633 7.260   1.00 13.84 ?  151 VAL   A CG2  1 
ATOM   3119 H H    . VAL   A 1 151 ? 19.296 -13.965 9.678   1.00 15.04 ?  151 VAL   A H    1 
ATOM   3120 H HA   . VAL   A 1 151 ? 20.274 -11.440 9.755   1.00 15.34 ?  151 VAL   A HA   1 
ATOM   3121 H HB   . VAL   A 1 151 ? 20.861 -12.257 7.709   1.00 16.23 ?  151 VAL   A HB   1 
ATOM   3122 H HG11 . VAL   A 1 151 ? 19.312 -13.028 6.142   1.00 18.10 ?  151 VAL   A HG11 1 
ATOM   3123 H HG12 . VAL   A 1 151 ? 19.365 -13.974 7.418   1.00 18.10 ?  151 VAL   A HG12 1 
ATOM   3124 H HG13 . VAL   A 1 151 ? 18.172 -12.938 7.245   1.00 18.10 ?  151 VAL   A HG13 1 
ATOM   3125 H HG21 . VAL   A 1 151 ? 20.031 -10.618 6.341   1.00 16.58 ?  151 VAL   A HG21 1 
ATOM   3126 H HG22 . VAL   A 1 151 ? 18.762 -10.422 7.276   1.00 16.58 ?  151 VAL   A HG22 1 
ATOM   3127 H HG23 . VAL   A 1 151 ? 20.203 -9.991  7.790   1.00 16.58 ?  151 VAL   A HG23 1 
ATOM   3128 N N    . TYR   A 1 152 ? 18.227 -10.306 10.220  1.00 12.32 ?  152 TYR   A N    1 
ATOM   3129 C CA   . TYR   A 1 152 ? 17.033 -9.574  10.606  1.00 12.11 ?  152 TYR   A CA   1 
ATOM   3130 C C    . TYR   A 1 152 ? 16.841 -8.470  9.579   1.00 11.85 ?  152 TYR   A C    1 
ATOM   3131 O O    . TYR   A 1 152 ? 17.613 -7.503  9.542   1.00 12.22 ?  152 TYR   A O    1 
ATOM   3132 C CB   . TYR   A 1 152 ? 17.206 -9.029  12.019  1.00 12.63 ?  152 TYR   A CB   1 
ATOM   3133 C CG   . TYR   A 1 152 ? 17.153 -10.156 13.014  1.00 13.27 ?  152 TYR   A CG   1 
ATOM   3134 C CD1  . TYR   A 1 152 ? 18.277 -10.927 13.282  1.00 15.07 ?  152 TYR   A CD1  1 
ATOM   3135 C CD2  . TYR   A 1 152 ? 15.965 -10.491 13.648  1.00 13.54 ?  152 TYR   A CD2  1 
ATOM   3136 C CE1  . TYR   A 1 152 ? 18.226 -11.988 14.168  1.00 16.46 ?  152 TYR   A CE1  1 
ATOM   3137 C CE2  . TYR   A 1 152 ? 15.903 -11.559 14.539  1.00 15.48 ?  152 TYR   A CE2  1 
ATOM   3138 C CZ   . TYR   A 1 152 ? 17.040 -12.301 14.796  1.00 16.53 ?  152 TYR   A CZ   1 
ATOM   3139 O OH   . TYR   A 1 152 ? 16.995 -13.369 15.673  1.00 18.87 ?  152 TYR   A OH   1 
ATOM   3140 H H    . TYR   A 1 152 ? 18.947 -9.840  10.333  1.00 14.75 ?  152 TYR   A H    1 
ATOM   3141 H HA   . TYR   A 1 152 ? 16.266 -10.164 10.584  1.00 14.50 ?  152 TYR   A HA   1 
ATOM   3142 H HB2  . TYR   A 1 152 ? 18.070 -8.597  12.094  1.00 15.13 ?  152 TYR   A HB2  1 
ATOM   3143 H HB3  . TYR   A 1 152 ? 16.495 -8.404  12.217  1.00 15.13 ?  152 TYR   A HB3  1 
ATOM   3144 H HD1  . TYR   A 1 152 ? 19.078 -10.721 12.856  1.00 18.05 ?  152 TYR   A HD1  1 
ATOM   3145 H HD2  . TYR   A 1 152 ? 15.193 -9.992  13.472  1.00 16.22 ?  152 TYR   A HD2  1 
ATOM   3146 H HE1  . TYR   A 1 152 ? 18.989 -12.485 14.338  1.00 19.72 ?  152 TYR   A HE1  1 
ATOM   3147 H HE2  . TYR   A 1 152 ? 15.099 -11.763 14.962  1.00 18.55 ?  152 TYR   A HE2  1 
ATOM   3148 H HH   . TYR   A 1 152 ? 16.218 -13.441 15.987  1.00 22.62 ?  152 TYR   A HH   1 
ATOM   3149 N N    A LEU   A 1 153 ? 15.840 -8.647  8.716   0.66 12.06 ?  153 LEU   A N    1 
ATOM   3150 N N    B LEU   A 1 153 ? 15.810 -8.602  8.755   0.34 11.97 ?  153 LEU   A N    1 
ATOM   3151 C CA   A LEU   A 1 153 ? 15.569 -7.758  7.592   0.66 12.27 ?  153 LEU   A CA   1 
ATOM   3152 C CA   B LEU   A 1 153 ? 15.550 -7.648  7.687   0.34 11.94 ?  153 LEU   A CA   1 
ATOM   3153 C C    A LEU   A 1 153 ? 14.565 -6.679  7.976   0.66 12.46 ?  153 LEU   A C    1 
ATOM   3154 C C    B LEU   A 1 153 ? 14.583 -6.577  8.177   0.34 11.88 ?  153 LEU   A C    1 
ATOM   3155 O O    A LEU   A 1 153 ? 13.464 -6.979  8.450   0.66 13.47 ?  153 LEU   A O    1 
ATOM   3156 O O    B LEU   A 1 153 ? 13.484 -6.891  8.648   0.34 12.42 ?  153 LEU   A O    1 
ATOM   3157 C CB   A LEU   A 1 153 ? 14.998 -8.562  6.421   0.66 11.84 ?  153 LEU   A CB   1 
ATOM   3158 C CB   B LEU   A 1 153 ? 14.985 -8.364  6.463   0.34 12.15 ?  153 LEU   A CB   1 
ATOM   3159 C CG   A LEU   A 1 153 ? 15.952 -9.533  5.725   0.66 11.92 ?  153 LEU   A CG   1 
ATOM   3160 C CG   B LEU   A 1 153 ? 15.906 -9.420  5.851   0.34 12.60 ?  153 LEU   A CG   1 
ATOM   3161 C CD1  A LEU   A 1 153 ? 15.182 -10.468 4.807   0.66 11.85 ?  153 LEU   A CD1  1 
ATOM   3162 C CD1  B LEU   A 1 153 ? 15.181 -10.171 4.748   0.34 12.98 ?  153 LEU   A CD1  1 
ATOM   3163 C CD2  A LEU   A 1 153 ? 17.004 -8.761  4.938   0.66 11.65 ?  153 LEU   A CD2  1 
ATOM   3164 C CD2  B LEU   A 1 153 ? 17.196 -8.794  5.324   0.34 12.98 ?  153 LEU   A CD2  1 
ATOM   3165 H H    A LEU   A 1 153 ? 15.284 -9.309  8.768   0.66 14.44 ?  153 LEU   A H    1 
ATOM   3166 H H    B LEU   A 1 153 ? 15.232 -9.241  8.799   0.34 14.33 ?  153 LEU   A H    1 
ATOM   3167 H HA   A LEU   A 1 153 ? 16.390 -7.338  7.309   0.66 14.69 ?  153 LEU   A HA   1 
ATOM   3168 H HA   B LEU   A 1 153 ? 16.376 -7.222  7.441   0.34 14.30 ?  153 LEU   A HA   1 
ATOM   3169 H HB2  A LEU   A 1 153 ? 14.242 -9.081  6.745   0.66 14.18 ?  153 LEU   A HB2  1 
ATOM   3170 H HB2  B LEU   A 1 153 ? 14.160 -8.805  6.718   0.34 14.55 ?  153 LEU   A HB2  1 
ATOM   3171 H HB3  A LEU   A 1 153 ? 14.686 -7.936  5.747   0.66 14.18 ?  153 LEU   A HB3  1 
ATOM   3172 H HB3  B LEU   A 1 153 ? 14.802 -7.702  5.779   0.34 14.55 ?  153 LEU   A HB3  1 
ATOM   3173 H HG   A LEU   A 1 153 ? 16.406 -10.071 6.398   0.66 14.27 ?  153 LEU   A HG   1 
ATOM   3174 H HG   B LEU   A 1 153 ? 16.148 -10.060 6.540   0.34 15.09 ?  153 LEU   A HG   1 
ATOM   3175 H HD11 A LEU   A 1 153 ? 15.781 -11.160 4.488   0.66 14.20 ?  153 LEU   A HD11 1 
ATOM   3176 H HD11 B LEU   A 1 153 ? 15.752 -10.884 4.425   0.34 15.55 ?  153 LEU   A HD11 1 
ATOM   3177 H HD12 A LEU   A 1 153 ? 14.451 -10.864 5.301   0.66 14.20 ?  153 LEU   A HD12 1 
ATOM   3178 H HD12 B LEU   A 1 153 ? 14.360 -10.540 5.107   0.34 15.55 ?  153 LEU   A HD12 1 
ATOM   3179 H HD13 A LEU   A 1 153 ? 14.838 -9.954  4.059   0.66 14.20 ?  153 LEU   A HD13 1 
ATOM   3180 H HD13 B LEU   A 1 153 ? 14.981 -9.553  4.028   0.34 15.55 ?  153 LEU   A HD13 1 
ATOM   3181 H HD21 A LEU   A 1 153 ? 17.589 -9.392  4.503   0.66 13.96 ?  153 LEU   A HD21 1 
ATOM   3182 H HD21 B LEU   A 1 153 ? 17.706 -9.472  4.856   0.34 15.55 ?  153 LEU   A HD21 1 
ATOM   3183 H HD22 A LEU   A 1 153 ? 16.549 -8.212  4.282   0.66 13.96 ?  153 LEU   A HD22 1 
ATOM   3184 H HD22 B LEU   A 1 153 ? 16.970 -8.071  4.719   0.34 15.55 ?  153 LEU   A HD22 1 
ATOM   3185 H HD23 A LEU   A 1 153 ? 17.502 -8.205  5.553   0.66 13.96 ?  153 LEU   A HD23 1 
ATOM   3186 H HD23 B LEU   A 1 153 ? 17.711 -8.451  6.072   0.34 15.55 ?  153 LEU   A HD23 1 
ATOM   3187 N N    A ALA   A 1 154 ? 14.940 -5.428  7.732   0.66 12.04 ?  154 ALA   A N    1 
ATOM   3188 N N    B ALA   A 1 154 ? 15.005 -5.320  8.079   0.34 11.21 ?  154 ALA   A N    1 
ATOM   3189 C CA   A ALA   A 1 154 ? 14.075 -4.275  7.943   0.66 12.18 ?  154 ALA   A CA   1 
ATOM   3190 C CA   B ALA   A 1 154 ? 14.149 -4.171  8.340   0.34 11.65 ?  154 ALA   A CA   1 
ATOM   3191 C C    A ALA   A 1 154 ? 13.585 -3.783  6.586   0.66 11.70 ?  154 ALA   A C    1 
ATOM   3192 C C    B ALA   A 1 154 ? 13.677 -3.627  6.998   0.34 11.39 ?  154 ALA   A C    1 
ATOM   3193 O O    A ALA   A 1 154 ? 14.396 -3.425  5.725   0.66 12.24 ?  154 ALA   A O    1 
ATOM   3194 O O    B ALA   A 1 154 ? 14.498 -3.230  6.164   0.34 11.34 ?  154 ALA   A O    1 
ATOM   3195 C CB   A ALA   A 1 154 ? 14.843 -3.164  8.658   0.66 12.74 ?  154 ALA   A CB   1 
ATOM   3196 C CB   B ALA   A 1 154 ? 14.909 -3.096  9.118   0.34 12.00 ?  154 ALA   A CB   1 
ATOM   3197 H H    A ALA   A 1 154 ? 15.715 -5.222  7.427   0.66 14.42 ?  154 ALA   A H    1 
ATOM   3198 H H    B ALA   A 1 154 ? 15.808 -5.097  7.855   0.34 13.43 ?  154 ALA   A H    1 
ATOM   3199 H HA   A ALA   A 1 154 ? 13.312 -4.529  8.486   0.66 14.59 ?  154 ALA   A HA   1 
ATOM   3200 H HA   B ALA   A 1 154 ? 13.375 -4.438  8.854   0.34 13.96 ?  154 ALA   A HA   1 
ATOM   3201 H HB1  A ALA   A 1 154 ? 14.254 -2.408  8.787   0.66 15.26 ?  154 ALA   A HB1  1 
ATOM   3202 H HB1  B ALA   A 1 154 ? 14.321 -2.341  9.279   0.34 14.37 ?  154 ALA   A HB1  1 
ATOM   3203 H HB2  A ALA   A 1 154 ? 15.157 -3.494  9.515   0.66 15.26 ?  154 ALA   A HB2  1 
ATOM   3204 H HB2  B ALA   A 1 154 ? 15.206 -3.470  9.962   0.34 14.37 ?  154 ALA   A HB2  1 
ATOM   3205 H HB3  A ALA   A 1 154 ? 15.602 -2.904  8.109   0.66 15.26 ?  154 ALA   A HB3  1 
ATOM   3206 H HB3  B ALA   A 1 154 ? 15.678 -2.809  8.597   0.34 14.37 ?  154 ALA   A HB3  1 
ATOM   3207 N N    A VAL   A 1 155 ? 12.267 -3.772  6.401   0.46 10.40 ?  155 VAL   A N    1 
ATOM   3208 N N    B VAL   A 1 155 ? 12.363 -3.624  6.786   0.34 11.22 ?  155 VAL   A N    1 
ATOM   3209 C CA   A VAL   A 1 155 ? 11.622 -3.327  5.169   0.46 12.18 ?  155 VAL   A CA   1 
ATOM   3210 C CA   B VAL   A 1 155 ? 11.754 -3.161  5.545   0.34 12.60 ?  155 VAL   A CA   1 
ATOM   3211 C CA   T VAL   A 1 155 ? 11.628 -3.337  5.280   0.20 13.46 ?  155 VAL   A CA   1 
ATOM   3212 C C    A VAL   A 1 155 ? 10.876 -2.036  5.486   0.46 13.69 ?  155 VAL   A C    1 
ATOM   3213 C C    B VAL   A 1 155 ? 11.044 -1.847  5.841   0.34 13.68 ?  155 VAL   A C    1 
ATOM   3214 C C    T VAL   A 1 155 ? 11.014 -1.969  5.579   0.20 13.44 ?  155 VAL   A C    1 
ATOM   3215 O O    A VAL   A 1 155 ? 9.890  -2.050  6.233   0.46 13.84 ?  155 VAL   A O    1 
ATOM   3216 O O    B VAL   A 1 155 ? 10.114 -1.803  6.657   0.34 13.26 ?  155 VAL   A O    1 
ATOM   3217 O O    T VAL   A 1 155 ? 10.176 -1.834  6.471   0.20 13.32 ?  155 VAL   A O    1 
ATOM   3218 C CB   A VAL   A 1 155 ? 10.665 -4.394  4.621   0.46 12.93 ?  155 VAL   A CB   1 
ATOM   3219 C CB   B VAL   A 1 155 ? 10.799 -4.213  4.959   0.34 12.92 ?  155 VAL   A CB   1 
ATOM   3220 C CB   T VAL   A 1 155 ? 10.597 -4.334  4.716   0.20 13.67 ?  155 VAL   A CB   1 
ATOM   3221 C CG1  A VAL   A 1 155 ? 9.970  -3.898  3.356   0.46 13.57 ?  155 VAL   A CG1  1 
ATOM   3222 C CG1  B VAL   A 1 155 ? 10.105 -3.681  3.711   0.34 13.47 ?  155 VAL   A CG1  1 
ATOM   3223 C CG1  T VAL   A 1 155 ? 9.908  -3.753  3.491   0.20 14.03 ?  155 VAL   A CG1  1 
ATOM   3224 C CG2  A VAL   A 1 155 ? 11.408 -5.698  4.355   0.46 13.82 ?  155 VAL   A CG2  1 
ATOM   3225 C CG2  B VAL   A 1 155 ? 11.567 -5.497  4.643   0.34 13.71 ?  155 VAL   A CG2  1 
ATOM   3226 C CG2  T VAL   A 1 155 ? 11.270 -5.661  4.374   0.20 13.88 ?  155 VAL   A CG2  1 
ATOM   3227 H H    A VAL   A 1 155 ? 11.711 -4.060  6.991   0.46 12.45 ?  155 VAL   A H    1 
ATOM   3228 H H    B VAL   A 1 155 ? 11.787 -3.888  7.365   0.34 13.44 ?  155 VAL   A H    1 
ATOM   3229 H HA   A VAL   A 1 155 ? 12.299 -3.143  4.497   0.46 14.59 ?  155 VAL   A HA   1 
ATOM   3230 H HA   B VAL   A 1 155 ? 12.448 -2.990  4.887   0.34 15.09 ?  155 VAL   A HA   1 
ATOM   3231 H HB   A VAL   A 1 155 ? 9.981  -4.574  5.287   0.46 15.49 ?  155 VAL   A HB   1 
ATOM   3232 H HB   B VAL   A 1 155 ? 10.119 -4.426  5.616   0.34 15.48 ?  155 VAL   A HB   1 
ATOM   3233 H HB   T VAL   A 1 155 ? 9.921  -4.508  5.390   0.20 16.37 ?  155 VAL   A HB   1 
ATOM   3234 H HG11 A VAL   A 1 155 ? 9.483  -4.635  2.955   0.46 16.26 ?  155 VAL   A HG11 1 
ATOM   3235 H HG11 B VAL   A 1 155 ? 9.656  -4.417  3.262   0.34 16.13 ?  155 VAL   A HG11 1 
ATOM   3236 H HG11 T VAL   A 1 155 ? 9.411  -4.458  3.047   0.20 16.81 ?  155 VAL   A HG11 1 
ATOM   3237 H HG12 A VAL   A 1 155 ? 9.353  -3.186  3.591   0.46 16.26 ?  155 VAL   A HG12 1 
ATOM   3238 H HG12 B VAL   A 1 155 ? 9.455  -3.009  3.970   0.34 16.13 ?  155 VAL   A HG12 1 
ATOM   3239 H HG12 T VAL   A 1 155 ? 9.303  -3.050  3.772   0.20 16.81 ?  155 VAL   A HG12 1 
ATOM   3240 H HG13 A VAL   A 1 155 ? 10.639 -3.568  2.738   0.46 16.26 ?  155 VAL   A HG13 1 
ATOM   3241 H HG13 B VAL   A 1 155 ? 10.769 -3.293  3.120   0.34 16.13 ?  155 VAL   A HG13 1 
ATOM   3242 H HG13 T VAL   A 1 155 ? 10.581 -3.395  2.892   0.20 16.81 ?  155 VAL   A HG13 1 
ATOM   3243 H HG21 A VAL   A 1 155 ? 10.798 -6.332  3.948   0.46 16.55 ?  155 VAL   A HG21 1 
ATOM   3244 H HG21 B VAL   A 1 155 ? 10.978 -6.115  4.183   0.34 16.43 ?  155 VAL   A HG21 1 
ATOM   3245 H HG21 T VAL   A 1 155 ? 10.604 -6.274  4.025   0.20 16.63 ?  155 VAL   A HG21 1 
ATOM   3246 H HG22 A VAL   A 1 155 ? 12.150 -5.520  3.757   0.46 16.55 ?  155 VAL   A HG22 1 
ATOM   3247 H HG22 B VAL   A 1 155 ? 12.325 -5.282  4.075   0.34 16.43 ?  155 VAL   A HG22 1 
ATOM   3248 H HG22 T VAL   A 1 155 ? 11.956 -5.504  3.705   0.20 16.63 ?  155 VAL   A HG22 1 
ATOM   3249 H HG23 A VAL   A 1 155 ? 11.739 -6.051  5.197   0.46 16.55 ?  155 VAL   A HG23 1 
ATOM   3250 H HG23 B VAL   A 1 155 ? 11.880 -5.893  5.472   0.34 16.43 ?  155 VAL   A HG23 1 
ATOM   3251 H HG23 T VAL   A 1 155 ? 11.671 -6.030  5.177   0.20 16.63 ?  155 VAL   A HG23 1 
ATOM   3252 N N    A PHE   A 1 156 ? 11.331 -0.919  4.905   0.46 15.50 ?  156 PHE   A N    1 
ATOM   3253 N N    B PHE   A 1 156 ? 11.495 -0.775  5.185   0.34 14.69 ?  156 PHE   A N    1 
ATOM   3254 N N    T PHE   A 1 156 ? 11.445 -0.955  4.824   0.20 13.56 ?  156 PHE   A N    1 
ATOM   3255 C CA   A PHE   A 1 156 ? 10.787 0.392   5.272   0.46 17.19 ?  156 PHE   A CA   1 
ATOM   3256 C CA   B PHE   A 1 156 ? 11.022 0.568   5.512   0.34 15.97 ?  156 PHE   A CA   1 
ATOM   3257 C CA   T PHE   A 1 156 ? 11.015 0.415   5.094   0.20 13.66 ?  156 PHE   A CA   1 
ATOM   3258 C C    A PHE   A 1 156 ? 9.320  0.535   4.878   0.46 17.13 ?  156 PHE   A C    1 
ATOM   3259 C C    B PHE   A 1 156 ? 9.513  0.692   5.336   0.34 16.07 ?  156 PHE   A C    1 
ATOM   3260 C C    T PHE   A 1 156 ? 9.553  0.630   4.726   0.20 14.31 ?  156 PHE   A C    1 
ATOM   3261 O O    A PHE   A 1 156 ? 8.514  1.069   5.651   0.46 17.46 ?  156 PHE   A O    1 
ATOM   3262 O O    B PHE   A 1 156 ? 8.807  1.169   6.233   0.34 15.91 ?  156 PHE   A O    1 
ATOM   3263 O O    T PHE   A 1 156 ? 8.812  1.289   5.465   0.20 14.93 ?  156 PHE   A O    1 
ATOM   3264 C CB   A PHE   A 1 156 ? 11.626 1.507   4.640   0.46 18.77 ?  156 PHE   A CB   1 
ATOM   3265 C CB   B PHE   A 1 156 ? 11.742 1.582   4.623   0.34 16.42 ?  156 PHE   A CB   1 
ATOM   3266 C CB   T PHE   A 1 156 ? 11.902 1.391   4.320   0.20 13.03 ?  156 PHE   A CB   1 
ATOM   3267 C CG   A PHE   A 1 156 ? 11.155 2.901   4.989   0.46 20.60 ?  156 PHE   A CG   1 
ATOM   3268 C CG   B PHE   A 1 156 ? 11.420 3.014   4.949   0.34 16.81 ?  156 PHE   A CG   1 
ATOM   3269 C CG   T PHE   A 1 156 ? 11.549 2.843   4.532   0.20 12.95 ?  156 PHE   A CG   1 
ATOM   3270 C CD1  A PHE   A 1 156 ? 11.121 3.326   6.309   0.46 21.67 ?  156 PHE   A CD1  1 
ATOM   3271 C CD1  B PHE   A 1 156 ? 10.315 3.642   4.394   0.34 17.27 ?  156 PHE   A CD1  1 
ATOM   3272 C CD1  T PHE   A 1 156 ? 11.908 3.494   5.705   0.20 13.20 ?  156 PHE   A CD1  1 
ATOM   3273 C CD2  A PHE   A 1 156 ? 10.765 3.791   3.998   0.46 21.80 ?  156 PHE   A CD2  1 
ATOM   3274 C CD2  B PHE   A 1 156 ? 12.231 3.734   5.811   0.34 16.38 ?  156 PHE   A CD2  1 
ATOM   3275 C CD2  T PHE   A 1 156 ? 10.875 3.559   3.555   0.20 13.35 ?  156 PHE   A CD2  1 
ATOM   3276 C CE1  A PHE   A 1 156 ? 10.695 4.605   6.637   0.46 22.49 ?  156 PHE   A CE1  1 
ATOM   3277 C CE1  B PHE   A 1 156 ? 10.022 4.962   4.697   0.34 17.40 ?  156 PHE   A CE1  1 
ATOM   3278 C CE1  T PHE   A 1 156 ? 11.590 4.827   5.903   0.20 13.86 ?  156 PHE   A CE1  1 
ATOM   3279 C CE2  A PHE   A 1 156 ? 10.336 5.074   4.319   0.46 22.52 ?  156 PHE   A CE2  1 
ATOM   3280 C CE2  B PHE   A 1 156 ? 11.947 5.054   6.116   0.34 16.74 ?  156 PHE   A CE2  1 
ATOM   3281 C CE2  T PHE   A 1 156 ? 10.557 4.893   3.748   0.20 13.68 ?  156 PHE   A CE2  1 
ATOM   3282 C CZ   A PHE   A 1 156 ? 10.303 5.479   5.641   0.46 22.82 ?  156 PHE   A CZ   1 
ATOM   3283 C CZ   B PHE   A 1 156 ? 10.844 5.669   5.559   0.34 17.32 ?  156 PHE   A CZ   1 
ATOM   3284 C CZ   T PHE   A 1 156 ? 10.916 5.527   4.924   0.20 13.96 ?  156 PHE   A CZ   1 
ATOM   3285 H H    A PHE   A 1 156 ? 11.948 -0.900  4.306   0.46 18.57 ?  156 PHE   A H    1 
ATOM   3286 H H    B PHE   A 1 156 ? 12.078 -0.800  4.553   0.34 17.61 ?  156 PHE   A H    1 
ATOM   3287 H H    T PHE   A 1 156 ? 11.984 -1.038  4.161   0.20 16.25 ?  156 PHE   A H    1 
ATOM   3288 H HA   A PHE   A 1 156 ? 10.849 0.491   6.234   0.46 20.60 ?  156 PHE   A HA   1 
ATOM   3289 H HA   B PHE   A 1 156 ? 11.243 0.767   6.437   0.34 19.13 ?  156 PHE   A HA   1 
ATOM   3290 H HA   T PHE   A 1 156 ? 11.120 0.596   6.041   0.20 16.36 ?  156 PHE   A HA   1 
ATOM   3291 H HB2  A PHE   A 1 156 ? 12.546 1.422   4.944   0.46 22.50 ?  156 PHE   A HB2  1 
ATOM   3292 H HB2  B PHE   A 1 156 ? 12.703 1.463   4.725   0.34 19.68 ?  156 PHE   A HB2  1 
ATOM   3293 H HB2  T PHE   A 1 156 ? 12.821 1.262   4.600   0.20 15.61 ?  156 PHE   A HB2  1 
ATOM   3294 H HB3  A PHE   A 1 156 ? 11.594 1.417   3.675   0.46 22.50 ?  156 PHE   A HB3  1 
ATOM   3295 H HB3  B PHE   A 1 156 ? 11.493 1.424   3.700   0.34 19.68 ?  156 PHE   A HB3  1 
ATOM   3296 H HB3  T PHE   A 1 156 ? 11.817 1.200   3.373   0.20 15.61 ?  156 PHE   A HB3  1 
ATOM   3297 H HD1  A PHE   A 1 156 ? 11.384 2.742   6.985   0.46 25.98 ?  156 PHE   A HD1  1 
ATOM   3298 H HD1  B PHE   A 1 156 ? 9.766  3.171   3.812   0.34 20.70 ?  156 PHE   A HD1  1 
ATOM   3299 H HD1  T PHE   A 1 156 ? 12.361 3.022   6.371   0.20 15.82 ?  156 PHE   A HD1  1 
ATOM   3300 H HD2  A PHE   A 1 156 ? 10.786 3.524   3.109   0.46 26.14 ?  156 PHE   A HD2  1 
ATOM   3301 H HD2  B PHE   A 1 156 ? 12.979 3.322   6.189   0.34 19.62 ?  156 PHE   A HD2  1 
ATOM   3302 H HD2  T PHE   A 1 156 ? 10.630 3.135   2.767   0.20 15.99 ?  156 PHE   A HD2  1 
ATOM   3303 H HE1  A PHE   A 1 156 ? 10.675 4.874   7.529   0.46 26.96 ?  156 PHE   A HE1  1 
ATOM   3304 H HE1  B PHE   A 1 156 ? 9.281  5.373   4.318   0.34 20.85 ?  156 PHE   A HE1  1 
ATOM   3305 H HE1  T PHE   A 1 156 ? 11.833 5.245   6.699   0.20 16.61 ?  156 PHE   A HE1  1 
ATOM   3306 H HE2  A PHE   A 1 156 ? 10.076 5.660   3.647   0.46 26.99 ?  156 PHE   A HE2  1 
ATOM   3307 H HE2  B PHE   A 1 156 ? 12.500 5.522   6.699   0.34 20.06 ?  156 PHE   A HE2  1 
ATOM   3308 H HE2  T PHE   A 1 156 ? 10.100 5.359   3.090   0.20 16.39 ?  156 PHE   A HE2  1 
ATOM   3309 H HZ   A PHE   A 1 156 ? 10.019 6.338   5.861   0.46 27.36 ?  156 PHE   A HZ   1 
ATOM   3310 H HZ   B PHE   A 1 156 ? 10.652 6.553   5.766   0.34 20.76 ?  156 PHE   A HZ   1 
ATOM   3311 H HZ   T PHE   A 1 156 ? 10.701 6.419   5.060   0.20 16.72 ?  156 PHE   A HZ   1 
ATOM   3312 N N    A ASP   A 1 157 ? 8.952  0.070   3.688   0.46 17.33 ?  157 ASP   A N    1 
ATOM   3313 N N    B ASP   A 1 157 ? 9.001  0.277   4.183   0.34 15.90 ?  157 ASP   A N    1 
ATOM   3314 N N    T ASP   A 1 157 ? 9.124  0.089   3.592   0.20 14.89 ?  157 ASP   A N    1 
ATOM   3315 C CA   A ASP   A 1 157 ? 7.622  0.311   3.138   0.46 17.88 ?  157 ASP   A CA   1 
ATOM   3316 C CA   B ASP   A 1 157 ? 7.626  0.568   3.795   0.34 16.89 ?  157 ASP   A CA   1 
ATOM   3317 C CA   T ASP   A 1 157 ? 7.809  0.378   3.037   0.20 15.75 ?  157 ASP   A CA   1 
ATOM   3318 C C    A ASP   A 1 157 ? 6.642  -0.741  3.648   0.46 18.09 ?  157 ASP   A C    1 
ATOM   3319 C C    B ASP   A 1 157 ? 6.680  -0.525  4.280   0.34 17.70 ?  157 ASP   A C    1 
ATOM   3320 C C    T ASP   A 1 157 ? 6.791  -0.618  3.580   0.20 16.70 ?  157 ASP   A C    1 
ATOM   3321 O O    A ASP   A 1 157 ? 6.814  -1.934  3.383   0.46 16.98 ?  157 ASP   A O    1 
ATOM   3322 O O    B ASP   A 1 157 ? 6.943  -1.715  4.084   0.34 17.37 ?  157 ASP   A O    1 
ATOM   3323 O O    T ASP   A 1 157 ? 6.936  -1.830  3.386   0.20 16.26 ?  157 ASP   A O    1 
ATOM   3324 C CB   A ASP   A 1 157 ? 7.683  0.283   1.613   0.46 18.54 ?  157 ASP   A CB   1 
ATOM   3325 C CB   B ASP   A 1 157 ? 7.538  0.676   2.275   0.34 17.33 ?  157 ASP   A CB   1 
ATOM   3326 C CB   T ASP   A 1 157 ? 7.883  0.307   1.514   0.20 15.85 ?  157 ASP   A CB   1 
ATOM   3327 C CG   A ASP   A 1 157 ? 6.428  0.838   0.969   0.46 19.25 ?  157 ASP   A CG   1 
ATOM   3328 C CG   B ASP   A 1 157 ? 6.152  1.047   1.799   0.34 17.95 ?  157 ASP   A CG   1 
ATOM   3329 C CG   T ASP   A 1 157 ? 6.681  0.919   0.845   0.20 15.88 ?  157 ASP   A CG   1 
ATOM   3330 O OD1  A ASP   A 1 157 ? 6.185  2.060   1.083   0.46 20.43 ?  157 ASP   A OD1  1 
ATOM   3331 O OD1  B ASP   A 1 157 ? 5.728  2.198   2.023   0.34 18.70 ?  157 ASP   A OD1  1 
ATOM   3332 O OD1  T ASP   A 1 157 ? 5.568  0.376   1.005   0.20 16.01 ?  157 ASP   A OD1  1 
ATOM   3333 O OD2  A ASP   A 1 157 ? 5.680  0.051   0.348   0.46 18.65 -1 157 ASP   A OD2  1 
ATOM   3334 O OD2  B ASP   A 1 157 ? 5.481  0.178   1.204   0.34 17.90 -1 157 ASP   A OD2  1 
ATOM   3335 O OD2  T ASP   A 1 157 ? 6.850  1.952   0.166   0.20 15.45 -1 157 ASP   A OD2  1 
ATOM   3336 H H    A ASP   A 1 157 ? 9.461  -0.399  3.175   0.46 20.77 ?  157 ASP   A H    1 
ATOM   3337 H H    B ASP   A 1 157 ? 9.444  -0.178  3.601   0.34 19.05 ?  157 ASP   A H    1 
ATOM   3338 H H    T ASP   A 1 157 ? 9.586  -0.458  3.116   0.20 17.84 ?  157 ASP   A H    1 
ATOM   3339 H HA   A ASP   A 1 157 ? 7.310  1.180   3.422   0.46 21.43 ?  157 ASP   A HA   1 
ATOM   3340 H HA   B ASP   A 1 157 ? 7.358  1.416   4.187   0.34 20.25 ?  157 ASP   A HA   1 
ATOM   3341 H HA   T ASP   A 1 157 ? 7.535  1.270   3.295   0.20 18.88 ?  157 ASP   A HA   1 
ATOM   3342 H HB2  A ASP   A 1 157 ? 8.448  0.805   1.323   0.46 22.22 ?  157 ASP   A HB2  1 
ATOM   3343 H HB2  B ASP   A 1 157 ? 8.180  1.338   1.972   0.34 20.77 ?  157 ASP   A HB2  1 
ATOM   3344 H HB2  T ASP   A 1 157 ? 8.672  0.785   1.217   0.20 18.99 ?  157 ASP   A HB2  1 
ATOM   3345 H HB3  A ASP   A 1 157 ? 7.782  -0.635  1.318   0.46 22.22 ?  157 ASP   A HB3  1 
ATOM   3346 H HB3  B ASP   A 1 157 ? 7.741  -0.187  1.889   0.34 20.77 ?  157 ASP   A HB3  1 
ATOM   3347 H HB3  T ASP   A 1 157 ? 7.937  -0.620  1.240   0.20 18.99 ?  157 ASP   A HB3  1 
ATOM   3348 N N    A LYS   A 1 158 ? 5.600  -0.293  4.359   0.46 19.26 ?  158 LYS   A N    1 
ATOM   3349 N N    B LYS   A 1 158 ? 5.559  -0.114  4.882   0.34 18.88 ?  158 LYS   A N    1 
ATOM   3350 N N    T LYS   A 1 158 ? 5.757  -0.104  4.254   0.20 18.18 ?  158 LYS   A N    1 
ATOM   3351 C CA   A LYS   A 1 158 ? 4.631  -1.222  4.939   0.46 20.02 ?  158 LYS   A CA   1 
ATOM   3352 C CA   B LYS   A 1 158 ? 4.595  -1.088  5.387   0.34 19.50 ?  158 LYS   A CA   1 
ATOM   3353 C CA   T LYS   A 1 158 ? 4.766  -0.981  4.874   0.20 19.62 ?  158 LYS   A CA   1 
ATOM   3354 C C    A LYS   A 1 158 ? 3.898  -2.002  3.853   0.46 19.42 ?  158 LYS   A C    1 
ATOM   3355 C C    B LYS   A 1 158 ? 3.908  -1.830  4.246   0.34 19.38 ?  158 LYS   A C    1 
ATOM   3356 C C    T LYS   A 1 158 ? 4.009  -1.789  3.826   0.20 19.93 ?  158 LYS   A C    1 
ATOM   3357 O O    A LYS   A 1 158 ? 3.707  -3.219  3.969   0.46 19.38 ?  158 LYS   A O    1 
ATOM   3358 O O    B LYS   A 1 158 ? 3.748  -3.055  4.305   0.34 19.88 ?  158 LYS   A O    1 
ATOM   3359 O O    T LYS   A 1 158 ? 3.802  -2.997  3.994   0.20 20.06 ?  158 LYS   A O    1 
ATOM   3360 C CB   A LYS   A 1 158 ? 3.651  -0.453  5.836   0.46 21.46 ?  158 LYS   A CB   1 
ATOM   3361 C CB   B LYS   A 1 158 ? 3.566  -0.393  6.281   0.34 20.34 ?  158 LYS   A CB   1 
ATOM   3362 C CB   T LYS   A 1 158 ? 3.802  -0.158  5.733   0.20 20.63 ?  158 LYS   A CB   1 
ATOM   3363 C CG   A LYS   A 1 158 ? 2.432  -1.245  6.310   0.46 22.92 ?  158 LYS   A CG   1 
ATOM   3364 C CG   B LYS   A 1 158 ? 2.371  -1.260  6.680   0.34 21.47 ?  158 LYS   A CG   1 
ATOM   3365 C CG   T LYS   A 1 158 ? 2.575  -0.924  6.222   0.20 21.63 ?  158 LYS   A CG   1 
ATOM   3366 C CD   A LYS   A 1 158 ? 2.804  -2.476  7.133   0.46 23.92 ?  158 LYS   A CD   1 
ATOM   3367 C CD   B LYS   A 1 158 ? 2.781  -2.475  7.507   0.34 22.35 ?  158 LYS   A CD   1 
ATOM   3368 C CD   T LYS   A 1 158 ? 2.955  -2.117  7.091   0.20 22.53 ?  158 LYS   A CD   1 
ATOM   3369 C CE   A LYS   A 1 158 ? 1.548  -3.151  7.680   0.46 24.58 ?  158 LYS   A CE   1 
ATOM   3370 C CE   B LYS   A 1 158 ? 1.554  -3.199  8.045   0.34 23.02 ?  158 LYS   A CE   1 
ATOM   3371 C CE   T LYS   A 1 158 ? 1.724  -2.920  7.492   0.20 23.10 ?  158 LYS   A CE   1 
ATOM   3372 N NZ   A LYS   A 1 158 ? 1.812  -4.489  8.284   0.46 24.89 ?  158 LYS   A NZ   1 
ATOM   3373 N NZ   B LYS   A 1 158 ? 1.896  -4.488  8.710   0.34 23.52 ?  158 LYS   A NZ   1 
ATOM   3374 N NZ   T LYS   A 1 158 ? 2.068  -4.119  8.307   0.20 23.38 ?  158 LYS   A NZ   1 
ATOM   3375 H H    A LYS   A 1 158 ? 5.436  0.534   4.519   0.46 23.08 ?  158 LYS   A H    1 
ATOM   3376 H H    B LYS   A 1 158 ? 5.342  0.708   5.000   0.34 22.63 ?  158 LYS   A H    1 
ATOM   3377 H H    T LYS   A 1 158 ? 5.609  0.735   4.364   0.20 21.79 ?  158 LYS   A H    1 
ATOM   3378 H HA   A LYS   A 1 158 ? 5.097  -1.860  5.501   0.46 24.00 ?  158 LYS   A HA   1 
ATOM   3379 H HA   B LYS   A 1 158 ? 5.066  -1.740  5.930   0.34 23.37 ?  158 LYS   A HA   1 
ATOM   3380 H HA   T LYS   A 1 158 ? 5.220  -1.604  5.461   0.20 23.51 ?  158 LYS   A HA   1 
ATOM   3381 H HB2  A LYS   A 1 158 ? 4.126  -0.154  6.632   0.46 25.72 ?  158 LYS   A HB2  1 
ATOM   3382 H HB2  B LYS   A 1 158 ? 4.007  -0.110  7.098   0.34 24.38 ?  158 LYS   A HB2  1 
ATOM   3383 H HB2  T LYS   A 1 158 ? 4.277  0.161   6.520   0.20 24.73 ?  158 LYS   A HB2  1 
ATOM   3384 H HB3  A LYS   A 1 158 ? 3.324  0.320   5.350   0.46 25.72 ?  158 LYS   A HB3  1 
ATOM   3385 H HB3  B LYS   A 1 158 ? 3.223  0.383   5.811   0.34 24.38 ?  158 LYS   A HB3  1 
ATOM   3386 H HB3  T LYS   A 1 158 ? 3.487  0.599   5.216   0.20 24.73 ?  158 LYS   A HB3  1 
ATOM   3387 H HG2  A LYS   A 1 158 ? 1.884  -0.669  6.869   0.46 27.47 ?  158 LYS   A HG2  1 
ATOM   3388 H HG2  B LYS   A 1 158 ? 1.766  -0.726  7.215   0.34 25.73 ?  158 LYS   A HG2  1 
ATOM   3389 H HG2  T LYS   A 1 158 ? 2.027  -0.331  6.757   0.20 25.93 ?  158 LYS   A HG2  1 
ATOM   3390 H HG3  A LYS   A 1 158 ? 1.918  -1.536  5.541   0.46 27.47 ?  158 LYS   A HG3  1 
ATOM   3391 H HG3  B LYS   A 1 158 ? 1.914  -1.574  5.883   0.34 25.73 ?  158 LYS   A HG3  1 
ATOM   3392 H HG3  T LYS   A 1 158 ? 2.064  -1.248  5.463   0.20 25.93 ?  158 LYS   A HG3  1 
ATOM   3393 H HD2  A LYS   A 1 158 ? 3.275  -3.109  6.571   0.46 28.68 ?  158 LYS   A HD2  1 
ATOM   3394 H HD2  B LYS   A 1 158 ? 3.283  -3.091  6.952   0.34 26.80 ?  158 LYS   A HD2  1 
ATOM   3395 H HD2  T LYS   A 1 158 ? 3.549  -2.702  6.597   0.20 27.01 ?  158 LYS   A HD2  1 
ATOM   3396 H HD3  A LYS   A 1 158 ? 3.359  -2.207  7.882   0.46 28.68 ?  158 LYS   A HD3  1 
ATOM   3397 H HD3  B LYS   A 1 158 ? 3.318  -2.183  8.262   0.34 26.80 ?  158 LYS   A HD3  1 
ATOM   3398 H HD3  T LYS   A 1 158 ? 3.389  -1.800  7.899   0.20 27.01 ?  158 LYS   A HD3  1 
ATOM   3399 H HE2  A LYS   A 1 158 ? 1.157  -2.585  8.364   0.46 29.46 ?  158 LYS   A HE2  1 
ATOM   3400 H HE2  B LYS   A 1 158 ? 1.116  -2.634  8.700   0.34 27.60 ?  158 LYS   A HE2  1 
ATOM   3401 H HE2  T LYS   A 1 158 ? 1.134  -2.357  8.018   0.20 27.69 ?  158 LYS   A HE2  1 
ATOM   3402 H HE3  A LYS   A 1 158 ? 0.917  -3.272  6.954   0.46 29.46 ?  158 LYS   A HE3  1 
ATOM   3403 H HE3  B LYS   A 1 158 ? 0.945  -3.384  7.313   0.34 27.60 ?  158 LYS   A HE3  1 
ATOM   3404 H HE3  T LYS   A 1 158 ? 1.267  -3.222  6.691   0.20 27.69 ?  158 LYS   A HE3  1 
ATOM   3405 H HZ1  A LYS   A 1 158 ? 1.053  -4.841  8.588   0.46 29.84 ?  158 LYS   A HZ1  1 
ATOM   3406 H HZ1  B LYS   A 1 158 ? 1.156  -4.882  9.009   0.34 28.20 ?  158 LYS   A HZ1  1 
ATOM   3407 H HZ1  T LYS   A 1 158 ? 1.327  -4.564  8.523   0.20 28.03 ?  158 LYS   A HZ1  1 
ATOM   3408 H HZ2  A LYS   A 1 158 ? 2.159  -5.035  7.673   0.46 29.84 ?  158 LYS   A HZ2  1 
ATOM   3409 H HZ2  B LYS   A 1 158 ? 2.300  -5.031  8.132   0.34 28.20 ?  158 LYS   A HZ2  1 
ATOM   3410 H HZ2  T LYS   A 1 158 ? 2.603  -4.659  7.843   0.20 28.03 ?  158 LYS   A HZ2  1 
ATOM   3411 H HZ3  A LYS   A 1 158 ? 2.385  -4.410  8.960   0.46 29.84 ?  158 LYS   A HZ3  1 
ATOM   3412 H HZ3  B LYS   A 1 158 ? 2.442  -4.339  9.396   0.34 28.20 ?  158 LYS   A HZ3  1 
ATOM   3413 H HZ3  T LYS   A 1 158 ? 2.484  -3.871  9.053   0.20 28.03 ?  158 LYS   A HZ3  1 
ATOM   3414 N N    A ASN   A 1 159 ? 3.487  -1.321  2.783   0.46 20.19 ?  159 ASN   A N    1 
ATOM   3415 N N    B ASN   A 1 159 ? 3.485  -1.109  3.205   0.34 19.11 ?  159 ASN   A N    1 
ATOM   3416 N N    T ASN   A 1 159 ? 3.585  -1.145  2.745   0.20 20.49 ?  159 ASN   A N    1 
ATOM   3417 C CA   A ASN   A 1 159 ? 2.797  -2.009  1.698   0.46 20.34 ?  159 ASN   A CA   1 
ATOM   3418 C CA   B ASN   A 1 159 ? 2.863  -1.769  2.061   0.34 18.24 ?  159 ASN   A CA   1 
ATOM   3419 C CA   T ASN   A 1 159 ? 2.847  -1.833  1.691   0.20 20.92 ?  159 ASN   A CA   1 
ATOM   3420 C C    A ASN   A 1 159 ? 3.681  -3.090  1.074   0.46 19.03 ?  159 ASN   A C    1 
ATOM   3421 C C    B ASN   A 1 159 ? 3.786  -2.840  1.491   0.34 17.50 ?  159 ASN   A C    1 
ATOM   3422 C C    T ASN   A 1 159 ? 3.684  -2.932  1.039   0.20 20.73 ?  159 ASN   A C    1 
ATOM   3423 O O    A ASN   A 1 159 ? 3.216  -4.203  0.797   0.46 19.05 ?  159 ASN   A O    1 
ATOM   3424 O O    B ASN   A 1 159 ? 3.370  -3.981  1.261   0.34 16.53 ?  159 ASN   A O    1 
ATOM   3425 O O    T ASN   A 1 159 ? 3.156  -3.972  0.648   0.20 20.81 ?  159 ASN   A O    1 
ATOM   3426 C CB   A ASN   A 1 159 ? 2.317  -0.982  0.669   0.46 22.07 ?  159 ASN   A CB   1 
ATOM   3427 C CB   B ASN   A 1 159 ? 2.499  -0.737  0.990   0.34 18.59 ?  159 ASN   A CB   1 
ATOM   3428 C CB   T ASN   A 1 159 ? 2.361  -0.835  0.637   0.20 21.64 ?  159 ASN   A CB   1 
ATOM   3429 C CG   A ASN   A 1 159 ? 1.184  -0.112  1.202   0.46 23.94 ?  159 ASN   A CG   1 
ATOM   3430 C CG   B ASN   A 1 159 ? 1.736  -1.346  -0.179  0.34 19.44 ?  159 ASN   A CG   1 
ATOM   3431 C CG   T ASN   A 1 159 ? 1.193  0.004   1.125   0.20 22.36 ?  159 ASN   A CG   1 
ATOM   3432 O OD1  A ASN   A 1 159 ? 0.337  -0.589  1.955   0.46 24.96 ?  159 ASN   A OD1  1 
ATOM   3433 O OD1  B ASN   A 1 159 ? 0.512  -1.235  -0.256  0.34 20.58 ?  159 ASN   A OD1  1 
ATOM   3434 O OD1  T ASN   A 1 159 ? 0.371  -0.461  1.914   0.20 22.88 ?  159 ASN   A OD1  1 
ATOM   3435 N ND2  A ASN   A 1 159 ? 1.164  1.165   0.815   0.46 24.91 ?  159 ASN   A ND2  1 
ATOM   3436 N ND2  B ASN   A 1 159 ? 2.458  -1.978  -1.100  0.34 19.18 ?  159 ASN   A ND2  1 
ATOM   3437 N ND2  T ASN   A 1 159 ? 1.114  1.243   0.657   0.20 22.66 ?  159 ASN   A ND2  1 
ATOM   3438 H H    A ASN   A 1 159 ? 3.600  -0.476  2.668   0.46 24.20 ?  159 ASN   A H    1 
ATOM   3439 H H    B ASN   A 1 159 ? 3.554  -0.256  3.138   0.34 22.90 ?  159 ASN   A H    1 
ATOM   3440 H H    T ASN   A 1 159 ? 3.706  -0.307  2.602   0.20 24.56 ?  159 ASN   A H    1 
ATOM   3441 H HA   A ASN   A 1 159 ? 2.010  -2.443  2.062   0.46 24.38 ?  159 ASN   A HA   1 
ATOM   3442 H HA   B ASN   A 1 159 ? 2.042  -2.198  2.353   0.34 21.86 ?  159 ASN   A HA   1 
ATOM   3443 H HA   T ASN   A 1 159 ? 2.068  -2.254  2.082   0.20 25.08 ?  159 ASN   A HA   1 
ATOM   3444 H HB2  A ASN   A 1 159 ? 3.048  -0.393  0.433   0.46 26.45 ?  159 ASN   A HB2  1 
ATOM   3445 H HB2  B ASN   A 1 159 ? 1.935  -0.051  1.386   0.34 22.28 ?  159 ASN   A HB2  1 
ATOM   3446 H HB2  T ASN   A 1 159 ? 3.087  -0.235  0.409   0.20 25.94 ?  159 ASN   A HB2  1 
ATOM   3447 H HB3  A ASN   A 1 159 ? 1.988  -1.442  -0.116  0.46 26.45 ?  159 ASN   A HB3  1 
ATOM   3448 H HB3  B ASN   A 1 159 ? 3.309  -0.339  0.641   0.34 22.28 ?  159 ASN   A HB3  1 
ATOM   3449 H HB3  T ASN   A 1 159 ? 2.074  -1.325  -0.151  0.20 25.94 ?  159 ASN   A HB3  1 
ATOM   3450 H HD21 A ASN   A 1 159 ? 0.542  1.695   1.090   0.46 29.87 ?  159 ASN   A HD21 1 
ATOM   3451 H HD21 B ASN   A 1 159 ? 2.073  -2.345  -1.778  0.34 22.99 ?  159 ASN   A HD21 1 
ATOM   3452 H HD21 T ASN   A 1 159 ? 0.468  1.755   0.904   0.20 27.16 ?  159 ASN   A HD21 1 
ATOM   3453 H HD22 A ASN   A 1 159 ? 1.778  1.463   0.293   0.46 29.87 ?  159 ASN   A HD22 1 
ATOM   3454 H HD22 B ASN   A 1 159 ? 3.313  -2.033  -1.015  0.34 22.99 ?  159 ASN   A HD22 1 
ATOM   3455 H HD22 T ASN   A 1 159 ? 1.708  1.533   0.109   0.20 27.16 ?  159 ASN   A HD22 1 
ATOM   3456 N N    A LEU   A 1 160 ? 4.968  -2.799  0.884   0.46 17.51 ?  160 LEU   A N    1 
ATOM   3457 N N    B LEU   A 1 160 ? 5.051  -2.489  1.267   0.34 16.97 ?  160 LEU   A N    1 
ATOM   3458 N N    T LEU   A 1 160 ? 4.987  -2.701  0.926   0.20 20.31 ?  160 LEU   A N    1 
ATOM   3459 C CA   A LEU   A 1 160 ? 5.869  -3.795  0.313   0.46 16.44 ?  160 LEU   A CA   1 
ATOM   3460 C CA   B LEU   A 1 160 ? 6.000  -3.471  0.756   0.34 15.89 ?  160 LEU   A CA   1 
ATOM   3461 C CA   T LEU   A 1 160 ? 5.885  -3.698  0.357   0.20 19.96 ?  160 LEU   A CA   1 
ATOM   3462 C C    A LEU   A 1 160 ? 6.081  -4.955  1.274   0.46 14.90 ?  160 LEU   A C    1 
ATOM   3463 C C    B LEU   A 1 160 ? 6.200  -4.606  1.749   0.34 14.01 ?  160 LEU   A C    1 
ATOM   3464 O O    A LEU   A 1 160 ? 6.099  -6.121  0.860   0.46 14.66 ?  160 LEU   A O    1 
ATOM   3465 O O    B LEU   A 1 160 ? 6.225  -5.780  1.364   0.34 14.22 ?  160 LEU   A O    1 
ATOM   3466 C CB   A LEU   A 1 160 ? 7.204  -3.143  -0.028  0.46 16.24 ?  160 LEU   A CB   1 
ATOM   3467 C CB   B LEU   A 1 160 ? 7.332  -2.796  0.442   0.34 16.24 ?  160 LEU   A CB   1 
ATOM   3468 C CB   T LEU   A 1 160 ? 7.258  -3.089  0.082   0.20 19.57 ?  160 LEU   A CB   1 
ATOM   3469 C CG   A LEU   A 1 160 ? 8.303  -4.121  -0.430  0.46 16.90 ?  160 LEU   A CG   1 
ATOM   3470 C CG   B LEU   A 1 160 ? 8.439  -3.780  0.073   0.34 16.73 ?  160 LEU   A CG   1 
ATOM   3471 C CG   T LEU   A 1 160 ? 8.333  -4.085  -0.352  0.20 19.52 ?  160 LEU   A CG   1 
ATOM   3472 C CD1  A LEU   A 1 160 ? 7.869  -4.894  -1.655  0.46 17.75 ?  160 LEU   A CD1  1 
ATOM   3473 C CD1  B LEU   A 1 160 ? 8.046  -4.563  -1.166  0.34 16.91 ?  160 LEU   A CD1  1 
ATOM   3474 C CD1  T LEU   A 1 160 ? 7.905  -4.828  -1.603  0.20 19.66 ?  160 LEU   A CD1  1 
ATOM   3475 C CD2  A LEU   A 1 160 ? 9.608  -3.387  -0.680  0.46 16.85 ?  160 LEU   A CD2  1 
ATOM   3476 C CD2  B LEU   A 1 160 ? 9.753  -3.060  -0.137  0.34 16.63 ?  160 LEU   A CD2  1 
ATOM   3477 C CD2  T LEU   A 1 160 ? 9.654  -3.375  -0.576  0.20 19.35 ?  160 LEU   A CD2  1 
ATOM   3478 H H    A LEU   A 1 160 ? 5.339  -2.054  1.100   0.46 20.98 ?  160 LEU   A H    1 
ATOM   3479 H H    B LEU   A 1 160 ? 5.376  -1.706  1.410   0.34 20.33 ?  160 LEU   A H    1 
ATOM   3480 H H    T LEU   A 1 160 ? 5.377  -1.974  1.171   0.20 24.34 ?  160 LEU   A H    1 
ATOM   3481 H HA   A LEU   A 1 160 ? 5.477  -4.139  -0.502  0.46 19.70 ?  160 LEU   A HA   1 
ATOM   3482 H HA   B LEU   A 1 160 ? 5.646  -3.844  -0.066  0.34 19.04 ?  160 LEU   A HA   1 
ATOM   3483 H HB2  A LEU   A 1 160 ? 7.070  -2.523  -0.763  0.46 19.46 ?  160 LEU   A HB2  1 
ATOM   3484 H HB2  B LEU   A 1 160 ? 7.207  -2.189  -0.307  0.34 19.47 ?  160 LEU   A HB2  1 
ATOM   3485 H HB2  T LEU   A 1 160 ? 7.168  -2.423  -0.619  0.20 23.46 ?  160 LEU   A HB2  1 
ATOM   3486 H HB3  A LEU   A 1 160 ? 7.515  -2.662  0.754   0.46 19.46 ?  160 LEU   A HB3  1 
ATOM   3487 H HB3  B LEU   A 1 160 ? 7.621  -2.300  1.222   0.34 19.47 ?  160 LEU   A HB3  1 
ATOM   3488 H HB3  T LEU   A 1 160 ? 7.573  -2.667  0.896   0.20 23.46 ?  160 LEU   A HB3  1 
ATOM   3489 H HG   A LEU   A 1 160 ? 8.458  -4.750  0.291   0.46 20.25 ?  160 LEU   A HG   1 
ATOM   3490 H HG   B LEU   A 1 160 ? 8.568  -4.412  0.797   0.34 20.05 ?  160 LEU   A HG   1 
ATOM   3491 H HG   T LEU   A 1 160 ? 8.462  -4.736  0.356   0.20 23.39 ?  160 LEU   A HG   1 
ATOM   3492 H HD11 A LEU   A 1 160 ? 8.600  -5.458  -1.939  0.46 21.27 ?  160 LEU   A HD11 1 
ATOM   3493 H HD11 B LEU   A 1 160 ? 8.806  -5.086  -1.460  0.34 20.26 ?  160 LEU   A HD11 1 
ATOM   3494 H HD11 T LEU   A 1 160 ? 8.645  -5.372  -1.913  0.20 23.57 ?  160 LEU   A HD11 1 
ATOM   3495 H HD12 A LEU   A 1 160 ? 7.099  -5.437  -1.429  0.46 21.27 ?  160 LEU   A HD12 1 
ATOM   3496 H HD12 B LEU   A 1 160 ? 7.305  -5.152  -0.948  0.34 20.26 ?  160 LEU   A HD12 1 
ATOM   3497 H HD12 T LEU   A 1 160 ? 7.145  -5.391  -1.391  0.20 23.57 ?  160 LEU   A HD12 1 
ATOM   3498 H HD13 A LEU   A 1 160 ? 7.638  -4.265  -2.356  0.46 21.27 ?  160 LEU   A HD13 1 
ATOM   3499 H HD13 B LEU   A 1 160 ? 7.780  -3.941  -1.861  0.34 20.26 ?  160 LEU   A HD13 1 
ATOM   3500 H HD13 T LEU   A 1 160 ? 7.661  -4.181  -2.284  0.20 23.57 ?  160 LEU   A HD13 1 
ATOM   3501 H HD21 A LEU   A 1 160 ? 10.290 -4.030  -0.932  0.46 20.19 ?  160 LEU   A HD21 1 
ATOM   3502 H HD21 B LEU   A 1 160 ? 10.435 -3.711  -0.365  0.34 19.93 ?  160 LEU   A HD21 1 
ATOM   3503 H HD21 T LEU   A 1 160 ? 10.319 -4.026  -0.848  0.20 23.19 ?  160 LEU   A HD21 1 
ATOM   3504 H HD22 A LEU   A 1 160 ? 9.480  -2.745  -1.397  0.46 20.19 ?  160 LEU   A HD22 1 
ATOM   3505 H HD22 B LEU   A 1 160 ? 9.651  -2.421  -0.859  0.34 19.93 ?  160 LEU   A HD22 1 
ATOM   3506 H HD22 T LEU   A 1 160 ? 9.538  -2.709  -1.272  0.20 23.19 ?  160 LEU   A HD22 1 
ATOM   3507 H HD23 A LEU   A 1 160 ? 9.876  -2.924  0.131   0.46 20.19 ?  160 LEU   A HD23 1 
ATOM   3508 H HD23 B LEU   A 1 160 ? 9.995  -2.601  0.682   0.34 19.93 ?  160 LEU   A HD23 1 
ATOM   3509 H HD23 T LEU   A 1 160 ? 9.927  -2.947  0.250   0.20 23.19 ?  160 LEU   A HD23 1 
ATOM   3510 N N    A TYR   A 1 161 ? 6.261  -4.648  2.558   0.66 15.36 ?  161 TYR   A N    1 
ATOM   3511 N N    B TYR   A 1 161 ? 6.352  -4.275  3.032   0.34 13.58 ?  161 TYR   A N    1 
ATOM   3512 C CA   A TYR   A 1 161 ? 6.414  -5.686  3.569   0.66 14.98 ?  161 TYR   A CA   1 
ATOM   3513 C CA   B TYR   A 1 161 ? 6.512  -5.314  4.042   0.34 12.74 ?  161 TYR   A CA   1 
ATOM   3514 C C    A TYR   A 1 161 ? 5.261  -6.680  3.516   0.66 15.20 ?  161 TYR   A C    1 
ATOM   3515 C C    B TYR   A 1 161 ? 5.365  -6.313  3.989   0.34 13.07 ?  161 TYR   A C    1 
ATOM   3516 O O    A TYR   A 1 161 ? 5.475  -7.895  3.481   0.66 14.45 ?  161 TYR   A O    1 
ATOM   3517 O O    B TYR   A 1 161 ? 5.586  -7.528  4.032   0.34 12.46 ?  161 TYR   A O    1 
ATOM   3518 C CB   A TYR   A 1 161 ? 6.508  -5.046  4.955   0.66 15.12 ?  161 TYR   A CB   1 
ATOM   3519 C CB   B TYR   A 1 161 ? 6.627  -4.684  5.430   0.34 12.68 ?  161 TYR   A CB   1 
ATOM   3520 C CG   A TYR   A 1 161 ? 6.404  -6.048  6.079   0.66 14.90 ?  161 TYR   A CG   1 
ATOM   3521 C CG   B TYR   A 1 161 ? 6.516  -5.672  6.568   0.34 12.52 ?  161 TYR   A CG   1 
ATOM   3522 C CD1  A TYR   A 1 161 ? 7.512  -6.772  6.489   0.66 14.61 ?  161 TYR   A CD1  1 
ATOM   3523 C CD1  B TYR   A 1 161 ? 7.611  -6.422  6.980   0.34 12.10 ?  161 TYR   A CD1  1 
ATOM   3524 C CD2  A TYR   A 1 161 ? 5.196  -6.274  6.734   0.66 15.09 ?  161 TYR   A CD2  1 
ATOM   3525 C CD2  B TYR   A 1 161 ? 5.316  -5.843  7.241   0.34 12.80 ?  161 TYR   A CD2  1 
ATOM   3526 C CE1  A TYR   A 1 161 ? 7.424  -7.698  7.508   0.66 14.04 ?  161 TYR   A CE1  1 
ATOM   3527 C CE1  B TYR   A 1 161 ? 7.506  -7.325  8.025   0.34 12.77 ?  161 TYR   A CE1  1 
ATOM   3528 C CE2  A TYR   A 1 161 ? 5.099  -7.206  7.757   0.66 14.47 ?  161 TYR   A CE2  1 
ATOM   3529 C CE2  B TYR   A 1 161 ? 5.200  -6.739  8.284   0.34 13.59 ?  161 TYR   A CE2  1 
ATOM   3530 C CZ   A TYR   A 1 161 ? 6.217  -7.915  8.140   0.66 14.38 ?  161 TYR   A CZ   1 
ATOM   3531 C CZ   B TYR   A 1 161 ? 6.295  -7.475  8.674   0.34 14.14 ?  161 TYR   A CZ   1 
ATOM   3532 O OH   A TYR   A 1 161 ? 6.135  -8.842  9.155   0.66 15.13 ?  161 TYR   A OH   1 
ATOM   3533 O OH   B TYR   A 1 161 ? 6.162  -8.359  9.718   0.34 15.56 ?  161 TYR   A OH   1 
ATOM   3534 H H    A TYR   A 1 161 ? 6.298  -3.858  2.867   0.66 18.40 ?  161 TYR   A H    1 
ATOM   3535 H H    B TYR   A 1 161 ? 6.361  -3.471  3.339   0.34 16.27 ?  161 TYR   A H    1 
ATOM   3536 H HA   A TYR   A 1 161 ? 7.229  -6.186  3.408   0.66 17.95 ?  161 TYR   A HA   1 
ATOM   3537 H HA   B TYR   A 1 161 ? 7.329  -5.799  3.870   0.34 15.26 ?  161 TYR   A HA   1 
ATOM   3538 H HB2  A TYR   A 1 161 ? 7.363  -4.601  5.034   0.66 18.11 ?  161 TYR   A HB2  1 
ATOM   3539 H HB2  B TYR   A 1 161 ? 7.489  -4.249  5.504   0.34 15.19 ?  161 TYR   A HB2  1 
ATOM   3540 H HB3  A TYR   A 1 161 ? 5.786  -4.409  5.058   0.66 18.11 ?  161 TYR   A HB3  1 
ATOM   3541 H HB3  B TYR   A 1 161 ? 5.918  -4.030  5.539   0.34 15.19 ?  161 TYR   A HB3  1 
ATOM   3542 H HD1  A TYR   A 1 161 ? 8.326  -6.643  6.066   0.66 17.51 ?  161 TYR   A HD1  1 
ATOM   3543 H HD1  B TYR   A 1 161 ? 8.426  -6.321  6.546   0.34 14.49 ?  161 TYR   A HD1  1 
ATOM   3544 H HD2  A TYR   A 1 161 ? 4.435  -5.803  6.478   0.66 18.08 ?  161 TYR   A HD2  1 
ATOM   3545 H HD2  B TYR   A 1 161 ? 4.570  -5.350  6.985   0.34 15.34 ?  161 TYR   A HD2  1 
ATOM   3546 H HE1  A TYR   A 1 161 ? 8.175  -8.181  7.767   0.66 16.82 ?  161 TYR   A HE1  1 
ATOM   3547 H HE1  B TYR   A 1 161 ? 8.246  -7.820  8.294   0.34 15.30 ?  161 TYR   A HE1  1 
ATOM   3548 H HE2  A TYR   A 1 161 ? 4.279  -7.346  8.186   0.66 17.34 ?  161 TYR   A HE2  1 
ATOM   3549 H HE2  B TYR   A 1 161 ? 4.385  -6.839  8.725   0.34 16.29 ?  161 TYR   A HE2  1 
ATOM   3550 H HH   A TYR   A 1 161 ? 6.880  -9.201  9.283   0.66 18.13 ?  161 TYR   A HH   1 
ATOM   3551 H HH   B TYR   A 1 161 ? 5.365  -8.352  9.998   0.34 18.65 ?  161 TYR   A HH   1 
ATOM   3552 N N    A ASP   A 1 162 ? 4.023  -6.177  3.512   0.66 16.48 ?  162 ASP   A N    1 
ATOM   3553 N N    B ASP   A 1 162 ? 4.128  -5.824  3.875   0.34 13.98 ?  162 ASP   A N    1 
ATOM   3554 C CA   A ASP   A 1 162 ? 2.865  -7.068  3.452   0.66 17.43 ?  162 ASP   A CA   1 
ATOM   3555 C CA   B ASP   A 1 162 ? 2.997  -6.745  3.858   0.34 14.75 ?  162 ASP   A CA   1 
ATOM   3556 C C    A ASP   A 1 162 ? 2.904  -7.917  2.189   0.66 17.29 ?  162 ASP   A C    1 
ATOM   3557 C C    B ASP   A 1 162 ? 3.001  -7.622  2.610   0.34 15.24 ?  162 ASP   A C    1 
ATOM   3558 O O    A ASP   A 1 162 ? 2.604  -9.117  2.226   0.66 17.12 ?  162 ASP   A O    1 
ATOM   3559 O O    B ASP   A 1 162 ? 2.585  -8.786  2.674   0.34 15.42 ?  162 ASP   A O    1 
ATOM   3560 C CB   A ASP   A 1 162 ? 1.560  -6.263  3.518   0.66 18.81 ?  162 ASP   A CB   1 
ATOM   3561 C CB   B ASP   A 1 162 ? 1.672  -5.988  3.993   0.34 15.38 ?  162 ASP   A CB   1 
ATOM   3562 C CG   A ASP   A 1 162 ? 1.281  -5.693  4.894   0.66 20.30 ?  162 ASP   A CG   1 
ATOM   3563 C CG   B ASP   A 1 162 ? 1.428  -5.470  5.401   0.34 16.36 ?  162 ASP   A CG   1 
ATOM   3564 O OD1  A ASP   A 1 162 ? 1.888  -6.155  5.882   0.66 20.85 ?  162 ASP   A OD1  1 
ATOM   3565 O OD1  B ASP   A 1 162 ? 2.164  -5.867  6.328   0.34 16.92 ?  162 ASP   A OD1  1 
ATOM   3566 O OD2  A ASP   A 1 162 ? 0.422  -4.785  4.982   0.66 21.67 -1 162 ASP   A OD2  1 
ATOM   3567 O OD2  B ASP   A 1 162 ? 0.487  -4.665  5.578   0.34 17.48 -1 162 ASP   A OD2  1 
ATOM   3568 H H    A ASP   A 1 162 ? 3.823  -5.348  3.545   0.66 19.74 ?  162 ASP   A H    1 
ATOM   3569 H H    B ASP   A 1 162 ? 3.921  -4.988  3.805   0.34 16.75 ?  162 ASP   A H    1 
ATOM   3570 H HA   A ASP   A 1 162 ? 2.873  -7.674  4.210   0.66 20.89 ?  162 ASP   A HA   1 
ATOM   3571 H HA   B ASP   A 1 162 ? 3.072  -7.336  4.618   0.34 17.67 ?  162 ASP   A HA   1 
ATOM   3572 H HB2  A ASP   A 1 162 ? 1.608  -5.515  2.910   0.66 22.54 ?  162 ASP   A HB2  1 
ATOM   3573 H HB2  B ASP   A 1 162 ? 1.678  -5.223  3.405   0.34 18.43 ?  162 ASP   A HB2  1 
ATOM   3574 H HB3  A ASP   A 1 162 ? 0.808  -6.834  3.287   0.66 22.54 ?  162 ASP   A HB3  1 
ATOM   3575 H HB3  B ASP   A 1 162 ? 0.942  -6.585  3.764   0.34 18.43 ?  162 ASP   A HB3  1 
ATOM   3576 N N    A LYS   A 1 163 ? 3.277  -7.312  1.061   0.66 18.48 ?  163 LYS   A N    1 
ATOM   3577 N N    B LYS   A 1 163 ? 3.479  -7.102  1.477   0.34 16.62 ?  163 LYS   A N    1 
ATOM   3578 C CA   A LYS   A 1 163 ? 3.400  -8.072  -0.177  0.66 19.25 ?  163 LYS   A CA   1 
ATOM   3579 C CA   B LYS   A 1 163 ? 3.463  -7.894  0.249   0.34 17.72 ?  163 LYS   A CA   1 
ATOM   3580 C C    A LYS   A 1 163 ? 4.506  -9.112  -0.066  0.66 18.44 ?  163 LYS   A C    1 
ATOM   3581 C C    B LYS   A 1 163 ? 4.536  -8.977  0.262   0.34 17.58 ?  163 LYS   A C    1 
ATOM   3582 O O    A LYS   A 1 163 ? 4.371  -10.231 -0.574  0.66 19.07 ?  163 LYS   A O    1 
ATOM   3583 O O    B LYS   A 1 163 ? 4.300  -10.092 -0.218  0.34 18.09 ?  163 LYS   A O    1 
ATOM   3584 C CB   A LYS   A 1 163 ? 3.670  -7.116  -1.338  0.66 22.30 ?  163 LYS   A CB   1 
ATOM   3585 C CB   B LYS   A 1 163 ? 3.610  -6.992  -0.975  0.34 19.87 ?  163 LYS   A CB   1 
ATOM   3586 C CG   A LYS   A 1 163 ? 3.697  -7.782  -2.695  0.66 25.89 ?  163 LYS   A CG   1 
ATOM   3587 C CG   B LYS   A 1 163 ? 3.787  -7.752  -2.281  0.34 22.07 ?  163 LYS   A CG   1 
ATOM   3588 C CD   A LYS   A 1 163 ? 4.129  -6.809  -3.772  0.66 28.79 ?  163 LYS   A CD   1 
ATOM   3589 C CD   B LYS   A 1 163 ? 3.093  -7.034  -3.424  0.34 23.71 ?  163 LYS   A CD   1 
ATOM   3590 C CE   A LYS   A 1 163 ? 4.081  -7.459  -5.142  0.66 30.94 ?  163 LYS   A CE   1 
ATOM   3591 C CE   B LYS   A 1 163 ? 3.499  -7.597  -4.774  0.34 25.11 ?  163 LYS   A CE   1 
ATOM   3592 N NZ   A LYS   A 1 163 ? 4.776  -6.642  -6.171  0.66 32.58 ?  163 LYS   A NZ   1 
ATOM   3593 N NZ   B LYS   A 1 163 ? 3.681  -6.504  -5.770  0.34 25.74 ?  163 LYS   A NZ   1 
ATOM   3594 H H    A LYS   A 1 163 ? 3.456  -6.475  0.990   0.66 22.15 ?  163 LYS   A H    1 
ATOM   3595 H H    B LYS   A 1 163 ? 3.807  -6.309  1.393   0.34 19.91 ?  163 LYS   A H    1 
ATOM   3596 H HA   A LYS   A 1 163 ? 2.562  -8.530  -0.355  0.66 23.07 ?  163 LYS   A HA   1 
ATOM   3597 H HA   B LYS   A 1 163 ? 2.606  -8.339  0.181   0.34 21.23 ?  163 LYS   A HA   1 
ATOM   3598 H HB2  A LYS   A 1 163 ? 2.970  -6.439  -1.357  0.66 26.73 ?  163 LYS   A HB2  1 
ATOM   3599 H HB2  B LYS   A 1 163 ? 2.811  -6.446  -1.058  0.34 23.82 ?  163 LYS   A HB2  1 
ATOM   3600 H HB3  A LYS   A 1 163 ? 4.529  -6.692  -1.199  0.66 26.73 ?  163 LYS   A HB3  1 
ATOM   3601 H HB3  B LYS   A 1 163 ? 4.385  -6.423  -0.856  0.34 23.82 ?  163 LYS   A HB3  1 
ATOM   3602 H HG2  A LYS   A 1 163 ? 4.327  -8.519  -2.679  0.66 31.04 ?  163 LYS   A HG2  1 
ATOM   3603 H HG2  B LYS   A 1 163 ? 4.734  -7.817  -2.489  0.34 26.45 ?  163 LYS   A HG2  1 
ATOM   3604 H HG3  A LYS   A 1 163 ? 2.808  -8.105  -2.912  0.66 31.04 ?  163 LYS   A HG3  1 
ATOM   3605 H HG3  B LYS   A 1 163 ? 3.399  -8.638  -2.197  0.34 26.45 ?  163 LYS   A HG3  1 
ATOM   3606 H HD2  A LYS   A 1 163 ? 3.530  -6.045  -3.775  0.66 34.52 ?  163 LYS   A HD2  1 
ATOM   3607 H HD2  B LYS   A 1 163 ? 2.132  -7.139  -3.330  0.34 28.42 ?  163 LYS   A HD2  1 
ATOM   3608 H HD3  A LYS   A 1 163 ? 5.040  -6.522  -3.599  0.66 34.52 ?  163 LYS   A HD3  1 
ATOM   3609 H HD3  B LYS   A 1 163 ? 3.331  -6.095  -3.404  0.34 28.42 ?  163 LYS   A HD3  1 
ATOM   3610 H HE2  A LYS   A 1 163 ? 4.504  -8.330  -5.096  0.66 37.10 ?  163 LYS   A HE2  1 
ATOM   3611 H HE2  B LYS   A 1 163 ? 4.337  -8.076  -4.687  0.34 30.10 ?  163 LYS   A HE2  1 
ATOM   3612 H HE3  A LYS   A 1 163 ? 3.155  -7.556  -5.410  0.66 37.10 ?  163 LYS   A HE3  1 
ATOM   3613 H HE3  B LYS   A 1 163 ? 2.804  -8.192  -5.099  0.34 30.10 ?  163 LYS   A HE3  1 
ATOM   3614 H HZ1  A LYS   A 1 163 ? 4.732  -7.048  -6.961  0.66 39.07 ?  163 LYS   A HZ1  1 
ATOM   3615 H HZ1  B LYS   A 1 163 ? 3.920  -6.842  -6.556  0.34 30.86 ?  163 LYS   A HZ1  1 
ATOM   3616 H HZ2  A LYS   A 1 163 ? 4.390  -5.842  -6.234  0.66 39.07 ?  163 LYS   A HZ2  1 
ATOM   3617 H HZ2  B LYS   A 1 163 ? 2.921  -6.051  -5.867  0.34 30.86 ?  163 LYS   A HZ2  1 
ATOM   3618 H HZ3  A LYS   A 1 163 ? 5.631  -6.534  -5.947  0.66 39.07 ?  163 LYS   A HZ3  1 
ATOM   3619 H HZ3  B LYS   A 1 163 ? 4.316  -5.943  -5.492  0.34 30.86 ?  163 LYS   A HZ3  1 
ATOM   3620 N N    A LEU   A 1 164 ? 5.611  -8.754  0.593   0.66 17.08 ?  164 LEU   A N    1 
ATOM   3621 N N    B LEU   A 1 164 ? 5.721  -8.673  0.801   0.34 16.72 ?  164 LEU   A N    1 
ATOM   3622 C CA   A LEU   A 1 164 ? 6.714  -9.694  0.783   0.66 16.64 ?  164 LEU   A CA   1 
ATOM   3623 C CA   B LEU   A 1 164 ? 6.783  -9.675  0.863   0.34 16.38 ?  164 LEU   A CA   1 
ATOM   3624 C C    A LEU   A 1 164 ? 6.292  -10.874 1.652   0.66 16.65 ?  164 LEU   A C    1 
ATOM   3625 C C    B LEU   A 1 164 ? 6.355  -10.867 1.705   0.34 16.15 ?  164 LEU   A C    1 
ATOM   3626 O O    A LEU   A 1 164 ? 6.609  -12.030 1.349   0.66 17.34 ?  164 LEU   A O    1 
ATOM   3627 O O    B LEU   A 1 164 ? 6.612  -12.022 1.345   0.34 16.52 ?  164 LEU   A O    1 
ATOM   3628 C CB   A LEU   A 1 164 ? 7.896  -8.962  1.412   0.66 16.23 ?  164 LEU   A CB   1 
ATOM   3629 C CB   B LEU   A 1 164 ? 8.047  -9.057  1.459   0.34 16.50 ?  164 LEU   A CB   1 
ATOM   3630 C CG   A LEU   A 1 164 ? 8.661  -8.021  0.480   0.66 16.55 ?  164 LEU   A CG   1 
ATOM   3631 C CG   B LEU   A 1 164 ? 8.761  -7.973  0.653   0.34 16.87 ?  164 LEU   A CG   1 
ATOM   3632 C CD1  A LEU   A 1 164 ? 9.594  -7.129  1.283   0.66 16.11 ?  164 LEU   A CD1  1 
ATOM   3633 C CD1  B LEU   A 1 164 ? 9.699  -7.184  1.553   0.34 17.02 ?  164 LEU   A CD1  1 
ATOM   3634 C CD2  A LEU   A 1 164 ? 9.445  -8.796  -0.567  0.66 16.96 ?  164 LEU   A CD2  1 
ATOM   3635 C CD2  B LEU   A 1 164 ? 9.530  -8.590  -0.500  0.34 17.08 ?  164 LEU   A CD2  1 
ATOM   3636 H H    A LEU   A 1 164 ? 5.745  -7.970  0.930   0.66 20.47 ?  164 LEU   A H    1 
ATOM   3637 H H    B LEU   A 1 164 ? 5.928  -7.911  1.142   0.34 20.04 ?  164 LEU   A H    1 
ATOM   3638 H HA   A LEU   A 1 164 ? 6.989  -10.032 -0.081  0.66 19.94 ?  164 LEU   A HA   1 
ATOM   3639 H HA   B LEU   A 1 164 ? 6.988  -9.989  -0.031  0.34 19.63 ?  164 LEU   A HA   1 
ATOM   3640 H HB2  A LEU   A 1 164 ? 7.568  -8.428  2.154   0.66 19.45 ?  164 LEU   A HB2  1 
ATOM   3641 H HB2  B LEU   A 1 164 ? 7.816  -8.667  2.313   0.34 19.78 ?  164 LEU   A HB2  1 
ATOM   3642 H HB3  A LEU   A 1 164 ? 8.524  -9.620  1.737   0.66 19.45 ?  164 LEU   A HB3  1 
ATOM   3643 H HB3  B LEU   A 1 164 ? 8.691  -9.770  1.598   0.34 19.78 ?  164 LEU   A HB3  1 
ATOM   3644 H HG   A LEU   A 1 164 ? 8.029  -7.447  0.018   0.66 19.84 ?  164 LEU   A HG   1 
ATOM   3645 H HG   B LEU   A 1 164 ? 8.106  -7.358  0.289   0.34 20.21 ?  164 LEU   A HG   1 
ATOM   3646 H HD11 A LEU   A 1 164 ? 10.048 -6.520  0.682   0.66 19.30 ?  164 LEU   A HD11 1 
ATOM   3647 H HD11 B LEU   A 1 164 ? 10.118 -6.479  1.034   0.34 20.39 ?  164 LEU   A HD11 1 
ATOM   3648 H HD12 A LEU   A 1 164 ? 9.071  -6.628  1.930   0.66 19.30 ?  164 LEU   A HD12 1 
ATOM   3649 H HD12 B LEU   A 1 164 ? 9.188  -6.799  2.283   0.34 20.39 ?  164 LEU   A HD12 1 
ATOM   3650 H HD13 A LEU   A 1 164 ? 10.242 -7.685  1.744   0.66 19.30 ?  164 LEU   A HD13 1 
ATOM   3651 H HD13 B LEU   A 1 164 ? 10.377 -7.783  1.905   0.34 20.39 ?  164 LEU   A HD13 1 
ATOM   3652 H HD21 A LEU   A 1 164 ? 9.989  -8.174  -1.080  0.66 20.33 ?  164 LEU   A HD21 1 
ATOM   3653 H HD21 B LEU   A 1 164 ? 9.972  -7.885  -0.998  0.34 20.47 ?  164 LEU   A HD21 1 
ATOM   3654 H HD22 A LEU   A 1 164 ? 10.014 -9.442  -0.123  0.66 20.33 ?  164 LEU   A HD22 1 
ATOM   3655 H HD22 B LEU   A 1 164 ? 10.188 -9.208  -0.144  0.34 20.47 ?  164 LEU   A HD22 1 
ATOM   3656 H HD23 A LEU   A 1 164 ? 8.823  -9.251  -1.156  0.66 20.33 ?  164 LEU   A HD23 1 
ATOM   3657 H HD23 B LEU   A 1 164 ? 8.908  -9.062  -1.074  0.34 20.47 ?  164 LEU   A HD23 1 
ATOM   3658 N N    A VAL   A 1 165 ? 5.598  -10.597 2.755   0.66 16.04 ?  165 VAL   A N    1 
ATOM   3659 N N    B VAL   A 1 165 ? 5.709  -10.603 2.839   0.34 15.57 ?  165 VAL   A N    1 
ATOM   3660 C CA   A VAL   A 1 165 ? 5.120  -11.669 3.626   0.66 16.06 ?  165 VAL   A CA   1 
ATOM   3661 C CA   B VAL   A 1 165 ? 5.271  -11.678 3.720   0.34 15.49 ?  165 VAL   A CA   1 
ATOM   3662 C C    A VAL   A 1 165 ? 4.106  -12.536 2.891   0.66 15.73 ?  165 VAL   A C    1 
ATOM   3663 C C    B VAL   A 1 165 ? 4.178  -12.502 3.055   0.34 15.24 ?  165 VAL   A C    1 
ATOM   3664 O O    A VAL   A 1 165 ? 4.243  -13.765 2.819   0.66 15.50 ?  165 VAL   A O    1 
ATOM   3665 O O    B VAL   A 1 165 ? 4.198  -13.739 3.097   0.34 15.08 ?  165 VAL   A O    1 
ATOM   3666 C CB   A VAL   A 1 165 ? 4.532  -11.076 4.921   0.66 16.44 ?  165 VAL   A CB   1 
ATOM   3667 C CB   B VAL   A 1 165 ? 4.806  -11.089 5.063   0.34 15.45 ?  165 VAL   A CB   1 
ATOM   3668 C CG1  A VAL   A 1 165 ? 3.780  -12.141 5.718   0.66 16.86 ?  165 VAL   A CG1  1 
ATOM   3669 C CG1  B VAL   A 1 165 ? 4.121  -12.147 5.892   0.34 15.32 ?  165 VAL   A CG1  1 
ATOM   3670 C CG2  A VAL   A 1 165 ? 5.628  -10.425 5.762   0.66 16.80 ?  165 VAL   A CG2  1 
ATOM   3671 C CG2  B VAL   A 1 165 ? 5.985  -10.502 5.817   0.34 16.00 ?  165 VAL   A CG2  1 
ATOM   3672 H H    A VAL   A 1 165 ? 5.392  -9.807  3.023   0.66 19.22 ?  165 VAL   A H    1 
ATOM   3673 H H    B VAL   A 1 165 ? 5.517  -9.814  3.115   0.34 18.66 ?  165 VAL   A H    1 
ATOM   3674 H HA   A VAL   A 1 165 ? 5.870  -12.234 3.872   0.66 19.25 ?  165 VAL   A HA   1 
ATOM   3675 H HA   B VAL   A 1 165 ? 6.020  -12.265 3.898   0.34 18.56 ?  165 VAL   A HA   1 
ATOM   3676 H HB   A VAL   A 1 165 ? 3.898  -10.382 4.684   0.66 19.70 ?  165 VAL   A HB   1 
ATOM   3677 H HB   B VAL   A 1 165 ? 4.167  -10.377 4.896   0.34 18.51 ?  165 VAL   A HB   1 
ATOM   3678 H HG11 A VAL   A 1 165 ? 3.662  -11.826 6.629   0.66 20.21 ?  165 VAL   A HG11 1 
ATOM   3679 H HG11 B VAL   A 1 165 ? 4.091  -11.847 6.812   0.34 18.35 ?  165 VAL   A HG11 1 
ATOM   3680 H HG12 A VAL   A 1 165 ? 2.913  -12.289 5.308   0.66 20.21 ?  165 VAL   A HG12 1 
ATOM   3681 H HG12 B VAL   A 1 165 ? 3.222  -12.278 5.555   0.34 18.35 ?  165 VAL   A HG12 1 
ATOM   3682 H HG13 A VAL   A 1 165 ? 4.296  -12.960 5.716   0.66 20.21 ?  165 VAL   A HG13 1 
ATOM   3683 H HG13 B VAL   A 1 165 ? 4.629  -12.969 5.826   0.34 18.35 ?  165 VAL   A HG13 1 
ATOM   3684 H HG21 A VAL   A 1 165 ? 5.237  -10.075 6.578   0.66 20.13 ?  165 VAL   A HG21 1 
ATOM   3685 H HG21 B VAL   A 1 165 ? 5.671  -10.137 6.658   0.34 19.17 ?  165 VAL   A HG21 1 
ATOM   3686 H HG22 A VAL   A 1 165 ? 6.301  -11.091 5.978   0.66 20.13 ?  165 VAL   A HG22 1 
ATOM   3687 H HG22 B VAL   A 1 165 ? 6.633  -11.205 5.980   0.34 19.17 ?  165 VAL   A HG22 1 
ATOM   3688 H HG23 A VAL   A 1 165 ? 6.032  -9.703  5.254   0.66 20.13 ?  165 VAL   A HG23 1 
ATOM   3689 H HG23 B VAL   A 1 165 ? 6.384  -9.801  5.279   0.34 19.17 ?  165 VAL   A HG23 1 
ATOM   3690 N N    A SER   A 1 166 ? 3.081  -11.902 2.317   0.66 16.18 ?  166 SER   A N    1 
ATOM   3691 N N    B SER   A 1 166 ? 3.210  -11.831 2.425   0.34 15.43 ?  166 SER   A N    1 
ATOM   3692 C CA   A SER   A 1 166 ? 1.979  -12.652 1.721   0.66 17.12 ?  166 SER   A CA   1 
ATOM   3693 C CA   B SER   A 1 166 ? 2.052  -12.534 1.887   0.34 16.24 ?  166 SER   A CA   1 
ATOM   3694 C C    A SER   A 1 166 ? 2.417  -13.440 0.495   0.66 18.01 ?  166 SER   A C    1 
ATOM   3695 C C    B SER   A 1 166 ? 2.434  -13.507 0.776   0.34 16.90 ?  166 SER   A C    1 
ATOM   3696 O O    A SER   A 1 166 ? 1.770  -14.434 0.140   0.66 19.67 ?  166 SER   A O    1 
ATOM   3697 O O    B SER   A 1 166 ? 1.803  -14.561 0.636   0.34 17.69 ?  166 SER   A O    1 
ATOM   3698 C CB   A SER   A 1 166 ? 0.839  -11.706 1.333   0.66 18.18 ?  166 SER   A CB   1 
ATOM   3699 C CB   B SER   A 1 166 ? 0.999  -11.525 1.412   0.34 17.31 ?  166 SER   A CB   1 
ATOM   3700 O OG   A SER   A 1 166 ? 0.188  -11.157 2.468   0.66 20.10 ?  166 SER   A OG   1 
ATOM   3701 O OG   B SER   A 1 166 ? 0.453  -10.799 2.503   0.34 18.86 ?  166 SER   A OG   1 
ATOM   3702 H H    A SER   A 1 166 ? 2.999  -11.050 2.262   0.66 19.39 ?  166 SER   A H    1 
ATOM   3703 H H    B SER   A 1 166 ? 3.199  -10.978 2.306   0.34 18.49 ?  166 SER   A H    1 
ATOM   3704 H HA   A SER   A 1 166 ? 1.629  -13.280 2.373   0.66 20.52 ?  166 SER   A HA   1 
ATOM   3705 H HA   B SER   A 1 166 ? 1.648  -13.056 2.595   0.34 19.46 ?  166 SER   A HA   1 
ATOM   3706 H HB2  A SER   A 1 166 ? 1.200  -10.996 0.775   0.66 21.78 ?  166 SER   A HB2  1 
ATOM   3707 H HB2  B SER   A 1 166 ? 1.410  -10.894 0.804   0.34 20.75 ?  166 SER   A HB2  1 
ATOM   3708 H HB3  A SER   A 1 166 ? 0.171  -12.203 0.835   0.66 21.78 ?  166 SER   A HB3  1 
ATOM   3709 H HB3  B SER   A 1 166 ? 0.280  -11.997 0.966   0.34 20.75 ?  166 SER   A HB3  1 
ATOM   3710 H HG   A SER   A 1 166 ? -0.395 -10.608 2.228   0.66 24.10 ?  166 SER   A HG   1 
ATOM   3711 H HG   B SER   A 1 166 ? -0.127 -10.251 2.233   0.34 22.60 ?  166 SER   A HG   1 
ATOM   3712 N N    A SER   A 1 167 ? 3.480  -13.006 -0.180  0.66 17.31 ?  167 SER   A N    1 
ATOM   3713 N N    B SER   A 1 167 ? 3.472  -13.198 -0.003  0.34 17.13 ?  167 SER   A N    1 
ATOM   3714 C CA   A SER   A 1 167 ? 3.969  -13.690 -1.368  0.66 17.97 ?  167 SER   A CA   1 
ATOM   3715 C CA   B SER   A 1 167 ? 3.820  -13.993 -1.175  0.34 17.59 ?  167 SER   A CA   1 
ATOM   3716 C C    A SER   A 1 167 ? 5.120  -14.643 -1.072  0.66 18.19 ?  167 SER   A C    1 
ATOM   3717 C C    B SER   A 1 167 ? 5.007  -14.921 -0.942  0.34 18.16 ?  167 SER   A C    1 
ATOM   3718 O O    A SER   A 1 167 ? 5.625  -15.287 -1.996  0.66 19.35 ?  167 SER   A O    1 
ATOM   3719 O O    B SER   A 1 167 ? 5.479  -15.550 -1.895  0.34 18.72 ?  167 SER   A O    1 
ATOM   3720 C CB   A SER   A 1 167 ? 4.402  -12.671 -2.433  0.66 18.49 ?  167 SER   A CB   1 
ATOM   3721 C CB   B SER   A 1 167 ? 4.087  -13.087 -2.382  0.34 17.73 ?  167 SER   A CB   1 
ATOM   3722 O OG   A SER   A 1 167 ? 5.448  -11.840 -1.946  0.66 19.22 ?  167 SER   A OG   1 
ATOM   3723 O OG   B SER   A 1 167 ? 5.307  -12.375 -2.240  0.34 18.06 ?  167 SER   A OG   1 
ATOM   3724 H H    A SER   A 1 167 ? 3.927  -12.301 0.031   0.66 20.74 ?  167 SER   A H    1 
ATOM   3725 H H    B SER   A 1 167 ? 3.999  -12.531 0.138   0.34 20.53 ?  167 SER   A H    1 
ATOM   3726 H HA   A SER   A 1 167 ? 3.240  -14.206 -1.743  0.66 21.53 ?  167 SER   A HA   1 
ATOM   3727 H HA   B SER   A 1 167 ? 3.063  -14.550 -1.401  0.34 21.08 ?  167 SER   A HA   1 
ATOM   3728 H HB2  A SER   A 1 167 ? 4.723  -13.152 -3.213  0.66 22.16 ?  167 SER   A HB2  1 
ATOM   3729 H HB2  B SER   A 1 167 ? 4.136  -13.636 -3.181  0.34 21.25 ?  167 SER   A HB2  1 
ATOM   3730 H HB3  A SER   A 1 167 ? 3.631  -12.128 -2.682  0.66 22.16 ?  167 SER   A HB3  1 
ATOM   3731 H HB3  B SER   A 1 167 ? 3.356  -12.452 -2.467  0.34 21.25 ?  167 SER   A HB3  1 
ATOM   3732 H HG   A SER   A 1 167 ? 5.202  -11.475 -1.226  0.66 23.03 ?  167 SER   A HG   1 
ATOM   3733 H HG   B SER   A 1 167 ? 5.273  -11.887 -1.556  0.34 21.64 ?  167 SER   A HG   1 
ATOM   3734 N N    A PHE   A 1 168 ? 5.550  -14.747 0.185   0.66 17.92 ?  168 PHE   A N    1 
ATOM   3735 N N    B PHE   A 1 168 ? 5.487  -15.041 0.293   0.34 18.39 ?  168 PHE   A N    1 
ATOM   3736 C CA   A PHE   A 1 168 ? 6.719  -15.558 0.502   0.66 18.41 ?  168 PHE   A CA   1 
ATOM   3737 C CA   B PHE   A 1 168 ? 6.701  -15.810 0.539   0.34 19.15 ?  168 PHE   A CA   1 
ATOM   3738 C C    A PHE   A 1 168 ? 6.397  -17.041 0.396   0.66 20.07 ?  168 PHE   A C    1 
ATOM   3739 C C    B PHE   A 1 168 ? 6.448  -17.298 0.336   0.34 21.79 ?  168 PHE   A C    1 
ATOM   3740 O O    A PHE   A 1 168 ? 5.404  -17.517 0.957   0.66 21.96 ?  168 PHE   A O    1 
ATOM   3741 O O    B PHE   A 1 168 ? 5.526  -17.872 0.922   0.34 22.33 ?  168 PHE   A O    1 
ATOM   3742 C CB   A PHE   A 1 168 ? 7.222  -15.259 1.910   0.66 17.92 ?  168 PHE   A CB   1 
ATOM   3743 C CB   B PHE   A 1 168 ? 7.225  -15.565 1.951   0.34 17.92 ?  168 PHE   A CB   1 
ATOM   3744 C CG   A PHE   A 1 168 ? 8.493  -15.985 2.243   0.66 17.34 ?  168 PHE   A CG   1 
ATOM   3745 C CG   B PHE   A 1 168 ? 8.462  -16.357 2.270   0.34 16.82 ?  168 PHE   A CG   1 
ATOM   3746 C CD1  A PHE   A 1 168 ? 9.686  -15.583 1.678   0.66 17.39 ?  168 PHE   A CD1  1 
ATOM   3747 C CD1  B PHE   A 1 168 ? 9.637  -16.131 1.573   0.34 16.53 ?  168 PHE   A CD1  1 
ATOM   3748 C CD2  A PHE   A 1 168 ? 8.499  -17.085 3.085   0.66 17.41 ?  168 PHE   A CD2  1 
ATOM   3749 C CD2  B PHE   A 1 168 ? 8.448  -17.339 3.249   0.34 16.53 ?  168 PHE   A CD2  1 
ATOM   3750 C CE1  A PHE   A 1 168 ? 10.861 -16.247 1.958   0.66 17.13 ?  168 PHE   A CE1  1 
ATOM   3751 C CE1  B PHE   A 1 168 ? 10.778 -16.858 1.853   0.34 16.51 ?  168 PHE   A CE1  1 
ATOM   3752 C CE2  A PHE   A 1 168 ? 9.683  -17.750 3.371   0.66 17.59 ?  168 PHE   A CE2  1 
ATOM   3753 C CE2  B PHE   A 1 168 ? 9.589  -18.068 3.534   0.34 16.77 ?  168 PHE   A CE2  1 
ATOM   3754 C CZ   A PHE   A 1 168 ? 10.858 -17.328 2.806   0.66 17.36 ?  168 PHE   A CZ   1 
ATOM   3755 C CZ   B PHE   A 1 168 ? 10.752 -17.828 2.833   0.34 16.84 ?  168 PHE   A CZ   1 
ATOM   3756 H H    A PHE   A 1 168 ? 5.196  -14.344 0.860   0.66 21.47 ?  168 PHE   A H    1 
ATOM   3757 H H    B PHE   A 1 168 ? 5.133  -14.692 0.995   0.34 22.04 ?  168 PHE   A H    1 
ATOM   3758 H HA   A PHE   A 1 168 ? 7.430  -15.349 -0.128  0.66 22.07 ?  168 PHE   A HA   1 
ATOM   3759 H HA   B PHE   A 1 168 ? 7.385  -15.532 -0.090  0.34 22.95 ?  168 PHE   A HA   1 
ATOM   3760 H HB2  A PHE   A 1 168 ? 7.391  -14.306 1.991   0.66 21.48 ?  168 PHE   A HB2  1 
ATOM   3761 H HB2  B PHE   A 1 168 ? 7.442  -14.625 2.046   0.34 21.48 ?  168 PHE   A HB2  1 
ATOM   3762 H HB3  A PHE   A 1 168 ? 6.546  -15.531 2.549   0.66 21.48 ?  168 PHE   A HB3  1 
ATOM   3763 H HB3  B PHE   A 1 168 ? 6.539  -15.814 2.589   0.34 21.48 ?  168 PHE   A HB3  1 
ATOM   3764 H HD1  A PHE   A 1 168 ? 9.702  -14.849 1.104   0.66 20.84 ?  168 PHE   A HD1  1 
ATOM   3765 H HD1  B PHE   A 1 168 ? 9.661  -15.480 0.909   0.34 19.81 ?  168 PHE   A HD1  1 
ATOM   3766 H HD2  A PHE   A 1 168 ? 7.702  -17.371 3.470   0.66 20.86 ?  168 PHE   A HD2  1 
ATOM   3767 H HD2  B PHE   A 1 168 ? 7.665  -17.503 3.723   0.34 19.81 ?  168 PHE   A HD2  1 
ATOM   3768 H HE1  A PHE   A 1 168 ? 11.664 -15.961 1.578   0.66 20.53 ?  168 PHE   A HE1  1 
ATOM   3769 H HE1  B PHE   A 1 168 ? 11.562 -16.697 1.378   0.34 19.78 ?  168 PHE   A HE1  1 
ATOM   3770 H HE2  A PHE   A 1 168 ? 9.673  -18.483 3.942   0.66 21.09 ?  168 PHE   A HE2  1 
ATOM   3771 H HE2  B PHE   A 1 168 ? 9.568  -18.723 4.195   0.34 20.10 ?  168 PHE   A HE2  1 
ATOM   3772 H HZ   A PHE   A 1 168 ? 11.651 -17.775 2.996   0.66 20.81 ?  168 PHE   A HZ   1 
ATOM   3773 H HZ   B PHE   A 1 168 ? 11.520 -18.320 3.021   0.34 20.18 ?  168 PHE   A HZ   1 
ATOM   3774 N N    A LEU   A 1 169 ? 7.259  -17.778 -0.297  0.66 21.65 ?  169 LEU   A N    1 
ATOM   3775 N N    B LEU   A 1 169 ? 7.289  -17.924 -0.480  0.34 24.39 ?  169 LEU   A N    1 
ATOM   3776 C CA   A LEU   A 1 169 ? 7.066  -19.209 -0.444  0.66 25.18 ?  169 LEU   A CA   1 
ATOM   3777 C CA   B LEU   A 1 169 ? 7.144  -19.337 -0.792  0.34 27.30 ?  169 LEU   A CA   1 
ATOM   3778 C C    A LEU   A 1 169 ? 7.923  -19.946 0.573   0.66 25.32 ?  169 LEU   A C    1 
ATOM   3779 C C    B LEU   A 1 169 ? 8.117  -20.168 0.034   0.34 28.30 ?  169 LEU   A C    1 
ATOM   3780 O O    A LEU   A 1 169 ? 7.396  -20.424 1.579   0.66 25.70 ?  169 LEU   A O    1 
ATOM   3781 O O    B LEU   A 1 169 ? 7.714  -20.909 0.931   0.34 29.08 ?  169 LEU   A O    1 
ATOM   3782 C CB   A LEU   A 1 169 ? 7.384  -19.656 -1.876  0.66 27.58 ?  169 LEU   A CB   1 
ATOM   3783 C CB   B LEU   A 1 169 ? 7.396  -19.573 -2.281  0.34 28.59 ?  169 LEU   A CB   1 
ATOM   3784 C CG   A LEU   A 1 169 ? 7.042  -21.110 -2.221  0.66 29.86 ?  169 LEU   A CG   1 
ATOM   3785 C CG   B LEU   A 1 169 ? 7.102  -20.980 -2.802  0.34 29.82 ?  169 LEU   A CG   1 
ATOM   3786 C CD1  A LEU   A 1 169 ? 5.616  -21.443 -1.815  0.66 30.56 ?  169 LEU   A CD1  1 
ATOM   3787 C CD1  B LEU   A 1 169 ? 5.614  -21.282 -2.718  0.34 30.02 ?  169 LEU   A CD1  1 
ATOM   3788 C CD2  A LEU   A 1 169 ? 7.245  -21.371 -3.708  0.66 30.55 ?  169 LEU   A CD2  1 
ATOM   3789 C CD2  B LEU   A 1 169 ? 7.608  -21.134 -4.226  0.34 30.28 ?  169 LEU   A CD2  1 
ATOM   3790 O OXT  A LEU   A 1 169 ? 9.140  -20.064 0.432   0.66 24.64 -1 169 LEU   A OXT  1 
ATOM   3791 O OXT  B LEU   A 1 169 ? 9.329  -20.114 -0.175  0.34 28.30 -1 169 LEU   A OXT  1 
ATOM   3792 H H    A LEU   A 1 169 ? 7.959  -17.468 -0.691  0.66 25.95 ?  169 LEU   A H    1 
ATOM   3793 H H    B LEU   A 1 169 ? 7.957  -17.546 -0.868  0.34 29.24 ?  169 LEU   A H    1 
ATOM   3794 H HA   A LEU   A 1 169 ? 6.144  -19.424 -0.253  0.66 30.18 ?  169 LEU   A HA   1 
ATOM   3795 H HA   B LEU   A 1 169 ? 6.241  -19.620 -0.582  0.34 32.73 ?  169 LEU   A HA   1 
ATOM   3796 H HB2  A LEU   A 1 169 ? 6.884  -19.093 -2.489  0.66 33.07 ?  169 LEU   A HB2  1 
ATOM   3797 H HB2  B LEU   A 1 169 ? 6.840  -18.958 -2.783  0.34 34.28 ?  169 LEU   A HB2  1 
ATOM   3798 H HB3  A LEU   A 1 169 ? 8.332  -19.539 -2.032  0.66 33.07 ?  169 LEU   A HB3  1 
ATOM   3799 H HB3  B LEU   A 1 169 ? 8.329  -19.388 -2.463  0.34 34.28 ?  169 LEU   A HB3  1 
ATOM   3800 H HG   A LEU   A 1 169 ? 7.638  -21.700 -1.733  0.66 35.81 ?  169 LEU   A HG   1 
ATOM   3801 H HG   B LEU   A 1 169 ? 7.569  -21.626 -2.249  0.34 35.76 ?  169 LEU   A HG   1 
ATOM   3802 H HD11 A LEU   A 1 169 ? 5.355  -22.277 -2.234  0.66 36.65 ?  169 LEU   A HD11 1 
ATOM   3803 H HD11 B LEU   A 1 169 ? 5.440  -22.131 -3.152  0.34 36.00 ?  169 LEU   A HD11 1 
ATOM   3804 H HD12 A LEU   A 1 169 ? 5.574  -21.530 -0.850  0.66 36.65 ?  169 LEU   A HD12 1 
ATOM   3805 H HD12 B LEU   A 1 169 ? 5.352  -21.326 -1.785  0.34 36.00 ?  169 LEU   A HD12 1 
ATOM   3806 H HD13 A LEU   A 1 169 ? 5.030  -20.728 -2.110  0.66 36.65 ?  169 LEU   A HD13 1 
ATOM   3807 H HD13 B LEU   A 1 169 ? 5.124  -20.575 -3.167  0.34 36.00 ?  169 LEU   A HD13 1 
ATOM   3808 H HD21 A LEU   A 1 169 ? 7.031  -22.299 -3.899  0.66 36.63 ?  169 LEU   A HD21 1 
ATOM   3809 H HD21 B LEU   A 1 169 ? 7.410  -22.032 -4.535  0.34 36.30 ?  169 LEU   A HD21 1 
ATOM   3810 H HD22 A LEU   A 1 169 ? 6.657  -20.787 -4.214  0.66 36.63 ?  169 LEU   A HD22 1 
ATOM   3811 H HD22 B LEU   A 1 169 ? 7.163  -20.483 -4.791  0.34 36.30 ?  169 LEU   A HD22 1 
ATOM   3812 H HD23 A LEU   A 1 169 ? 8.169  -21.191 -3.938  0.66 36.63 ?  169 LEU   A HD23 1 
ATOM   3813 H HD23 B LEU   A 1 169 ? 8.566  -20.983 -4.238  0.34 36.30 ?  169 LEU   A HD23 1 
ATOM   3814 N N    A SER   B 1 1   ? 50.783 -9.255  -23.709 0.66 29.48 ?  1   SER   B N    1 
ATOM   3815 N N    B SER   B 1 1   ? 50.700 -9.384  -23.722 0.34 26.78 ?  1   SER   B N    1 
ATOM   3816 C CA   A SER   B 1 1   ? 51.296 -10.313 -22.816 0.66 29.65 ?  1   SER   B CA   1 
ATOM   3817 C CA   B SER   B 1 1   ? 51.210 -10.390 -22.765 0.34 26.82 ?  1   SER   B CA   1 
ATOM   3818 C C    A SER   B 1 1   ? 50.228 -11.371 -22.570 0.66 28.51 ?  1   SER   B C    1 
ATOM   3819 C C    B SER   B 1 1   ? 50.172 -11.484 -22.538 0.34 26.11 ?  1   SER   B C    1 
ATOM   3820 O O    A SER   B 1 1   ? 49.034 -11.164 -22.826 0.66 28.23 ?  1   SER   B O    1 
ATOM   3821 O O    B SER   B 1 1   ? 48.978 -11.301 -22.805 0.34 25.76 ?  1   SER   B O    1 
ATOM   3822 C CB   A SER   B 1 1   ? 51.761 -9.721  -21.488 0.66 30.07 ?  1   SER   B CB   1 
ATOM   3823 C CB   B SER   B 1 1   ? 51.568 -9.731  -21.436 0.34 26.95 ?  1   SER   B CB   1 
ATOM   3824 O OG   A SER   B 1 1   ? 50.661 -9.452  -20.640 0.66 31.67 ?  1   SER   B OG   1 
ATOM   3825 O OG   B SER   B 1 1   ? 50.405 -9.490  -20.665 0.34 27.81 ?  1   SER   B OG   1 
ATOM   3826 H H1   A SER   B 1 1   ? 50.551 -9.620  -24.484 0.66 35.35 ?  1   SER   B H1   1 
ATOM   3827 H H1   B SER   B 1 1   ? 50.656 -9.749  -24.530 0.34 32.11 ?  1   SER   B H1   1 
ATOM   3828 H H2   A SER   B 1 1   ? 50.079 -8.874  -23.329 0.66 35.35 ?  1   SER   B H2   1 
ATOM   3829 H H2   B SER   B 1 1   ? 49.894 -9.122  -23.463 0.34 32.11 ?  1   SER   B H2   1 
ATOM   3830 H H3   A SER   B 1 1   ? 51.423 -8.653  -23.837 0.66 35.35 ?  1   SER   B H3   1 
ATOM   3831 H H3   B SER   B 1 1   ? 51.255 -8.691  -23.734 0.34 32.11 ?  1   SER   B H3   1 
ATOM   3832 H HA   A SER   B 1 1   ? 52.054 -10.732 -23.247 0.66 35.55 ?  1   SER   B HA   1 
ATOM   3833 H HA   B SER   B 1 1   ? 52.008 -10.787 -23.140 0.34 32.15 ?  1   SER   B HA   1 
ATOM   3834 H HB2  A SER   B 1 1   ? 52.342 -10.360 -21.051 0.66 36.06 ?  1   SER   B HB2  1 
ATOM   3835 H HB2  B SER   B 1 1   ? 52.157 -10.325 -20.948 0.34 32.32 ?  1   SER   B HB2  1 
ATOM   3836 H HB3  A SER   B 1 1   ? 52.245 -8.896  -21.660 0.66 36.06 ?  1   SER   B HB3  1 
ATOM   3837 H HB3  B SER   B 1 1   ? 52.015 -8.887  -21.610 0.34 32.32 ?  1   SER   B HB3  1 
ATOM   3838 H HG   A SER   B 1 1   ? 50.925 -9.035  -19.959 0.66 37.98 ?  1   SER   B HG   1 
ATOM   3839 H HG   B SER   B 1 1   ? 50.615 -9.104  -19.949 0.34 33.35 ?  1   SER   B HG   1 
ATOM   3840 N N    A MET   B 1 2   ? 50.678 -12.508 -22.059 0.66 27.34 ?  2   MET   B N    1 
ATOM   3841 N N    B MET   B 1 2   ? 50.638 -12.621 -22.039 0.34 25.50 ?  2   MET   B N    1 
ATOM   3842 C CA   A MET   B 1 2   ? 49.848 -13.691 -21.887 0.66 27.34 ?  2   MET   B CA   1 
ATOM   3843 C CA   B MET   B 1 2   ? 49.818 -13.818 -21.894 0.34 25.32 ?  2   MET   B CA   1 
ATOM   3844 C C    A MET   B 1 2   ? 49.598 -13.871 -20.395 0.66 24.79 ?  2   MET   B C    1 
ATOM   3845 C C    B MET   B 1 2   ? 49.549 -14.062 -20.418 0.34 24.08 ?  2   MET   B C    1 
ATOM   3846 O O    A MET   B 1 2   ? 50.539 -14.087 -19.624 0.66 24.72 ?  2   MET   B O    1 
ATOM   3847 O O    B MET   B 1 2   ? 50.417 -14.551 -19.689 0.34 24.73 ?  2   MET   B O    1 
ATOM   3848 C CB   A MET   B 1 2   ? 50.569 -14.893 -22.486 0.66 31.20 ?  2   MET   B CB   1 
ATOM   3849 C CB   B MET   B 1 2   ? 50.543 -14.997 -22.507 0.34 27.06 ?  2   MET   B CB   1 
ATOM   3850 C CG   A MET   B 1 2   ? 49.718 -16.139 -22.647 0.66 34.69 ?  2   MET   B CG   1 
ATOM   3851 C CG   B MET   B 1 2   ? 49.651 -16.179 -22.864 0.34 28.50 ?  2   MET   B CG   1 
ATOM   3852 S SD   A MET   B 1 2   ? 50.566 -17.362 -23.666 0.66 38.28 ?  2   MET   B SD   1 
ATOM   3853 S SD   B MET   B 1 2   ? 50.487 -17.275 -24.016 0.34 29.61 ?  2   MET   B SD   1 
ATOM   3854 C CE   A MET   B 1 2   ? 51.084 -16.324 -25.025 0.66 38.25 ?  2   MET   B CE   1 
ATOM   3855 C CE   B MET   B 1 2   ? 51.416 -16.074 -24.945 0.34 30.25 ?  2   MET   B CE   1 
ATOM   3856 H H    A MET   B 1 2   ? 51.491 -12.626 -21.793 0.66 32.78 ?  2   MET   B H    1 
ATOM   3857 H H    B MET   B 1 2   ? 51.455 -12.732 -21.785 0.34 30.57 ?  2   MET   B H    1 
ATOM   3858 H HA   A MET   B 1 2   ? 49.009 -13.581 -22.356 0.66 32.78 ?  2   MET   B HA   1 
ATOM   3859 H HA   B MET   B 1 2   ? 48.984 -13.702 -22.374 0.34 30.35 ?  2   MET   B HA   1 
ATOM   3860 H HB2  A MET   B 1 2   ? 50.894 -14.616 -23.356 0.66 37.41 ?  2   MET   B HB2  1 
ATOM   3861 H HB2  B MET   B 1 2   ? 50.955 -14.616 -23.287 0.34 32.44 ?  2   MET   B HB2  1 
ATOM   3862 H HB3  A MET   B 1 2   ? 51.320 -15.137 -21.927 0.66 37.41 ?  2   MET   B HB3  1 
ATOM   3863 H HB3  B MET   B 1 2   ? 51.224 -15.332 -21.909 0.34 32.44 ?  2   MET   B HB3  1 
ATOM   3864 H HG2  A MET   B 1 2   ? 49.550 -16.530 -21.772 0.66 41.60 ?  2   MET   B HG2  1 
ATOM   3865 H HG2  B MET   B 1 2   ? 49.437 -16.682 -22.054 0.34 34.17 ?  2   MET   B HG2  1 
ATOM   3866 H HG3  A MET   B 1 2   ? 48.880 -15.909 -23.079 0.66 41.60 ?  2   MET   B HG3  1 
ATOM   3867 H HG3  B MET   B 1 2   ? 48.838 -15.867 -23.286 0.34 34.17 ?  2   MET   B HG3  1 
ATOM   3868 H HE1  A MET   B 1 2   ? 51.230 -16.875 -25.798 0.66 45.88 ?  2   MET   B HE1  1 
ATOM   3869 H HE1  B MET   B 1 2   ? 51.692 -16.506 -25.733 0.34 36.27 ?  2   MET   B HE1  1 
ATOM   3870 H HE2  A MET   B 1 2   ? 50.386 -15.670 -25.204 0.66 45.88 ?  2   MET   B HE2  1 
ATOM   3871 H HE2  B MET   B 1 2   ? 50.838 -15.317 -25.164 0.34 36.27 ?  2   MET   B HE2  1 
ATOM   3872 H HE3  A MET   B 1 2   ? 51.906 -15.868 -24.776 0.66 45.88 ?  2   MET   B HE3  1 
ATOM   3873 H HE3  B MET   B 1 2   ? 52.194 -15.775 -24.430 0.34 36.27 ?  2   MET   B HE3  1 
ATOM   3874 N N    . VAL   B 1 3   ? 48.338 -13.737 -19.987 1.00 22.42 ?  3   VAL   B N    1 
ATOM   3875 C CA   . VAL   B 1 3   ? 47.922 -13.962 -18.612 1.00 20.81 ?  3   VAL   B CA   1 
ATOM   3876 C C    . VAL   B 1 3   ? 46.681 -14.841 -18.625 1.00 18.59 ?  3   VAL   B C    1 
ATOM   3877 O O    . VAL   B 1 3   ? 45.941 -14.907 -19.610 1.00 19.25 ?  3   VAL   B O    1 
ATOM   3878 C CB   . VAL   B 1 3   ? 47.650 -12.646 -17.857 1.00 22.61 ?  3   VAL   B CB   1 
ATOM   3879 C CG1  . VAL   B 1 3   ? 48.929 -11.799 -17.762 1.00 23.20 ?  3   VAL   B CG1  1 
ATOM   3880 C CG2  . VAL   B 1 3   ? 46.528 -11.874 -18.531 1.00 23.05 ?  3   VAL   B CG2  1 
ATOM   3881 H H    A VAL   B 1 3   ? 47.697 -13.503 -20.511 0.66 26.87 ?  3   VAL   B H    1 
ATOM   3882 H H    B VAL   B 1 3   ? 47.728 -13.401 -20.490 0.34 26.87 ?  3   VAL   B H    1 
ATOM   3883 H HA   . VAL   B 1 3   ? 48.623 -14.443 -18.142 1.00 24.94 ?  3   VAL   B HA   1 
ATOM   3884 H HB   . VAL   B 1 3   ? 47.373 -12.862 -16.954 1.00 27.11 ?  3   VAL   B HB   1 
ATOM   3885 H HG11 . VAL   B 1 3   ? 48.728 -10.988 -17.274 1.00 27.82 ?  3   VAL   B HG11 1 
ATOM   3886 H HG12 . VAL   B 1 3   ? 49.610 -12.309 -17.295 1.00 27.82 ?  3   VAL   B HG12 1 
ATOM   3887 H HG13 . VAL   B 1 3   ? 49.229 -11.585 -18.658 1.00 27.82 ?  3   VAL   B HG13 1 
ATOM   3888 H HG21 . VAL   B 1 3   ? 46.472 -10.995 -18.131 1.00 27.64 ?  3   VAL   B HG21 1 
ATOM   3889 H HG22 . VAL   B 1 3   ? 46.720 -11.798 -19.478 1.00 27.64 ?  3   VAL   B HG22 1 
ATOM   3890 H HG23 . VAL   B 1 3   ? 45.694 -12.352 -18.399 1.00 27.64 ?  3   VAL   B HG23 1 
ATOM   3891 N N    . ASN   B 1 4   ? 46.459 -15.529 -17.507 1.00 16.23 ?  4   ASN   B N    1 
ATOM   3892 C CA   . ASN   B 1 4   ? 45.318 -16.429 -17.376 1.00 15.27 ?  4   ASN   B CA   1 
ATOM   3893 C C    . ASN   B 1 4   ? 45.247 -17.399 -18.551 1.00 15.86 ?  4   ASN   B C    1 
ATOM   3894 O O    . ASN   B 1 4   ? 44.183 -17.639 -19.116 1.00 16.45 ?  4   ASN   B O    1 
ATOM   3895 C CB   . ASN   B 1 4   ? 44.011 -15.647 -17.224 1.00 14.82 ?  4   ASN   B CB   1 
ATOM   3896 C CG   . ASN   B 1 4   ? 43.965 -14.846 -15.941 1.00 14.29 ?  4   ASN   B CG   1 
ATOM   3897 O OD1  . ASN   B 1 4   ? 44.254 -15.366 -14.862 1.00 14.23 ?  4   ASN   B OD1  1 
ATOM   3898 N ND2  . ASN   B 1 4   ? 43.620 -13.569 -16.049 1.00 14.91 ?  4   ASN   B ND2  1 
ATOM   3899 H H    . ASN   B 1 4   ? 46.965 -15.499 -16.812 1.00 19.44 ?  4   ASN   B H    1 
ATOM   3900 H HA   . ASN   B 1 4   ? 45.441 -16.960 -16.573 1.00 18.29 ?  4   ASN   B HA   1 
ATOM   3901 H HB2  . ASN   B 1 4   ? 43.926 -15.031 -17.968 1.00 17.76 ?  4   ASN   B HB2  1 
ATOM   3902 H HB3  . ASN   B 1 4   ? 43.270 -16.270 -17.220 1.00 17.76 ?  4   ASN   B HB3  1 
ATOM   3903 H HD21 . ASN   B 1 4   ? 43.580 -13.069 -15.346 1.00 17.87 ?  4   ASN   B HD21 1 
ATOM   3904 H HD22 . ASN   B 1 4   ? 43.430 -13.235 -16.819 1.00 17.87 ?  4   ASN   B HD22 1 
ATOM   3905 N N    . SER   B 1 5   ? 46.397 -17.965 -18.922 1.00 17.13 ?  5   SER   B N    1 
ATOM   3906 C CA   . SER   B 1 5   ? 46.485 -18.890 -20.052 1.00 19.49 ?  5   SER   B CA   1 
ATOM   3907 C C    . SER   B 1 5   ? 46.513 -20.304 -19.486 1.00 20.84 ?  5   SER   B C    1 
ATOM   3908 O O    . SER   B 1 5   ? 47.563 -20.920 -19.320 1.00 23.11 ?  5   SER   B O    1 
ATOM   3909 C CB   . SER   B 1 5   ? 47.718 -18.587 -20.900 1.00 21.44 ?  5   SER   B CB   1 
ATOM   3910 O OG   . SER   B 1 5   ? 48.904 -18.747 -20.140 1.00 24.95 ?  5   SER   B OG   1 
ATOM   3911 H H    . SER   B 1 5   ? 47.153 -17.830 -18.530 1.00 20.53 ?  5   SER   B H    1 
ATOM   3912 H HA   . SER   B 1 5   ? 45.701 -18.801 -20.610 1.00 23.36 ?  5   SER   B HA   1 
ATOM   3913 H HB2  . SER   B 1 5   ? 47.736 -19.190 -21.663 1.00 25.70 ?  5   SER   B HB2  1 
ATOM   3914 H HB3  . SER   B 1 5   ? 47.660 -17.669 -21.212 1.00 25.70 ?  5   SER   B HB3  1 
ATOM   3915 H HG   . SER   B 1 5   ? 48.987 -19.548 -19.905 1.00 29.91 ?  5   SER   B HG   1 
ATOM   3916 N N    . PHE   B 1 6   ? 45.324 -20.804 -19.158 1.00 21.19 ?  6   PHE   B N    1 
ATOM   3917 C CA   . PHE   B 1 6   ? 45.169 -22.136 -18.590 1.00 20.76 ?  6   PHE   B CA   1 
ATOM   3918 C C    . PHE   B 1 6   ? 45.116 -23.157 -19.716 1.00 24.62 ?  6   PHE   B C    1 
ATOM   3919 O O    . PHE   B 1 6   ? 44.391 -22.972 -20.697 1.00 27.44 ?  6   PHE   B O    1 
ATOM   3920 C CB   . PHE   B 1 6   ? 43.884 -22.202 -17.763 1.00 18.39 ?  6   PHE   B CB   1 
ATOM   3921 C CG   . PHE   B 1 6   ? 43.892 -21.309 -16.551 1.00 16.53 ?  6   PHE   B CG   1 
ATOM   3922 C CD1  . PHE   B 1 6   ? 44.407 -21.758 -15.350 1.00 15.34 ?  6   PHE   B CD1  1 
ATOM   3923 C CD2  . PHE   B 1 6   ? 43.387 -20.021 -16.615 1.00 16.56 ?  6   PHE   B CD2  1 
ATOM   3924 C CE1  . PHE   B 1 6   ? 44.406 -20.942 -14.225 1.00 15.34 ?  6   PHE   B CE1  1 
ATOM   3925 C CE2  . PHE   B 1 6   ? 43.393 -19.195 -15.502 1.00 17.33 ?  6   PHE   B CE2  1 
ATOM   3926 C CZ   . PHE   B 1 6   ? 43.907 -19.649 -14.308 1.00 16.08 ?  6   PHE   B CZ   1 
ATOM   3927 H H    . PHE   B 1 6   ? 44.584 -20.384 -19.258 1.00 25.41 ?  6   PHE   B H    1 
ATOM   3928 H HA   . PHE   B 1 6   ? 45.921 -22.345 -18.015 1.00 24.88 ?  6   PHE   B HA   1 
ATOM   3929 H HB2  . PHE   B 1 6   ? 43.138 -21.934 -18.321 1.00 22.04 ?  6   PHE   B HB2  1 
ATOM   3930 H HB3  . PHE   B 1 6   ? 43.753 -23.115 -17.457 1.00 22.04 ?  6   PHE   B HB3  1 
ATOM   3931 H HD1  . PHE   B 1 6   ? 44.753 -22.623 -15.288 1.00 18.39 ?  6   PHE   B HD1  1 
ATOM   3932 H HD2  . PHE   B 1 6   ? 43.039 -19.710 -17.416 1.00 19.85 ?  6   PHE   B HD2  1 
ATOM   3933 H HE1  . PHE   B 1 6   ? 44.767 -21.250 -13.421 1.00 18.38 ?  6   PHE   B HE1  1 
ATOM   3934 H HE2  . PHE   B 1 6   ? 43.050 -18.334 -15.562 1.00 20.77 ?  6   PHE   B HE2  1 
ATOM   3935 H HZ   . PHE   B 1 6   ? 43.913 -19.098 -13.559 1.00 19.26 ?  6   PHE   B HZ   1 
ATOM   3936 N N    A SER   B 1 7   ? 45.881 -24.238 -19.579 0.66 25.09 ?  7   SER   B N    1 
ATOM   3937 N N    B SER   B 1 7   ? 45.893 -24.230 -19.574 0.34 25.34 ?  7   SER   B N    1 
ATOM   3938 C CA   A SER   B 1 7   ? 45.957 -25.246 -20.626 0.66 26.74 ?  7   SER   B CA   1 
ATOM   3939 C CA   B SER   B 1 7   ? 46.035 -25.241 -20.611 0.34 26.45 ?  7   SER   B CA   1 
ATOM   3940 C C    A SER   B 1 7   ? 45.923 -26.640 -20.016 0.66 25.71 ?  7   SER   B C    1 
ATOM   3941 C C    B SER   B 1 7   ? 45.970 -26.626 -19.987 0.34 25.89 ?  7   SER   B C    1 
ATOM   3942 O O    A SER   B 1 7   ? 46.512 -26.882 -18.958 0.66 26.24 ?  7   SER   B O    1 
ATOM   3943 O O    B SER   B 1 7   ? 46.534 -26.862 -18.914 0.34 26.15 ?  7   SER   B O    1 
ATOM   3944 C CB   A SER   B 1 7   ? 47.228 -25.070 -21.466 0.66 29.05 ?  7   SER   B CB   1 
ATOM   3945 C CB   B SER   B 1 7   ? 47.371 -25.077 -21.348 0.34 27.75 ?  7   SER   B CB   1 
ATOM   3946 O OG   A SER   B 1 7   ? 47.147 -25.809 -22.671 0.66 30.75 ?  7   SER   B OG   1 
ATOM   3947 O OG   B SER   B 1 7   ? 47.560 -26.109 -22.301 0.34 28.97 ?  7   SER   B OG   1 
ATOM   3948 H H    A SER   B 1 7   ? 46.364 -24.407 -18.887 0.66 30.09 ?  7   SER   B H    1 
ATOM   3949 H H    B SER   B 1 7   ? 46.356 -24.395 -18.868 0.34 30.38 ?  7   SER   B H    1 
ATOM   3950 H HA   A SER   B 1 7   ? 45.192 -25.157 -21.214 0.66 32.06 ?  7   SER   B HA   1 
ATOM   3951 H HA   B SER   B 1 7   ? 45.314 -25.157 -21.254 0.34 31.71 ?  7   SER   B HA   1 
ATOM   3952 H HB2  A SER   B 1 7   ? 47.335 -24.131 -21.685 0.66 34.84 ?  7   SER   B HB2  1 
ATOM   3953 H HB2  B SER   B 1 7   ? 47.377 -24.219 -21.802 0.34 33.27 ?  7   SER   B HB2  1 
ATOM   3954 H HB3  A SER   B 1 7   ? 47.990 -25.378 -20.951 0.66 34.84 ?  7   SER   B HB3  1 
ATOM   3955 H HB3  B SER   B 1 7   ? 48.094 -25.113 -20.702 0.34 33.27 ?  7   SER   B HB3  1 
ATOM   3956 H HG   A SER   B 1 7   ? 47.852 -25.714 -23.116 0.66 36.87 ?  7   SER   B HG   1 
ATOM   3957 H HG   B SER   B 1 7   ? 48.290 -26.000 -22.700 0.34 34.74 ?  7   SER   B HG   1 
ATOM   3958 N N    A GLY   B 1 8   ? 45.229 -27.552 -20.693 0.66 25.54 ?  8   GLY   B N    1 
ATOM   3959 N N    B GLY   B 1 8   ? 45.277 -27.537 -20.666 0.34 25.65 ?  8   GLY   B N    1 
ATOM   3960 C CA   A GLY   B 1 8   ? 45.193 -28.937 -20.275 0.66 24.61 ?  8   GLY   B CA   1 
ATOM   3961 C CA   B GLY   B 1 8   ? 45.224 -28.919 -20.237 0.34 24.89 ?  8   GLY   B CA   1 
ATOM   3962 C C    A GLY   B 1 8   ? 44.203 -29.253 -19.182 0.66 23.55 ?  8   GLY   B C    1 
ATOM   3963 C C    B GLY   B 1 8   ? 44.253 -29.212 -19.121 0.34 23.82 ?  8   GLY   B C    1 
ATOM   3964 O O    A GLY   B 1 8   ? 44.294 -30.327 -18.575 0.66 24.14 ?  8   GLY   B O    1 
ATOM   3965 O O    B GLY   B 1 8   ? 44.412 -30.226 -18.433 0.34 24.32 ?  8   GLY   B O    1 
ATOM   3966 H H    A GLY   B 1 8   ? 44.774 -27.384 -21.403 0.66 30.62 ?  8   GLY   B H    1 
ATOM   3967 H H    B GLY   B 1 8   ? 44.830 -27.373 -21.381 0.34 30.75 ?  8   GLY   B H    1 
ATOM   3968 H HA2  A GLY   B 1 8   ? 44.975 -29.489 -21.040 0.66 29.50 ?  8   GLY   B HA2  1 
ATOM   3969 H HA2  B GLY   B 1 8   ? 44.987 -29.473 -20.997 0.34 29.84 ?  8   GLY   B HA2  1 
ATOM   3970 H HA3  A GLY   B 1 8   ? 46.070 -29.193 -19.957 0.66 29.50 ?  8   GLY   B HA3  1 
ATOM   3971 H HA3  B GLY   B 1 8   ? 46.103 -29.188 -19.933 0.34 29.84 ?  8   GLY   B HA3  1 
ATOM   3972 N N    . TYR   B 1 9   ? 43.247 -28.367 -18.916 1.00 22.60 ?  9   TYR   B N    1 
ATOM   3973 C CA   . TYR   B 1 9   ? 42.261 -28.603 -17.873 1.00 20.27 ?  9   TYR   B CA   1 
ATOM   3974 C C    . TYR   B 1 9   ? 41.073 -29.385 -18.406 1.00 19.84 ?  9   TYR   B C    1 
ATOM   3975 O O    . TYR   B 1 9   ? 40.684 -29.258 -19.570 1.00 22.49 ?  9   TYR   B O    1 
ATOM   3976 C CB   . TYR   B 1 9   ? 41.764 -27.296 -17.267 1.00 20.20 ?  9   TYR   B CB   1 
ATOM   3977 C CG   . TYR   B 1 9   ? 42.772 -26.678 -16.335 1.00 19.24 ?  9   TYR   B CG   1 
ATOM   3978 C CD1  . TYR   B 1 9   ? 43.897 -26.033 -16.830 1.00 20.30 ?  9   TYR   B CD1  1 
ATOM   3979 C CD2  . TYR   B 1 9   ? 42.613 -26.758 -14.960 1.00 18.33 ?  9   TYR   B CD2  1 
ATOM   3980 C CE1  . TYR   B 1 9   ? 44.830 -25.482 -15.984 1.00 20.27 ?  9   TYR   B CE1  1 
ATOM   3981 C CE2  . TYR   B 1 9   ? 43.540 -26.203 -14.103 1.00 18.92 ?  9   TYR   B CE2  1 
ATOM   3982 C CZ   . TYR   B 1 9   ? 44.645 -25.561 -14.624 1.00 20.17 ?  9   TYR   B CZ   1 
ATOM   3983 O OH   . TYR   B 1 9   ? 45.582 -25.015 -13.785 1.00 20.82 ?  9   TYR   B OH   1 
ATOM   3984 H H    A TYR   B 1 9   ? 43.136 -27.626 -19.339 0.66 27.09 ?  9   TYR   B H    1 
ATOM   3985 H H    B TYR   B 1 9   ? 43.106 -27.652 -19.375 0.34 27.09 ?  9   TYR   B H    1 
ATOM   3986 H HA   . TYR   B 1 9   ? 42.662 -29.121 -17.163 1.00 24.30 ?  9   TYR   B HA   1 
ATOM   3987 H HB2  . TYR   B 1 9   ? 41.582 -26.655 -17.973 1.00 24.21 ?  9   TYR   B HB2  1 
ATOM   3988 H HB3  . TYR   B 1 9   ? 40.962 -27.471 -16.757 1.00 24.21 ?  9   TYR   B HB3  1 
ATOM   3989 H HD1  . TYR   B 1 9   ? 44.024 -25.974 -17.748 1.00 24.33 ?  9   TYR   B HD1  1 
ATOM   3990 H HD2  . TYR   B 1 9   ? 41.865 -27.187 -14.608 1.00 21.97 ?  9   TYR   B HD2  1 
ATOM   3991 H HE1  . TYR   B 1 9   ? 45.576 -25.050 -16.327 1.00 24.30 ?  9   TYR   B HE1  1 
ATOM   3992 H HE2  . TYR   B 1 9   ? 43.416 -26.263 -13.181 1.00 22.68 ?  9   TYR   B HE2  1 
ATOM   3993 H HH   . TYR   B 1 9   ? 46.194 -24.663 -14.229 1.00 24.96 ?  9   TYR   B HH   1 
ATOM   3994 N N    . LEU   B 1 10  ? 40.503 -30.202 -17.529 1.00 18.03 ?  10  LEU   B N    1 
ATOM   3995 C CA   . LEU   B 1 10  ? 39.301 -30.966 -17.815 1.00 17.64 ?  10  LEU   B CA   1 
ATOM   3996 C C    . LEU   B 1 10  ? 38.104 -30.200 -17.264 1.00 17.11 ?  10  LEU   B C    1 
ATOM   3997 O O    . LEU   B 1 10  ? 38.113 -29.776 -16.104 1.00 16.95 ?  10  LEU   B O    1 
ATOM   3998 C CB   . LEU   B 1 10  ? 39.403 -32.339 -17.155 1.00 18.47 ?  10  LEU   B CB   1 
ATOM   3999 C CG   . LEU   B 1 10  ? 38.261 -33.285 -17.496 1.00 19.91 ?  10  LEU   B CG   1 
ATOM   4000 C CD1  . LEU   B 1 10  ? 38.406 -33.798 -18.923 1.00 21.46 ?  10  LEU   B CD1  1 
ATOM   4001 C CD2  . LEU   B 1 10  ? 38.194 -34.429 -16.502 1.00 21.38 ?  10  LEU   B CD2  1 
ATOM   4002 H H    . LEU   B 1 10  ? 40.803 -30.329 -16.725 1.00 21.61 ?  10  LEU   B H    1 
ATOM   4003 H HA   . LEU   B 1 10  ? 39.198 -31.076 -18.769 1.00 21.15 ?  10  LEU   B HA   1 
ATOM   4004 H HB2  . LEU   B 1 10  ? 40.232 -32.759 -17.439 1.00 22.13 ?  10  LEU   B HB2  1 
ATOM   4005 H HB3  . LEU   B 1 10  ? 39.414 -32.223 -16.190 1.00 22.13 ?  10  LEU   B HB3  1 
ATOM   4006 H HG   . LEU   B 1 10  ? 37.427 -32.797 -17.441 1.00 23.86 ?  10  LEU   B HG   1 
ATOM   4007 H HD11 . LEU   B 1 10  ? 37.699 -34.435 -19.098 1.00 25.72 ?  10  LEU   B HD11 1 
ATOM   4008 H HD12 . LEU   B 1 10  ? 38.335 -33.047 -19.535 1.00 25.72 ?  10  LEU   B HD12 1 
ATOM   4009 H HD13 . LEU   B 1 10  ? 39.271 -34.223 -19.019 1.00 25.72 ?  10  LEU   B HD13 1 
ATOM   4010 H HD21 . LEU   B 1 10  ? 37.463 -35.013 -16.750 1.00 25.63 ?  10  LEU   B HD21 1 
ATOM   4011 H HD22 . LEU   B 1 10  ? 39.033 -34.912 -16.523 1.00 25.63 ?  10  LEU   B HD22 1 
ATOM   4012 H HD23 . LEU   B 1 10  ? 38.042 -34.063 -15.616 1.00 25.63 ?  10  LEU   B HD23 1 
ATOM   4013 N N    . LYS   B 1 11  ? 37.087 -30.015 -18.096 1.00 18.50 ?  11  LYS   B N    1 
ATOM   4014 C CA   . LYS   B 1 11  ? 35.890 -29.296 -17.686 1.00 20.63 ?  11  LYS   B CA   1 
ATOM   4015 C C    . LYS   B 1 11  ? 34.994 -30.219 -16.863 1.00 20.13 ?  11  LYS   B C    1 
ATOM   4016 O O    . LYS   B 1 11  ? 34.607 -31.299 -17.330 1.00 22.41 ?  11  LYS   B O    1 
ATOM   4017 C CB   . LYS   B 1 11  ? 35.156 -28.801 -18.931 1.00 24.90 ?  11  LYS   B CB   1 
ATOM   4018 C CG   . LYS   B 1 11  ? 33.962 -27.906 -18.665 1.00 28.37 ?  11  LYS   B CG   1 
ATOM   4019 C CD   . LYS   B 1 11  ? 33.195 -27.648 -19.956 1.00 31.39 ?  11  LYS   B CD   1 
ATOM   4020 C CE   . LYS   B 1 11  ? 32.183 -26.527 -19.799 1.00 33.52 ?  11  LYS   B CE   1 
ATOM   4021 N NZ   . LYS   B 1 11  ? 32.847 -25.205 -19.643 1.00 34.52 ?  11  LYS   B NZ   1 
ATOM   4022 H H    . LYS   B 1 11  ? 37.064 -30.305 -18.907 1.00 22.18 ?  11  LYS   B H    1 
ATOM   4023 H HA   . LYS   B 1 11  ? 36.138 -28.530 -17.144 1.00 24.73 ?  11  LYS   B HA   1 
ATOM   4024 H HB2  . LYS   B 1 11  ? 35.782 -28.297 -19.476 1.00 29.85 ?  11  LYS   B HB2  1 
ATOM   4025 H HB3  . LYS   B 1 11  ? 34.840 -29.570 -19.428 1.00 29.85 ?  11  LYS   B HB3  1 
ATOM   4026 H HG2  . LYS   B 1 11  ? 33.365 -28.339 -18.037 1.00 34.01 ?  11  LYS   B HG2  1 
ATOM   4027 H HG3  . LYS   B 1 11  ? 34.267 -27.055 -18.314 1.00 34.01 ?  11  LYS   B HG3  1 
ATOM   4028 H HD2  . LYS   B 1 11  ? 33.821 -27.397 -20.654 1.00 37.64 ?  11  LYS   B HD2  1 
ATOM   4029 H HD3  . LYS   B 1 11  ? 32.719 -28.455 -20.211 1.00 37.64 ?  11  LYS   B HD3  1 
ATOM   4030 H HE2  . LYS   B 1 11  ? 31.619 -26.493 -20.587 1.00 40.19 ?  11  LYS   B HE2  1 
ATOM   4031 H HE3  . LYS   B 1 11  ? 31.646 -26.694 -19.009 1.00 40.19 ?  11  LYS   B HE3  1 
ATOM   4032 H HZ1  . LYS   B 1 11  ? 32.234 -24.564 -19.574 1.00 41.40 ?  11  LYS   B HZ1  1 
ATOM   4033 H HZ2  . LYS   B 1 11  ? 33.353 -25.202 -18.912 1.00 41.40 ?  11  LYS   B HZ2  1 
ATOM   4034 H HZ3  . LYS   B 1 11  ? 33.361 -25.038 -20.351 1.00 41.40 ?  11  LYS   B HZ3  1 
ATOM   4035 N N    . LEU   B 1 12  ? 34.658 -29.796 -15.642 1.00 18.57 ?  12  LEU   B N    1 
ATOM   4036 C CA   . LEU   B 1 12  ? 33.700 -30.504 -14.796 1.00 18.17 ?  12  LEU   B CA   1 
ATOM   4037 C C    . LEU   B 1 12  ? 32.307 -29.898 -14.884 1.00 18.01 ?  12  LEU   B C    1 
ATOM   4038 O O    . LEU   B 1 12  ? 31.320 -30.620 -15.052 1.00 18.54 ?  12  LEU   B O    1 
ATOM   4039 C CB   . LEU   B 1 12  ? 34.165 -30.517 -13.333 1.00 17.17 ?  12  LEU   B CB   1 
ATOM   4040 C CG   . LEU   B 1 12  ? 35.501 -31.204 -13.047 1.00 17.14 ?  12  LEU   B CG   1 
ATOM   4041 C CD1  . LEU   B 1 12  ? 35.827 -31.151 -11.566 1.00 17.13 ?  12  LEU   B CD1  1 
ATOM   4042 C CD2  . LEU   B 1 12  ? 35.497 -32.644 -13.545 1.00 17.86 ?  12  LEU   B CD2  1 
ATOM   4043 H H    . LEU   B 1 12  ? 34.976 -29.083 -15.276 1.00 22.26 ?  12  LEU   B H    1 
ATOM   4044 H HA   . LEU   B 1 12  ? 33.633 -31.419 -15.100 1.00 21.77 ?  12  LEU   B HA   1 
ATOM   4045 H HB2  . LEU   B 1 12  ? 34.241 -29.599 -13.032 1.00 20.57 ?  12  LEU   B HB2  1 
ATOM   4046 H HB3  . LEU   B 1 12  ? 33.487 -30.971 -12.807 1.00 20.57 ?  12  LEU   B HB3  1 
ATOM   4047 H HG   . LEU   B 1 12  ? 36.200 -30.731 -13.520 1.00 20.54 ?  12  LEU   B HG   1 
ATOM   4048 H HD11 . LEU   B 1 12  ? 36.681 -31.593 -11.415 1.00 20.53 ?  12  LEU   B HD11 1 
ATOM   4049 H HD12 . LEU   B 1 12  ? 35.884 -30.225 -11.285 1.00 20.53 ?  12  LEU   B HD12 1 
ATOM   4050 H HD13 . LEU   B 1 12  ? 35.131 -31.608 -11.069 1.00 20.53 ?  12  LEU   B HD13 1 
ATOM   4051 H HD21 . LEU   B 1 12  ? 36.301 -33.087 -13.235 1.00 21.40 ?  12  LEU   B HD21 1 
ATOM   4052 H HD22 . LEU   B 1 12  ? 34.713 -33.097 -13.197 1.00 21.40 ?  12  LEU   B HD22 1 
ATOM   4053 H HD23 . LEU   B 1 12  ? 35.473 -32.642 -14.516 1.00 21.40 ?  12  LEU   B HD23 1 
ATOM   4054 N N    . THR   B 1 13  ? 32.212 -28.580 -14.767 1.00 17.69 ?  13  THR   B N    1 
ATOM   4055 C CA   . THR   B 1 13  ? 30.982 -27.837 -14.978 1.00 17.79 ?  13  THR   B CA   1 
ATOM   4056 C C    . THR   B 1 13  ? 31.308 -26.639 -15.863 1.00 19.20 ?  13  THR   B C    1 
ATOM   4057 O O    . THR   B 1 13  ? 32.453 -26.443 -16.289 1.00 20.24 ?  13  THR   B O    1 
ATOM   4058 C CB   . THR   B 1 13  ? 30.374 -27.367 -13.651 1.00 17.15 ?  13  THR   B CB   1 
ATOM   4059 O OG1  . THR   B 1 13  ? 31.210 -26.337 -13.101 1.00 17.38 ?  13  THR   B OG1  1 
ATOM   4060 C CG2  . THR   B 1 13  ? 30.263 -28.518 -12.658 1.00 17.92 ?  13  THR   B CG2  1 
ATOM   4061 H H    . THR   B 1 13  ? 32.878 -28.074 -14.554 1.00 21.20 ?  13  THR   B H    1 
ATOM   4062 H HA   . THR   B 1 13  ? 30.333 -28.397 -15.428 1.00 21.32 ?  13  THR   B HA   1 
ATOM   4063 H HB   . THR   B 1 13  ? 29.481 -27.009 -13.808 1.00 20.55 ?  13  THR   B HB   1 
ATOM   4064 H HG1  . THR   B 1 13  ? 30.895 -25.576 -13.300 1.00 20.83 ?  13  THR   B HG1  1 
ATOM   4065 H HG21 . THR   B 1 13  ? 29.721 -28.250 -11.897 1.00 21.47 ?  13  THR   B HG21 1 
ATOM   4066 H HG22 . THR   B 1 13  ? 29.841 -29.280 -13.087 1.00 21.47 ?  13  THR   B HG22 1 
ATOM   4067 H HG23 . THR   B 1 13  ? 31.141 -28.775 -12.347 1.00 21.47 ?  13  THR   B HG23 1 
ATOM   4068 N N    A ASP   B 1 14  ? 30.292 -25.816 -16.124 0.66 20.15 ?  14  ASP   B N    1 
ATOM   4069 N N    B ASP   B 1 14  ? 30.296 -25.807 -16.123 0.34 19.98 ?  14  ASP   B N    1 
ATOM   4070 C CA   A ASP   B 1 14  ? 30.495 -24.650 -16.974 0.66 21.40 ?  14  ASP   B CA   1 
ATOM   4071 C CA   B ASP   B 1 14  ? 30.498 -24.646 -16.983 0.34 20.80 ?  14  ASP   B CA   1 
ATOM   4072 C C    A ASP   B 1 14  ? 31.597 -23.741 -16.442 0.66 19.82 ?  14  ASP   B C    1 
ATOM   4073 C C    B ASP   B 1 14  ? 31.519 -23.665 -16.425 0.34 19.26 ?  14  ASP   B C    1 
ATOM   4074 O O    A ASP   B 1 14  ? 32.263 -23.056 -17.228 0.66 21.25 ?  14  ASP   B O    1 
ATOM   4075 O O    B ASP   B 1 14  ? 32.027 -22.828 -17.180 0.34 19.90 ?  14  ASP   B O    1 
ATOM   4076 C CB   A ASP   B 1 14  ? 29.188 -23.872 -17.121 0.66 25.15 ?  14  ASP   B CB   1 
ATOM   4077 C CB   B ASP   B 1 14  ? 29.177 -23.913 -17.217 0.34 23.53 ?  14  ASP   B CB   1 
ATOM   4078 C CG   A ASP   B 1 14  ? 28.212 -24.536 -18.069 0.66 28.93 ?  14  ASP   B CG   1 
ATOM   4079 C CG   B ASP   B 1 14  ? 28.298 -24.610 -18.237 0.34 26.24 ?  14  ASP   B CG   1 
ATOM   4080 O OD1  A ASP   B 1 14  ? 28.575 -25.545 -18.713 0.66 30.04 ?  14  ASP   B OD1  1 
ATOM   4081 O OD1  B ASP   B 1 14  ? 28.849 -25.249 -19.159 0.34 27.06 ?  14  ASP   B OD1  1 
ATOM   4082 O OD2  A ASP   B 1 14  ? 27.068 -24.046 -18.161 0.66 30.66 -1 14  ASP   B OD2  1 
ATOM   4083 O OD2  B ASP   B 1 14  ? 27.058 -24.526 -18.118 0.34 27.19 -1 14  ASP   B OD2  1 
ATOM   4084 H H    A ASP   B 1 14  ? 29.492 -25.902 -15.817 0.66 24.16 ?  14  ASP   B H    1 
ATOM   4085 H H    B ASP   B 1 14  ? 29.497 -25.892 -15.816 0.34 23.95 ?  14  ASP   B H    1 
ATOM   4086 H HA   A ASP   B 1 14  ? 30.769 -24.945 -17.851 0.66 25.65 ?  14  ASP   B HA   1 
ATOM   4087 H HA   B ASP   B 1 14  ? 30.823 -24.953 -17.842 0.34 24.93 ?  14  ASP   B HA   1 
ATOM   4088 H HB2  A ASP   B 1 14  ? 28.744 -23.821 -16.262 0.66 30.15 ?  14  ASP   B HB2  1 
ATOM   4089 H HB2  B ASP   B 1 14  ? 28.689 -23.868 -16.380 0.34 28.21 ?  14  ASP   B HB2  1 
ATOM   4090 H HB3  A ASP   B 1 14  ? 29.382 -22.980 -17.451 0.66 30.15 ?  14  ASP   B HB3  1 
ATOM   4091 H HB3  B ASP   B 1 14  ? 29.372 -23.012 -17.532 0.34 28.21 ?  14  ASP   B HB3  1 
ATOM   4092 N N    . ASN   B 1 15  ? 31.816 -23.726 -15.124 1.00 17.45 ?  15  ASN   B N    1 
ATOM   4093 C CA   . ASN   B 1 15  ? 32.778 -22.808 -14.521 1.00 15.51 ?  15  ASN   B CA   1 
ATOM   4094 C C    . ASN   B 1 15  ? 33.868 -23.463 -13.682 1.00 14.36 ?  15  ASN   B C    1 
ATOM   4095 O O    . ASN   B 1 15  ? 34.705 -22.736 -13.137 1.00 14.39 ?  15  ASN   B O    1 
ATOM   4096 C CB   . ASN   B 1 15  ? 32.061 -21.752 -13.663 1.00 15.86 ?  15  ASN   B CB   1 
ATOM   4097 C CG   . ASN   B 1 15  ? 31.435 -22.349 -12.424 1.00 14.86 ?  15  ASN   B CG   1 
ATOM   4098 O OD1  . ASN   B 1 15  ? 30.495 -23.149 -12.512 1.00 16.87 ?  15  ASN   B OD1  1 
ATOM   4099 N ND2  . ASN   B 1 15  ? 31.949 -21.986 -11.265 1.00 14.18 ?  15  ASN   B ND2  1 
ATOM   4100 H H    A ASN   B 1 15  ? 31.416 -24.239 -14.557 0.66 20.92 ?  15  ASN   B H    1 
ATOM   4101 H H    B ASN   B 1 15  ? 31.451 -24.271 -14.565 0.34 20.92 ?  15  ASN   B H    1 
ATOM   4102 H HA   . ASN   B 1 15  ? 33.226 -22.328 -15.226 1.00 18.59 ?  15  ASN   B HA   1 
ATOM   4103 H HB2  . ASN   B 1 15  ? 32.707 -21.074 -13.384 1.00 19.01 ?  15  ASN   B HB2  1 
ATOM   4104 H HB3  . ASN   B 1 15  ? 31.359 -21.329 -14.188 1.00 19.01 ?  15  ASN   B HB3  1 
ATOM   4105 H HD21 . ASN   B 1 15  ? 31.620 -22.291 -10.530 1.00 16.99 ?  15  ASN   B HD21 1 
ATOM   4106 H HD22 . ASN   B 1 15  ? 32.611 -21.429 -11.233 1.00 16.99 ?  15  ASN   B HD22 1 
ATOM   4107 N N    . VAL   B 1 16  ? 33.892 -24.788 -13.552 1.00 14.37 ?  16  VAL   B N    1 
ATOM   4108 C CA   . VAL   B 1 16  ? 34.891 -25.477 -12.739 1.00 13.80 ?  16  VAL   B CA   1 
ATOM   4109 C C    . VAL   B 1 16  ? 35.685 -26.423 -13.628 1.00 14.20 ?  16  VAL   B C    1 
ATOM   4110 O O    . VAL   B 1 16  ? 35.108 -27.300 -14.288 1.00 15.36 ?  16  VAL   B O    1 
ATOM   4111 C CB   . VAL   B 1 16  ? 34.258 -26.237 -11.560 1.00 14.50 ?  16  VAL   B CB   1 
ATOM   4112 C CG1  . VAL   B 1 16  ? 35.338 -26.957 -10.752 1.00 14.42 ?  16  VAL   B CG1  1 
ATOM   4113 C CG2  . VAL   B 1 16  ? 33.451 -25.289 -10.681 1.00 15.38 ?  16  VAL   B CG2  1 
ATOM   4114 H H    . VAL   B 1 16  ? 33.328 -25.321 -13.932 1.00 17.22 ?  16  VAL   B H    1 
ATOM   4115 H HA   . VAL   B 1 16  ? 35.506 -24.823 -12.372 1.00 16.54 ?  16  VAL   B HA   1 
ATOM   4116 H HB   . VAL   B 1 16  ? 33.654 -26.910 -11.910 1.00 17.37 ?  16  VAL   B HB   1 
ATOM   4117 H HG11 . VAL   B 1 16  ? 34.954 -27.258 -9.914  1.00 17.28 ?  16  VAL   B HG11 1 
ATOM   4118 H HG12 . VAL   B 1 16  ? 35.666 -27.715 -11.258 1.00 17.28 ?  16  VAL   B HG12 1 
ATOM   4119 H HG13 . VAL   B 1 16  ? 36.064 -26.336 -10.574 1.00 17.28 ?  16  VAL   B HG13 1 
ATOM   4120 H HG21 . VAL   B 1 16  ? 33.113 -25.780 -9.917  1.00 18.43 ?  16  VAL   B HG21 1 
ATOM   4121 H HG22 . VAL   B 1 16  ? 34.024 -24.567 -10.386 1.00 18.43 ?  16  VAL   B HG22 1 
ATOM   4122 H HG23 . VAL   B 1 16  ? 32.710 -24.935 -11.200 1.00 18.43 ?  16  VAL   B HG23 1 
ATOM   4123 N N    . TYR   B 1 17  ? 37.011 -26.260 -13.599 1.00 14.11 ?  17  TYR   B N    1 
ATOM   4124 C CA   . TYR   B 1 17  ? 37.963 -27.011 -14.405 1.00 14.70 ?  17  TYR   B CA   1 
ATOM   4125 C C    . TYR   B 1 17  ? 39.011 -27.615 -13.483 1.00 13.73 ?  17  TYR   B C    1 
ATOM   4126 O O    . TYR   B 1 17  ? 39.278 -27.081 -12.404 1.00 13.85 ?  17  TYR   B O    1 
ATOM   4127 C CB   . TYR   B 1 17  ? 38.671 -26.082 -15.396 1.00 17.08 ?  17  TYR   B CB   1 
ATOM   4128 C CG   . TYR   B 1 17  ? 37.744 -25.311 -16.303 1.00 20.06 ?  17  TYR   B CG   1 
ATOM   4129 C CD1  . TYR   B 1 17  ? 37.166 -24.115 -15.892 1.00 21.68 ?  17  TYR   B CD1  1 
ATOM   4130 C CD2  . TYR   B 1 17  ? 37.450 -25.775 -17.577 1.00 22.46 ?  17  TYR   B CD2  1 
ATOM   4131 C CE1  . TYR   B 1 17  ? 36.316 -23.405 -16.725 1.00 23.11 ?  17  TYR   B CE1  1 
ATOM   4132 C CE2  . TYR   B 1 17  ? 36.604 -25.074 -18.418 1.00 24.03 ?  17  TYR   B CE2  1 
ATOM   4133 C CZ   . TYR   B 1 17  ? 36.040 -23.893 -17.985 1.00 24.42 ?  17  TYR   B CZ   1 
ATOM   4134 O OH   . TYR   B 1 17  ? 35.203 -23.192 -18.821 1.00 25.89 ?  17  TYR   B OH   1 
ATOM   4135 H H    . TYR   B 1 17  ? 37.404 -25.685 -13.087 1.00 16.90 ?  17  TYR   B H    1 
ATOM   4136 H HA   . TYR   B 1 17  ? 37.504 -27.719 -14.892 1.00 17.61 ?  17  TYR   B HA   1 
ATOM   4137 H HB2  . TYR   B 1 17  ? 39.200 -25.440 -14.899 1.00 20.47 ?  17  TYR   B HB2  1 
ATOM   4138 H HB3  . TYR   B 1 17  ? 39.243 -26.616 -15.961 1.00 20.47 ?  17  TYR   B HB3  1 
ATOM   4139 H HD1  . TYR   B 1 17  ? 37.348 -23.783 -15.044 1.00 25.99 ?  17  TYR   B HD1  1 
ATOM   4140 H HD2  . TYR   B 1 17  ? 37.824 -26.571 -17.872 1.00 26.93 ?  17  TYR   B HD2  1 
ATOM   4141 H HE1  . TYR   B 1 17  ? 35.933 -22.604 -16.439 1.00 27.70 ?  17  TYR   B HE1  1 
ATOM   4142 H HE2  . TYR   B 1 17  ? 36.412 -25.399 -19.270 1.00 28.81 ?  17  TYR   B HE2  1 
ATOM   4143 H HH   . TYR   B 1 17  ? 35.115 -23.593 -19.553 1.00 31.04 ?  17  TYR   B HH   1 
ATOM   4144 N N    . ILE   B 1 18  ? 39.626 -28.723 -13.905 1.00 13.99 ?  18  ILE   B N    1 
ATOM   4145 C CA   . ILE   B 1 18  ? 40.553 -29.438 -13.033 1.00 13.85 ?  18  ILE   B CA   1 
ATOM   4146 C C    . ILE   B 1 18  ? 41.724 -29.994 -13.839 1.00 14.07 ?  18  ILE   B C    1 
ATOM   4147 O O    . ILE   B 1 18  ? 41.573 -30.392 -14.999 1.00 15.71 ?  18  ILE   B O    1 
ATOM   4148 C CB   . ILE   B 1 18  ? 39.801 -30.533 -12.231 1.00 14.17 ?  18  ILE   B CB   1 
ATOM   4149 C CG1  . ILE   B 1 18  ? 40.661 -31.081 -11.089 1.00 14.43 ?  18  ILE   B CG1  1 
ATOM   4150 C CG2  . ILE   B 1 18  ? 39.282 -31.647 -13.156 1.00 14.92 ?  18  ILE   B CG2  1 
ATOM   4151 C CD1  . ILE   B 1 18  ? 39.852 -31.878 -10.076 1.00 15.78 ?  18  ILE   B CD1  1 
ATOM   4152 H H    . ILE   B 1 18  ? 39.522 -29.079 -14.682 1.00 16.76 ?  18  ILE   B H    1 
ATOM   4153 H HA   . ILE   B 1 18  ? 40.910 -28.816 -12.386 1.00 16.59 ?  18  ILE   B HA   1 
ATOM   4154 H HB   . ILE   B 1 18  ? 39.024 -30.122 -11.825 1.00 16.97 ?  18  ILE   B HB   1 
ATOM   4155 H HG12 . ILE   B 1 18  ? 41.344 -31.662 -11.453 1.00 17.29 ?  18  ILE   B HG12 1 
ATOM   4156 H HG13 . ILE   B 1 18  ? 41.071 -30.335 -10.622 1.00 17.29 ?  18  ILE   B HG13 1 
ATOM   4157 H HG21 . ILE   B 1 18  ? 38.704 -32.240 -12.645 1.00 17.88 ?  18  ILE   B HG21 1 
ATOM   4158 H HG22 . ILE   B 1 18  ? 38.775 -31.240 -13.877 1.00 17.88 ?  18  ILE   B HG22 1 
ATOM   4159 H HG23 . ILE   B 1 18  ? 40.031 -32.141 -13.512 1.00 17.88 ?  18  ILE   B HG23 1 
ATOM   4160 H HD11 . ILE   B 1 18  ? 40.434 -32.151 -9.350  1.00 18.91 ?  18  ILE   B HD11 1 
ATOM   4161 H HD12 . ILE   B 1 18  ? 39.135 -31.321 -9.734  1.00 18.91 ?  18  ILE   B HD12 1 
ATOM   4162 H HD13 . ILE   B 1 18  ? 39.481 -32.661 -10.514 1.00 18.91 ?  18  ILE   B HD13 1 
ATOM   4163 N N    . LYS   B 1 19  ? 42.900 -30.024 -13.206 1.00 14.73 ?  19  LYS   B N    1 
ATOM   4164 C CA   . LYS   B 1 19  ? 44.115 -30.501 -13.851 1.00 15.02 ?  19  LYS   B CA   1 
ATOM   4165 C C    . LYS   B 1 19  ? 45.001 -31.184 -12.821 1.00 14.99 ?  19  LYS   B C    1 
ATOM   4166 O O    . LYS   B 1 19  ? 45.082 -30.739 -11.675 1.00 14.45 ?  19  LYS   B O    1 
ATOM   4167 C CB   . LYS   B 1 19  ? 44.899 -29.339 -14.478 1.00 16.47 ?  19  LYS   B CB   1 
ATOM   4168 C CG   . LYS   B 1 19  ? 46.099 -29.755 -15.310 1.00 18.42 ?  19  LYS   B CG   1 
ATOM   4169 C CD   . LYS   B 1 19  ? 46.841 -28.532 -15.841 1.00 20.02 ?  19  LYS   B CD   1 
ATOM   4170 C CE   . LYS   B 1 19  ? 48.008 -28.921 -16.733 1.00 21.95 ?  19  LYS   B CE   1 
ATOM   4171 N NZ   . LYS   B 1 19  ? 48.776 -27.737 -17.207 1.00 22.59 ?  19  LYS   B NZ   1 
ATOM   4172 H H    . LYS   B 1 19  ? 43.010 -29.764 -12.388 1.00 17.65 ?  19  LYS   B H    1 
ATOM   4173 H HA   . LYS   B 1 19  ? 43.884 -31.138 -14.542 1.00 17.99 ?  19  LYS   B HA   1 
ATOM   4174 H HB2  . LYS   B 1 19  ? 44.299 -28.844 -15.055 1.00 19.74 ?  19  LYS   B HB2  1 
ATOM   4175 H HB3  . LYS   B 1 19  ? 45.214 -28.760 -13.763 1.00 19.74 ?  19  LYS   B HB3  1 
ATOM   4176 H HG2  . LYS   B 1 19  ? 46.705 -30.272 -14.759 1.00 22.08 ?  19  LYS   B HG2  1 
ATOM   4177 H HG3  . LYS   B 1 19  ? 45.791 -30.284 -16.063 1.00 22.08 ?  19  LYS   B HG3  1 
ATOM   4178 H HD2  . LYS   B 1 19  ? 46.227 -27.989 -16.360 1.00 23.99 ?  19  LYS   B HD2  1 
ATOM   4179 H HD3  . LYS   B 1 19  ? 47.186 -28.022 -15.092 1.00 23.99 ?  19  LYS   B HD3  1 
ATOM   4180 H HE2  . LYS   B 1 19  ? 48.609 -29.496 -16.233 1.00 26.31 ?  19  LYS   B HE2  1 
ATOM   4181 H HE3  . LYS   B 1 19  ? 47.666 -29.394 -17.510 1.00 26.31 ?  19  LYS   B HE3  1 
ATOM   4182 H HZ1  . LYS   B 1 19  ? 49.412 -27.995 -17.773 1.00 27.08 ?  19  LYS   B HZ1  1 
ATOM   4183 H HZ2  . LYS   B 1 19  ? 48.232 -27.168 -17.622 1.00 27.08 ?  19  LYS   B HZ2  1 
ATOM   4184 H HZ3  . LYS   B 1 19  ? 49.154 -27.324 -16.516 1.00 27.08 ?  19  LYS   B HZ3  1 
ATOM   4185 N N    . ASN   B 1 20  ? 45.686 -32.244 -13.244 1.00 16.10 ?  20  ASN   B N    1 
ATOM   4186 C CA   . ASN   B 1 20  ? 46.714 -32.876 -12.418 1.00 17.34 ?  20  ASN   B CA   1 
ATOM   4187 C C    . ASN   B 1 20  ? 47.990 -32.063 -12.607 1.00 17.79 ?  20  ASN   B C    1 
ATOM   4188 O O    . ASN   B 1 20  ? 48.650 -32.158 -13.647 1.00 19.80 ?  20  ASN   B O    1 
ATOM   4189 C CB   . ASN   B 1 20  ? 46.888 -34.332 -12.840 1.00 19.17 ?  20  ASN   B CB   1 
ATOM   4190 C CG   . ASN   B 1 20  ? 48.056 -35.024 -12.157 1.00 20.53 ?  20  ASN   B CG   1 
ATOM   4191 O OD1  . ASN   B 1 20  ? 48.744 -35.847 -12.774 1.00 22.77 ?  20  ASN   B OD1  1 
ATOM   4192 N ND2  . ASN   B 1 20  ? 48.277 -34.720 -10.887 1.00 19.88 ?  20  ASN   B ND2  1 
ATOM   4193 H H    . ASN   B 1 20  ? 45.571 -32.618 -14.008 1.00 19.29 ?  20  ASN   B H    1 
ATOM   4194 H HA   . ASN   B 1 20  ? 46.437 -32.850 -11.485 1.00 20.79 ?  20  ASN   B HA   1 
ATOM   4195 H HB2  . ASN   B 1 20  ? 46.081 -34.826 -12.617 1.00 22.98 ?  20  ASN   B HB2  1 
ATOM   4196 H HB3  . ASN   B 1 20  ? 47.038 -34.363 -13.796 1.00 22.98 ?  20  ASN   B HB3  1 
ATOM   4197 H HD21 . ASN   B 1 20  ? 48.932 -35.083 -10.465 1.00 23.83 ?  20  ASN   B HD21 1 
ATOM   4198 H HD22 . ASN   B 1 20  ? 47.772 -34.150 -10.480 1.00 23.83 ?  20  ASN   B HD22 1 
ATOM   4199 N N    . ALA   B 1 21  ? 48.330 -31.240 -11.611 1.00 17.28 ?  21  ALA   B N    1 
ATOM   4200 C CA   . ALA   B 1 21  ? 49.445 -30.319 -11.762 1.00 18.17 ?  21  ALA   B CA   1 
ATOM   4201 C C    . ALA   B 1 21  ? 49.900 -29.813 -10.402 1.00 17.15 ?  21  ALA   B C    1 
ATOM   4202 O O    . ALA   B 1 21  ? 49.153 -29.844 -9.419  1.00 16.78 ?  21  ALA   B O    1 
ATOM   4203 C CB   . ALA   B 1 21  ? 49.064 -29.143 -12.663 1.00 19.72 ?  21  ALA   B CB   1 
ATOM   4204 H H    . ALA   B 1 21  ? 47.928 -31.200 -10.842 1.00 20.71 ?  21  ALA   B H    1 
ATOM   4205 H HA   . ALA   B 1 21  ? 50.185 -30.794 -12.169 1.00 21.78 ?  21  ALA   B HA   1 
ATOM   4206 H HB1  . ALA   B 1 21  ? 49.849 -28.597 -12.799 1.00 23.63 ?  21  ALA   B HB1  1 
ATOM   4207 H HB2  . ALA   B 1 21  ? 48.749 -29.494 -13.510 1.00 23.63 ?  21  ALA   B HB2  1 
ATOM   4208 H HB3  . ALA   B 1 21  ? 48.363 -28.633 -12.232 1.00 23.63 ?  21  ALA   B HB3  1 
ATOM   4209 N N    . ASP   B 1 22  ? 51.153 -29.353 -10.381 1.00 16.60 ?  22  ASP   B N    1 
ATOM   4210 C CA   . ASP   B 1 22  ? 51.759 -28.651 -9.256  1.00 16.13 ?  22  ASP   B CA   1 
ATOM   4211 C C    . ASP   B 1 22  ? 51.355 -27.181 -9.349  1.00 14.48 ?  22  ASP   B C    1 
ATOM   4212 O O    . ASP   B 1 22  ? 51.661 -26.515 -10.341 1.00 14.75 ?  22  ASP   B O    1 
ATOM   4213 C CB   . ASP   B 1 22  ? 53.278 -28.835 -9.393  1.00 17.08 ?  22  ASP   B CB   1 
ATOM   4214 C CG   . ASP   B 1 22  ? 54.099 -28.063 -8.364  1.00 19.22 ?  22  ASP   B CG   1 
ATOM   4215 O OD1  . ASP   B 1 22  ? 53.741 -26.938 -7.980  1.00 19.00 ?  22  ASP   B OD1  1 
ATOM   4216 O OD2  . ASP   B 1 22  ? 55.164 -28.581 -7.964  1.00 21.78 -1 22  ASP   B OD2  1 
ATOM   4217 H H    . ASP   B 1 22  ? 51.692 -29.439 -11.049 1.00 19.90 ?  22  ASP   B H    1 
ATOM   4218 H HA   . ASP   B 1 22  ? 51.458 -29.029 -8.413  1.00 19.33 ?  22  ASP   B HA   1 
ATOM   4219 H HB2  . ASP   B 1 22  ? 53.492 -29.773 -9.298  1.00 20.47 ?  22  ASP   B HB2  1 
ATOM   4220 H HB3  . ASP   B 1 22  ? 53.550 -28.521 -10.271 1.00 20.47 ?  22  ASP   B HB3  1 
ATOM   4221 N N    . ILE   B 1 23  ? 50.643 -26.684 -8.333  1.00 13.53 ?  23  ILE   B N    1 
ATOM   4222 C CA   . ILE   B 1 23  ? 50.045 -25.349 -8.412  1.00 13.12 ?  23  ILE   B CA   1 
ATOM   4223 C C    . ILE   B 1 23  ? 51.099 -24.258 -8.551  1.00 12.83 ?  23  ILE   B C    1 
ATOM   4224 O O    . ILE   B 1 23  ? 50.830 -23.212 -9.152  1.00 12.57 ?  23  ILE   B O    1 
ATOM   4225 C CB   . ILE   B 1 23  ? 49.095 -25.102 -7.224  1.00 13.80 ?  23  ILE   B CB   1 
ATOM   4226 C CG1  . ILE   B 1 23  ? 48.263 -23.839 -7.444  1.00 14.45 ?  23  ILE   B CG1  1 
ATOM   4227 C CG2  . ILE   B 1 23  ? 49.855 -25.049 -5.915  1.00 15.10 ?  23  ILE   B CG2  1 
ATOM   4228 C CD1  . ILE   B 1 23  ? 47.131 -23.673 -6.440  1.00 14.95 ?  23  ILE   B CD1  1 
ATOM   4229 H H    . ILE   B 1 23  ? 50.491 -27.102 -7.594  1.00 16.21 ?  23  ILE   B H    1 
ATOM   4230 H HA   . ILE   B 1 23  ? 49.505 -25.318 -9.214  1.00 15.71 ?  23  ILE   B HA   1 
ATOM   4231 H HB   . ILE   B 1 23  ? 48.481 -25.850 -7.179  1.00 16.53 ?  23  ILE   B HB   1 
ATOM   4232 H HG12 . ILE   B 1 23  ? 48.846 -23.062 -7.368  1.00 17.31 ?  23  ILE   B HG12 1 
ATOM   4233 H HG13 . ILE   B 1 23  ? 47.876 -23.867 -8.334  1.00 17.31 ?  23  ILE   B HG13 1 
ATOM   4234 H HG21 . ILE   B 1 23  ? 49.222 -25.044 -5.182  1.00 18.09 ?  23  ILE   B HG21 1 
ATOM   4235 H HG22 . ILE   B 1 23  ? 50.429 -25.828 -5.852  1.00 18.09 ?  23  ILE   B HG22 1 
ATOM   4236 H HG23 . ILE   B 1 23  ? 50.393 -24.241 -5.894  1.00 18.09 ?  23  ILE   B HG23 1 
ATOM   4237 H HD11 . ILE   B 1 23  ? 46.603 -22.900 -6.686  1.00 17.91 ?  23  ILE   B HD11 1 
ATOM   4238 H HD12 . ILE   B 1 23  ? 46.580 -24.472 -6.460  1.00 17.91 ?  23  ILE   B HD12 1 
ATOM   4239 H HD13 . ILE   B 1 23  ? 47.509 -23.553 -5.557  1.00 17.91 ?  23  ILE   B HD13 1 
ATOM   4240 N N    . VAL   B 1 24  ? 52.296 -24.462 -7.992  1.00 13.38 ?  24  VAL   B N    1 
ATOM   4241 C CA   . VAL   B 1 24  ? 53.369 -23.480 -8.160  1.00 14.21 ?  24  VAL   B CA   1 
ATOM   4242 C C    . VAL   B 1 24  ? 53.828 -23.445 -9.611  1.00 14.26 ?  24  VAL   B C    1 
ATOM   4243 O O    . VAL   B 1 24  ? 53.966 -22.373 -10.215 1.00 14.38 ?  24  VAL   B O    1 
ATOM   4244 C CB   . VAL   B 1 24  ? 54.538 -23.788 -7.205  1.00 14.95 ?  24  VAL   B CB   1 
ATOM   4245 C CG1  . VAL   B 1 24  ? 55.748 -22.901 -7.517  1.00 16.02 ?  24  VAL   B CG1  1 
ATOM   4246 C CG2  . VAL   B 1 24  ? 54.107 -23.605 -5.777  1.00 15.72 ?  24  VAL   B CG2  1 
ATOM   4247 H H    . VAL   B 1 24  ? 52.511 -25.150 -7.519  1.00 16.03 ?  24  VAL   B H    1 
ATOM   4248 H HA   . VAL   B 1 24  ? 53.030 -22.604 -7.936  1.00 17.03 ?  24  VAL   B HA   1 
ATOM   4249 H HB   . VAL   B 1 24  ? 54.811 -24.714 -7.318  1.00 17.91 ?  24  VAL   B HB   1 
ATOM   4250 H HG11 . VAL   B 1 24  ? 56.348 -22.906 -6.753  1.00 19.19 ?  24  VAL   B HG11 1 
ATOM   4251 H HG12 . VAL   B 1 24  ? 56.206 -23.251 -8.296  1.00 19.19 ?  24  VAL   B HG12 1 
ATOM   4252 H HG13 . VAL   B 1 24  ? 55.441 -21.996 -7.687  1.00 19.19 ?  24  VAL   B HG13 1 
ATOM   4253 H HG21 . VAL   B 1 24  ? 54.832 -23.868 -5.189  1.00 18.84 ?  24  VAL   B HG21 1 
ATOM   4254 H HG22 . VAL   B 1 24  ? 53.888 -22.670 -5.633  1.00 18.84 ?  24  VAL   B HG22 1 
ATOM   4255 H HG23 . VAL   B 1 24  ? 53.327 -24.157 -5.608  1.00 18.84 ?  24  VAL   B HG23 1 
ATOM   4256 N N    . GLU   B 1 25  ? 54.080 -24.621 -10.191 1.00 14.95 ?  25  GLU   B N    1 
ATOM   4257 C CA   . GLU   B 1 25  ? 54.471 -24.668 -11.594 1.00 16.07 ?  25  GLU   B CA   1 
ATOM   4258 C C    . GLU   B 1 25  ? 53.365 -24.118 -12.481 1.00 15.13 ?  25  GLU   B C    1 
ATOM   4259 O O    . GLU   B 1 25  ? 53.636 -23.402 -13.454 1.00 16.00 ?  25  GLU   B O    1 
ATOM   4260 C CB   . GLU   B 1 25  ? 54.854 -26.095 -11.983 1.00 19.10 ?  25  GLU   B CB   1 
ATOM   4261 C CG   . GLU   B 1 25  ? 56.164 -26.539 -11.352 1.00 24.70 ?  25  GLU   B CG   1 
ATOM   4262 C CD   . GLU   B 1 25  ? 57.279 -25.509 -11.491 1.00 30.26 ?  25  GLU   B CD   1 
ATOM   4263 O OE1  . GLU   B 1 25  ? 57.661 -25.191 -12.637 1.00 32.12 ?  25  GLU   B OE1  1 
ATOM   4264 O OE2  . GLU   B 1 25  ? 57.767 -25.000 -10.453 1.00 31.80 -1 25  GLU   B OE2  1 
ATOM   4265 H H    . GLU   B 1 25  ? 54.031 -25.388 -9.800  1.00 17.91 ?  25  GLU   B H    1 
ATOM   4266 H HA   . GLU   B 1 25  ? 55.234 -24.090 -11.720 1.00 19.25 ?  25  GLU   B HA   1 
ATOM   4267 H HB2  . GLU   B 1 25  ? 54.157 -26.704 -11.683 1.00 22.90 ?  25  GLU   B HB2  1 
ATOM   4268 H HB3  . GLU   B 1 25  ? 54.945 -26.148 -12.947 1.00 22.90 ?  25  GLU   B HB3  1 
ATOM   4269 H HG2  . GLU   B 1 25  ? 56.027 -26.691 -10.410 1.00 29.61 ?  25  GLU   B HG2  1 
ATOM   4270 H HG3  . GLU   B 1 25  ? 56.464 -27.350 -11.790 1.00 29.61 ?  25  GLU   B HG3  1 
ATOM   4271 N N    . GLU   B 1 26  ? 52.111 -24.430 -12.153 1.00 14.37 ?  26  GLU   B N    1 
ATOM   4272 C CA   . GLU   B 1 26  ? 50.993 -23.899 -12.922 1.00 15.09 ?  26  GLU   B CA   1 
ATOM   4273 C C    . GLU   B 1 26  ? 50.955 -22.383 -12.848 1.00 14.18 ?  26  GLU   B C    1 
ATOM   4274 O O    . GLU   B 1 26  ? 50.771 -21.710 -13.865 1.00 15.52 ?  26  GLU   B O    1 
ATOM   4275 C CB   . GLU   B 1 26  ? 49.676 -24.476 -12.405 1.00 16.02 ?  26  GLU   B CB   1 
ATOM   4276 C CG   . GLU   B 1 26  ? 49.287 -25.788 -13.035 1.00 20.25 ?  26  GLU   B CG   1 
ATOM   4277 C CD   . GLU   B 1 26  ? 49.073 -25.691 -14.539 1.00 21.58 ?  26  GLU   B CD   1 
ATOM   4278 O OE1  . GLU   B 1 26  ? 48.128 -25.008 -14.992 1.00 21.81 ?  26  GLU   B OE1  1 
ATOM   4279 O OE2  . GLU   B 1 26  ? 49.850 -26.324 -15.266 1.00 23.96 -1 26  GLU   B OE2  1 
ATOM   4280 H H    . GLU   B 1 26  ? 51.884 -24.946 -11.499 1.00 17.22 ?  26  GLU   B H    1 
ATOM   4281 H HA   . GLU   B 1 26  ? 51.096 -24.153 -13.850 1.00 18.08 ?  26  GLU   B HA   1 
ATOM   4282 H HB2  . GLU   B 1 26  ? 49.749 -24.620 -11.448 1.00 19.19 ?  26  GLU   B HB2  1 
ATOM   4283 H HB3  . GLU   B 1 26  ? 48.964 -23.840 -12.585 1.00 19.19 ?  26  GLU   B HB3  1 
ATOM   4284 H HG2  . GLU   B 1 26  ? 49.996 -26.426 -12.879 1.00 24.28 ?  26  GLU   B HG2  1 
ATOM   4285 H HG3  . GLU   B 1 26  ? 48.459 -26.098 -12.637 1.00 24.28 ?  26  GLU   B HG3  1 
ATOM   4286 N N    . ALA   B 1 27  ? 51.096 -21.830 -11.644 1.00 13.47 ?  27  ALA   B N    1 
ATOM   4287 C CA   . ALA   B 1 27  ? 51.052 -20.380 -11.503 1.00 13.84 ?  27  ALA   B CA   1 
ATOM   4288 C C    . ALA   B 1 27  ? 52.122 -19.716 -12.362 1.00 14.56 ?  27  ALA   B C    1 
ATOM   4289 O O    . ALA   B 1 27  ? 51.855 -18.717 -13.048 1.00 15.24 ?  27  ALA   B O    1 
ATOM   4290 C CB   . ALA   B 1 27  ? 51.196 -19.991 -10.031 1.00 14.06 ?  27  ALA   B CB   1 
ATOM   4291 H H    . ALA   B 1 27  ? 51.207 -22.266 -10.906 1.00 16.13 ?  27  ALA   B H    1 
ATOM   4292 H HA   . ALA   B 1 27  ? 50.191 -20.063 -11.805 1.00 16.58 ?  27  ALA   B HA   1 
ATOM   4293 H HB1  . ALA   B 1 27  ? 51.159 -19.024 -9.955  1.00 16.84 ?  27  ALA   B HB1  1 
ATOM   4294 H HB2  . ALA   B 1 27  ? 50.466 -20.387 -9.526  1.00 16.84 ?  27  ALA   B HB2  1 
ATOM   4295 H HB3  . ALA   B 1 27  ? 52.044 -20.317 -9.695  1.00 16.84 ?  27  ALA   B HB3  1 
ATOM   4296 N N    . LYS   B 1 28  ? 53.338 -20.267 -12.353 1.00 15.94 ?  28  LYS   B N    1 
ATOM   4297 C CA   . LYS   B 1 28  ? 54.411 -19.655 -13.128 1.00 18.34 ?  28  LYS   B CA   1 
ATOM   4298 C C    . LYS   B 1 28  ? 54.153 -19.741 -14.628 1.00 18.56 ?  28  LYS   B C    1 
ATOM   4299 O O    . LYS   B 1 28  ? 54.553 -18.839 -15.374 1.00 19.68 ?  28  LYS   B O    1 
ATOM   4300 C CB   . LYS   B 1 28  ? 55.764 -20.254 -12.734 1.00 21.89 ?  28  LYS   B CB   1 
ATOM   4301 C CG   . LYS   B 1 28  ? 56.158 -19.906 -11.304 1.00 24.79 ?  28  LYS   B CG   1 
ATOM   4302 C CD   . LYS   B 1 28  ? 57.590 -20.288 -10.966 1.00 29.09 ?  28  LYS   B CD   1 
ATOM   4303 C CE   . LYS   B 1 28  ? 57.713 -21.750 -10.615 1.00 34.08 ?  28  LYS   B CE   1 
ATOM   4304 N NZ   . LYS   B 1 28  ? 59.063 -22.060 -10.065 1.00 36.95 ?  28  LYS   B NZ   1 
ATOM   4305 H H    . LYS   B 1 28  ? 53.564 -20.973 -11.914 1.00 19.10 ?  28  LYS   B H    1 
ATOM   4306 H HA   . LYS   B 1 28  ? 54.443 -18.714 -12.907 1.00 21.98 ?  28  LYS   B HA   1 
ATOM   4307 H HB2  . LYS   B 1 28  ? 55.722 -21.218 -12.807 1.00 26.24 ?  28  LYS   B HB2  1 
ATOM   4308 H HB3  . LYS   B 1 28  ? 56.451 -19.904 -13.325 1.00 26.24 ?  28  LYS   B HB3  1 
ATOM   4309 H HG2  . LYS   B 1 28  ? 56.062 -18.948 -11.179 1.00 29.72 ?  28  LYS   B HG2  1 
ATOM   4310 H HG3  . LYS   B 1 28  ? 55.568 -20.378 -10.696 1.00 29.72 ?  28  LYS   B HG3  1 
ATOM   4311 H HD2  . LYS   B 1 28  ? 58.155 -20.107 -11.734 1.00 34.88 ?  28  LYS   B HD2  1 
ATOM   4312 H HD3  . LYS   B 1 28  ? 57.884 -19.763 -10.204 1.00 34.88 ?  28  LYS   B HD3  1 
ATOM   4313 H HE2  . LYS   B 1 28  ? 57.050 -21.976 -9.943  1.00 40.87 ?  28  LYS   B HE2  1 
ATOM   4314 H HE3  . LYS   B 1 28  ? 57.578 -22.285 -11.413 1.00 40.87 ?  28  LYS   B HE3  1 
ATOM   4315 H HZ1  . LYS   B 1 28  ? 59.119 -22.924 -9.864  1.00 44.31 ?  28  LYS   B HZ1  1 
ATOM   4316 H HZ2  . LYS   B 1 28  ? 59.689 -21.861 -10.666 1.00 44.31 ?  28  LYS   B HZ2  1 
ATOM   4317 H HZ3  . LYS   B 1 28  ? 59.208 -21.581 -9.329  1.00 44.31 ?  28  LYS   B HZ3  1 
ATOM   4318 N N    . LYS   B 1 29  ? 53.456 -20.783 -15.083 1.00 19.41 ?  29  LYS   B N    1 
ATOM   4319 C CA   . LYS   B 1 29  ? 53.175 -20.943 -16.506 1.00 22.09 ?  29  LYS   B CA   1 
ATOM   4320 C C    . LYS   B 1 29  ? 51.925 -20.192 -16.955 1.00 20.75 ?  29  LYS   B C    1 
ATOM   4321 O O    . LYS   B 1 29  ? 51.932 -19.567 -18.020 1.00 21.99 ?  29  LYS   B O    1 
ATOM   4322 C CB   . LYS   B 1 29  ? 53.024 -22.428 -16.845 1.00 26.64 ?  29  LYS   B CB   1 
ATOM   4323 C CG   . LYS   B 1 29  ? 52.910 -22.708 -18.336 1.00 31.42 ?  29  LYS   B CG   1 
ATOM   4324 C CD   . LYS   B 1 29  ? 53.171 -24.174 -18.657 1.00 34.82 ?  29  LYS   B CD   1 
ATOM   4325 C CE   . LYS   B 1 29  ? 52.092 -25.078 -18.087 1.00 37.07 ?  29  LYS   B CE   1 
ATOM   4326 N NZ   . LYS   B 1 29  ? 52.369 -26.516 -18.369 1.00 38.99 ?  29  LYS   B NZ   1 
ATOM   4327 H H    . LYS   B 1 29  ? 53.128 -21.411 -14.583 1.00 23.27 ?  29  LYS   B H    1 
ATOM   4328 H HA   . LYS   B 1 29  ? 53.924 -20.598 -17.009 1.00 26.48 ?  29  LYS   B HA   1 
ATOM   4329 H HB2  . LYS   B 1 29  ? 53.803 -22.903 -16.513 1.00 31.94 ?  29  LYS   B HB2  1 
ATOM   4330 H HB3  . LYS   B 1 29  ? 52.224 -22.768 -16.417 1.00 31.94 ?  29  LYS   B HB3  1 
ATOM   4331 H HG2  . LYS   B 1 29  ? 52.014 -22.488 -18.633 1.00 37.68 ?  29  LYS   B HG2  1 
ATOM   4332 H HG3  . LYS   B 1 29  ? 53.563 -22.172 -18.812 1.00 37.68 ?  29  LYS   B HG3  1 
ATOM   4333 H HD2  . LYS   B 1 29  ? 53.188 -24.293 -19.620 1.00 41.76 ?  29  LYS   B HD2  1 
ATOM   4334 H HD3  . LYS   B 1 29  ? 54.022 -24.440 -18.273 1.00 41.76 ?  29  LYS   B HD3  1 
ATOM   4335 H HE2  . LYS   B 1 29  ? 52.051 -24.961 -17.125 1.00 44.46 ?  29  LYS   B HE2  1 
ATOM   4336 H HE3  . LYS   B 1 29  ? 51.239 -24.848 -18.489 1.00 44.46 ?  29  LYS   B HE3  1 
ATOM   4337 H HZ1  . LYS   B 1 29  ? 51.723 -27.023 -18.025 1.00 46.76 ?  29  LYS   B HZ1  1 
ATOM   4338 H HZ2  . LYS   B 1 29  ? 52.407 -26.652 -19.248 1.00 46.76 ?  29  LYS   B HZ2  1 
ATOM   4339 H HZ3  . LYS   B 1 29  ? 53.146 -26.753 -18.006 1.00 46.76 ?  29  LYS   B HZ3  1 
ATOM   4340 N N    . VAL   B 1 30  ? 50.851 -20.257 -16.163 1.00 19.27 ?  30  VAL   B N    1 
ATOM   4341 C CA   . VAL   B 1 30  ? 49.558 -19.678 -16.541 1.00 19.36 ?  30  VAL   B CA   1 
ATOM   4342 C C    . VAL   B 1 30  ? 49.558 -18.167 -16.395 1.00 18.00 ?  30  VAL   B C    1 
ATOM   4343 O O    . VAL   B 1 30  ? 48.812 -17.464 -17.096 1.00 18.85 ?  30  VAL   B O    1 
ATOM   4344 C CB   . VAL   B 1 30  ? 48.471 -20.286 -15.634 1.00 21.17 ?  30  VAL   B CB   1 
ATOM   4345 C CG1  . VAL   B 1 30  ? 47.197 -19.447 -15.659 1.00 21.74 ?  30  VAL   B CG1  1 
ATOM   4346 C CG2  . VAL   B 1 30  ? 48.188 -21.733 -16.021 1.00 22.03 ?  30  VAL   B CG2  1 
ATOM   4347 H H    . VAL   B 1 30  ? 50.837 -20.651 -15.390 1.00 23.10 ?  30  VAL   B H    1 
ATOM   4348 H HA   . VAL   B 1 30  ? 49.351 -19.919 -17.460 1.00 23.21 ?  30  VAL   B HA   1 
ATOM   4349 H HB   . VAL   B 1 30  ? 48.793 -20.299 -14.719 1.00 25.38 ?  30  VAL   B HB   1 
ATOM   4350 H HG11 . VAL   B 1 30  ? 46.452 -20.013 -15.405 1.00 26.06 ?  30  VAL   B HG11 1 
ATOM   4351 H HG12 . VAL   B 1 30  ? 47.281 -18.718 -15.027 1.00 26.06 ?  30  VAL   B HG12 1 
ATOM   4352 H HG13 . VAL   B 1 30  ? 47.052 -19.112 -16.552 1.00 26.06 ?  30  VAL   B HG13 1 
ATOM   4353 H HG21 . VAL   B 1 30  ? 47.490 -22.091 -15.441 1.00 26.40 ?  30  VAL   B HG21 1 
ATOM   4354 H HG22 . VAL   B 1 30  ? 47.888 -21.762 -16.944 1.00 26.40 ?  30  VAL   B HG22 1 
ATOM   4355 H HG23 . VAL   B 1 30  ? 48.997 -22.255 -15.918 1.00 26.40 ?  30  VAL   B HG23 1 
ATOM   4356 N N    A LYS   B 1 31  ? 50.358 -17.646 -15.473 0.66 17.14 ?  31  LYS   B N    1 
ATOM   4357 N N    B LYS   B 1 31  ? 50.365 -17.650 -15.478 0.34 17.73 ?  31  LYS   B N    1 
ATOM   4358 C CA   A LYS   B 1 31  ? 50.373 -16.229 -15.129 0.66 17.48 ?  31  LYS   B CA   1 
ATOM   4359 C CA   B LYS   B 1 31  ? 50.371 -16.237 -15.127 0.34 18.01 ?  31  LYS   B CA   1 
ATOM   4360 C C    A LYS   B 1 31  ? 48.982 -15.724 -14.730 0.66 15.97 ?  31  LYS   B C    1 
ATOM   4361 C C    B LYS   B 1 31  ? 48.967 -15.753 -14.751 0.34 16.23 ?  31  LYS   B C    1 
ATOM   4362 O O    A LYS   B 1 31  ? 48.446 -14.800 -15.350 0.66 16.79 ?  31  LYS   B O    1 
ATOM   4363 O O    B LYS   B 1 31  ? 48.401 -14.884 -15.422 0.34 16.39 ?  31  LYS   B O    1 
ATOM   4364 C CB   A LYS   B 1 31  ? 50.978 -15.394 -16.249 0.66 20.33 ?  31  LYS   B CB   1 
ATOM   4365 C CB   B LYS   B 1 31  ? 50.975 -15.395 -16.243 0.34 20.25 ?  31  LYS   B CB   1 
ATOM   4366 C CG   A LYS   B 1 31  ? 52.427 -15.789 -16.560 0.66 23.11 ?  31  LYS   B CG   1 
ATOM   4367 C CG   B LYS   B 1 31  ? 52.403 -15.821 -16.580 0.34 22.38 ?  31  LYS   B CG   1 
ATOM   4368 C CD   A LYS   B 1 31  ? 53.020 -14.962 -17.682 0.66 25.87 ?  31  LYS   B CD   1 
ATOM   4369 C CD   B LYS   B 1 31  ? 52.953 -15.081 -17.781 0.34 24.30 ?  31  LYS   B CD   1 
ATOM   4370 C CE   A LYS   B 1 31  ? 54.494 -15.265 -17.861 0.66 28.11 ?  31  LYS   B CE   1 
ATOM   4371 C CE   B LYS   B 1 31  ? 54.433 -15.364 -17.967 0.34 25.78 ?  31  LYS   B CE   1 
ATOM   4372 N NZ   A LYS   B 1 31  ? 55.266 -14.938 -16.629 0.66 29.49 ?  31  LYS   B NZ   1 
ATOM   4373 N NZ   B LYS   B 1 31  ? 55.231 -14.913 -16.791 0.34 26.58 ?  31  LYS   B NZ   1 
ATOM   4374 H H    A LYS   B 1 31  ? 50.921 -18.119 -15.025 0.66 20.54 ?  31  LYS   B H    1 
ATOM   4375 H H    B LYS   B 1 31  ? 50.936 -18.118 -15.038 0.34 21.25 ?  31  LYS   B H    1 
ATOM   4376 H HA   A LYS   B 1 31  ? 50.938 -16.132 -14.359 0.66 20.95 ?  31  LYS   B HA   1 
ATOM   4377 H HA   B LYS   B 1 31  ? 50.931 -16.134 -14.354 0.34 21.58 ?  31  LYS   B HA   1 
ATOM   4378 H HB2  A LYS   B 1 31  ? 50.455 -15.512 -17.057 0.66 24.37 ?  31  LYS   B HB2  1 
ATOM   4379 H HB2  B LYS   B 1 31  ? 50.437 -15.485 -17.043 0.34 24.28 ?  31  LYS   B HB2  1 
ATOM   4380 H HB3  A LYS   B 1 31  ? 50.972 -14.465 -15.978 0.66 24.37 ?  31  LYS   B HB3  1 
ATOM   4381 H HB3  B LYS   B 1 31  ? 50.998 -14.469 -15.955 0.34 24.28 ?  31  LYS   B HB3  1 
ATOM   4382 H HG2  A LYS   B 1 31  ? 52.965 -15.658 -15.763 0.66 27.71 ?  31  LYS   B HG2  1 
ATOM   4383 H HG2  B LYS   B 1 31  ? 52.976 -15.637 -15.818 0.34 26.83 ?  31  LYS   B HG2  1 
ATOM   4384 H HG3  A LYS   B 1 31  ? 52.451 -16.724 -16.826 0.66 27.71 ?  31  LYS   B HG3  1 
ATOM   4385 H HG3  B LYS   B 1 31  ? 52.415 -16.772 -16.781 0.34 26.83 ?  31  LYS   B HG3  1 
ATOM   4386 H HD2  A LYS   B 1 31  ? 52.559 -15.172 -18.509 0.66 31.01 ?  31  LYS   B HD2  1 
ATOM   4387 H HD2  B LYS   B 1 31  ? 52.483 -15.373 -18.577 0.34 29.14 ?  31  LYS   B HD2  1 
ATOM   4388 H HD3  A LYS   B 1 31  ? 52.922 -14.022 -17.469 0.66 31.01 ?  31  LYS   B HD3  1 
ATOM   4389 H HD3  B LYS   B 1 31  ? 52.837 -14.129 -17.649 0.34 29.14 ?  31  LYS   B HD3  1 
ATOM   4390 H HE2  A LYS   B 1 31  ? 54.608 -16.211 -18.051 0.66 33.71 ?  31  LYS   B HE2  1 
ATOM   4391 H HE2  B LYS   B 1 31  ? 54.566 -16.320 -18.076 0.34 30.91 ?  31  LYS   B HE2  1 
ATOM   4392 H HE3  A LYS   B 1 31  ? 54.844 -14.731 -18.592 0.66 33.71 ?  31  LYS   B HE3  1 
ATOM   4393 H HE3  B LYS   B 1 31  ? 54.752 -14.890 -18.750 0.34 30.91 ?  31  LYS   B HE3  1 
ATOM   4394 H HZ1  A LYS   B 1 31  ? 56.137 -15.016 -16.785 0.66 35.36 ?  31  LYS   B HZ1  1 
ATOM   4395 H HZ1  B LYS   B 1 31  ? 56.100 -14.988 -16.966 0.34 31.87 ?  31  LYS   B HZ1  1 
ATOM   4396 H HZ2  A LYS   B 1 31  ? 55.091 -14.103 -16.374 0.66 35.36 ?  31  LYS   B HZ2  1 
ATOM   4397 H HZ2  B LYS   B 1 31  ? 55.045 -14.063 -16.605 0.34 31.87 ?  31  LYS   B HZ2  1 
ATOM   4398 H HZ3  A LYS   B 1 31  ? 55.039 -15.493 -15.970 0.66 35.36 ?  31  LYS   B HZ3  1 
ATOM   4399 H HZ3  B LYS   B 1 31  ? 55.036 -15.413 -16.080 0.34 31.87 ?  31  LYS   B HZ3  1 
ATOM   4400 N N    . PRO   B 1 32  ? 48.384 -16.300 -13.683 1.00 14.53 ?  32  PRO   B N    1 
ATOM   4401 C CA   . PRO   B 1 32  ? 47.009 -15.939 -13.319 1.00 13.37 ?  32  PRO   B CA   1 
ATOM   4402 C C    . PRO   B 1 32  ? 46.929 -14.599 -12.606 1.00 13.61 ?  32  PRO   B C    1 
ATOM   4403 O O    . PRO   B 1 32  ? 47.857 -14.174 -11.909 1.00 14.78 ?  32  PRO   B O    1 
ATOM   4404 C CB   . PRO   B 1 32  ? 46.618 -17.056 -12.343 1.00 13.42 ?  32  PRO   B CB   1 
ATOM   4405 C CG   . PRO   B 1 32  ? 47.923 -17.390 -11.664 1.00 13.96 ?  32  PRO   B CG   1 
ATOM   4406 C CD   . PRO   B 1 32  ? 48.968 -17.278 -12.739 1.00 14.43 ?  32  PRO   B CD   1 
ATOM   4407 H HA   . PRO   B 1 32  ? 46.424 -15.952 -14.099 1.00 16.01 ?  32  PRO   B HA   1 
ATOM   4408 H HB2  . PRO   B 1 32  ? 45.966 -16.725 -11.704 1.00 16.07 ?  32  PRO   B HB2  1 
ATOM   4409 H HB3  . PRO   B 1 32  ? 46.273 -17.821 -12.828 1.00 16.07 ?  32  PRO   B HB3  1 
ATOM   4410 H HG2  . PRO   B 1 32  ? 48.097 -16.751 -10.950 1.00 16.72 ?  32  PRO   B HG2  1 
ATOM   4411 H HG3  . PRO   B 1 32  ? 47.893 -18.293 -11.310 1.00 16.72 ?  32  PRO   B HG3  1 
ATOM   4412 H HD2  . PRO   B 1 32  ? 49.794 -16.932 -12.367 1.00 17.29 ?  32  PRO   B HD2  1 
ATOM   4413 H HD3  . PRO   B 1 32  ? 49.097 -18.133 -13.167 1.00 17.29 ?  32  PRO   B HD3  1 
ATOM   4414 N N    . THR   B 1 33  ? 45.773 -13.948 -12.766 1.00 13.17 ?  33  THR   B N    1 
ATOM   4415 C CA   . THR   B 1 33  ? 45.479 -12.774 -11.953 1.00 13.21 ?  33  THR   B CA   1 
ATOM   4416 C C    . THR   B 1 33  ? 45.437 -13.128 -10.472 1.00 13.21 ?  33  THR   B C    1 
ATOM   4417 O O    . THR   B 1 33  ? 45.914 -12.354 -9.631  1.00 14.10 ?  33  THR   B O    1 
ATOM   4418 C CB   . THR   B 1 33  ? 44.159 -12.135 -12.395 1.00 13.78 ?  33  THR   B CB   1 
ATOM   4419 O OG1  . THR   B 1 33  ? 44.189 -11.876 -13.802 1.00 13.60 ?  33  THR   B OG1  1 
ATOM   4420 C CG2  . THR   B 1 33  ? 43.909 -10.841 -11.638 1.00 14.89 ?  33  THR   B CG2  1 
ATOM   4421 H H    . THR   B 1 33  ? 45.151 -14.167 -13.326 1.00 15.78 ?  33  THR   B H    1 
ATOM   4422 H HA   . THR   B 1 33  ? 46.180 -12.122 -12.082 1.00 15.82 ?  33  THR   B HA   1 
ATOM   4423 H HB   . THR   B 1 33  ? 43.425 -12.747 -12.199 1.00 16.51 ?  33  THR   B HB   1 
ATOM   4424 H HG1  . THR   B 1 33  ? 43.465 -11.515 -14.042 1.00 16.30 ?  33  THR   B HG1  1 
ATOM   4425 H HG21 . THR   B 1 33  ? 43.159 -10.371 -12.025 1.00 17.84 ?  33  THR   B HG21 1 
ATOM   4426 H HG22 . THR   B 1 33  ? 43.716 -11.033 -10.705 1.00 17.84 ?  33  THR   B HG22 1 
ATOM   4427 H HG23 . THR   B 1 33  ? 44.697 -10.278 -11.686 1.00 17.84 ?  33  THR   B HG23 1 
ATOM   4428 N N    . VAL   B 1 34  ? 44.870 -14.290 -10.130 1.00 12.43 ?  34  VAL   B N    1 
ATOM   4429 C CA   . VAL   B 1 34  ? 44.671 -14.682 -8.740  1.00 11.98 ?  34  VAL   B CA   1 
ATOM   4430 C C    . VAL   B 1 34  ? 45.098 -16.130 -8.567  1.00 11.41 ?  34  VAL   B C    1 
ATOM   4431 O O    . VAL   B 1 34  ? 44.587 -17.016 -9.261  1.00 11.70 ?  34  VAL   B O    1 
ATOM   4432 C CB   . VAL   B 1 34  ? 43.199 -14.537 -8.304  1.00 13.04 ?  34  VAL   B CB   1 
ATOM   4433 C CG1  . VAL   B 1 34  ? 43.026 -14.998 -6.862  1.00 13.16 ?  34  VAL   B CG1  1 
ATOM   4434 C CG2  . VAL   B 1 34  ? 42.699 -13.109 -8.491  1.00 13.86 ?  34  VAL   B CG2  1 
ATOM   4435 H H    . VAL   B 1 34  ? 44.599 -14.881 -10.697 1.00 14.89 ?  34  VAL   B H    1 
ATOM   4436 H HA   . VAL   B 1 34  ? 45.223 -14.133 -8.164  1.00 14.35 ?  34  VAL   B HA   1 
ATOM   4437 H HB   . VAL   B 1 34  ? 42.654 -15.112 -8.863  1.00 15.63 ?  34  VAL   B HB   1 
ATOM   4438 H HG11 . VAL   B 1 34  ? 42.173 -14.674 -6.528  1.00 15.77 ?  34  VAL   B HG11 1 
ATOM   4439 H HG12 . VAL   B 1 34  ? 43.043 -15.967 -6.830  1.00 15.77 ?  34  VAL   B HG12 1 
ATOM   4440 H HG13 . VAL   B 1 34  ? 43.747 -14.635 -6.323  1.00 15.77 ?  34  VAL   B HG13 1 
ATOM   4441 H HG21 . VAL   B 1 34  ? 41.780 -13.053 -8.189  1.00 16.61 ?  34  VAL   B HG21 1 
ATOM   4442 H HG22 . VAL   B 1 34  ? 43.256 -12.507 -7.973  1.00 16.61 ?  34  VAL   B HG22 1 
ATOM   4443 H HG23 . VAL   B 1 34  ? 42.751 -12.875 -9.433  1.00 16.61 ?  34  VAL   B HG23 1 
ATOM   4444 N N    . VAL   B 1 35  ? 45.996 -16.378 -7.617  1.00 10.81 ?  35  VAL   B N    1 
ATOM   4445 C CA   . VAL   B 1 35  ? 46.235 -17.722 -7.099  1.00 10.51 ?  35  VAL   B CA   1 
ATOM   4446 C C    . VAL   B 1 35  ? 45.696 -17.776 -5.678  1.00 10.32 ?  35  VAL   B C    1 
ATOM   4447 O O    . VAL   B 1 35  ? 45.900 -16.846 -4.890  1.00 10.64 ?  35  VAL   B O    1 
ATOM   4448 C CB   . VAL   B 1 35  ? 47.718 -18.144 -7.182  1.00 11.37 ?  35  VAL   B CB   1 
ATOM   4449 C CG1  . VAL   B 1 35  ? 48.624 -17.304 -6.265  1.00 11.83 ?  35  VAL   B CG1  1 
ATOM   4450 C CG2  . VAL   B 1 35  ? 47.860 -19.640 -6.872  1.00 11.80 ?  35  VAL   B CG2  1 
ATOM   4451 H H    . VAL   B 1 35  ? 46.488 -15.774 -7.251  1.00 12.94 ?  35  VAL   B H    1 
ATOM   4452 H HA   . VAL   B 1 35  ? 45.720 -18.352 -7.627  1.00 12.58 ?  35  VAL   B HA   1 
ATOM   4453 H HB   . VAL   B 1 35  ? 48.022 -18.016 -8.094  1.00 13.62 ?  35  VAL   B HB   1 
ATOM   4454 H HG11 . VAL   B 1 35  ? 49.545 -17.537 -6.441  1.00 14.17 ?  35  VAL   B HG11 1 
ATOM   4455 H HG12 . VAL   B 1 35  ? 48.467 -16.370 -6.452  1.00 14.17 ?  35  VAL   B HG12 1 
ATOM   4456 H HG13 . VAL   B 1 35  ? 48.399 -17.504 -5.341  1.00 14.17 ?  35  VAL   B HG13 1 
ATOM   4457 H HG21 . VAL   B 1 35  ? 48.787 -19.904 -6.974  1.00 14.13 ?  35  VAL   B HG21 1 
ATOM   4458 H HG22 . VAL   B 1 35  ? 47.566 -19.811 -5.962  1.00 14.13 ?  35  VAL   B HG22 1 
ATOM   4459 H HG23 . VAL   B 1 35  ? 47.306 -20.152 -7.492  1.00 14.13 ?  35  VAL   B HG23 1 
ATOM   4460 N N    . VAL   B 1 36  ? 44.975 -18.850 -5.362  1.00 10.46 ?  36  VAL   B N    1 
ATOM   4461 C CA   . VAL   B 1 36  ? 44.420 -19.058 -4.032  1.00 10.07 ?  36  VAL   B CA   1 
ATOM   4462 C C    . VAL   B 1 36  ? 45.422 -19.823 -3.178  1.00 9.86  ?  36  VAL   B C    1 
ATOM   4463 O O    . VAL   B 1 36  ? 45.972 -20.853 -3.602  1.00 10.66 ?  36  VAL   B O    1 
ATOM   4464 C CB   . VAL   B 1 36  ? 43.082 -19.812 -4.115  1.00 10.38 ?  36  VAL   B CB   1 
ATOM   4465 C CG1  . VAL   B 1 36  ? 42.577 -20.174 -2.719  1.00 10.98 ?  36  VAL   B CG1  1 
ATOM   4466 C CG2  . VAL   B 1 36  ? 42.057 -18.968 -4.843  1.00 10.81 ?  36  VAL   B CG2  1 
ATOM   4467 H H    . VAL   B 1 36  ? 44.799 -19.486 -5.913  1.00 12.53 ?  36  VAL   B H    1 
ATOM   4468 H HA   . VAL   B 1 36  ? 44.257 -18.195 -3.619  1.00 12.06 ?  36  VAL   B HA   1 
ATOM   4469 H HB   . VAL   B 1 36  ? 43.205 -20.629 -4.618  1.00 12.43 ?  36  VAL   B HB   1 
ATOM   4470 H HG11 . VAL   B 1 36  ? 41.637 -20.398 -2.772  1.00 13.15 ?  36  VAL   B HG11 1 
ATOM   4471 H HG12 . VAL   B 1 36  ? 43.083 -20.927 -2.384  1.00 13.15 ?  36  VAL   B HG12 1 
ATOM   4472 H HG13 . VAL   B 1 36  ? 42.698 -19.405 -2.133  1.00 13.15 ?  36  VAL   B HG13 1 
ATOM   4473 H HG21 . VAL   B 1 36  ? 41.214 -19.441 -4.870  1.00 12.94 ?  36  VAL   B HG21 1 
ATOM   4474 H HG22 . VAL   B 1 36  ? 41.947 -18.124 -4.368  1.00 12.94 ?  36  VAL   B HG22 1 
ATOM   4475 H HG23 . VAL   B 1 36  ? 42.370 -18.792 -5.745  1.00 12.94 ?  36  VAL   B HG23 1 
ATOM   4476 N N    . ASN   B 1 37  ? 45.640 -19.328 -1.961  1.00 10.11 ?  37  ASN   B N    1 
ATOM   4477 C CA   . ASN   B 1 37  ? 46.389 -20.048 -0.947  1.00 10.43 ?  37  ASN   B CA   1 
ATOM   4478 C C    . ASN   B 1 37  ? 45.440 -20.719 0.033   1.00 10.56 ?  37  ASN   B C    1 
ATOM   4479 O O    . ASN   B 1 37  ? 44.430 -20.141 0.439   1.00 10.81 ?  37  ASN   B O    1 
ATOM   4480 C CB   . ASN   B 1 37  ? 47.316 -19.100 -0.187  1.00 10.47 ?  37  ASN   B CB   1 
ATOM   4481 C CG   . ASN   B 1 37  ? 48.169 -19.816 0.829   1.00 10.98 ?  37  ASN   B CG   1 
ATOM   4482 O OD1  . ASN   B 1 37  ? 48.517 -20.985 0.653   1.00 11.42 ?  37  ASN   B OD1  1 
ATOM   4483 N ND2  . ASN   B 1 37  ? 48.506 -19.119 1.906   1.00 11.06 ?  37  ASN   B ND2  1 
ATOM   4484 H H    . ASN   B 1 37  ? 45.351 -18.557 -1.694  1.00 12.11 ?  37  ASN   B H    1 
ATOM   4485 H HA   . ASN   B 1 37  ? 46.925 -20.735 -1.369  1.00 12.49 ?  37  ASN   B HA   1 
ATOM   4486 H HB2  . ASN   B 1 37  ? 47.912 -18.671 -0.822  1.00 12.54 ?  37  ASN   B HB2  1 
ATOM   4487 H HB3  . ASN   B 1 37  ? 46.787 -18.438 0.277   1.00 12.54 ?  37  ASN   B HB3  1 
ATOM   4488 H HD21 . ASN   B 1 37  ? 48.998 -19.477 2.515   1.00 13.25 ?  37  ASN   B HD21 1 
ATOM   4489 H HD22 . ASN   B 1 37  ? 48.251 -18.307 1.993   1.00 13.25 ?  37  ASN   B HD22 1 
ATOM   4490 N N    . ALA   B 1 38  ? 45.796 -21.944 0.416   1.00 10.58 ?  38  ALA   B N    1 
ATOM   4491 C CA   . ALA   B 1 38  ? 45.131 -22.693 1.484   1.00 10.99 ?  38  ALA   B CA   1 
ATOM   4492 C C    . ALA   B 1 38  ? 45.713 -22.214 2.812   1.00 10.64 ?  38  ALA   B C    1 
ATOM   4493 O O    . ALA   B 1 38  ? 46.614 -22.826 3.396   1.00 11.66 ?  38  ALA   B O    1 
ATOM   4494 C CB   . ALA   B 1 38  ? 45.349 -24.186 1.286   1.00 12.33 ?  38  ALA   B CB   1 
ATOM   4495 H H    . ALA   B 1 38  ? 46.453 -22.376 0.067   1.00 12.67 ?  38  ALA   B H    1 
ATOM   4496 H HA   . ALA   B 1 38  ? 44.181 -22.509 1.474   1.00 13.17 ?  38  ALA   B HA   1 
ATOM   4497 H HB1  . ALA   B 1 38  ? 44.897 -24.669 2.003   1.00 14.77 ?  38  ALA   B HB1  1 
ATOM   4498 H HB2  . ALA   B 1 38  ? 44.971 -24.450 0.431   1.00 14.77 ?  38  ALA   B HB2  1 
ATOM   4499 H HB3  . ALA   B 1 38  ? 46.295 -24.379 1.306   1.00 14.77 ?  38  ALA   B HB3  1 
ATOM   4500 N N    . ALA   B 1 39  ? 45.190 -21.077 3.275   1.00 10.63 ?  39  ALA   B N    1 
ATOM   4501 C CA   . ALA   B 1 39  ? 45.734 -20.344 4.409   1.00 11.29 ?  39  ALA   B CA   1 
ATOM   4502 C C    . ALA   B 1 39  ? 45.111 -20.787 5.731   1.00 11.04 ?  39  ALA   B C    1 
ATOM   4503 O O    . ALA   B 1 39  ? 44.081 -21.465 5.774   1.00 11.87 ?  39  ALA   B O    1 
ATOM   4504 C CB   . ALA   B 1 39  ? 45.497 -18.843 4.217   1.00 12.14 ?  39  ALA   B CB   1 
ATOM   4505 H H    . ALA   B 1 39  ? 44.496 -20.705 2.931   1.00 12.73 ?  39  ALA   B H    1 
ATOM   4506 H HA   . ALA   B 1 39  ? 46.688 -20.498 4.457   1.00 13.52 ?  39  ALA   B HA   1 
ATOM   4507 H HB1  . ALA   B 1 39  ? 45.863 -18.366 4.976   1.00 14.54 ?  39  ALA   B HB1  1 
ATOM   4508 H HB2  . ALA   B 1 39  ? 45.940 -18.557 3.401   1.00 14.54 ?  39  ALA   B HB2  1 
ATOM   4509 H HB3  . ALA   B 1 39  ? 44.543 -18.678 4.149   1.00 14.54 ?  39  ALA   B HB3  1 
ATOM   4510 N N    . ASN   B 1 40  ? 45.753 -20.365 6.820   1.00 11.94 ?  40  ASN   B N    1 
ATOM   4511 C CA   . ASN   B 1 40  ? 45.189 -20.421 8.158   1.00 12.38 ?  40  ASN   B CA   1 
ATOM   4512 C C    . ASN   B 1 40  ? 45.009 -18.997 8.686   1.00 12.27 ?  40  ASN   B C    1 
ATOM   4513 O O    . ASN   B 1 40  ? 45.422 -18.018 8.057   1.00 12.22 ?  40  ASN   B O    1 
ATOM   4514 C CB   . ASN   B 1 40  ? 46.037 -21.299 9.093   1.00 13.66 ?  40  ASN   B CB   1 
ATOM   4515 C CG   . ASN   B 1 40  ? 47.494 -20.897 9.121   1.00 14.50 ?  40  ASN   B CG   1 
ATOM   4516 O OD1  . ASN   B 1 40  ? 47.818 -19.715 9.167   1.00 16.33 ?  40  ASN   B OD1  1 
ATOM   4517 N ND2  . ASN   B 1 40  ? 48.385 -21.879 9.096   1.00 14.19 ?  40  ASN   B ND2  1 
ATOM   4518 H H    . ASN   B 1 40  ? 46.549 -20.045 6.799   1.00 14.30 ?  40  ASN   B H    1 
ATOM   4519 H HA   . ASN   B 1 40  ? 44.309 -20.820 8.107   1.00 14.83 ?  40  ASN   B HA   1 
ATOM   4520 H HB2  . ASN   B 1 40  ? 45.687 -21.224 9.996   1.00 16.36 ?  40  ASN   B HB2  1 
ATOM   4521 H HB3  . ASN   B 1 40  ? 45.984 -22.219 8.793   1.00 16.36 ?  40  ASN   B HB3  1 
ATOM   4522 H HD21 . ASN   B 1 40  ? 49.225 -21.703 9.115   1.00 17.00 ?  40  ASN   B HD21 1 
ATOM   4523 H HD22 . ASN   B 1 40  ? 48.119 -22.699 9.064   1.00 17.00 ?  40  ASN   B HD22 1 
ATOM   4524 N N    . VAL   B 1 41  ? 44.351 -18.873 9.842   1.00 12.73 ?  41  VAL   B N    1 
ATOM   4525 C CA   . VAL   B 1 41  ? 43.890 -17.553 10.282  1.00 13.56 ?  41  VAL   B CA   1 
ATOM   4526 C C    . VAL   B 1 41  ? 45.040 -16.602 10.587  1.00 13.27 ?  41  VAL   B C    1 
ATOM   4527 O O    . VAL   B 1 41  ? 44.865 -15.380 10.505  1.00 13.41 ?  41  VAL   B O    1 
ATOM   4528 C CB   . VAL   B 1 41  ? 42.901 -17.633 11.461  1.00 14.64 ?  41  VAL   B CB   1 
ATOM   4529 C CG1  . VAL   B 1 41  ? 41.605 -18.301 11.030  1.00 14.81 ?  41  VAL   B CG1  1 
ATOM   4530 C CG2  . VAL   B 1 41  ? 43.526 -18.337 12.660  1.00 15.87 ?  41  VAL   B CG2  1 
ATOM   4531 H H    . VAL   B 1 41  ? 44.161 -19.516 10.372  1.00 15.25 ?  41  VAL   B H    1 
ATOM   4532 H HA   . VAL   B 1 41  ? 43.402 -17.154 9.547   1.00 16.25 ?  41  VAL   B HA   1 
ATOM   4533 H HB   . VAL   B 1 41  ? 42.682 -16.732 11.742  1.00 17.54 ?  41  VAL   B HB   1 
ATOM   4534 H HG11 . VAL   B 1 41  ? 40.981 -18.294 11.773  1.00 17.75 ?  41  VAL   B HG11 1 
ATOM   4535 H HG12 . VAL   B 1 41  ? 41.232 -17.811 10.280  1.00 17.75 ?  41  VAL   B HG12 1 
ATOM   4536 H HG13 . VAL   B 1 41  ? 41.793 -19.216 10.765  1.00 17.75 ?  41  VAL   B HG13 1 
ATOM   4537 H HG21 . VAL   B 1 41  ? 42.886 -18.349 13.387  1.00 19.02 ?  41  VAL   B HG21 1 
ATOM   4538 H HG22 . VAL   B 1 41  ? 43.757 -19.246 12.409  1.00 19.02 ?  41  VAL   B HG22 1 
ATOM   4539 H HG23 . VAL   B 1 41  ? 44.324 -17.856 12.928  1.00 19.02 ?  41  VAL   B HG23 1 
ATOM   4540 N N    . TYR   B 1 42  ? 46.205 -17.119 10.969  1.00 13.23 ?  42  TYR   B N    1 
ATOM   4541 C CA   . TYR   B 1 42  ? 47.357 -16.274 11.250  1.00 13.88 ?  42  TYR   B CA   1 
ATOM   4542 C C    . TYR   B 1 42  ? 48.328 -16.196 10.072  1.00 13.28 ?  42  TYR   B C    1 
ATOM   4543 O O    . TYR   B 1 42  ? 49.416 -15.628 10.209  1.00 14.22 ?  42  TYR   B O    1 
ATOM   4544 C CB   . TYR   B 1 42  ? 48.036 -16.701 12.558  1.00 15.76 ?  42  TYR   B CB   1 
ATOM   4545 C CG   . TYR   B 1 42  ? 47.462 -15.995 13.785  1.00 15.58 ?  42  TYR   B CG   1 
ATOM   4546 C CD1  . TYR   B 1 42  ? 47.700 -14.644 13.996  1.00 14.48 ?  42  TYR   B CD1  1 
ATOM   4547 C CD2  . TYR   B 1 42  ? 46.697 -16.670 14.725  1.00 17.37 ?  42  TYR   B CD2  1 
ATOM   4548 C CE1  . TYR   B 1 42  ? 47.197 -13.987 15.096  1.00 15.18 ?  42  TYR   B CE1  1 
ATOM   4549 C CE2  . TYR   B 1 42  ? 46.189 -16.014 15.841  1.00 17.07 ?  42  TYR   B CE2  1 
ATOM   4550 C CZ   . TYR   B 1 42  ? 46.442 -14.668 16.020  1.00 17.70 ?  42  TYR   B CZ   1 
ATOM   4551 O OH   . TYR   B 1 42  ? 45.950 -13.984 17.119  1.00 20.74 ?  42  TYR   B OH   1 
ATOM   4552 H H    . TYR   B 1 42  ? 46.354 -17.966 11.057  1.00 15.84 ?  42  TYR   B H    1 
ATOM   4553 H HA   . TYR   B 1 42  ? 47.026 -15.378 11.393  1.00 16.63 ?  42  TYR   B HA   1 
ATOM   4554 H HB2  . TYR   B 1 42  ? 47.918 -17.656 12.680  1.00 18.88 ?  42  TYR   B HB2  1 
ATOM   4555 H HB3  . TYR   B 1 42  ? 48.981 -16.488 12.502  1.00 18.88 ?  42  TYR   B HB3  1 
ATOM   4556 H HD1  . TYR   B 1 42  ? 48.216 -14.171 13.369  1.00 17.35 ?  42  TYR   B HD1  1 
ATOM   4557 H HD2  . TYR   B 1 42  ? 46.524 -17.579 14.606  1.00 20.82 ?  42  TYR   B HD2  1 
ATOM   4558 H HE1  . TYR   B 1 42  ? 47.375 -13.078 15.208  1.00 18.19 ?  42  TYR   B HE1  1 
ATOM   4559 H HE2  . TYR   B 1 42  ? 45.676 -16.480 16.459  1.00 20.45 ?  42  TYR   B HE2  1 
ATOM   4560 H HH   . TYR   B 1 42  ? 46.194 -13.184 17.075  1.00 24.86 ?  42  TYR   B HH   1 
ATOM   4561 N N    . LEU   B 1 43  ? 47.935 -16.705 8.908   1.00 12.31 ?  43  LEU   B N    1 
ATOM   4562 C CA   . LEU   B 1 43  ? 48.749 -16.625 7.698   1.00 12.17 ?  43  LEU   B CA   1 
ATOM   4563 C C    . LEU   B 1 43  ? 50.162 -17.138 7.952   1.00 12.45 ?  43  LEU   B C    1 
ATOM   4564 O O    . LEU   B 1 43  ? 51.146 -16.549 7.502   1.00 13.23 ?  43  LEU   B O    1 
ATOM   4565 C CB   . LEU   B 1 43  ? 48.767 -15.219 7.091   1.00 12.77 ?  43  LEU   B CB   1 
ATOM   4566 C CG   . LEU   B 1 43  ? 47.409 -14.612 6.719   1.00 12.93 ?  43  LEU   B CG   1 
ATOM   4567 C CD1  . LEU   B 1 43  ? 47.607 -13.218 6.145   1.00 14.18 ?  43  LEU   B CD1  1 
ATOM   4568 C CD2  . LEU   B 1 43  ? 46.631 -15.491 5.744   1.00 13.43 ?  43  LEU   B CD2  1 
ATOM   4569 H H    . LEU   B 1 43  ? 47.192 -17.117 8.793   1.00 14.74 ?  43  LEU   B H    1 
ATOM   4570 H HA   . LEU   B 1 43  ? 48.351 -17.216 7.035   1.00 14.57 ?  43  LEU   B HA   1 
ATOM   4571 H HB2  . LEU   B 1 43  ? 49.188 -14.623 7.724   1.00 15.30 ?  43  LEU   B HB2  1 
ATOM   4572 H HB3  . LEU   B 1 43  ? 49.295 -15.253 6.277   1.00 15.30 ?  43  LEU   B HB3  1 
ATOM   4573 H HG   . LEU   B 1 43  ? 46.881 -14.525 7.526   1.00 15.49 ?  43  LEU   B HG   1 
ATOM   4574 H HD11 . LEU   B 1 43  ? 46.740 -12.845 5.919   1.00 16.99 ?  43  LEU   B HD11 1 
ATOM   4575 H HD12 . LEU   B 1 43  ? 48.042 -12.660 6.811   1.00 16.99 ?  43  LEU   B HD12 1 
ATOM   4576 H HD13 . LEU   B 1 43  ? 48.161 -13.276 5.352   1.00 16.99 ?  43  LEU   B HD13 1 
ATOM   4577 H HD21 . LEU   B 1 43  ? 45.822 -15.024 5.479   1.00 16.09 ?  43  LEU   B HD21 1 
ATOM   4578 H HD22 . LEU   B 1 43  ? 47.182 -15.666 4.967   1.00 16.09 ?  43  LEU   B HD22 1 
ATOM   4579 H HD23 . LEU   B 1 43  ? 46.402 -16.324 6.185   1.00 16.09 ?  43  LEU   B HD23 1 
ATOM   4580 N N    . LYS   B 1 44  ? 50.261 -18.261 8.667   1.00 12.19 ?  44  LYS   B N    1 
ATOM   4581 C CA   . LYS   B 1 44  ? 51.530 -18.938 8.901   1.00 13.05 ?  44  LYS   B CA   1 
ATOM   4582 C C    . LYS   B 1 44  ? 51.652 -20.057 7.877   1.00 12.80 ?  44  LYS   B C    1 
ATOM   4583 O O    . LYS   B 1 44  ? 50.954 -21.072 7.964   1.00 13.68 ?  44  LYS   B O    1 
ATOM   4584 C CB   . LYS   B 1 44  ? 51.605 -19.453 10.337  1.00 14.66 ?  44  LYS   B CB   1 
ATOM   4585 C CG   . LYS   B 1 44  ? 51.792 -18.341 11.357  1.00 17.61 ?  44  LYS   B CG   1 
ATOM   4586 C CD   . LYS   B 1 44  ? 52.969 -17.453 10.937  1.00 20.99 ?  44  LYS   B CD   1 
ATOM   4587 C CE   . LYS   B 1 44  ? 53.511 -16.604 12.054  1.00 23.62 ?  44  LYS   B CE   1 
ATOM   4588 N NZ   . LYS   B 1 44  ? 54.697 -15.816 11.643  1.00 24.87 ?  44  LYS   B NZ   1 
ATOM   4589 H H    . LYS   B 1 44  ? 49.588 -18.652 9.031   1.00 14.60 ?  44  LYS   B H    1 
ATOM   4590 H HA   . LYS   B 1 44  ? 52.256 -18.321 8.732   1.00 15.63 ?  44  LYS   B HA   1 
ATOM   4591 H HB2  . LYS   B 1 44  ? 50.777 -19.914 10.552  1.00 17.57 ?  44  LYS   B HB2  1 
ATOM   4592 H HB3  . LYS   B 1 44  ? 52.354 -20.060 10.417  1.00 17.57 ?  44  LYS   B HB3  1 
ATOM   4593 H HG2  . LYS   B 1 44  ? 50.992 -17.801 11.404  1.00 21.11 ?  44  LYS   B HG2  1 
ATOM   4594 H HG3  . LYS   B 1 44  ? 51.996 -18.731 12.226  1.00 21.11 ?  44  LYS   B HG3  1 
ATOM   4595 H HD2  . LYS   B 1 44  ? 53.682 -18.024 10.598  1.00 25.16 ?  44  LYS   B HD2  1 
ATOM   4596 H HD3  . LYS   B 1 44  ? 52.665 -16.856 10.233  1.00 25.16 ?  44  LYS   B HD3  1 
ATOM   4597 H HE2  . LYS   B 1 44  ? 52.833 -15.967 12.300  1.00 28.31 ?  44  LYS   B HE2  1 
ATOM   4598 H HE3  . LYS   B 1 44  ? 53.751 -17.170 12.807  1.00 28.31 ?  44  LYS   B HE3  1 
ATOM   4599 H HZ1  . LYS   B 1 44  ? 54.978 -15.314 12.323  1.00 29.81 ?  44  LYS   B HZ1  1 
ATOM   4600 H HZ2  . LYS   B 1 44  ? 55.357 -16.358 11.392  1.00 29.81 ?  44  LYS   B HZ2  1 
ATOM   4601 H HZ3  . LYS   B 1 44  ? 54.486 -15.283 10.960  1.00 29.81 ?  44  LYS   B HZ3  1 
ATOM   4602 N N    . HIS   B 1 45  ? 52.511 -19.847 6.884   1.00 12.54 ?  45  HIS   B N    1 
ATOM   4603 C CA   . HIS   B 1 45  ? 52.537 -20.672 5.677   1.00 12.45 ?  45  HIS   B CA   1 
ATOM   4604 C C    . HIS   B 1 45  ? 53.552 -21.798 5.844   1.00 14.45 ?  45  HIS   B C    1 
ATOM   4605 O O    . HIS   B 1 45  ? 54.608 -21.828 5.223   1.00 16.95 ?  45  HIS   B O    1 
ATOM   4606 C CB   . HIS   B 1 45  ? 52.856 -19.812 4.465   1.00 12.64 ?  45  HIS   B CB   1 
ATOM   4607 C CG   . HIS   B 1 45  ? 51.982 -18.611 4.359   1.00 12.11 ?  45  HIS   B CG   1 
ATOM   4608 N ND1  . HIS   B 1 45  ? 50.606 -18.694 4.325   1.00 12.40 ?  45  HIS   B ND1  1 
ATOM   4609 C CD2  . HIS   B 1 45  ? 52.294 -17.296 4.311   1.00 12.90 ?  45  HIS   B CD2  1 
ATOM   4610 C CE1  . HIS   B 1 45  ? 50.113 -17.472 4.233   1.00 12.18 ?  45  HIS   B CE1  1 
ATOM   4611 N NE2  . HIS   B 1 45  ? 51.113 -16.606 4.223   1.00 12.65 ?  45  HIS   B NE2  1 
ATOM   4612 H H    . HIS   B 1 45  ? 53.090 -19.212 6.882   1.00 15.02 ?  45  HIS   B H    1 
ATOM   4613 H HA   . HIS   B 1 45  ? 51.659 -21.067 5.541   1.00 14.92 ?  45  HIS   B HA   1 
ATOM   4614 H HB2  . HIS   B 1 45  ? 53.775 -19.510 4.526   1.00 15.14 ?  45  HIS   B HB2  1 
ATOM   4615 H HB3  . HIS   B 1 45  ? 52.734 -20.341 3.661   1.00 15.14 ?  45  HIS   B HB3  1 
ATOM   4616 H HD2  . HIS   B 1 45  ? 53.150 -16.927 4.328   1.00 15.45 ?  45  HIS   B HD2  1 
ATOM   4617 H HE1  . HIS   B 1 45  ? 49.210 -17.253 4.183   1.00 14.59 ?  45  HIS   B HE1  1 
ATOM   4618 H HE2  . HIS   B 1 45  ? 51.035 -15.749 4.182   1.00 15.15 ?  45  HIS   B HE2  1 
ATOM   4619 N N    A GLY   B 1 46  ? 53.184 -22.759 6.688   0.66 16.04 ?  46  GLY   B N    1 
ATOM   4620 N N    B GLY   B 1 46  ? 53.203 -22.738 6.713   0.34 15.60 ?  46  GLY   B N    1 
ATOM   4621 C CA   A GLY   B 1 46  ? 54.106 -23.805 7.093   0.66 17.95 ?  46  GLY   B CA   1 
ATOM   4622 C CA   B GLY   B 1 46  ? 54.121 -23.803 7.054   0.34 16.90 ?  46  GLY   B CA   1 
ATOM   4623 C C    A GLY   B 1 46  ? 54.171 -25.037 6.213   0.66 19.55 ?  46  GLY   B C    1 
ATOM   4624 C C    B GLY   B 1 46  ? 54.156 -24.931 6.043   0.34 18.19 ?  46  GLY   B C    1 
ATOM   4625 O O    A GLY   B 1 46  ? 55.263 -25.507 5.884   0.66 22.75 ?  46  GLY   B O    1 
ATOM   4626 O O    B GLY   B 1 46  ? 55.189 -25.187 5.418   0.34 19.22 ?  46  GLY   B O    1 
ATOM   4627 H H    A GLY   B 1 46  ? 52.407 -22.805 7.058   0.66 19.22 ?  46  GLY   B H    1 
ATOM   4628 H H    B GLY   B 1 46  ? 52.444 -22.769 7.121   0.34 18.70 ?  46  GLY   B H    1 
ATOM   4629 H HA2  A GLY   B 1 46  ? 54.996 -23.426 7.144   0.66 21.51 ?  46  GLY   B HA2  1 
ATOM   4630 H HA2  B GLY   B 1 46  ? 55.015 -23.434 7.128   0.34 20.25 ?  46  GLY   B HA2  1 
ATOM   4631 H HA3  A GLY   B 1 46  ? 53.859 -24.104 7.980   0.66 21.51 ?  46  GLY   B HA3  1 
ATOM   4632 H HA3  B GLY   B 1 46  ? 53.873 -24.162 7.921   0.34 20.25 ?  46  GLY   B HA3  1 
ATOM   4633 N N    . GLY   B 1 47  ? 53.018 -25.598 5.848   1.00 18.29 ?  47  GLY   B N    1 
ATOM   4634 C CA   . GLY   B 1 47  ? 52.972 -26.864 5.146   1.00 16.06 ?  47  GLY   B CA   1 
ATOM   4635 C C    . GLY   B 1 47  ? 52.051 -26.850 3.940   1.00 13.96 ?  47  GLY   B C    1 
ATOM   4636 O O    . GLY   B 1 47  ? 51.395 -25.851 3.640   1.00 14.29 ?  47  GLY   B O    1 
ATOM   4637 H H    A GLY   B 1 47  ? 52.243 -25.271 6.024   0.66 21.92 ?  47  GLY   B H    1 
ATOM   4638 H H    B GLY   B 1 47  ? 52.248 -25.324 6.115   0.34 21.92 ?  47  GLY   B H    1 
ATOM   4639 H HA2  . GLY   B 1 47  ? 53.864 -27.104 4.844   1.00 19.25 ?  47  GLY   B HA2  1 
ATOM   4640 H HA3  . GLY   B 1 47  ? 52.668 -27.556 5.757   1.00 19.25 ?  47  GLY   B HA3  1 
ATOM   4641 N N    . GLY   B 1 48  ? 52.010 -27.994 3.259   1.00 13.10 ?  48  GLY   B N    1 
ATOM   4642 C CA   . GLY   B 1 48  ? 51.102 -28.155 2.139   1.00 13.13 ?  48  GLY   B CA   1 
ATOM   4643 C C    . GLY   B 1 48  ? 51.233 -27.040 1.125   1.00 12.59 ?  48  GLY   B C    1 
ATOM   4644 O O    . GLY   B 1 48  ? 52.334 -26.578 0.802   1.00 13.20 ?  48  GLY   B O    1 
ATOM   4645 H H    . GLY   B 1 48  ? 52.501 -28.677 3.419   1.00 15.69 ?  48  GLY   B H    1 
ATOM   4646 H HA2  . GLY   B 1 48  ? 51.283 -28.999 1.696   1.00 15.73 ?  48  GLY   B HA2  1 
ATOM   4647 H HA3  . GLY   B 1 48  ? 50.188 -28.167 2.462   1.00 15.73 ?  48  GLY   B HA3  1 
ATOM   4648 N N    . VAL   B 1 49  ? 50.086 -26.602 0.608   1.00 12.60 ?  49  VAL   B N    1 
ATOM   4649 C CA   . VAL   B 1 49  ? 50.067 -25.586 -0.440  1.00 12.59 ?  49  VAL   B CA   1 
ATOM   4650 C C    . VAL   B 1 49  ? 50.718 -24.295 0.045   1.00 11.54 ?  49  VAL   B C    1 
ATOM   4651 O O    . VAL   B 1 49  ? 51.505 -23.673 -0.675  1.00 12.51 ?  49  VAL   B O    1 
ATOM   4652 C CB   . VAL   B 1 49  ? 48.626 -25.344 -0.924  1.00 13.95 ?  49  VAL   B CB   1 
ATOM   4653 C CG1  . VAL   B 1 49  ? 48.560 -24.109 -1.811  1.00 14.05 ?  49  VAL   B CG1  1 
ATOM   4654 C CG2  . VAL   B 1 49  ? 48.094 -26.571 -1.660  1.00 15.43 ?  49  VAL   B CG2  1 
ATOM   4655 H H    . VAL   B 1 49  ? 49.303 -26.870 0.848   1.00 15.09 ?  49  VAL   B H    1 
ATOM   4656 H HA   . VAL   B 1 49  ? 50.578 -25.906 -1.196  1.00 15.09 ?  49  VAL   B HA   1 
ATOM   4657 H HB   . VAL   B 1 49  ? 48.054 -25.189 -0.158  1.00 16.71 ?  49  VAL   B HB   1 
ATOM   4658 H HG11 . VAL   B 1 49  ? 47.735 -24.135 -2.324  1.00 16.83 ?  49  VAL   B HG11 1 
ATOM   4659 H HG12 . VAL   B 1 49  ? 48.574 -23.317 -1.253  1.00 16.83 ?  49  VAL   B HG12 1 
ATOM   4660 H HG13 . VAL   B 1 49  ? 49.320 -24.111 -2.412  1.00 16.83 ?  49  VAL   B HG13 1 
ATOM   4661 H HG21 . VAL   B 1 49  ? 47.188 -26.397 -1.958  1.00 18.49 ?  49  VAL   B HG21 1 
ATOM   4662 H HG22 . VAL   B 1 49  ? 48.663 -26.750 -2.429  1.00 18.49 ?  49  VAL   B HG22 1 
ATOM   4663 H HG23 . VAL   B 1 49  ? 48.106 -27.330 -1.058  1.00 18.49 ?  49  VAL   B HG23 1 
ATOM   4664 N N    . ALA   B 1 50  ? 50.370 -23.853 1.254   1.00 11.63 ?  50  ALA   B N    1 
ATOM   4665 C CA   . ALA   B 1 50  ? 50.880 -22.573 1.735   1.00 11.31 ?  50  ALA   B CA   1 
ATOM   4666 C C    . ALA   B 1 50  ? 52.398 -22.597 1.848   1.00 11.54 ?  50  ALA   B C    1 
ATOM   4667 O O    . ALA   B 1 50  ? 53.080 -21.634 1.477   1.00 11.60 ?  50  ALA   B O    1 
ATOM   4668 C CB   . ALA   B 1 50  ? 50.246 -22.220 3.079   1.00 11.82 ?  50  ALA   B CB   1 
ATOM   4669 H H    . ALA   B 1 50  ? 49.850 -24.261 1.803   1.00 13.93 ?  50  ALA   B H    1 
ATOM   4670 H HA   . ALA   B 1 50  ? 50.645 -21.877 1.106   1.00 13.54 ?  50  ALA   B HA   1 
ATOM   4671 H HB1  . ALA   B 1 50  ? 50.596 -21.366 3.384   1.00 14.16 ?  50  ALA   B HB1  1 
ATOM   4672 H HB2  . ALA   B 1 50  ? 49.283 -22.158 2.969   1.00 14.16 ?  50  ALA   B HB2  1 
ATOM   4673 H HB3  . ALA   B 1 50  ? 50.459 -22.912 3.725   1.00 14.16 ?  50  ALA   B HB3  1 
ATOM   4674 N N    . GLY   B 1 51  ? 52.949 -23.695 2.356   1.00 12.24 ?  51  GLY   B N    1 
ATOM   4675 C CA   . GLY   B 1 51  ? 54.392 -23.797 2.433   1.00 12.86 ?  51  GLY   B CA   1 
ATOM   4676 C C    . GLY   B 1 51  ? 55.043 -23.744 1.067   1.00 12.34 ?  51  GLY   B C    1 
ATOM   4677 O O    . GLY   B 1 51  ? 56.085 -23.110 0.890   1.00 13.39 ?  51  GLY   B O    1 
ATOM   4678 H H    . GLY   B 1 51  ? 52.517 -24.379 2.652   1.00 14.67 ?  51  GLY   B H    1 
ATOM   4679 H HA2  . GLY   B 1 51  ? 54.740 -23.064 2.965   1.00 15.41 ?  51  GLY   B HA2  1 
ATOM   4680 H HA3  . GLY   B 1 51  ? 54.637 -24.632 2.859   1.00 15.41 ?  51  GLY   B HA3  1 
ATOM   4681 N N    . ALA   B 1 52  ? 54.443 -24.410 0.081   1.00 12.20 ?  52  ALA   B N    1 
ATOM   4682 C CA   . ALA   B 1 52  ? 55.013 -24.409 -1.260  1.00 12.79 ?  52  ALA   B CA   1 
ATOM   4683 C C    . ALA   B 1 52  ? 54.936 -23.028 -1.903  1.00 12.41 ?  52  ALA   B C    1 
ATOM   4684 O O    . ALA   B 1 52  ? 55.904 -22.577 -2.535  1.00 12.98 ?  52  ALA   B O    1 
ATOM   4685 C CB   . ALA   B 1 52  ? 54.303 -25.440 -2.131  1.00 13.68 ?  52  ALA   B CB   1 
ATOM   4686 H H    . ALA   B 1 52  ? 53.706 -24.854 0.160   1.00 14.61 ?  52  ALA   B H    1 
ATOM   4687 H HA   . ALA   B 1 52  ? 55.944 -24.657 -1.202  1.00 15.33 ?  52  ALA   B HA   1 
ATOM   4688 H HB1  . ALA   B 1 52  ? 54.699 -25.426 -3.020  1.00 16.39 ?  52  ALA   B HB1  1 
ATOM   4689 H HB2  . ALA   B 1 52  ? 54.417 -26.318 -1.736  1.00 16.39 ?  52  ALA   B HB2  1 
ATOM   4690 H HB3  . ALA   B 1 52  ? 53.362 -25.220 -2.187  1.00 16.39 ?  52  ALA   B HB3  1 
ATOM   4691 N N    . LEU   B 1 53  ? 53.787 -22.355 -1.786  1.00 11.86 ?  53  LEU   B N    1 
ATOM   4692 C CA   . LEU   B 1 53  ? 53.671 -21.013 -2.350  1.00 12.00 ?  53  LEU   B CA   1 
ATOM   4693 C C    . LEU   B 1 53  ? 54.674 -20.070 -1.698  1.00 11.73 ?  53  LEU   B C    1 
ATOM   4694 O O    . LEU   B 1 53  ? 55.385 -19.325 -2.384  1.00 12.61 ?  53  LEU   B O    1 
ATOM   4695 C CB   . LEU   B 1 53  ? 52.245 -20.475 -2.184  1.00 12.65 ?  53  LEU   B CB   1 
ATOM   4696 C CG   . LEU   B 1 53  ? 51.121 -21.204 -2.925  1.00 12.79 ?  53  LEU   B CG   1 
ATOM   4697 C CD1  . LEU   B 1 53  ? 49.772 -20.591 -2.577  1.00 14.29 ?  53  LEU   B CD1  1 
ATOM   4698 C CD2  . LEU   B 1 53  ? 51.329 -21.194 -4.435  1.00 14.82 ?  53  LEU   B CD2  1 
ATOM   4699 H H    . LEU   B 1 53  ? 53.079 -22.642 -1.390  1.00 14.20 ?  53  LEU   B H    1 
ATOM   4700 H HA   . LEU   B 1 53  ? 53.873 -21.053 -3.301  1.00 14.37 ?  53  LEU   B HA   1 
ATOM   4701 H HB2  . LEU   B 1 53  ? 52.024 -20.501 -1.242  1.00 15.16 ?  53  LEU   B HB2  1 
ATOM   4702 H HB3  . LEU   B 1 53  ? 52.235 -19.556 -2.491  1.00 15.16 ?  53  LEU   B HB3  1 
ATOM   4703 H HG   . LEU   B 1 53  ? 51.100 -22.128 -2.637  1.00 15.32 ?  53  LEU   B HG   1 
ATOM   4704 H HD11 . LEU   B 1 53  ? 49.072 -21.068 -3.054  1.00 17.12 ?  53  LEU   B HD11 1 
ATOM   4705 H HD12 . LEU   B 1 53  ? 49.627 -20.668 -1.620  1.00 17.12 ?  53  LEU   B HD12 1 
ATOM   4706 H HD13 . LEU   B 1 53  ? 49.770 -19.657 -2.837  1.00 17.12 ?  53  LEU   B HD13 1 
ATOM   4707 H HD21 . LEU   B 1 53  ? 50.630 -21.724 -4.853  1.00 17.76 ?  53  LEU   B HD21 1 
ATOM   4708 H HD22 . LEU   B 1 53  ? 51.281 -20.280 -4.755  1.00 17.76 ?  53  LEU   B HD22 1 
ATOM   4709 H HD23 . LEU   B 1 53  ? 52.195 -21.575 -4.639  1.00 17.76 ?  53  LEU   B HD23 1 
ATOM   4710 N N    . ASN   B 1 54  ? 54.762 -20.103 -0.369  1.00 11.58 ?  54  ASN   B N    1 
ATOM   4711 C CA   . ASN   B 1 54  ? 55.676 -19.195 0.308   1.00 12.15 ?  54  ASN   B CA   1 
ATOM   4712 C C    . ASN   B 1 54  ? 57.121 -19.473 -0.087  1.00 12.51 ?  54  ASN   B C    1 
ATOM   4713 O O    . ASN   B 1 54  ? 57.900 -18.537 -0.315  1.00 12.93 ?  54  ASN   B O    1 
ATOM   4714 C CB   . ASN   B 1 54  ? 55.510 -19.275 1.818   1.00 13.05 ?  54  ASN   B CB   1 
ATOM   4715 C CG   . ASN   B 1 54  ? 56.487 -18.369 2.533   1.00 13.39 ?  54  ASN   B CG   1 
ATOM   4716 O OD1  . ASN   B 1 54  ? 56.514 -17.158 2.291   1.00 13.73 ?  54  ASN   B OD1  1 
ATOM   4717 N ND2  . ASN   B 1 54  ? 57.322 -18.949 3.388   1.00 15.04 ?  54  ASN   B ND2  1 
ATOM   4718 H H    . ASN   B 1 54  ? 54.311 -20.624 0.145   1.00 13.87 ?  54  ASN   B H    1 
ATOM   4719 H HA   . ASN   B 1 54  ? 55.466 -18.289 0.037   1.00 14.55 ?  54  ASN   B HA   1 
ATOM   4720 H HB2  . ASN   B 1 54  ? 54.609 -18.998 2.058   1.00 15.64 ?  54  ASN   B HB2  1 
ATOM   4721 H HB3  . ASN   B 1 54  ? 55.668 -20.185 2.113   1.00 15.64 ?  54  ASN   B HB3  1 
ATOM   4722 H HD21 . ASN   B 1 54  ? 57.903 -18.476 3.814   1.00 18.02 ?  54  ASN   B HD21 1 
ATOM   4723 H HD22 . ASN   B 1 54  ? 57.282 -19.798 3.522   1.00 18.02 ?  54  ASN   B HD22 1 
ATOM   4724 N N    . LYS   B 1 55  ? 57.504 -20.753 -0.157  1.00 13.33 ?  55  LYS   B N    1 
ATOM   4725 C CA   . LYS   B 1 55  ? 58.859 -21.095 -0.574  1.00 14.23 ?  55  LYS   B CA   1 
ATOM   4726 C C    . LYS   B 1 55  ? 59.160 -20.549 -1.964  1.00 14.04 ?  55  LYS   B C    1 
ATOM   4727 O O    . LYS   B 1 55  ? 60.258 -20.036 -2.211  1.00 14.78 ?  55  LYS   B O    1 
ATOM   4728 C CB   . LYS   B 1 55  ? 59.060 -22.610 -0.526  1.00 16.10 ?  55  LYS   B CB   1 
ATOM   4729 C CG   . LYS   B 1 55  ? 60.436 -23.062 -0.959  1.00 19.91 ?  55  LYS   B CG   1 
ATOM   4730 C CD   . LYS   B 1 55  ? 60.616 -24.558 -0.785  1.00 23.05 ?  55  LYS   B CD   1 
ATOM   4731 C CE   . LYS   B 1 55  ? 60.738 -24.953 0.687   1.00 26.07 ?  55  LYS   B CE   1 
ATOM   4732 N NZ   . LYS   B 1 55  ? 61.081 -26.388 0.848   1.00 27.67 ?  55  LYS   B NZ   1 
ATOM   4733 H H    . LYS   B 1 55  ? 56.999 -21.424 0.027   1.00 15.97 ?  55  LYS   B H    1 
ATOM   4734 H HA   . LYS   B 1 55  ? 59.485 -20.690 0.041   1.00 17.05 ?  55  LYS   B HA   1 
ATOM   4735 H HB2  . LYS   B 1 55  ? 58.920 -22.908 0.388   1.00 19.30 ?  55  LYS   B HB2  1 
ATOM   4736 H HB3  . LYS   B 1 55  ? 58.411 -23.031 -1.110  1.00 19.30 ?  55  LYS   B HB3  1 
ATOM   4737 H HG2  . LYS   B 1 55  ? 60.561 -22.850 -1.896  1.00 23.86 ?  55  LYS   B HG2  1 
ATOM   4738 H HG3  . LYS   B 1 55  ? 61.103 -22.608 -0.420  1.00 23.86 ?  55  LYS   B HG3  1 
ATOM   4739 H HD2  . LYS   B 1 55  ? 59.850 -25.021 -1.158  1.00 27.64 ?  55  LYS   B HD2  1 
ATOM   4740 H HD3  . LYS   B 1 55  ? 61.428 -24.838 -1.237  1.00 27.64 ?  55  LYS   B HD3  1 
ATOM   4741 H HE2  . LYS   B 1 55  ? 61.437 -24.418 1.100   1.00 31.26 ?  55  LYS   B HE2  1 
ATOM   4742 H HE3  . LYS   B 1 55  ? 59.889 -24.786 1.130   1.00 31.26 ?  55  LYS   B HE3  1 
ATOM   4743 H HZ1  . LYS   B 1 55  ? 61.103 -26.597 1.713   1.00 33.18 ?  55  LYS   B HZ1  1 
ATOM   4744 H HZ2  . LYS   B 1 55  ? 60.468 -26.891 0.444   1.00 33.18 ?  55  LYS   B HZ2  1 
ATOM   4745 H HZ3  . LYS   B 1 55  ? 61.876 -26.551 0.488   1.00 33.18 ?  55  LYS   B HZ3  1 
ATOM   4746 N N    . ALA   B 1 56  ? 58.194 -20.637 -2.885  1.00 13.50 ?  56  ALA   B N    1 
ATOM   4747 C CA   . ALA   B 1 56  ? 58.422 -20.130 -4.233  1.00 14.13 ?  56  ALA   B CA   1 
ATOM   4748 C C    . ALA   B 1 56  ? 58.696 -18.634 -4.227  1.00 13.98 ?  56  ALA   B C    1 
ATOM   4749 O O    . ALA   B 1 56  ? 59.431 -18.134 -5.092  1.00 15.09 ?  56  ALA   B O    1 
ATOM   4750 C CB   . ALA   B 1 56  ? 57.230 -20.461 -5.132  1.00 15.15 ?  56  ALA   B CB   1 
ATOM   4751 H H    . ALA   B 1 56  ? 57.408 -20.973 -2.757  1.00 16.18 ?  56  ALA   B H    1 
ATOM   4752 H HA   . ALA   B 1 56  ? 59.201 -20.567 -4.605  1.00 16.93 ?  56  ALA   B HA   1 
ATOM   4753 H HB1  . ALA   B 1 56  ? 57.405 -20.123 -6.028  1.00 18.15 ?  56  ALA   B HB1  1 
ATOM   4754 H HB2  . ALA   B 1 56  ? 57.116 -21.424 -5.163  1.00 18.15 ?  56  ALA   B HB2  1 
ATOM   4755 H HB3  . ALA   B 1 56  ? 56.433 -20.043 -4.773  1.00 18.15 ?  56  ALA   B HB3  1 
ATOM   4756 N N    . THR   B 1 57  ? 58.127 -17.906 -3.264  1.00 13.94 ?  57  THR   B N    1 
ATOM   4757 C CA   . THR   B 1 57  ? 58.362 -16.471 -3.142  1.00 13.79 ?  57  THR   B CA   1 
ATOM   4758 C C    . THR   B 1 57  ? 59.606 -16.141 -2.327  1.00 14.58 ?  57  THR   B C    1 
ATOM   4759 O O    . THR   B 1 57  ? 59.843 -14.964 -2.029  1.00 15.08 ?  57  THR   B O    1 
ATOM   4760 C CB   . THR   B 1 57  ? 57.159 -15.744 -2.515  1.00 12.95 ?  57  THR   B CB   1 
ATOM   4761 O OG1  . THR   B 1 57  ? 57.132 -15.960 -1.098  1.00 13.47 ?  57  THR   B OG1  1 
ATOM   4762 C CG2  . THR   B 1 57  ? 55.843 -16.170 -3.159  1.00 13.47 ?  57  THR   B CG2  1 
ATOM   4763 H H    . THR   B 1 57  ? 57.589 -18.223 -2.669  1.00 16.70 ?  57  THR   B H    1 
ATOM   4764 H HA   . THR   B 1 57  ? 58.486 -16.108 -4.031  1.00 16.52 ?  57  THR   B HA   1 
ATOM   4765 H HB   . THR   B 1 57  ? 57.259 -14.793 -2.679  1.00 15.52 ?  57  THR   B HB   1 
ATOM   4766 H HG1  . THR   B 1 57  ? 57.050 -16.782 -0.936  1.00 16.13 ?  57  THR   B HG1  1 
ATOM   4767 H HG21 . THR   B 1 57  ? 55.114 -15.634 -2.822  1.00 16.13 ?  57  THR   B HG21 1 
ATOM   4768 H HG22 . THR   B 1 57  ? 55.894 -16.066 -4.124  1.00 16.13 ?  57  THR   B HG22 1 
ATOM   4769 H HG23 . THR   B 1 57  ? 55.664 -17.105 -2.961  1.00 16.13 ?  57  THR   B HG23 1 
ATOM   4770 N N    . ASN   B 1 58  ? 60.397 -17.144 -1.958  1.00 15.36 ?  58  ASN   B N    1 
ATOM   4771 C CA   . ASN   B 1 58  ? 61.599 -16.924 -1.158  1.00 18.46 ?  58  ASN   B CA   1 
ATOM   4772 C C    . ASN   B 1 58  ? 61.264 -16.211 0.151   1.00 16.47 ?  58  ASN   B C    1 
ATOM   4773 O O    . ASN   B 1 58  ? 62.006 -15.341 0.617   1.00 17.22 ?  58  ASN   B O    1 
ATOM   4774 C CB   . ASN   B 1 58  ? 62.687 -16.180 -1.940  1.00 25.65 ?  58  ASN   B CB   1 
ATOM   4775 C CG   . ASN   B 1 58  ? 64.056 -16.308 -1.297  1.00 35.66 ?  58  ASN   B CG   1 
ATOM   4776 O OD1  . ASN   B 1 58  ? 64.370 -17.325 -0.676  1.00 38.89 ?  58  ASN   B OD1  1 
ATOM   4777 N ND2  . ASN   B 1 58  ? 64.877 -15.274 -1.437  1.00 40.66 ?  58  ASN   B ND2  1 
ATOM   4778 H H    . ASN   B 1 58  ? 60.259 -17.973 -2.156  1.00 18.41 ?  58  ASN   B H    1 
ATOM   4779 H HA   . ASN   B 1 58  ? 61.966 -17.794 -0.929  1.00 22.12 ?  58  ASN   B HA   1 
ATOM   4780 H HB2  . ASN   B 1 58  ? 62.741 -16.547 -2.839  1.00 30.75 ?  58  ASN   B HB2  1 
ATOM   4781 H HB3  . ASN   B 1 58  ? 62.463 -15.238 -1.980  1.00 30.75 ?  58  ASN   B HB3  1 
ATOM   4782 H HD21 . ASN   B 1 58  ? 65.665 -15.300 -1.091  1.00 48.77 ?  58  ASN   B HD21 1 
ATOM   4783 H HD22 . ASN   B 1 58  ? 64.623 -14.579 -1.874  1.00 48.77 ?  58  ASN   B HD22 1 
ATOM   4784 N N    . ASN   B 1 59  ? 60.138 -16.595 0.755   1.00 15.36 ?  59  ASN   B N    1 
ATOM   4785 C CA   . ASN   B 1 59  ? 59.654 -16.126 2.053   1.00 15.19 ?  59  ASN   B CA   1 
ATOM   4786 C C    . ASN   B 1 59  ? 59.055 -14.721 1.998   1.00 14.33 ?  59  ASN   B C    1 
ATOM   4787 O O    . ASN   B 1 59  ? 58.619 -14.217 3.038   1.00 14.45 ?  59  ASN   B O    1 
ATOM   4788 C CB   . ASN   B 1 59  ? 60.720 -16.189 3.161   1.00 15.88 ?  59  ASN   B CB   1 
ATOM   4789 C CG   . ASN   B 1 59  ? 60.123 -16.359 4.537   1.00 17.59 ?  59  ASN   B CG   1 
ATOM   4790 O OD1  . ASN   B 1 59  ? 59.294 -17.245 4.759   1.00 17.72 ?  59  ASN   B OD1  1 
ATOM   4791 N ND2  . ASN   B 1 59  ? 60.544 -15.516 5.476   1.00 17.74 ?  59  ASN   B ND2  1 
ATOM   4792 H H    . ASN   B 1 59  ? 59.600 -17.168 0.404   1.00 18.41 ?  59  ASN   B H    1 
ATOM   4793 H HA   . ASN   B 1 59  ? 58.947 -16.728 2.330   1.00 18.20 ?  59  ASN   B HA   1 
ATOM   4794 H HB2  . ASN   B 1 59  ? 61.311 -16.945 3.004   1.00 19.02 ?  59  ASN   B HB2  1 
ATOM   4795 H HB3  . ASN   B 1 59  ? 61.231 -15.366 3.166   1.00 19.02 ?  59  ASN   B HB3  1 
ATOM   4796 H HD21 . ASN   B 1 59  ? 60.236 -15.574 6.280   1.00 21.26 ?  59  ASN   B HD21 1 
ATOM   4797 H HD22 . ASN   B 1 59  ? 61.123 -14.912 5.284   1.00 21.26 ?  59  ASN   B HD22 1 
ATOM   4798 N N    . ALA   B 1 60  ? 58.993 -14.080 0.828   1.00 14.26 ?  60  ALA   B N    1 
ATOM   4799 C CA   . ALA   B 1 60  ? 58.398 -12.747 0.757   1.00 14.38 ?  60  ALA   B CA   1 
ATOM   4800 C C    . ALA   B 1 60  ? 56.926 -12.777 1.154   1.00 13.47 ?  60  ALA   B C    1 
ATOM   4801 O O    . ALA   B 1 60  ? 56.419 -11.831 1.770   1.00 13.83 ?  60  ALA   B O    1 
ATOM   4802 C CB   . ALA   B 1 60  ? 58.566 -12.168 -0.647  1.00 15.41 ?  60  ALA   B CB   1 
ATOM   4803 H H    . ALA   B 1 60  ? 59.283 -14.392 0.083   1.00 17.08 ?  60  ALA   B H    1 
ATOM   4804 H HA   . ALA   B 1 60  ? 58.860 -12.168 1.380   1.00 17.23 ?  60  ALA   B HA   1 
ATOM   4805 H HB1  . ALA   B 1 60  ? 58.169 -11.287 -0.672  1.00 18.47 ?  60  ALA   B HB1  1 
ATOM   4806 H HB2  . ALA   B 1 60  ? 59.515 -12.111 -0.850  1.00 18.47 ?  60  ALA   B HB2  1 
ATOM   4807 H HB3  . ALA   B 1 60  ? 58.128 -12.752 -1.284  1.00 18.47 ?  60  ALA   B HB3  1 
ATOM   4808 N N    . MET   B 1 61  ? 56.218 -13.848 0.796   1.00 12.73 ?  61  MET   B N    1 
ATOM   4809 C CA   . MET   B 1 61  ? 54.822 -13.978 1.196   1.00 12.71 ?  61  MET   B CA   1 
ATOM   4810 C C    . MET   B 1 61  ? 54.684 -13.989 2.718   1.00 12.75 ?  61  MET   B C    1 
ATOM   4811 O O    . MET   B 1 61  ? 53.780 -13.345 3.271   1.00 12.15 ?  61  MET   B O    1 
ATOM   4812 C CB   . MET   B 1 61  ? 54.251 -15.251 0.570   1.00 12.70 ?  61  MET   B CB   1 
ATOM   4813 C CG   . MET   B 1 61  ? 52.811 -15.547 0.975   1.00 12.07 ?  61  MET   B CG   1 
ATOM   4814 S SD   . MET   B 1 61  ? 52.173 -17.052 0.206   1.00 12.94 ?  61  MET   B SD   1 
ATOM   4815 C CE   . MET   B 1 61  ? 51.937 -16.469 -1.472  1.00 14.00 ?  61  MET   B CE   1 
ATOM   4816 H H    . MET   B 1 61  ? 56.523 -14.510 0.329   1.00 15.25 ?  61  MET   B H    1 
ATOM   4817 H HA   . MET   B 1 61  ? 54.324 -13.231 0.837   1.00 15.23 ?  61  MET   B HA   1 
ATOM   4818 H HB2  . MET   B 1 61  ? 54.269 -15.167 -0.400  1.00 15.21 ?  61  MET   B HB2  1 
ATOM   4819 H HB3  . MET   B 1 61  ? 54.794 -16.011 0.838   1.00 15.21 ?  61  MET   B HB3  1 
ATOM   4820 H HG2  . MET   B 1 61  ? 52.768 -15.668 1.940   1.00 14.46 ?  61  MET   B HG2  1 
ATOM   4821 H HG3  . MET   B 1 61  ? 52.246 -14.805 0.711   1.00 14.46 ?  61  MET   B HG3  1 
ATOM   4822 H HE1  . MET   B 1 61  ? 51.551 -17.182 -2.002  1.00 16.77 ?  61  MET   B HE1  1 
ATOM   4823 H HE2  . MET   B 1 61  ? 51.339 -15.703 -1.461  1.00 16.77 ?  61  MET   B HE2  1 
ATOM   4824 H HE3  . MET   B 1 61  ? 52.797 -16.210 -1.840  1.00 16.77 ?  61  MET   B HE3  1 
ATOM   4825 N N    . GLN   B 1 62  ? 55.569 -14.709 3.416   1.00 12.23 ?  62  GLN   B N    1 
ATOM   4826 C CA   . GLN   B 1 62  ? 55.462 -14.780 4.869   1.00 12.74 ?  62  GLN   B CA   1 
ATOM   4827 C C    . GLN   B 1 62  ? 55.738 -13.428 5.510   1.00 13.23 ?  62  GLN   B C    1 
ATOM   4828 O O    . GLN   B 1 62  ? 55.047 -13.030 6.457   1.00 13.56 ?  62  GLN   B O    1 
ATOM   4829 C CB   . GLN   B 1 62  ? 56.409 -15.838 5.432   1.00 13.14 ?  62  GLN   B CB   1 
ATOM   4830 C CG   . GLN   B 1 62  ? 56.174 -16.096 6.915   1.00 13.32 ?  62  GLN   B CG   1 
ATOM   4831 C CD   . GLN   B 1 62  ? 54.802 -16.688 7.156   1.00 12.97 ?  62  GLN   B CD   1 
ATOM   4832 O OE1  . GLN   B 1 62  ? 54.550 -17.836 6.795   1.00 13.26 ?  62  GLN   B OE1  1 
ATOM   4833 N NE2  . GLN   B 1 62  ? 53.893 -15.900 7.719   1.00 13.45 ?  62  GLN   B NE2  1 
ATOM   4834 H H    . GLN   B 1 62  ? 56.221 -15.158 3.073   1.00 14.65 ?  62  GLN   B H    1 
ATOM   4835 H HA   . GLN   B 1 62  ? 54.557 -15.038 5.097   1.00 15.26 ?  62  GLN   B HA   1 
ATOM   4836 H HB2  . GLN   B 1 62  ? 56.276 -16.675 4.957   1.00 15.75 ?  62  GLN   B HB2  1 
ATOM   4837 H HB3  . GLN   B 1 62  ? 57.327 -15.538 5.320   1.00 15.75 ?  62  GLN   B HB3  1 
ATOM   4838 H HG2  . GLN   B 1 62  ? 56.839 -16.725 7.238   1.00 15.96 ?  62  GLN   B HG2  1 
ATOM   4839 H HG3  . GLN   B 1 62  ? 56.239 -15.260 7.403   1.00 15.96 ?  62  GLN   B HG3  1 
ATOM   4840 H HE21 . GLN   B 1 62  ? 54.104 -15.099 7.949   1.00 16.11 ?  62  GLN   B HE21 1 
ATOM   4841 H HE22 . GLN   B 1 62  ? 53.101 -16.197 7.865   1.00 16.11 ?  62  GLN   B HE22 1 
ATOM   4842 N N    . VAL   B 1 63  ? 56.748 -12.711 5.018   1.00 13.56 ?  63  VAL   B N    1 
ATOM   4843 C CA   . VAL   B 1 63  ? 57.050 -11.395 5.576   1.00 14.72 ?  63  VAL   B CA   1 
ATOM   4844 C C    . VAL   B 1 63  ? 55.858 -10.462 5.394   1.00 13.79 ?  63  VAL   B C    1 
ATOM   4845 O O    . VAL   B 1 63  ? 55.443 -9.753  6.324   1.00 14.52 ?  63  VAL   B O    1 
ATOM   4846 C CB   . VAL   B 1 63  ? 58.341 -10.833 4.950   1.00 16.21 ?  63  VAL   B CB   1 
ATOM   4847 C CG1  . VAL   B 1 63  ? 58.566 -9.391  5.387   1.00 16.81 ?  63  VAL   B CG1  1 
ATOM   4848 C CG2  . VAL   B 1 63  ? 59.528 -11.699 5.342   1.00 16.86 ?  63  VAL   B CG2  1 
ATOM   4849 H H    . VAL   B 1 63  ? 57.262 -12.958 4.369   1.00 16.25 ?  63  VAL   B H    1 
ATOM   4850 H HA   . VAL   B 1 63  ? 57.207 -11.494 6.524   1.00 17.64 ?  63  VAL   B HA   1 
ATOM   4851 H HB   . VAL   B 1 63  ? 58.267 -10.851 3.982   1.00 19.43 ?  63  VAL   B HB   1 
ATOM   4852 H HG11 . VAL   B 1 63  ? 59.483 -9.142  5.189   1.00 20.14 ?  63  VAL   B HG11 1 
ATOM   4853 H HG12 . VAL   B 1 63  ? 57.956 -8.816  4.904   1.00 20.14 ?  63  VAL   B HG12 1 
ATOM   4854 H HG13 . VAL   B 1 63  ? 58.406 -9.325  6.341   1.00 20.14 ?  63  VAL   B HG13 1 
ATOM   4855 H HG21 . VAL   B 1 63  ? 60.338 -11.324 4.958   1.00 20.20 ?  63  VAL   B HG21 1 
ATOM   4856 H HG22 . VAL   B 1 63  ? 59.602 -11.715 6.311   1.00 20.20 ?  63  VAL   B HG22 1 
ATOM   4857 H HG23 . VAL   B 1 63  ? 59.392 -12.599 5.009   1.00 20.20 ?  63  VAL   B HG23 1 
ATOM   4858 N N    . GLU   B 1 64  ? 55.293 -10.447 4.188   1.00 13.38 ?  64  GLU   B N    1 
ATOM   4859 C CA   . GLU   B 1 64  ? 54.132 -9.606  3.911   1.00 13.16 ?  64  GLU   B CA   1 
ATOM   4860 C C    . GLU   B 1 64  ? 52.946 -10.008 4.783   1.00 12.90 ?  64  GLU   B C    1 
ATOM   4861 O O    . GLU   B 1 64  ? 52.196 -9.151  5.281   1.00 13.55 ?  64  GLU   B O    1 
ATOM   4862 C CB   . GLU   B 1 64  ? 53.779 -9.751  2.430   1.00 13.47 ?  64  GLU   B CB   1 
ATOM   4863 C CG   . GLU   B 1 64  ? 52.521 -9.018  1.993   1.00 14.01 ?  64  GLU   B CG   1 
ATOM   4864 C CD   . GLU   B 1 64  ? 51.988 -9.521  0.664   1.00 14.26 ?  64  GLU   B CD   1 
ATOM   4865 O OE1  . GLU   B 1 64  ? 52.163 -10.729 0.357   1.00 14.92 ?  64  GLU   B OE1  1 
ATOM   4866 O OE2  . GLU   B 1 64  ? 51.371 -8.705  -0.061  1.00 14.81 -1 64  GLU   B OE2  1 
ATOM   4867 H H    . GLU   B 1 64  ? 55.560 -10.918 3.513   1.00 16.03 ?  64  GLU   B H    1 
ATOM   4868 H HA   . GLU   B 1 64  ? 54.353 -8.679  4.088   1.00 15.77 ?  64  GLU   B HA   1 
ATOM   4869 H HB2  . GLU   B 1 64  ? 54.514 -9.397  1.897   1.00 16.14 ?  64  GLU   B HB2  1 
ATOM   4870 H HB3  . GLU   B 1 64  ? 53.656 -10.687 2.229   1.00 16.14 ?  64  GLU   B HB3  1 
ATOM   4871 H HG2  . GLU   B 1 64  ? 51.821 -9.139  2.653   1.00 16.79 ?  64  GLU   B HG2  1 
ATOM   4872 H HG3  . GLU   B 1 64  ? 52.722 -8.070  1.899   1.00 16.79 ?  64  GLU   B HG3  1 
ATOM   4873 N N    . SER   B 1 65  ? 52.767 -11.315 4.972   1.00 12.74 ?  65  SER   B N    1 
ATOM   4874 C CA   . SER   B 1 65  ? 51.659 -11.824 5.769   1.00 12.73 ?  65  SER   B CA   1 
ATOM   4875 C C    . SER   B 1 65  ? 51.789 -11.425 7.234   1.00 13.09 ?  65  SER   B C    1 
ATOM   4876 O O    . SER   B 1 65  ? 50.791 -11.065 7.872   1.00 13.09 ?  65  SER   B O    1 
ATOM   4877 C CB   . SER   B 1 65  ? 51.584 -13.346 5.639   1.00 12.78 ?  65  SER   B CB   1 
ATOM   4878 O OG   . SER   B 1 65  ? 51.232 -13.748 4.326   1.00 12.90 ?  65  SER   B OG   1 
ATOM   4879 H H    . SER   B 1 65  ? 53.278 -11.930 4.650   1.00 15.27 ?  65  SER   B H    1 
ATOM   4880 H HA   . SER   B 1 65  ? 50.828 -11.454 5.431   1.00 15.25 ?  65  SER   B HA   1 
ATOM   4881 H HB2  . SER   B 1 65  ? 52.447 -13.722 5.857   1.00 15.31 ?  65  SER   B HB2  1 
ATOM   4882 H HB3  . SER   B 1 65  ? 50.912 -13.678 6.259   1.00 15.31 ?  65  SER   B HB3  1 
ATOM   4883 H HG   . SER   B 1 65  ? 51.796 -13.457 3.772   1.00 15.45 ?  65  SER   B HG   1 
ATOM   4884 N N    . ASP   B 1 66  ? 52.994 -11.530 7.804   1.00 13.16 ?  66  ASP   B N    1 
ATOM   4885 C CA   . ASP   B 1 66  ? 53.179 -11.140 9.198   1.00 13.16 ?  66  ASP   B CA   1 
ATOM   4886 C C    . ASP   B 1 66  ? 52.865 -9.662  9.395   1.00 13.69 ?  66  ASP   B C    1 
ATOM   4887 O O    . ASP   B 1 66  ? 52.283 -9.268  10.414  1.00 14.39 ?  66  ASP   B O    1 
ATOM   4888 C CB   . ASP   B 1 66  ? 54.606 -11.459 9.651   1.00 14.80 ?  66  ASP   B CB   1 
ATOM   4889 C CG   . ASP   B 1 66  ? 54.862 -12.954 9.807   1.00 16.86 ?  66  ASP   B CG   1 
ATOM   4890 O OD1  . ASP   B 1 66  ? 53.908 -13.759 9.723   1.00 17.52 ?  66  ASP   B OD1  1 
ATOM   4891 O OD2  . ASP   B 1 66  ? 56.035 -13.319 10.023  1.00 19.81 -1 66  ASP   B OD2  1 
ATOM   4892 H H    . ASP   B 1 66  ? 53.702 -11.826 7.413   1.00 15.76 ?  66  ASP   B H    1 
ATOM   4893 H HA   . ASP   B 1 66  ? 52.572 -11.644 9.756   1.00 15.77 ?  66  ASP   B HA   1 
ATOM   4894 H HB2  . ASP   B 1 66  ? 55.234 -11.126 8.990   1.00 17.74 ?  66  ASP   B HB2  1 
ATOM   4895 H HB3  . ASP   B 1 66  ? 54.773 -11.027 10.508  1.00 17.74 ?  66  ASP   B HB3  1 
ATOM   4896 N N    . ASP   B 1 67  ? 53.243 -8.823  8.432   1.00 13.63 ?  67  ASP   B N    1 
ATOM   4897 C CA   . ASP   B 1 67  ? 52.899 -7.411  8.522   1.00 14.14 ?  67  ASP   B CA   1 
ATOM   4898 C C    . ASP   B 1 67  ? 51.387 -7.201  8.441   1.00 14.52 ?  67  ASP   B C    1 
ATOM   4899 O O    . ASP   B 1 67  ? 50.826 -6.385  9.184   1.00 14.73 ?  67  ASP   B O    1 
ATOM   4900 C CB   . ASP   B 1 67  ? 53.617 -6.637  7.423   1.00 15.42 ?  67  ASP   B CB   1 
ATOM   4901 C CG   . ASP   B 1 67  ? 53.191 -5.196  7.381   1.00 16.88 ?  67  ASP   B CG   1 
ATOM   4902 O OD1  . ASP   B 1 67  ? 53.666 -4.396  8.220   1.00 18.14 ?  67  ASP   B OD1  1 
ATOM   4903 O OD2  . ASP   B 1 67  ? 52.349 -4.880  6.525   1.00 18.00 -1 67  ASP   B OD2  1 
ATOM   4904 H H    . ASP   B 1 67  ? 53.696 -9.040  7.735   1.00 16.33 ?  67  ASP   B H    1 
ATOM   4905 H HA   . ASP   B 1 67  ? 53.205 -7.061  9.374   1.00 16.94 ?  67  ASP   B HA   1 
ATOM   4906 H HB2  . ASP   B 1 67  ? 54.576 -6.666  7.583   1.00 18.48 ?  67  ASP   B HB2  1 
ATOM   4907 H HB3  . ASP   B 1 67  ? 53.417 -7.046  6.562   1.00 18.48 ?  67  ASP   B HB3  1 
ATOM   4908 N N    . TYR   B 1 68  ? 50.710 -7.928  7.549   1.00 13.63 ?  68  TYR   B N    1 
ATOM   4909 C CA   . TYR   B 1 68  ? 49.252 -7.847  7.478   1.00 14.24 ?  68  TYR   B CA   1 
ATOM   4910 C C    . TYR   B 1 68  ? 48.614 -8.191  8.821   1.00 13.86 ?  68  TYR   B C    1 
ATOM   4911 O O    . TYR   B 1 68  ? 47.681 -7.510  9.269   1.00 14.58 ?  68  TYR   B O    1 
ATOM   4912 C CB   . TYR   B 1 68  ? 48.720 -8.774  6.380   1.00 15.16 ?  68  TYR   B CB   1 
ATOM   4913 C CG   . TYR   B 1 68  ? 47.214 -8.934  6.435   1.00 16.08 ?  68  TYR   B CG   1 
ATOM   4914 C CD1  . TYR   B 1 68  ? 46.627 -9.888  7.261   1.00 17.05 ?  68  TYR   B CD1  1 
ATOM   4915 C CD2  . TYR   B 1 68  ? 46.381 -8.102  5.705   1.00 17.46 ?  68  TYR   B CD2  1 
ATOM   4916 C CE1  . TYR   B 1 68  ? 45.260 -10.017 7.350   1.00 18.64 ?  68  TYR   B CE1  1 
ATOM   4917 C CE2  . TYR   B 1 68  ? 44.997 -8.236  5.778   1.00 18.29 ?  68  TYR   B CE2  1 
ATOM   4918 C CZ   . TYR   B 1 68  ? 44.457 -9.188  6.607   1.00 19.15 ?  68  TYR   B CZ   1 
ATOM   4919 O OH   . TYR   B 1 68  ? 43.089 -9.312  6.695   1.00 20.46 ?  68  TYR   B OH   1 
ATOM   4920 H H    . TYR   B 1 68  ? 51.068 -8.476  6.986   1.00 16.33 ?  68  TYR   B H    1 
ATOM   4921 H HA   . TYR   B 1 68  ? 49.003 -6.939  7.251   1.00 17.06 ?  68  TYR   B HA   1 
ATOM   4922 H HB2  . TYR   B 1 68  ? 48.945 -8.402  5.515   1.00 18.16 ?  68  TYR   B HB2  1 
ATOM   4923 H HB3  . TYR   B 1 68  ? 49.116 -9.651  6.483   1.00 18.16 ?  68  TYR   B HB3  1 
ATOM   4924 H HD1  . TYR   B 1 68  ? 47.169 -10.452 7.768   1.00 20.43 ?  68  TYR   B HD1  1 
ATOM   4925 H HD2  . TYR   B 1 68  ? 46.749 -7.451  5.159   1.00 20.93 ?  68  TYR   B HD2  1 
ATOM   4926 H HE1  . TYR   B 1 68  ? 44.880 -10.673 7.897   1.00 22.34 ?  68  TYR   B HE1  1 
ATOM   4927 H HE2  . TYR   B 1 68  ? 44.440 -7.673  5.287   1.00 21.92 ?  68  TYR   B HE2  1 
ATOM   4928 H HH   . TYR   B 1 68  ? 42.703 -8.759  6.186   1.00 24.53 ?  68  TYR   B HH   1 
ATOM   4929 N N    . ILE   B 1 69  ? 49.094 -9.257  9.469   1.00 13.74 ?  69  ILE   B N    1 
ATOM   4930 C CA   . ILE   B 1 69  ? 48.527 -9.685  10.747  1.00 14.34 ?  69  ILE   B CA   1 
ATOM   4931 C C    . ILE   B 1 69  ? 48.783 -8.641  11.828  1.00 14.22 ?  69  ILE   B C    1 
ATOM   4932 O O    . ILE   B 1 69  ? 47.915 -8.363  12.663  1.00 14.45 ?  69  ILE   B O    1 
ATOM   4933 C CB   . ILE   B 1 69  ? 49.105 -11.058 11.141  1.00 15.37 ?  69  ILE   B CB   1 
ATOM   4934 C CG1  . ILE   B 1 69  ? 48.600 -12.165 10.203  1.00 15.34 ?  69  ILE   B CG1  1 
ATOM   4935 C CG2  . ILE   B 1 69  ? 48.809 -11.363 12.600  1.00 15.82 ?  69  ILE   B CG2  1 
ATOM   4936 C CD1  . ILE   B 1 69  ? 47.134 -12.515 10.360  1.00 15.58 ?  69  ILE   B CD1  1 
ATOM   4937 H H    . ILE   B 1 69  ? 49.742 -9.741  9.193   1.00 16.46 ?  69  ILE   B H    1 
ATOM   4938 H HA   . ILE   B 1 69  ? 47.566 -9.779  10.646  1.00 17.18 ?  69  ILE   B HA   1 
ATOM   4939 H HB   . ILE   B 1 69  ? 50.068 -11.003 11.042  1.00 18.42 ?  69  ILE   B HB   1 
ATOM   4940 H HG12 . ILE   B 1 69  ? 48.739 -11.876 9.286   1.00 18.38 ?  69  ILE   B HG12 1 
ATOM   4941 H HG13 . ILE   B 1 69  ? 49.119 -12.966 10.372  1.00 18.38 ?  69  ILE   B HG13 1 
ATOM   4942 H HG21 . ILE   B 1 69  ? 48.933 -12.313 12.748  1.00 18.96 ?  69  ILE   B HG21 1 
ATOM   4943 H HG22 . ILE   B 1 69  ? 49.423 -10.862 13.162  1.00 18.96 ?  69  ILE   B HG22 1 
ATOM   4944 H HG23 . ILE   B 1 69  ? 47.895 -11.114 12.798  1.00 18.96 ?  69  ILE   B HG23 1 
ATOM   4945 H HD11 . ILE   B 1 69  ? 46.912 -13.208 9.715   1.00 18.67 ?  69  ILE   B HD11 1 
ATOM   4946 H HD12 . ILE   B 1 69  ? 46.983 -12.845 11.259  1.00 18.67 ?  69  ILE   B HD12 1 
ATOM   4947 H HD13 . ILE   B 1 69  ? 46.598 -11.728 10.196  1.00 18.67 ?  69  ILE   B HD13 1 
ATOM   4948 N N    . ALA   B 1 70  ? 49.978 -8.058  11.848  1.00 13.95 ?  70  ALA   B N    1 
ATOM   4949 C CA   . ALA   B 1 70  ? 50.263 -7.024  12.836  1.00 13.97 ?  70  ALA   B CA   1 
ATOM   4950 C C    . ALA   B 1 70  ? 49.272 -5.872  12.726  1.00 14.32 ?  70  ALA   B C    1 
ATOM   4951 O O    . ALA   B 1 70  ? 48.839 -5.315  13.740  1.00 14.68 ?  70  ALA   B O    1 
ATOM   4952 C CB   . ALA   B 1 70  ? 51.691 -6.516  12.654  1.00 14.73 ?  70  ALA   B CB   1 
ATOM   4953 H H    . ALA   B 1 70  ? 50.616 -8.240  11.313  1.00 16.71 ?  70  ALA   B H    1 
ATOM   4954 H HA   . ALA   B 1 70  ? 50.191 -7.404  13.726  1.00 16.74 ?  70  ALA   B HA   1 
ATOM   4955 H HB1  . ALA   B 1 70  ? 51.886 -5.858  13.339  1.00 17.65 ?  70  ALA   B HB1  1 
ATOM   4956 H HB2  . ALA   B 1 70  ? 52.307 -7.265  12.736  1.00 17.65 ?  70  ALA   B HB2  1 
ATOM   4957 H HB3  . ALA   B 1 70  ? 51.778 -6.116  11.774  1.00 17.65 ?  70  ALA   B HB3  1 
ATOM   4958 N N    . THR   B 1 71  ? 48.889 -5.510  11.503  1.00 14.48 ?  71  THR   B N    1 
ATOM   4959 C CA   . THR   B 1 71  ? 47.989 -4.379  11.297  1.00 16.05 ?  71  THR   B CA   1 
ATOM   4960 C C    . THR   B 1 71  ? 46.525 -4.754  11.510  1.00 16.55 ?  71  THR   B C    1 
ATOM   4961 O O    . THR   B 1 71  ? 45.750 -3.951  12.044  1.00 17.68 ?  71  THR   B O    1 
ATOM   4962 C CB   . THR   B 1 71  ? 48.202 -3.808  9.892   1.00 17.89 ?  71  THR   B CB   1 
ATOM   4963 O OG1  . THR   B 1 71  ? 49.524 -3.264  9.793   1.00 19.94 ?  71  THR   B OG1  1 
ATOM   4964 C CG2  . THR   B 1 71  ? 47.176 -2.723  9.571   1.00 19.05 ?  71  THR   B CG2  1 
ATOM   4965 H H    . THR   B 1 71  ? 49.132 -5.904  10.784  1.00 17.35 ?  71  THR   B H    1 
ATOM   4966 H HA   . THR   B 1 71  ? 48.210 -3.680  11.935  1.00 19.24 ?  71  THR   B HA   1 
ATOM   4967 H HB   . THR   B 1 71  ? 48.110 -4.514  9.238   1.00 21.44 ?  71  THR   B HB   1 
ATOM   4968 H HG1  . THR   B 1 71  ? 49.646 -2.928  9.029   1.00 23.91 ?  71  THR   B HG1  1 
ATOM   4969 H HG21 . THR   B 1 71  ? 47.474 -2.200  8.808   1.00 22.83 ?  71  THR   B HG21 1 
ATOM   4970 H HG22 . THR   B 1 71  ? 46.320 -3.123  9.361   1.00 22.83 ?  71  THR   B HG22 1 
ATOM   4971 H HG23 . THR   B 1 71  ? 47.072 -2.128  10.332  1.00 22.83 ?  71  THR   B HG23 1 
ATOM   4972 N N    . ASN   B 1 72  ? 46.130 -5.962  11.111  1.00 16.22 ?  72  ASN   B N    1 
ATOM   4973 C CA   . ASN   B 1 72  ? 44.727 -6.323  10.989  1.00 16.82 ?  72  ASN   B CA   1 
ATOM   4974 C C    . ASN   B 1 72  ? 44.261 -7.424  11.931  1.00 17.27 ?  72  ASN   B C    1 
ATOM   4975 O O    . ASN   B 1 72  ? 43.046 -7.582  12.107  1.00 18.06 ?  72  ASN   B O    1 
ATOM   4976 C CB   . ASN   B 1 72  ? 44.418 -6.744  9.543   1.00 17.35 ?  72  ASN   B CB   1 
ATOM   4977 C CG   . ASN   B 1 72  ? 44.704 -5.642  8.548   1.00 18.42 ?  72  ASN   B CG   1 
ATOM   4978 O OD1  . ASN   B 1 72  ? 45.718 -5.661  7.842   1.00 19.67 ?  72  ASN   B OD1  1 
ATOM   4979 N ND2  . ASN   B 1 72  ? 43.831 -4.653  8.512   1.00 19.91 ?  72  ASN   B ND2  1 
ATOM   4980 H H    . ASN   B 1 72  ? 46.674 -6.603  10.906  1.00 19.44 ?  72  ASN   B H    1 
ATOM   4981 H HA   . ASN   B 1 72  ? 44.196 -5.537  11.178  1.00 20.15 ?  72  ASN   B HA   1 
ATOM   4982 H HB2  . ASN   B 1 72  ? 44.970 -7.507  9.309   1.00 20.79 ?  72  ASN   B HB2  1 
ATOM   4983 H HB3  . ASN   B 1 72  ? 43.481 -6.973  9.473   1.00 20.79 ?  72  ASN   B HB3  1 
ATOM   4984 H HD21 . ASN   B 1 72  ? 43.941 -3.996  7.964   1.00 23.87 ?  72  ASN   B HD21 1 
ATOM   4985 H HD22 . ASN   B 1 72  ? 43.135 -4.670  9.020   1.00 23.87 ?  72  ASN   B HD22 1 
ATOM   4986 N N    . GLY   B 1 73  ? 45.165 -8.188  12.531  1.00 16.16 ?  73  GLY   B N    1 
ATOM   4987 C CA   . GLY   B 1 73  ? 44.765 -9.330  13.316  1.00 15.77 ?  73  GLY   B CA   1 
ATOM   4988 C C    . GLY   B 1 73  ? 44.411 -10.512 12.441  1.00 14.44 ?  73  GLY   B C    1 
ATOM   4989 O O    . GLY   B 1 73  ? 44.393 -10.419 11.210  1.00 14.51 ?  73  GLY   B O    1 
ATOM   4990 H H    . GLY   B 1 73  ? 46.016 -8.064  12.493  1.00 19.37 ?  73  GLY   B H    1 
ATOM   4991 H HA2  . GLY   B 1 73  ? 45.487 -9.586  13.910  1.00 18.90 ?  73  GLY   B HA2  1 
ATOM   4992 H HA3  . GLY   B 1 73  ? 43.988 -9.101  13.852  1.00 18.90 ?  73  GLY   B HA3  1 
ATOM   4993 N N    . PRO   B 1 74  ? 44.117 -11.648 13.070  1.00 14.68 ?  74  PRO   B N    1 
ATOM   4994 C CA   . PRO   B 1 74  ? 43.864 -12.875 12.313  1.00 14.21 ?  74  PRO   B CA   1 
ATOM   4995 C C    . PRO   B 1 74  ? 42.562 -12.813 11.530  1.00 13.63 ?  74  PRO   B C    1 
ATOM   4996 O O    . PRO   B 1 74  ? 41.626 -12.074 11.856  1.00 14.87 ?  74  PRO   B O    1 
ATOM   4997 C CB   . PRO   B 1 74  ? 43.797 -13.950 13.405  1.00 14.95 ?  74  PRO   B CB   1 
ATOM   4998 C CG   . PRO   B 1 74  ? 43.343 -13.210 14.623  1.00 16.19 ?  74  PRO   B CG   1 
ATOM   4999 C CD   . PRO   B 1 74  ? 44.011 -11.867 14.523  1.00 15.70 ?  74  PRO   B CD   1 
ATOM   5000 H HA   . PRO   B 1 74  ? 44.604 -13.063 11.709  1.00 17.03 ?  74  PRO   B HA   1 
ATOM   5001 H HB2  . PRO   B 1 74  ? 43.156 -14.633 13.151  1.00 17.91 ?  74  PRO   B HB2  1 
ATOM   5002 H HB3  . PRO   B 1 74  ? 44.677 -14.335 13.539  1.00 17.91 ?  74  PRO   B HB3  1 
ATOM   5003 H HG2  . PRO   B 1 74  ? 42.377 -13.117 14.608  1.00 19.40 ?  74  PRO   B HG2  1 
ATOM   5004 H HG3  . PRO   B 1 74  ? 43.632 -13.681 15.419  1.00 19.40 ?  74  PRO   B HG3  1 
ATOM   5005 H HD2  . PRO   B 1 74  ? 43.457 -11.183 14.935  1.00 18.81 ?  74  PRO   B HD2  1 
ATOM   5006 H HD3  . PRO   B 1 74  ? 44.894 -11.897 14.922  1.00 18.81 ?  74  PRO   B HD3  1 
ATOM   5007 N N    . LEU   B 1 75  ? 42.527 -13.610 10.467  1.00 12.89 ?  75  LEU   B N    1 
ATOM   5008 C CA   . LEU   B 1 75  ? 41.312 -13.826 9.702   1.00 12.99 ?  75  LEU   B CA   1 
ATOM   5009 C C    . LEU   B 1 75  ? 40.343 -14.693 10.502  1.00 13.32 ?  75  LEU   B C    1 
ATOM   5010 O O    . LEU   B 1 75  ? 40.686 -15.250 11.546  1.00 14.40 ?  75  LEU   B O    1 
ATOM   5011 C CB   . LEU   B 1 75  ? 41.636 -14.533 8.384   1.00 13.25 ?  75  LEU   B CB   1 
ATOM   5012 C CG   . LEU   B 1 75  ? 42.477 -13.777 7.351   1.00 14.96 ?  75  LEU   B CG   1 
ATOM   5013 C CD1  . LEU   B 1 75  ? 42.643 -14.592 6.068   1.00 16.22 ?  75  LEU   B CD1  1 
ATOM   5014 C CD2  . LEU   B 1 75  ? 41.890 -12.425 7.043   1.00 19.05 ?  75  LEU   B CD2  1 
ATOM   5015 H H    . LEU   B 1 75  ? 43.204 -14.048 10.166  1.00 15.44 ?  75  LEU   B H    1 
ATOM   5016 H HA   . LEU   B 1 75  ? 40.885 -12.980 9.506   1.00 15.56 ?  75  LEU   B HA   1 
ATOM   5017 H HB2  . LEU   B 1 75  ? 42.118 -15.352 8.593   1.00 15.87 ?  75  LEU   B HB2  1 
ATOM   5018 H HB3  . LEU   B 1 75  ? 40.799 -14.766 7.950   1.00 15.87 ?  75  LEU   B HB3  1 
ATOM   5019 H HG   . LEU   B 1 75  ? 43.361 -13.634 7.721   1.00 17.92 ?  75  LEU   B HG   1 
ATOM   5020 H HD11 . LEU   B 1 75  ? 43.184 -14.083 5.438   1.00 19.44 ?  75  LEU   B HD11 1 
ATOM   5021 H HD12 . LEU   B 1 75  ? 43.085 -15.429 6.276   1.00 19.44 ?  75  LEU   B HD12 1 
ATOM   5022 H HD13 . LEU   B 1 75  ? 41.770 -14.764 5.683   1.00 19.44 ?  75  LEU   B HD13 1 
ATOM   5023 H HD21 . LEU   B 1 75  ? 42.378 -12.030 6.306   1.00 22.83 ?  75  LEU   B HD21 1 
ATOM   5024 H HD22 . LEU   B 1 75  ? 40.957 -12.535 6.805   1.00 22.83 ?  75  LEU   B HD22 1 
ATOM   5025 H HD23 . LEU   B 1 75  ? 41.966 -11.862 7.831   1.00 22.83 ?  75  LEU   B HD23 1 
ATOM   5026 N N    . LYS   B 1 76  ? 39.114 -14.798 9.993   1.00 14.87 ?  76  LYS   B N    1 
ATOM   5027 C CA   . LYS   B 1 76  ? 38.127 -15.757 10.471  1.00 16.27 ?  76  LYS   B CA   1 
ATOM   5028 C C    . LYS   B 1 76  ? 38.213 -17.020 9.620   1.00 14.35 ?  76  LYS   B C    1 
ATOM   5029 O O    . LYS   B 1 76  ? 38.488 -16.951 8.421   1.00 14.05 ?  76  LYS   B O    1 
ATOM   5030 C CB   . LYS   B 1 76  ? 36.710 -15.187 10.300  1.00 19.03 ?  76  LYS   B CB   1 
ATOM   5031 C CG   . LYS   B 1 76  ? 36.448 -13.794 10.894  1.00 20.90 ?  76  LYS   B CG   1 
ATOM   5032 C CD   . LYS   B 1 76  ? 35.026 -13.290 10.577  1.00 21.99 ?  76  LYS   B CD   1 
ATOM   5033 C CE   . LYS   B 1 76  ? 34.780 -11.898 11.145  1.00 24.46 ?  76  LYS   B CE   1 
ATOM   5034 N NZ   . LYS   B 1 76  ? 33.482 -11.308 10.709  1.00 25.00 ?  76  LYS   B NZ   1 
ATOM   5035 H H    . LYS   B 1 76  ? 38.824 -14.317 9.343   1.00 17.82 ?  76  LYS   B H    1 
ATOM   5036 H HA   . LYS   B 1 76  ? 38.284 -15.983 11.402  1.00 19.50 ?  76  LYS   B HA   1 
ATOM   5037 H HB2  . LYS   B 1 76  ? 36.520 -15.136 9.350   1.00 22.81 ?  76  LYS   B HB2  1 
ATOM   5038 H HB3  . LYS   B 1 76  ? 36.086 -15.800 10.718  1.00 22.81 ?  76  LYS   B HB3  1 
ATOM   5039 H HG2  . LYS   B 1 76  ? 36.551 -13.836 11.857  1.00 25.05 ?  76  LYS   B HG2  1 
ATOM   5040 H HG3  . LYS   B 1 76  ? 37.086 -13.165 10.518  1.00 25.05 ?  76  LYS   B HG3  1 
ATOM   5041 H HD2  . LYS   B 1 76  ? 34.911 -13.252 9.614   1.00 26.36 ?  76  LYS   B HD2  1 
ATOM   5042 H HD3  . LYS   B 1 76  ? 34.381 -13.899 10.968  1.00 26.36 ?  76  LYS   B HD3  1 
ATOM   5043 H HE2  . LYS   B 1 76  ? 34.776 -11.951 12.113  1.00 29.33 ?  76  LYS   B HE2  1 
ATOM   5044 H HE3  . LYS   B 1 76  ? 35.491 -11.308 10.849  1.00 29.33 ?  76  LYS   B HE3  1 
ATOM   5045 H HZ1  . LYS   B 1 76  ? 33.381 -10.496 11.065  1.00 29.98 ?  76  LYS   B HZ1  1 
ATOM   5046 H HZ2  . LYS   B 1 76  ? 33.459 -11.237 9.822   1.00 29.98 ?  76  LYS   B HZ2  1 
ATOM   5047 H HZ3  . LYS   B 1 76  ? 32.806 -11.823 10.975  1.00 29.98 ?  76  LYS   B HZ3  1 
ATOM   5048 N N    . VAL   B 1 77  ? 37.960 -18.181 10.238  1.00 14.80 ?  77  VAL   B N    1 
ATOM   5049 C CA   . VAL   B 1 77  ? 37.751 -19.388 9.445   1.00 15.13 ?  77  VAL   B CA   1 
ATOM   5050 C C    . VAL   B 1 77  ? 36.563 -19.151 8.527   1.00 13.91 ?  77  VAL   B C    1 
ATOM   5051 O O    . VAL   B 1 77  ? 35.496 -18.707 8.971   1.00 14.03 ?  77  VAL   B O    1 
ATOM   5052 C CB   . VAL   B 1 77  ? 37.550 -20.619 10.343  1.00 16.90 ?  77  VAL   B CB   1 
ATOM   5053 C CG1  . VAL   B 1 77  ? 37.277 -21.849 9.485   1.00 17.58 ?  77  VAL   B CG1  1 
ATOM   5054 C CG2  . VAL   B 1 77  ? 38.774 -20.844 11.234  1.00 18.36 ?  77  VAL   B CG2  1 
ATOM   5055 H H    . VAL   B 1 77  ? 37.910 -18.293 11.089  1.00 17.73 ?  77  VAL   B H    1 
ATOM   5056 H HA   . VAL   B 1 77  ? 38.528 -19.543 8.890   1.00 18.13 ?  77  VAL   B HA   1 
ATOM   5057 H HB   . VAL   B 1 77  ? 36.777 -20.475 10.914  1.00 20.25 ?  77  VAL   B HB   1 
ATOM   5058 H HG11 . VAL   B 1 77  ? 37.335 -22.640 10.043  1.00 21.07 ?  77  VAL   B HG11 1 
ATOM   5059 H HG12 . VAL   B 1 77  ? 36.384 -21.782 9.105   1.00 21.07 ?  77  VAL   B HG12 1 
ATOM   5060 H HG13 . VAL   B 1 77  ? 37.936 -21.893 8.777   1.00 21.07 ?  77  VAL   B HG13 1 
ATOM   5061 H HG21 . VAL   B 1 77  ? 38.639 -21.651 11.753  1.00 22.01 ?  77  VAL   B HG21 1 
ATOM   5062 H HG22 . VAL   B 1 77  ? 39.556 -20.935 10.670  1.00 22.01 ?  77  VAL   B HG22 1 
ATOM   5063 H HG23 . VAL   B 1 77  ? 38.875 -20.081 11.824  1.00 22.01 ?  77  VAL   B HG23 1 
ATOM   5064 N N    . GLY   B 1 78  ? 36.747 -19.425 7.240   1.00 13.20 ?  78  GLY   B N    1 
ATOM   5065 C CA   . GLY   B 1 78  ? 35.770 -19.097 6.226   1.00 12.95 ?  78  GLY   B CA   1 
ATOM   5066 C C    . GLY   B 1 78  ? 36.021 -17.781 5.527   1.00 12.49 ?  78  GLY   B C    1 
ATOM   5067 O O    . GLY   B 1 78  ? 35.338 -17.488 4.539   1.00 12.92 ?  78  GLY   B O    1 
ATOM   5068 H H    . GLY   B 1 78  ? 37.445 -19.814 6.925   1.00 15.81 ?  78  GLY   B H    1 
ATOM   5069 H HA2  . GLY   B 1 78  ? 35.761 -19.793 5.553   1.00 15.51 ?  78  GLY   B HA2  1 
ATOM   5070 H HA3  . GLY   B 1 78  ? 34.889 -19.055 6.631   1.00 15.51 ?  78  GLY   B HA3  1 
ATOM   5071 N N    . GLY   B 1 79  ? 36.971 -16.982 6.017   1.00 12.87 ?  79  GLY   B N    1 
ATOM   5072 C CA   . GLY   B 1 79  ? 37.272 -15.687 5.443   1.00 12.86 ?  79  GLY   B CA   1 
ATOM   5073 C C    . GLY   B 1 79  ? 38.513 -15.700 4.561   1.00 11.87 ?  79  GLY   B C    1 
ATOM   5074 O O    . GLY   B 1 79  ? 39.125 -16.733 4.305   1.00 12.05 ?  79  GLY   B O    1 
ATOM   5075 H H    . GLY   B 1 79  ? 37.469 -17.180 6.684   1.00 15.42 ?  79  GLY   B H    1 
ATOM   5076 H HA2  . GLY   B 1 79  ? 36.524 -15.388 4.902   1.00 15.40 ?  79  GLY   B HA2  1 
ATOM   5077 H HA3  . GLY   B 1 79  ? 37.418 -15.047 6.150   1.00 15.40 ?  79  GLY   B HA3  1 
ATOM   5078 N N    . SER   B 1 80  ? 38.878 -14.505 4.090   1.00 11.93 ?  80  SER   B N    1 
ATOM   5079 C CA   . SER   B 1 80  ? 39.986 -14.369 3.156   1.00 11.84 ?  80  SER   B CA   1 
ATOM   5080 C C    . SER   B 1 80  ? 40.567 -12.963 3.222   1.00 11.84 ?  80  SER   B C    1 
ATOM   5081 O O    . SER   B 1 80  ? 39.945 -12.027 3.730   1.00 12.85 ?  80  SER   B O    1 
ATOM   5082 C CB   . SER   B 1 80  ? 39.542 -14.655 1.716   1.00 12.38 ?  80  SER   B CB   1 
ATOM   5083 O OG   . SER   B 1 80  ? 38.711 -13.617 1.217   1.00 13.61 ?  80  SER   B OG   1 
ATOM   5084 H H    . SER   B 1 80  ? 38.497 -13.765 4.291   1.00 14.29 ?  80  SER   B H    1 
ATOM   5085 H HA   . SER   B 1 80  ? 40.677 -14.999 3.396   1.00 14.19 ?  80  SER   B HA   1 
ATOM   5086 H HB2  . SER   B 1 80  ? 40.326 -14.728 1.146   1.00 14.83 ?  80  SER   B HB2  1 
ATOM   5087 H HB3  . SER   B 1 80  ? 39.047 -15.494 1.696   1.00 14.83 ?  80  SER   B HB3  1 
ATOM   5088 H HG   . SER   B 1 80  ? 38.022 -13.550 1.698   1.00 16.30 ?  80  SER   B HG   1 
ATOM   5089 N N    . CYS   B 1 81  ? 41.753 -12.818 2.636   1.00 11.50 ?  81  CYS   B N    1 
ATOM   5090 C CA   . CYS   B 1 81  ? 42.301 -11.504 2.330   1.00 11.57 ?  81  CYS   B CA   1 
ATOM   5091 C C    . CYS   B 1 81  ? 43.076 -11.589 1.024   1.00 11.11 ?  81  CYS   B C    1 
ATOM   5092 O O    . CYS   B 1 81  ? 43.589 -12.651 0.652   1.00 11.98 ?  81  CYS   B O    1 
ATOM   5093 C CB   . CYS   B 1 81  ? 43.190 -10.949 3.454   1.00 12.66 ?  81  CYS   B CB   1 
ATOM   5094 S SG   . CYS   B 1 81  ? 44.704 -11.887 3.714   1.00 13.09 ?  81  CYS   B SG   1 
ATOM   5095 H H    . CYS   B 1 81  ? 42.264 -13.471 2.396   1.00 13.78 ?  81  CYS   B H    1 
ATOM   5096 H HA   . CYS   B 1 81  ? 41.567 -10.880 2.198   1.00 13.86 ?  81  CYS   B HA   1 
ATOM   5097 H HB2  . CYS   B 1 81  ? 43.436 -10.038 3.236   1.00 15.17 ?  81  CYS   B HB2  1 
ATOM   5098 H HB3  . CYS   B 1 81  ? 42.680 -10.960 4.283   1.00 15.17 ?  81  CYS   B HB3  1 
ATOM   5099 H HG   . CYS   B 1 81  ? 45.324 -11.384 4.617   1.00 15.69 ?  81  CYS   B HG   1 
ATOM   5100 N N    . VAL   B 1 82  ? 43.185 -10.447 0.350   1.00 11.39 ?  82  VAL   B N    1 
ATOM   5101 C CA   . VAL   B 1 82  ? 43.954 -10.322 -0.884  1.00 11.49 ?  82  VAL   B CA   1 
ATOM   5102 C C    . VAL   B 1 82  ? 45.295 -9.683  -0.557  1.00 11.79 ?  82  VAL   B C    1 
ATOM   5103 O O    . VAL   B 1 82  ? 45.344 -8.568  -0.019  1.00 13.04 ?  82  VAL   B O    1 
ATOM   5104 C CB   . VAL   B 1 82  ? 43.209 -9.481  -1.933  1.00 12.64 ?  82  VAL   B CB   1 
ATOM   5105 C CG1  . VAL   B 1 82  ? 44.063 -9.322  -3.186  1.00 13.91 ?  82  VAL   B CG1  1 
ATOM   5106 C CG2  . VAL   B 1 82  ? 41.855 -10.087 -2.262  1.00 13.60 ?  82  VAL   B CG2  1 
ATOM   5107 H H    . VAL   B 1 82  ? 42.813 -9.706  0.591   1.00 13.65 ?  82  VAL   B H    1 
ATOM   5108 H HA   . VAL   B 1 82  ? 44.116 -11.204 -1.255  1.00 13.76 ?  82  VAL   B HA   1 
ATOM   5109 H HB   . VAL   B 1 82  ? 43.054 -8.599  -1.569  1.00 15.14 ?  82  VAL   B HB   1 
ATOM   5110 H HG11 . VAL   B 1 82  ? 43.502 -9.003  -3.909  1.00 16.66 ?  82  VAL   B HG11 1 
ATOM   5111 H HG12 . VAL   B 1 82  ? 44.767 -8.675  -3.008  1.00 16.66 ?  82  VAL   B HG12 1 
ATOM   5112 H HG13 . VAL   B 1 82  ? 44.450 -10.178 -3.418  1.00 16.66 ?  82  VAL   B HG13 1 
ATOM   5113 H HG21 . VAL   B 1 82  ? 41.422 -9.555  -2.949  1.00 16.30 ?  82  VAL   B HG21 1 
ATOM   5114 H HG22 . VAL   B 1 82  ? 41.977 -10.997 -2.584  1.00 16.30 ?  82  VAL   B HG22 1 
ATOM   5115 H HG23 . VAL   B 1 82  ? 41.304 -10.098 -1.461  1.00 16.30 ?  82  VAL   B HG23 1 
ATOM   5116 N N    . LEU   B 1 83  ? 46.379 -10.369 -0.915  1.00 11.51 ?  83  LEU   B N    1 
ATOM   5117 C CA   . LEU   B 1 83  ? 47.734 -9.849  -0.795  1.00 11.40 ?  83  LEU   B CA   1 
ATOM   5118 C C    . LEU   B 1 83  ? 48.434 -9.989  -2.146  1.00 11.39 ?  83  LEU   B C    1 
ATOM   5119 O O    . LEU   B 1 83  ? 47.835 -10.408 -3.139  1.00 11.34 ?  83  LEU   B O    1 
ATOM   5120 C CB   . LEU   B 1 83  ? 48.483 -10.524 0.364   1.00 11.96 ?  83  LEU   B CB   1 
ATOM   5121 C CG   . LEU   B 1 83  ? 47.953 -10.166 1.757   1.00 13.38 ?  83  LEU   B CG   1 
ATOM   5122 C CD1  . LEU   B 1 83  ? 48.571 -11.046 2.825   1.00 13.79 ?  83  LEU   B CD1  1 
ATOM   5123 C CD2  . LEU   B 1 83  ? 48.167 -8.686  2.098   1.00 14.19 ?  83  LEU   B CD2  1 
ATOM   5124 H H    . LEU   B 1 83  ? 46.344 -11.170 -1.239  1.00 13.79 ?  83  LEU   B H    1 
ATOM   5125 H HA   . LEU   B 1 83  ? 47.678 -8.908  -0.599  1.00 13.65 ?  83  LEU   B HA   1 
ATOM   5126 H HB2  . LEU   B 1 83  ? 48.420 -11.484 0.262   1.00 14.32 ?  83  LEU   B HB2  1 
ATOM   5127 H HB3  . LEU   B 1 83  ? 49.414 -10.250 0.325   1.00 14.32 ?  83  LEU   B HB3  1 
ATOM   5128 H HG   . LEU   B 1 83  ? 46.998 -10.327 1.768   1.00 16.03 ?  83  LEU   B HG   1 
ATOM   5129 H HD11 . LEU   B 1 83  ? 48.206 -10.797 3.691   1.00 16.52 ?  83  LEU   B HD11 1 
ATOM   5130 H HD12 . LEU   B 1 83  ? 48.353 -11.974 2.634   1.00 16.52 ?  83  LEU   B HD12 1 
ATOM   5131 H HD13 . LEU   B 1 83  ? 49.531 -10.925 2.823   1.00 16.52 ?  83  LEU   B HD13 1 
ATOM   5132 H HD21 . LEU   B 1 83  ? 47.929 -8.537  3.028   1.00 17.00 ?  83  LEU   B HD21 1 
ATOM   5133 H HD22 . LEU   B 1 83  ? 49.100 -8.459  1.957   1.00 17.00 ?  83  LEU   B HD22 1 
ATOM   5134 H HD23 . LEU   B 1 83  ? 47.605 -8.142  1.524   1.00 17.00 ?  83  LEU   B HD23 1 
ATOM   5135 N N    . SER   B 1 84  ? 49.709 -9.615  -2.198  1.00 12.52 ?  84  SER   B N    1 
ATOM   5136 C CA   . SER   B 1 84  ? 50.449 -9.730  -3.445  1.00 12.54 ?  84  SER   B CA   1 
ATOM   5137 C C    . SER   B 1 84  ? 50.605 -11.189 -3.855  1.00 12.18 ?  84  SER   B C    1 
ATOM   5138 O O    . SER   B 1 84  ? 50.715 -12.086 -3.019  1.00 12.04 ?  84  SER   B O    1 
ATOM   5139 C CB   . SER   B 1 84  ? 51.846 -9.131  -3.290  1.00 14.48 ?  84  SER   B CB   1 
ATOM   5140 O OG   . SER   B 1 84  ? 52.589 -9.330  -4.475  1.00 16.24 ?  84  SER   B OG   1 
ATOM   5141 H H    . SER   B 1 84  ? 50.152 -9.281  -1.541  1.00 15.00 ?  84  SER   B H    1 
ATOM   5142 H HA   . SER   B 1 84  ? 49.986 -9.258  -4.153  1.00 15.02 ?  84  SER   B HA   1 
ATOM   5143 H HB2  . SER   B 1 84  ? 51.766 -8.176  -3.112  1.00 17.34 ?  84  SER   B HB2  1 
ATOM   5144 H HB3  . SER   B 1 84  ? 52.304 -9.565  -2.554  1.00 17.34 ?  84  SER   B HB3  1 
ATOM   5145 H HG   . SER   B 1 84  ? 53.358 -8.985  -4.394  1.00 19.46 ?  84  SER   B HG   1 
ATOM   5146 N N    . GLY   B 1 85  ? 50.664 -11.414 -5.163  1.00 12.87 ?  85  GLY   B N    1 
ATOM   5147 C CA   . GLY   B 1 85  ? 51.014 -12.706 -5.703  1.00 13.64 ?  85  GLY   B CA   1 
ATOM   5148 C C    . GLY   B 1 85  ? 52.485 -12.894 -6.005  1.00 12.87 ?  85  GLY   B C    1 
ATOM   5149 O O    . GLY   B 1 85  ? 52.868 -13.969 -6.466  1.00 13.27 ?  85  GLY   B O    1 
ATOM   5150 H H    . GLY   B 1 85  ? 50.517 -10.822 -5.760  1.00 15.42 ?  85  GLY   B H    1 
ATOM   5151 H HA2  . GLY   B 1 85  ? 50.748 -13.399 -5.074  1.00 16.34 ?  85  GLY   B HA2  1 
ATOM   5152 H HA3  . GLY   B 1 85  ? 50.523 -12.850 -6.525  1.00 16.34 ?  85  GLY   B HA3  1 
ATOM   5153 N N    . HIS   B 1 86  ? 53.331 -11.891 -5.775  1.00 12.59 ?  86  HIS   B N    1 
ATOM   5154 C CA   . HIS   B 1 86  ? 54.792 -12.056 -5.854  1.00 12.61 ?  86  HIS   B CA   1 
ATOM   5155 C C    . HIS   B 1 86  ? 55.167 -12.566 -7.244  1.00 12.65 ?  86  HIS   B C    1 
ATOM   5156 O O    . HIS   B 1 86  ? 54.780 -11.948 -8.248  1.00 13.72 ?  86  HIS   B O    1 
ATOM   5157 C CB   . HIS   B 1 86  ? 55.260 -12.905 -4.677  1.00 13.26 ?  86  HIS   B CB   1 
ATOM   5158 C CG   . HIS   B 1 86  ? 54.957 -12.290 -3.352  1.00 13.41 ?  86  HIS   B CG   1 
ATOM   5159 N ND1  . HIS   B 1 86  ? 55.793 -11.377 -2.746  1.00 14.47 ?  86  HIS   B ND1  1 
ATOM   5160 C CD2  . HIS   B 1 86  ? 53.888 -12.432 -2.533  1.00 13.54 ?  86  HIS   B CD2  1 
ATOM   5161 C CE1  . HIS   B 1 86  ? 55.245 -10.979 -1.611  1.00 14.48 ?  86  HIS   B CE1  1 
ATOM   5162 N NE2  . HIS   B 1 86  ? 54.092 -11.607 -1.456  1.00 13.88 ?  86  HIS   B NE2  1 
ATOM   5163 H H    . HIS   B 1 86  ? 53.083 -11.093 -5.584  1.00 15.08 ?  86  HIS   B H    1 
ATOM   5164 H HA   . HIS   B 1 86  ? 55.201 -11.183 -5.750  1.00 15.10 ?  86  HIS   B HA   1 
ATOM   5165 H HB2  . HIS   B 1 86  ? 54.819 -13.769 -4.717  1.00 15.89 ?  86  HIS   B HB2  1 
ATOM   5166 H HB3  . HIS   B 1 86  ? 56.220 -13.023 -4.734  1.00 15.89 ?  86  HIS   B HB3  1 
ATOM   5167 H HD2  . HIS   B 1 86  ? 53.142 -12.977 -2.675  1.00 16.22 ?  86  HIS   B HD2  1 
ATOM   5168 H HE1  . HIS   B 1 86  ? 55.620 -10.378 -1.012  1.00 17.35 ?  86  HIS   B HE1  1 
ATOM   5169 H HE2  . HIS   B 1 86  ? 53.558 -11.518 -0.783  1.00 16.63 ?  86  HIS   B HE2  1 
ATOM   5170 N N    . ASN   B 1 87  ? 55.936 -13.648 -7.351  1.00 13.38 ?  87  ASN   B N    1 
ATOM   5171 C CA   . ASN   B 1 87  ? 56.339 -14.224 -8.625  1.00 14.17 ?  87  ASN   B CA   1 
ATOM   5172 C C    . ASN   B 1 87  ? 55.361 -15.273 -9.125  1.00 14.06 ?  87  ASN   B C    1 
ATOM   5173 O O    . ASN   B 1 87  ? 55.686 -15.995 -10.074 1.00 15.82 ?  87  ASN   B O    1 
ATOM   5174 C CB   . ASN   B 1 87  ? 57.736 -14.848 -8.504  1.00 16.26 ?  87  ASN   B CB   1 
ATOM   5175 C CG   . ASN   B 1 87  ? 57.795 -15.958 -7.461  1.00 17.27 ?  87  ASN   B CG   1 
ATOM   5176 O OD1  . ASN   B 1 87  ? 57.160 -15.872 -6.408  1.00 16.28 ?  87  ASN   B OD1  1 
ATOM   5177 N ND2  . ASN   B 1 87  ? 58.543 -17.022 -7.764  1.00 19.63 ?  87  ASN   B ND2  1 
ATOM   5178 H H    . ASN   B 1 87  ? 56.244 -14.078 -6.675  1.00 16.03 ?  87  ASN   B H    1 
ATOM   5179 H HA   . ASN   B 1 87  ? 56.383 -13.522 -9.290  1.00 16.98 ?  87  ASN   B HA   1 
ATOM   5180 H HB2  . ASN   B 1 87  ? 57.987 -15.226 -9.361  1.00 19.49 ?  87  ASN   B HB2  1 
ATOM   5181 H HB3  . ASN   B 1 87  ? 58.365 -14.160 -8.245  1.00 19.49 ?  87  ASN   B HB3  1 
ATOM   5182 H HD21 . ASN   B 1 87  ? 58.610 -17.674 -7.210  1.00 23.53 ?  87  ASN   B HD21 1 
ATOM   5183 H HD22 . ASN   B 1 87  ? 58.965 -17.050 -8.515  1.00 23.53 ?  87  ASN   B HD22 1 
ATOM   5184 N N    . LEU   B 1 88  ? 54.178 -15.373 -8.513  1.00 12.73 ?  88  LEU   B N    1 
ATOM   5185 C CA   . LEU   B 1 88  ? 53.200 -16.406 -8.841  1.00 12.88 ?  88  LEU   B CA   1 
ATOM   5186 C C    . LEU   B 1 88  ? 51.970 -15.888 -9.562  1.00 12.55 ?  88  LEU   B C    1 
ATOM   5187 O O    . LEU   B 1 88  ? 51.373 -16.630 -10.352 1.00 14.19 ?  88  LEU   B O    1 
ATOM   5188 C CB   . LEU   B 1 88  ? 52.727 -17.092 -7.557  1.00 14.00 ?  88  LEU   B CB   1 
ATOM   5189 C CG   . LEU   B 1 88  ? 53.851 -17.737 -6.760  1.00 16.90 ?  88  LEU   B CG   1 
ATOM   5190 C CD1  . LEU   B 1 88  ? 53.353 -18.133 -5.381  1.00 18.53 ?  88  LEU   B CD1  1 
ATOM   5191 C CD2  . LEU   B 1 88  ? 54.390 -18.936 -7.517  1.00 20.12 ?  88  LEU   B CD2  1 
ATOM   5192 H H    . LEU   B 1 88  ? 53.913 -14.842 -7.883  1.00 15.25 ?  88  LEU   B H    1 
ATOM   5193 H HA   . LEU   B 1 88  ? 53.617 -17.070 -9.402  1.00 15.43 ?  88  LEU   B HA   1 
ATOM   5194 H HB2  . LEU   B 1 88  ? 52.296 -16.437 -6.987  1.00 16.77 ?  88  LEU   B HB2  1 
ATOM   5195 H HB3  . LEU   B 1 88  ? 52.091 -17.790 -7.793  1.00 16.77 ?  88  LEU   B HB3  1 
ATOM   5196 H HG   . LEU   B 1 88  ? 54.571 -17.099 -6.650  1.00 20.25 ?  88  LEU   B HG   1 
ATOM   5197 H HD11 . LEU   B 1 88  ? 54.026 -18.678 -4.947  1.00 22.21 ?  88  LEU   B HD11 1 
ATOM   5198 H HD12 . LEU   B 1 88  ? 53.189 -17.330 -4.863  1.00 22.21 ?  88  LEU   B HD12 1 
ATOM   5199 H HD13 . LEU   B 1 88  ? 52.530 -18.637 -5.479  1.00 22.21 ?  88  LEU   B HD13 1 
ATOM   5200 H HD21 . LEU   B 1 88  ? 55.017 -19.409 -6.949  1.00 24.12 ?  88  LEU   B HD21 1 
ATOM   5201 H HD22 . LEU   B 1 88  ? 53.652 -19.518 -7.753  1.00 24.12 ?  88  LEU   B HD22 1 
ATOM   5202 H HD23 . LEU   B 1 88  ? 54.839 -18.628 -8.320  1.00 24.12 ?  88  LEU   B HD23 1 
ATOM   5203 N N    . ALA   B 1 89  ? 51.558 -14.658 -9.284  1.00 12.22 ?  89  ALA   B N    1 
ATOM   5204 C CA   . ALA   B 1 89  ? 50.276 -14.157 -9.755  1.00 12.04 ?  89  ALA   B CA   1 
ATOM   5205 C C    . ALA   B 1 89  ? 50.248 -12.668 -9.474  1.00 12.37 ?  89  ALA   B C    1 
ATOM   5206 O O    . ALA   B 1 89  ? 51.081 -12.147 -8.730  1.00 12.98 ?  89  ALA   B O    1 
ATOM   5207 C CB   . ALA   B 1 89  ? 49.116 -14.823 -9.017  1.00 12.45 ?  89  ALA   B CB   1 
ATOM   5208 H H    . ALA   B 1 89  ? 51.996 -14.088 -8.811  1.00 14.63 ?  89  ALA   B H    1 
ATOM   5209 H HA   . ALA   B 1 89  ? 50.180 -14.308 -10.710 1.00 14.42 ?  89  ALA   B HA   1 
ATOM   5210 H HB1  . ALA   B 1 89  ? 48.276 -14.482 -9.374  1.00 14.91 ?  89  ALA   B HB1  1 
ATOM   5211 H HB2  . ALA   B 1 89  ? 49.162 -15.782 -9.157  1.00 14.91 ?  89  ALA   B HB2  1 
ATOM   5212 H HB3  . ALA   B 1 89  ? 49.180 -14.619 -8.075  1.00 14.91 ?  89  ALA   B HB3  1 
ATOM   5213 N N    . LYS   B 1 90  ? 49.266 -11.979 -10.048 1.00 13.11 ?  90  LYS   B N    1 
ATOM   5214 C CA   . LYS   B 1 90  ? 49.081 -10.591 -9.648  1.00 13.06 ?  90  LYS   B CA   1 
ATOM   5215 C C    . LYS   B 1 90  ? 48.753 -10.514 -8.160  1.00 13.22 ?  90  LYS   B C    1 
ATOM   5216 O O    . LYS   B 1 90  ? 49.396 -9.767  -7.406  1.00 14.62 ?  90  LYS   B O    1 
ATOM   5217 C CB   . LYS   B 1 90  ? 48.009 -9.931  -10.510 1.00 14.80 ?  90  LYS   B CB   1 
ATOM   5218 C CG   . LYS   B 1 90  ? 47.698 -8.497  -10.119 1.00 15.44 ?  90  LYS   B CG   1 
ATOM   5219 C CD   . LYS   B 1 90  ? 48.897 -7.582  -10.183 1.00 17.75 ?  90  LYS   B CD   1 
ATOM   5220 C CE   . LYS   B 1 90  ? 48.444 -6.160  -9.916  1.00 20.18 ?  90  LYS   B CE   1 
ATOM   5221 N NZ   . LYS   B 1 90  ? 49.588 -5.219  -9.839  1.00 19.74 ?  90  LYS   B NZ   1 
ATOM   5222 H H    . LYS   B 1 90  ? 48.722 -12.278 -10.645 1.00 15.71 ?  90  LYS   B H    1 
ATOM   5223 H HA   . LYS   B 1 90  ? 49.911 -10.116 -9.792  1.00 15.65 ?  90  LYS   B HA   1 
ATOM   5224 H HB2  . LYS   B 1 90  ? 48.314 -9.923  -11.434 1.00 17.74 ?  90  LYS   B HB2  1 
ATOM   5225 H HB3  . LYS   B 1 90  ? 47.189 -10.442 -10.442 1.00 17.74 ?  90  LYS   B HB3  1 
ATOM   5226 H HG2  . LYS   B 1 90  ? 47.025 -8.146  -10.723 1.00 18.50 ?  90  LYS   B HG2  1 
ATOM   5227 H HG3  . LYS   B 1 90  ? 47.358 -8.482  -9.209  1.00 18.50 ?  90  LYS   B HG3  1 
ATOM   5228 H HD2  . LYS   B 1 90  ? 49.543 -7.832  -9.502  1.00 21.28 ?  90  LYS   B HD2  1 
ATOM   5229 H HD3  . LYS   B 1 90  ? 49.296 -7.620  -11.066 1.00 21.28 ?  90  LYS   B HD3  1 
ATOM   5230 H HE2  . LYS   B 1 90  ? 47.863 -5.863  -10.637 1.00 24.19 ?  90  LYS   B HE2  1 
ATOM   5231 H HE3  . LYS   B 1 90  ? 47.970 -6.121  -9.070  1.00 24.19 ?  90  LYS   B HE3  1 
ATOM   5232 H HZ1  . LYS   B 1 90  ? 49.299 -4.391  -9.684  1.00 23.66 ?  90  LYS   B HZ1  1 
ATOM   5233 H HZ2  . LYS   B 1 90  ? 50.138 -5.460  -9.181  1.00 23.66 ?  90  LYS   B HZ2  1 
ATOM   5234 H HZ3  . LYS   B 1 90  ? 50.041 -5.225  -10.608 1.00 23.66 ?  90  LYS   B HZ3  1 
ATOM   5235 N N    . HIS   B 1 91  ? 47.781 -11.321 -7.717  1.00 11.68 ?  91  HIS   B N    1 
ATOM   5236 C CA   . HIS   B 1 91  ? 47.317 -11.343 -6.342  1.00 11.50 ?  91  HIS   B CA   1 
ATOM   5237 C C    . HIS   B 1 91  ? 47.315 -12.771 -5.825  1.00 11.00 ?  91  HIS   B C    1 
ATOM   5238 O O    . HIS   B 1 91  ? 47.094 -13.720 -6.583  1.00 11.42 ?  91  HIS   B O    1 
ATOM   5239 C CB   . HIS   B 1 91  ? 45.864 -10.867 -6.232  1.00 12.92 ?  91  HIS   B CB   1 
ATOM   5240 C CG   . HIS   B 1 91  ? 45.650 -9.460  -6.672  1.00 16.75 ?  91  HIS   B CG   1 
ATOM   5241 N ND1  . HIS   B 1 91  ? 46.237 -8.382  -6.043  1.00 19.51 ?  91  HIS   B ND1  1 
ATOM   5242 C CD2  . HIS   B 1 91  ? 44.882 -8.948  -7.659  1.00 19.43 ?  91  HIS   B CD2  1 
ATOM   5243 C CE1  . HIS   B 1 91  ? 45.856 -7.265  -6.639  1.00 20.44 ?  91  HIS   B CE1  1 
ATOM   5244 N NE2  . HIS   B 1 91  ? 45.030 -7.581  -7.621  1.00 20.75 ?  91  HIS   B NE2  1 
ATOM   5245 H H    . HIS   B 1 91  ? 47.354 -11.874 -8.219  1.00 13.99 ?  91  HIS   B H    1 
ATOM   5246 H HA   . HIS   B 1 91  ? 47.887 -10.787 -5.777  1.00 13.77 ?  91  HIS   B HA   1 
ATOM   5247 H HB2  . HIS   B 1 91  ? 45.307 -11.436 -6.780  1.00 15.47 ?  91  HIS   B HB2  1 
ATOM   5248 H HB3  . HIS   B 1 91  ? 45.584 -10.932 -5.301  1.00 15.47 ?  91  HIS   B HB3  1 
ATOM   5249 H HD1  . HIS   B 1 91  ? 46.776 -8.428  -5.369  1.00 23.39 ?  91  HIS   B HD1  1 
ATOM   5250 H HD2  . HIS   B 1 91  ? 44.361 -9.423  -8.258  1.00 23.29 ?  91  HIS   B HD2  1 
ATOM   5251 H HE1  . HIS   B 1 91  ? 46.125 -6.403  -6.401  1.00 24.50 ?  91  HIS   B HE1  1 
ATOM   5252 N N    . CYS   B 1 92  ? 47.504 -12.908 -4.519  1.00 11.04 ?  92  CYS   B N    1 
ATOM   5253 C CA   . CYS   B 1 92  ? 47.202 -14.144 -3.811  1.00 10.80 ?  92  CYS   B CA   1 
ATOM   5254 C C    . CYS   B 1 92  ? 45.984 -13.909 -2.927  1.00 10.32 ?  92  CYS   B C    1 
ATOM   5255 O O    . CYS   B 1 92  ? 45.982 -13.004 -2.081  1.00 11.24 ?  92  CYS   B O    1 
ATOM   5256 C CB   . CYS   B 1 92  ? 48.380 -14.607 -2.960  1.00 11.00 ?  92  CYS   B CB   1 
ATOM   5257 S SG   . CYS   B 1 92  ? 48.024 -16.135 -2.061  1.00 11.40 ?  92  CYS   B SG   1 
ATOM   5258 H H    . CYS   B 1 92  ? 47.825 -12.289 -4.010  1.00 13.23 ?  92  CYS   B H    1 
ATOM   5259 H HA   . CYS   B 1 92  ? 46.997 -14.841 -4.457  1.00 12.93 ?  92  CYS   B HA   1 
ATOM   5260 H HB2  . CYS   B 1 92  ? 49.141 -14.766 -3.533  1.00 13.18 ?  92  CYS   B HB2  1 
ATOM   5261 H HB3  . CYS   B 1 92  ? 48.583 -13.918 -2.310  1.00 13.18 ?  92  CYS   B HB3  1 
ATOM   5262 H HG   . CYS   B 1 92  ? 48.999 -16.442 -1.434  1.00 13.66 ?  92  CYS   B HG   1 
ATOM   5263 N N    . LEU   B 1 93  ? 44.944 -14.716 -3.139  1.00 10.22 ?  93  LEU   B N    1 
ATOM   5264 C CA   . LEU   B 1 93  ? 43.767 -14.727 -2.280  1.00 10.41 ?  93  LEU   B CA   1 
ATOM   5265 C C    . LEU   B 1 93  ? 43.987 -15.796 -1.214  1.00 9.91  ?  93  LEU   B C    1 
ATOM   5266 O O    . LEU   B 1 93  ? 43.937 -17.000 -1.507  1.00 10.52 ?  93  LEU   B O    1 
ATOM   5267 C CB   . LEU   B 1 93  ? 42.505 -15.011 -3.092  1.00 10.66 ?  93  LEU   B CB   1 
ATOM   5268 C CG   . LEU   B 1 93  ? 41.204 -15.040 -2.287  1.00 11.48 ?  93  LEU   B CG   1 
ATOM   5269 C CD1  . LEU   B 1 93  ? 40.839 -13.651 -1.804  1.00 11.69 ?  93  LEU   B CD1  1 
ATOM   5270 C CD2  . LEU   B 1 93  ? 40.081 -15.644 -3.116  1.00 11.74 ?  93  LEU   B CD2  1 
ATOM   5271 H H    . LEU   B 1 93  ? 44.900 -15.292 -3.789  1.00 12.23 ?  93  LEU   B H    1 
ATOM   5272 H HA   . LEU   B 1 93  ? 43.679 -13.864 -1.847  1.00 12.47 ?  93  LEU   B HA   1 
ATOM   5273 H HB2  . LEU   B 1 93  ? 42.414 -14.318 -3.764  1.00 12.76 ?  93  LEU   B HB2  1 
ATOM   5274 H HB3  . LEU   B 1 93  ? 42.601 -15.871 -3.517  1.00 12.76 ?  93  LEU   B HB3  1 
ATOM   5275 H HG   . LEU   B 1 93  ? 41.326 -15.595 -1.505  1.00 13.75 ?  93  LEU   B HG   1 
ATOM   5276 H HD11 . LEU   B 1 93  ? 39.989 -13.689 -1.341  1.00 14.00 ?  93  LEU   B HD11 1 
ATOM   5277 H HD12 . LEU   B 1 93  ? 41.530 -13.331 -1.204  1.00 14.00 ?  93  LEU   B HD12 1 
ATOM   5278 H HD13 . LEU   B 1 93  ? 40.769 -13.057 -2.572  1.00 14.00 ?  93  LEU   B HD13 1 
ATOM   5279 H HD21 . LEU   B 1 93  ? 39.267 -15.647 -2.589  1.00 14.07 ?  93  LEU   B HD21 1 
ATOM   5280 H HD22 . LEU   B 1 93  ? 39.957 -15.111 -3.916  1.00 14.07 ?  93  LEU   B HD22 1 
ATOM   5281 H HD23 . LEU   B 1 93  ? 40.324 -16.552 -3.356  1.00 14.07 ?  93  LEU   B HD23 1 
ATOM   5282 N N    . HIS   B 1 94  ? 44.259 -15.360 0.010   1.00 10.16 ?  94  HIS   B N    1 
ATOM   5283 C CA   . HIS   B 1 94  ? 44.473 -16.268 1.129   1.00 10.22 ?  94  HIS   B CA   1 
ATOM   5284 C C    . HIS   B 1 94  ? 43.113 -16.625 1.702   1.00 10.45 ?  94  HIS   B C    1 
ATOM   5285 O O    . HIS   B 1 94  ? 42.440 -15.753 2.249   1.00 11.82 ?  94  HIS   B O    1 
ATOM   5286 C CB   . HIS   B 1 94  ? 45.341 -15.592 2.187   1.00 10.82 ?  94  HIS   B CB   1 
ATOM   5287 C CG   . HIS   B 1 94  ? 46.724 -15.293 1.717   1.00 10.81 ?  94  HIS   B CG   1 
ATOM   5288 N ND1  . HIS   B 1 94  ? 47.751 -16.206 1.807   1.00 10.83 ?  94  HIS   B ND1  1 
ATOM   5289 C CD2  . HIS   B 1 94  ? 47.234 -14.191 1.114   1.00 11.07 ?  94  HIS   B CD2  1 
ATOM   5290 C CE1  . HIS   B 1 94  ? 48.842 -15.661 1.299   1.00 11.04 ?  94  HIS   B CE1  1 
ATOM   5291 N NE2  . HIS   B 1 94  ? 48.560 -14.439 0.876   1.00 11.27 ?  94  HIS   B NE2  1 
ATOM   5292 H H    . HIS   B 1 94  ? 44.325 -14.522 0.219   1.00 12.16 ?  94  HIS   B H    1 
ATOM   5293 H HA   . HIS   B 1 94  ? 44.908 -17.074 0.818   1.00 12.24 ?  94  HIS   B HA   1 
ATOM   5294 H HB2  . HIS   B 1 94  ? 44.926 -14.753 2.439   1.00 12.96 ?  94  HIS   B HB2  1 
ATOM   5295 H HB3  . HIS   B 1 94  ? 45.407 -16.177 2.952   1.00 12.96 ?  94  HIS   B HB3  1 
ATOM   5296 H HD2  . HIS   B 1 94  ? 46.780 -13.411 0.908   1.00 13.26 ?  94  HIS   B HD2  1 
ATOM   5297 H HE1  . HIS   B 1 94  ? 49.676 -16.080 1.249   1.00 13.23 ?  94  HIS   B HE1  1 
ATOM   5298 H HE2  . HIS   B 1 94  ? 49.118 -13.906 0.501   1.00 13.50 ?  94  HIS   B HE2  1 
ATOM   5299 N N    . VAL   B 1 95  ? 42.687 -17.880 1.555   1.00 10.47 ?  95  VAL   B N    1 
ATOM   5300 C CA   . VAL   B 1 95  ? 41.358 -18.321 1.978   1.00 10.73 ?  95  VAL   B CA   1 
ATOM   5301 C C    . VAL   B 1 95  ? 41.521 -19.357 3.076   1.00 10.97 ?  95  VAL   B C    1 
ATOM   5302 O O    . VAL   B 1 95  ? 42.292 -20.311 2.922   1.00 11.29 ?  95  VAL   B O    1 
ATOM   5303 C CB   . VAL   B 1 95  ? 40.550 -18.924 0.815   1.00 11.16 ?  95  VAL   B CB   1 
ATOM   5304 C CG1  . VAL   B 1 95  ? 39.165 -19.372 1.298   1.00 12.16 ?  95  VAL   B CG1  1 
ATOM   5305 C CG2  . VAL   B 1 95  ? 40.431 -17.939 -0.329  1.00 11.12 ?  95  VAL   B CG2  1 
ATOM   5306 H H    . VAL   B 1 95  ? 43.153 -18.509 1.200   1.00 12.53 ?  95  VAL   B H    1 
ATOM   5307 H HA   . VAL   B 1 95  ? 40.858 -17.569 2.338   1.00 12.84 ?  95  VAL   B HA   1 
ATOM   5308 H HB   . VAL   B 1 95  ? 41.005 -19.704 0.484   1.00 13.37 ?  95  VAL   B HB   1 
ATOM   5309 H HG11 . VAL   B 1 95  ? 38.601 -19.560 0.524   1.00 14.56 ?  95  VAL   B HG11 1 
ATOM   5310 H HG12 . VAL   B 1 95  ? 39.253 -20.172 1.835   1.00 14.56 ?  95  VAL   B HG12 1 
ATOM   5311 H HG13 . VAL   B 1 95  ? 38.759 -18.662 1.823   1.00 14.56 ?  95  VAL   B HG13 1 
ATOM   5312 H HG21 . VAL   B 1 95  ? 39.862 -18.322 -1.015  1.00 13.32 ?  95  VAL   B HG21 1 
ATOM   5313 H HG22 . VAL   B 1 95  ? 40.043 -17.116 0.002   1.00 13.32 ?  95  VAL   B HG22 1 
ATOM   5314 H HG23 . VAL   B 1 95  ? 41.316 -17.774 -0.684  1.00 13.32 ?  95  VAL   B HG23 1 
ATOM   5315 N N    . VAL   B 1 96  ? 40.787 -19.184 4.170   1.00 11.19 ?  96  VAL   B N    1 
ATOM   5316 C CA   . VAL   B 1 96  ? 40.864 -20.098 5.307   1.00 11.64 ?  96  VAL   B CA   1 
ATOM   5317 C C    . VAL   B 1 96  ? 39.676 -21.058 5.257   1.00 11.73 ?  96  VAL   B C    1 
ATOM   5318 O O    . VAL   B 1 96  ? 38.554 -20.703 5.628   1.00 12.69 ?  96  VAL   B O    1 
ATOM   5319 C CB   . VAL   B 1 96  ? 40.916 -19.352 6.644   1.00 12.30 ?  96  VAL   B CB   1 
ATOM   5320 C CG1  . VAL   B 1 96  ? 41.094 -20.342 7.788   1.00 13.37 ?  96  VAL   B CG1  1 
ATOM   5321 C CG2  . VAL   B 1 96  ? 42.039 -18.316 6.656   1.00 13.15 ?  96  VAL   B CG2  1 
ATOM   5322 H H    . VAL   B 1 96  ? 40.230 -18.540 4.284   1.00 13.40 ?  96  VAL   B H    1 
ATOM   5323 H HA   . VAL   B 1 96  ? 41.678 -20.626 5.235   1.00 13.94 ?  96  VAL   B HA   1 
ATOM   5324 H HB   . VAL   B 1 96  ? 40.077 -18.888 6.783   1.00 14.74 ?  96  VAL   B HB   1 
ATOM   5325 H HG11 . VAL   B 1 96  ? 41.278 -19.848 8.607   1.00 16.02 ?  96  VAL   B HG11 1 
ATOM   5326 H HG12 . VAL   B 1 96  ? 40.284 -20.861 7.893   1.00 16.02 ?  96  VAL   B HG12 1 
ATOM   5327 H HG13 . VAL   B 1 96  ? 41.843 -20.927 7.587   1.00 16.02 ?  96  VAL   B HG13 1 
ATOM   5328 H HG21 . VAL   B 1 96  ? 42.085 -17.901 7.536   1.00 15.75 ?  96  VAL   B HG21 1 
ATOM   5329 H HG22 . VAL   B 1 96  ? 42.881 -18.751 6.455   1.00 15.75 ?  96  VAL   B HG22 1 
ATOM   5330 H HG23 . VAL   B 1 96  ? 41.852 -17.635 5.987   1.00 15.75 ?  96  VAL   B HG23 1 
ATOM   5331 N N    . GLY   B 1 97  ? 39.916 -22.293 4.828   1.00 12.06 ?  97  GLY   B N    1 
ATOM   5332 C CA   . GLY   B 1 97  ? 38.929 -23.342 4.972   1.00 12.59 ?  97  GLY   B CA   1 
ATOM   5333 C C    . GLY   B 1 97  ? 39.035 -23.964 6.348   1.00 13.56 ?  97  GLY   B C    1 
ATOM   5334 O O    . GLY   B 1 97  ? 40.072 -23.845 7.015   1.00 14.19 ?  97  GLY   B O    1 
ATOM   5335 H H    . GLY   B 1 97  ? 40.653 -22.547 4.453   1.00 14.45 ?  97  GLY   B H    1 
ATOM   5336 H HA2  . GLY   B 1 97  ? 38.040 -22.965 4.850   1.00 15.08 ?  97  GLY   B HA2  1 
ATOM   5337 H HA3  . GLY   B 1 97  ? 39.071 -24.022 4.291   1.00 15.08 ?  97  GLY   B HA3  1 
ATOM   5338 N N    . PRO   B 1 98  ? 37.984 -24.646 6.805   1.00 14.22 ?  98  PRO   B N    1 
ATOM   5339 C CA   . PRO   B 1 98  ? 38.079 -25.345 8.091   1.00 15.07 ?  98  PRO   B CA   1 
ATOM   5340 C C    . PRO   B 1 98  ? 39.104 -26.468 8.048   1.00 13.90 ?  98  PRO   B C    1 
ATOM   5341 O O    . PRO   B 1 98  ? 39.206 -27.210 7.072   1.00 14.65 ?  98  PRO   B O    1 
ATOM   5342 C CB   . PRO   B 1 98  ? 36.665 -25.894 8.297   1.00 15.58 ?  98  PRO   B CB   1 
ATOM   5343 C CG   . PRO   B 1 98  ? 36.105 -26.016 6.927   1.00 15.05 ?  98  PRO   B CG   1 
ATOM   5344 C CD   . PRO   B 1 98  ? 36.667 -24.838 6.173   1.00 14.36 ?  98  PRO   B CD   1 
ATOM   5345 H HA   . PRO   B 1 98  ? 38.301 -24.723 8.794   1.00 18.06 ?  98  PRO   B HA   1 
ATOM   5346 H HB2  . PRO   B 1 98  ? 36.714 -26.766 8.728   1.00 18.67 ?  98  PRO   B HB2  1 
ATOM   5347 H HB3  . PRO   B 1 98  ? 36.147 -25.276 8.828   1.00 18.67 ?  98  PRO   B HB3  1 
ATOM   5348 H HG2  . PRO   B 1 98  ? 36.395 -26.856 6.530   1.00 18.03 ?  98  PRO   B HG2  1 
ATOM   5349 H HG3  . PRO   B 1 98  ? 35.137 -25.976 6.969   1.00 18.03 ?  98  PRO   B HG3  1 
ATOM   5350 H HD2  . PRO   B 1 98  ? 36.757 -25.052 5.228   1.00 17.20 ?  98  PRO   B HD2  1 
ATOM   5351 H HD3  . PRO   B 1 98  ? 36.115 -24.052 6.308   1.00 17.20 ?  98  PRO   B HD3  1 
ATOM   5352 N N    . ASN   B 1 99  ? 39.856 -26.595 9.133   1.00 15.10 ?  99  ASN   B N    1 
ATOM   5353 C CA   . ASN   B 1 99  ? 40.837 -27.665 9.297   1.00 16.10 ?  99  ASN   B CA   1 
ATOM   5354 C C    . ASN   B 1 99  ? 40.202 -28.751 10.166  1.00 18.67 ?  99  ASN   B C    1 
ATOM   5355 O O    . ASN   B 1 99  ? 40.107 -28.609 11.388  1.00 19.34 ?  99  ASN   B O    1 
ATOM   5356 C CB   . ASN   B 1 99  ? 42.112 -27.108 9.919   1.00 16.17 ?  99  ASN   B CB   1 
ATOM   5357 C CG   . ASN   B 1 99  ? 43.244 -28.112 9.923   1.00 17.55 ?  99  ASN   B CG   1 
ATOM   5358 O OD1  . ASN   B 1 99  ? 43.016 -29.305 10.080  1.00 18.73 ?  99  ASN   B OD1  1 
ATOM   5359 N ND2  . ASN   B 1 99  ? 44.472 -27.634 9.749   1.00 18.14 ?  99  ASN   B ND2  1 
ATOM   5360 H H    . ASN   B 1 99  ? 39.820 -26.057 9.804   1.00 18.09 ?  99  ASN   B H    1 
ATOM   5361 H HA   . ASN   B 1 99  ? 41.055 -28.048 8.434   1.00 19.29 ?  99  ASN   B HA   1 
ATOM   5362 H HB2  . ASN   B 1 99  ? 42.398 -26.332 9.418   1.00 19.38 ?  99  ASN   B HB2  1 
ATOM   5363 H HB3  . ASN   B 1 99  ? 41.931 -26.860 10.842  1.00 19.38 ?  99  ASN   B HB3  1 
ATOM   5364 H HD21 . ASN   B 1 99  ? 45.146 -28.166 9.740   1.00 21.75 ?  99  ASN   B HD21 1 
ATOM   5365 H HD22 . ASN   B 1 99  ? 44.590 -26.787 9.647   1.00 21.75 ?  99  ASN   B HD22 1 
ATOM   5366 N N    A VAL   B 1 100 ? 39.738 -29.828 9.526   0.66 20.65 ?  100 VAL   B N    1 
ATOM   5367 N N    B VAL   B 1 100 ? 39.760 -29.835 9.522   0.34 20.86 ?  100 VAL   B N    1 
ATOM   5368 C CA   A VAL   B 1 100 ? 39.117 -30.924 10.268  0.66 23.48 ?  100 VAL   B CA   1 
ATOM   5369 C CA   B VAL   B 1 100 ? 39.126 -30.936 10.243  0.34 23.26 ?  100 VAL   B CA   1 
ATOM   5370 C C    A VAL   B 1 100 ? 40.118 -31.591 11.203  0.66 23.87 ?  100 VAL   B C    1 
ATOM   5371 C C    B VAL   B 1 100 ? 40.114 -31.610 11.185  0.34 23.84 ?  100 VAL   B C    1 
ATOM   5372 O O    A VAL   B 1 100 ? 39.740 -32.104 12.263  0.66 24.27 ?  100 VAL   B O    1 
ATOM   5373 O O    B VAL   B 1 100 ? 39.725 -32.137 12.233  0.34 23.97 ?  100 VAL   B O    1 
ATOM   5374 C CB   A VAL   B 1 100 ? 38.468 -31.933 9.298   0.66 26.12 ?  100 VAL   B CB   1 
ATOM   5375 C CB   B VAL   B 1 100 ? 38.498 -31.934 9.248   0.34 25.07 ?  100 VAL   B CB   1 
ATOM   5376 C CG1  A VAL   B 1 100 ? 37.994 -33.169 10.049  0.66 27.58 ?  100 VAL   B CG1  1 
ATOM   5377 C CG1  B VAL   B 1 100 ? 37.956 -33.156 9.978   0.34 25.96 ?  100 VAL   B CG1  1 
ATOM   5378 C CG2  A VAL   B 1 100 ? 37.305 -31.286 8.559   0.66 26.85 ?  100 VAL   B CG2  1 
ATOM   5379 C CG2  B VAL   B 1 100 ? 37.394 -31.260 8.450   0.34 25.70 ?  100 VAL   B CG2  1 
ATOM   5380 H H    A VAL   B 1 100 ? 39.755 -29.934 8.671   0.66 24.75 ?  100 VAL   B H    1 
ATOM   5381 H H    B VAL   B 1 100 ? 39.814 -29.950 8.671   0.34 25.01 ?  100 VAL   B H    1 
ATOM   5382 H HA   A VAL   B 1 100 ? 38.404 -30.554 10.815  0.66 28.15 ?  100 VAL   B HA   1 
ATOM   5383 H HA   B VAL   B 1 100 ? 38.406 -30.574 10.783  0.34 27.88 ?  100 VAL   B HA   1 
ATOM   5384 H HB   A VAL   B 1 100 ? 39.126 -32.214 8.645   0.66 31.32 ?  100 VAL   B HB   1 
ATOM   5385 H HB   B VAL   B 1 100 ? 39.178 -32.235 8.626   0.34 30.05 ?  100 VAL   B HB   1 
ATOM   5386 H HG11 A VAL   B 1 100 ? 37.395 -33.674 9.475   0.66 33.07 ?  100 VAL   B HG11 1 
ATOM   5387 H HG11 B VAL   B 1 100 ? 37.388 -33.658 9.371   0.34 31.12 ?  100 VAL   B HG11 1 
ATOM   5388 H HG12 A VAL   B 1 100 ? 38.760 -33.715 10.284  0.66 33.07 ?  100 VAL   B HG12 1 
ATOM   5389 H HG12 B VAL   B 1 100 ? 38.697 -33.710 10.267  0.34 31.12 ?  100 VAL   B HG12 1 
ATOM   5390 H HG13 A VAL   B 1 100 ? 37.523 -32.892 10.851  0.66 33.07 ?  100 VAL   B HG13 1 
ATOM   5391 H HG13 B VAL   B 1 100 ? 37.439 -32.863 10.744  0.34 31.12 ?  100 VAL   B HG13 1 
ATOM   5392 H HG21 A VAL   B 1 100 ? 36.916 -31.938 7.952   0.66 32.19 ?  100 VAL   B HG21 1 
ATOM   5393 H HG21 B VAL   B 1 100 ? 36.995 -31.911 7.851   0.34 30.81 ?  100 VAL   B HG21 1 
ATOM   5394 H HG22 A VAL   B 1 100 ? 36.639 -31.000 9.205   0.66 32.19 ?  100 VAL   B HG22 1 
ATOM   5395 H HG22 B VAL   B 1 100 ? 36.723 -30.922 9.064   0.34 30.81 ?  100 VAL   B HG22 1 
ATOM   5396 H HG23 A VAL   B 1 100 ? 37.632 -30.524 8.060   0.66 32.19 ?  100 VAL   B HG23 1 
ATOM   5397 H HG23 B VAL   B 1 100 ? 37.774 -30.530 7.939   0.34 30.81 ?  100 VAL   B HG23 1 
ATOM   5398 N N    . ASN   B 1 101 ? 41.401 -31.618 10.828  1.00 24.45 ?  101 ASN   B N    1 
ATOM   5399 C CA   . ASN   B 1 101 ? 42.426 -32.164 11.715  1.00 25.96 ?  101 ASN   B CA   1 
ATOM   5400 C C    . ASN   B 1 101 ? 42.604 -31.340 12.984  1.00 27.81 ?  101 ASN   B C    1 
ATOM   5401 O O    . ASN   B 1 101 ? 43.231 -31.826 13.934  1.00 29.75 ?  101 ASN   B O    1 
ATOM   5402 C CB   . ASN   B 1 101 ? 43.763 -32.288 10.976  1.00 26.40 ?  101 ASN   B CB   1 
ATOM   5403 C CG   . ASN   B 1 101 ? 43.774 -33.433 9.981   1.00 26.51 ?  101 ASN   B CG   1 
ATOM   5404 O OD1  . ASN   B 1 101 ? 43.125 -34.450 10.192  1.00 27.31 ?  101 ASN   B OD1  1 
ATOM   5405 N ND2  . ASN   B 1 101 ? 44.508 -33.267 8.889   1.00 26.00 ?  101 ASN   B ND2  1 
ATOM   5406 H H    A ASN   B 1 101 ? 41.694 -31.344 10.068  0.66 29.31 ?  101 ASN   B H    1 
ATOM   5407 H H    B ASN   B 1 101 ? 41.700 -31.323 10.079  0.34 29.31 ?  101 ASN   B H    1 
ATOM   5408 H HA   . ASN   B 1 101 ? 42.154 -33.051 11.986  1.00 31.13 ?  101 ASN   B HA   1 
ATOM   5409 H HB2  . ASN   B 1 101 ? 43.941 -31.470 10.490  1.00 31.65 ?  101 ASN   B HB2  1 
ATOM   5410 H HB3  . ASN   B 1 101 ? 44.467 -32.447 11.626  1.00 31.65 ?  101 ASN   B HB3  1 
ATOM   5411 H HD21 . ASN   B 1 101 ? 44.544 -33.891 8.297   1.00 31.17 ?  101 ASN   B HD21 1 
ATOM   5412 H HD22 . ASN   B 1 101 ? 44.944 -32.537 8.772   1.00 31.17 ?  101 ASN   B HD22 1 
ATOM   5413 N N    . LYS   B 1 102 ? 42.082 -30.112 13.014  1.00 29.61 ?  102 LYS   B N    1 
ATOM   5414 C CA   . LYS   B 1 102 ? 42.034 -29.285 14.213  1.00 31.79 ?  102 LYS   B CA   1 
ATOM   5415 C C    . LYS   B 1 102 ? 40.640 -29.238 14.828  1.00 31.47 ?  102 LYS   B C    1 
ATOM   5416 O O    . LYS   B 1 102 ? 40.400 -28.433 15.731  1.00 32.45 ?  102 LYS   B O    1 
ATOM   5417 C CB   . LYS   B 1 102 ? 42.484 -27.858 13.893  1.00 35.12 ?  102 LYS   B CB   1 
ATOM   5418 C CG   . LYS   B 1 102 ? 43.947 -27.706 13.516  1.00 38.34 ?  102 LYS   B CG   1 
ATOM   5419 C CD   . LYS   B 1 102 ? 44.215 -26.282 13.052  1.00 41.51 ?  102 LYS   B CD   1 
ATOM   5420 C CE   . LYS   B 1 102 ? 45.692 -26.017 12.828  1.00 43.77 ?  102 LYS   B CE   1 
ATOM   5421 N NZ   . LYS   B 1 102 ? 45.924 -24.616 12.367  1.00 45.19 ?  102 LYS   B NZ   1 
ATOM   5422 H H    . LYS   B 1 102 ? 41.734 -29.725 12.329  1.00 35.51 ?  102 LYS   B H    1 
ATOM   5423 H HA   . LYS   B 1 102 ? 42.645 -29.648 14.871  1.00 38.12 ?  102 LYS   B HA   1 
ATOM   5424 H HB2  . LYS   B 1 102 ? 41.956 -27.526 13.151  1.00 42.12 ?  102 LYS   B HB2  1 
ATOM   5425 H HB3  . LYS   B 1 102 ? 42.327 -27.302 14.674  1.00 42.12 ?  102 LYS   B HB3  1 
ATOM   5426 H HG2  . LYS   B 1 102 ? 44.505 -27.887 14.289  1.00 45.99 ?  102 LYS   B HG2  1 
ATOM   5427 H HG3  . LYS   B 1 102 ? 44.162 -28.313 12.791  1.00 45.99 ?  102 LYS   B HG3  1 
ATOM   5428 H HD2  . LYS   B 1 102 ? 43.751 -26.130 12.213  1.00 49.79 ?  102 LYS   B HD2  1 
ATOM   5429 H HD3  . LYS   B 1 102 ? 43.895 -25.662 13.726  1.00 49.79 ?  102 LYS   B HD3  1 
ATOM   5430 H HE2  . LYS   B 1 102 ? 46.172 -26.148 13.661  1.00 52.50 ?  102 LYS   B HE2  1 
ATOM   5431 H HE3  . LYS   B 1 102 ? 46.029 -26.622 12.148  1.00 52.50 ?  102 LYS   B HE3  1 
ATOM   5432 H HZ1  . LYS   B 1 102 ? 46.793 -24.476 12.241  1.00 54.21 ?  102 LYS   B HZ1  1 
ATOM   5433 H HZ2  . LYS   B 1 102 ? 45.493 -24.474 11.601  1.00 54.21 ?  102 LYS   B HZ2  1 
ATOM   5434 H HZ3  . LYS   B 1 102 ? 45.624 -24.042 12.978  1.00 54.21 ?  102 LYS   B HZ3  1 
ATOM   5435 N N    . GLY   B 1 103 ? 39.715 -30.068 14.351  1.00 30.86 ?  103 GLY   B N    1 
ATOM   5436 C CA   . GLY   B 1 103 ? 38.375 -30.112 14.900  1.00 30.49 ?  103 GLY   B CA   1 
ATOM   5437 C C    . GLY   B 1 103 ? 37.455 -29.000 14.453  1.00 29.12 ?  103 GLY   B C    1 
ATOM   5438 O O    . GLY   B 1 103 ? 36.375 -28.842 15.036  1.00 29.72 ?  103 GLY   B O    1 
ATOM   5439 H H    . GLY   B 1 103 ? 39.844 -30.619 13.706  1.00 37.00 ?  103 GLY   B H    1 
ATOM   5440 H HA2  . GLY   B 1 103 ? 37.963 -30.954 14.651  1.00 36.56 ?  103 GLY   B HA2  1 
ATOM   5441 H HA3  . GLY   B 1 103 ? 38.430 -30.082 15.869  1.00 36.56 ?  103 GLY   B HA3  1 
ATOM   5442 N N    A GLU   B 1 104 ? 37.851 -28.214 13.456  0.66 27.61 ?  104 GLU   B N    1 
ATOM   5443 N N    B GLU   B 1 104 ? 37.824 -28.241 13.427  0.34 28.28 ?  104 GLU   B N    1 
ATOM   5444 C CA   A GLU   B 1 104 ? 37.034 -27.102 13.001  0.66 26.07 ?  104 GLU   B CA   1 
ATOM   5445 C CA   B GLU   B 1 104 ? 36.987 -27.144 12.967  0.34 27.23 ?  104 GLU   B CA   1 
ATOM   5446 C C    A GLU   B 1 104 ? 35.854 -27.611 12.177  0.66 26.76 ?  104 GLU   B C    1 
ATOM   5447 C C    B GLU   B 1 104 ? 35.828 -27.667 12.125  0.34 27.46 ?  104 GLU   B C    1 
ATOM   5448 O O    A GLU   B 1 104 ? 35.898 -28.697 11.590  0.66 27.87 ?  104 GLU   B O    1 
ATOM   5449 O O    B GLU   B 1 104 ? 35.909 -28.734 11.507  0.34 27.87 ?  104 GLU   B O    1 
ATOM   5450 C CB   A GLU   B 1 104 ? 37.889 -26.112 12.209  0.66 24.60 ?  104 GLU   B CB   1 
ATOM   5451 C CB   B GLU   B 1 104 ? 37.828 -26.134 12.186  0.34 26.19 ?  104 GLU   B CB   1 
ATOM   5452 C CG   A GLU   B 1 104 ? 39.012 -25.523 13.058  0.66 23.26 ?  104 GLU   B CG   1 
ATOM   5453 C CG   B GLU   B 1 104 ? 38.928 -25.522 13.044  0.34 25.37 ?  104 GLU   B CG   1 
ATOM   5454 C CD   A GLU   B 1 104 ? 39.942 -24.605 12.298  0.66 21.39 ?  104 GLU   B CD   1 
ATOM   5455 C CD   B GLU   B 1 104 ? 39.879 -24.636 12.269  0.34 24.52 ?  104 GLU   B CD   1 
ATOM   5456 O OE1  A GLU   B 1 104 ? 39.957 -24.628 11.047  0.66 19.52 ?  104 GLU   B OE1  1 
ATOM   5457 O OE1  B GLU   B 1 104 ? 39.831 -24.636 11.020  0.34 23.94 ?  104 GLU   B OE1  1 
ATOM   5458 O OE2  A GLU   B 1 104 ? 40.672 -23.853 12.975  0.66 21.62 -1 104 GLU   B OE2  1 
ATOM   5459 O OE2  B GLU   B 1 104 ? 40.682 -23.935 12.919  0.34 24.57 -1 104 GLU   B OE2  1 
ATOM   5460 H H    A GLU   B 1 104 ? 38.596 -28.303 13.031  0.66 33.10 ?  104 GLU   B H    1 
ATOM   5461 H H    B GLU   B 1 104 ? 38.555 -28.339 12.983  0.34 33.91 ?  104 GLU   B H    1 
ATOM   5462 H HA   A GLU   B 1 104 ? 36.682 -26.634 13.775  0.66 31.25 ?  104 GLU   B HA   1 
ATOM   5463 H HA   B GLU   B 1 104 ? 36.615 -26.688 13.738  0.34 32.65 ?  104 GLU   B HA   1 
ATOM   5464 H HB2  A GLU   B 1 104 ? 38.291 -26.566 11.454  0.66 29.49 ?  104 GLU   B HB2  1 
ATOM   5465 H HB2  B GLU   B 1 104 ? 38.245 -26.580 11.433  0.34 31.40 ?  104 GLU   B HB2  1 
ATOM   5466 H HB3  A GLU   B 1 104 ? 37.331 -25.380 11.903  0.66 29.49 ?  104 GLU   B HB3  1 
ATOM   5467 H HB3  B GLU   B 1 104 ? 37.255 -25.416 11.874  0.34 31.40 ?  104 GLU   B HB3  1 
ATOM   5468 H HG2  A GLU   B 1 104 ? 38.628 -25.008 13.785  0.66 27.89 ?  104 GLU   B HG2  1 
ATOM   5469 H HG2  B GLU   B 1 104 ? 38.520 -24.984 13.741  0.34 30.42 ?  104 GLU   B HG2  1 
ATOM   5470 H HG3  A GLU   B 1 104 ? 39.554 -26.242 13.418  0.66 27.89 ?  104 GLU   B HG3  1 
ATOM   5471 H HG3  B GLU   B 1 104 ? 39.449 -26.236 13.446  0.34 30.42 ?  104 GLU   B HG3  1 
ATOM   5472 N N    A ASP   B 1 105 ? 34.787 -26.817 12.155  0.66 26.14 ?  105 ASP   B N    1 
ATOM   5473 N N    B ASP   B 1 105 ? 34.737 -26.902 12.112  0.34 26.97 ?  105 ASP   B N    1 
ATOM   5474 C CA   A ASP   B 1 105 ? 33.511 -27.270 11.614  0.66 26.92 ?  105 ASP   B CA   1 
ATOM   5475 C CA   B ASP   B 1 105 ? 33.478 -27.378 11.549  0.34 27.15 ?  105 ASP   B CA   1 
ATOM   5476 C C    A ASP   B 1 105 ? 33.557 -27.313 10.090  0.66 25.59 ?  105 ASP   B C    1 
ATOM   5477 C C    B ASP   B 1 105 ? 33.544 -27.386 10.025  0.34 26.34 ?  105 ASP   B C    1 
ATOM   5478 O O    A ASP   B 1 105 ? 33.698 -26.277 9.434   0.66 25.01 ?  105 ASP   B O    1 
ATOM   5479 O O    B ASP   B 1 105 ? 33.733 -26.341 9.396   0.34 25.75 ?  105 ASP   B O    1 
ATOM   5480 C CB   A ASP   B 1 105 ? 32.395 -26.342 12.090  0.66 30.04 ?  105 ASP   B CB   1 
ATOM   5481 C CB   B ASP   B 1 105 ? 32.332 -26.491 12.031  0.34 28.21 ?  105 ASP   B CB   1 
ATOM   5482 C CG   A ASP   B 1 105 ? 31.019 -26.808 11.654  0.66 33.12 ?  105 ASP   B CG   1 
ATOM   5483 C CG   B ASP   B 1 105 ? 30.967 -27.067 11.692  0.34 29.49 ?  105 ASP   B CG   1 
ATOM   5484 O OD1  A ASP   B 1 105 ? 30.915 -27.904 11.064  0.66 33.16 ?  105 ASP   B OD1  1 
ATOM   5485 O OD1  B ASP   B 1 105 ? 30.909 -28.065 10.942  0.34 29.58 ?  105 ASP   B OD1  1 
ATOM   5486 O OD2  A ASP   B 1 105 ? 30.039 -26.070 11.898  0.66 35.03 -1 105 ASP   B OD2  1 
ATOM   5487 O OD2  B ASP   B 1 105 ? 29.951 -26.530 12.184  0.34 29.82 -1 105 ASP   B OD2  1 
ATOM   5488 H H    A ASP   B 1 105 ? 34.779 -26.007 12.445  0.66 31.34 ?  105 ASP   B H    1 
ATOM   5489 H H    B ASP   B 1 105 ? 34.702 -26.101 12.421  0.34 32.34 ?  105 ASP   B H    1 
ATOM   5490 H HA   A ASP   B 1 105 ? 33.322 -28.163 11.941  0.66 32.27 ?  105 ASP   B HA   1 
ATOM   5491 H HA   B ASP   B 1 105 ? 33.307 -28.283 11.852  0.34 32.55 ?  105 ASP   B HA   1 
ATOM   5492 H HB2  A ASP   B 1 105 ? 32.418 -26.290 13.062  0.66 36.02 ?  105 ASP   B HB2  1 
ATOM   5493 H HB2  B ASP   B 1 105 ? 32.385 -26.400 12.996  0.34 33.82 ?  105 ASP   B HB2  1 
ATOM   5494 H HB3  A ASP   B 1 105 ? 32.528 -25.461 11.711  0.66 36.02 ?  105 ASP   B HB3  1 
ATOM   5495 H HB3  B ASP   B 1 105 ? 32.411 -25.616 11.614  0.34 33.82 ?  105 ASP   B HB3  1 
ATOM   5496 N N    A ILE   B 1 106 ? 33.412 -28.517 9.530   0.66 25.32 ?  106 ILE   B N    1 
ATOM   5497 N N    B ILE   B 1 106 ? 33.373 -28.573 9.436   0.34 25.88 ?  106 ILE   B N    1 
ATOM   5498 C CA   A ILE   B 1 106 ? 33.410 -28.697 8.083   0.66 24.31 ?  106 ILE   B CA   1 
ATOM   5499 C CA   B ILE   B 1 106 ? 33.376 -28.718 7.984   0.34 25.43 ?  106 ILE   B CA   1 
ATOM   5500 C C    A ILE   B 1 106 ? 32.312 -27.879 7.408   0.66 22.63 ?  106 ILE   B C    1 
ATOM   5501 C C    B ILE   B 1 106 ? 32.280 -27.886 7.329   0.34 24.57 ?  106 ILE   B C    1 
ATOM   5502 O O    A ILE   B 1 106 ? 32.414 -27.566 6.217   0.66 21.72 ?  106 ILE   B O    1 
ATOM   5503 O O    B ILE   B 1 106 ? 32.369 -27.575 6.136   0.34 24.05 ?  106 ILE   B O    1 
ATOM   5504 C CB   A ILE   B 1 106 ? 33.308 -30.206 7.755   0.66 25.67 ?  106 ILE   B CB   1 
ATOM   5505 C CB   B ILE   B 1 106 ? 33.273 -30.217 7.615   0.34 26.05 ?  106 ILE   B CB   1 
ATOM   5506 C CG1  A ILE   B 1 106 ? 33.573 -30.466 6.272   0.66 25.98 ?  106 ILE   B CG1  1 
ATOM   5507 C CG1  B ILE   B 1 106 ? 33.541 -30.437 6.123   0.34 26.09 ?  106 ILE   B CG1  1 
ATOM   5508 C CG2  A ILE   B 1 106 ? 31.945 -30.756 8.161   0.66 26.66 ?  106 ILE   B CG2  1 
ATOM   5509 C CG2  B ILE   B 1 106 ? 31.908 -30.771 7.998   0.34 26.64 ?  106 ILE   B CG2  1 
ATOM   5510 C CD1  A ILE   B 1 106 ? 34.940 -30.008 5.815   0.66 26.11 ?  106 ILE   B CD1  1 
ATOM   5511 C CD1  B ILE   B 1 106 ? 34.916 -29.991 5.682   0.34 26.17 ?  106 ILE   B CD1  1 
ATOM   5512 H H    A ILE   B 1 106 ? 33.318 -29.244 9.975   0.66 30.35 ?  106 ILE   B H    1 
ATOM   5513 H H    B ILE   B 1 106 ? 33.262 -29.310 9.860   0.34 31.03 ?  106 ILE   B H    1 
ATOM   5514 H HA   A ILE   B 1 106 ? 34.258 -28.378 7.743   0.66 29.14 ?  106 ILE   B HA   1 
ATOM   5515 H HA   B ILE   B 1 106 ? 34.222 -28.389 7.653   0.34 30.49 ?  106 ILE   B HA   1 
ATOM   5516 H HB   A ILE   B 1 106 ? 33.985 -30.673 8.269   0.66 30.78 ?  106 ILE   B HB   1 
ATOM   5517 H HB   B ILE   B 1 106 ? 33.946 -30.700 8.117   0.34 31.23 ?  106 ILE   B HB   1 
ATOM   5518 H HG12 A ILE   B 1 106 ? 33.513 -31.421 6.106   0.66 31.15 ?  106 ILE   B HG12 1 
ATOM   5519 H HG12 B ILE   B 1 106 ? 33.464 -31.386 5.929   0.34 31.28 ?  106 ILE   B HG12 1 
ATOM   5520 H HG13 A ILE   B 1 106 ? 32.911 -29.997 5.744   0.66 31.15 ?  106 ILE   B HG13 1 
ATOM   5521 H HG13 B ILE   B 1 106 ? 32.887 -29.944 5.607   0.34 31.28 ?  106 ILE   B HG13 1 
ATOM   5522 H HG21 A ILE   B 1 106 ? 31.957 -31.722 8.073   0.66 31.96 ?  106 ILE   B HG21 1 
ATOM   5523 H HG21 B ILE   B 1 106 ? 31.921 -31.736 7.900   0.34 31.94 ?  106 ILE   B HG21 1 
ATOM   5524 H HG22 A ILE   B 1 106 ? 31.769 -30.511 9.084   0.66 31.96 ?  106 ILE   B HG22 1 
ATOM   5525 H HG22 B ILE   B 1 106 ? 31.720 -30.536 8.920   0.34 31.94 ?  106 ILE   B HG22 1 
ATOM   5526 H HG23 A ILE   B 1 106 ? 31.265 -30.379 7.583   0.66 31.96 ?  106 ILE   B HG23 1 
ATOM   5527 H HG23 B ILE   B 1 106 ? 31.234 -30.389 7.415   0.34 31.94 ?  106 ILE   B HG23 1 
ATOM   5528 H HD11 A ILE   B 1 106 ? 35.143 -30.423 4.963   0.66 31.30 ?  106 ILE   B HD11 1 
ATOM   5529 H HD11 B ILE   B 1 106 ? 35.106 -30.374 4.812   0.34 31.38 ?  106 ILE   B HD11 1 
ATOM   5530 H HD12 A ILE   B 1 106 ? 34.936 -29.042 5.719   0.66 31.30 ?  106 ILE   B HD12 1 
ATOM   5531 H HD12 B ILE   B 1 106 ? 34.931 -29.023 5.628   0.34 31.38 ?  106 ILE   B HD12 1 
ATOM   5532 H HD13 A ILE   B 1 106 ? 35.600 -30.272 6.477   0.66 31.30 ?  106 ILE   B HD13 1 
ATOM   5533 H HD13 B ILE   B 1 106 ? 35.570 -30.299 6.329   0.34 31.38 ?  106 ILE   B HD13 1 
ATOM   5534 N N    A GLN   B 1 107 ? 31.266 -27.504 8.147   0.66 23.21 ?  107 GLN   B N    1 
ATOM   5535 N N    B GLN   B 1 107 ? 31.243 -27.515 8.083   0.34 24.75 ?  107 GLN   B N    1 
ATOM   5536 C CA   A GLN   B 1 107 ? 30.186 -26.713 7.566   0.66 23.93 ?  107 GLN   B CA   1 
ATOM   5537 C CA   B GLN   B 1 107 ? 30.165 -26.700 7.532   0.34 24.96 ?  107 GLN   B CA   1 
ATOM   5538 C C    A GLN   B 1 107 ? 30.671 -25.367 7.041   0.66 22.17 ?  107 GLN   B C    1 
ATOM   5539 C C    B GLN   B 1 107 ? 30.651 -25.336 7.053   0.34 22.72 ?  107 GLN   B C    1 
ATOM   5540 O O    A GLN   B 1 107 ? 30.035 -24.796 6.149   0.66 23.32 ?  107 GLN   B O    1 
ATOM   5541 O O    B GLN   B 1 107 ? 29.991 -24.718 6.213   0.34 23.38 ?  107 GLN   B O    1 
ATOM   5542 C CB   A GLN   B 1 107 ? 29.080 -26.511 8.606   0.66 27.96 ?  107 GLN   B CB   1 
ATOM   5543 C CB   B GLN   B 1 107 ? 29.058 -26.534 8.579   0.34 27.84 ?  107 GLN   B CB   1 
ATOM   5544 C CG   A GLN   B 1 107 ? 27.759 -25.996 8.045   0.66 32.05 ?  107 GLN   B CG   1 
ATOM   5545 C CG   B GLN   B 1 107 ? 27.715 -26.080 8.019   0.34 30.59 ?  107 GLN   B CG   1 
ATOM   5546 C CD   A GLN   B 1 107 ? 27.711 -24.484 7.932   0.66 35.14 ?  107 GLN   B CD   1 
ATOM   5547 C CD   B GLN   B 1 107 ? 27.588 -24.570 7.937   0.34 32.77 ?  107 GLN   B CD   1 
ATOM   5548 O OE1  A GLN   B 1 107 ? 28.551 -23.778 8.495   0.66 36.32 ?  107 GLN   B OE1  1 
ATOM   5549 O OE1  B GLN   B 1 107 ? 28.397 -23.833 8.503   0.34 33.60 ?  107 GLN   B OE1  1 
ATOM   5550 N NE2  A GLN   B 1 107 ? 26.722 -23.977 7.200   0.66 36.10 ?  107 GLN   B NE2  1 
ATOM   5551 N NE2  B GLN   B 1 107 ? 26.564 -24.101 7.230   0.34 33.46 ?  107 GLN   B NE2  1 
ATOM   5552 H H    A GLN   B 1 107 ? 31.167 -27.684 8.979   0.66 27.83 ?  107 GLN   B H    1 
ATOM   5553 H H    B GLN   B 1 107 ? 31.137 -27.727 8.907   0.34 29.67 ?  107 GLN   B H    1 
ATOM   5554 H HA   A GLN   B 1 107 ? 29.806 -27.208 6.822   0.66 28.68 ?  107 GLN   B HA   1 
ATOM   5555 H HA   B GLN   B 1 107 ? 29.780 -27.162 6.772   0.34 29.92 ?  107 GLN   B HA   1 
ATOM   5556 H HB2  A GLN   B 1 107 ? 28.902 -27.361 9.034   0.66 33.52 ?  107 GLN   B HB2  1 
ATOM   5557 H HB2  B GLN   B 1 107 ? 28.916 -27.387 9.016   0.34 33.38 ?  107 GLN   B HB2  1 
ATOM   5558 H HB3  A GLN   B 1 107 ? 29.389 -25.872 9.267   0.66 33.52 ?  107 GLN   B HB3  1 
ATOM   5559 H HB3  B GLN   B 1 107 ? 29.343 -25.878 9.234   0.34 33.38 ?  107 GLN   B HB3  1 
ATOM   5560 H HG2  A GLN   B 1 107 ? 27.624 -26.364 7.158   0.66 38.44 ?  107 GLN   B HG2  1 
ATOM   5561 H HG2  B GLN   B 1 107 ? 27.607 -26.437 7.124   0.34 36.68 ?  107 GLN   B HG2  1 
ATOM   5562 H HG3  A GLN   B 1 107 ? 27.035 -26.279 8.632   0.66 38.44 ?  107 GLN   B HG3  1 
ATOM   5563 H HG3  B GLN   B 1 107 ? 27.005 -26.412 8.594   0.34 36.68 ?  107 GLN   B HG3  1 
ATOM   5564 H HE21 A GLN   B 1 107 ? 26.155 -24.501 6.819   0.66 43.29 ?  107 GLN   B HE21 1 
ATOM   5565 H HE21 B GLN   B 1 107 ? 26.020 -24.646 6.847   0.34 40.12 ?  107 GLN   B HE21 1 
ATOM   5566 H HE22 A GLN   B 1 107 ? 26.646 -23.125 7.108   0.66 43.29 ?  107 GLN   B HE22 1 
ATOM   5567 H HE22 B GLN   B 1 107 ? 26.446 -23.252 7.156   0.34 40.12 ?  107 GLN   B HE22 1 
ATOM   5568 N N    . LEU   B 1 108 ? 31.788 -24.856 7.559   1.00 20.42 ?  108 LEU   B N    1 
ATOM   5569 C CA   . LEU   B 1 108 ? 32.336 -23.564 7.148   1.00 18.14 ?  108 LEU   B CA   1 
ATOM   5570 C C    . LEU   B 1 108 ? 32.986 -23.588 5.773   1.00 16.02 ?  108 LEU   B C    1 
ATOM   5571 O O    . LEU   B 1 108 ? 33.427 -22.534 5.291   1.00 15.23 ?  108 LEU   B O    1 
ATOM   5572 C CB   . LEU   B 1 108 ? 33.351 -23.086 8.184   1.00 18.69 ?  108 LEU   B CB   1 
ATOM   5573 C CG   . LEU   B 1 108 ? 32.717 -22.644 9.499   1.00 20.31 ?  108 LEU   B CG   1 
ATOM   5574 C CD1  . LEU   B 1 108 ? 33.736 -22.592 10.623  1.00 20.24 ?  108 LEU   B CD1  1 
ATOM   5575 C CD2  . LEU   B 1 108 ? 32.068 -21.283 9.314   1.00 21.69 ?  108 LEU   B CD2  1 
ATOM   5576 H H    A LEU   B 1 108 ? 32.244 -25.244 8.172   0.66 24.47 ?  108 LEU   B H    1 
ATOM   5577 H H    B LEU   B 1 108 ? 32.256 -25.261 8.152   0.34 24.47 ?  108 LEU   B H    1 
ATOM   5578 H HA   . LEU   B 1 108 ? 31.614 -22.918 7.122   1.00 21.75 ?  108 LEU   B HA   1 
ATOM   5579 H HB2  . LEU   B 1 108 ? 33.961 -23.811 8.382   1.00 22.40 ?  108 LEU   B HB2  1 
ATOM   5580 H HB3  . LEU   B 1 108 ? 33.836 -22.331 7.822   1.00 22.40 ?  108 LEU   B HB3  1 
ATOM   5581 H HG   . LEU   B 1 108 ? 32.021 -23.275 9.751   1.00 24.35 ?  108 LEU   B HG   1 
ATOM   5582 H HD11 . LEU   B 1 108 ? 33.292 -22.318 11.443  1.00 24.27 ?  108 LEU   B HD11 1 
ATOM   5583 H HD12 . LEU   B 1 108 ? 34.126 -23.472 10.738  1.00 24.27 ?  108 LEU   B HD12 1 
ATOM   5584 H HD13 . LEU   B 1 108 ? 34.427 -21.951 10.393  1.00 24.27 ?  108 LEU   B HD13 1 
ATOM   5585 H HD21 . LEU   B 1 108 ? 31.752 -20.962 10.173  1.00 26.00 ?  108 LEU   B HD21 1 
ATOM   5586 H HD22 . LEU   B 1 108 ? 32.725 -20.668 8.952   1.00 26.00 ?  108 LEU   B HD22 1 
ATOM   5587 H HD23 . LEU   B 1 108 ? 31.321 -21.368 8.699   1.00 26.00 ?  108 LEU   B HD23 1 
ATOM   5588 N N    . LEU   B 1 109 ? 33.055 -24.755 5.139   1.00 14.67 ?  109 LEU   B N    1 
ATOM   5589 C CA   . LEU   B 1 109 ? 33.695 -24.864 3.837   1.00 14.08 ?  109 LEU   B CA   1 
ATOM   5590 C C    . LEU   B 1 109 ? 32.940 -24.082 2.770   1.00 13.51 ?  109 LEU   B C    1 
ATOM   5591 O O    . LEU   B 1 109 ? 33.561 -23.486 1.884   1.00 13.22 ?  109 LEU   B O    1 
ATOM   5592 C CB   . LEU   B 1 109 ? 33.810 -26.339 3.461   1.00 14.11 ?  109 LEU   B CB   1 
ATOM   5593 C CG   . LEU   B 1 109 ? 34.601 -26.678 2.204   1.00 14.07 ?  109 LEU   B CG   1 
ATOM   5594 C CD1  . LEU   B 1 109 ? 35.983 -26.034 2.231   1.00 14.00 ?  109 LEU   B CD1  1 
ATOM   5595 C CD2  . LEU   B 1 109 ? 34.733 -28.183 2.063   1.00 14.50 ?  109 LEU   B CD2  1 
ATOM   5596 H H    . LEU   B 1 109 ? 32.743 -25.495 5.440   1.00 17.57 ?  109 LEU   B H    1 
ATOM   5597 H HA   . LEU   B 1 109 ? 34.587 -24.496 3.894   1.00 16.87 ?  109 LEU   B HA   1 
ATOM   5598 H HB2  . LEU   B 1 109 ? 34.235 -26.805 4.195   1.00 16.90 ?  109 LEU   B HB2  1 
ATOM   5599 H HB3  . LEU   B 1 109 ? 32.914 -26.691 3.334   1.00 16.90 ?  109 LEU   B HB3  1 
ATOM   5600 H HG   . LEU   B 1 109 ? 34.126 -26.346 1.422   1.00 16.86 ?  109 LEU   B HG   1 
ATOM   5601 H HD11 . LEU   B 1 109 ? 36.516 -26.399 1.508   1.00 16.77 ?  109 LEU   B HD11 1 
ATOM   5602 H HD12 . LEU   B 1 109 ? 35.886 -25.076 2.120   1.00 16.77 ?  109 LEU   B HD12 1 
ATOM   5603 H HD13 . LEU   B 1 109 ? 36.402 -26.231 3.083   1.00 16.77 ?  109 LEU   B HD13 1 
ATOM   5604 H HD21 . LEU   B 1 109 ? 35.295 -28.382 1.294   1.00 17.37 ?  109 LEU   B HD21 1 
ATOM   5605 H HD22 . LEU   B 1 109 ? 35.138 -28.541 2.867   1.00 17.37 ?  109 LEU   B HD22 1 
ATOM   5606 H HD23 . LEU   B 1 109 ? 33.853 -28.570 1.933   1.00 17.37 ?  109 LEU   B HD23 1 
ATOM   5607 N N    . LYS   B 1 110 ? 31.607 -24.047 2.839   1.00 13.43 ?  110 LYS   B N    1 
ATOM   5608 C CA   . LYS   B 1 110 ? 30.860 -23.283 1.845   1.00 12.95 ?  110 LYS   B CA   1 
ATOM   5609 C C    . LYS   B 1 110 ? 31.196 -21.793 1.939   1.00 12.64 ?  110 LYS   B C    1 
ATOM   5610 O O    . LYS   B 1 110 ? 31.447 -21.135 0.924   1.00 12.41 ?  110 LYS   B O    1 
ATOM   5611 C CB   . LYS   B 1 110 ? 29.354 -23.532 1.991   1.00 13.65 ?  110 LYS   B CB   1 
ATOM   5612 C CG   . LYS   B 1 110 ? 28.546 -22.891 0.868   1.00 14.67 ?  110 LYS   B CG   1 
ATOM   5613 C CD   . LYS   B 1 110 ? 27.082 -23.321 0.874   1.00 14.59 ?  110 LYS   B CD   1 
ATOM   5614 C CE   . LYS   B 1 110 ? 26.330 -22.797 -0.352  1.00 15.07 ?  110 LYS   B CE   1 
ATOM   5615 N NZ   . LYS   B 1 110 ? 26.669 -23.519 -1.602  1.00 15.09 ?  110 LYS   B NZ   1 
ATOM   5616 H H    . LYS   B 1 110 ? 31.127 -24.449 3.426   1.00 16.09 ?  110 LYS   B H    1 
ATOM   5617 H HA   . LYS   B 1 110 ? 31.117 -23.588 0.956   1.00 15.51 ?  110 LYS   B HA   1 
ATOM   5618 H HB2  . LYS   B 1 110 ? 29.186 -24.493 1.968   1.00 16.35 ?  110 LYS   B HB2  1 
ATOM   5619 H HB3  . LYS   B 1 110 ? 29.049 -23.165 2.833   1.00 16.35 ?  110 LYS   B HB3  1 
ATOM   5620 H HG2  . LYS   B 1 110 ? 28.566 -21.925 0.970   1.00 17.57 ?  110 LYS   B HG2  1 
ATOM   5621 H HG3  . LYS   B 1 110 ? 28.921 -23.142 0.012   1.00 17.57 ?  110 LYS   B HG3  1 
ATOM   5622 H HD2  . LYS   B 1 110 ? 27.026 -24.291 0.868   1.00 17.48 ?  110 LYS   B HD2  1 
ATOM   5623 H HD3  . LYS   B 1 110 ? 26.640 -22.969 1.666   1.00 17.48 ?  110 LYS   B HD3  1 
ATOM   5624 H HE2  . LYS   B 1 110 ? 25.376 -22.892 -0.207  1.00 18.06 ?  110 LYS   B HE2  1 
ATOM   5625 H HE3  . LYS   B 1 110 ? 26.554 -21.863 -0.481  1.00 18.06 ?  110 LYS   B HE3  1 
ATOM   5626 H HZ1  . LYS   B 1 110 ? 26.215 -23.181 -2.287  1.00 18.08 ?  110 LYS   B HZ1  1 
ATOM   5627 H HZ2  . LYS   B 1 110 ? 27.543 -23.445 -1.770  1.00 18.08 ?  110 LYS   B HZ2  1 
ATOM   5628 H HZ3  . LYS   B 1 110 ? 26.468 -24.384 -1.520  1.00 18.08 ?  110 LYS   B HZ3  1 
ATOM   5629 N N    . SER   B 1 111 ? 31.213 -21.247 3.158   1.00 13.45 ?  111 SER   B N    1 
ATOM   5630 C CA   . SER   B 1 111 ? 31.604 -19.850 3.340   1.00 13.27 ?  111 SER   B CA   1 
ATOM   5631 C C    . SER   B 1 111 ? 32.987 -19.586 2.760   1.00 12.63 ?  111 SER   B C    1 
ATOM   5632 O O    . SER   B 1 111 ? 33.217 -18.554 2.114   1.00 12.69 ?  111 SER   B O    1 
ATOM   5633 C CB   . SER   B 1 111 ? 31.590 -19.497 4.827   1.00 14.73 ?  111 SER   B CB   1 
ATOM   5634 O OG   . SER   B 1 111 ? 30.280 -19.517 5.354   1.00 15.96 ?  111 SER   B OG   1 
ATOM   5635 H H    . SER   B 1 111 ? 31.009 -21.667 3.880   1.00 16.11 ?  111 SER   B H    1 
ATOM   5636 H HA   . SER   B 1 111 ? 30.966 -19.281 2.883   1.00 15.90 ?  111 SER   B HA   1 
ATOM   5637 H HB2  . SER   B 1 111 ? 32.130 -20.144 5.306   1.00 17.65 ?  111 SER   B HB2  1 
ATOM   5638 H HB3  . SER   B 1 111 ? 31.956 -18.610 4.939   1.00 17.65 ?  111 SER   B HB3  1 
ATOM   5639 H HG   . SER   B 1 111 ? 30.296 -19.324 6.176   1.00 19.12 ?  111 SER   B HG   1 
ATOM   5640 N N    . ALA   B 1 112 ? 33.925 -20.504 2.989   1.00 12.57 ?  112 ALA   B N    1 
ATOM   5641 C CA   . ALA   B 1 112 ? 35.271 -20.338 2.450   1.00 12.27 ?  112 ALA   B CA   1 
ATOM   5642 C C    . ALA   B 1 112 ? 35.249 -20.241 0.927   1.00 11.60 ?  112 ALA   B C    1 
ATOM   5643 O O    . ALA   B 1 112 ? 35.883 -19.354 0.340   1.00 12.04 ?  112 ALA   B O    1 
ATOM   5644 C CB   . ALA   B 1 112 ? 36.172 -21.483 2.925   1.00 12.71 ?  112 ALA   B CB   1 
ATOM   5645 H H    . ALA   B 1 112 ? 33.812 -21.221 3.458   1.00 15.05 ?  112 ALA   B H    1 
ATOM   5646 H HA   . ALA   B 1 112 ? 35.640 -19.510 2.794   1.00 14.69 ?  112 ALA   B HA   1 
ATOM   5647 H HB1  . ALA   B 1 112 ? 37.064 -21.348 2.563   1.00 15.22 ?  112 ALA   B HB1  1 
ATOM   5648 H HB2  . ALA   B 1 112 ? 36.211 -21.471 3.897   1.00 15.22 ?  112 ALA   B HB2  1 
ATOM   5649 H HB3  . ALA   B 1 112 ? 35.810 -22.322 2.617   1.00 15.22 ?  112 ALA   B HB3  1 
ATOM   5650 N N    . TYR   B 1 113 ? 34.519 -21.147 0.266   1.00 11.87 ?  113 TYR   B N    1 
ATOM   5651 C CA   . TYR   B 1 113 ? 34.444 -21.101 -1.191  1.00 11.45 ?  113 TYR   B CA   1 
ATOM   5652 C C    . TYR   B 1 113 ? 33.743 -19.848 -1.705  1.00 11.08 ?  113 TYR   B C    1 
ATOM   5653 O O    . TYR   B 1 113 ? 34.021 -19.412 -2.826  1.00 11.25 ?  113 TYR   B O    1 
ATOM   5654 C CB   . TYR   B 1 113 ? 33.765 -22.353 -1.743  1.00 11.82 ?  113 TYR   B CB   1 
ATOM   5655 C CG   . TYR   B 1 113 ? 34.730 -23.506 -1.996  1.00 12.20 ?  113 TYR   B CG   1 
ATOM   5656 C CD1  . TYR   B 1 113 ? 35.723 -23.403 -2.965  1.00 12.66 ?  113 TYR   B CD1  1 
ATOM   5657 C CD2  . TYR   B 1 113 ? 34.634 -24.692 -1.286  1.00 12.33 ?  113 TYR   B CD2  1 
ATOM   5658 C CE1  . TYR   B 1 113 ? 36.609 -24.441 -3.204  1.00 12.87 ?  113 TYR   B CE1  1 
ATOM   5659 C CE2  . TYR   B 1 113 ? 35.508 -25.747 -1.524  1.00 12.59 ?  113 TYR   B CE2  1 
ATOM   5660 C CZ   . TYR   B 1 113 ? 36.487 -25.619 -2.491  1.00 12.74 ?  113 TYR   B CZ   1 
ATOM   5661 O OH   . TYR   B 1 113 ? 37.374 -26.641 -2.758  1.00 13.55 ?  113 TYR   B OH   1 
ATOM   5662 H H    . TYR   B 1 113 ? 34.060 -21.781 0.636   1.00 14.22 ?  113 TYR   B H    1 
ATOM   5663 H HA   . TYR   B 1 113 ? 35.347 -21.086 -1.528  1.00 13.72 ?  113 TYR   B HA   1 
ATOM   5664 H HB2  . TYR   B 1 113 ? 33.101 -22.663 -1.106  1.00 14.15 ?  113 TYR   B HB2  1 
ATOM   5665 H HB3  . TYR   B 1 113 ? 33.337 -22.131 -2.583  1.00 14.15 ?  113 TYR   B HB3  1 
ATOM   5666 H HD1  . TYR   B 1 113 ? 35.807 -22.613 -3.455  1.00 15.16 ?  113 TYR   B HD1  1 
ATOM   5667 H HD2  . TYR   B 1 113 ? 33.969 -24.782 -0.645  1.00 14.77 ?  113 TYR   B HD2  1 
ATOM   5668 H HE1  . TYR   B 1 113 ? 37.265 -24.360 -3.862  1.00 15.42 ?  113 TYR   B HE1  1 
ATOM   5669 H HE2  . TYR   B 1 113 ? 35.424 -26.538 -1.047  1.00 15.08 ?  113 TYR   B HE2  1 
ATOM   5670 H HH   . TYR   B 1 113 ? 37.168 -27.319 -2.304  1.00 16.24 ?  113 TYR   B HH   1 
ATOM   5671 N N    . GLU   B 1 114 ? 32.820 -19.270 -0.927  1.00 11.24 ?  114 GLU   B N    1 
ATOM   5672 C CA   . GLU   B 1 114 ? 32.141 -18.060 -1.381  1.00 11.17 ?  114 GLU   B CA   1 
ATOM   5673 C C    . GLU   B 1 114 ? 33.124 -16.941 -1.684  1.00 11.19 ?  114 GLU   B C    1 
ATOM   5674 O O    . GLU   B 1 114 ? 32.845 -16.082 -2.523  1.00 11.44 ?  114 GLU   B O    1 
ATOM   5675 C CB   . GLU   B 1 114 ? 31.084 -17.628 -0.363  1.00 12.10 ?  114 GLU   B CB   1 
ATOM   5676 C CG   . GLU   B 1 114 ? 29.856 -18.544 -0.432  1.00 12.23 ?  114 GLU   B CG   1 
ATOM   5677 C CD   . GLU   B 1 114 ? 28.839 -18.351 0.673   1.00 12.32 ?  114 GLU   B CD   1 
ATOM   5678 O OE1  . GLU   B 1 114 ? 29.125 -17.728 1.715   1.00 12.43 ?  114 GLU   B OE1  1 
ATOM   5679 O OE2  . GLU   B 1 114 ? 27.716 -18.884 0.505   1.00 13.46 -1 114 GLU   B OE2  1 
ATOM   5680 H H    . GLU   B 1 114 ? 32.566 -19.563 -0.158  1.00 13.46 ?  114 GLU   B H    1 
ATOM   5681 H HA   . GLU   B 1 114 ? 31.679 -18.258 -2.206  1.00 13.37 ?  114 GLU   B HA   1 
ATOM   5682 H HB2  . GLU   B 1 114 ? 31.456 -17.684 0.533   1.00 14.49 ?  114 GLU   B HB2  1 
ATOM   5683 H HB3  . GLU   B 1 114 ? 30.799 -16.724 -0.555  1.00 14.49 ?  114 GLU   B HB3  1 
ATOM   5684 H HG2  . GLU   B 1 114 ? 29.406 -18.390 -1.272  1.00 14.65 ?  114 GLU   B HG2  1 
ATOM   5685 H HG3  . GLU   B 1 114 ? 30.161 -19.467 -0.389  1.00 14.65 ?  114 GLU   B HG3  1 
ATOM   5686 N N    . ASN   B 1 115 ? 34.287 -16.939 -1.031  1.00 11.06 ?  115 ASN   B N    1 
ATOM   5687 C CA   . ASN   B 1 115 ? 35.278 -15.905 -1.322  1.00 10.97 ?  115 ASN   B CA   1 
ATOM   5688 C C    . ASN   B 1 115 ? 35.691 -15.925 -2.785  1.00 10.82 ?  115 ASN   B C    1 
ATOM   5689 O O    . ASN   B 1 115 ? 36.085 -14.888 -3.335  1.00 11.29 ?  115 ASN   B O    1 
ATOM   5690 C CB   . ASN   B 1 115 ? 36.510 -16.081 -0.431  1.00 11.93 ?  115 ASN   B CB   1 
ATOM   5691 C CG   . ASN   B 1 115 ? 36.230 -15.821 1.030   1.00 12.52 ?  115 ASN   B CG   1 
ATOM   5692 O OD1  . ASN   B 1 115 ? 36.205 -14.677 1.472   1.00 14.40 ?  115 ASN   B OD1  1 
ATOM   5693 N ND2  . ASN   B 1 115 ? 36.071 -16.889 1.804   1.00 12.22 ?  115 ASN   B ND2  1 
ATOM   5694 H H    . ASN   B 1 115 ? 34.525 -17.506 -0.420  1.00 13.24 ?  115 ASN   B H    1 
ATOM   5695 H HA   . ASN   B 1 115 ? 34.899 -15.036 -1.129  1.00 13.13 ?  115 ASN   B HA   1 
ATOM   5696 H HB2  . ASN   B 1 115 ? 36.842 -16.989 -0.517  1.00 14.29 ?  115 ASN   B HB2  1 
ATOM   5697 H HB3  . ASN   B 1 115 ? 37.199 -15.454 -0.713  1.00 14.29 ?  115 ASN   B HB3  1 
ATOM   5698 H HD21 . ASN   B 1 115 ? 35.919 -16.792 2.646   1.00 14.64 ?  115 ASN   B HD21 1 
ATOM   5699 H HD22 . ASN   B 1 115 ? 36.104 -17.680 1.465   1.00 14.64 ?  115 ASN   B HD22 1 
ATOM   5700 N N    . PHE   B 1 116 ? 35.668 -17.101 -3.418  1.00 10.67 ?  116 PHE   B N    1 
ATOM   5701 C CA   . PHE   B 1 116 ? 36.104 -17.197 -4.805  1.00 10.98 ?  116 PHE   B CA   1 
ATOM   5702 C C    . PHE   B 1 116 ? 35.207 -16.370 -5.722  1.00 10.81 ?  116 PHE   B C    1 
ATOM   5703 O O    . PHE   B 1 116 ? 35.645 -15.945 -6.794  1.00 11.37 ?  116 PHE   B O    1 
ATOM   5704 C CB   . PHE   B 1 116 ? 36.078 -18.643 -5.325  1.00 10.69 ?  116 PHE   B CB   1 
ATOM   5705 C CG   . PHE   B 1 116 ? 37.142 -19.593 -4.770  1.00 10.71 ?  116 PHE   B CG   1 
ATOM   5706 C CD1  . PHE   B 1 116 ? 37.787 -19.413 -3.555  1.00 11.56 ?  116 PHE   B CD1  1 
ATOM   5707 C CD2  . PHE   B 1 116 ? 37.443 -20.732 -5.503  1.00 10.92 ?  116 PHE   B CD2  1 
ATOM   5708 C CE1  . PHE   B 1 116 ? 38.715 -20.349 -3.098  1.00 11.85 ?  116 PHE   B CE1  1 
ATOM   5709 C CE2  . PHE   B 1 116 ? 38.362 -21.669 -5.052  1.00 11.21 ?  116 PHE   B CE2  1 
ATOM   5710 C CZ   . PHE   B 1 116 ? 38.993 -21.483 -3.852  1.00 11.44 ?  116 PHE   B CZ   1 
ATOM   5711 H H    . PHE   B 1 116 ? 35.399 -17.844 -3.074  1.00 12.78 ?  116 PHE   B H    1 
ATOM   5712 H HA   . PHE   B 1 116 ? 37.011 -16.866 -4.884  1.00 13.15 ?  116 PHE   B HA   1 
ATOM   5713 H HB2  . PHE   B 1 116 ? 35.206 -19.023 -5.114  1.00 12.80 ?  116 PHE   B HB2  1 
ATOM   5714 H HB3  . PHE   B 1 116 ? 36.183 -18.620 -6.291  1.00 12.80 ?  116 PHE   B HB3  1 
ATOM   5715 H HD1  . PHE   B 1 116 ? 37.589 -18.662 -3.038  1.00 13.85 ?  116 PHE   B HD1  1 
ATOM   5716 H HD2  . PHE   B 1 116 ? 37.007 -20.879 -6.312  1.00 13.08 ?  116 PHE   B HD2  1 
ATOM   5717 H HE1  . PHE   B 1 116 ? 39.146 -20.217 -2.284  1.00 14.20 ?  116 PHE   B HE1  1 
ATOM   5718 H HE2  . PHE   B 1 116 ? 38.550 -22.419 -5.565  1.00 13.43 ?  116 PHE   B HE2  1 
ATOM   5719 H HZ   . PHE   B 1 116 ? 39.622 -22.096 -3.554  1.00 13.71 ?  116 PHE   B HZ   1 
ATOM   5720 N N    . ASN   B 1 117 ? 33.936 -16.170 -5.345  1.00 11.18 ?  117 ASN   B N    1 
ATOM   5721 C CA   . ASN   B 1 117 ? 32.997 -15.468 -6.217  1.00 11.45 ?  117 ASN   B CA   1 
ATOM   5722 C C    . ASN   B 1 117 ? 33.315 -13.990 -6.367  1.00 12.24 ?  117 ASN   B C    1 
ATOM   5723 O O    . ASN   B 1 117 ? 32.723 -13.335 -7.228  1.00 12.84 ?  117 ASN   B O    1 
ATOM   5724 C CB   . ASN   B 1 117 ? 31.579 -15.689 -5.717  1.00 11.53 ?  117 ASN   B CB   1 
ATOM   5725 C CG   . ASN   B 1 117 ? 31.119 -17.094 -5.971  1.00 11.92 ?  117 ASN   B CG   1 
ATOM   5726 O OD1  . ASN   B 1 117 ? 31.470 -17.686 -6.996  1.00 13.02 ?  117 ASN   B OD1  1 
ATOM   5727 N ND2  . ASN   B 1 117 ? 30.373 -17.660 -5.034  1.00 12.13 ?  117 ASN   B ND2  1 
ATOM   5728 H H    . ASN   B 1 117 ? 33.607 -16.430 -4.592  1.00 13.39 ?  117 ASN   B H    1 
ATOM   5729 H HA   . ASN   B 1 117 ? 33.059 -15.869 -7.097  1.00 13.71 ?  117 ASN   B HA   1 
ATOM   5730 H HB2  . ASN   B 1 117 ? 31.550 -15.526 -4.759  1.00 13.81 ?  117 ASN   B HB2  1 
ATOM   5731 H HB3  . ASN   B 1 117 ? 30.985 -15.075 -6.177  1.00 13.81 ?  117 ASN   B HB3  1 
ATOM   5732 H HD21 . ASN   B 1 117 ? 30.086 -18.462 -5.140  1.00 14.52 ?  117 ASN   B HD21 1 
ATOM   5733 H HD22 . ASN   B 1 117 ? 30.160 -17.216 -4.329  1.00 14.52 ?  117 ASN   B HD22 1 
ATOM   5734 N N    . GLN   B 1 118 ? 34.255 -13.467 -5.590  1.00 11.39 ?  118 GLN   B N    1 
ATOM   5735 C CA   . GLN   B 1 118 ? 34.682 -12.078 -5.727  1.00 12.24 ?  118 GLN   B CA   1 
ATOM   5736 C C    . GLN   B 1 118 ? 35.745 -11.887 -6.805  1.00 12.32 ?  118 GLN   B C    1 
ATOM   5737 O O    . GLN   B 1 118 ? 36.223 -10.762 -6.989  1.00 13.58 ?  118 GLN   B O    1 
ATOM   5738 C CB   . GLN   B 1 118 ? 35.162 -11.542 -4.374  1.00 12.82 ?  118 GLN   B CB   1 
ATOM   5739 C CG   . GLN   B 1 118 ? 34.080 -11.591 -3.307  1.00 12.66 ?  118 GLN   B CG   1 
ATOM   5740 C CD   . GLN   B 1 118 ? 32.913 -10.668 -3.625  1.00 12.82 ?  118 GLN   B CD   1 
ATOM   5741 O OE1  . GLN   B 1 118 ? 33.104 -9.522  -4.043  1.00 13.27 ?  118 GLN   B OE1  1 
ATOM   5742 N NE2  . GLN   B 1 118 ? 31.702 -11.165 -3.441  1.00 13.10 ?  118 GLN   B NE2  1 
ATOM   5743 H H    . GLN   B 1 118 ? 34.684 -13.897 -4.975  1.00 13.64 ?  118 GLN   B H    1 
ATOM   5744 H HA   . GLN   B 1 118 ? 33.917 -11.551 -5.996  1.00 14.66 ?  118 GLN   B HA   1 
ATOM   5745 H HB2  . GLN   B 1 118 ? 35.914 -12.071 -4.070  1.00 15.36 ?  118 GLN   B HB2  1 
ATOM   5746 H HB3  . GLN   B 1 118 ? 35.436 -10.613 -4.481  1.00 15.36 ?  118 GLN   B HB3  1 
ATOM   5747 H HG2  . GLN   B 1 118 ? 33.743 -12.498 -3.245  1.00 15.17 ?  118 GLN   B HG2  1 
ATOM   5748 H HG3  . GLN   B 1 118 ? 34.463 -11.318 -2.460  1.00 15.17 ?  118 GLN   B HG3  1 
ATOM   5749 H HE21 . GLN   B 1 118 ? 31.612 -11.968 -3.149  1.00 15.70 ?  118 GLN   B HE21 1 
ATOM   5750 H HE22 . GLN   B 1 118 ? 31.018 -10.682 -3.611  1.00 15.70 ?  118 GLN   B HE22 1 
ATOM   5751 N N    . HIS   B 1 119 ? 36.100 -12.948 -7.532  1.00 11.73 ?  119 HIS   B N    1 
ATOM   5752 C CA   . HIS   B 1 119 ? 37.151 -12.908 -8.541  1.00 11.79 ?  119 HIS   B CA   1 
ATOM   5753 C C    . HIS   B 1 119 ? 36.673 -13.641 -9.779  1.00 11.79 ?  119 HIS   B C    1 
ATOM   5754 O O    . HIS   B 1 119 ? 36.163 -14.759 -9.675  1.00 12.51 ?  119 HIS   B O    1 
ATOM   5755 C CB   . HIS   B 1 119 ? 38.425 -13.544 -7.986  1.00 12.57 ?  119 HIS   B CB   1 
ATOM   5756 C CG   . HIS   B 1 119 ? 38.907 -12.845 -6.763  1.00 13.55 ?  119 HIS   B CG   1 
ATOM   5757 N ND1  . HIS   B 1 119 ? 39.720 -11.732 -6.820  1.00 15.20 ?  119 HIS   B ND1  1 
ATOM   5758 C CD2  . HIS   B 1 119 ? 38.604 -13.027 -5.458  1.00 14.86 ?  119 HIS   B CD2  1 
ATOM   5759 C CE1  . HIS   B 1 119 ? 39.928 -11.286 -5.595  1.00 16.65 ?  119 HIS   B CE1  1 
ATOM   5760 N NE2  . HIS   B 1 119 ? 39.258 -12.049 -4.751  1.00 16.68 ?  119 HIS   B NE2  1 
ATOM   5761 H H    . HIS   B 1 119 ? 35.730 -13.724 -7.462  1.00 14.05 ?  119 HIS   B H    1 
ATOM   5762 H HA   . HIS   B 1 119 ? 37.337 -11.983 -8.783  1.00 14.12 ?  119 HIS   B HA   1 
ATOM   5763 H HB2  . HIS   B 1 119 ? 38.244 -14.468 -7.764  1.00 15.06 ?  119 HIS   B HB2  1 
ATOM   5764 H HB3  . HIS   B 1 119 ? 39.122 -13.494 -8.664  1.00 15.06 ?  119 HIS   B HB3  1 
ATOM   5765 H HD2  . HIS   B 1 119 ? 38.056 -13.694 -5.109  1.00 17.81 ?  119 HIS   B HD2  1 
ATOM   5766 H HE1  . HIS   B 1 119 ? 40.468 -10.567 -5.363  1.00 19.95 ?  119 HIS   B HE1  1 
ATOM   5767 H HE2  . HIS   B 1 119 ? 39.254 -11.966 -3.896  1.00 19.99 ?  119 HIS   B HE2  1 
ATOM   5768 N N    . GLU   B 1 120 ? 36.836 -13.027 -10.953 1.00 12.48 ?  120 GLU   B N    1 
ATOM   5769 C CA   . GLU   B 1 120 ? 36.244 -13.615 -12.150 1.00 14.25 ?  120 GLU   B CA   1 
ATOM   5770 C C    . GLU   B 1 120 ? 36.921 -14.915 -12.563 1.00 13.09 ?  120 GLU   B C    1 
ATOM   5771 O O    . GLU   B 1 120 ? 36.260 -15.787 -13.134 1.00 13.40 ?  120 GLU   B O    1 
ATOM   5772 C CB   . GLU   B 1 120 ? 36.238 -12.610 -13.301 1.00 18.83 ?  120 GLU   B CB   1 
ATOM   5773 C CG   . GLU   B 1 120 ? 35.285 -11.453 -13.070 1.00 25.02 ?  120 GLU   B CG   1 
ATOM   5774 C CD   . GLU   B 1 120 ? 35.120 -10.566 -14.288 1.00 32.37 ?  120 GLU   B CD   1 
ATOM   5775 O OE1  . GLU   B 1 120 ? 36.108 -10.381 -15.031 1.00 35.08 ?  120 GLU   B OE1  1 
ATOM   5776 O OE2  . GLU   B 1 120 ? 34.000 -10.056 -14.501 1.00 35.63 -1 120 GLU   B OE2  1 
ATOM   5777 H H    . GLU   B 1 120 ? 37.274 -12.294 -11.085 1.00 14.94 ?  120 GLU   B H    1 
ATOM   5778 H HA   . GLU   B 1 120 ? 35.324 -13.833 -11.955 1.00 17.08 ?  120 GLU   B HA   1 
ATOM   5779 H HB2  . GLU   B 1 120 ? 37.126 -12.245 -13.414 1.00 22.57 ?  120 GLU   B HB2  1 
ATOM   5780 H HB3  . GLU   B 1 120 ? 35.960 -13.063 -14.117 1.00 22.57 ?  120 GLU   B HB3  1 
ATOM   5781 H HG2  . GLU   B 1 120 ? 34.409 -11.805 -12.838 1.00 30.00 ?  120 GLU   B HG2  1 
ATOM   5782 H HG3  . GLU   B 1 120 ? 35.622 -10.906 -12.346 1.00 30.00 ?  120 GLU   B HG3  1 
ATOM   5783 N N    . VAL   B 1 121 ? 38.218 -15.059 -12.297 1.00 12.51 ?  121 VAL   B N    1 
ATOM   5784 C CA   . VAL   B 1 121 ? 38.962 -16.267 -12.642 1.00 12.11 ?  121 VAL   B CA   1 
ATOM   5785 C C    . VAL   B 1 121 ? 40.074 -16.466 -11.623 1.00 11.56 ?  121 VAL   B C    1 
ATOM   5786 O O    . VAL   B 1 121 ? 40.753 -15.507 -11.237 1.00 12.35 ?  121 VAL   B O    1 
ATOM   5787 C CB   . VAL   B 1 121 ? 39.478 -16.230 -14.100 1.00 13.78 ?  121 VAL   B CB   1 
ATOM   5788 C CG1  . VAL   B 1 121 ? 40.354 -15.007 -14.354 1.00 15.25 ?  121 VAL   B CG1  1 
ATOM   5789 C CG2  . VAL   B 1 121 ? 40.218 -17.522 -14.446 1.00 15.22 ?  121 VAL   B CG2  1 
ATOM   5790 H H    . VAL   B 1 121 ? 38.705 -14.455 -11.926 1.00 14.99 ?  121 VAL   B H    1 
ATOM   5791 H HA   . VAL   B 1 121 ? 38.360 -17.023 -12.573 1.00 14.50 ?  121 VAL   B HA   1 
ATOM   5792 H HB   . VAL   B 1 121 ? 38.713 -16.172 -14.697 1.00 16.51 ?  121 VAL   B HB   1 
ATOM   5793 H HG11 . VAL   B 1 121 ? 40.658 -15.022 -15.276 1.00 18.27 ?  121 VAL   B HG11 1 
ATOM   5794 H HG12 . VAL   B 1 121 ? 39.830 -14.208 -14.193 1.00 18.27 ?  121 VAL   B HG12 1 
ATOM   5795 H HG13 . VAL   B 1 121 ? 41.114 -15.034 -13.754 1.00 18.27 ?  121 VAL   B HG13 1 
ATOM   5796 H HG21 . VAL   B 1 121 ? 40.418 -17.528 -15.399 1.00 18.24 ?  121 VAL   B HG21 1 
ATOM   5797 H HG22 . VAL   B 1 121 ? 41.044 -17.562 -13.939 1.00 18.24 ?  121 VAL   B HG22 1 
ATOM   5798 H HG23 . VAL   B 1 121 ? 39.656 -18.281 -14.226 1.00 18.24 ?  121 VAL   B HG23 1 
ATOM   5799 N N    . LEU   B 1 122 ? 40.257 -17.715 -11.184 1.00 11.32 ?  122 LEU   B N    1 
ATOM   5800 C CA   . LEU   B 1 122 ? 41.231 -18.064 -10.153 1.00 10.82 ?  122 LEU   B CA   1 
ATOM   5801 C C    . LEU   B 1 122 ? 41.888 -19.394 -10.472 1.00 10.94 ?  122 LEU   B C    1 
ATOM   5802 O O    . LEU   B 1 122 ? 41.229 -20.314 -10.970 1.00 12.22 ?  122 LEU   B O    1 
ATOM   5803 C CB   . LEU   B 1 122 ? 40.566 -18.297 -8.785  1.00 13.03 ?  122 LEU   B CB   1 
ATOM   5804 C CG   . LEU   B 1 122 ? 39.549 -17.264 -8.292  1.00 13.05 ?  122 LEU   B CG   1 
ATOM   5805 C CD1  . LEU   B 1 122 ? 38.152 -17.632 -8.762  1.00 13.82 ?  122 LEU   B CD1  1 
ATOM   5806 C CD2  . LEU   B 1 122 ? 39.587 -17.148 -6.781  1.00 12.49 ?  122 LEU   B CD2  1 
ATOM   5807 H H    . LEU   B 1 122 ? 39.818 -18.396 -11.475 1.00 13.56 ?  122 LEU   B H    1 
ATOM   5808 H HA   . LEU   B 1 122 ? 41.911 -17.373 -10.072 1.00 12.96 ?  122 LEU   B HA   1 
ATOM   5809 H HB2  . LEU   B 1 122 ? 40.108 -19.149 -8.821  1.00 15.61 ?  122 LEU   B HB2  1 
ATOM   5810 H HB3  . LEU   B 1 122 ? 41.266 -18.339 -8.117  1.00 15.61 ?  122 LEU   B HB3  1 
ATOM   5811 H HG   . LEU   B 1 122 ? 39.767 -16.396 -8.663  1.00 15.64 ?  122 LEU   B HG   1 
ATOM   5812 H HD11 . LEU   B 1 122 ? 37.523 -16.972 -8.424  1.00 16.56 ?  122 LEU   B HD11 1 
ATOM   5813 H HD12 . LEU   B 1 122 ? 38.136 -17.631 -9.733  1.00 16.56 ?  122 LEU   B HD12 1 
ATOM   5814 H HD13 . LEU   B 1 122 ? 37.924 -18.508 -8.425  1.00 16.56 ?  122 LEU   B HD13 1 
ATOM   5815 H HD21 . LEU   B 1 122 ? 38.917 -16.509 -6.491  1.00 14.96 ?  122 LEU   B HD21 1 
ATOM   5816 H HD22 . LEU   B 1 122 ? 39.405 -18.018 -6.390  1.00 14.96 ?  122 LEU   B HD22 1 
ATOM   5817 H HD23 . LEU   B 1 122 ? 40.470 -16.844 -6.510  1.00 14.96 ?  122 LEU   B HD23 1 
ATOM   5818 N N    . LEU   B 1 123 ? 43.173 -19.502 -10.118 1.00 10.59 ?  123 LEU   B N    1 
ATOM   5819 C CA   . LEU   B 1 123 ? 43.884 -20.771 -9.990  1.00 10.83 ?  123 LEU   B CA   1 
ATOM   5820 C C    . LEU   B 1 123 ? 43.853 -21.160 -8.517  1.00 10.79 ?  123 LEU   B C    1 
ATOM   5821 O O    . LEU   B 1 123 ? 44.202 -20.340 -7.663  1.00 11.10 ?  123 LEU   B O    1 
ATOM   5822 C CB   . LEU   B 1 123 ? 45.332 -20.591 -10.454 1.00 11.36 ?  123 LEU   B CB   1 
ATOM   5823 C CG   . LEU   B 1 123 ? 46.276 -21.770 -10.202 1.00 11.67 ?  123 LEU   B CG   1 
ATOM   5824 C CD1  . LEU   B 1 123 ? 45.863 -23.015 -10.990 1.00 12.50 ?  123 LEU   B CD1  1 
ATOM   5825 C CD2  . LEU   B 1 123 ? 47.699 -21.376 -10.553 1.00 12.53 ?  123 LEU   B CD2  1 
ATOM   5826 H H    . LEU   B 1 123 ? 43.669 -18.824 -9.930  1.00 12.68 ?  123 LEU   B H    1 
ATOM   5827 H HA   . LEU   B 1 123 ? 43.451 -21.463 -10.517 1.00 12.96 ?  123 LEU   B HA   1 
ATOM   5828 H HB2  . LEU   B 1 123 ? 45.321 -20.433 -11.410 1.00 13.60 ?  123 LEU   B HB2  1 
ATOM   5829 H HB3  . LEU   B 1 123 ? 45.701 -19.824 -10.000 1.00 13.60 ?  123 LEU   B HB3  1 
ATOM   5830 H HG   . LEU   B 1 123 ? 46.257 -22.001 -9.257  1.00 13.98 ?  123 LEU   B HG   1 
ATOM   5831 H HD11 . LEU   B 1 123 ? 46.498 -23.724 -10.809 1.00 14.97 ?  123 LEU   B HD11 1 
ATOM   5832 H HD12 . LEU   B 1 123 ? 44.975 -23.283 -10.710 1.00 14.97 ?  123 LEU   B HD12 1 
ATOM   5833 H HD13 . LEU   B 1 123 ? 45.865 -22.798 -11.934 1.00 14.97 ?  123 LEU   B HD13 1 
ATOM   5834 H HD21 . LEU   B 1 123 ? 48.285 -22.131 -10.388 1.00 15.01 ?  123 LEU   B HD21 1 
ATOM   5835 H HD22 . LEU   B 1 123 ? 47.733 -21.127 -11.489 1.00 15.01 ?  123 LEU   B HD22 1 
ATOM   5836 H HD23 . LEU   B 1 123 ? 47.962 -20.625 -9.999  1.00 15.01 ?  123 LEU   B HD23 1 
ATOM   5837 N N    . ALA   B 1 124 ? 43.418 -22.388 -8.211  1.00 10.67 ?  124 ALA   B N    1 
ATOM   5838 C CA   . ALA   B 1 124 ? 43.160 -22.711 -6.816  1.00 10.70 ?  124 ALA   B CA   1 
ATOM   5839 C C    . ALA   B 1 124 ? 43.424 -24.170 -6.480  1.00 10.66 ?  124 ALA   B C    1 
ATOM   5840 O O    . ALA   B 1 124 ? 43.297 -25.044 -7.346  1.00 11.13 ?  124 ALA   B O    1 
ATOM   5841 C CB   . ALA   B 1 124 ? 41.702 -22.391 -6.456  1.00 11.27 ?  124 ALA   B CB   1 
ATOM   5842 H H    . ALA   B 1 124 ? 43.250 -23.020 -8.772  1.00 12.78 ?  124 ALA   B H    1 
ATOM   5843 H HA   . ALA   B 1 124 ? 43.732 -22.161 -6.263  1.00 12.82 ?  124 ALA   B HA   1 
ATOM   5844 H HB1  . ALA   B 1 124 ? 41.540 -22.612 -5.528  1.00 13.50 ?  124 ALA   B HB1  1 
ATOM   5845 H HB2  . ALA   B 1 124 ? 41.541 -21.444 -6.605  1.00 13.50 ?  124 ALA   B HB2  1 
ATOM   5846 H HB3  . ALA   B 1 124 ? 41.111 -22.914 -7.028  1.00 13.50 ?  124 ALA   B HB3  1 
ATOM   5847 N N    . PRO   B 1 125 ? 43.720 -24.459 -5.216  1.00 10.79 ?  125 PRO   B N    1 
ATOM   5848 C CA   . PRO   B 1 125 ? 43.656 -25.820 -4.684  1.00 11.69 ?  125 PRO   B CA   1 
ATOM   5849 C C    . PRO   B 1 125 ? 42.254 -26.098 -4.148  1.00 11.59 ?  125 PRO   B C    1 
ATOM   5850 O O    . PRO   B 1 125 ? 41.461 -25.183 -3.930  1.00 11.93 ?  125 PRO   B O    1 
ATOM   5851 C CB   . PRO   B 1 125 ? 44.631 -25.738 -3.502  1.00 12.69 ?  125 PRO   B CB   1 
ATOM   5852 C CG   . PRO   B 1 125 ? 44.372 -24.353 -2.938  1.00 12.44 ?  125 PRO   B CG   1 
ATOM   5853 C CD   . PRO   B 1 125 ? 44.046 -23.487 -4.153  1.00 11.61 ?  125 PRO   B CD   1 
ATOM   5854 H HA   . PRO   B 1 125 ? 43.941 -26.488 -5.327  1.00 14.00 ?  125 PRO   B HA   1 
ATOM   5855 H HB2  . PRO   B 1 125 ? 44.419 -26.421 -2.844  1.00 15.20 ?  125 PRO   B HB2  1 
ATOM   5856 H HB3  . PRO   B 1 125 ? 45.543 -25.818 -3.810  1.00 15.20 ?  125 PRO   B HB3  1 
ATOM   5857 H HG2  . PRO   B 1 125 ? 43.612 -24.374 -2.325  1.00 14.90 ?  125 PRO   B HG2  1 
ATOM   5858 H HG3  . PRO   B 1 125 ? 45.161 -24.020 -2.480  1.00 14.90 ?  125 PRO   B HG3  1 
ATOM   5859 H HD2  . PRO   B 1 125 ? 43.284 -22.910 -3.969  1.00 13.90 ?  125 PRO   B HD2  1 
ATOM   5860 H HD3  . PRO   B 1 125 ? 44.825 -22.958 -4.405  1.00 13.90 ?  125 PRO   B HD3  1 
ATOM   5861 N N    . LEU   B 1 126 ? 41.977 -27.377 -3.882  1.00 12.04 ?  126 LEU   B N    1 
ATOM   5862 C CA   . LEU   B 1 126 ? 40.753 -27.738 -3.174  1.00 12.57 ?  126 LEU   B CA   1 
ATOM   5863 C C    . LEU   B 1 126 ? 40.862 -27.337 -1.711  1.00 13.00 ?  126 LEU   B C    1 
ATOM   5864 O O    . LEU   B 1 126 ? 41.751 -27.798 -0.988  1.00 14.53 ?  126 LEU   B O    1 
ATOM   5865 C CB   . LEU   B 1 126 ? 40.486 -29.234 -3.283  1.00 14.19 ?  126 LEU   B CB   1 
ATOM   5866 C CG   . LEU   B 1 126 ? 39.964 -29.715 -4.637  1.00 15.15 ?  126 LEU   B CG   1 
ATOM   5867 C CD1  . LEU   B 1 126 ? 40.009 -31.229 -4.710  1.00 17.12 ?  126 LEU   B CD1  1 
ATOM   5868 C CD2  . LEU   B 1 126 ? 38.553 -29.216 -4.898  1.00 15.22 ?  126 LEU   B CD2  1 
ATOM   5869 H H    . LEU   B 1 126 ? 42.486 -28.045 -4.084  1.00 14.42 ?  126 LEU   B H    1 
ATOM   5870 H HA   . LEU   B 1 126 ? 40.010 -27.260 -3.566  1.00 15.06 ?  126 LEU   B HA   1 
ATOM   5871 H HB2  . LEU   B 1 126 ? 41.309 -29.711 -3.106  1.00 17.00 ?  126 LEU   B HB2  1 
ATOM   5872 H HB3  . LEU   B 1 126 ? 39.821 -29.476 -2.618  1.00 17.00 ?  126 LEU   B HB3  1 
ATOM   5873 H HG   . LEU   B 1 126 ? 40.539 -29.366 -5.337  1.00 18.16 ?  126 LEU   B HG   1 
ATOM   5874 H HD11 . LEU   B 1 126 ? 39.672 -31.513 -5.575  1.00 20.51 ?  126 LEU   B HD11 1 
ATOM   5875 H HD12 . LEU   B 1 126 ? 40.924 -31.524 -4.596  1.00 20.51 ?  126 LEU   B HD12 1 
ATOM   5876 H HD13 . LEU   B 1 126 ? 39.452 -31.594 -4.004  1.00 20.51 ?  126 LEU   B HD13 1 
ATOM   5877 H HD21 . LEU   B 1 126 ? 38.220 -29.624 -5.715  1.00 18.23 ?  126 LEU   B HD21 1 
ATOM   5878 H HD22 . LEU   B 1 126 ? 37.987 -29.463 -4.151  1.00 18.23 ?  126 LEU   B HD22 1 
ATOM   5879 H HD23 . LEU   B 1 126 ? 38.570 -28.251 -4.997  1.00 18.23 ?  126 LEU   B HD23 1 
ATOM   5880 N N    . LEU   B 1 127 ? 39.928 -26.511 -1.258  1.00 12.89 ?  127 LEU   B N    1 
ATOM   5881 C CA   . LEU   B 1 127 ? 39.983 -26.018 0.104   1.00 13.20 ?  127 LEU   B CA   1 
ATOM   5882 C C    . LEU   B 1 127 ? 39.716 -27.138 1.101   1.00 12.88 ?  127 LEU   B C    1 
ATOM   5883 O O    . LEU   B 1 127 ? 38.894 -28.032 0.872   1.00 12.85 ?  127 LEU   B O    1 
ATOM   5884 C CB   . LEU   B 1 127 ? 38.960 -24.904 0.301   1.00 13.50 ?  127 LEU   B CB   1 
ATOM   5885 C CG   . LEU   B 1 127 ? 39.139 -23.635 -0.536  1.00 14.10 ?  127 LEU   B CG   1 
ATOM   5886 C CD1  . LEU   B 1 127 ? 38.026 -22.657 -0.199  1.00 14.37 ?  127 LEU   B CD1  1 
ATOM   5887 C CD2  . LEU   B 1 127 ? 40.507 -22.984 -0.316  1.00 14.84 ?  127 LEU   B CD2  1 
ATOM   5888 H H    . LEU   B 1 127 ? 39.264 -26.216 -1.721  1.00 15.44 ?  127 LEU   B H    1 
ATOM   5889 H HA   . LEU   B 1 127 ? 40.867 -25.651 0.277   1.00 15.82 ?  127 LEU   B HA   1 
ATOM   5890 H HB2  . LEU   B 1 127 ? 38.081 -25.260 0.093   1.00 16.17 ?  127 LEU   B HB2  1 
ATOM   5891 H HB3  . LEU   B 1 127 ? 38.982 -24.633 1.231   1.00 16.17 ?  127 LEU   B HB3  1 
ATOM   5892 H HG   . LEU   B 1 127 ? 39.050 -23.857 -1.475  1.00 16.90 ?  127 LEU   B HG   1 
ATOM   5893 H HD11 . LEU   B 1 127 ? 38.144 -21.846 -0.724  1.00 17.22 ?  127 LEU   B HD11 1 
ATOM   5894 H HD12 . LEU   B 1 127 ? 37.167 -23.059 -0.406  1.00 17.22 ?  127 LEU   B HD12 1 
ATOM   5895 H HD13 . LEU   B 1 127 ? 38.067 -22.440 0.747   1.00 17.22 ?  127 LEU   B HD13 1 
ATOM   5896 H HD21 . LEU   B 1 127 ? 40.535 -22.137 -0.792  1.00 17.79 ?  127 LEU   B HD21 1 
ATOM   5897 H HD22 . LEU   B 1 127 ? 40.635 -22.832 0.633   1.00 17.79 ?  127 LEU   B HD22 1 
ATOM   5898 H HD23 . LEU   B 1 127 ? 41.192 -23.577 -0.654  1.00 17.79 ?  127 LEU   B HD23 1 
ATOM   5899 N N    . SER   B 1 128 ? 40.401 -27.056 2.231   1.00 12.87 ?  128 SER   B N    1 
ATOM   5900 C CA   . SER   B 1 128 ? 40.285 -27.973 3.353   1.00 13.27 ?  128 SER   B CA   1 
ATOM   5901 C C    . SER   B 1 128 ? 40.782 -29.379 3.029   1.00 14.32 ?  128 SER   B C    1 
ATOM   5902 O O    . SER   B 1 128 ? 40.670 -30.265 3.873   1.00 15.39 ?  128 SER   B O    1 
ATOM   5903 C CB   . SER   B 1 128 ? 38.877 -27.983 3.966   1.00 13.81 ?  128 SER   B CB   1 
ATOM   5904 O OG   . SER   B 1 128 ? 38.564 -26.710 4.530   1.00 14.17 ?  128 SER   B OG   1 
ATOM   5905 H H    . SER   B 1 128 ? 40.973 -26.426 2.378   1.00 15.41 ?  128 SER   B H    1 
ATOM   5906 H HA   . SER   B 1 128 ? 40.865 -27.640 4.042   1.00 15.90 ?  128 SER   B HA   1 
ATOM   5907 H HB2  . SER   B 1 128 ? 38.222 -28.199 3.281   1.00 16.54 ?  128 SER   B HB2  1 
ATOM   5908 H HB3  . SER   B 1 128 ? 38.843 -28.662 4.670   1.00 16.54 ?  128 SER   B HB3  1 
ATOM   5909 H HG   . SER   B 1 128 ? 39.124 -26.526 5.130   1.00 16.97 ?  128 SER   B HG   1 
ATOM   5910 N N    . ALA   B 1 129 ? 41.363 -29.593 1.848   1.00 15.26 ?  129 ALA   B N    1 
ATOM   5911 C CA   . ALA   B 1 129 ? 41.909 -30.890 1.488   1.00 16.00 ?  129 ALA   B CA   1 
ATOM   5912 C C    . ALA   B 1 129 ? 43.298 -31.073 2.088   1.00 15.26 ?  129 ALA   B C    1 
ATOM   5913 O O    . ALA   B 1 129 ? 43.867 -30.176 2.724   1.00 15.18 ?  129 ALA   B O    1 
ATOM   5914 C CB   . ALA   B 1 129 ? 41.959 -31.048 -0.029  1.00 18.40 ?  129 ALA   B CB   1 
ATOM   5915 H H    . ALA   B 1 129 ? 41.457 -28.991 1.234   1.00 18.28 ?  129 ALA   B H    1 
ATOM   5916 H HA   . ALA   B 1 129 ? 41.334 -31.581 1.846   1.00 19.18 ?  129 ALA   B HA   1 
ATOM   5917 H HB1  . ALA   B 1 129 ? 42.317 -31.925 -0.241  1.00 22.05 ?  129 ALA   B HB1  1 
ATOM   5918 H HB2  . ALA   B 1 129 ? 41.062 -30.962 -0.383  1.00 22.05 ?  129 ALA   B HB2  1 
ATOM   5919 H HB3  . ALA   B 1 129 ? 42.531 -30.359 -0.400  1.00 22.05 ?  129 ALA   B HB3  1 
ATOM   5920 N N    . GLY   B 1 130 ? 43.846 -32.268 1.878   1.00 15.16 ?  130 GLY   B N    1 
ATOM   5921 C CA   . GLY   B 1 130 ? 45.233 -32.509 2.235   1.00 15.93 ?  130 GLY   B CA   1 
ATOM   5922 C C    . GLY   B 1 130 ? 45.444 -32.404 3.728   1.00 16.14 ?  130 GLY   B C    1 
ATOM   5923 O O    . GLY   B 1 130 ? 44.744 -33.042 4.527   1.00 16.76 ?  130 GLY   B O    1 
ATOM   5924 H H    . GLY   B 1 130 ? 43.438 -32.945 1.535   1.00 18.17 ?  130 GLY   B H    1 
ATOM   5925 H HA2  . GLY   B 1 130 ? 45.496 -33.398 1.945   1.00 19.09 ?  130 GLY   B HA2  1 
ATOM   5926 H HA3  . GLY   B 1 130 ? 45.802 -31.859 1.793   1.00 19.09 ?  130 GLY   B HA3  1 
ATOM   5927 N N    . ILE   B 1 131 ? 46.422 -31.580 4.117   1.00 16.53 ?  131 ILE   B N    1 
ATOM   5928 C CA   . ILE   B 1 131 ? 46.776 -31.433 5.517   1.00 17.32 ?  131 ILE   B CA   1 
ATOM   5929 C C    . ILE   B 1 131 ? 45.652 -30.837 6.347   1.00 16.67 ?  131 ILE   B C    1 
ATOM   5930 O O    . ILE   B 1 131 ? 45.712 -30.907 7.577   1.00 18.29 ?  131 ILE   B O    1 
ATOM   5931 C CB   . ILE   B 1 131 ? 48.096 -30.643 5.704   1.00 19.27 ?  131 ILE   B CB   1 
ATOM   5932 C CG1  . ILE   B 1 131 ? 47.923 -29.165 5.322   1.00 20.67 ?  131 ILE   B CG1  1 
ATOM   5933 C CG2  . ILE   B 1 131 ? 49.215 -31.277 4.892   1.00 20.63 ?  131 ILE   B CG2  1 
ATOM   5934 C CD1  . ILE   B 1 131 ? 49.137 -28.303 5.636   1.00 22.08 ?  131 ILE   B CD1  1 
ATOM   5935 H H    . ILE   B 1 131 ? 46.893 -31.097 3.585   1.00 19.81 ?  131 ILE   B H    1 
ATOM   5936 H HA   . ILE   B 1 131 ? 46.929 -32.315 5.877   1.00 20.76 ?  131 ILE   B HA   1 
ATOM   5937 H HB   . ILE   B 1 131 ? 48.338 -30.682 6.643   1.00 23.10 ?  131 ILE   B HB   1 
ATOM   5938 H HG12 . ILE   B 1 131 ? 47.754 -29.110 4.369   1.00 24.77 ?  131 ILE   B HG12 1 
ATOM   5939 H HG13 . ILE   B 1 131 ? 47.169 -28.794 5.810   1.00 24.77 ?  131 ILE   B HG13 1 
ATOM   5940 H HG21 . ILE   B 1 131 ? 50.056 -30.872 5.148   1.00 24.73 ?  131 ILE   B HG21 1 
ATOM   5941 H HG22 . ILE   B 1 131 ? 49.231 -32.227 5.075   1.00 24.73 ?  131 ILE   B HG22 1 
ATOM   5942 H HG23 . ILE   B 1 131 ? 49.042 -31.123 3.950   1.00 24.73 ?  131 ILE   B HG23 1 
ATOM   5943 H HD11 . ILE   B 1 131 ? 48.914 -27.375 5.462   1.00 26.47 ?  131 ILE   B HD11 1 
ATOM   5944 H HD12 . ILE   B 1 131 ? 49.372 -28.418 6.569   1.00 26.47 ?  131 ILE   B HD12 1 
ATOM   5945 H HD13 . ILE   B 1 131 ? 49.873 -28.579 5.070   1.00 26.47 ?  131 ILE   B HD13 1 
ATOM   5946 N N    . PHE   B 1 132 ? 44.627 -30.260 5.709   1.00 15.31 ?  132 PHE   B N    1 
ATOM   5947 C CA   . PHE   B 1 132 ? 43.458 -29.759 6.429   1.00 15.52 ?  132 PHE   B CA   1 
ATOM   5948 C C    . PHE   B 1 132 ? 42.433 -30.849 6.743   1.00 17.11 ?  132 PHE   B C    1 
ATOM   5949 O O    . PHE   B 1 132 ? 41.521 -30.599 7.539   1.00 18.58 ?  132 PHE   B O    1 
ATOM   5950 C CB   . PHE   B 1 132 ? 42.778 -28.622 5.654   1.00 14.68 ?  132 PHE   B CB   1 
ATOM   5951 C CG   . PHE   B 1 132 ? 43.478 -27.282 5.766   1.00 14.90 ?  132 PHE   B CG   1 
ATOM   5952 C CD1  . PHE   B 1 132 ? 44.766 -27.101 5.285   1.00 16.13 ?  132 PHE   B CD1  1 
ATOM   5953 C CD2  . PHE   B 1 132 ? 42.814 -26.187 6.297   1.00 14.59 ?  132 PHE   B CD2  1 
ATOM   5954 C CE1  . PHE   B 1 132 ? 45.392 -25.865 5.378   1.00 16.59 ?  132 PHE   B CE1  1 
ATOM   5955 C CE2  . PHE   B 1 132 ? 43.432 -24.945 6.384   1.00 15.21 ?  132 PHE   B CE2  1 
ATOM   5956 C CZ   . PHE   B 1 132 ? 44.720 -24.790 5.926   1.00 16.37 ?  132 PHE   B CZ   1 
ATOM   5957 H H    . PHE   B 1 132 ? 44.583 -30.138 4.857   1.00 18.35 ?  132 PHE   B H    1 
ATOM   5958 H HA   . PHE   B 1 132 ? 43.752 -29.390 7.274   1.00 18.60 ?  132 PHE   B HA   1 
ATOM   5959 H HB2  . PHE   B 1 132 ? 42.755 -28.861 4.717   1.00 17.59 ?  132 PHE   B HB2  1 
ATOM   5960 H HB3  . PHE   B 1 132 ? 41.871 -28.513 5.989   1.00 17.59 ?  132 PHE   B HB3  1 
ATOM   5961 H HD1  . PHE   B 1 132 ? 45.226 -27.826 4.923   1.00 19.33 ?  132 PHE   B HD1  1 
ATOM   5962 H HD2  . PHE   B 1 132 ? 41.944 -26.287 6.613   1.00 17.48 ?  132 PHE   B HD2  1 
ATOM   5963 H HE1  . PHE   B 1 132 ? 46.263 -25.761 5.067   1.00 19.88 ?  132 PHE   B HE1  1 
ATOM   5964 H HE2  . PHE   B 1 132 ? 42.980 -24.220 6.757   1.00 18.23 ?  132 PHE   B HE2  1 
ATOM   5965 H HZ   . PHE   B 1 132 ? 45.139 -23.957 5.987   1.00 19.61 ?  132 PHE   B HZ   1 
ATOM   5966 N N    . GLY   B 1 133 ? 42.539 -32.036 6.133   1.00 16.90 ?  133 GLY   B N    1 
ATOM   5967 C CA   . GLY   B 1 133 ? 41.834 -33.209 6.617   1.00 17.36 ?  133 GLY   B CA   1 
ATOM   5968 C C    . GLY   B 1 133 ? 40.432 -33.463 6.095   1.00 17.56 ?  133 GLY   B C    1 
ATOM   5969 O O    . GLY   B 1 133 ? 39.847 -34.487 6.460   1.00 19.39 ?  133 GLY   B O    1 
ATOM   5970 H H    . GLY   B 1 133 ? 43.028 -32.180 5.435   1.00 20.25 ?  133 GLY   B H    1 
ATOM   5971 H HA2  . GLY   B 1 133 ? 42.368 -33.989 6.408   1.00 20.81 ?  133 GLY   B HA2  1 
ATOM   5972 H HA3  . GLY   B 1 133 ? 41.773 -33.143 7.581   1.00 20.81 ?  133 GLY   B HA3  1 
ATOM   5973 N N    . ALA   B 1 134 ? 39.862 -32.584 5.279   1.00 16.67 ?  134 ALA   B N    1 
ATOM   5974 C CA   . ALA   B 1 134 ? 38.537 -32.869 4.747   1.00 16.58 ?  134 ALA   B CA   1 
ATOM   5975 C C    . ALA   B 1 134 ? 38.620 -33.877 3.604   1.00 16.77 ?  134 ALA   B C    1 
ATOM   5976 O O    . ALA   B 1 134 ? 39.673 -34.084 2.998   1.00 17.66 ?  134 ALA   B O    1 
ATOM   5977 C CB   . ALA   B 1 134 ? 37.862 -31.587 4.257   1.00 17.13 ?  134 ALA   B CB   1 
ATOM   5978 H H    . ALA   B 1 134 ? 40.206 -31.827 5.033   1.00 19.98 ?  134 ALA   B H    1 
ATOM   5979 H HA   . ALA   B 1 134 ? 37.989 -33.244 5.452   1.00 19.86 ?  134 ALA   B HA   1 
ATOM   5980 H HB1  . ALA   B 1 134 ? 36.977 -31.806 3.927   1.00 20.52 ?  134 ALA   B HB1  1 
ATOM   5981 H HB2  . ALA   B 1 134 ? 37.795 -30.962 4.995   1.00 20.52 ?  134 ALA   B HB2  1 
ATOM   5982 H HB3  . ALA   B 1 134 ? 38.395 -31.202 3.544   1.00 20.52 ?  134 ALA   B HB3  1 
ATOM   5983 N N    . ASP   B 1 135 ? 37.485 -34.499 3.313   1.00 17.17 ?  135 ASP   B N    1 
ATOM   5984 C CA   . ASP   B 1 135 ? 37.386 -35.392 2.168   1.00 17.86 ?  135 ASP   B CA   1 
ATOM   5985 C C    . ASP   B 1 135 ? 37.493 -34.556 0.898   1.00 16.56 ?  135 ASP   B C    1 
ATOM   5986 O O    . ASP   B 1 135 ? 36.640 -33.684 0.669   1.00 16.55 ?  135 ASP   B O    1 
ATOM   5987 C CB   . ASP   B 1 135 ? 36.040 -36.114 2.223   1.00 19.64 ?  135 ASP   B CB   1 
ATOM   5988 C CG   . ASP   B 1 135 ? 35.847 -37.100 1.089   1.00 21.94 ?  135 ASP   B CG   1 
ATOM   5989 O OD1  . ASP   B 1 135 ? 36.708 -37.173 0.188   1.00 21.26 ?  135 ASP   B OD1  1 
ATOM   5990 O OD2  . ASP   B 1 135 ? 34.827 -37.825 1.115   1.00 25.18 -1 135 ASP   B OD2  1 
ATOM   5991 H H    . ASP   B 1 135 ? 36.758 -34.417 3.763   1.00 20.57 ?  135 ASP   B H    1 
ATOM   5992 H HA   . ASP   B 1 135 ? 38.101 -36.049 2.202   1.00 21.40 ?  135 ASP   B HA   1 
ATOM   5993 H HB2  . ASP   B 1 135 ? 35.981 -36.602 3.057   1.00 23.55 ?  135 ASP   B HB2  1 
ATOM   5994 H HB3  . ASP   B 1 135 ? 35.332 -35.457 2.166   1.00 23.55 ?  135 ASP   B HB3  1 
ATOM   5995 N N    . PRO   B 1 136 ? 38.505 -34.768 0.055   1.00 16.68 ?  136 PRO   B N    1 
ATOM   5996 C CA   . PRO   B 1 136 ? 38.609 -33.947 -1.160  1.00 15.99 ?  136 PRO   B CA   1 
ATOM   5997 C C    . PRO   B 1 136 ? 37.422 -34.095 -2.087  1.00 15.41 ?  136 PRO   B C    1 
ATOM   5998 O O    . PRO   B 1 136 ? 37.107 -33.147 -2.811  1.00 14.46 ?  136 PRO   B O    1 
ATOM   5999 C CB   . PRO   B 1 136 ? 39.917 -34.430 -1.803  1.00 17.30 ?  136 PRO   B CB   1 
ATOM   6000 C CG   . PRO   B 1 136 ? 40.101 -35.821 -1.273  1.00 18.52 ?  136 PRO   B CG   1 
ATOM   6001 C CD   . PRO   B 1 136 ? 39.584 -35.768 0.135   1.00 17.79 ?  136 PRO   B CD   1 
ATOM   6002 H HA   . PRO   B 1 136 ? 38.703 -33.010 -0.925  1.00 19.16 ?  136 PRO   B HA   1 
ATOM   6003 H HB2  . PRO   B 1 136 ? 39.828 -34.437 -2.771  1.00 20.73 ?  136 PRO   B HB2  1 
ATOM   6004 H HB3  . PRO   B 1 136 ? 40.649 -33.854 -1.531  1.00 20.73 ?  136 PRO   B HB3  1 
ATOM   6005 H HG2  . PRO   B 1 136 ? 39.585 -36.447 -1.804  1.00 22.20 ?  136 PRO   B HG2  1 
ATOM   6006 H HG3  . PRO   B 1 136 ? 41.042 -36.054 -1.283  1.00 22.20 ?  136 PRO   B HG3  1 
ATOM   6007 H HD2  . PRO   B 1 136 ? 39.226 -36.630 0.399   1.00 21.32 ?  136 PRO   B HD2  1 
ATOM   6008 H HD3  . PRO   B 1 136 ? 40.277 -35.467 0.746   1.00 21.32 ?  136 PRO   B HD3  1 
ATOM   6009 N N    . ILE   B 1 137 ? 36.761 -35.257 -2.097  1.00 16.23 ?  137 ILE   B N    1 
ATOM   6010 C CA   . ILE   B 1 137 ? 35.552 -35.425 -2.898  1.00 16.48 ?  137 ILE   B CA   1 
ATOM   6011 C C    . ILE   B 1 137 ? 34.476 -34.455 -2.428  1.00 15.97 ?  137 ILE   B C    1 
ATOM   6012 O O    . ILE   B 1 137 ? 33.767 -33.840 -3.234  1.00 15.29 ?  137 ILE   B O    1 
ATOM   6013 C CB   . ILE   B 1 137 ? 35.078 -36.892 -2.828  1.00 18.69 ?  137 ILE   B CB   1 
ATOM   6014 C CG1  . ILE   B 1 137 ? 36.091 -37.806 -3.523  1.00 21.67 ?  137 ILE   B CG1  1 
ATOM   6015 C CG2  . ILE   B 1 137 ? 33.683 -37.045 -3.439  1.00 19.34 ?  137 ILE   B CG2  1 
ATOM   6016 C CD1  . ILE   B 1 137 ? 35.781 -39.281 -3.389  1.00 24.13 ?  137 ILE   B CD1  1 
ATOM   6017 H H    . ILE   B 1 137 ? 36.988 -35.956 -1.652  1.00 19.45 ?  137 ILE   B H    1 
ATOM   6018 H HA   . ILE   B 1 137 ? 35.752 -35.223 -3.827  1.00 19.75 ?  137 ILE   B HA   1 
ATOM   6019 H HB   . ILE   B 1 137 ? 35.026 -37.150 -1.899  1.00 22.40 ?  137 ILE   B HB   1 
ATOM   6020 H HG12 . ILE   B 1 137 ? 36.110 -37.593 -4.469  1.00 25.98 ?  137 ILE   B HG12 1 
ATOM   6021 H HG13 . ILE   B 1 137 ? 36.966 -37.652 -3.134  1.00 25.98 ?  137 ILE   B HG13 1 
ATOM   6022 H HG21 . ILE   B 1 137 ? 33.444 -37.986 -3.474  1.00 23.18 ?  137 ILE   B HG21 1 
ATOM   6023 H HG22 . ILE   B 1 137 ? 33.037 -36.577 -2.889  1.00 23.18 ?  137 ILE   B HG22 1 
ATOM   6024 H HG23 . ILE   B 1 137 ? 33.685 -36.677 -4.336  1.00 23.18 ?  137 ILE   B HG23 1 
ATOM   6025 H HD11 . ILE   B 1 137 ? 36.483 -39.777 -3.830  1.00 28.93 ?  137 ILE   B HD11 1 
ATOM   6026 H HD12 . ILE   B 1 137 ? 35.745 -39.515 -2.447  1.00 28.93 ?  137 ILE   B HD12 1 
ATOM   6027 H HD13 . ILE   B 1 137 ? 34.931 -39.475 -3.812  1.00 28.93 ?  137 ILE   B HD13 1 
ATOM   6028 N N    . HIS   B 1 138 ? 34.333 -34.308 -1.114  1.00 15.98 ?  138 HIS   B N    1 
ATOM   6029 C CA   . HIS   B 1 138 ? 33.386 -33.337 -0.585  1.00 16.39 ?  138 HIS   B CA   1 
ATOM   6030 C C    . HIS   B 1 138 ? 33.814 -31.909 -0.902  1.00 15.39 ?  138 HIS   B C    1 
ATOM   6031 O O    . HIS   B 1 138 ? 32.971 -31.062 -1.206  1.00 15.89 ?  138 HIS   B O    1 
ATOM   6032 C CB   . HIS   B 1 138 ? 33.253 -33.517 0.920   1.00 17.71 ?  138 HIS   B CB   1 
ATOM   6033 C CG   . HIS   B 1 138 ? 32.324 -32.532 1.549   1.00 18.35 ?  138 HIS   B CG   1 
ATOM   6034 N ND1  . HIS   B 1 138 ? 30.986 -32.462 1.224   1.00 19.93 ?  138 HIS   B ND1  1 
ATOM   6035 C CD2  . HIS   B 1 138 ? 32.543 -31.555 2.459   1.00 18.81 ?  138 HIS   B CD2  1 
ATOM   6036 C CE1  . HIS   B 1 138 ? 30.418 -31.493 1.920   1.00 20.45 ?  138 HIS   B CE1  1 
ATOM   6037 N NE2  . HIS   B 1 138 ? 31.340 -30.931 2.681   1.00 19.37 ?  138 HIS   B NE2  1 
ATOM   6038 H H    . HIS   B 1 138 ? 34.764 -34.756 -0.524  1.00 19.15 ?  138 HIS   B H    1 
ATOM   6039 H HA   . HIS   B 1 138 ? 32.513 -33.493 -0.987  1.00 19.64 ?  138 HIS   B HA   1 
ATOM   6040 H HB2  . HIS   B 1 138 ? 32.910 -34.405 1.102   1.00 21.22 ?  138 HIS   B HB2  1 
ATOM   6041 H HB3  . HIS   B 1 138 ? 34.124 -33.406 1.326   1.00 21.22 ?  138 HIS   B HB3  1 
ATOM   6042 H HD1  . HIS   B 1 138 ? 30.584 -32.975 0.658   1.00 23.89 ?  138 HIS   B HD1  1 
ATOM   6043 H HD2  . HIS   B 1 138 ? 33.347 -31.351 2.870   1.00 22.54 ?  138 HIS   B HD2  1 
ATOM   6044 H HE1  . HIS   B 1 138 ? 29.516 -31.258 1.884   1.00 24.51 ?  138 HIS   B HE1  1 
ATOM   6045 N N    . SER   B 1 139 ? 35.110 -31.617 -0.826  1.00 14.84 ?  139 SER   B N    1 
ATOM   6046 C CA   . SER   B 1 139 ? 35.552 -30.268 -1.141  1.00 14.36 ?  139 SER   B CA   1 
ATOM   6047 C C    . SER   B 1 139 ? 35.223 -29.914 -2.582  1.00 13.47 ?  139 SER   B C    1 
ATOM   6048 O O    . SER   B 1 139 ? 34.778 -28.797 -2.864  1.00 13.55 ?  139 SER   B O    1 
ATOM   6049 C CB   . SER   B 1 139 ? 37.044 -30.127 -0.861  1.00 14.90 ?  139 SER   B CB   1 
ATOM   6050 O OG   . SER   B 1 139 ? 37.452 -28.797 -1.134  1.00 14.41 ?  139 SER   B OG   1 
ATOM   6051 H H    . SER   B 1 139 ? 35.729 -32.166 -0.614  1.00 17.79 ?  139 SER   B H    1 
ATOM   6052 H HA   . SER   B 1 139 ? 35.076 -29.642 -0.580  1.00 17.21 ?  139 SER   B HA   1 
ATOM   6053 H HB2  . SER   B 1 139 ? 37.209 -30.324 0.075   1.00 17.85 ?  139 SER   B HB2  1 
ATOM   6054 H HB3  . SER   B 1 139 ? 37.540 -30.735 -1.427  1.00 17.85 ?  139 SER   B HB3  1 
ATOM   6055 H HG   . SER   B 1 139 ? 37.066 -28.262 -0.612  1.00 17.27 ?  139 SER   B HG   1 
ATOM   6056 N N    . LEU   B 1 140 ? 35.413 -30.859 -3.506  1.00 12.90 ?  140 LEU   B N    1 
ATOM   6057 C CA   . LEU   B 1 140 ? 35.053 -30.610 -4.894  1.00 13.27 ?  140 LEU   B CA   1 
ATOM   6058 C C    . LEU   B 1 140 ? 33.551 -30.379 -5.031  1.00 13.42 ?  140 LEU   B C    1 
ATOM   6059 O O    . LEU   B 1 140 ? 33.121 -29.492 -5.771  1.00 13.42 ?  140 LEU   B O    1 
ATOM   6060 C CB   . LEU   B 1 140 ? 35.527 -31.772 -5.771  1.00 13.63 ?  140 LEU   B CB   1 
ATOM   6061 C CG   . LEU   B 1 140 ? 35.175 -31.664 -7.247  1.00 13.69 ?  140 LEU   B CG   1 
ATOM   6062 C CD1  . LEU   B 1 140 ? 35.745 -30.391 -7.838  1.00 14.66 ?  140 LEU   B CD1  1 
ATOM   6063 C CD2  . LEU   B 1 140 ? 35.676 -32.891 -7.978  1.00 14.71 ?  140 LEU   B CD2  1 
ATOM   6064 H H    . LEU   B 1 140 ? 35.740 -31.643 -3.359  1.00 15.46 ?  140 LEU   B H    1 
ATOM   6065 H HA   . LEU   B 1 140 ? 35.509 -29.811 -5.200  1.00 15.90 ?  140 LEU   B HA   1 
ATOM   6066 H HB2  . LEU   B 1 140 ? 36.495 -31.835 -5.714  1.00 16.33 ?  140 LEU   B HB2  1 
ATOM   6067 H HB3  . LEU   B 1 140 ? 35.131 -32.595 -5.443  1.00 16.33 ?  140 LEU   B HB3  1 
ATOM   6068 H HG   . LEU   B 1 140 ? 34.208 -31.628 -7.342  1.00 16.40 ?  140 LEU   B HG   1 
ATOM   6069 H HD11 . LEU   B 1 140 ? 35.643 -30.418 -8.800  1.00 17.57 ?  140 LEU   B HD11 1 
ATOM   6070 H HD12 . LEU   B 1 140 ? 35.263 -29.630 -7.475  1.00 17.57 ?  140 LEU   B HD12 1 
ATOM   6071 H HD13 . LEU   B 1 140 ? 36.684 -30.331 -7.604  1.00 17.57 ?  140 LEU   B HD13 1 
ATOM   6072 H HD21 . LEU   B 1 140 ? 35.437 -32.809 -8.915  1.00 17.62 ?  140 LEU   B HD21 1 
ATOM   6073 H HD22 . LEU   B 1 140 ? 36.630 -32.946 -7.874  1.00 17.62 ?  140 LEU   B HD22 1 
ATOM   6074 H HD23 . LEU   B 1 140 ? 35.244 -33.671 -7.595  1.00 17.62 ?  140 LEU   B HD23 1 
ATOM   6075 N N    . ARG   B 1 141 ? 32.746 -31.174 -4.323  1.00 13.55 ?  141 ARG   B N    1 
ATOM   6076 C CA   . ARG   B 1 141 ? 31.293 -30.995 -4.306  1.00 14.55 ?  141 ARG   B CA   1 
ATOM   6077 C C    . ARG   B 1 141 ? 30.916 -29.580 -3.887  1.00 14.45 ?  141 ARG   B C    1 
ATOM   6078 O O    . ARG   B 1 141 ? 30.112 -28.907 -4.550  1.00 14.36 ?  141 ARG   B O    1 
ATOM   6079 C CB   . ARG   B 1 141 ? 30.704 -32.004 -3.312  1.00 16.42 ?  141 ARG   B CB   1 
ATOM   6080 C CG   . ARG   B 1 141 ? 29.239 -31.872 -2.986  1.00 19.00 ?  141 ARG   B CG   1 
ATOM   6081 C CD   . ARG   B 1 141 ? 28.442 -32.528 -4.035  1.00 20.80 ?  141 ARG   B CD   1 
ATOM   6082 N NE   . ARG   B 1 141 ? 28.188 -31.636 -5.154  1.00 21.56 ?  141 ARG   B NE   1 
ATOM   6083 C CZ   . ARG   B 1 141 ? 28.201 -32.003 -6.427  1.00 20.97 ?  141 ARG   B CZ   1 
ATOM   6084 N NH1  . ARG   B 1 141 ? 28.638 -33.197 -6.800  1.00 20.41 ?  141 ARG   B NH1  1 
ATOM   6085 N NH2  . ARG   B 1 141 ? 27.767 -31.149 -7.350  1.00 21.76 ?  141 ARG   B NH2  1 
ATOM   6086 H H    . ARG   B 1 141 ? 33.023 -31.821 -3.836  1.00 16.23 ?  141 ARG   B H    1 
ATOM   6087 H HA   . ARG   B 1 141 ? 30.929 -31.165 -5.186  1.00 17.43 ?  141 ARG   B HA   1 
ATOM   6088 H HB2  . ARG   B 1 141 ? 30.852 -32.894 -3.666  1.00 19.67 ?  141 ARG   B HB2  1 
ATOM   6089 H HB3  . ARG   B 1 141 ? 31.187 -31.916 -2.477  1.00 19.67 ?  141 ARG   B HB3  1 
ATOM   6090 H HG2  . ARG   B 1 141 ? 29.062 -32.302 -2.138  1.00 22.77 ?  141 ARG   B HG2  1 
ATOM   6091 H HG3  . ARG   B 1 141 ? 28.986 -30.931 -2.943  1.00 22.77 ?  141 ARG   B HG3  1 
ATOM   6092 H HD2  . ARG   B 1 141 ? 28.919 -33.313 -4.357  1.00 24.93 ?  141 ARG   B HD2  1 
ATOM   6093 H HD3  . ARG   B 1 141 ? 27.596 -32.797 -3.658  1.00 24.93 ?  141 ARG   B HD3  1 
ATOM   6094 H HE   . ARG   B 1 141 ? 27.990 -30.818 -4.974  1.00 25.85 ?  141 ARG   B HE   1 
ATOM   6095 H HH11 . ARG   B 1 141 ? 28.909 -33.766 -6.217  1.00 24.46 ?  141 ARG   B HH11 1 
ATOM   6096 H HH12 . ARG   B 1 141 ? 28.643 -33.407 -7.633  1.00 24.46 ?  141 ARG   B HH12 1 
ATOM   6097 H HH21 . ARG   B 1 141 ? 27.489 -30.367 -7.119  1.00 26.09 ?  141 ARG   B HH21 1 
ATOM   6098 H HH22 . ARG   B 1 141 ? 27.790 -31.365 -8.183  1.00 26.09 ?  141 ARG   B HH22 1 
ATOM   6099 N N    . VAL   B 1 142 ? 31.453 -29.131 -2.756  1.00 14.04 ?  142 VAL   B N    1 
ATOM   6100 C CA   . VAL   B 1 142 ? 31.120 -27.799 -2.273  1.00 13.81 ?  142 VAL   B CA   1 
ATOM   6101 C C    . VAL   B 1 142 ? 31.604 -26.745 -3.258  1.00 13.61 ?  142 VAL   B C    1 
ATOM   6102 O O    . VAL   B 1 142 ? 30.914 -25.756 -3.517  1.00 13.94 ?  142 VAL   B O    1 
ATOM   6103 C CB   . VAL   B 1 142 ? 31.665 -27.574 -0.852  1.00 14.41 ?  142 VAL   B CB   1 
ATOM   6104 C CG1  . VAL   B 1 142 ? 31.350 -26.153 -0.384  1.00 14.37 ?  142 VAL   B CG1  1 
ATOM   6105 C CG2  . VAL   B 1 142 ? 31.086 -28.598 0.115   1.00 14.82 ?  142 VAL   B CG2  1 
ATOM   6106 H H    . VAL   B 1 142 ? 32.002 -29.570 -2.258  1.00 16.82 ?  142 VAL   B H    1 
ATOM   6107 H HA   . VAL   B 1 142 ? 30.159 -27.724 -2.224  1.00 16.54 ?  142 VAL   B HA   1 
ATOM   6108 H HB   . VAL   B 1 142 ? 32.629 -27.676 -0.859  1.00 17.26 ?  142 VAL   B HB   1 
ATOM   6109 H HG11 . VAL   B 1 142 ? 31.523 -26.089 0.567   1.00 17.22 ?  142 VAL   B HG11 1 
ATOM   6110 H HG12 . VAL   B 1 142 ? 31.917 -25.527 -0.865  1.00 17.22 ?  142 VAL   B HG12 1 
ATOM   6111 H HG13 . VAL   B 1 142 ? 30.417 -25.961 -0.566  1.00 17.22 ?  142 VAL   B HG13 1 
ATOM   6112 H HG21 . VAL   B 1 142 ? 31.412 -28.408 1.007   1.00 17.75 ?  142 VAL   B HG21 1 
ATOM   6113 H HG22 . VAL   B 1 142 ? 30.119 -28.538 0.093   1.00 17.75 ?  142 VAL   B HG22 1 
ATOM   6114 H HG23 . VAL   B 1 142 ? 31.370 -29.483 -0.161  1.00 17.75 ?  142 VAL   B HG23 1 
ATOM   6115 N N    . CYS   B 1 143 ? 32.792 -26.939 -3.829  1.00 13.09 ?  143 CYS   B N    1 
ATOM   6116 C CA   . CYS   B 1 143 ? 33.289 -26.000 -4.831  1.00 12.84 ?  143 CYS   B CA   1 
ATOM   6117 C C    . CYS   B 1 143 ? 32.294 -25.854 -5.976  1.00 12.77 ?  143 CYS   B C    1 
ATOM   6118 O O    . CYS   B 1 143 ? 31.894 -24.743 -6.336  1.00 13.02 ?  143 CYS   B O    1 
ATOM   6119 C CB   . CYS   B 1 143 ? 34.648 -26.481 -5.351  1.00 13.50 ?  143 CYS   B CB   1 
ATOM   6120 S SG   . CYS   B 1 143 ? 35.405 -25.392 -6.576  1.00 13.74 ?  143 CYS   B SG   1 
ATOM   6121 H H    . CYS   B 1 143 ? 33.325 -27.590 -3.658  1.00 15.68 ?  143 CYS   B H    1 
ATOM   6122 H HA   . CYS   B 1 143 ? 33.416 -25.128 -4.429  1.00 15.38 ?  143 CYS   B HA   1 
ATOM   6123 H HB2  . CYS   B 1 143 ? 35.268 -26.557 -4.604  1.00 16.17 ?  143 CYS   B HB2  1 
ATOM   6124 H HB3  . CYS   B 1 143 ? 34.540 -27.351 -5.761  1.00 16.17 ?  143 CYS   B HB3  1 
ATOM   6125 H HG   . CYS   B 1 143 ? 36.481 -25.831 -6.884  1.00 16.46 ?  143 CYS   B HG   1 
ATOM   6126 N N    . VAL   B 1 144 ? 31.888 -26.974 -6.571  1.00 13.45 ?  144 VAL   B N    1 
ATOM   6127 C CA   . VAL   B 1 144 ? 30.991 -26.917 -7.720  1.00 14.39 ?  144 VAL   B CA   1 
ATOM   6128 C C    . VAL   B 1 144 ? 29.651 -26.301 -7.349  1.00 14.57 ?  144 VAL   B C    1 
ATOM   6129 O O    . VAL   B 1 144 ? 29.037 -25.601 -8.163  1.00 16.13 ?  144 VAL   B O    1 
ATOM   6130 C CB   . VAL   B 1 144 ? 30.835 -28.329 -8.306  1.00 17.25 ?  144 VAL   B CB   1 
ATOM   6131 C CG1  . VAL   B 1 144 ? 29.578 -28.447 -9.163  1.00 20.08 ?  144 VAL   B CG1  1 
ATOM   6132 C CG2  . VAL   B 1 144 ? 32.093 -28.731 -9.085  1.00 17.14 ?  144 VAL   B CG2  1 
ATOM   6133 H H    . VAL   B 1 144 ? 32.118 -27.770 -6.337  1.00 16.12 ?  144 VAL   B H    1 
ATOM   6134 H HA   . VAL   B 1 144 ? 31.385 -26.362 -8.407  1.00 17.24 ?  144 VAL   B HA   1 
ATOM   6135 H HB   . VAL   B 1 144 ? 30.742 -28.962 -7.576  1.00 20.67 ?  144 VAL   B HB   1 
ATOM   6136 H HG11 . VAL   B 1 144 ? 29.660 -29.232 -9.737  1.00 24.07 ?  144 VAL   B HG11 1 
ATOM   6137 H HG12 . VAL   B 1 144 ? 28.808 -28.552 -8.583  1.00 24.07 ?  144 VAL   B HG12 1 
ATOM   6138 H HG13 . VAL   B 1 144 ? 29.487 -27.654 -9.708  1.00 24.07 ?  144 VAL   B HG13 1 
ATOM   6139 H HG21 . VAL   B 1 144 ? 31.975 -29.627 -9.442  1.00 20.54 ?  144 VAL   B HG21 1 
ATOM   6140 H HG22 . VAL   B 1 144 ? 32.225 -28.103 -9.815  1.00 20.54 ?  144 VAL   B HG22 1 
ATOM   6141 H HG23 . VAL   B 1 144 ? 32.854 -28.710 -8.488  1.00 20.54 ?  144 VAL   B HG23 1 
ATOM   6142 N N    . ASP   B 1 145 ? 29.176 -26.543 -6.133  1.00 14.89 ?  145 ASP   B N    1 
ATOM   6143 C CA   . ASP   B 1 145 ? 27.866 -26.071 -5.708  1.00 15.39 ?  145 ASP   B CA   1 
ATOM   6144 C C    . ASP   B 1 145 ? 27.900 -24.649 -5.162  1.00 14.84 ?  145 ASP   B C    1 
ATOM   6145 O O    . ASP   B 1 145 ? 26.839 -24.105 -4.833  1.00 16.68 ?  145 ASP   B O    1 
ATOM   6146 C CB   . ASP   B 1 145 ? 27.277 -26.987 -4.624  1.00 17.34 ?  145 ASP   B CB   1 
ATOM   6147 C CG   . ASP   B 1 145 ? 26.918 -28.369 -5.133  1.00 19.05 ?  145 ASP   B CG   1 
ATOM   6148 O OD1  . ASP   B 1 145 ? 26.820 -28.569 -6.362  1.00 19.02 ?  145 ASP   B OD1  1 
ATOM   6149 O OD2  . ASP   B 1 145 ? 26.723 -29.258 -4.282  1.00 21.10 -1 145 ASP   B OD2  1 
ATOM   6150 H H    . ASP   B 1 145 ? 29.601 -26.977 -5.528  1.00 17.84 ?  145 ASP   B H    1 
ATOM   6151 H HA   . ASP   B 1 145 ? 27.266 -26.069 -6.471  1.00 18.44 ?  145 ASP   B HA   1 
ATOM   6152 H HB2  . ASP   B 1 145 ? 27.922 -27.091 -3.919  1.00 20.78 ?  145 ASP   B HB2  1 
ATOM   6153 H HB3  . ASP   B 1 145 ? 26.465 -26.572 -4.279  1.00 20.78 ?  145 ASP   B HB3  1 
ATOM   6154 N N    . THR   B 1 146 ? 29.078 -24.040 -5.038  1.00 13.29 ?  146 THR   B N    1 
ATOM   6155 C CA   . THR   B 1 146 ? 29.204 -22.716 -4.435  1.00 12.81 ?  146 THR   B CA   1 
ATOM   6156 C C    . THR   B 1 146 ? 29.840 -21.686 -5.348  1.00 12.75 ?  146 THR   B C    1 
ATOM   6157 O O    . THR   B 1 146 ? 29.391 -20.524 -5.383  1.00 13.19 ?  146 THR   B O    1 
ATOM   6158 C CB   . THR   B 1 146 ? 30.027 -22.815 -3.146  1.00 13.54 ?  146 THR   B CB   1 
ATOM   6159 O OG1  . THR   B 1 146 ? 29.450 -23.805 -2.287  1.00 13.50 ?  146 THR   B OG1  1 
ATOM   6160 C CG2  . THR   B 1 146 ? 30.088 -21.473 -2.434  1.00 13.46 ?  146 THR   B CG2  1 
ATOM   6161 H H    . THR   B 1 146 ? 29.831 -24.371 -5.300  1.00 15.92 ?  146 THR   B H    1 
ATOM   6162 H HA   . THR   B 1 146 ? 28.324 -22.389 -4.203  1.00 15.35 ?  146 THR   B HA   1 
ATOM   6163 H HB   . THR   B 1 146 ? 30.935 -23.072 -3.371  1.00 16.23 ?  146 THR   B HB   1 
ATOM   6164 H HG1  . THR   B 1 146 ? 29.489 -24.564 -2.664  1.00 16.18 ?  146 THR   B HG1  1 
ATOM   6165 H HG21 . THR   B 1 146 ? 30.427 -21.592 -1.536  1.00 16.12 ?  146 THR   B HG21 1 
ATOM   6166 H HG22 . THR   B 1 146 ? 30.677 -20.867 -2.914  1.00 16.12 ?  146 THR   B HG22 1 
ATOM   6167 H HG23 . THR   B 1 146 ? 29.202 -21.081 -2.390  1.00 16.12 ?  146 THR   B HG23 1 
ATOM   6168 N N    . VAL   B 1 147 ? 30.906 -22.062 -6.047  1.00 12.58 ?  147 VAL   B N    1 
ATOM   6169 C CA   . VAL   B 1 147 ? 31.638 -21.124 -6.883  1.00 12.54 ?  147 VAL   B CA   1 
ATOM   6170 C C    . VAL   B 1 147 ? 30.911 -20.989 -8.207  1.00 12.74 ?  147 VAL   B C    1 
ATOM   6171 O O    . VAL   B 1 147 ? 30.550 -21.992 -8.838  1.00 13.42 ?  147 VAL   B O    1 
ATOM   6172 C CB   . VAL   B 1 147 ? 33.088 -21.591 -7.085  1.00 12.42 ?  147 VAL   B CB   1 
ATOM   6173 C CG1  . VAL   B 1 147 ? 33.847 -20.567 -7.912  1.00 12.89 ?  147 VAL   B CG1  1 
ATOM   6174 C CG2  . VAL   B 1 147 ? 33.771 -21.801 -5.745  1.00 12.41 ?  147 VAL   B CG2  1 
ATOM   6175 H H    . VAL   B 1 147 ? 31.223 -22.866 -6.065  1.00 15.06 ?  147 VAL   B H    1 
ATOM   6176 H HA   . VAL   B 1 147 ? 31.659 -20.258 -6.458  1.00 15.02 ?  147 VAL   B HA   1 
ATOM   6177 H HB   . VAL   B 1 147 ? 33.097 -22.435 -7.571  1.00 14.88 ?  147 VAL   B HB   1 
ATOM   6178 H HG11 . VAL   B 1 147 ? 34.795 -20.777 -7.889  1.00 15.44 ?  147 VAL   B HG11 1 
ATOM   6179 H HG12 . VAL   B 1 147 ? 33.529 -20.590 -8.828  1.00 15.44 ?  147 VAL   B HG12 1 
ATOM   6180 H HG13 . VAL   B 1 147 ? 33.700 -19.684 -7.533  1.00 15.44 ?  147 VAL   B HG13 1 
ATOM   6181 H HG21 . VAL   B 1 147 ? 34.707 -22.008 -5.894  1.00 14.86 ?  147 VAL   B HG21 1 
ATOM   6182 H HG22 . VAL   B 1 147 ? 33.691 -20.987 -5.224  1.00 14.86 ?  147 VAL   B HG22 1 
ATOM   6183 H HG23 . VAL   B 1 147 ? 33.339 -22.534 -5.283  1.00 14.86 ?  147 VAL   B HG23 1 
ATOM   6184 N N    . ARG   B 1 148 ? 30.701 -19.743 -8.628  1.00 12.68 ?  148 ARG   B N    1 
ATOM   6185 C CA   . ARG   B 1 148 ? 30.076 -19.429 -9.903  1.00 13.12 ?  148 ARG   B CA   1 
ATOM   6186 C C    . ARG   B 1 148 ? 31.037 -18.767 -10.878 1.00 13.13 ?  148 ARG   B C    1 
ATOM   6187 O O    . ARG   B 1 148 ? 30.753 -18.746 -12.077 1.00 14.39 ?  148 ARG   B O    1 
ATOM   6188 C CB   . ARG   B 1 148 ? 28.843 -18.532 -9.691  1.00 13.57 ?  148 ARG   B CB   1 
ATOM   6189 C CG   . ARG   B 1 148 ? 27.755 -19.229 -8.879  1.00 14.17 ?  148 ARG   B CG   1 
ATOM   6190 C CD   . ARG   B 1 148 ? 26.559 -18.328 -8.576  1.00 14.90 ?  148 ARG   B CD   1 
ATOM   6191 N NE   . ARG   B 1 148 ? 26.954 -17.132 -7.842  1.00 14.67 ?  148 ARG   B NE   1 
ATOM   6192 C CZ   . ARG   B 1 148 ? 27.255 -17.102 -6.550  1.00 13.75 ?  148 ARG   B CZ   1 
ATOM   6193 N NH1  . ARG   B 1 148 ? 27.167 -18.184 -5.791  1.00 13.93 ?  148 ARG   B NH1  1 
ATOM   6194 N NH2  . ARG   B 1 148 ? 27.662 -15.956 -6.005  1.00 14.28 ?  148 ARG   B NH2  1 
ATOM   6195 H H    . ARG   B 1 148 ? 30.922 -19.041 -8.176  1.00 15.19 ?  148 ARG   B H    1 
ATOM   6196 H HA   . ARG   B 1 148 ? 29.768 -20.252 -10.308 1.00 15.72 ?  148 ARG   B HA   1 
ATOM   6197 H HB2  . ARG   B 1 148 ? 29.108 -17.731 -9.211  1.00 16.26 ?  148 ARG   B HB2  1 
ATOM   6198 H HB3  . ARG   B 1 148 ? 28.468 -18.294 -10.554 1.00 16.26 ?  148 ARG   B HB3  1 
ATOM   6199 H HG2  . ARG   B 1 148 ? 27.430 -19.996 -9.380  1.00 16.97 ?  148 ARG   B HG2  1 
ATOM   6200 H HG3  . ARG   B 1 148 ? 28.129 -19.522 -8.034  1.00 16.97 ?  148 ARG   B HG3  1 
ATOM   6201 H HD2  . ARG   B 1 148 ? 26.149 -18.048 -9.409  1.00 17.85 ?  148 ARG   B HD2  1 
ATOM   6202 H HD3  . ARG   B 1 148 ? 25.916 -18.818 -8.036  1.00 17.85 ?  148 ARG   B HD3  1 
ATOM   6203 H HE   . ARG   B 1 148 ? 27.007 -16.398 -8.277  1.00 17.58 ?  148 ARG   B HE   1 
ATOM   6204 H HH11 . ARG   B 1 148 ? 26.902 -18.933 -6.126  1.00 16.69 ?  148 ARG   B HH11 1 
ATOM   6205 H HH12 . ARG   B 1 148 ? 27.361 -18.142 -4.951  1.00 16.69 ?  148 ARG   B HH12 1 
ATOM   6206 H HH21 . ARG   B 1 148 ? 27.728 -15.253 -6.491  1.00 17.11 ?  148 ARG   B HH21 1 
ATOM   6207 H HH22 . ARG   B 1 148 ? 27.860 -15.925 -5.169  1.00 17.11 ?  148 ARG   B HH22 1 
ATOM   6208 N N    . THR   B 1 149 ? 32.144 -18.209 -10.390 1.00 13.13 ?  149 THR   B N    1 
ATOM   6209 C CA   . THR   B 1 149 ? 33.192 -17.652 -11.232 1.00 12.90 ?  149 THR   B CA   1 
ATOM   6210 C C    . THR   B 1 149 ? 34.076 -18.793 -11.739 1.00 12.55 ?  149 THR   B C    1 
ATOM   6211 O O    . THR   B 1 149 ? 33.882 -19.961 -11.393 1.00 12.85 ?  149 THR   B O    1 
ATOM   6212 C CB   . THR   B 1 149 ? 33.963 -16.597 -10.448 1.00 12.98 ?  149 THR   B CB   1 
ATOM   6213 O OG1  . THR   B 1 149 ? 34.410 -17.184 -9.225  1.00 13.04 ?  149 THR   B OG1  1 
ATOM   6214 C CG2  . THR   B 1 149 ? 33.077 -15.392 -10.155 1.00 13.49 ?  149 THR   B CG2  1 
ATOM   6215 H H    . THR   B 1 149 ? 32.306 -18.136 -9.550  1.00 15.73 ?  149 THR   B H    1 
ATOM   6216 H HA   . THR   B 1 149 ? 32.787 -17.215 -11.997 1.00 15.46 ?  149 THR   B HA   1 
ATOM   6217 H HB   . THR   B 1 149 ? 34.728 -16.306 -10.957 1.00 15.55 ?  149 THR   B HB   1 
ATOM   6218 H HG1  . THR   B 1 149 ? 34.828 -16.613 -8.761  1.00 15.62 ?  149 THR   B HG1  1 
ATOM   6219 H HG21 . THR   B 1 149 ? 33.581 -14.721 -9.666  1.00 16.17 ?  149 THR   B HG21 1 
ATOM   6220 H HG22 . THR   B 1 149 ? 32.763 -15.003 -10.986 1.00 16.17 ?  149 THR   B HG22 1 
ATOM   6221 H HG23 . THR   B 1 149 ? 32.311 -15.658 -9.622  1.00 16.17 ?  149 THR   B HG23 1 
ATOM   6222 N N    . ASN   B 1 150 ? 35.043 -18.476 -12.590 1.00 12.49 ?  150 ASN   B N    1 
ATOM   6223 C CA   . ASN   B 1 150 ? 35.817 -19.504 -13.279 1.00 13.00 ?  150 ASN   B CA   1 
ATOM   6224 C C    . ASN   B 1 150 ? 36.979 -19.950 -12.401 1.00 12.64 ?  150 ASN   B C    1 
ATOM   6225 O O    . ASN   B 1 150 ? 37.905 -19.176 -12.135 1.00 13.13 ?  150 ASN   B O    1 
ATOM   6226 C CB   . ASN   B 1 150 ? 36.289 -18.985 -14.627 1.00 15.00 ?  150 ASN   B CB   1 
ATOM   6227 C CG   . ASN   B 1 150 ? 35.143 -18.773 -15.572 1.00 17.49 ?  150 ASN   B CG   1 
ATOM   6228 O OD1  . ASN   B 1 150 ? 34.258 -19.615 -15.674 1.00 18.51 ?  150 ASN   B OD1  1 
ATOM   6229 N ND2  . ASN   B 1 150 ? 35.123 -17.634 -16.240 1.00 19.18 ?  150 ASN   B ND2  1 
ATOM   6230 H H    . ASN   B 1 150 ? 35.283 -17.668 -12.778 1.00 14.96 ?  150 ASN   B H    1 
ATOM   6231 H HA   . ASN   B 1 150 ? 35.242 -20.272 -13.438 1.00 15.57 ?  150 ASN   B HA   1 
ATOM   6232 H HB2  . ASN   B 1 150 ? 36.737 -18.132 -14.500 1.00 17.97 ?  150 ASN   B HB2  1 
ATOM   6233 H HB3  . ASN   B 1 150 ? 36.897 -19.627 -15.022 1.00 17.97 ?  150 ASN   B HB3  1 
ATOM   6234 H HD21 . ASN   B 1 150 ? 34.486 -17.469 -16.793 1.00 22.99 ?  150 ASN   B HD21 1 
ATOM   6235 H HD22 . ASN   B 1 150 ? 35.759 -17.061 -16.135 1.00 22.99 ?  150 ASN   B HD22 1 
ATOM   6236 N N    . VAL   B 1 151 ? 36.934 -21.200 -11.954 1.00 12.30 ?  151 VAL   B N    1 
ATOM   6237 C CA   . VAL   B 1 151 ? 37.945 -21.732 -11.055 1.00 12.66 ?  151 VAL   B CA   1 
ATOM   6238 C C    . VAL   B 1 151 ? 38.653 -22.901 -11.725 1.00 12.20 ?  151 VAL   B C    1 
ATOM   6239 O O    . VAL   B 1 151 ? 38.013 -23.838 -12.226 1.00 13.39 ?  151 VAL   B O    1 
ATOM   6240 C CB   . VAL   B 1 151 ? 37.374 -22.065 -9.662  1.00 14.04 ?  151 VAL   B CB   1 
ATOM   6241 C CG1  . VAL   B 1 151 ? 36.213 -23.060 -9.747  1.00 15.15 ?  151 VAL   B CG1  1 
ATOM   6242 C CG2  . VAL   B 1 151 ? 38.484 -22.547 -8.734  1.00 14.22 ?  151 VAL   B CG2  1 
ATOM   6243 H H    . VAL   B 1 151 ? 36.312 -21.763 -12.158 1.00 14.73 ?  151 VAL   B H    1 
ATOM   6244 H HA   . VAL   B 1 151 ? 38.610 -21.038 -10.919 1.00 15.17 ?  151 VAL   B HA   1 
ATOM   6245 H HB   . VAL   B 1 151 ? 37.018 -21.247 -9.277  1.00 16.82 ?  151 VAL   B HB   1 
ATOM   6246 H HG11 . VAL   B 1 151 ? 35.886 -23.246 -8.851  1.00 18.15 ?  151 VAL   B HG11 1 
ATOM   6247 H HG12 . VAL   B 1 151 ? 35.499 -22.672 -10.281 1.00 18.15 ?  151 VAL   B HG12 1 
ATOM   6248 H HG13 . VAL   B 1 151 ? 36.524 -23.880 -10.161 1.00 18.15 ?  151 VAL   B HG13 1 
ATOM   6249 H HG21 . VAL   B 1 151 ? 38.127 -22.628 -7.833  1.00 17.04 ?  151 VAL   B HG21 1 
ATOM   6250 H HG22 . VAL   B 1 151 ? 38.807 -23.405 -9.040  1.00 17.04 ?  151 VAL   B HG22 1 
ATOM   6251 H HG23 . VAL   B 1 151 ? 39.205 -21.896 -8.740  1.00 17.04 ?  151 VAL   B HG23 1 
ATOM   6252 N N    . TYR   B 1 152 ? 39.982 -22.812 -11.747 1.00 11.67 ?  152 TYR   B N    1 
ATOM   6253 C CA   . TYR   B 1 152 ? 40.887 -23.801 -12.319 1.00 11.79 ?  152 TYR   B CA   1 
ATOM   6254 C C    . TYR   B 1 152 ? 41.603 -24.470 -11.153 1.00 11.19 ?  152 TYR   B C    1 
ATOM   6255 O O    . TYR   B 1 152 ? 42.440 -23.845 -10.495 1.00 11.95 ?  152 TYR   B O    1 
ATOM   6256 C CB   . TYR   B 1 152 ? 41.863 -23.102 -13.269 1.00 12.85 ?  152 TYR   B CB   1 
ATOM   6257 C CG   . TYR   B 1 152 ? 41.185 -22.641 -14.540 1.00 13.38 ?  152 TYR   B CG   1 
ATOM   6258 C CD1  . TYR   B 1 152 ? 40.503 -21.430 -14.603 1.00 13.78 ?  152 TYR   B CD1  1 
ATOM   6259 C CD2  . TYR   B 1 152 ? 41.195 -23.446 -15.665 1.00 13.95 ?  152 TYR   B CD2  1 
ATOM   6260 C CE1  . TYR   B 1 152 ? 39.869 -21.032 -15.763 1.00 14.88 ?  152 TYR   B CE1  1 
ATOM   6261 C CE2  . TYR   B 1 152 ? 40.563 -23.062 -16.827 1.00 15.47 ?  152 TYR   B CE2  1 
ATOM   6262 C CZ   . TYR   B 1 152 ? 39.898 -21.853 -16.876 1.00 15.40 ?  152 TYR   B CZ   1 
ATOM   6263 O OH   . TYR   B 1 152 ? 39.272 -21.475 -18.037 1.00 18.22 ?  152 TYR   B OH   1 
ATOM   6264 H H    . TYR   B 1 152 ? 40.407 -22.138 -11.412 1.00 13.98 ?  152 TYR   B H    1 
ATOM   6265 H HA   . TYR   B 1 152 ? 40.378 -24.470 -12.806 1.00 14.12 ?  152 TYR   B HA   1 
ATOM   6266 H HB2  . TYR   B 1 152 ? 42.232 -22.328 -12.819 1.00 15.39 ?  152 TYR   B HB2  1 
ATOM   6267 H HB3  . TYR   B 1 152 ? 42.569 -23.724 -13.501 1.00 15.39 ?  152 TYR   B HB3  1 
ATOM   6268 H HD1  . TYR   B 1 152 ? 40.475 -20.881 -13.849 1.00 16.51 ?  152 TYR   B HD1  1 
ATOM   6269 H HD2  . TYR   B 1 152 ? 41.642 -24.268 -15.633 1.00 16.71 ?  152 TYR   B HD2  1 
ATOM   6270 H HE1  . TYR   B 1 152 ? 39.422 -20.221 -15.793 1.00 17.83 ?  152 TYR   B HE1  1 
ATOM   6271 H HE2  . TYR   B 1 152 ? 40.592 -23.612 -17.575 1.00 18.54 ?  152 TYR   B HE2  1 
ATOM   6272 H HH   . TYR   B 1 152 ? 38.916 -20.722 -17.926 1.00 21.83 ?  152 TYR   B HH   1 
ATOM   6273 N N    . LEU   B 1 153 ? 41.246 -25.727 -10.880 1.00 11.57 ?  153 LEU   B N    1 
ATOM   6274 C CA   . LEU   B 1 153 ? 41.749 -26.467 -9.731  1.00 11.61 ?  153 LEU   B CA   1 
ATOM   6275 C C    . LEU   B 1 153 ? 42.981 -27.271 -10.117 1.00 11.71 ?  153 LEU   B C    1 
ATOM   6276 O O    . LEU   B 1 153 ? 42.966 -27.999 -11.111 1.00 12.67 ?  153 LEU   B O    1 
ATOM   6277 C CB   . LEU   B 1 153 ? 40.670 -27.424 -9.215  1.00 11.99 ?  153 LEU   B CB   1 
ATOM   6278 C CG   . LEU   B 1 153 ? 39.406 -26.769 -8.665  1.00 13.15 ?  153 LEU   B CG   1 
ATOM   6279 C CD1  . LEU   B 1 153 ? 38.300 -27.806 -8.505  1.00 13.74 ?  153 LEU   B CD1  1 
ATOM   6280 C CD2  . LEU   B 1 153 ? 39.697 -26.084 -7.341  1.00 13.58 ?  153 LEU   B CD2  1 
ATOM   6281 H H    . LEU   B 1 153 ? 40.687 -26.179 -11.356 1.00 13.85 ?  153 LEU   B H    1 
ATOM   6282 H HA   . LEU   B 1 153 ? 41.979 -25.849 -9.024  1.00 13.91 ?  153 LEU   B HA   1 
ATOM   6283 H HB2  . LEU   B 1 153 ? 40.401 -28.007 -9.938  1.00 14.36 ?  153 LEU   B HB2  1 
ATOM   6284 H HB3  . LEU   B 1 153 ? 41.052 -27.956 -8.495  1.00 14.36 ?  153 LEU   B HB3  1 
ATOM   6285 H HG   . LEU   B 1 153 ? 39.098 -26.090 -9.289  1.00 15.76 ?  153 LEU   B HG   1 
ATOM   6286 H HD11 . LEU   B 1 153 ? 37.493 -27.357 -8.201  1.00 16.46 ?  153 LEU   B HD11 1 
ATOM   6287 H HD12 . LEU   B 1 153 ? 38.144 -28.228 -9.358  1.00 16.46 ?  153 LEU   B HD12 1 
ATOM   6288 H HD13 . LEU   B 1 153 ? 38.581 -28.460 -7.848  1.00 16.46 ?  153 LEU   B HD13 1 
ATOM   6289 H HD21 . LEU   B 1 153 ? 38.879 -25.714 -6.982  1.00 16.27 ?  153 LEU   B HD21 1 
ATOM   6290 H HD22 . LEU   B 1 153 ? 40.068 -26.735 -6.724  1.00 16.27 ?  153 LEU   B HD22 1 
ATOM   6291 H HD23 . LEU   B 1 153 ? 40.345 -25.371 -7.489  1.00 16.27 ?  153 LEU   B HD23 1 
ATOM   6292 N N    . ALA   B 1 154 ? 44.032 -27.155 -9.313  1.00 11.69 ?  154 ALA   B N    1 
ATOM   6293 C CA   . ALA   B 1 154 ? 45.259 -27.923 -9.489  1.00 13.18 ?  154 ALA   B CA   1 
ATOM   6294 C C    . ALA   B 1 154 ? 45.320 -28.999 -8.410  1.00 13.60 ?  154 ALA   B C    1 
ATOM   6295 O O    . ALA   B 1 154 ? 45.238 -28.700 -7.211  1.00 14.59 ?  154 ALA   B O    1 
ATOM   6296 C CB   . ALA   B 1 154 ? 46.487 -27.018 -9.428  1.00 14.03 ?  154 ALA   B CB   1 
ATOM   6297 H H    . ALA   B 1 154 ? 44.051 -26.623 -8.635  1.00 14.00 ?  154 ALA   B H    1 
ATOM   6298 H HA   . ALA   B 1 154 ? 45.243 -28.355 -10.355 1.00 15.79 ?  154 ALA   B HA   1 
ATOM   6299 H HB1  . ALA   B 1 154 ? 47.284 -27.557 -9.549  1.00 16.81 ?  154 ALA   B HB1  1 
ATOM   6300 H HB2  . ALA   B 1 154 ? 46.429 -26.352 -10.134 1.00 16.81 ?  154 ALA   B HB2  1 
ATOM   6301 H HB3  . ALA   B 1 154 ? 46.516 -26.576 -8.563  1.00 16.81 ?  154 ALA   B HB3  1 
ATOM   6302 N N    . VAL   B 1 155 ? 45.444 -30.248 -8.841  1.00 13.03 ?  155 VAL   B N    1 
ATOM   6303 C CA   . VAL   B 1 155 ? 45.549 -31.397 -7.951  1.00 13.36 ?  155 VAL   B CA   1 
ATOM   6304 C C    . VAL   B 1 155 ? 46.893 -32.064 -8.224  1.00 12.93 ?  155 VAL   B C    1 
ATOM   6305 O O    . VAL   B 1 155 ? 47.137 -32.556 -9.333  1.00 14.73 ?  155 VAL   B O    1 
ATOM   6306 C CB   . VAL   B 1 155 ? 44.395 -32.391 -8.165  1.00 14.66 ?  155 VAL   B CB   1 
ATOM   6307 C CG1  . VAL   B 1 155 ? 44.570 -33.598 -7.260  1.00 15.03 ?  155 VAL   B CG1  1 
ATOM   6308 C CG2  . VAL   B 1 155 ? 43.058 -31.696 -7.921  1.00 15.54 ?  155 VAL   B CG2  1 
ATOM   6309 H H    . VAL   B 1 155 ? 45.477 -30.460 -9.675  1.00 15.61 ?  155 VAL   B H    1 
ATOM   6310 H HA   . VAL   B 1 155 ? 45.534 -31.099 -7.029  1.00 16.01 ?  155 VAL   B HA   1 
ATOM   6311 H HB   . VAL   B 1 155 ? 44.408 -32.694 -9.087  1.00 17.56 ?  155 VAL   B HB   1 
ATOM   6312 H HG11 . VAL   B 1 155 ? 43.743 -34.103 -7.242  1.00 18.01 ?  155 VAL   B HG11 1 
ATOM   6313 H HG12 . VAL   B 1 155 ? 45.286 -34.156 -7.608  1.00 18.01 ?  155 VAL   B HG12 1 
ATOM   6314 H HG13 . VAL   B 1 155 ? 44.792 -33.296 -6.366  1.00 18.01 ?  155 VAL   B HG13 1 
ATOM   6315 H HG21 . VAL   B 1 155 ? 42.347 -32.349 -8.003  1.00 18.62 ?  155 VAL   B HG21 1 
ATOM   6316 H HG22 . VAL   B 1 155 ? 43.060 -31.317 -7.028  1.00 18.62 ?  155 VAL   B HG22 1 
ATOM   6317 H HG23 . VAL   B 1 155 ? 42.940 -30.993 -8.579  1.00 18.62 ?  155 VAL   B HG23 1 
ATOM   6318 N N    . PHE   B 1 156 ? 47.757 -32.096 -7.207  1.00 13.23 ?  156 PHE   B N    1 
ATOM   6319 C CA   . PHE   B 1 156 ? 49.135 -32.552 -7.398  1.00 14.76 ?  156 PHE   B CA   1 
ATOM   6320 C C    . PHE   B 1 156 ? 49.234 -34.052 -7.673  1.00 15.65 ?  156 PHE   B C    1 
ATOM   6321 O O    . PHE   B 1 156 ? 49.958 -34.476 -8.581  1.00 17.38 ?  156 PHE   B O    1 
ATOM   6322 C CB   . PHE   B 1 156 ? 49.958 -32.185 -6.170  1.00 14.94 ?  156 PHE   B CB   1 
ATOM   6323 C CG   . PHE   B 1 156 ? 51.384 -32.654 -6.229  1.00 15.55 ?  156 PHE   B CG   1 
ATOM   6324 C CD1  . PHE   B 1 156 ? 52.268 -32.106 -7.136  1.00 17.26 ?  156 PHE   B CD1  1 
ATOM   6325 C CD2  . PHE   B 1 156 ? 51.841 -33.625 -5.362  1.00 15.99 ?  156 PHE   B CD2  1 
ATOM   6326 C CE1  . PHE   B 1 156 ? 53.587 -32.520 -7.187  1.00 18.20 ?  156 PHE   B CE1  1 
ATOM   6327 C CE2  . PHE   B 1 156 ? 53.163 -34.046 -5.407  1.00 17.37 ?  156 PHE   B CE2  1 
ATOM   6328 C CZ   . PHE   B 1 156 ? 54.031 -33.494 -6.325  1.00 18.20 ?  156 PHE   B CZ   1 
ATOM   6329 H H    . PHE   B 1 156 ? 47.568 -31.868 -6.400  1.00 15.84 ?  156 PHE   B H    1 
ATOM   6330 H HA   . PHE   B 1 156 ? 49.512 -32.087 -8.160  1.00 17.69 ?  156 PHE   B HA   1 
ATOM   6331 H HB2  . PHE   B 1 156 ? 49.969 -31.220 -6.082  1.00 17.91 ?  156 PHE   B HB2  1 
ATOM   6332 H HB3  . PHE   B 1 156 ? 49.549 -32.584 -5.388  1.00 17.91 ?  156 PHE   B HB3  1 
ATOM   6333 H HD1  . PHE   B 1 156 ? 51.975 -31.444 -7.722  1.00 20.69 ?  156 PHE   B HD1  1 
ATOM   6334 H HD2  . PHE   B 1 156 ? 51.255 -34.006 -4.746  1.00 19.16 ?  156 PHE   B HD2  1 
ATOM   6335 H HE1  . PHE   B 1 156 ? 54.175 -32.143 -7.807  1.00 21.82 ?  156 PHE   B HE1  1 
ATOM   6336 H HE2  . PHE   B 1 156 ? 53.459 -34.712 -4.825  1.00 20.82 ?  156 PHE   B HE2  1 
ATOM   6337 H HZ   . PHE   B 1 156 ? 54.918 -33.779 -6.358  1.00 21.81 ?  156 PHE   B HZ   1 
ATOM   6338 N N    . ASP   B 1 157 ? 48.566 -34.871 -6.872  1.00 15.92 ?  157 ASP   B N    1 
ATOM   6339 C CA   . ASP   B 1 157 ? 48.709 -36.320 -6.969  1.00 17.51 ?  157 ASP   B CA   1 
ATOM   6340 C C    . ASP   B 1 157 ? 47.794 -36.864 -8.061  1.00 17.33 ?  157 ASP   B C    1 
ATOM   6341 O O    . ASP   B 1 157 ? 46.568 -36.760 -7.952  1.00 16.74 ?  157 ASP   B O    1 
ATOM   6342 C CB   . ASP   B 1 157 ? 48.334 -36.933 -5.626  1.00 19.22 ?  157 ASP   B CB   1 
ATOM   6343 C CG   . ASP   B 1 157 ? 48.476 -38.441 -5.607  1.00 21.58 ?  157 ASP   B CG   1 
ATOM   6344 O OD1  . ASP   B 1 157 ? 48.803 -39.044 -6.655  1.00 21.74 ?  157 ASP   B OD1  1 
ATOM   6345 O OD2  . ASP   B 1 157 ? 48.271 -39.019 -4.523  1.00 23.61 -1 157 ASP   B OD2  1 
ATOM   6346 H H    . ASP   B 1 157 ? 48.024 -34.612 -6.260  1.00 19.08 ?  157 ASP   B H    1 
ATOM   6347 H HA   . ASP   B 1 157 ? 49.629 -36.553 -7.177  1.00 20.99 ?  157 ASP   B HA   1 
ATOM   6348 H HB2  . ASP   B 1 157 ? 48.903 -36.557 -4.939  1.00 23.04 ?  157 ASP   B HB2  1 
ATOM   6349 H HB3  . ASP   B 1 157 ? 47.404 -36.720 -5.434  1.00 23.04 ?  157 ASP   B HB3  1 
ATOM   6350 N N    . LYS   B 1 158 ? 48.386 -37.479 -9.094  1.00 18.51 ?  158 LYS   B N    1 
ATOM   6351 C CA   . LYS   B 1 158 ? 47.605 -38.091 -10.174 1.00 19.89 ?  158 LYS   B CA   1 
ATOM   6352 C C    . LYS   B 1 158 ? 46.546 -39.056 -9.642  1.00 19.68 ?  158 LYS   B C    1 
ATOM   6353 O O    . LYS   B 1 158 ? 45.442 -39.149 -10.195 1.00 19.66 ?  158 LYS   B O    1 
ATOM   6354 C CB   . LYS   B 1 158 ? 48.547 -38.811 -11.147 1.00 21.44 ?  158 LYS   B CB   1 
ATOM   6355 C CG   . LYS   B 1 158 ? 47.864 -39.711 -12.168 1.00 23.16 ?  158 LYS   B CG   1 
ATOM   6356 C CD   . LYS   B 1 158 ? 47.037 -38.930 -13.165 1.00 25.34 ?  158 LYS   B CD   1 
ATOM   6357 C CE   . LYS   B 1 158 ? 46.447 -39.854 -14.219 1.00 27.23 ?  158 LYS   B CE   1 
ATOM   6358 N NZ   . LYS   B 1 158 ? 45.369 -39.193 -15.007 1.00 27.28 ?  158 LYS   B NZ   1 
ATOM   6359 H H    . LYS   B 1 158 ? 49.242 -37.550 -9.194  1.00 22.18 ?  158 LYS   B H    1 
ATOM   6360 H HA   . LYS   B 1 158 ? 47.153 -37.389 -10.671 1.00 23.84 ?  158 LYS   B HA   1 
ATOM   6361 H HB2  . LYS   B 1 158 ? 49.049 -38.142 -11.648 1.00 25.70 ?  158 LYS   B HB2  1 
ATOM   6362 H HB3  . LYS   B 1 158 ? 49.162 -39.359 -10.640 1.00 25.70 ?  158 LYS   B HB3  1 
ATOM   6363 H HG2  . LYS   B 1 158 ? 48.545 -40.192 -12.665 1.00 27.77 ?  158 LYS   B HG2  1 
ATOM   6364 H HG3  . LYS   B 1 158 ? 47.284 -40.349 -11.720 1.00 27.77 ?  158 LYS   B HG3  1 
ATOM   6365 H HD2  . LYS   B 1 158 ? 46.309 -38.486 -12.704 1.00 30.38 ?  158 LYS   B HD2  1 
ATOM   6366 H HD3  . LYS   B 1 158 ? 47.602 -38.281 -13.612 1.00 30.38 ?  158 LYS   B HD3  1 
ATOM   6367 H HE2  . LYS   B 1 158 ? 47.144 -40.126 -14.833 1.00 32.65 ?  158 LYS   B HE2  1 
ATOM   6368 H HE3  . LYS   B 1 158 ? 46.064 -40.633 -13.783 1.00 32.65 ?  158 LYS   B HE3  1 
ATOM   6369 H HZ1  . LYS   B 1 158 ? 45.043 -39.756 -15.613 1.00 32.71 ?  158 LYS   B HZ1  1 
ATOM   6370 H HZ2  . LYS   B 1 158 ? 44.710 -38.935 -14.466 1.00 32.71 ?  158 LYS   B HZ2  1 
ATOM   6371 H HZ3  . LYS   B 1 158 ? 45.696 -38.476 -15.424 1.00 32.71 ?  158 LYS   B HZ3  1 
ATOM   6372 N N    . ASN   B 1 159 ? 46.870 -39.814 -8.594  1.00 19.92 ?  159 ASN   B N    1 
ATOM   6373 C CA   . ASN   B 1 159 ? 45.916 -40.798 -8.091  1.00 20.59 ?  159 ASN   B CA   1 
ATOM   6374 C C    . ASN   B 1 159 ? 44.717 -40.127 -7.422  1.00 19.21 ?  159 ASN   B C    1 
ATOM   6375 O O    . ASN   B 1 159 ? 43.586 -40.621 -7.526  1.00 19.49 ?  159 ASN   B O    1 
ATOM   6376 C CB   . ASN   B 1 159 ? 46.616 -41.778 -7.153  1.00 22.19 ?  159 ASN   B CB   1 
ATOM   6377 C CG   . ASN   B 1 159 ? 47.643 -42.624 -7.866  1.00 24.62 ?  159 ASN   B CG   1 
ATOM   6378 O OD1  . ASN   B 1 159 ? 47.395 -43.123 -8.970  1.00 25.00 ?  159 ASN   B OD1  1 
ATOM   6379 N ND2  . ASN   B 1 159 ? 48.807 -42.798 -7.241  1.00 25.26 ?  159 ASN   B ND2  1 
ATOM   6380 H H    . ASN   B 1 159 ? 47.619 -39.771 -8.173  1.00 23.87 ?  159 ASN   B H    1 
ATOM   6381 H HA   . ASN   B 1 159 ? 45.586 -41.305 -8.851  1.00 24.68 ?  159 ASN   B HA   1 
ATOM   6382 H HB2  . ASN   B 1 159 ? 47.070 -41.283 -6.456  1.00 26.61 ?  159 ASN   B HB2  1 
ATOM   6383 H HB3  . ASN   B 1 159 ? 45.958 -42.374 -6.774  1.00 26.61 ?  159 ASN   B HB3  1 
ATOM   6384 H HD21 . ASN   B 1 159 ? 49.432 -43.271 -7.604  1.00 30.29 ?  159 ASN   B HD21 1 
ATOM   6385 H HD22 . ASN   B 1 159 ? 48.939 -42.446 -6.466  1.00 30.29 ?  159 ASN   B HD22 1 
ATOM   6386 N N    . LEU   B 1 160 ? 44.929 -38.996 -6.740  1.00 18.18 ?  160 LEU   B N    1 
ATOM   6387 C CA   . LEU   B 1 160 ? 43.795 -38.259 -6.197  1.00 17.15 ?  160 LEU   B CA   1 
ATOM   6388 C C    . LEU   B 1 160 ? 43.012 -37.590 -7.314  1.00 16.20 ?  160 LEU   B C    1 
ATOM   6389 O O    . LEU   B 1 160 ? 41.775 -37.592 -7.303  1.00 15.84 ?  160 LEU   B O    1 
ATOM   6390 C CB   . LEU   B 1 160 ? 44.256 -37.234 -5.163  1.00 17.07 ?  160 LEU   B CB   1 
ATOM   6391 C CG   . LEU   B 1 160 ? 43.130 -36.334 -4.636  1.00 16.84 ?  160 LEU   B CG   1 
ATOM   6392 C CD1  . LEU   B 1 160 ? 42.001 -37.169 -4.050  1.00 17.47 ?  160 LEU   B CD1  1 
ATOM   6393 C CD2  . LEU   B 1 160 ? 43.661 -35.345 -3.607  1.00 17.06 ?  160 LEU   B CD2  1 
ATOM   6394 H H    . LEU   B 1 160 ? 45.704 -38.646 -6.590  1.00 21.79 ?  160 LEU   B H    1 
ATOM   6395 H HA   . LEU   B 1 160 ? 43.206 -38.890 -5.760  1.00 20.55 ?  160 LEU   B HA   1 
ATOM   6396 H HB2  . LEU   B 1 160 ? 44.640 -37.712 -4.408  1.00 20.45 ?  160 LEU   B HB2  1 
ATOM   6397 H HB3  . LEU   B 1 160 ? 44.933 -36.668 -5.567  1.00 20.45 ?  160 LEU   B HB3  1 
ATOM   6398 H HG   . LEU   B 1 160 ? 42.771 -35.823 -5.375  1.00 20.18 ?  160 LEU   B HG   1 
ATOM   6399 H HD11 . LEU   B 1 160 ? 41.378 -36.579 -3.603  1.00 20.94 ?  160 LEU   B HD11 1 
ATOM   6400 H HD12 . LEU   B 1 160 ? 41.550 -37.644 -4.767  1.00 20.94 ?  160 LEU   B HD12 1 
ATOM   6401 H HD13 . LEU   B 1 160 ? 42.372 -37.804 -3.416  1.00 20.94 ?  160 LEU   B HD13 1 
ATOM   6402 H HD21 . LEU   B 1 160 ? 42.935 -34.774 -3.320  1.00 20.44 ?  160 LEU   B HD21 1 
ATOM   6403 H HD22 . LEU   B 1 160 ? 44.018 -35.837 -2.851  1.00 20.44 ?  160 LEU   B HD22 1 
ATOM   6404 H HD23 . LEU   B 1 160 ? 44.363 -34.811 -4.015  1.00 20.44 ?  160 LEU   B HD23 1 
ATOM   6405 N N    . TYR   B 1 161 ? 43.715 -37.018 -8.293  1.00 16.61 ?  161 TYR   B N    1 
ATOM   6406 C CA   . TYR   B 1 161 ? 43.048 -36.462 -9.464  1.00 16.32 ?  161 TYR   B CA   1 
ATOM   6407 C C    . TYR   B 1 161 ? 42.105 -37.485 -10.086 1.00 16.25 ?  161 TYR   B C    1 
ATOM   6408 O O    . TYR   B 1 161 ? 40.933 -37.193 -10.345 1.00 16.06 ?  161 TYR   B O    1 
ATOM   6409 C CB   . TYR   B 1 161 ? 44.096 -35.990 -10.478 1.00 17.49 ?  161 TYR   B CB   1 
ATOM   6410 C CG   . TYR   B 1 161 ? 43.523 -35.526 -11.794 1.00 17.97 ?  161 TYR   B CG   1 
ATOM   6411 C CD1  . TYR   B 1 161 ? 43.124 -34.205 -11.966 1.00 17.93 ?  161 TYR   B CD1  1 
ATOM   6412 C CD2  . TYR   B 1 161 ? 43.366 -36.403 -12.864 1.00 18.64 ?  161 TYR   B CD2  1 
ATOM   6413 C CE1  . TYR   B 1 161 ? 42.595 -33.773 -13.155 1.00 18.81 ?  161 TYR   B CE1  1 
ATOM   6414 C CE2  . TYR   B 1 161 ? 42.831 -35.978 -14.059 1.00 19.98 ?  161 TYR   B CE2  1 
ATOM   6415 C CZ   . TYR   B 1 161 ? 42.451 -34.659 -14.199 1.00 19.90 ?  161 TYR   B CZ   1 
ATOM   6416 O OH   . TYR   B 1 161 ? 41.916 -34.208 -15.380 1.00 21.56 ?  161 TYR   B OH   1 
ATOM   6417 H H    . TYR   B 1 161 ? 44.568 -36.948 -8.309  1.00 19.91 ?  161 TYR   B H    1 
ATOM   6418 H HA   . TYR   B 1 161 ? 42.520 -35.694 -9.199  1.00 19.56 ?  161 TYR   B HA   1 
ATOM   6419 H HB2  . TYR   B 1 161 ? 44.588 -35.245 -10.094 1.00 20.96 ?  161 TYR   B HB2  1 
ATOM   6420 H HB3  . TYR   B 1 161 ? 44.704 -36.720 -10.667 1.00 20.96 ?  161 TYR   B HB3  1 
ATOM   6421 H HD1  . TYR   B 1 161 ? 43.220 -33.596 -11.267 1.00 21.49 ?  161 TYR   B HD1  1 
ATOM   6422 H HD2  . TYR   B 1 161 ? 43.620 -37.291 -12.771 1.00 22.34 ?  161 TYR   B HD2  1 
ATOM   6423 H HE1  . TYR   B 1 161 ? 42.337 -32.881 -13.252 1.00 22.55 ?  161 TYR   B HE1  1 
ATOM   6424 H HE2  . TYR   B 1 161 ? 42.732 -36.571 -14.769 1.00 23.95 ?  161 TYR   B HE2  1 
ATOM   6425 H HH   . TYR   B 1 161 ? 41.876 -34.838 -15.935 1.00 25.85 ?  161 TYR   B HH   1 
ATOM   6426 N N    . ASP   B 1 162 ? 42.600 -38.705 -10.314 1.00 16.72 ?  162 ASP   B N    1 
ATOM   6427 C CA   . ASP   B 1 162 ? 41.771 -39.739 -10.929 1.00 17.30 ?  162 ASP   B CA   1 
ATOM   6428 C C    . ASP   B 1 162 ? 40.562 -40.076 -10.064 1.00 16.62 ?  162 ASP   B C    1 
ATOM   6429 O O    . ASP   B 1 162 ? 39.459 -40.292 -10.583 1.00 17.11 ?  162 ASP   B O    1 
ATOM   6430 C CB   . ASP   B 1 162 ? 42.594 -41.003 -11.182 1.00 18.59 ?  162 ASP   B CB   1 
ATOM   6431 C CG   . ASP   B 1 162 ? 43.609 -40.833 -12.293 1.00 20.40 ?  162 ASP   B CG   1 
ATOM   6432 O OD1  . ASP   B 1 162 ? 43.477 -39.891 -13.098 1.00 20.33 ?  162 ASP   B OD1  1 
ATOM   6433 O OD2  . ASP   B 1 162 ? 44.531 -41.669 -12.378 1.00 22.12 -1 162 ASP   B OD2  1 
ATOM   6434 H H    . ASP   B 1 162 ? 43.403 -38.950 -10.132 1.00 20.03 ?  162 ASP   B H    1 
ATOM   6435 H HA   . ASP   B 1 162 ? 41.446 -39.421 -11.784 1.00 20.73 ?  162 ASP   B HA   1 
ATOM   6436 H HB2  . ASP   B 1 162 ? 43.077 -41.238 -10.376 1.00 22.28 ?  162 ASP   B HB2  1 
ATOM   6437 H HB3  . ASP   B 1 162 ? 41.999 -41.726 -11.436 1.00 22.28 ?  162 ASP   B HB3  1 
ATOM   6438 N N    A LYS   B 1 163 ? 40.751 -40.150 -8.745  0.66 15.78 ?  163 LYS   B N    1 
ATOM   6439 N N    B LYS   B 1 163 ? 40.747 -40.138 -8.743  0.34 16.66 ?  163 LYS   B N    1 
ATOM   6440 C CA   A LYS   B 1 163 ? 39.625 -40.423 -7.859  0.66 16.22 ?  163 LYS   B CA   1 
ATOM   6441 C CA   B LYS   B 1 163 ? 39.622 -40.425 -7.859  0.34 17.38 ?  163 LYS   B CA   1 
ATOM   6442 C C    A LYS   B 1 163 ? 38.584 -39.314 -7.932  0.66 15.28 ?  163 LYS   B C    1 
ATOM   6443 C C    B LYS   B 1 163 ? 38.584 -39.311 -7.908  0.34 15.92 ?  163 LYS   B C    1 
ATOM   6444 O O    A LYS   B 1 163 ? 37.374 -39.584 -7.948  0.66 16.02 ?  163 LYS   B O    1 
ATOM   6445 O O    B LYS   B 1 163 ? 37.375 -39.577 -7.879  0.34 16.37 ?  163 LYS   B O    1 
ATOM   6446 C CB   A LYS   B 1 163 ? 40.106 -40.601 -6.421  0.66 18.77 ?  163 LYS   B CB   1 
ATOM   6447 C CB   B LYS   B 1 163 ? 40.113 -40.628 -6.427  0.34 20.08 ?  163 LYS   B CB   1 
ATOM   6448 C CG   A LYS   B 1 163 ? 39.029 -41.167 -5.518  0.66 23.52 ?  163 LYS   B CG   1 
ATOM   6449 C CG   B LYS   B 1 163 ? 39.025 -41.122 -5.495  0.34 23.46 ?  163 LYS   B CG   1 
ATOM   6450 C CD   A LYS   B 1 163 ? 39.413 -41.153 -4.052  0.66 28.17 ?  163 LYS   B CD   1 
ATOM   6451 C CD   B LYS   B 1 163 ? 39.512 -41.298 -4.071  0.34 26.43 ?  163 LYS   B CD   1 
ATOM   6452 C CE   A LYS   B 1 163 ? 38.340 -41.850 -3.227  0.66 31.47 ?  163 LYS   B CE   1 
ATOM   6453 C CE   B LYS   B 1 163 ? 38.443 -41.981 -3.232  0.34 28.74 ?  163 LYS   B CE   1 
ATOM   6454 N NZ   A LYS   B 1 163 ? 38.378 -41.464 -1.791  0.66 33.62 ?  163 LYS   B NZ   1 
ATOM   6455 N NZ   B LYS   B 1 163 ? 38.579 -41.689 -1.779  0.34 30.65 ?  163 LYS   B NZ   1 
ATOM   6456 H H    A LYS   B 1 163 ? 41.510 -40.049 -8.350  0.66 18.91 ?  163 LYS   B H    1 
ATOM   6457 H H    B LYS   B 1 163 ? 41.501 -40.021 -8.344  0.34 19.96 ?  163 LYS   B H    1 
ATOM   6458 H HA   A LYS   B 1 163 ? 39.204 -41.250 -8.137  0.66 19.44 ?  163 LYS   B HA   1 
ATOM   6459 H HA   B LYS   B 1 163 ? 39.195 -41.245 -8.149  0.34 20.83 ?  163 LYS   B HA   1 
ATOM   6460 H HB2  A LYS   B 1 163 ? 40.860 -41.217 -6.412  0.66 22.50 ?  163 LYS   B HB2  1 
ATOM   6461 H HB2  B LYS   B 1 163 ? 40.827 -41.286 -6.428  0.34 24.07 ?  163 LYS   B HB2  1 
ATOM   6462 H HB3  A LYS   B 1 163 ? 40.376 -39.742 -6.066  0.66 22.50 ?  163 LYS   B HB3  1 
ATOM   6463 H HB3  B LYS   B 1 163 ? 40.441 -39.784 -6.082  0.34 24.07 ?  163 LYS   B HB3  1 
ATOM   6464 H HG2  A LYS   B 1 163 ? 38.220 -40.643 -5.617  0.66 28.19 ?  163 LYS   B HG2  1 
ATOM   6465 H HG2  B LYS   B 1 163 ? 38.297 -40.481 -5.484  0.34 28.12 ?  163 LYS   B HG2  1 
ATOM   6466 H HG3  A LYS   B 1 163 ? 38.856 -42.090 -5.771  0.66 28.19 ?  163 LYS   B HG3  1 
ATOM   6467 H HG3  B LYS   B 1 163 ? 38.703 -41.982 -5.810  0.34 28.12 ?  163 LYS   B HG3  1 
ATOM   6468 H HD2  A LYS   B 1 163 ? 40.251 -41.628 -3.930  0.66 33.78 ?  163 LYS   B HD2  1 
ATOM   6469 H HD2  B LYS   B 1 163 ? 40.309 -41.852 -4.067  0.34 31.69 ?  163 LYS   B HD2  1 
ATOM   6470 H HD3  A LYS   B 1 163 ? 39.492 -40.237 -3.746  0.66 33.78 ?  163 LYS   B HD3  1 
ATOM   6471 H HD3  B LYS   B 1 163 ? 39.701 -40.429 -3.683  0.34 31.69 ?  163 LYS   B HD3  1 
ATOM   6472 H HE2  A LYS   B 1 163 ? 37.465 -41.627 -3.583  0.66 37.74 ?  163 LYS   B HE2  1 
ATOM   6473 H HE2  B LYS   B 1 163 ? 37.569 -41.677 -3.524  0.34 34.46 ?  163 LYS   B HE2  1 
ATOM   6474 H HE3  A LYS   B 1 163 ? 38.478 -42.807 -3.282  0.66 37.74 ?  163 LYS   B HE3  1 
ATOM   6475 H HE3  B LYS   B 1 163 ? 38.515 -42.941 -3.353  0.34 34.46 ?  163 LYS   B HE3  1 
ATOM   6476 H HZ1  A LYS   B 1 163 ? 37.736 -41.891 -1.346  0.66 40.32 ?  163 LYS   B HZ1  1 
ATOM   6477 H HZ1  B LYS   B 1 163 ? 37.936 -42.104 -1.325  0.34 36.75 ?  163 LYS   B HZ1  1 
ATOM   6478 H HZ2  A LYS   B 1 163 ? 39.167 -41.681 -1.441  0.66 40.32 ?  163 LYS   B HZ2  1 
ATOM   6479 H HZ2  B LYS   B 1 163 ? 39.370 -41.969 -1.486  0.34 36.75 ?  163 LYS   B HZ2  1 
ATOM   6480 H HZ3  A LYS   B 1 163 ? 38.255 -40.587 -1.708  0.66 40.32 ?  163 LYS   B HZ3  1 
ATOM   6481 H HZ3  B LYS   B 1 163 ? 38.511 -40.812 -1.639  0.34 36.75 ?  163 LYS   B HZ3  1 
ATOM   6482 N N    . LEU   B 1 164 ? 39.039 -38.058 -7.976  1.00 14.74 ?  164 LEU   B N    1 
ATOM   6483 C CA   . LEU   B 1 164 ? 38.120 -36.924 -8.037  1.00 14.53 ?  164 LEU   B CA   1 
ATOM   6484 C C    . LEU   B 1 164 ? 37.345 -36.912 -9.348  1.00 14.47 ?  164 LEU   B C    1 
ATOM   6485 O O    . LEU   B 1 164 ? 36.119 -36.724 -9.358  1.00 15.62 ?  164 LEU   B O    1 
ATOM   6486 C CB   . LEU   B 1 164 ? 38.920 -35.631 -7.874  1.00 13.63 ?  164 LEU   B CB   1 
ATOM   6487 C CG   . LEU   B 1 164 ? 39.437 -35.344 -6.467  1.00 14.25 ?  164 LEU   B CG   1 
ATOM   6488 C CD1  . LEU   B 1 164 ? 40.533 -34.285 -6.520  1.00 14.55 ?  164 LEU   B CD1  1 
ATOM   6489 C CD2  . LEU   B 1 164 ? 38.325 -34.890 -5.553  1.00 16.55 ?  164 LEU   B CD2  1 
ATOM   6490 H H    A LEU   B 1 164 ? 39.875 -37.840 -7.972  0.66 17.66 ?  164 LEU   B H    1 
ATOM   6491 H H    B LEU   B 1 164 ? 39.875 -37.841 -7.992  0.34 17.66 ?  164 LEU   B H    1 
ATOM   6492 H HA   . LEU   B 1 164 ? 37.488 -36.986 -7.313  1.00 17.41 ?  164 LEU   B HA   1 
ATOM   6493 H HB2  . LEU   B 1 164 ? 39.693 -35.668 -8.465  1.00 16.33 ?  164 LEU   B HB2  1 
ATOM   6494 H HB3  . LEU   B 1 164 ? 38.358 -34.887 -8.131  1.00 16.33 ?  164 LEU   B HB3  1 
ATOM   6495 H HG   . LEU   B 1 164 ? 39.831 -36.148 -6.100  1.00 17.07 ?  164 LEU   B HG   1 
ATOM   6496 H HD11 . LEU   B 1 164 ? 40.850 -34.104 -5.618  1.00 17.44 ?  164 LEU   B HD11 1 
ATOM   6497 H HD12 . LEU   B 1 164 ? 41.273 -34.607 -7.064  1.00 17.44 ?  164 LEU   B HD12 1 
ATOM   6498 H HD13 . LEU   B 1 164 ? 40.176 -33.468 -6.908  1.00 17.44 ?  164 LEU   B HD13 1 
ATOM   6499 H HD21 . LEU   B 1 164 ? 38.699 -34.666 -4.686  1.00 19.84 ?  164 LEU   B HD21 1 
ATOM   6500 H HD22 . LEU   B 1 164 ? 37.897 -34.110 -5.939  1.00 19.84 ?  164 LEU   B HD22 1 
ATOM   6501 H HD23 . LEU   B 1 164 ? 37.685 -35.610 -5.462  1.00 19.84 ?  164 LEU   B HD23 1 
ATOM   6502 N N    . VAL   B 1 165 ? 38.046 -37.088 -10.470 1.00 15.84 ?  165 VAL   B N    1 
ATOM   6503 C CA   . VAL   B 1 165 ? 37.395 -37.029 -11.774 1.00 16.99 ?  165 VAL   B CA   1 
ATOM   6504 C C    . VAL   B 1 165 ? 36.474 -38.229 -11.959 1.00 18.64 ?  165 VAL   B C    1 
ATOM   6505 O O    . VAL   B 1 165 ? 35.318 -38.092 -12.379 1.00 19.89 ?  165 VAL   B O    1 
ATOM   6506 C CB   . VAL   B 1 165 ? 38.444 -36.941 -12.899 1.00 18.30 ?  165 VAL   B CB   1 
ATOM   6507 C CG1  . VAL   B 1 165 ? 37.780 -37.032 -14.256 1.00 19.91 ?  165 VAL   B CG1  1 
ATOM   6508 C CG2  . VAL   B 1 165 ? 39.242 -35.652 -12.786 1.00 18.11 ?  165 VAL   B CG2  1 
ATOM   6509 H H    . VAL   B 1 165 ? 38.897 -37.240 -10.505 1.00 18.98 ?  165 VAL   B H    1 
ATOM   6510 H HA   . VAL   B 1 165 ? 36.851 -36.233 -11.819 1.00 20.37 ?  165 VAL   B HA   1 
ATOM   6511 H HB   . VAL   B 1 165 ? 39.067 -37.682 -12.817 1.00 21.93 ?  165 VAL   B HB   1 
ATOM   6512 H HG11 . VAL   B 1 165 ? 38.406 -36.743 -14.935 1.00 23.86 ?  165 VAL   B HG11 1 
ATOM   6513 H HG12 . VAL   B 1 165 ? 37.525 -37.955 -14.419 1.00 23.86 ?  165 VAL   B HG12 1 
ATOM   6514 H HG13 . VAL   B 1 165 ? 36.995 -36.466 -14.262 1.00 23.86 ?  165 VAL   B HG13 1 
ATOM   6515 H HG21 . VAL   B 1 165 ? 39.878 -35.606 -13.520 1.00 21.70 ?  165 VAL   B HG21 1 
ATOM   6516 H HG22 . VAL   B 1 165 ? 38.633 -34.898 -12.832 1.00 21.70 ?  165 VAL   B HG22 1 
ATOM   6517 H HG23 . VAL   B 1 165 ? 39.716 -35.643 -11.940 1.00 21.70 ?  165 VAL   B HG23 1 
ATOM   6518 N N    . SER   B 1 166 ? 36.977 -39.428 -11.649 1.00 19.17 ?  166 SER   B N    1 
ATOM   6519 C CA   . SER   B 1 166 ? 36.213 -40.639 -11.926 1.00 20.68 ?  166 SER   B CA   1 
ATOM   6520 C C    . SER   B 1 166 ? 34.949 -40.716 -11.084 1.00 20.91 ?  166 SER   B C    1 
ATOM   6521 O O    . SER   B 1 166 ? 33.976 -41.336 -11.509 1.00 22.32 ?  166 SER   B O    1 
ATOM   6522 C CB   . SER   B 1 166 ? 37.065 -41.901 -11.736 1.00 21.51 ?  166 SER   B CB   1 
ATOM   6523 O OG   . SER   B 1 166 ? 37.447 -42.086 -10.382 1.00 21.62 ?  166 SER   B OG   1 
ATOM   6524 H H    . SER   B 1 166 ? 37.750 -39.565 -11.291 1.00 22.97 ?  166 SER   B H    1 
ATOM   6525 H HA   . SER   B 1 166 ? 35.941 -40.624 -12.856 1.00 24.78 ?  166 SER   B HA   1 
ATOM   6526 H HB2  . SER   B 1 166 ? 36.550 -42.672 -12.021 1.00 25.78 ?  166 SER   B HB2  1 
ATOM   6527 H HB3  . SER   B 1 166 ? 37.865 -41.824 -12.282 1.00 25.78 ?  166 SER   B HB3  1 
ATOM   6528 H HG   . SER   B 1 166 ? 37.910 -41.434 -10.125 1.00 25.91 ?  166 SER   B HG   1 
ATOM   6529 N N    . SER   B 1 167 ? 34.934 -40.110 -9.899  1.00 19.44 ?  167 SER   B N    1 
ATOM   6530 C CA   . SER   B 1 167 ? 33.781 -40.163 -9.010  1.00 18.95 ?  167 SER   B CA   1 
ATOM   6531 C C    . SER   B 1 167 ? 32.869 -38.942 -9.117  1.00 18.67 ?  167 SER   B C    1 
ATOM   6532 O O    . SER   B 1 167 ? 31.792 -38.933 -8.509  1.00 18.75 ?  167 SER   B O    1 
ATOM   6533 C CB   . SER   B 1 167 ? 34.233 -40.333 -7.556  1.00 19.07 ?  167 SER   B CB   1 
ATOM   6534 O OG   . SER   B 1 167 ? 34.893 -39.165 -7.087  1.00 18.98 ?  167 SER   B OG   1 
ATOM   6535 H H    . SER   B 1 167 ? 35.590 -39.657 -9.591  1.00 23.30 ?  167 SER   B H    1 
ATOM   6536 H HA   . SER   B 1 167 ? 33.255 -40.946 -9.239  1.00 22.71 ?  167 SER   B HA   1 
ATOM   6537 H HB2  . SER   B 1 167 ? 33.453 -40.502 -7.004  1.00 22.86 ?  167 SER   B HB2  1 
ATOM   6538 H HB3  . SER   B 1 167 ? 34.840 -41.093 -7.503  1.00 22.86 ?  167 SER   B HB3  1 
ATOM   6539 H HG   . SER   B 1 167 ? 35.578 -39.022 -7.554  1.00 22.74 ?  167 SER   B HG   1 
ATOM   6540 N N    . PHE   B 1 168 ? 33.250 -37.921 -9.884  1.00 18.18 ?  168 PHE   B N    1 
ATOM   6541 C CA   . PHE   B 1 168 ? 32.426 -36.717 -9.952  1.00 17.56 ?  168 PHE   B CA   1 
ATOM   6542 C C    . PHE   B 1 168 ? 31.106 -36.976 -10.666 1.00 16.07 ?  168 PHE   B C    1 
ATOM   6543 O O    . PHE   B 1 168 ? 30.076 -36.367 -10.321 1.00 16.43 ?  168 PHE   B O    1 
ATOM   6544 C CB   . PHE   B 1 168 ? 33.189 -35.595 -10.655 1.00 18.68 ?  168 PHE   B CB   1 
ATOM   6545 C CG   . PHE   B 1 168 ? 32.391 -34.334 -10.789 1.00 18.75 ?  168 PHE   B CG   1 
ATOM   6546 C CD1  . PHE   B 1 168 ? 32.072 -33.588 -9.665  1.00 20.20 ?  168 PHE   B CD1  1 
ATOM   6547 C CD2  . PHE   B 1 168 ? 31.937 -33.903 -12.023 1.00 18.35 ?  168 PHE   B CD2  1 
ATOM   6548 C CE1  . PHE   B 1 168 ? 31.320 -32.435 -9.765  1.00 20.88 ?  168 PHE   B CE1  1 
ATOM   6549 C CE2  . PHE   B 1 168 ? 31.195 -32.733 -12.135 1.00 19.27 ?  168 PHE   B CE2  1 
ATOM   6550 C CZ   . PHE   B 1 168 ? 30.881 -32.000 -11.003 1.00 20.18 ?  168 PHE   B CZ   1 
ATOM   6551 H H    . PHE   B 1 168 ? 33.967 -37.900 -10.361 1.00 21.79 ?  168 PHE   B H    1 
ATOM   6552 H HA   . PHE   B 1 168 ? 32.224 -36.422 -9.055  1.00 21.05 ?  168 PHE   B HA   1 
ATOM   6553 H HB2  . PHE   B 1 168 ? 33.987 -35.388 -10.142 1.00 22.38 ?  168 PHE   B HB2  1 
ATOM   6554 H HB3  . PHE   B 1 168 ? 33.435 -35.885 -11.546 1.00 22.38 ?  168 PHE   B HB3  1 
ATOM   6555 H HD1  . PHE   B 1 168 ? 32.360 -33.879 -8.831  1.00 24.21 ?  168 PHE   B HD1  1 
ATOM   6556 H HD2  . PHE   B 1 168 ? 32.147 -34.387 -12.788 1.00 22.00 ?  168 PHE   B HD2  1 
ATOM   6557 H HE1  . PHE   B 1 168 ? 31.114 -31.948 -9.001  1.00 25.03 ?  168 PHE   B HE1  1 
ATOM   6558 H HE2  . PHE   B 1 168 ? 30.896 -32.450 -12.971 1.00 23.10 ?  168 PHE   B HE2  1 
ATOM   6559 H HZ   . PHE   B 1 168 ? 30.376 -31.224 -11.075 1.00 24.19 ?  168 PHE   B HZ   1 
ATOM   6560 N N    . LEU   B 1 169 ? 31.125 -37.852 -11.667 1.00 16.15 ?  169 LEU   B N    1 
ATOM   6561 C CA   . LEU   B 1 169 ? 29.947 -38.154 -12.463 1.00 18.31 ?  169 LEU   B CA   1 
ATOM   6562 C C    . LEU   B 1 169 ? 29.951 -39.587 -12.985 1.00 21.14 ?  169 LEU   B C    1 
ATOM   6563 O O    . LEU   B 1 169 ? 29.046 -39.995 -13.717 1.00 23.86 ?  169 LEU   B O    1 
ATOM   6564 C CB   . LEU   B 1 169 ? 29.865 -37.193 -13.646 1.00 20.43 ?  169 LEU   B CB   1 
ATOM   6565 C CG   . LEU   B 1 169 ? 28.584 -36.371 -13.770 1.00 23.69 ?  169 LEU   B CG   1 
ATOM   6566 C CD1  . LEU   B 1 169 ? 28.542 -35.713 -15.130 1.00 24.64 ?  169 LEU   B CD1  1 
ATOM   6567 C CD2  . LEU   B 1 169 ? 27.341 -37.217 -13.538 1.00 23.86 ?  169 LEU   B CD2  1 
ATOM   6568 O OXT  . LEU   B 1 169 ? 30.864 -40.356 -12.697 1.00 21.82 -1 169 LEU   B OXT  1 
ATOM   6569 H H    . LEU   B 1 169 ? 31.832 -38.285 -11.919 1.00 19.35 ?  169 LEU   B H    1 
ATOM   6570 H HA   . LEU   B 1 169 ? 29.166 -38.032 -11.909 1.00 21.94 ?  169 LEU   B HA   1 
ATOM   6571 H HB2  . LEU   B 1 169 ? 30.603 -36.563 -13.583 1.00 24.49 ?  169 LEU   B HB2  1 
ATOM   6572 H HB3  . LEU   B 1 169 ? 29.954 -37.705 -14.465 1.00 24.49 ?  169 LEU   B HB3  1 
ATOM   6573 H HG   . LEU   B 1 169 ? 28.595 -35.666 -13.103 1.00 28.40 ?  169 LEU   B HG   1 
ATOM   6574 H HD11 . LEU   B 1 169 ? 27.741 -35.170 -15.192 1.00 29.55 ?  169 LEU   B HD11 1 
ATOM   6575 H HD12 . LEU   B 1 169 ? 29.329 -35.157 -15.234 1.00 29.55 ?  169 LEU   B HD12 1 
ATOM   6576 H HD13 . LEU   B 1 169 ? 28.530 -36.403 -15.810 1.00 29.55 ?  169 LEU   B HD13 1 
ATOM   6577 H HD21 . LEU   B 1 169 ? 26.579 -36.781 -13.944 1.00 28.60 ?  169 LEU   B HD21 1 
ATOM   6578 H HD22 . LEU   B 1 169 ? 27.477 -38.091 -13.941 1.00 28.60 ?  169 LEU   B HD22 1 
ATOM   6579 H HD23 . LEU   B 1 169 ? 27.202 -37.312 -12.584 1.00 28.60 ?  169 LEU   B HD23 1 
HETATM 6580 C C1   T TFA   C 2 .   ? 12.120 -1.338  1.432   0.20 9.64  ?  201 TFA   A C1   1 
HETATM 6581 C C2   T TFA   C 2 .   ? 12.734 -1.767  0.072   0.20 12.51 ?  201 TFA   A C2   1 
HETATM 6582 O O    T TFA   C 2 .   ? 12.864 -1.583  2.392   0.20 8.75  ?  201 TFA   A O    1 
HETATM 6583 F F1   T TFA   C 2 .   ? 12.816 -3.108  0.017   0.20 13.34 ?  201 TFA   A F1   1 
HETATM 6584 F F2   T TFA   C 2 .   ? 11.991 -1.378  -0.980  0.20 13.17 ?  201 TFA   A F2   1 
HETATM 6585 F F3   T TFA   C 2 .   ? 13.967 -1.294  -0.142  0.20 13.33 ?  201 TFA   A F3   1 
HETATM 6586 O OXT  T TFA   C 2 .   ? 10.998 -0.828  1.376   0.20 10.05 ?  201 TFA   A OXT  1 
HETATM 6587 C C1   B TFA   D 2 .   ? 16.210 2.961   -0.749  0.34 10.70 ?  202 TFA   A C1   1 
HETATM 6588 C C2   B TFA   D 2 .   ? 14.851 3.686   -0.928  0.34 13.31 ?  202 TFA   A C2   1 
HETATM 6589 O O    B TFA   D 2 .   ? 16.703 2.575   -1.809  0.34 11.02 ?  202 TFA   A O    1 
HETATM 6590 F F1   B TFA   D 2 .   ? 14.983 5.020   -0.795  0.34 14.22 ?  202 TFA   A F1   1 
HETATM 6591 F F2   B TFA   D 2 .   ? 13.962 3.283   -0.006  0.34 13.78 ?  202 TFA   A F2   1 
HETATM 6592 F F3   B TFA   D 2 .   ? 14.291 3.491   -2.126  0.34 14.89 ?  202 TFA   A F3   1 
HETATM 6593 O OXT  B TFA   D 2 .   ? 16.626 2.888   0.407   0.34 11.39 ?  202 TFA   A OXT  1 
HETATM 6594 N N2   B A1A9L E 3 .   ? 15.014 -0.307  3.956   0.34 12.52 ?  203 A1A9L A N2   1 
HETATM 6595 C C3   B A1A9L E 3 .   ? 14.151 -0.331  -0.031  0.34 14.84 ?  203 A1A9L A C3   1 
HETATM 6596 C C6   B A1A9L E 3 .   ? 10.464 0.383   0.394   0.34 16.00 ?  203 A1A9L A C6   1 
HETATM 6597 C C9   B A1A9L E 3 .   ? 14.931 -0.182  5.315   0.34 12.29 ?  203 A1A9L A C9   1 
HETATM 6598 C C12  B A1A9L E 3 .   ? 15.762 3.469   3.635   0.34 11.21 ?  203 A1A9L A C12  1 
HETATM 6599 C C1   B A1A9L E 3 .   ? 16.717 -0.568  0.276   0.34 15.24 ?  203 A1A9L A C1   1 
HETATM 6600 C C10  B A1A9L E 3 .   ? 15.350 2.025   5.333   0.34 11.54 ?  203 A1A9L A C10  1 
HETATM 6601 C C11  B A1A9L E 3 .   ? 15.467 2.078   3.921   0.34 11.63 ?  203 A1A9L A C11  1 
HETATM 6602 C C13  B A1A9L E 3 .   ? 15.798 4.168   4.818   0.34 11.48 ?  203 A1A9L A C13  1 
HETATM 6603 C C2   B A1A9L E 3 .   ? 15.320 -0.419  0.981   0.34 14.30 ?  203 A1A9L A C2   1 
HETATM 6604 C C4   B A1A9L E 3 .   ? 12.862 0.259   0.583   0.34 15.61 ?  203 A1A9L A C4   1 
HETATM 6605 C C5   B A1A9L E 3 .   ? 11.745 0.537   -0.422  0.34 16.02 ?  203 A1A9L A C5   1 
HETATM 6606 C C7   B A1A9L E 3 .   ? 12.129 -0.686  1.548   0.34 15.75 ?  203 A1A9L A C7   1 
HETATM 6607 C C8   B A1A9L E 3 .   ? 15.289 0.827   3.214   0.34 12.11 ?  203 A1A9L A C8   1 
HETATM 6608 N N1   B A1A9L E 3 .   ? 15.380 0.749   1.864   0.34 12.41 ?  203 A1A9L A N1   1 
HETATM 6609 N N3   B A1A9L E 3 .   ? 15.074 0.899   6.046   0.34 12.06 ?  203 A1A9L A N3   1 
HETATM 6610 N N4   B A1A9L E 3 .   ? 15.557 3.274   5.846   0.34 11.13 ?  203 A1A9L A N4   1 
HETATM 6611 O O1   B A1A9L E 3 .   ? 16.801 -1.750  -0.408  0.34 16.27 ?  203 A1A9L A O1   1 
HETATM 6612 O O2   B A1A9L E 3 .   ? 10.790 -0.324  1.558   0.34 16.44 ?  203 A1A9L A O2   1 
HETATM 6613 H H6   B A1A9L E 3 .   ? 14.426 0.267   -0.925  0.34 17.78 ?  203 A1A9L A H6   1 
HETATM 6614 H H7   B A1A9L E 3 .   ? 13.926 -1.315  -0.489  0.34 17.78 ?  203 A1A9L A H7   1 
HETATM 6615 H H11  B A1A9L E 3 .   ? 9.658  -0.129  -0.177  0.34 19.17 ?  203 A1A9L A H11  1 
HETATM 6616 H H10  B A1A9L E 3 .   ? 9.978  1.364   0.620   0.34 19.17 ?  203 A1A9L A H10  1 
HETATM 6617 H H15  B A1A9L E 3 .   ? 14.697 -1.085  5.918   0.34 14.73 ?  203 A1A9L A H15  1 
HETATM 6618 H H16  B A1A9L E 3 .   ? 15.920 3.921   2.677   0.34 13.42 ?  203 A1A9L A H16  1 
HETATM 6619 H H5   B A1A9L E 3 .   ? 16.865 0.336   -0.353  0.34 18.26 ?  203 A1A9L A H5   1 
HETATM 6620 H H4   B A1A9L E 3 .   ? 17.568 -0.519  0.994   0.34 18.26 ?  203 A1A9L A H4   1 
HETATM 6621 H H17  B A1A9L E 3 .   ? 15.981 5.209   5.082   0.34 13.75 ?  203 A1A9L A H17  1 
HETATM 6622 H H1   B A1A9L E 3 .   ? 15.139 -1.325  1.625   0.34 17.14 ?  203 A1A9L A H1   1 
HETATM 6623 H H2   B A1A9L E 3 .   ? 13.086 1.221   1.111   0.34 18.71 ?  203 A1A9L A H2   1 
HETATM 6624 H H9   B A1A9L E 3 .   ? 11.831 1.545   -0.878  0.34 19.20 ?  203 A1A9L A H9   1 
HETATM 6625 H H8   B A1A9L E 3 .   ? 11.761 -0.146  -1.292  0.34 19.20 ?  203 A1A9L A H8   1 
HETATM 6626 H H13  B A1A9L E 3 .   ? 12.562 -0.659  2.579   0.34 18.87 ?  203 A1A9L A H13  1 
HETATM 6627 H H12  B A1A9L E 3 .   ? 12.238 -1.768  1.293   0.34 18.87 ?  203 A1A9L A H12  1 
HETATM 6628 H H14  B A1A9L E 3 .   ? 15.499 1.617   1.360   0.34 14.86 ?  203 A1A9L A H14  1 
HETATM 6629 H H18  B A1A9L E 3 .   ? 15.516 3.504   6.838   0.34 13.33 ?  203 A1A9L A H18  1 
HETATM 6630 H H3   B A1A9L E 3 .   ? 17.712 -1.890  -0.663  0.34 19.50 ?  203 A1A9L A H3   1 
HETATM 6631 O O    . HOH   F 4 .   ? 17.130 -18.038 15.027  1.00 26.73 ?  301 HOH   A O    1 
HETATM 6632 O O    . HOH   F 4 .   ? 29.066 0.531   -9.640  1.00 22.71 ?  302 HOH   A O    1 
HETATM 6633 O O    . HOH   F 4 .   ? 12.068 0.286   14.707  1.00 30.69 ?  303 HOH   A O    1 
HETATM 6634 O O    . HOH   F 4 .   ? 14.787 -4.569  20.498  1.00 45.54 ?  304 HOH   A O    1 
HETATM 6635 O O    A HOH   F 4 .   ? 4.704  3.957   0.576   0.66 20.62 ?  305 HOH   A O    1 
HETATM 6636 O O    . HOH   F 4 .   ? 7.682  -6.316  -6.631  1.00 36.75 ?  306 HOH   A O    1 
HETATM 6637 O O    . HOH   F 4 .   ? 34.302 -1.898  12.503  1.00 34.79 ?  307 HOH   A O    1 
HETATM 6638 O O    . HOH   F 4 .   ? 10.381 -22.072 -1.331  1.00 42.04 ?  308 HOH   A O    1 
HETATM 6639 O O    B HOH   F 4 .   ? 22.692 5.643   -1.746  0.34 19.92 ?  309 HOH   A O    1 
HETATM 6640 O O    . HOH   F 4 .   ? 11.744 -10.774 -10.160 1.00 43.23 ?  310 HOH   A O    1 
HETATM 6641 O O    . HOH   F 4 .   ? -0.609 -8.470  2.248   1.00 43.56 ?  311 HOH   A O    1 
HETATM 6642 O O    . HOH   F 4 .   ? 15.104 -12.220 18.717  1.00 34.18 ?  312 HOH   A O    1 
HETATM 6643 O O    . HOH   F 4 .   ? 42.457 10.550  5.165   1.00 19.88 ?  313 HOH   A O    1 
HETATM 6644 O O    B HOH   F 4 .   ? 15.240 6.920   7.139   0.34 17.19 ?  314 HOH   A O    1 
HETATM 6645 O O    . HOH   F 4 .   ? 0.610  -4.468  0.364   1.00 31.44 ?  315 HOH   A O    1 
HETATM 6646 O O    . HOH   F 4 .   ? 14.676 -13.952 16.726  1.00 22.64 ?  316 HOH   A O    1 
HETATM 6647 O O    . HOH   F 4 .   ? 8.794  -12.059 17.103  1.00 39.24 ?  317 HOH   A O    1 
HETATM 6648 O O    . HOH   F 4 .   ? 36.159 -5.074  -0.505  1.00 27.98 ?  318 HOH   A O    1 
HETATM 6649 O O    . HOH   F 4 .   ? 9.207  -10.128 19.367  1.00 39.04 ?  319 HOH   A O    1 
HETATM 6650 O O    . HOH   F 4 .   ? 15.042 3.922   17.672  1.00 41.71 ?  320 HOH   A O    1 
HETATM 6651 O O    . HOH   F 4 .   ? 14.433 -24.724 11.586  1.00 36.49 ?  321 HOH   A O    1 
HETATM 6652 O O    . HOH   F 4 .   ? 18.620 9.540   8.965   1.00 21.51 ?  322 HOH   A O    1 
HETATM 6653 O O    . HOH   F 4 .   ? 14.244 -4.469  -11.931 1.00 29.66 ?  323 HOH   A O    1 
HETATM 6654 O O    . HOH   F 4 .   ? 13.300 -1.390  -6.669  1.00 16.16 ?  324 HOH   A O    1 
HETATM 6655 O O    . HOH   F 4 .   ? 25.762 -0.740  -7.305  1.00 15.52 ?  325 HOH   A O    1 
HETATM 6656 O O    . HOH   F 4 .   ? 38.268 10.197  7.186   1.00 50.62 ?  326 HOH   A O    1 
HETATM 6657 O O    . HOH   F 4 .   ? 30.266 -13.328 -8.576  1.00 19.76 ?  327 HOH   A O    1 
HETATM 6658 O O    . HOH   F 4 .   ? 28.421 -0.088  -13.350 1.00 32.67 ?  328 HOH   A O    1 
HETATM 6659 O O    . HOH   F 4 .   ? 13.575 -15.142 -7.559  1.00 25.32 ?  329 HOH   A O    1 
HETATM 6660 O O    . HOH   F 4 .   ? 19.897 -12.410 -9.014  1.00 24.10 ?  330 HOH   A O    1 
HETATM 6661 O O    . HOH   F 4 .   ? 28.176 -6.355  19.662  1.00 42.41 ?  331 HOH   A O    1 
HETATM 6662 O O    . HOH   F 4 .   ? 34.047 -0.999  -8.882  1.00 27.90 ?  332 HOH   A O    1 
HETATM 6663 O O    B HOH   F 4 .   ? 21.723 3.179   -0.161  0.34 13.16 ?  333 HOH   A O    1 
HETATM 6664 O O    . HOH   F 4 .   ? 7.955  -12.562 -0.890  1.00 21.67 ?  334 HOH   A O    1 
HETATM 6665 O O    . HOH   F 4 .   ? 8.166  -21.489 3.896   1.00 50.81 ?  335 HOH   A O    1 
HETATM 6666 O O    . HOH   F 4 .   ? 26.458 -19.304 -1.813  1.00 14.02 ?  336 HOH   A O    1 
HETATM 6667 O O    . HOH   F 4 .   ? 18.821 -21.940 6.853   1.00 32.90 ?  337 HOH   A O    1 
HETATM 6668 O O    . HOH   F 4 .   ? 37.538 2.792   10.255  1.00 27.89 ?  338 HOH   A O    1 
HETATM 6669 O O    A HOH   F 4 .   ? 14.630 -3.630  3.070   0.66 14.82 ?  339 HOH   A O    1 
HETATM 6670 O O    . HOH   F 4 .   ? 22.287 5.412   18.917  1.00 42.56 ?  340 HOH   A O    1 
HETATM 6671 O O    . HOH   F 4 .   ? 30.953 -18.162 7.769   1.00 20.09 ?  341 HOH   A O    1 
HETATM 6672 O O    . HOH   F 4 .   ? 18.655 -19.421 13.542  1.00 39.86 ?  342 HOH   A O    1 
HETATM 6673 O O    A HOH   F 4 .   ? 3.572  -9.435  9.670   0.66 25.95 ?  343 HOH   A O    1 
HETATM 6674 O O    B HOH   F 4 .   ? 12.160 -1.504  -3.714  0.34 16.15 ?  344 HOH   A O    1 
HETATM 6675 O O    . HOH   F 4 .   ? 9.815  -21.391 5.661   1.00 18.52 ?  345 HOH   A O    1 
HETATM 6676 O O    . HOH   F 4 .   ? 22.765 12.516  1.612   1.00 15.28 ?  346 HOH   A O    1 
HETATM 6677 O O    . HOH   F 4 .   ? 27.344 13.794  2.908   1.00 32.47 ?  347 HOH   A O    1 
HETATM 6678 O O    . HOH   F 4 .   ? -0.417 -3.069  3.069   1.00 37.72 ?  348 HOH   A O    1 
HETATM 6679 O O    . HOH   F 4 .   ? 39.807 -0.985  -5.135  1.00 22.06 ?  349 HOH   A O    1 
HETATM 6680 O O    . HOH   F 4 .   ? 22.208 -19.338 11.311  1.00 36.23 ?  350 HOH   A O    1 
HETATM 6681 O O    . HOH   F 4 .   ? 44.375 7.132   6.494   1.00 27.76 ?  351 HOH   A O    1 
HETATM 6682 O O    . HOH   F 4 .   ? 17.148 -17.794 -5.091  1.00 25.73 ?  352 HOH   A O    1 
HETATM 6683 O O    . HOH   F 4 .   ? 26.914 11.429  1.670   1.00 17.53 ?  353 HOH   A O    1 
HETATM 6684 O O    . HOH   F 4 .   ? 23.532 11.421  4.066   1.00 13.17 ?  354 HOH   A O    1 
HETATM 6685 O O    . HOH   F 4 .   ? 24.094 -2.060  -2.069  1.00 10.71 ?  355 HOH   A O    1 
HETATM 6686 O O    . HOH   F 4 .   ? 20.660 -19.699 -5.139  1.00 27.74 ?  356 HOH   A O    1 
HETATM 6687 O O    B HOH   F 4 .   ? 14.819 -2.965  3.424   0.34 13.64 ?  357 HOH   A O    1 
HETATM 6688 O O    . HOH   F 4 .   ? 42.624 4.312   5.453   1.00 31.60 ?  358 HOH   A O    1 
HETATM 6689 O O    . HOH   F 4 .   ? 21.340 -2.355  -2.296  1.00 14.77 ?  359 HOH   A O    1 
HETATM 6690 O O    . HOH   F 4 .   ? 14.353 -21.081 -4.348  1.00 30.45 ?  360 HOH   A O    1 
HETATM 6691 O O    . HOH   F 4 .   ? 31.700 8.169   14.915  1.00 24.01 ?  361 HOH   A O    1 
HETATM 6692 O O    A HOH   F 4 .   ? 14.267 0.593   6.778   0.66 21.50 ?  362 HOH   A O    1 
HETATM 6693 O O    . HOH   F 4 .   ? 38.567 4.969   7.063   1.00 15.92 ?  363 HOH   A O    1 
HETATM 6694 O O    . HOH   F 4 .   ? 35.740 -12.666 6.836   1.00 16.43 ?  364 HOH   A O    1 
HETATM 6695 O O    . HOH   F 4 .   ? 37.236 -2.821  9.709   1.00 40.34 ?  365 HOH   A O    1 
HETATM 6696 O O    . HOH   F 4 .   ? 31.071 -13.933 -2.503  1.00 13.87 ?  366 HOH   A O    1 
HETATM 6697 O O    . HOH   F 4 .   ? 30.815 3.081   8.319   1.00 12.05 ?  367 HOH   A O    1 
HETATM 6698 O O    . HOH   F 4 .   ? 21.821 -13.691 -8.187  1.00 40.74 ?  368 HOH   A O    1 
HETATM 6699 O O    . HOH   F 4 .   ? 27.440 -5.926  -13.960 1.00 37.01 ?  369 HOH   A O    1 
HETATM 6700 O O    . HOH   F 4 .   ? 21.864 -21.900 8.374   1.00 29.10 ?  370 HOH   A O    1 
HETATM 6701 O O    A HOH   F 4 .   ? 17.500 -1.690  0.424   0.66 16.64 ?  371 HOH   A O    1 
HETATM 6702 O O    . HOH   F 4 .   ? 31.933 -9.281  -6.645  1.00 21.99 ?  372 HOH   A O    1 
HETATM 6703 O O    . HOH   F 4 .   ? 27.439 -10.651 14.063  1.00 17.53 ?  373 HOH   A O    1 
HETATM 6704 O O    . HOH   F 4 .   ? 16.983 -19.243 4.849   1.00 15.09 ?  374 HOH   A O    1 
HETATM 6705 O O    . HOH   F 4 .   ? 33.627 -7.162  4.342   1.00 16.62 ?  375 HOH   A O    1 
HETATM 6706 O O    B HOH   F 4 .   ? 11.301 1.940   12.150  0.34 22.38 ?  376 HOH   A O    1 
HETATM 6707 O O    . HOH   F 4 .   ? 6.455  -5.482  11.145  1.00 19.04 ?  377 HOH   A O    1 
HETATM 6708 O O    . HOH   F 4 .   ? 37.379 11.971  4.996   1.00 28.47 ?  378 HOH   A O    1 
HETATM 6709 O O    . HOH   F 4 .   ? 16.503 -21.999 0.894   1.00 27.20 ?  379 HOH   A O    1 
HETATM 6710 O O    . HOH   F 4 .   ? 22.574 -11.908 21.784  1.00 44.84 ?  380 HOH   A O    1 
HETATM 6711 O O    . HOH   F 4 .   ? 15.193 -21.581 14.209  1.00 18.43 ?  381 HOH   A O    1 
HETATM 6712 O O    . HOH   F 4 .   ? 13.931 -4.988  17.486  1.00 24.76 ?  382 HOH   A O    1 
HETATM 6713 O O    A HOH   F 4 .   ? 6.918  -8.140  11.797  0.66 16.12 ?  383 HOH   A O    1 
HETATM 6714 O O    B HOH   F 4 .   ? 5.387  2.459   5.957   0.34 29.86 ?  384 HOH   A O    1 
HETATM 6715 O O    . HOH   F 4 .   ? 24.462 3.587   -1.800  1.00 14.96 ?  385 HOH   A O    1 
HETATM 6716 O O    . HOH   F 4 .   ? 43.394 7.836   2.781   1.00 30.82 ?  386 HOH   A O    1 
HETATM 6717 O O    . HOH   F 4 .   ? 31.809 -7.280  -9.848  1.00 21.28 ?  387 HOH   A O    1 
HETATM 6718 O O    A HOH   F 4 .   ? 11.069 -0.350  1.903   0.46 22.83 ?  388 HOH   A O    1 
HETATM 6719 O O    . HOH   F 4 .   ? 43.864 8.438   -3.102  1.00 28.32 ?  389 HOH   A O    1 
HETATM 6720 O O    . HOH   F 4 .   ? 24.201 -7.794  14.438  1.00 16.91 ?  390 HOH   A O    1 
HETATM 6721 O O    T HOH   F 4 .   ? 15.408 -0.398  2.365   0.20 10.00 ?  391 HOH   A O    1 
HETATM 6722 O O    . HOH   F 4 .   ? 24.716 -17.545 12.688  1.00 24.08 ?  392 HOH   A O    1 
HETATM 6723 O O    . HOH   F 4 .   ? 14.044 -23.052 7.394   1.00 17.79 ?  393 HOH   A O    1 
HETATM 6724 O O    . HOH   F 4 .   ? 21.210 10.254  15.051  1.00 38.45 ?  394 HOH   A O    1 
HETATM 6725 O O    B HOH   F 4 .   ? 4.516  4.370   0.697   0.34 33.46 ?  395 HOH   A O    1 
HETATM 6726 O O    . HOH   F 4 .   ? 28.569 -10.605 -13.961 1.00 44.89 ?  396 HOH   A O    1 
HETATM 6727 O O    . HOH   F 4 .   ? 37.553 -2.074  5.836   1.00 27.79 ?  397 HOH   A O    1 
HETATM 6728 O O    . HOH   F 4 .   ? 15.193 -8.009  -9.698  1.00 21.11 ?  398 HOH   A O    1 
HETATM 6729 O O    . HOH   F 4 .   ? 31.066 6.174   -12.225 1.00 29.57 ?  399 HOH   A O    1 
HETATM 6730 O O    B HOH   F 4 .   ? 19.339 1.826   -1.039  0.34 14.35 ?  400 HOH   A O    1 
HETATM 6731 O O    . HOH   F 4 .   ? 20.539 -19.992 2.731   1.00 17.37 ?  401 HOH   A O    1 
HETATM 6732 O O    . HOH   F 4 .   ? 23.908 -20.251 -1.405  1.00 16.09 ?  402 HOH   A O    1 
HETATM 6733 O O    . HOH   F 4 .   ? 14.582 -0.454  -12.145 1.00 21.75 ?  403 HOH   A O    1 
HETATM 6734 O O    . HOH   F 4 .   ? 15.526 11.767  7.927   1.00 41.51 ?  404 HOH   A O    1 
HETATM 6735 O O    . HOH   F 4 .   ? 30.674 1.867   16.705  1.00 21.43 ?  405 HOH   A O    1 
HETATM 6736 O O    . HOH   F 4 .   ? 27.239 2.292   18.691  1.00 29.09 ?  406 HOH   A O    1 
HETATM 6737 O O    B HOH   F 4 .   ? 19.157 -0.985  -2.001  0.34 16.79 ?  407 HOH   A O    1 
HETATM 6738 O O    . HOH   F 4 .   ? 32.771 -9.248  5.961   1.00 20.48 ?  408 HOH   A O    1 
HETATM 6739 O O    . HOH   F 4 .   ? 30.021 -10.107 13.029  1.00 21.19 ?  409 HOH   A O    1 
HETATM 6740 O O    . HOH   F 4 .   ? 24.611 2.031   -6.965  1.00 17.99 ?  410 HOH   A O    1 
HETATM 6741 O O    . HOH   F 4 .   ? 23.970 -15.654 -9.228  1.00 34.03 ?  411 HOH   A O    1 
HETATM 6742 O O    . HOH   F 4 .   ? 40.912 -8.284  -6.777  1.00 37.50 ?  412 HOH   A O    1 
HETATM 6743 O O    . HOH   F 4 .   ? 26.976 4.188   -0.655  1.00 13.05 ?  413 HOH   A O    1 
HETATM 6744 O O    . HOH   F 4 .   ? 32.654 -4.134  -9.878  1.00 28.11 ?  414 HOH   A O    1 
HETATM 6745 O O    A HOH   F 4 .   ? 15.794 -0.926  5.250   0.66 20.40 ?  415 HOH   A O    1 
HETATM 6746 O O    A HOH   F 4 .   ? 18.968 -0.644  -1.639  0.66 11.82 ?  416 HOH   A O    1 
HETATM 6747 O O    . HOH   F 4 .   ? 38.117 -1.316  -1.890  1.00 19.52 ?  417 HOH   A O    1 
HETATM 6748 O O    . HOH   F 4 .   ? 18.804 -2.370  -16.459 1.00 47.58 ?  418 HOH   A O    1 
HETATM 6749 O O    . HOH   F 4 .   ? 16.259 16.668  8.610   1.00 36.23 ?  419 HOH   A O    1 
HETATM 6750 O O    A HOH   F 4 .   ? 21.359 3.176   -0.351  0.66 11.58 ?  420 HOH   A O    1 
HETATM 6751 O O    A HOH   F 4 .   ? 20.128 4.575   -7.549  0.66 15.92 ?  421 HOH   A O    1 
HETATM 6752 O O    . HOH   F 4 .   ? 6.801  -3.312  13.001  1.00 31.87 ?  422 HOH   A O    1 
HETATM 6753 O O    . HOH   F 4 .   ? 30.293 -12.940 13.518  1.00 19.80 ?  423 HOH   A O    1 
HETATM 6754 O O    . HOH   F 4 .   ? 10.409 -13.693 -1.734  1.00 17.00 ?  424 HOH   A O    1 
HETATM 6755 O O    . HOH   F 4 .   ? 27.994 0.854   -7.107  1.00 14.10 ?  425 HOH   A O    1 
HETATM 6756 O O    . HOH   F 4 .   ? 35.151 -5.224  -3.112  1.00 17.81 ?  426 HOH   A O    1 
HETATM 6757 O O    A HOH   F 4 .   ? 16.026 6.977   2.981   0.66 18.22 ?  427 HOH   A O    1 
HETATM 6758 O O    . HOH   F 4 .   ? 44.972 -0.643  3.085   1.00 39.22 ?  428 HOH   A O    1 
HETATM 6759 O O    . HOH   F 4 .   ? 24.109 3.947   -4.807  1.00 20.46 ?  429 HOH   A O    1 
HETATM 6760 O O    . HOH   F 4 .   ? 36.732 -4.985  5.409   1.00 23.79 ?  430 HOH   A O    1 
HETATM 6761 O O    . HOH   F 4 .   ? 16.178 -14.131 20.211  1.00 45.35 ?  431 HOH   A O    1 
HETATM 6762 O O    . HOH   F 4 .   ? 32.549 -10.627 3.222   1.00 32.05 ?  432 HOH   A O    1 
HETATM 6763 O O    . HOH   F 4 .   ? 41.627 1.570   5.072   1.00 36.04 ?  433 HOH   A O    1 
HETATM 6764 O O    . HOH   F 4 .   ? 15.855 2.108   24.745  1.00 42.23 ?  434 HOH   A O    1 
HETATM 6765 O O    A HOH   F 4 .   ? 11.015 1.567   12.723  0.66 19.67 ?  435 HOH   A O    1 
HETATM 6766 O O    . HOH   F 4 .   ? 22.642 8.150   18.404  1.00 47.43 ?  436 HOH   A O    1 
HETATM 6767 O O    B HOH   F 4 .   ? 20.256 4.941   -7.934  0.34 24.52 ?  437 HOH   A O    1 
HETATM 6768 O O    . HOH   F 4 .   ? 20.511 -17.743 24.795  1.00 54.70 ?  438 HOH   A O    1 
HETATM 6769 O O    . HOH   F 4 .   ? 11.650 -10.770 17.001  1.00 22.11 ?  439 HOH   A O    1 
HETATM 6770 O O    B HOH   F 4 .   ? 7.922  4.084   1.165   0.34 27.58 ?  440 HOH   A O    1 
HETATM 6771 O O    A HOH   F 4 .   ? 16.272 2.976   -1.455  0.66 16.07 ?  441 HOH   A O    1 
HETATM 6772 O O    . HOH   F 4 .   ? 37.745 -8.879  -3.530  1.00 23.95 ?  442 HOH   A O    1 
HETATM 6773 O O    . HOH   F 4 .   ? 23.470 -8.048  17.111  1.00 20.44 ?  443 HOH   A O    1 
HETATM 6774 O O    . HOH   F 4 .   ? 9.474  -16.230 -2.014  1.00 38.90 ?  444 HOH   A O    1 
HETATM 6775 O O    . HOH   F 4 .   ? 21.256 -9.216  21.276  1.00 48.02 ?  445 HOH   A O    1 
HETATM 6776 O O    . HOH   F 4 .   ? 18.395 -15.996 16.348  1.00 36.17 ?  446 HOH   A O    1 
HETATM 6777 O O    . HOH   F 4 .   ? 21.471 -14.677 17.998  1.00 49.72 ?  447 HOH   A O    1 
HETATM 6778 O O    . HOH   F 4 .   ? 18.536 4.884   -15.119 1.00 48.55 ?  448 HOH   A O    1 
HETATM 6779 O O    . HOH   F 4 .   ? 23.272 -20.917 1.277   1.00 18.34 ?  449 HOH   A O    1 
HETATM 6780 O O    . HOH   F 4 .   ? 34.406 -8.088  -0.527  1.00 24.06 ?  450 HOH   A O    1 
HETATM 6781 O O    . HOH   F 4 .   ? 27.092 -3.183  19.384  1.00 39.70 ?  451 HOH   A O    1 
HETATM 6782 O O    A HOH   F 4 .   ? 5.301  2.669   5.232   0.66 27.29 ?  452 HOH   A O    1 
HETATM 6783 O O    . HOH   F 4 .   ? 30.614 14.780  2.824   1.00 19.11 ?  453 HOH   A O    1 
HETATM 6784 O O    A HOH   F 4 .   ? 14.026 -0.314  3.438   0.46 36.42 ?  454 HOH   A O    1 
HETATM 6785 O O    . HOH   F 4 .   ? 19.401 -11.007 24.067  1.00 60.18 ?  455 HOH   A O    1 
HETATM 6786 O O    B HOH   F 4 .   ? 16.048 6.898   2.458   0.34 17.28 ?  456 HOH   A O    1 
HETATM 6787 O O    A HOH   F 4 .   ? 18.874 2.057   -0.761  0.66 12.35 ?  457 HOH   A O    1 
HETATM 6788 O O    . HOH   F 4 .   ? 31.311 -12.726 -0.018  1.00 19.99 ?  458 HOH   A O    1 
HETATM 6789 O O    B HOH   F 4 .   ? 5.210  -1.274  -2.460  0.34 26.44 ?  459 HOH   A O    1 
HETATM 6790 O O    A HOH   F 4 .   ? 23.223 7.535   -3.228  0.66 28.89 ?  460 HOH   A O    1 
HETATM 6791 O O    A HOH   F 4 .   ? -1.446 -4.906  7.579   0.66 38.41 ?  461 HOH   A O    1 
HETATM 6792 O O    . HOH   F 4 .   ? 29.811 -16.047 10.672  1.00 34.94 ?  462 HOH   A O    1 
HETATM 6793 O O    B HOH   F 4 .   ? 9.013  3.921   8.053   0.34 26.93 ?  463 HOH   A O    1 
HETATM 6794 O O    . HOH   F 4 .   ? 27.825 7.016   -6.504  1.00 38.32 ?  464 HOH   A O    1 
HETATM 6795 O O    . HOH   F 4 .   ? 32.415 -15.922 10.840  1.00 36.68 ?  465 HOH   A O    1 
HETATM 6796 O O    . HOH   F 4 .   ? 25.405 8.193   -4.794  1.00 28.92 ?  466 HOH   A O    1 
HETATM 6797 O O    . HOH   F 4 .   ? 29.824 -1.941  -12.717 1.00 41.59 ?  467 HOH   A O    1 
HETATM 6798 O O    . HOH   F 4 .   ? 24.775 5.676   20.744  1.00 50.91 ?  468 HOH   A O    1 
HETATM 6799 O O    . HOH   F 4 .   ? 19.877 -17.279 -5.108  1.00 23.52 ?  469 HOH   A O    1 
HETATM 6800 O O    B HOH   F 4 .   ? 22.638 7.401   -3.915  0.34 20.49 ?  470 HOH   A O    1 
HETATM 6801 O O    . HOH   F 4 .   ? 23.179 -22.356 -3.321  1.00 34.66 ?  471 HOH   A O    1 
HETATM 6802 O O    . HOH   F 4 .   ? 24.651 14.658  7.829   1.00 37.28 ?  472 HOH   A O    1 
HETATM 6803 O O    . HOH   F 4 .   ? 26.988 11.621  -1.406  1.00 32.65 ?  473 HOH   A O    1 
HETATM 6804 O O    . HOH   F 4 .   ? 18.806 10.962  11.247  1.00 32.12 ?  474 HOH   A O    1 
HETATM 6805 O O    . HOH   F 4 .   ? 15.716 -21.485 3.648   1.00 22.69 ?  475 HOH   A O    1 
HETATM 6806 O O    . HOH   F 4 .   ? 39.632 -7.023  -3.522  1.00 43.91 ?  476 HOH   A O    1 
HETATM 6807 O O    . HOH   F 4 .   ? 23.513 13.746  5.514   1.00 19.27 ?  477 HOH   A O    1 
HETATM 6808 O O    A HOH   F 4 .   ? 21.992 5.294   -5.833  0.66 27.04 ?  478 HOH   A O    1 
HETATM 6809 O O    . HOH   F 4 .   ? 27.453 -11.418 16.584  1.00 38.45 ?  479 HOH   A O    1 
HETATM 6810 O O    . HOH   F 4 .   ? 12.350 1.539   17.280  1.00 42.17 ?  480 HOH   A O    1 
HETATM 6811 O O    . HOH   F 4 .   ? 11.979 -13.430 16.333  1.00 49.60 ?  481 HOH   A O    1 
HETATM 6812 O O    B HOH   F 4 .   ? 22.210 5.328   -6.119  0.34 24.53 ?  482 HOH   A O    1 
HETATM 6813 O O    B HOH   F 4 .   ? 7.731  -0.470  -1.956  0.34 22.98 ?  483 HOH   A O    1 
HETATM 6814 O O    . HOH   F 4 .   ? 14.035 -10.281 -10.897 1.00 31.83 ?  484 HOH   A O    1 
HETATM 6815 O O    . HOH   F 4 .   ? 15.680 -16.992 -7.054  1.00 30.46 ?  485 HOH   A O    1 
HETATM 6816 O O    . HOH   F 4 .   ? 10.965 -14.990 -6.156  1.00 35.45 ?  486 HOH   A O    1 
HETATM 6817 O O    . HOH   F 4 .   ? 18.045 -16.158 -8.852  1.00 38.62 ?  487 HOH   A O    1 
HETATM 6818 O O    . HOH   F 4 .   ? 25.802 10.812  -3.897  1.00 27.60 ?  488 HOH   A O    1 
HETATM 6819 O O    . HOH   F 4 .   ? 23.139 11.817  -4.110  1.00 19.29 ?  489 HOH   A O    1 
HETATM 6820 O O    . HOH   F 4 .   ? 35.152 7.443   12.332  1.00 47.43 ?  490 HOH   A O    1 
HETATM 6821 O O    . HOH   F 4 .   ? 16.848 -20.558 16.113  1.00 28.44 ?  491 HOH   A O    1 
HETATM 6822 O O    . HOH   F 4 .   ? 28.841 9.026   17.558  1.00 37.89 ?  492 HOH   A O    1 
HETATM 6823 O O    . HOH   F 4 .   ? 17.409 -18.686 19.803  1.00 50.31 ?  493 HOH   A O    1 
HETATM 6824 O O    . HOH   F 4 .   ? 30.818 0.750   19.168  1.00 40.47 ?  494 HOH   A O    1 
HETATM 6825 O O    . HOH   F 4 .   ? 31.537 -0.547  -10.545 1.00 31.34 ?  495 HOH   A O    1 
HETATM 6826 O O    . HOH   F 4 .   ? 40.995 -3.988  -0.363  1.00 39.25 ?  496 HOH   A O    1 
HETATM 6827 O O    . HOH   F 4 .   ? 44.544 10.401  -1.652  1.00 34.84 ?  497 HOH   A O    1 
HETATM 6828 O O    . HOH   F 4 .   ? 23.238 -12.924 19.302  1.00 44.30 ?  498 HOH   A O    1 
HETATM 6829 O O    . HOH   F 4 .   ? 41.766 9.273   -3.991  1.00 34.53 ?  499 HOH   A O    1 
HETATM 6830 O O    . HOH   F 4 .   ? 28.690 -7.889  -15.276 1.00 44.73 ?  500 HOH   A O    1 
HETATM 6831 O O    . HOH   F 4 .   ? 28.640 -4.552  -12.267 1.00 36.17 ?  501 HOH   A O    1 
HETATM 6832 O O    B HOH   F 4 .   ? 15.194 10.580  5.586   0.34 34.16 ?  502 HOH   A O    1 
HETATM 6833 O O    . HOH   F 4 .   ? 39.177 2.392   7.558   1.00 31.77 ?  503 HOH   A O    1 
HETATM 6834 O O    . HOH   F 4 .   ? 18.427 -23.180 1.853   1.00 40.91 ?  504 HOH   A O    1 
HETATM 6835 O O    . HOH   F 4 .   ? 16.060 -6.670  -11.896 1.00 39.73 ?  505 HOH   A O    1 
HETATM 6836 O O    . HOH   F 4 .   ? 40.626 -0.193  -7.787  1.00 35.43 ?  506 HOH   A O    1 
HETATM 6837 O O    . HOH   F 4 .   ? 19.964 -22.306 4.071   1.00 28.50 ?  507 HOH   A O    1 
HETATM 6838 O O    . HOH   F 4 .   ? 13.978 -25.322 8.831   1.00 29.98 ?  508 HOH   A O    1 
HETATM 6839 O O    . HOH   F 4 .   ? 16.143 -23.363 5.664   1.00 26.63 ?  509 HOH   A O    1 
HETATM 6840 O O    . HOH   F 4 .   ? 30.784 -5.800  -11.820 1.00 46.75 ?  510 HOH   A O    1 
HETATM 6841 O O    . HOH   F 4 .   ? 37.370 -6.645  7.590   1.00 27.80 ?  511 HOH   A O    1 
HETATM 6842 O O    . HOH   F 4 .   ? 23.091 -23.744 1.563   1.00 30.42 ?  512 HOH   A O    1 
HETATM 6843 O O    . HOH   F 4 .   ? 39.512 -0.047  6.670   1.00 31.20 ?  513 HOH   A O    1 
HETATM 6844 O O    . HOH   F 4 .   ? 30.750 5.856   -14.668 1.00 35.81 ?  514 HOH   A O    1 
HETATM 6845 O O    . HOH   F 4 .   ? 38.013 13.914  6.764   1.00 33.57 ?  515 HOH   A O    1 
HETATM 6846 O O    . HOH   F 4 .   ? 29.038 14.459  0.917   1.00 43.93 ?  516 HOH   A O    1 
HETATM 6847 O O    B HOH   F 4 .   ? 14.768 7.890   4.869   0.34 19.86 ?  517 HOH   A O    1 
HETATM 6848 O O    . HOH   F 4 .   ? 8.020  -3.015  -5.683  1.00 36.68 ?  518 HOH   A O    1 
HETATM 6849 O O    . HOH   F 4 .   ? 20.490 -16.044 -7.416  1.00 27.43 ?  519 HOH   A O    1 
HETATM 6850 O O    . HOH   F 4 .   ? 36.495 -6.451  10.178  1.00 43.86 ?  520 HOH   A O    1 
HETATM 6851 O O    . HOH   F 4 .   ? 24.109 9.039   -7.201  1.00 38.63 ?  521 HOH   A O    1 
HETATM 6852 O O    . HOH   F 4 .   ? 21.988 -24.028 4.412   1.00 26.36 ?  522 HOH   A O    1 
HETATM 6853 O O    B HOH   F 4 .   ? 9.623  -1.406  -3.957  0.34 19.02 ?  523 HOH   A O    1 
HETATM 6854 O O    B HOH   F 4 .   ? 10.051 1.264   -4.912  0.34 19.18 ?  524 HOH   A O    1 
HETATM 6855 O O    A HOH   F 4 .   ? 14.856 8.672   4.879   0.66 45.35 ?  525 HOH   A O    1 
HETATM 6856 O O    T HOH   F 4 .   ? 11.934 -2.112  -3.686  0.20 8.96  ?  526 HOH   A O    1 
HETATM 6857 O O    . HOH   F 4 .   ? 17.399 -6.504  -14.226 1.00 36.58 ?  527 HOH   A O    1 
HETATM 6858 O O    B HOH   F 4 .   ? 8.865  2.432   -2.716  0.34 21.68 ?  528 HOH   A O    1 
HETATM 6859 O O    . HOH   F 4 .   ? 16.302 -21.195 18.708  1.00 36.22 ?  529 HOH   A O    1 
HETATM 6860 O O    . HOH   F 4 .   ? 15.860 -12.188 27.434  1.00 44.25 ?  530 HOH   A O    1 
HETATM 6861 O O    . HOH   F 4 .   ? 14.681 -22.749 19.773  1.00 39.42 ?  531 HOH   A O    1 
HETATM 6862 O O    . HOH   G 4 .   ? 29.779 -22.415 5.438   1.00 21.64 ?  201 HOH   B O    1 
HETATM 6863 O O    . HOH   G 4 .   ? 41.869 -35.978 -17.204 1.00 28.69 ?  202 HOH   B O    1 
HETATM 6864 O O    . HOH   G 4 .   ? 47.353 -7.478  -3.921  1.00 38.89 ?  203 HOH   B O    1 
HETATM 6865 O O    . HOH   G 4 .   ? 49.447 -22.621 -19.698 1.00 46.05 ?  204 HOH   B O    1 
HETATM 6866 O O    . HOH   G 4 .   ? 52.902 -13.452 -20.423 1.00 41.29 ?  205 HOH   B O    1 
HETATM 6867 O O    . HOH   G 4 .   ? 27.672 -29.181 -1.889  1.00 37.56 ?  206 HOH   B O    1 
HETATM 6868 O O    . HOH   G 4 .   ? 37.948 -39.468 -0.207  1.00 42.27 ?  207 HOH   B O    1 
HETATM 6869 O O    . HOH   G 4 .   ? 27.854 -41.828 -15.114 1.00 35.53 ?  208 HOH   B O    1 
HETATM 6870 O O    . HOH   G 4 .   ? 59.119 -18.715 6.893   1.00 36.67 ?  209 HOH   B O    1 
HETATM 6871 O O    . HOH   G 4 .   ? 41.299 -7.847  5.513   1.00 39.49 ?  210 HOH   B O    1 
HETATM 6872 O O    . HOH   G 4 .   ? 57.694 -24.538 5.019   1.00 35.47 ?  211 HOH   B O    1 
HETATM 6873 O O    . HOH   G 4 .   ? 56.305 -19.712 7.392   1.00 34.22 ?  212 HOH   B O    1 
HETATM 6874 O O    . HOH   G 4 .   ? 47.971 -6.904  15.660  1.00 34.27 ?  213 HOH   B O    1 
HETATM 6875 O O    . HOH   G 4 .   ? 54.481 -9.363  -8.707  1.00 19.00 ?  214 HOH   B O    1 
HETATM 6876 O O    . HOH   G 4 .   ? 56.673 -30.751 -7.753  1.00 32.92 ?  215 HOH   B O    1 
HETATM 6877 O O    . HOH   G 4 .   ? 35.982 -43.246 -8.496  1.00 29.57 ?  216 HOH   B O    1 
HETATM 6878 O O    . HOH   G 4 .   ? 30.219 -41.035 -8.106  1.00 17.16 ?  217 HOH   B O    1 
HETATM 6879 O O    . HOH   G 4 .   ? 58.172 -12.919 8.493   1.00 34.08 ?  218 HOH   B O    1 
HETATM 6880 O O    . HOH   G 4 .   ? 50.244 -3.323  7.216   1.00 37.14 ?  219 HOH   B O    1 
HETATM 6881 O O    . HOH   G 4 .   ? 50.672 -6.136  0.243   1.00 25.91 ?  220 HOH   B O    1 
HETATM 6882 O O    . HOH   G 4 .   ? 29.827 -26.275 3.917   1.00 30.09 ?  221 HOH   B O    1 
HETATM 6883 O O    . HOH   G 4 .   ? 39.274 -10.931 6.089   1.00 27.74 ?  222 HOH   B O    1 
HETATM 6884 O O    . HOH   G 4 .   ? 44.447 -7.350  2.205   1.00 32.86 ?  223 HOH   B O    1 
HETATM 6885 O O    . HOH   G 4 .   ? 29.704 -34.148 -0.445  1.00 37.68 ?  224 HOH   B O    1 
HETATM 6886 O O    . HOH   G 4 .   ? 37.129 -19.836 -18.116 1.00 37.95 ?  225 HOH   B O    1 
HETATM 6887 O O    . HOH   G 4 .   ? 34.534 -36.376 -7.190  1.00 17.80 ?  226 HOH   B O    1 
HETATM 6888 O O    . HOH   G 4 .   ? 57.200 -26.834 -7.559  1.00 42.22 ?  227 HOH   B O    1 
HETATM 6889 O O    . HOH   G 4 .   ? 41.317 -9.679  13.097  1.00 22.70 ?  228 HOH   B O    1 
HETATM 6890 O O    . HOH   G 4 .   ? 45.114 -34.951 6.846   1.00 41.00 ?  229 HOH   B O    1 
HETATM 6891 O O    . HOH   G 4 .   ? 41.501 -39.197 -14.834 1.00 22.08 ?  230 HOH   B O    1 
HETATM 6892 O O    . HOH   G 4 .   ? 51.659 -6.492  4.443   1.00 20.81 ?  231 HOH   B O    1 
HETATM 6893 O O    . HOH   G 4 .   ? 48.164 -24.606 -17.685 1.00 27.37 ?  232 HOH   B O    1 
HETATM 6894 O O    . HOH   G 4 .   ? 55.301 -16.464 -14.269 1.00 31.00 ?  233 HOH   B O    1 
HETATM 6895 O O    . HOH   G 4 .   ? 57.344 -16.248 -12.228 1.00 19.19 ?  234 HOH   B O    1 
HETATM 6896 O O    . HOH   G 4 .   ? 30.768 -28.775 4.256   1.00 25.18 ?  235 HOH   B O    1 
HETATM 6897 O O    . HOH   G 4 .   ? 48.520 -36.537 -15.409 1.00 44.45 ?  236 HOH   B O    1 
HETATM 6898 O O    . HOH   G 4 .   ? 28.433 -19.723 -13.146 1.00 24.60 ?  237 HOH   B O    1 
HETATM 6899 O O    . HOH   G 4 .   ? 42.524 -25.378 2.637   1.00 15.31 ?  238 HOH   B O    1 
HETATM 6900 O O    . HOH   G 4 .   ? 50.714 -12.979 -0.432  1.00 12.42 ?  239 HOH   B O    1 
HETATM 6901 O O    . HOH   G 4 .   ? 35.155 -8.003  -3.052  1.00 17.78 ?  240 HOH   B O    1 
HETATM 6902 O O    . HOH   G 4 .   ? 44.475 -27.725 -0.685  1.00 22.94 ?  241 HOH   B O    1 
HETATM 6903 O O    . HOH   G 4 .   ? 46.349 -1.571  13.267  1.00 28.91 ?  242 HOH   B O    1 
HETATM 6904 O O    . HOH   G 4 .   ? 44.939 -43.586 -10.458 1.00 28.57 ?  243 HOH   B O    1 
HETATM 6905 O O    . HOH   G 4 .   ? 39.482 -11.136 0.326   1.00 16.71 ?  244 HOH   B O    1 
HETATM 6906 O O    . HOH   G 4 .   ? 34.804 -24.647 13.840  1.00 31.41 ?  245 HOH   B O    1 
HETATM 6907 O O    . HOH   G 4 .   ? 42.609 -22.880 3.855   1.00 11.90 ?  246 HOH   B O    1 
HETATM 6908 O O    . HOH   G 4 .   ? 32.837 -43.837 -11.293 1.00 19.40 ?  247 HOH   B O    1 
HETATM 6909 O O    . HOH   G 4 .   ? 40.665 -16.030 14.190  1.00 23.42 ?  248 HOH   B O    1 
HETATM 6910 O O    . HOH   G 4 .   ? 50.954 -39.972 -8.112  1.00 30.84 ?  249 HOH   B O    1 
HETATM 6911 O O    . HOH   G 4 .   ? 57.606 -24.384 -3.752  1.00 22.72 ?  250 HOH   B O    1 
HETATM 6912 O O    . HOH   G 4 .   ? 43.101 -43.261 -8.191  1.00 29.75 ?  251 HOH   B O    1 
HETATM 6913 O O    . HOH   G 4 .   ? 41.819 -23.543 9.309   1.00 17.41 ?  252 HOH   B O    1 
HETATM 6914 O O    . HOH   G 4 .   ? 25.381 -25.958 -1.362  1.00 32.98 ?  253 HOH   B O    1 
HETATM 6915 O O    . HOH   G 4 .   ? 34.153 -18.555 11.395  1.00 23.75 ?  254 HOH   B O    1 
HETATM 6916 O O    . HOH   G 4 .   ? 29.745 -25.239 -10.840 1.00 17.25 ?  255 HOH   B O    1 
HETATM 6917 O O    . HOH   G 4 .   ? 40.338 -12.773 -11.526 1.00 15.28 ?  256 HOH   B O    1 
HETATM 6918 O O    . HOH   G 4 .   ? 30.831 -15.730 2.627   1.00 13.66 ?  257 HOH   B O    1 
HETATM 6919 O O    . HOH   G 4 .   ? 51.490 -13.879 11.093  1.00 29.48 ?  258 HOH   B O    1 
HETATM 6920 O O    . HOH   G 4 .   ? 38.468 -11.102 -2.256  1.00 19.22 ?  259 HOH   B O    1 
HETATM 6921 O O    . HOH   G 4 .   ? 47.947 -22.773 5.842   1.00 17.29 ?  260 HOH   B O    1 
HETATM 6922 O O    . HOH   G 4 .   ? 43.267 -32.408 -17.033 1.00 23.16 ?  261 HOH   B O    1 
HETATM 6923 O O    . HOH   G 4 .   ? 49.693 -0.521  10.296  1.00 31.34 ?  262 HOH   B O    1 
HETATM 6924 O O    . HOH   G 4 .   ? 27.128 -31.847 -9.981  1.00 22.93 ?  263 HOH   B O    1 
HETATM 6925 O O    . HOH   G 4 .   ? 33.464 -17.022 8.041   1.00 19.21 ?  264 HOH   B O    1 
HETATM 6926 O O    . HOH   G 4 .   ? 38.882 -11.996 12.423  1.00 33.93 ?  265 HOH   B O    1 
HETATM 6927 O O    . HOH   G 4 .   ? 57.478 -9.246  1.511   1.00 20.15 ?  266 HOH   B O    1 
HETATM 6928 O O    . HOH   G 4 .   ? 58.161 -10.626 -4.053  1.00 20.25 ?  267 HOH   B O    1 
HETATM 6929 O O    . HOH   G 4 .   ? 30.670 -42.229 -10.613 1.00 27.63 ?  268 HOH   B O    1 
HETATM 6930 O O    . HOH   G 4 .   ? 49.333 -28.706 -6.853  1.00 15.58 ?  269 HOH   B O    1 
HETATM 6931 O O    . HOH   G 4 .   ? 43.386 -15.809 -12.180 1.00 14.43 ?  270 HOH   B O    1 
HETATM 6932 O O    . HOH   G 4 .   ? 42.259 -9.921  9.437   1.00 21.27 ?  271 HOH   B O    1 
HETATM 6933 O O    . HOH   G 4 .   ? 34.954 -33.427 -19.153 1.00 30.10 ?  272 HOH   B O    1 
HETATM 6934 O O    . HOH   G 4 .   ? 34.443 -12.768 2.589   1.00 26.82 ?  273 HOH   B O    1 
HETATM 6935 O O    . HOH   G 4 .   ? 56.192 -23.572 -14.657 1.00 26.78 ?  274 HOH   B O    1 
HETATM 6936 O O    . HOH   G 4 .   ? 31.847 -17.956 -14.566 1.00 31.93 ?  275 HOH   B O    1 
HETATM 6937 O O    . HOH   G 4 .   ? 46.617 -31.264 -4.749  1.00 22.75 ?  276 HOH   B O    1 
HETATM 6938 O O    . HOH   G 4 .   ? 56.893 -8.656  8.502   1.00 19.94 ?  277 HOH   B O    1 
HETATM 6939 O O    . HOH   G 4 .   ? 28.269 -34.371 -9.425  1.00 21.23 ?  278 HOH   B O    1 
HETATM 6940 O O    . HOH   G 4 .   ? 42.339 -34.717 3.755   1.00 26.05 ?  279 HOH   B O    1 
HETATM 6941 O O    . HOH   G 4 .   ? 48.375 -25.048 3.137   1.00 13.58 ?  280 HOH   B O    1 
HETATM 6942 O O    . HOH   G 4 .   ? 59.716 -15.270 8.200   1.00 30.72 ?  281 HOH   B O    1 
HETATM 6943 O O    . HOH   G 4 .   ? 49.929 -24.648 5.778   1.00 33.65 ?  282 HOH   B O    1 
HETATM 6944 O O    . HOH   G 4 .   ? 46.815 -29.558 9.843   1.00 31.78 ?  283 HOH   B O    1 
HETATM 6945 O O    . HOH   G 4 .   ? 27.961 -22.900 -8.017  1.00 17.46 ?  284 HOH   B O    1 
HETATM 6946 O O    . HOH   G 4 .   ? 28.491 -30.928 -14.699 1.00 32.12 ?  285 HOH   B O    1 
HETATM 6947 O O    . HOH   G 4 .   ? 51.229 -37.630 -9.464  1.00 25.93 ?  286 HOH   B O    1 
HETATM 6948 O O    . HOH   G 4 .   ? 33.550 -15.328 -13.967 1.00 21.70 ?  287 HOH   B O    1 
HETATM 6949 O O    . HOH   G 4 .   ? 27.595 -26.693 -15.661 1.00 31.37 ?  288 HOH   B O    1 
HETATM 6950 O O    . HOH   G 4 .   ? 52.479 -10.406 13.051  1.00 22.99 ?  289 HOH   B O    1 
HETATM 6951 O O    . HOH   G 4 .   ? 48.667 -20.049 5.976   1.00 14.49 ?  290 HOH   B O    1 
HETATM 6952 O O    . HOH   G 4 .   ? 41.066 -5.546  11.585  1.00 45.24 ?  291 HOH   B O    1 
HETATM 6953 O O    . HOH   G 4 .   ? 36.839 -12.763 -1.518  1.00 26.95 ?  292 HOH   B O    1 
HETATM 6954 O O    . HOH   G 4 .   ? 37.448 -18.180 13.090  1.00 30.41 ?  293 HOH   B O    1 
HETATM 6955 O O    . HOH   G 4 .   ? 45.419 -33.483 -15.850 1.00 24.16 ?  294 HOH   B O    1 
HETATM 6956 O O    . HOH   G 4 .   ? 44.611 -27.466 2.002   1.00 15.85 ?  295 HOH   B O    1 
HETATM 6957 O O    . HOH   G 4 .   ? 42.794 -12.229 -18.493 1.00 28.13 ?  296 HOH   B O    1 
HETATM 6958 O O    . HOH   G 4 .   ? 45.923 -40.410 -3.520  1.00 28.90 ?  297 HOH   B O    1 
HETATM 6959 O O    . HOH   G 4 .   ? 47.074 -34.002 -4.531  1.00 17.60 ?  298 HOH   B O    1 
HETATM 6960 O O    . HOH   G 4 .   ? 44.026 -29.358 -4.649  1.00 25.33 ?  299 HOH   B O    1 
HETATM 6961 O O    . HOH   G 4 .   ? 42.932 -20.320 -20.755 1.00 32.39 ?  300 HOH   B O    1 
HETATM 6962 O O    . HOH   G 4 .   ? 40.254 -10.851 -9.549  1.00 17.35 ?  301 HOH   B O    1 
HETATM 6963 O O    . HOH   G 4 .   ? 57.092 -12.047 12.430  1.00 37.61 ?  302 HOH   B O    1 
HETATM 6964 O O    . HOH   G 4 .   ? 52.627 -35.667 -8.555  1.00 26.89 ?  303 HOH   B O    1 
HETATM 6965 O O    . HOH   G 4 .   ? 34.981 -33.538 4.489   1.00 28.65 ?  304 HOH   B O    1 
HETATM 6966 O O    . HOH   G 4 .   ? 25.955 -21.459 -3.571  1.00 16.53 ?  305 HOH   B O    1 
HETATM 6967 O O    . HOH   G 4 .   ? 37.847 -10.273 -10.781 1.00 17.69 ?  306 HOH   B O    1 
HETATM 6968 O O    . HOH   G 4 .   ? 48.586 -12.056 -14.303 1.00 28.28 ?  307 HOH   B O    1 
HETATM 6969 O O    . HOH   G 4 .   ? 32.797 -34.586 -5.911  1.00 17.16 ?  308 HOH   B O    1 
HETATM 6970 O O    . HOH   G 4 .   ? 42.324 -9.867  -14.880 1.00 39.33 ?  309 HOH   B O    1 
HETATM 6971 O O    . HOH   G 4 .   ? 52.587 -29.257 -12.954 1.00 25.07 ?  310 HOH   B O    1 
HETATM 6972 O O    . HOH   G 4 .   ? 52.958 -15.953 -12.743 1.00 26.83 ?  311 HOH   B O    1 
HETATM 6973 O O    . HOH   G 4 .   ? 53.465 -30.204 4.559   1.00 19.16 ?  312 HOH   B O    1 
HETATM 6974 O O    . HOH   G 4 .   ? 59.953 -17.121 -10.372 1.00 33.38 ?  313 HOH   B O    1 
HETATM 6975 O O    . HOH   G 4 .   ? 37.220 -35.681 7.176   1.00 36.14 ?  314 HOH   B O    1 
HETATM 6976 O O    . HOH   G 4 .   ? 41.695 -8.084  1.379   1.00 25.15 ?  315 HOH   B O    1 
HETATM 6977 O O    . HOH   G 4 .   ? 51.368 -32.946 -10.713 1.00 37.81 ?  316 HOH   B O    1 
HETATM 6978 O O    . HOH   G 4 .   ? 41.154 -24.492 15.846  1.00 42.51 ?  317 HOH   B O    1 
HETATM 6979 O O    . HOH   G 4 .   ? 51.694 -5.909  -7.842  1.00 45.29 ?  318 HOH   B O    1 
HETATM 6980 O O    . HOH   G 4 .   ? 53.656 -12.586 -22.231 1.00 35.69 ?  319 HOH   B O    1 
HETATM 6981 O O    . HOH   G 4 .   ? 62.831 -20.186 -0.707  1.00 36.78 ?  320 HOH   B O    1 
HETATM 6982 O O    . HOH   G 4 .   ? 62.650 -13.514 4.791   1.00 28.73 ?  321 HOH   B O    1 
HETATM 6983 O O    . HOH   G 4 .   ? 43.144 -21.479 10.671  1.00 16.21 ?  322 HOH   B O    1 
HETATM 6984 O O    . HOH   G 4 .   ? 38.305 -12.808 7.907   1.00 19.19 ?  323 HOH   B O    1 
HETATM 6985 O O    . HOH   G 4 .   ? 38.355 -9.394  -13.313 1.00 27.77 ?  324 HOH   B O    1 
HETATM 6986 O O    . HOH   G 4 .   ? 26.335 -21.026 -6.256  1.00 16.88 ?  325 HOH   B O    1 
HETATM 6987 O O    . HOH   G 4 .   ? 37.233 -30.623 -21.031 1.00 31.07 ?  326 HOH   B O    1 
HETATM 6988 O O    . HOH   G 4 .   ? 27.982 -14.781 -9.413  1.00 32.10 ?  327 HOH   B O    1 
HETATM 6989 O O    . HOH   G 4 .   ? 44.522 -24.622 9.596   1.00 20.31 ?  328 HOH   B O    1 
HETATM 6990 O O    . HOH   G 4 .   ? 36.690 -12.421 4.280   1.00 18.74 ?  329 HOH   B O    1 
HETATM 6991 O O    . HOH   G 4 .   ? 57.585 -22.003 3.297   1.00 29.94 ?  330 HOH   B O    1 
HETATM 6992 O O    . HOH   G 4 .   ? 44.136 -1.765  7.594   1.00 46.12 ?  331 HOH   B O    1 
HETATM 6993 O O    . HOH   G 4 .   ? 48.077 -32.658 -16.606 1.00 44.62 ?  332 HOH   B O    1 
HETATM 6994 O O    . HOH   G 4 .   ? 39.468 -23.528 -20.298 1.00 33.93 ?  333 HOH   B O    1 
HETATM 6995 O O    . HOH   G 4 .   ? 47.099 -24.513 8.198   1.00 26.61 ?  334 HOH   B O    1 
HETATM 6996 O O    . HOH   G 4 .   ? 33.489 -31.178 11.063  1.00 33.22 ?  335 HOH   B O    1 
HETATM 6997 O O    . HOH   G 4 .   ? 43.081 -34.710 0.110   1.00 19.09 ?  336 HOH   B O    1 
HETATM 6998 O O    . HOH   G 4 .   ? 43.449 -15.452 18.251  1.00 32.19 ?  337 HOH   B O    1 
HETATM 6999 O O    . HOH   G 4 .   ? 47.451 -27.448 2.041   1.00 15.03 ?  338 HOH   B O    1 
HETATM 7000 O O    . HOH   G 4 .   ? 42.887 -43.511 -14.307 1.00 43.76 ?  339 HOH   B O    1 
HETATM 7001 O O    . HOH   G 4 .   ? 45.765 -36.278 -16.095 1.00 33.10 ?  340 HOH   B O    1 
HETATM 7002 O O    . HOH   G 4 .   ? 37.049 -15.146 -16.500 1.00 38.45 ?  341 HOH   B O    1 
HETATM 7003 O O    . HOH   G 4 .   ? 46.763 -19.939 12.333  1.00 31.87 ?  342 HOH   B O    1 
HETATM 7004 O O    . HOH   G 4 .   ? 32.979 -14.682 1.040   1.00 19.07 ?  343 HOH   B O    1 
HETATM 7005 O O    . HOH   G 4 .   ? 37.095 -45.277 -9.753  1.00 38.84 ?  344 HOH   B O    1 
HETATM 7006 O O    . HOH   G 4 .   ? 38.507 -12.264 -16.224 1.00 42.65 ?  345 HOH   B O    1 
HETATM 7007 O O    . HOH   G 4 .   ? 28.884 -42.975 -12.320 1.00 39.65 ?  346 HOH   B O    1 
HETATM 7008 O O    . HOH   G 4 .   ? 38.496 -22.357 15.007  1.00 42.41 ?  347 HOH   B O    1 
HETATM 7009 O O    . HOH   G 4 .   ? 39.809 -44.348 -11.191 1.00 38.12 ?  348 HOH   B O    1 
HETATM 7010 O O    . HOH   G 4 .   ? 33.752 -9.470  -8.896  1.00 33.23 ?  349 HOH   B O    1 
HETATM 7011 O O    . HOH   G 4 .   ? 40.413 -43.515 -9.061  1.00 26.79 ?  350 HOH   B O    1 
HETATM 7012 O O    . HOH   G 4 .   ? 27.732 -26.612 -0.616  1.00 30.17 ?  351 HOH   B O    1 
HETATM 7013 O O    . HOH   G 4 .   ? 62.554 -20.133 -4.741  1.00 44.78 ?  352 HOH   B O    1 
HETATM 7014 O O    . HOH   G 4 .   ? 23.199 -23.673 6.794   1.00 32.97 ?  353 HOH   B O    1 
HETATM 7015 O O    . HOH   G 4 .   ? 44.178 -37.372 -17.666 1.00 33.56 ?  354 HOH   B O    1 
HETATM 7016 O O    . HOH   G 4 .   ? 55.590 -8.293  10.930  1.00 26.76 ?  355 HOH   B O    1 
HETATM 7017 O O    . HOH   G 4 .   ? 36.058 -8.585  -9.741  1.00 34.64 ?  356 HOH   B O    1 
HETATM 7018 O O    . HOH   G 4 .   ? 34.630 -10.324 7.526   1.00 24.20 ?  357 HOH   B O    1 
HETATM 7019 O O    . HOH   G 4 .   ? 56.481 -7.258  3.168   1.00 27.68 ?  358 HOH   B O    1 
HETATM 7020 O O    . HOH   G 4 .   ? 34.104 -7.776  11.456  1.00 39.13 ?  359 HOH   B O    1 
HETATM 7021 O O    . HOH   G 4 .   ? 61.468 -19.924 1.776   1.00 37.05 ?  360 HOH   B O    1 
HETATM 7022 O O    . HOH   G 4 .   ? 56.955 -21.569 -16.374 1.00 39.85 ?  361 HOH   B O    1 
HETATM 7023 O O    . HOH   G 4 .   ? 40.217 -8.857  9.920   1.00 39.25 ?  362 HOH   B O    1 
HETATM 7024 O O    . HOH   G 4 .   ? 27.182 -25.998 -11.452 1.00 32.51 ?  363 HOH   B O    1 
HETATM 7025 O O    . HOH   G 4 .   ? 43.196 -12.734 -21.174 1.00 37.04 ?  364 HOH   B O    1 
HETATM 7026 O O    . HOH   G 4 .   ? 40.207 -11.362 -13.950 1.00 31.34 ?  365 HOH   B O    1 
HETATM 7027 O O    . HOH   G 4 .   ? 32.473 -23.675 14.060  1.00 40.26 ?  366 HOH   B O    1 
HETATM 7028 O O    . HOH   G 4 .   ? 48.304 -26.570 8.898   1.00 39.18 ?  367 HOH   B O    1 
HETATM 7029 O O    . HOH   G 4 .   ? 39.889 -6.991  7.861   1.00 40.51 ?  368 HOH   B O    1 
HETATM 7030 O O    . HOH   G 4 .   ? 58.898 -10.429 9.290   1.00 38.63 ?  369 HOH   B O    1 
HETATM 7031 O O    . HOH   G 4 .   ? 36.125 -8.636  8.985   1.00 40.93 ?  370 HOH   B O    1 
HETATM 7032 O O    . HOH   G 4 .   ? 54.233 -5.799  2.960   1.00 35.76 ?  371 HOH   B O    1 
HETATM 7033 O O    . HOH   G 4 .   ? 56.110 -7.838  -0.585  1.00 34.07 ?  372 HOH   B O    1 
HETATM 7034 O O    . HOH   G 4 .   ? 41.826 -9.992  -17.410 1.00 55.21 ?  373 HOH   B O    1 
HETATM 7035 O O    . HOH   G 4 .   ? 38.041 -10.661 10.080  1.00 30.53 ?  374 HOH   B O    1 
HETATM 7036 O O    . HOH   G 4 .   ? 62.947 -12.332 6.984   1.00 39.49 ?  375 HOH   B O    1 
HETATM 7037 O O    . HOH   G 4 .   ? 51.944 -12.967 13.459  1.00 30.13 ?  376 HOH   B O    1 
HETATM 7038 O O    . HOH   G 4 .   ? 36.501 -22.825 13.311  1.00 27.01 ?  377 HOH   B O    1 
HETATM 7039 O O    . HOH   G 4 .   ? 41.815 -6.746  -4.846  1.00 46.05 ?  378 HOH   B O    1 
HETATM 7040 O O    . HOH   G 4 .   ? 44.064 -5.626  -3.458  1.00 42.29 ?  379 HOH   B O    1 
HETATM 7041 O O    . HOH   G 4 .   ? 42.655 -17.095 -23.200 1.00 41.38 ?  380 HOH   B O    1 
HETATM 7042 O O    . HOH   G 4 .   ? 40.081 -7.628  3.274   1.00 35.24 ?  381 HOH   B O    1 
HETATM 7043 O O    . HOH   G 4 .   ? 39.669 -14.056 15.736  1.00 44.76 ?  382 HOH   B O    1 
HETATM 7044 O O    . HOH   G 4 .   ? 52.839 -29.871 7.255   1.00 23.45 ?  383 HOH   B O    1 
HETATM 7045 O O    . HOH   G 4 .   ? 60.488 -22.292 2.899   1.00 46.07 ?  384 HOH   B O    1 
HETATM 7046 O O    . HOH   G 4 .   ? 25.818 -18.854 -11.892 1.00 38.57 ?  385 HOH   B O    1 
HETATM 7047 O O    . HOH   G 4 .   ? 23.946 -20.855 -7.703  1.00 28.87 ?  386 HOH   B O    1 
HETATM 7048 O O    . HOH   G 4 .   ? 35.309 -20.319 13.332  1.00 29.00 ?  387 HOH   B O    1 
HETATM 7049 O O    . HOH   G 4 .   ? 46.762 -5.304  2.927   1.00 40.35 ?  388 HOH   B O    1 
HETATM 7050 O O    . HOH   G 4 .   ? 35.294 -33.731 7.308   1.00 40.67 ?  389 HOH   B O    1 
HETATM 7051 O O    . HOH   G 4 .   ? 40.860 -9.833  15.836  1.00 41.28 ?  390 HOH   B O    1 
HETATM 7052 O O    . HOH   G 4 .   ? 40.716 -6.626  -0.812  1.00 24.64 ?  391 HOH   B O    1 
HETATM 7053 O O    . HOH   G 4 .   ? 44.032 -31.678 -3.712  1.00 34.17 ?  392 HOH   B O    1 
HETATM 7054 O O    . HOH   G 4 .   ? 26.662 -28.047 -13.580 1.00 35.43 ?  393 HOH   B O    1 
HETATM 7055 O O    . HOH   G 4 .   ? 27.862 -27.104 2.150   1.00 31.08 ?  394 HOH   B O    1 
HETATM 7056 O O    . HOH   G 4 .   ? 24.594 -20.654 -10.499 1.00 37.53 ?  395 HOH   B O    1 
HETATM 7057 O O    . HOH   G 4 .   ? 34.351 -33.485 9.632   1.00 34.67 ?  396 HOH   B O    1 
HETATM 7058 O O    . HOH   G 4 .   ? 50.622 -30.792 8.720   1.00 28.22 ?  397 HOH   B O    1 
HETATM 7059 O O    . HOH   G 4 .   ? 26.867 -30.709 -12.606 1.00 30.35 ?  398 HOH   B O    1 
HETATM 7060 O O    . HOH   G 4 .   ? 45.728 -20.298 15.201  1.00 47.38 ?  399 HOH   B O    1 
HETATM 7061 O O    . HOH   G 4 .   ? 57.753 -6.543  -2.348  1.00 35.50 ?  400 HOH   B O    1 
HETATM 7062 O O    . HOH   G 4 .   ? 40.897 -11.820 -22.344 1.00 36.56 ?  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   ? 0.6073 0.6102 0.6699 0.0072  -0.0315 0.0798  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6044 0.6081 0.6451 0.0015  -0.0263 0.0623  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6061 0.6089 0.6593 0.0040  -0.0269 0.0800  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6028 0.6067 0.6372 -0.0006 -0.0245 0.0634  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.5921 0.6007 0.6266 -0.0045 -0.0313 0.0846  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.5909 0.5991 0.6142 -0.0070 -0.0296 0.0746  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.5933 0.6033 0.6363 -0.0032 -0.0370 0.0880  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.5929 0.6011 0.6236 -0.0065 -0.0330 0.0763  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6165 0.6143 0.6735 0.0073  -0.0226 0.0760  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6107 0.6113 0.6472 0.0025  -0.0202 0.0550  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6207 0.6155 0.6729 0.0104  -0.0229 0.0729  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6136 0.6124 0.6465 0.0044  -0.0193 0.0511  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6191 0.6164 0.6735 0.0064  -0.0217 0.0763  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6129 0.6130 0.6465 0.0029  -0.0187 0.0534  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.5738 0.5874 0.5795 -0.0143 -0.0329 0.0847  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.5351 0.5604 0.4881 -0.0329 -0.0392 0.0929  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.4897 0.5369 0.4260 -0.0449 -0.0361 0.0702  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.4868 0.5359 0.4079 -0.0457 -0.0394 0.0764  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.5371 0.5562 0.4464 -0.0402 -0.0485 0.1250  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.5338 0.5499 0.4065 -0.0485 -0.0598 0.1560  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.5343 0.5462 0.3962 -0.0520 -0.0707 0.1662  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.5298 0.5479 0.4001 -0.0503 -0.0601 0.1701  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.4455 0.5122 0.3754 -0.0576 -0.0296 0.0403  5   SER   A N   
47   C CA  . SER   A 5   ? 0.3996 0.4827 0.3336 -0.0701 -0.0158 0.0060  5   SER   A CA  
48   C C   . SER   A 5   ? 0.3510 0.4418 0.2940 -0.0702 -0.0040 -0.0162 5   SER   A C   
49   O O   . SER   A 5   ? 0.3541 0.4450 0.2832 -0.0572 -0.0111 -0.0356 5   SER   A O   
50   C CB  . SER   A 5   ? 0.4051 0.4885 0.3629 -0.0808 -0.0137 -0.0057 5   SER   A CB  
51   O OG  . SER   A 5   ? 0.4092 0.4920 0.3728 -0.0870 -0.0102 -0.0136 5   SER   A OG  
57   N N   . PHE   A 6   ? 0.2958 0.3920 0.2244 -0.0826 0.0166  -0.0080 6   PHE   A N   
58   C CA  . PHE   A 6   ? 0.2524 0.3426 0.1797 -0.0827 0.0260  0.0169  6   PHE   A CA  
59   C C   . PHE   A 6   ? 0.2494 0.3339 0.2148 -0.0865 0.0486  0.0157  6   PHE   A C   
60   O O   . PHE   A 6   ? 0.2601 0.3347 0.2679 -0.0908 0.0506  0.0386  6   PHE   A O   
61   C CB  . PHE   A 6   ? 0.2338 0.3047 0.1671 -0.0681 0.0117  0.0334  6   PHE   A CB  
62   C CG  . PHE   A 6   ? 0.2206 0.2739 0.1734 -0.0557 0.0038  0.0405  6   PHE   A CG  
63   C CD1 . PHE   A 6   ? 0.2123 0.2634 0.1927 -0.0462 0.0009  0.0457  6   PHE   A CD1 
64   C CD2 . PHE   A 6   ? 0.2292 0.2627 0.1919 -0.0373 0.0084  0.0366  6   PHE   A CD2 
65   C CE1 . PHE   A 6   ? 0.2145 0.2593 0.2052 -0.0402 0.0080  0.0471  6   PHE   A CE1 
66   C CE2 . PHE   A 6   ? 0.2295 0.2577 0.2217 -0.0296 0.0112  0.0322  6   PHE   A CE2 
67   C CZ  . PHE   A 6   ? 0.2252 0.2604 0.2173 -0.0344 0.0037  0.0385  6   PHE   A CZ  
77   N N   A SER   A 7   ? 0.2443 0.3328 0.2109 -0.0914 0.0645  0.0030  7   SER   A N   
78   N N   B SER   A 7   ? 0.2454 0.3234 0.2267 -0.0781 0.0529  0.0056  7   SER   A N   
79   C CA  A SER   A 7   ? 0.2517 0.3287 0.2229 -0.0810 0.0621  -0.0146 7   SER   A CA  
80   C CA  B SER   A 7   ? 0.2475 0.3166 0.2388 -0.0626 0.0491  -0.0055 7   SER   A CA  
81   C C   A SER   A 7   ? 0.2323 0.2937 0.2069 -0.0793 0.0655  -0.0211 7   SER   A C   
82   C C   B SER   A 7   ? 0.2343 0.2905 0.2232 -0.0538 0.0536  -0.0042 7   SER   A C   
83   O O   A SER   A 7   ? 0.2407 0.2855 0.2025 -0.0840 0.0686  -0.0247 7   SER   A O   
84   O O   B SER   A 7   ? 0.2388 0.2859 0.2217 -0.0551 0.0526  -0.0074 7   SER   A O   
85   C CB  A SER   A 7   ? 0.2811 0.3543 0.2520 -0.0632 0.0610  -0.0124 7   SER   A CB  
86   C CB  B SER   A 7   ? 0.2631 0.3351 0.2633 -0.0516 0.0437  -0.0074 7   SER   A CB  
87   O OG  A SER   A 7   ? 0.3055 0.3755 0.2886 -0.0496 0.0506  -0.0134 7   SER   A OG  
88   O OG  B SER   A 7   ? 0.2758 0.3478 0.2938 -0.0428 0.0358  -0.0049 7   SER   A OG  
99   N N   A GLY   A 8   ? 0.2098 0.2583 0.1989 -0.0703 0.0606  -0.0357 8   GLY   A N   
100  N N   B GLY   A 8   ? 0.2175 0.2669 0.2070 -0.0431 0.0568  -0.0024 8   GLY   A N   
101  C CA  A GLY   A 8   ? 0.1981 0.2276 0.2155 -0.0472 0.0638  -0.0286 8   GLY   A CA  
102  C CA  B GLY   A 8   ? 0.2059 0.2413 0.2104 -0.0295 0.0485  0.0054  8   GLY   A CA  
103  C C   A GLY   A 8   ? 0.1842 0.2094 0.2050 -0.0354 0.0540  -0.0153 8   GLY   A C   
104  C C   B GLY   A 8   ? 0.1901 0.2175 0.1918 -0.0184 0.0409  0.0118  8   GLY   A C   
105  O O   A GLY   A 8   ? 0.1852 0.2077 0.2311 -0.0141 0.0556  -0.0347 8   GLY   A O   
106  O O   B GLY   A 8   ? 0.1903 0.2153 0.2020 -0.0072 0.0400  0.0073  8   GLY   A O   
113  N N   A TYR   A 9   ? 0.1695 0.1961 0.1868 -0.0282 0.0487  0.0049  9   TYR   A N   
114  N N   B TYR   A 9   ? 0.1766 0.1989 0.1756 -0.0110 0.0375  0.0215  9   TYR   A N   
115  C CA  A TYR   A 9   ? 0.1583 0.1879 0.1683 -0.0258 0.0401  0.0092  9   TYR   A CA  
116  C CA  B TYR   A 9   ? 0.1664 0.1886 0.1675 -0.0076 0.0350  0.0234  9   TYR   A CA  
117  C C   A TYR   A 9   ? 0.1634 0.1712 0.1600 -0.0197 0.0421  0.0204  9   TYR   A C   
118  C C   B TYR   A 9   ? 0.1618 0.1780 0.1653 0.0010  0.0391  0.0234  9   TYR   A C   
119  O O   A TYR   A 9   ? 0.1887 0.1749 0.1611 -0.0214 0.0354  0.0140  9   TYR   A O   
120  O O   B TYR   A 9   ? 0.1700 0.1825 0.1826 0.0075  0.0356  0.0223  9   TYR   A O   
121  C CB  A TYR   A 9   ? 0.1474 0.2030 0.1653 -0.0209 0.0357  0.0120  9   TYR   A CB  
122  C CB  B TYR   A 9   ? 0.1656 0.1942 0.1814 -0.0090 0.0251  0.0199  9   TYR   A CB  
123  C CG  A TYR   A 9   ? 0.1465 0.2089 0.1679 -0.0094 0.0352  0.0049  9   TYR   A CG  
124  C CG  B TYR   A 9   ? 0.1684 0.1942 0.1786 -0.0081 0.0221  0.0131  9   TYR   A CG  
125  C CD1 A TYR   A 9   ? 0.1521 0.2201 0.1742 -0.0199 0.0391  -0.0033 9   TYR   A CD1 
126  C CD1 B TYR   A 9   ? 0.1731 0.2002 0.1878 -0.0162 0.0242  0.0059  9   TYR   A CD1 
127  C CD2 A TYR   A 9   ? 0.1441 0.2053 0.1828 -0.0050 0.0289  0.0232  9   TYR   A CD2 
128  C CD2 B TYR   A 9   ? 0.1679 0.1884 0.1785 -0.0080 0.0175  0.0149  9   TYR   A CD2 
129  C CE1 A TYR   A 9   ? 0.1542 0.2257 0.1995 -0.0177 0.0399  -0.0046 9   TYR   A CE1 
130  C CE1 B TYR   A 9   ? 0.1750 0.2008 0.1979 -0.0184 0.0242  -0.0016 9   TYR   A CE1 
131  C CE2 A TYR   A 9   ? 0.1459 0.2142 0.1763 -0.0017 0.0320  0.0188  9   TYR   A CE2 
132  C CE2 B TYR   A 9   ? 0.1696 0.1934 0.1834 -0.0094 0.0181  0.0093  9   TYR   A CE2 
133  C CZ  A TYR   A 9   ? 0.1425 0.2210 0.1986 -0.0176 0.0470  0.0088  9   TYR   A CZ  
134  C CZ  B TYR   A 9   ? 0.1725 0.1980 0.2029 -0.0208 0.0286  0.0019  9   TYR   A CZ  
135  O OH  A TYR   A 9   ? 0.1441 0.2321 0.2280 -0.0257 0.0422  0.0024  9   TYR   A OH  
136  O OH  B TYR   A 9   ? 0.1798 0.2025 0.2225 -0.0271 0.0296  -0.0033 9   TYR   A OH  
155  N N   A LEU   A 10  ? 0.1595 0.1596 0.1705 -0.0241 0.0208  0.0274  10  LEU   A N   
156  N N   B LEU   A 10  ? 0.1615 0.1729 0.1533 -0.0070 0.0317  0.0190  10  LEU   A N   
157  C CA  A LEU   A 10  ? 0.1486 0.1568 0.1794 -0.0273 0.0181  0.0374  10  LEU   A CA  
158  C CA  B LEU   A 10  ? 0.1606 0.1718 0.1599 -0.0181 0.0210  0.0145  10  LEU   A CA  
159  C C   A LEU   A 10  ? 0.1440 0.1522 0.1783 -0.0222 0.0178  0.0317  10  LEU   A C   
160  C C   B LEU   A 10  ? 0.1627 0.1669 0.1544 -0.0198 0.0038  0.0229  10  LEU   A C   
161  O O   A LEU   A 10  ? 0.1485 0.1487 0.1594 -0.0196 0.0302  0.0248  10  LEU   A O   
162  O O   B LEU   A 10  ? 0.1637 0.1540 0.1378 -0.0277 0.0092  0.0253  10  LEU   A O   
163  C CB  A LEU   A 10  ? 0.1575 0.1706 0.2135 -0.0175 0.0029  0.0583  10  LEU   A CB  
164  C CB  B LEU   A 10  ? 0.1597 0.1747 0.1706 -0.0244 0.0180  0.0053  10  LEU   A CB  
165  C CG  A LEU   A 10  ? 0.1860 0.1968 0.2629 -0.0027 -0.0224 0.0624  10  LEU   A CG  
166  C CG  B LEU   A 10  ? 0.1723 0.1867 0.2117 -0.0218 0.0051  -0.0039 10  LEU   A CG  
167  C CD1 A LEU   A 10  ? 0.2046 0.2083 0.2969 -0.0125 -0.0242 0.0550  10  LEU   A CD1 
168  C CD1 B LEU   A 10  ? 0.1780 0.1883 0.2269 -0.0164 -0.0063 0.0001  10  LEU   A CD1 
169  C CD2 A LEU   A 10  ? 0.2027 0.2204 0.2887 0.0036  -0.0177 0.0460  10  LEU   A CD2 
170  C CD2 B LEU   A 10  ? 0.1778 0.1936 0.2078 -0.0167 0.0037  -0.0030 10  LEU   A CD2 
193  N N   A LYS   A 11  ? 0.1483 0.1507 0.2038 -0.0225 0.0201  0.0462  11  LYS   A N   
194  N N   B LYS   A 11  ? 0.1671 0.1705 0.1698 -0.0200 -0.0025 0.0337  11  LYS   A N   
195  C CA  A LYS   A 11  ? 0.1528 0.1512 0.2058 -0.0257 0.0195  0.0377  11  LYS   A CA  
196  C CA  B LYS   A 11  ? 0.1688 0.1704 0.1685 -0.0214 -0.0048 0.0286  11  LYS   A CA  
197  C C   A LYS   A 11  ? 0.1440 0.1555 0.1970 -0.0276 0.0240  0.0443  11  LYS   A C   
198  C C   B LYS   A 11  ? 0.1609 0.1750 0.1637 -0.0215 -0.0058 0.0360  11  LYS   A C   
199  O O   A LYS   A 11  ? 0.1409 0.1765 0.2083 -0.0426 0.0033  0.0603  11  LYS   A O   
200  O O   B LYS   A 11  ? 0.1638 0.1818 0.1665 -0.0262 -0.0147 0.0504  11  LYS   A O   
201  C CB  A LYS   A 11  ? 0.1612 0.1432 0.1816 -0.0242 0.0178  0.0225  11  LYS   A CB  
202  C CB  B LYS   A 11  ? 0.1759 0.1595 0.1555 -0.0204 -0.0022 0.0102  11  LYS   A CB  
203  C CG  A LYS   A 11  ? 0.1776 0.1406 0.1731 -0.0275 0.0233  0.0235  11  LYS   A CG  
204  C CG  B LYS   A 11  ? 0.1850 0.1558 0.1490 -0.0194 0.0013  0.0018  11  LYS   A CG  
205  C CD  A LYS   A 11  ? 0.1982 0.1450 0.1658 -0.0194 0.0156  0.0219  11  LYS   A CD  
206  C CD  B LYS   A 11  ? 0.1926 0.1550 0.1510 -0.0182 0.0099  0.0032  11  LYS   A CD  
207  C CE  A LYS   A 11  ? 0.2047 0.1453 0.1676 -0.0159 0.0109  0.0229  11  LYS   A CE  
208  C CE  B LYS   A 11  ? 0.1947 0.1556 0.1501 -0.0198 0.0129  0.0075  11  LYS   A CE  
209  N NZ  A LYS   A 11  ? 0.2033 0.1491 0.1879 -0.0092 -0.0097 0.0255  11  LYS   A NZ  
210  N NZ  B LYS   A 11  ? 0.1951 0.1607 0.1457 -0.0172 0.0111  0.0132  11  LYS   A NZ  
237  N N   A LEU   A 12  ? 0.1375 0.1339 0.1858 -0.0134 0.0266  0.0227  12  LEU   A N   
238  N N   B LEU   A 12  ? 0.1538 0.1674 0.1687 -0.0166 0.0055  0.0304  12  LEU   A N   
239  C CA  A LEU   A 12  ? 0.1426 0.1420 0.1782 -0.0056 0.0203  0.0278  12  LEU   A CA  
240  C CA  B LEU   A 12  ? 0.1461 0.1659 0.1666 -0.0072 0.0177  0.0329  12  LEU   A CA  
241  C C   A LEU   A 12  ? 0.1463 0.1327 0.1849 -0.0182 0.0186  0.0324  12  LEU   A C   
242  C C   B LEU   A 12  ? 0.1428 0.1576 0.1779 -0.0025 0.0323  0.0227  12  LEU   A C   
243  O O   A LEU   A 12  ? 0.1495 0.1365 0.2003 -0.0153 0.0236  0.0111  12  LEU   A O   
244  O O   B LEU   A 12  ? 0.1467 0.1577 0.1705 -0.0023 0.0308  0.0144  12  LEU   A O   
245  C CB  A LEU   A 12  ? 0.1495 0.1435 0.1954 -0.0037 0.0096  0.0307  12  LEU   A CB  
246  C CB  B LEU   A 12  ? 0.1453 0.1683 0.1854 -0.0067 0.0276  0.0386  12  LEU   A CB  
247  C CG  A LEU   A 12  ? 0.1604 0.1579 0.2116 -0.0005 0.0215  0.0329  12  LEU   A CG  
248  C CG  B LEU   A 12  ? 0.1453 0.1683 0.2084 -0.0023 0.0398  0.0276  12  LEU   A CG  
249  C CD1 A LEU   A 12  ? 0.1723 0.1608 0.2143 0.0134  0.0269  0.0465  12  LEU   A CD1 
250  C CD1 B LEU   A 12  ? 0.1450 0.1733 0.2114 0.0046  0.0487  0.0270  12  LEU   A CD1 
251  C CD2 A LEU   A 12  ? 0.1610 0.1697 0.2366 -0.0046 0.0273  0.0292  12  LEU   A CD2 
252  C CD2 B LEU   A 12  ? 0.1427 0.1654 0.2237 0.0005  0.0402  0.0161  12  LEU   A CD2 
275  N N   A THR   A 13  ? 0.1371 0.1336 0.2019 -0.0220 0.0112  0.0221  13  THR   A N   
276  N N   B THR   A 13  ? 0.1380 0.1495 0.1969 -0.0009 0.0279  0.0172  13  THR   A N   
277  C CA  A THR   A 13  ? 0.1407 0.1424 0.1979 -0.0140 0.0198  0.0201  13  THR   A CA  
278  C CA  B THR   A 13  ? 0.1416 0.1498 0.1898 -0.0064 0.0281  0.0159  13  THR   A CA  
279  C C   A THR   A 13  ? 0.1416 0.1399 0.2130 -0.0137 0.0098  0.0300  13  THR   A C   
280  C C   B THR   A 13  ? 0.1442 0.1545 0.1986 -0.0142 0.0333  0.0181  13  THR   A C   
281  O O   A THR   A 13  ? 0.1435 0.1411 0.2104 -0.0077 0.0083  0.0257  13  THR   A O   
282  O O   B THR   A 13  ? 0.1494 0.1608 0.2026 -0.0137 0.0299  0.0161  13  THR   A O   
283  C CB  A THR   A 13  ? 0.1426 0.1620 0.2200 -0.0133 0.0165  0.0262  13  THR   A CB  
284  C CB  B THR   A 13  ? 0.1411 0.1533 0.1916 -0.0036 0.0229  0.0146  13  THR   A CB  
285  O OG1 A THR   A 13  ? 0.1482 0.1562 0.2169 -0.0116 0.0016  0.0384  13  THR   A OG1 
286  O OG1 B THR   A 13  ? 0.1328 0.1541 0.1930 -0.0048 0.0316  0.0236  13  THR   A OG1 
287  C CG2 A THR   A 13  ? 0.1473 0.1800 0.2311 -0.0150 0.0201  0.0180  13  THR   A CG2 
288  C CG2 B THR   A 13  ? 0.1500 0.1620 0.1979 0.0061  0.0222  0.0091  13  THR   A CG2 
303  N N   A ASP   A 14  ? 0.1483 0.1416 0.2305 -0.0150 0.0067  0.0370  14  ASP   A N   
304  N N   B ASP   A 14  ? 0.1427 0.1530 0.2047 -0.0227 0.0388  0.0264  14  ASP   A N   
305  C CA  A ASP   A 14  ? 0.1485 0.1529 0.2478 -0.0066 0.0004  0.0516  14  ASP   A CA  
306  C CA  B ASP   A 14  ? 0.1512 0.1597 0.2211 -0.0262 0.0201  0.0471  14  ASP   A CA  
307  C C   A ASP   A 14  ? 0.1581 0.1549 0.2199 -0.0088 -0.0126 0.0451  14  ASP   A C   
308  C C   B ASP   A 14  ? 0.1498 0.1551 0.2139 -0.0234 0.0085  0.0524  14  ASP   A C   
309  O O   A ASP   A 14  ? 0.1705 0.1618 0.2206 -0.0107 -0.0243 0.0502  14  ASP   A O   
310  O O   B ASP   A 14  ? 0.1496 0.1545 0.2220 -0.0232 0.0014  0.0626  14  ASP   A O   
311  C CB  A ASP   A 14  ? 0.1495 0.1830 0.3220 -0.0091 0.0026  0.0626  14  ASP   A CB  
312  C CB  B ASP   A 14  ? 0.1641 0.1784 0.2596 -0.0280 0.0070  0.0523  14  ASP   A CB  
313  C CG  A ASP   A 14  ? 0.1627 0.2286 0.4014 -0.0140 0.0028  0.0699  14  ASP   A CG  
314  C CG  B ASP   A 14  ? 0.1641 0.2111 0.2956 -0.0347 0.0081  0.0510  14  ASP   A CG  
315  O OD1 A ASP   A 14  ? 0.1726 0.2426 0.4263 -0.0029 -0.0118 0.0691  14  ASP   A OD1 
316  O OD1 B ASP   A 14  ? 0.1568 0.2090 0.3103 -0.0388 0.0168  0.0485  14  ASP   A OD1 
317  O OD2 A ASP   A 14  ? 0.1849 0.2629 0.4413 -0.0189 -0.0098 0.0561  14  ASP   A OD2 
318  O OD2 B ASP   A 14  ? 0.1717 0.2445 0.3211 -0.0357 -0.0037 0.0432  14  ASP   A OD2 
327  N N   . ASN   A 15  ? 0.1495 0.1532 0.2073 -0.0239 0.0031  0.0506  15  ASN   A N   
328  C CA  . ASN   A 15  ? 0.1473 0.1581 0.2236 -0.0186 -0.0028 0.0432  15  ASN   A CA  
329  C C   . ASN   A 15  ? 0.1469 0.1497 0.2394 -0.0201 0.0027  0.0411  15  ASN   A C   
330  O O   . ASN   A 15  ? 0.1512 0.1462 0.2832 -0.0168 -0.0176 0.0383  15  ASN   A O   
331  C CB  . ASN   A 15  ? 0.1461 0.1617 0.2045 -0.0107 -0.0048 0.0457  15  ASN   A CB  
332  C CG  . ASN   A 15  ? 0.1493 0.1683 0.2087 -0.0061 0.0045  0.0301  15  ASN   A CG  
333  O OD1 . ASN   A 15  ? 0.1641 0.1689 0.2442 -0.0200 0.0103  0.0338  15  ASN   A OD1 
334  N ND2 . ASN   A 15  ? 0.1522 0.1802 0.2016 -0.0072 0.0165  0.0294  15  ASN   A ND2 
342  N N   A VAL   A 16  ? 0.1463 0.1465 0.2103 -0.0193 0.0058  0.0383  16  VAL   A N   
343  N N   B VAL   A 16  ? 0.1465 0.1569 0.2165 -0.0155 0.0106  0.0466  16  VAL   A N   
344  C CA  A VAL   A 16  ? 0.1433 0.1505 0.2141 -0.0168 0.0016  0.0320  16  VAL   A CA  
345  C CA  B VAL   A 16  ? 0.1455 0.1658 0.1964 -0.0102 0.0177  0.0512  16  VAL   A CA  
346  C C   A VAL   A 16  ? 0.1305 0.1452 0.1957 -0.0249 -0.0003 0.0268  16  VAL   A C   
347  C C   B VAL   A 16  ? 0.1399 0.1691 0.1854 -0.0075 0.0103  0.0559  16  VAL   A C   
348  O O   A VAL   A 16  ? 0.1275 0.1457 0.1991 -0.0279 0.0094  0.0092  16  VAL   A O   
349  O O   B VAL   A 16  ? 0.1386 0.1726 0.1853 -0.0027 0.0134  0.0586  16  VAL   A O   
350  C CB  A VAL   A 16  ? 0.1507 0.1634 0.2026 -0.0044 0.0078  0.0383  16  VAL   A CB  
351  C CB  B VAL   A 16  ? 0.1500 0.1728 0.1739 -0.0059 0.0343  0.0494  16  VAL   A CB  
352  C CG1 A VAL   A 16  ? 0.1625 0.1740 0.2056 0.0010  0.0080  0.0304  16  VAL   A CG1 
353  C CG1 B VAL   A 16  ? 0.1545 0.1772 0.1728 -0.0048 0.0357  0.0440  16  VAL   A CG1 
354  C CG2 A VAL   A 16  ? 0.1551 0.1739 0.2173 -0.0003 0.0201  0.0334  16  VAL   A CG2 
355  C CG2 B VAL   A 16  ? 0.1522 0.1796 0.1869 -0.0049 0.0416  0.0418  16  VAL   A CG2 
374  N N   A TYR   A 17  ? 0.1332 0.1392 0.2003 -0.0214 0.0147  0.0367  17  TYR   A N   
375  N N   B TYR   A 17  ? 0.1407 0.1665 0.1833 -0.0064 0.0060  0.0518  17  TYR   A N   
376  C CA  A TYR   A 17  ? 0.1458 0.1427 0.1842 -0.0174 0.0109  0.0415  17  TYR   A CA  
377  C CA  B TYR   A 17  ? 0.1384 0.1629 0.1653 -0.0084 -0.0029 0.0465  17  TYR   A CA  
378  C C   A TYR   A 17  ? 0.1392 0.1386 0.1947 -0.0206 0.0149  0.0276  17  TYR   A C   
379  C C   B TYR   A 17  ? 0.1364 0.1584 0.1634 -0.0138 -0.0050 0.0373  17  TYR   A C   
380  O O   A TYR   A 17  ? 0.1351 0.1374 0.1895 -0.0170 0.0225  0.0272  17  TYR   A O   
381  O O   B TYR   A 17  ? 0.1307 0.1631 0.1688 -0.0181 -0.0110 0.0415  17  TYR   A O   
382  C CB  A TYR   A 17  ? 0.1650 0.1470 0.1921 -0.0290 -0.0009 0.0439  17  TYR   A CB  
383  C CB  B TYR   A 17  ? 0.1427 0.1675 0.1709 -0.0084 -0.0039 0.0413  17  TYR   A CB  
384  C CG  A TYR   A 17  ? 0.1857 0.1630 0.2068 -0.0326 -0.0162 0.0396  17  TYR   A CG  
385  C CG  B TYR   A 17  ? 0.1489 0.1760 0.1762 -0.0057 -0.0049 0.0340  17  TYR   A CG  
386  C CD1 A TYR   A 17  ? 0.1928 0.1730 0.2197 -0.0262 -0.0232 0.0379  17  TYR   A CD1 
387  C CD1 B TYR   A 17  ? 0.1545 0.1805 0.1823 0.0063  -0.0087 0.0298  17  TYR   A CD1 
388  C CD2 A TYR   A 17  ? 0.1951 0.1670 0.1989 -0.0423 -0.0260 0.0552  17  TYR   A CD2 
389  C CD2 B TYR   A 17  ? 0.1540 0.1831 0.1725 -0.0066 -0.0090 0.0389  17  TYR   A CD2 
390  C CE1 A TYR   A 17  ? 0.1937 0.1712 0.2262 -0.0282 -0.0348 0.0456  17  TYR   A CE1 
391  C CE1 B TYR   A 17  ? 0.1600 0.1867 0.1977 0.0078  -0.0039 0.0321  17  TYR   A CE1 
392  C CE2 A TYR   A 17  ? 0.2001 0.1638 0.2110 -0.0379 -0.0375 0.0482  17  TYR   A CE2 
393  C CE2 B TYR   A 17  ? 0.1601 0.1874 0.1864 0.0003  -0.0056 0.0311  17  TYR   A CE2 
394  C CZ  A TYR   A 17  ? 0.1991 0.1644 0.2168 -0.0347 -0.0427 0.0501  17  TYR   A CZ  
395  C CZ  B TYR   A 17  ? 0.1613 0.1917 0.2011 0.0071  -0.0103 0.0302  17  TYR   A CZ  
396  O OH  A TYR   A 17  ? 0.2079 0.1587 0.2206 -0.0351 -0.0508 0.0497  17  TYR   A OH  
397  O OH  B TYR   A 17  ? 0.1613 0.1988 0.2249 0.0119  -0.0147 0.0281  17  TYR   A OH  
416  N N   A ILE   A 18  ? 0.1437 0.1419 0.1807 -0.0198 0.0143  0.0336  18  ILE   A N   
417  N N   B ILE   A 18  ? 0.1344 0.1518 0.1454 -0.0173 0.0016  0.0332  18  ILE   A N   
418  C CA  A ILE   A 18  ? 0.1500 0.1424 0.1610 -0.0107 0.0206  0.0227  18  ILE   A CA  
419  C CA  B ILE   A 18  ? 0.1314 0.1452 0.1291 -0.0147 0.0145  0.0176  18  ILE   A CA  
420  C C   A ILE   A 18  ? 0.1528 0.1536 0.1697 -0.0177 0.0170  0.0215  18  ILE   A C   
421  C C   B ILE   A 18  ? 0.1275 0.1541 0.1133 -0.0189 0.0096  0.0243  18  ILE   A C   
422  O O   A ILE   A 18  ? 0.1515 0.1640 0.1583 -0.0242 0.0157  0.0314  18  ILE   A O   
423  O O   B ILE   A 18  ? 0.1290 0.1653 0.1221 -0.0293 0.0206  0.0255  18  ILE   A O   
424  C CB  A ILE   A 18  ? 0.1606 0.1440 0.1487 -0.0021 0.0211  0.0289  18  ILE   A CB  
425  C CB  B ILE   A 18  ? 0.1366 0.1412 0.0971 -0.0092 0.0288  0.0138  18  ILE   A CB  
426  C CG1 A ILE   A 18  ? 0.1723 0.1445 0.1489 0.0085  0.0124  0.0238  18  ILE   A CG1 
427  C CG1 B ILE   A 18  ? 0.1537 0.1500 0.1278 -0.0117 0.0409  0.0170  18  ILE   A CG1 
428  C CG2 A ILE   A 18  ? 0.1619 0.1417 0.1542 0.0051  0.0154  0.0164  18  ILE   A CG2 
429  C CG2 B ILE   A 18  ? 0.1462 0.1484 0.1051 -0.0086 0.0226  0.0193  18  ILE   A CG2 
430  C CD1 A ILE   A 18  ? 0.1904 0.1476 0.1581 0.0250  0.0057  0.0314  18  ILE   A CD1 
431  C CD1 B ILE   A 18  ? 0.1674 0.1567 0.1382 -0.0078 0.0490  0.0047  18  ILE   A CD1 
454  N N   A LYS   A 19  ? 0.1529 0.1526 0.1722 -0.0125 0.0271  0.0232  19  LYS   A N   
455  N N   B LYS   A 19  ? 0.1289 0.1504 0.1141 -0.0108 0.0151  0.0196  19  LYS   A N   
456  C CA  A LYS   A 19  ? 0.1616 0.1662 0.1711 -0.0107 0.0239  0.0215  19  LYS   A CA  
457  C CA  B LYS   A 19  ? 0.1356 0.1605 0.1293 -0.0039 0.0214  0.0172  19  LYS   A CA  
458  C C   A LYS   A 19  ? 0.1546 0.1598 0.1813 -0.0053 0.0354  0.0298  19  LYS   A C   
459  C C   B LYS   A 19  ? 0.1415 0.1538 0.1278 0.0049  0.0209  0.0237  19  LYS   A C   
460  O O   A LYS   A 19  ? 0.1521 0.1602 0.1626 -0.0062 0.0274  0.0221  19  LYS   A O   
461  O O   B LYS   A 19  ? 0.1429 0.1522 0.1372 0.0007  0.0100  0.0236  19  LYS   A O   
462  C CB  A LYS   A 19  ? 0.1808 0.1873 0.1713 -0.0077 0.0125  0.0203  19  LYS   A CB  
463  C CB  B LYS   A 19  ? 0.1355 0.1783 0.1438 -0.0048 0.0283  0.0013  19  LYS   A CB  
464  C CG  A LYS   A 19  ? 0.2070 0.2087 0.1916 -0.0095 -0.0004 0.0098  19  LYS   A CG  
465  C CG  B LYS   A 19  ? 0.1565 0.1943 0.1459 -0.0062 0.0259  0.0059  19  LYS   A CG  
466  C CD  A LYS   A 19  ? 0.2362 0.2335 0.2083 -0.0164 -0.0095 -0.0081 19  LYS   A CD  
467  C CD  B LYS   A 19  ? 0.1734 0.2111 0.1531 -0.0145 0.0210  0.0215  19  LYS   A CD  
468  C CE  A LYS   A 19  ? 0.2588 0.2515 0.2253 -0.0327 -0.0096 -0.0168 19  LYS   A CE  
469  C CE  B LYS   A 19  ? 0.1794 0.2215 0.1756 -0.0244 0.0060  0.0270  19  LYS   A CE  
470  N NZ  A LYS   A 19  ? 0.2717 0.2624 0.2099 -0.0471 -0.0034 -0.0173 19  LYS   A NZ  
471  N NZ  B LYS   A 19  ? 0.1848 0.2265 0.1733 -0.0430 0.0111  0.0312  19  LYS   A NZ  
498  N N   A ASN   A 20  ? 0.1557 0.1656 0.2217 -0.0103 0.0389  0.0500  20  ASN   A N   
499  N N   B ASN   A 20  ? 0.1508 0.1567 0.1471 0.0084  0.0229  0.0231  20  ASN   A N   
500  C CA  A ASN   A 20  ? 0.1653 0.1827 0.2403 0.0041  0.0410  0.0434  20  ASN   A CA  
501  C CA  B ASN   A 20  ? 0.1626 0.1648 0.1502 0.0148  0.0195  0.0141  20  ASN   A CA  
502  C C   A ASN   A 20  ? 0.1840 0.1930 0.2563 -0.0094 0.0542  0.0266  20  ASN   A C   
503  C C   B ASN   A 20  ? 0.1653 0.1623 0.1474 0.0122  0.0216  0.0099  20  ASN   A C   
504  O O   A ASN   A 20  ? 0.1967 0.2030 0.2517 -0.0284 0.0458  0.0085  20  ASN   A O   
505  O O   B ASN   A 20  ? 0.1698 0.1651 0.1455 0.0015  0.0161  0.0039  20  ASN   A O   
506  C CB  A ASN   A 20  ? 0.1690 0.1978 0.2475 0.0166  0.0433  0.0503  20  ASN   A CB  
507  C CB  B ASN   A 20  ? 0.1742 0.1776 0.1581 0.0162  0.0102  0.0087  20  ASN   A CB  
508  C CG  A ASN   A 20  ? 0.1759 0.2087 0.2552 0.0363  0.0516  0.0545  20  ASN   A CG  
509  C CG  B ASN   A 20  ? 0.1854 0.1866 0.1675 0.0145  0.0053  0.0022  20  ASN   A CG  
510  O OD1 A ASN   A 20  ? 0.2009 0.2123 0.2984 0.0471  0.0670  0.0418  20  ASN   A OD1 
511  O OD1 B ASN   A 20  ? 0.1992 0.1950 0.1800 0.0167  -0.0088 -0.0025 20  ASN   A OD1 
512  N ND2 A ASN   A 20  ? 0.1847 0.2149 0.2569 0.0339  0.0285  0.0732  20  ASN   A ND2 
513  N ND2 B ASN   A 20  ? 0.1868 0.1864 0.1679 0.0145  0.0022  0.0015  20  ASN   A ND2 
526  N N   A ALA   A 21  ? 0.1935 0.1955 0.2626 -0.0055 0.0563  0.0216  21  ALA   A N   
527  N N   B ALA   A 21  ? 0.1677 0.1640 0.1610 0.0112  0.0343  0.0052  21  ALA   A N   
528  C CA  A ALA   A 21  ? 0.2031 0.1983 0.2611 -0.0108 0.0462  0.0317  21  ALA   A CA  
529  C CA  B ALA   A 21  ? 0.1743 0.1678 0.1774 -0.0017 0.0403  0.0115  21  ALA   A CA  
530  C C   A ALA   A 21  ? 0.1836 0.1895 0.2564 -0.0023 0.0450  0.0383  21  ALA   A C   
531  C C   B ALA   A 21  ? 0.1738 0.1686 0.1955 -0.0012 0.0556  0.0174  21  ALA   A C   
532  O O   A ALA   A 21  ? 0.1686 0.1896 0.2538 0.0144  0.0360  0.0482  21  ALA   A O   
533  O O   B ALA   A 21  ? 0.1733 0.1703 0.2078 0.0076  0.0586  0.0204  21  ALA   A O   
534  C CB  A ALA   A 21  ? 0.2297 0.2170 0.2873 -0.0219 0.0298  0.0310  21  ALA   A CB  
535  C CB  B ALA   A 21  ? 0.1827 0.1788 0.1931 -0.0195 0.0376  0.0233  21  ALA   A CB  
546  N N   A ASP   A 22  ? 0.1826 0.1792 0.2514 -0.0088 0.0551  0.0430  22  ASP   A N   
547  N N   B ASP   A 22  ? 0.1737 0.1670 0.2006 -0.0066 0.0698  0.0251  22  ASP   A N   
548  C CA  A ASP   A 22  ? 0.1849 0.1841 0.2425 -0.0082 0.0466  0.0325  22  ASP   A CA  
549  C CA  B ASP   A 22  ? 0.1769 0.1728 0.2089 -0.0045 0.0643  0.0290  22  ASP   A CA  
550  C C   A ASP   A 22  ? 0.1816 0.1914 0.2027 -0.0053 0.0447  0.0341  22  ASP   A C   
551  C C   B ASP   A 22  ? 0.1661 0.1814 0.1909 -0.0096 0.0608  0.0259  22  ASP   A C   
552  O O   A ASP   A 22  ? 0.1915 0.2062 0.2132 -0.0088 0.0461  0.0380  22  ASP   A O   
553  O O   B ASP   A 22  ? 0.1653 0.1949 0.1996 -0.0119 0.0623  0.0078  22  ASP   A O   
554  C CB  A ASP   A 22  ? 0.2003 0.1876 0.2902 -0.0078 0.0412  0.0278  22  ASP   A CB  
555  C CB  B ASP   A 22  ? 0.1931 0.1763 0.2401 0.0098  0.0646  0.0233  22  ASP   A CB  
556  C CG  A ASP   A 22  ? 0.2155 0.1971 0.3409 -0.0055 0.0279  0.0421  22  ASP   A CG  
557  C CG  B ASP   A 22  ? 0.2056 0.1845 0.2543 0.0179  0.0637  0.0267  22  ASP   A CG  
558  O OD1 A ASP   A 22  ? 0.2107 0.2010 0.3739 -0.0190 0.0145  0.0664  22  ASP   A OD1 
559  O OD1 B ASP   A 22  ? 0.2039 0.1821 0.2419 0.0161  0.0725  0.0195  22  ASP   A OD1 
560  O OD2 A ASP   A 22  ? 0.2384 0.2087 0.3753 0.0008  0.0306  0.0215  22  ASP   A OD2 
561  O OD2 B ASP   A 22  ? 0.2163 0.1993 0.2830 0.0178  0.0667  0.0249  22  ASP   A OD2 
570  N N   A ILE   A 23  ? 0.1794 0.1878 0.1948 -0.0063 0.0364  0.0171  23  ILE   A N   
571  N N   B ILE   A 23  ? 0.1610 0.1790 0.1838 -0.0151 0.0416  0.0279  23  ILE   A N   
572  C CA  A ILE   A 23  ? 0.1795 0.1818 0.1818 -0.0084 0.0340  0.0145  23  ILE   A CA  
573  C CA  B ILE   A 23  ? 0.1569 0.1787 0.1642 -0.0217 0.0303  0.0245  23  ILE   A CA  
574  C C   A ILE   A 23  ? 0.1785 0.1906 0.1755 -0.0043 0.0509  0.0148  23  ILE   A C   
575  C C   B ILE   A 23  ? 0.1688 0.1878 0.1635 -0.0341 0.0320  0.0094  23  ILE   A C   
576  O O   A ILE   A 23  ? 0.1853 0.2002 0.1792 -0.0019 0.0414  0.0160  23  ILE   A O   
577  O O   B ILE   A 23  ? 0.1730 0.1901 0.1566 -0.0328 0.0289  -0.0028 23  ILE   A O   
578  C CB  A ILE   A 23  ? 0.1849 0.1722 0.1597 -0.0069 0.0358  0.0082  23  ILE   A CB  
579  C CB  B ILE   A 23  ? 0.1522 0.1731 0.1515 -0.0115 0.0198  0.0271  23  ILE   A CB  
580  C CG1 A ILE   A 23  ? 0.1910 0.1782 0.1657 -0.0107 0.0304  0.0069  23  ILE   A CG1 
581  C CG1 B ILE   A 23  ? 0.1520 0.1700 0.1449 -0.0119 0.0119  0.0228  23  ILE   A CG1 
582  C CG2 A ILE   A 23  ? 0.1815 0.1701 0.1737 -0.0042 0.0421  0.0023  23  ILE   A CG2 
583  C CG2 B ILE   A 23  ? 0.1490 0.1711 0.1528 -0.0052 0.0177  0.0212  23  ILE   A CG2 
584  C CD1 A ILE   A 23  ? 0.1914 0.1844 0.1651 -0.0130 0.0113  -0.0019 23  ILE   A CD1 
585  C CD1 B ILE   A 23  ? 0.1511 0.1689 0.1515 -0.0080 -0.0013 0.0172  23  ILE   A CD1 
608  N N   A VAL   A 24  ? 0.1823 0.1928 0.1933 -0.0129 0.0522  0.0128  24  VAL   A N   
609  N N   B VAL   A 24  ? 0.1834 0.1926 0.1765 -0.0447 0.0259  0.0040  24  VAL   A N   
610  C CA  A VAL   A 24  ? 0.1982 0.2019 0.2029 -0.0221 0.0436  -0.0080 24  VAL   A CA  
611  C CA  B VAL   A 24  ? 0.2054 0.2012 0.1874 -0.0440 0.0263  -0.0005 24  VAL   A CA  
612  C C   A VAL   A 24  ? 0.2014 0.2194 0.2045 -0.0289 0.0309  -0.0149 24  VAL   A C   
613  C C   B VAL   A 24  ? 0.2175 0.2141 0.1961 -0.0357 0.0245  -0.0092 24  VAL   A C   
614  O O   A VAL   A 24  ? 0.2112 0.2169 0.2024 -0.0208 0.0393  -0.0189 24  VAL   A O   
615  O O   B VAL   A 24  ? 0.2288 0.2166 0.2079 -0.0312 0.0233  -0.0059 24  VAL   A O   
616  C CB  A VAL   A 24  ? 0.2095 0.2081 0.2167 -0.0272 0.0504  -0.0076 24  VAL   A CB  
617  C CB  B VAL   A 24  ? 0.2137 0.2040 0.1850 -0.0516 0.0264  0.0070  24  VAL   A CB  
618  C CG1 A VAL   A 24  ? 0.2218 0.2222 0.2423 -0.0248 0.0540  -0.0165 24  VAL   A CG1 
619  C CG1 B VAL   A 24  ? 0.2208 0.2142 0.1989 -0.0455 0.0298  0.0089  24  VAL   A CG1 
620  C CG2 A VAL   A 24  ? 0.2171 0.2162 0.2375 -0.0252 0.0503  -0.0016 24  VAL   A CG2 
621  C CG2 B VAL   A 24  ? 0.2171 0.1990 0.1749 -0.0617 0.0245  -0.0039 24  VAL   A CG2 
640  N N   A GLU   A 25  ? 0.2025 0.2465 0.2002 -0.0379 0.0404  -0.0216 25  GLU   A N   
641  N N   B GLU   A 25  ? 0.2178 0.2296 0.2003 -0.0308 0.0318  -0.0162 25  GLU   A N   
642  C CA  A GLU   A 25  ? 0.2192 0.2770 0.2029 -0.0360 0.0597  -0.0270 25  GLU   A CA  
643  C CA  B GLU   A 25  ? 0.2245 0.2449 0.2165 -0.0298 0.0376  -0.0119 25  GLU   A CA  
644  C C   A GLU   A 25  ? 0.2095 0.2825 0.1654 -0.0472 0.0649  -0.0348 25  GLU   A C   
645  C C   B GLU   A 25  ? 0.2254 0.2474 0.2143 -0.0268 0.0442  -0.0065 25  GLU   A C   
646  O O   A GLU   A 25  ? 0.2140 0.2952 0.1691 -0.0472 0.0532  -0.0413 25  GLU   A O   
647  O O   B GLU   A 25  ? 0.2290 0.2550 0.2207 -0.0256 0.0446  -0.0069 25  GLU   A O   
648  C CB  A GLU   A 25  ? 0.2449 0.3009 0.2529 -0.0290 0.0621  -0.0246 25  GLU   A CB  
649  C CB  B GLU   A 25  ? 0.2359 0.2574 0.2519 -0.0304 0.0377  -0.0144 25  GLU   A CB  
650  C CG  A GLU   A 25  ? 0.2726 0.3261 0.3224 -0.0280 0.0411  -0.0252 25  GLU   A CG  
651  C CG  B GLU   A 25  ? 0.2541 0.2734 0.3066 -0.0318 0.0315  -0.0179 25  GLU   A CG  
652  C CD  A GLU   A 25  ? 0.2913 0.3523 0.3856 -0.0214 0.0134  -0.0197 25  GLU   A CD  
653  C CD  B GLU   A 25  ? 0.2681 0.2916 0.3516 -0.0322 0.0203  -0.0202 25  GLU   A CD  
654  O OE1 A GLU   A 25  ? 0.3051 0.3669 0.3921 -0.0127 -0.0086 -0.0238 25  GLU   A OE1 
655  O OE1 B GLU   A 25  ? 0.2737 0.3020 0.3734 -0.0339 0.0181  -0.0196 25  GLU   A OE1 
656  O OE2 A GLU   A 25  ? 0.2928 0.3596 0.4149 -0.0206 0.0029  -0.0186 25  GLU   A OE2 
657  O OE2 B GLU   A 25  ? 0.2724 0.2964 0.3719 -0.0307 0.0144  -0.0184 25  GLU   A OE2 
670  N N   A GLU   A 26  ? 0.2057 0.2740 0.1728 -0.0619 0.0696  -0.0330 26  GLU   A N   
671  N N   B GLU   A 26  ? 0.2258 0.2375 0.2023 -0.0264 0.0526  -0.0015 26  GLU   A N   
672  C CA  A GLU   A 26  ? 0.2227 0.2762 0.1384 -0.0732 0.0633  -0.0196 26  GLU   A CA  
673  C CA  B GLU   A 26  ? 0.2361 0.2283 0.2034 -0.0269 0.0582  0.0151  26  GLU   A CA  
674  C C   A GLU   A 26  ? 0.2211 0.2663 0.1398 -0.0740 0.0532  -0.0045 26  GLU   A C   
675  C C   B GLU   A 26  ? 0.2338 0.2281 0.1909 -0.0221 0.0599  0.0176  26  GLU   A C   
676  O O   A GLU   A 26  ? 0.2271 0.2690 0.1510 -0.0846 0.0490  0.0067  26  GLU   A O   
677  O O   B GLU   A 26  ? 0.2368 0.2290 0.1883 -0.0263 0.0623  0.0247  26  GLU   A O   
678  C CB  A GLU   A 26  ? 0.2471 0.2844 0.1658 -0.0773 0.0578  -0.0179 26  GLU   A CB  
679  C CB  B GLU   A 26  ? 0.2477 0.2124 0.2291 -0.0348 0.0571  0.0220  26  GLU   A CB  
680  C CG  A GLU   A 26  ? 0.2739 0.2961 0.2435 -0.0732 0.0519  -0.0302 26  GLU   A CG  
681  C CG  B GLU   A 26  ? 0.2500 0.1921 0.2424 -0.0426 0.0788  0.0146  26  GLU   A CG  
682  C CD  A GLU   A 26  ? 0.2872 0.3006 0.2713 -0.0707 0.0588  -0.0330 26  GLU   A CD  
683  C CD  B GLU   A 26  ? 0.2407 0.1682 0.2303 -0.0553 0.1127  0.0056  26  GLU   A CD  
684  O OE1 A GLU   A 26  ? 0.2912 0.3111 0.2817 -0.0538 0.0748  -0.0406 26  GLU   A OE1 
685  O OE1 B GLU   A 26  ? 0.2371 0.1766 0.2085 -0.0393 0.1250  -0.0022 26  GLU   A OE1 
686  O OE2 A GLU   A 26  ? 0.2915 0.3008 0.3072 -0.0825 0.0606  -0.0294 26  GLU   A OE2 
687  O OE2 B GLU   A 26  ? 0.2349 0.1452 0.2547 -0.0718 0.1073  -0.0265 26  GLU   A OE2 
700  N N   A ALA   A 27  ? 0.2074 0.2480 0.1494 -0.0711 0.0510  -0.0054 27  ALA   A N   
701  N N   B ALA   A 27  ? 0.2300 0.2266 0.1789 -0.0165 0.0563  0.0145  27  ALA   A N   
702  C CA  A ALA   A 27  ? 0.2115 0.2450 0.1469 -0.0661 0.0502  -0.0102 27  ALA   A CA  
703  C CA  B ALA   A 27  ? 0.2372 0.2342 0.1726 -0.0097 0.0465  0.0054  27  ALA   A CA  
704  C C   A ALA   A 27  ? 0.2389 0.2552 0.1557 -0.0698 0.0614  -0.0201 27  ALA   A C   
705  C C   B ALA   A 27  ? 0.2592 0.2532 0.1845 -0.0064 0.0370  -0.0066 27  ALA   A C   
706  O O   A ALA   A 27  ? 0.2458 0.2537 0.1494 -0.0726 0.0497  -0.0127 27  ALA   A O   
707  O O   B ALA   A 27  ? 0.2618 0.2540 0.1990 -0.0052 0.0332  -0.0005 27  ALA   A O   
708  C CB  A ALA   A 27  ? 0.1973 0.2357 0.1542 -0.0658 0.0420  -0.0145 27  ALA   A CB  
709  C CB  B ALA   A 27  ? 0.2279 0.2281 0.1629 -0.0109 0.0433  0.0056  27  ALA   A CB  
720  N N   A LYS   A 28  ? 0.2696 0.2736 0.1798 -0.0648 0.0562  -0.0557 28  LYS   A N   
721  N N   B LYS   A 28  ? 0.2829 0.2742 0.2029 -0.0058 0.0263  -0.0250 28  LYS   A N   
722  C CA  A LYS   A 28  ? 0.3081 0.3089 0.2219 -0.0564 0.0538  -0.0669 28  LYS   A CA  
723  C CA  B LYS   A 28  ? 0.3102 0.3048 0.2342 -0.0054 0.0167  -0.0338 28  LYS   A CA  
724  C C   A LYS   A 28  ? 0.3348 0.3378 0.2142 -0.0644 0.0711  -0.0422 28  LYS   A C   
725  C C   B LYS   A 28  ? 0.3347 0.3315 0.2411 -0.0163 0.0284  -0.0219 28  LYS   A C   
726  O O   A LYS   A 28  ? 0.3480 0.3485 0.2604 -0.0681 0.0488  -0.0419 28  LYS   A O   
727  O O   B LYS   A 28  ? 0.3437 0.3396 0.2482 -0.0148 0.0184  -0.0213 28  LYS   A O   
728  C CB  A LYS   A 28  ? 0.3229 0.3211 0.2763 -0.0375 0.0379  -0.0864 28  LYS   A CB  
729  C CB  B LYS   A 28  ? 0.3157 0.3120 0.2704 0.0038  -0.0023 -0.0493 28  LYS   A CB  
730  C CG  A LYS   A 28  ? 0.3448 0.3343 0.3366 -0.0247 0.0189  -0.0858 28  LYS   A CG  
731  C CG  B LYS   A 28  ? 0.3257 0.3208 0.3143 0.0099  -0.0186 -0.0537 28  LYS   A CG  
732  C CD  A LYS   A 28  ? 0.3651 0.3525 0.4117 -0.0159 -0.0023 -0.0707 28  LYS   A CD  
733  C CD  B LYS   A 28  ? 0.3395 0.3324 0.3667 0.0134  -0.0298 -0.0526 28  LYS   A CD  
734  C CE  A LYS   A 28  ? 0.3776 0.3662 0.4532 -0.0109 -0.0164 -0.0718 28  LYS   A CE  
735  C CE  B LYS   A 28  ? 0.3525 0.3410 0.4016 0.0150  -0.0355 -0.0526 28  LYS   A CE  
736  N NZ  A LYS   A 28  ? 0.3871 0.3742 0.4911 -0.0074 -0.0193 -0.0852 28  LYS   A NZ  
737  N NZ  B LYS   A 28  ? 0.3601 0.3454 0.4206 0.0171  -0.0406 -0.0590 28  LYS   A NZ  
764  N N   A LYS   A 29  ? 0.3447 0.3565 0.2060 -0.0692 0.1082  -0.0155 29  LYS   A N   
765  N N   B LYS   A 29  ? 0.3480 0.3496 0.2554 -0.0311 0.0511  -0.0086 29  LYS   A N   
766  C CA  A LYS   A 29  ? 0.3613 0.3811 0.2285 -0.0694 0.1259  -0.0062 29  LYS   A CA  
767  C CA  B LYS   A 29  ? 0.3624 0.3696 0.2785 -0.0450 0.0693  -0.0030 29  LYS   A CA  
768  C C   A LYS   A 29  ? 0.3658 0.3817 0.2131 -0.0763 0.1105  0.0001  29  LYS   A C   
769  C C   B LYS   A 29  ? 0.3627 0.3720 0.2418 -0.0657 0.0825  0.0021  29  LYS   A C   
770  O O   A LYS   A 29  ? 0.3809 0.3973 0.2294 -0.0711 0.1073  0.0027  29  LYS   A O   
771  O O   B LYS   A 29  ? 0.3714 0.3808 0.2541 -0.0635 0.0809  0.0040  29  LYS   A O   
772  C CB  A LYS   A 29  ? 0.3754 0.4051 0.2885 -0.0618 0.1439  -0.0029 29  LYS   A CB  
773  C CB  B LYS   A 29  ? 0.3763 0.3870 0.3330 -0.0378 0.0711  -0.0009 29  LYS   A CB  
774  C CG  A LYS   A 29  ? 0.3947 0.4274 0.3605 -0.0551 0.1399  0.0057  29  LYS   A CG  
775  C CG  B LYS   A 29  ? 0.3907 0.4029 0.3878 -0.0309 0.0684  0.0048  29  LYS   A CG  
776  C CD  A LYS   A 29  ? 0.4123 0.4483 0.4343 -0.0488 0.1330  0.0089  29  LYS   A CD  
777  C CD  B LYS   A 29  ? 0.4023 0.4167 0.4375 -0.0247 0.0658  0.0085  29  LYS   A CD  
778  C CE  A LYS   A 29  ? 0.4246 0.4639 0.4690 -0.0433 0.1328  0.0057  29  LYS   A CE  
779  C CE  B LYS   A 29  ? 0.4100 0.4262 0.4641 -0.0198 0.0659  0.0077  29  LYS   A CE  
780  N NZ  A LYS   A 29  ? 0.4310 0.4729 0.5015 -0.0392 0.1310  0.0048  29  LYS   A NZ  
781  N NZ  B LYS   A 29  ? 0.4137 0.4310 0.4863 -0.0166 0.0641  0.0086  29  LYS   A NZ  
808  N N   . VAL   A 30  ? 0.3540 0.3649 0.1963 -0.0884 0.0968  0.0024  30  VAL   A N   
809  C CA  . VAL   A 30  ? 0.3467 0.3485 0.1816 -0.1120 0.0735  0.0204  30  VAL   A CA  
810  C C   . VAL   A 30  ? 0.3482 0.3381 0.1442 -0.1180 0.0500  0.0260  30  VAL   A C   
811  O O   . VAL   A 30  ? 0.3596 0.3506 0.1548 -0.1153 0.0381  0.0380  30  VAL   A O   
812  C CB  . VAL   A 30  ? 0.3460 0.3376 0.2223 -0.1242 0.0518  0.0317  30  VAL   A CB  
813  C CG1 . VAL   A 30  ? 0.3481 0.3273 0.2398 -0.1247 0.0367  0.0378  30  VAL   A CG1 
814  C CG2 . VAL   A 30  ? 0.3470 0.3410 0.2345 -0.1285 0.0466  0.0308  30  VAL   A CG2 
825  N N   . LYS   A 31  ? 0.3423 0.3163 0.1248 -0.1200 0.0271  0.0116  31  LYS   A N   
826  C CA  . LYS   A 31  ? 0.3536 0.3197 0.1445 -0.1033 0.0023  0.0169  31  LYS   A CA  
827  C C   . LYS   A 31  ? 0.3292 0.2987 0.1164 -0.0805 -0.0065 0.0520  31  LYS   A C   
828  O O   . LYS   A 31  ? 0.3474 0.3194 0.1391 -0.0744 -0.0266 0.0707  31  LYS   A O   
829  C CB  . LYS   A 31  ? 0.4018 0.3546 0.2553 -0.0962 -0.0241 -0.0031 31  LYS   A CB  
830  C CG  . LYS   A 31  ? 0.4584 0.3915 0.4082 -0.0847 -0.0455 -0.0118 31  LYS   A CG  
831  C CD  . LYS   A 31  ? 0.4978 0.4198 0.5102 -0.0737 -0.0612 -0.0235 31  LYS   A CD  
832  C CE  . LYS   A 31  ? 0.5183 0.4402 0.5711 -0.0640 -0.0711 -0.0379 31  LYS   A CE  
833  N NZ  . LYS   A 31  ? 0.5314 0.4630 0.6142 -0.0583 -0.0768 -0.0506 31  LYS   A NZ  
847  N N   . PRO   A 32  ? 0.2860 0.2648 0.1012 -0.0748 -0.0037 0.0330  32  PRO   A N   
848  C CA  . PRO   A 32  ? 0.2748 0.2433 0.1440 -0.0641 -0.0166 0.0491  32  PRO   A CA  
849  C C   . PRO   A 32  ? 0.2644 0.2350 0.1455 -0.0481 -0.0227 0.0555  32  PRO   A C   
850  O O   . PRO   A 32  ? 0.2552 0.2288 0.1661 -0.0478 -0.0384 0.0516  32  PRO   A O   
851  C CB  . PRO   A 32  ? 0.2636 0.2439 0.1649 -0.0687 -0.0176 0.0319  32  PRO   A CB  
852  C CG  . PRO   A 32  ? 0.2601 0.2491 0.1012 -0.0615 -0.0195 0.0152  32  PRO   A CG  
853  C CD  . PRO   A 32  ? 0.2685 0.2569 0.0921 -0.0645 -0.0043 0.0261  32  PRO   A CD  
861  N N   . THR   A 33  ? 0.2670 0.2344 0.1318 -0.0413 -0.0249 0.0530  33  THR   A N   
862  C CA  . THR   A 33  ? 0.2639 0.2384 0.1383 -0.0300 -0.0445 0.0493  33  THR   A CA  
863  C C   . THR   A 33  ? 0.2301 0.2230 0.1267 -0.0321 -0.0328 0.0399  33  THR   A C   
864  O O   . THR   A 33  ? 0.2275 0.2277 0.1589 -0.0341 -0.0362 0.0413  33  THR   A O   
865  C CB  . THR   A 33  ? 0.2940 0.2619 0.1637 -0.0198 -0.0495 0.0746  33  THR   A CB  
866  O OG1 . THR   A 33  ? 0.3222 0.2797 0.1889 -0.0051 -0.0415 0.0878  33  THR   A OG1 
867  C CG2 . THR   A 33  ? 0.2993 0.2726 0.1914 -0.0133 -0.0615 0.0733  33  THR   A CG2 
875  N N   . VAL   A 34  ? 0.2039 0.2041 0.1199 -0.0323 -0.0209 0.0359  34  VAL   A N   
876  C CA  . VAL   A 34  ? 0.1829 0.1921 0.1121 -0.0265 -0.0095 0.0269  34  VAL   A CA  
877  C C   . VAL   A 34  ? 0.1730 0.1742 0.1098 -0.0250 0.0019  0.0186  34  VAL   A C   
878  O O   . VAL   A 34  ? 0.1750 0.1767 0.1403 -0.0312 -0.0044 0.0329  34  VAL   A O   
879  C CB  . VAL   A 34  ? 0.1867 0.1940 0.1364 -0.0232 -0.0066 0.0172  34  VAL   A CB  
880  C CG1 . VAL   A 34  ? 0.1906 0.1902 0.1415 -0.0219 0.0089  0.0059  34  VAL   A CG1 
881  C CG2 . VAL   A 34  ? 0.1912 0.2047 0.1748 -0.0140 -0.0144 0.0143  34  VAL   A CG2 
891  N N   . VAL   A 35  ? 0.1616 0.1602 0.1145 -0.0281 -0.0082 0.0198  35  VAL   A N   
892  C CA  . VAL   A 35  ? 0.1544 0.1602 0.1056 -0.0218 -0.0002 0.0143  35  VAL   A CA  
893  C C   . VAL   A 35  ? 0.1463 0.1556 0.1148 -0.0172 0.0018  0.0218  35  VAL   A C   
894  O O   . VAL   A 35  ? 0.1389 0.1646 0.1223 -0.0255 0.0081  0.0139  35  VAL   A O   
895  C CB  . VAL   A 35  ? 0.1629 0.1636 0.1317 -0.0113 0.0043  0.0015  35  VAL   A CB  
896  C CG1 . VAL   A 35  ? 0.1705 0.1682 0.1425 -0.0122 -0.0004 -0.0029 35  VAL   A CG1 
897  C CG2 . VAL   A 35  ? 0.1601 0.1629 0.1533 -0.0096 0.0156  0.0055  35  VAL   A CG2 
907  N N   . VAL   A 36  ? 0.1347 0.1468 0.1096 -0.0163 0.0035  0.0190  36  VAL   A N   
908  C CA  . VAL   A 36  ? 0.1287 0.1353 0.0992 -0.0128 -0.0044 0.0099  36  VAL   A CA  
909  C C   . VAL   A 36  ? 0.1240 0.1387 0.1102 -0.0082 0.0036  0.0111  36  VAL   A C   
910  O O   . VAL   A 36  ? 0.1325 0.1411 0.1318 -0.0038 0.0133  0.0134  36  VAL   A O   
911  C CB  . VAL   A 36  ? 0.1337 0.1320 0.1181 -0.0143 -0.0021 0.0117  36  VAL   A CB  
912  C CG1 . VAL   A 36  ? 0.1397 0.1361 0.1241 -0.0175 -0.0026 0.0015  36  VAL   A CG1 
913  C CG2 . VAL   A 36  ? 0.1400 0.1325 0.1481 -0.0119 0.0032  0.0155  36  VAL   A CG2 
923  N N   . ASN   A 37  ? 0.1272 0.1296 0.1168 -0.0029 0.0030  0.0138  37  ASN   A N   
924  C CA  . ASN   A 37  ? 0.1271 0.1232 0.1090 0.0004  0.0063  0.0151  37  ASN   A CA  
925  C C   . ASN   A 37  ? 0.1245 0.1273 0.1121 -0.0050 0.0147  0.0188  37  ASN   A C   
926  O O   . ASN   A 37  ? 0.1357 0.1344 0.1191 0.0016  0.0145  0.0079  37  ASN   A O   
927  C CB  . ASN   A 37  ? 0.1281 0.1268 0.1239 0.0008  0.0036  0.0129  37  ASN   A CB  
928  C CG  . ASN   A 37  ? 0.1248 0.1302 0.1284 -0.0065 0.0075  0.0123  37  ASN   A CG  
929  O OD1 . ASN   A 37  ? 0.1241 0.1315 0.1401 -0.0034 0.0025  0.0138  37  ASN   A OD1 
930  N ND2 . ASN   A 37  ? 0.1358 0.1330 0.1312 -0.0024 -0.0011 0.0283  37  ASN   A ND2 
937  N N   A ALA   A 38  ? 0.1279 0.1347 0.1161 -0.0003 0.0170  0.0034  38  ALA   A N   
938  N N   B ALA   A 38  ? 0.1281 0.1340 0.1211 -0.0038 0.0112  0.0082  38  ALA   A N   
939  C CA  A ALA   A 38  ? 0.1391 0.1389 0.1084 -0.0053 0.0109  0.0016  38  ALA   A CA  
940  C CA  B ALA   A 38  ? 0.1369 0.1401 0.1226 -0.0086 0.0063  0.0063  38  ALA   A CA  
941  C C   A ALA   A 38  ? 0.1373 0.1376 0.1208 0.0054  0.0003  0.0050  38  ALA   A C   
942  C C   B ALA   A 38  ? 0.1375 0.1398 0.1290 -0.0042 -0.0012 0.0130  38  ALA   A C   
943  O O   A ALA   A 38  ? 0.1381 0.1335 0.1246 0.0085  0.0025  0.0099  38  ALA   A O   
944  O O   B ALA   A 38  ? 0.1405 0.1368 0.1319 -0.0012 -0.0015 0.0186  38  ALA   A O   
945  C CB  A ALA   A 38  ? 0.1471 0.1693 0.1315 -0.0149 -0.0071 -0.0084 38  ALA   A CB  
946  C CB  B ALA   A 38  ? 0.1426 0.1581 0.1365 -0.0151 -0.0009 -0.0058 38  ALA   A CB  
957  N N   A ALA   A 39  ? 0.1318 0.1325 0.1242 0.0062  0.0039  0.0121  39  ALA   A N   
958  N N   B ALA   A 39  ? 0.1341 0.1392 0.1298 -0.0076 0.0055  0.0177  39  ALA   A N   
959  C CA  A ALA   A 39  ? 0.1343 0.1285 0.1162 0.0045  0.0038  0.0024  39  ALA   A CA  
960  C CA  B ALA   A 39  ? 0.1390 0.1433 0.1341 -0.0069 0.0146  0.0199  39  ALA   A CA  
961  C C   A ALA   A 39  ? 0.1333 0.1271 0.1288 0.0001  -0.0014 0.0056  39  ALA   A C   
962  C C   B ALA   A 39  ? 0.1374 0.1383 0.1280 -0.0072 0.0126  0.0158  39  ALA   A C   
963  O O   A ALA   A 39  ? 0.1410 0.1282 0.1287 0.0037  -0.0045 0.0009  39  ALA   A O   
964  O O   B ALA   A 39  ? 0.1318 0.1388 0.1017 -0.0053 0.0175  0.0240  39  ALA   A O   
965  C CB  A ALA   A 39  ? 0.1368 0.1447 0.1225 -0.0037 -0.0031 -0.0078 39  ALA   A CB  
966  C CB  B ALA   A 39  ? 0.1459 0.1577 0.1492 -0.0071 0.0154  0.0173  39  ALA   A CB  
977  N N   . ASN   A 40  ? 0.1496 0.1354 0.1316 -0.0120 0.0155  0.0021  40  ASN   A N   
978  C CA  . ASN   A 40  ? 0.1588 0.1334 0.1312 -0.0051 0.0105  0.0084  40  ASN   A CA  
979  C C   . ASN   A 40  ? 0.1611 0.1240 0.1151 -0.0055 0.0259  0.0178  40  ASN   A C   
980  O O   . ASN   A 40  ? 0.1519 0.1295 0.1218 -0.0064 0.0223  0.0204  40  ASN   A O   
981  C CB  . ASN   A 40  ? 0.1684 0.1411 0.1386 0.0003  0.0020  0.0051  40  ASN   A CB  
982  C CG  . ASN   A 40  ? 0.1756 0.1424 0.1693 0.0015  0.0007  0.0027  40  ASN   A CG  
983  O OD1 . ASN   A 40  ? 0.1802 0.1456 0.1898 0.0014  0.0069  0.0010  40  ASN   A OD1 
984  N ND2 . ASN   A 40  ? 0.1814 0.1526 0.1866 0.0056  -0.0014 -0.0149 40  ASN   A ND2 
992  N N   . VAL   A 41  ? 0.1672 0.1290 0.1161 -0.0044 0.0237  0.0155  41  VAL   A N   
993  C CA  . VAL   A 41  ? 0.1703 0.1351 0.1303 -0.0020 0.0328  0.0138  41  VAL   A CA  
994  C C   . VAL   A 41  ? 0.1647 0.1338 0.1324 0.0008  0.0339  0.0151  41  VAL   A C   
995  O O   . VAL   A 41  ? 0.1671 0.1282 0.1665 0.0020  0.0309  0.0033  41  VAL   A O   
996  C CB  . VAL   A 41  ? 0.1882 0.1485 0.1553 -0.0080 0.0443  0.0086  41  VAL   A CB  
997  C CG1 . VAL   A 41  ? 0.2009 0.1501 0.1655 -0.0062 0.0372  -0.0028 41  VAL   A CG1 
998  C CG2 . VAL   A 41  ? 0.2081 0.1614 0.1539 -0.0169 0.0534  0.0110  41  VAL   A CG2 
1008 N N   . TYR   A 42  ? 0.1555 0.1259 0.1557 -0.0039 0.0315  0.0208  42  TYR   A N   
1009 C CA  . TYR   A 42  ? 0.1565 0.1230 0.1563 -0.0040 0.0309  0.0230  42  TYR   A CA  
1010 C C   . TYR   A 42  ? 0.1447 0.1256 0.1510 -0.0033 0.0294  0.0216  42  TYR   A C   
1011 O O   . TYR   A 42  ? 0.1460 0.1296 0.1693 -0.0161 0.0268  0.0060  42  TYR   A O   
1012 C CB  . TYR   A 42  ? 0.1777 0.1355 0.1585 -0.0069 0.0389  0.0164  42  TYR   A CB  
1013 C CG  . TYR   A 42  ? 0.1946 0.1469 0.1638 -0.0074 0.0357  0.0280  42  TYR   A CG  
1014 C CD1 . TYR   A 42  ? 0.2068 0.1583 0.1644 -0.0178 0.0383  0.0221  42  TYR   A CD1 
1015 C CD2 . TYR   A 42  ? 0.2094 0.1687 0.1759 -0.0075 0.0202  0.0160  42  TYR   A CD2 
1016 C CE1 . TYR   A 42  ? 0.2232 0.1731 0.1645 -0.0214 0.0412  0.0158  42  TYR   A CE1 
1017 C CE2 . TYR   A 42  ? 0.2219 0.1800 0.1901 -0.0236 0.0229  0.0164  42  TYR   A CE2 
1018 C CZ  . TYR   A 42  ? 0.2352 0.1843 0.1725 -0.0290 0.0401  0.0092  42  TYR   A CZ  
1019 O OH  . TYR   A 42  ? 0.2529 0.2076 0.1982 -0.0372 0.0366  0.0046  42  TYR   A OH  
1029 N N   . LEU   A 43  ? 0.1413 0.1269 0.1462 -0.0078 0.0223  0.0055  43  LEU   A N   
1030 C CA  . LEU   A 43  ? 0.1338 0.1297 0.1402 -0.0078 0.0161  0.0047  43  LEU   A CA  
1031 C C   . LEU   A 43  ? 0.1344 0.1325 0.1454 -0.0058 0.0118  0.0072  43  LEU   A C   
1032 O O   . LEU   A 43  ? 0.1526 0.1365 0.1600 -0.0047 -0.0015 0.0035  43  LEU   A O   
1033 C CB  . LEU   A 43  ? 0.1334 0.1254 0.1665 -0.0081 0.0173  0.0035  43  LEU   A CB  
1034 C CG  . LEU   A 43  ? 0.1426 0.1275 0.1729 -0.0070 0.0089  0.0076  43  LEU   A CG  
1035 C CD1 . LEU   A 43  ? 0.1484 0.1366 0.1884 -0.0023 0.0006  0.0142  43  LEU   A CD1 
1036 C CD2 . LEU   A 43  ? 0.1589 0.1299 0.1678 -0.0020 0.0159  0.0179  43  LEU   A CD2 
1048 N N   A LYS   A 44  ? 0.1389 0.1311 0.1377 -0.0050 0.0101  0.0083  44  LYS   A N   
1049 N N   B LYS   A 44  ? 0.1433 0.1369 0.1512 -0.0074 0.0090  0.0064  44  LYS   A N   
1050 C CA  A LYS   A 44  ? 0.1537 0.1413 0.1321 -0.0013 0.0138  0.0204  44  LYS   A CA  
1051 C CA  B LYS   A 44  ? 0.1586 0.1480 0.1641 -0.0054 0.0108  0.0108  44  LYS   A CA  
1052 C C   A LYS   A 44  ? 0.1458 0.1441 0.1126 0.0096  -0.0008 0.0194  44  LYS   A C   
1053 C C   B LYS   A 44  ? 0.1472 0.1433 0.1439 0.0012  0.0029  0.0138  44  LYS   A C   
1054 O O   A LYS   A 44  ? 0.1536 0.1591 0.1301 0.0065  0.0045  0.0000  44  LYS   A O   
1055 O O   B LYS   A 44  ? 0.1507 0.1478 0.1483 -0.0017 0.0042  0.0046  44  LYS   A O   
1056 C CB  A LYS   A 44  ? 0.1780 0.1513 0.1592 -0.0073 0.0204  0.0297  44  LYS   A CB  
1057 C CB  B LYS   A 44  ? 0.1860 0.1668 0.2058 -0.0083 0.0184  0.0130  44  LYS   A CB  
1058 C CG  A LYS   A 44  ? 0.2101 0.1778 0.2267 -0.0134 0.0307  0.0327  44  LYS   A CG  
1059 C CG  B LYS   A 44  ? 0.2135 0.1946 0.2667 -0.0115 0.0263  0.0199  44  LYS   A CG  
1060 C CD  A LYS   A 44  ? 0.2469 0.2270 0.3306 -0.0121 0.0257  0.0381  44  LYS   A CD  
1061 C CD  B LYS   A 44  ? 0.2385 0.2251 0.3320 -0.0139 0.0236  0.0260  44  LYS   A CD  
1062 C CE  A LYS   A 44  ? 0.2640 0.2502 0.3934 -0.0141 0.0224  0.0531  44  LYS   A CE  
1063 C CE  B LYS   A 44  ? 0.2520 0.2423 0.3746 -0.0154 0.0184  0.0367  44  LYS   A CE  
1064 N NZ  A LYS   A 44  ? 0.2679 0.2621 0.4086 -0.0159 0.0157  0.0627  44  LYS   A NZ  
1065 N NZ  B LYS   A 44  ? 0.2590 0.2496 0.3980 -0.0180 0.0144  0.0423  44  LYS   A NZ  
1092 N N   . HIS   A 45  ? 0.1338 0.1343 0.1371 0.0021  0.0001  0.0176  45  HIS   A N   
1093 C CA  . HIS   A 45  ? 0.1339 0.1362 0.1353 0.0032  -0.0061 0.0078  45  HIS   A CA  
1094 C C   . HIS   A 45  ? 0.1454 0.1502 0.1533 0.0105  0.0018  0.0132  45  HIS   A C   
1095 O O   . HIS   A 45  ? 0.1642 0.1567 0.1924 0.0230  -0.0073 -0.0076 45  HIS   A O   
1096 C CB  . HIS   A 45  ? 0.1334 0.1307 0.1306 -0.0020 0.0078  0.0012  45  HIS   A CB  
1097 C CG  . HIS   A 45  ? 0.1301 0.1315 0.1236 -0.0024 0.0087  0.0076  45  HIS   A CG  
1098 N ND1 . HIS   A 45  ? 0.1260 0.1382 0.1379 -0.0016 0.0028  0.0085  45  HIS   A ND1 
1099 C CD2 . HIS   A 45  ? 0.1324 0.1332 0.1463 -0.0075 -0.0031 0.0186  45  HIS   A CD2 
1100 C CE1 . HIS   A 45  ? 0.1288 0.1428 0.1234 -0.0024 -0.0066 0.0079  45  HIS   A CE1 
1101 N NE2 . HIS   A 45  ? 0.1299 0.1443 0.1360 0.0004  -0.0031 0.0222  45  HIS   A NE2 
1110 N N   A GLY   A 46  ? 0.1515 0.1492 0.1670 0.0065  -0.0128 0.0265  46  GLY   A N   
1111 N N   B GLY   A 46  ? 0.1475 0.1598 0.1652 0.0230  -0.0073 0.0181  46  GLY   A N   
1112 C CA  A GLY   A 46  ? 0.1518 0.1548 0.1824 0.0003  -0.0131 0.0319  46  GLY   A CA  
1113 C CA  B GLY   A 46  ? 0.1477 0.1614 0.1832 0.0188  -0.0161 0.0266  46  GLY   A CA  
1114 C C   A GLY   A 46  ? 0.1535 0.1494 0.1893 0.0068  -0.0182 0.0344  46  GLY   A C   
1115 C C   B GLY   A 46  ? 0.1445 0.1481 0.1799 0.0195  -0.0236 0.0399  46  GLY   A C   
1116 O O   A GLY   A 46  ? 0.1576 0.1554 0.2239 0.0080  -0.0209 0.0194  46  GLY   A O   
1117 O O   B GLY   A 46  ? 0.1429 0.1370 0.2108 0.0170  -0.0234 0.0507  46  GLY   A O   
1124 N N   A GLY   A 47  ? 0.1569 0.1505 0.1861 0.0055  -0.0201 0.0145  47  GLY   A N   
1125 N N   B GLY   A 47  ? 0.1391 0.1424 0.1618 0.0186  -0.0270 0.0254  47  GLY   A N   
1126 C CA  A GLY   A 47  ? 0.1533 0.1541 0.1896 0.0025  -0.0380 -0.0004 47  GLY   A CA  
1127 C CA  B GLY   A 47  ? 0.1404 0.1410 0.1705 0.0173  -0.0344 0.0084  47  GLY   A CA  
1128 C C   A GLY   A 47  ? 0.1465 0.1472 0.1710 0.0046  -0.0368 -0.0052 47  GLY   A C   
1129 C C   B GLY   A 47  ? 0.1364 0.1414 0.1652 0.0173  -0.0285 -0.0012 47  GLY   A C   
1130 O O   A GLY   A 47  ? 0.1384 0.1413 0.1728 0.0111  -0.0370 0.0089  47  GLY   A O   
1131 O O   B GLY   A 47  ? 0.1385 0.1406 0.1740 0.0243  -0.0154 0.0041  47  GLY   A O   
1138 N N   A GLY   A 48  ? 0.1437 0.1561 0.1614 0.0031  -0.0442 -0.0076 48  GLY   A N   
1139 N N   B GLY   A 48  ? 0.1348 0.1502 0.1704 0.0122  -0.0300 -0.0092 48  GLY   A N   
1140 C CA  A GLY   A 48  ? 0.1356 0.1472 0.1773 -0.0030 -0.0303 -0.0102 48  GLY   A CA  
1141 C CA  B GLY   A 48  ? 0.1306 0.1542 0.1775 0.0058  -0.0238 -0.0089 48  GLY   A CA  
1142 C C   A GLY   A 48  ? 0.1295 0.1494 0.1487 -0.0010 -0.0115 -0.0122 48  GLY   A C   
1143 C C   B GLY   A 48  ? 0.1268 0.1608 0.1649 0.0098  -0.0066 -0.0046 48  GLY   A C   
1144 O O   A GLY   A 48  ? 0.1398 0.1468 0.1698 0.0097  -0.0152 -0.0166 48  GLY   A O   
1145 O O   B GLY   A 48  ? 0.1308 0.1700 0.1825 0.0136  -0.0129 -0.0055 48  GLY   A O   
1152 N N   A VAL   A 49  ? 0.1226 0.1450 0.1375 -0.0073 0.0035  -0.0090 49  VAL   A N   
1153 N N   B VAL   A 49  ? 0.1278 0.1512 0.1613 0.0032  0.0049  0.0055  49  VAL   A N   
1154 C CA  A VAL   A 49  ? 0.1442 0.1482 0.1436 -0.0129 0.0164  -0.0098 49  VAL   A CA  
1155 C CA  B VAL   A 49  ? 0.1290 0.1457 0.1526 0.0027  0.0076  0.0105  49  VAL   A CA  
1156 C C   A VAL   A 49  ? 0.1347 0.1318 0.1179 -0.0026 0.0138  -0.0000 49  VAL   A C   
1157 C C   B VAL   A 49  ? 0.1268 0.1303 0.1267 0.0025  0.0094  0.0049  49  VAL   A C   
1158 O O   A VAL   A 49  ? 0.1475 0.1346 0.1293 -0.0089 0.0197  -0.0044 49  VAL   A O   
1159 O O   B VAL   A 49  ? 0.1301 0.1312 0.1276 0.0025  0.0089  0.0033  49  VAL   A O   
1160 C CB  A VAL   A 49  ? 0.1697 0.1493 0.1527 -0.0265 0.0136  -0.0015 49  VAL   A CB  
1161 C CB  B VAL   A 49  ? 0.1236 0.1422 0.1490 0.0062  0.0131  0.0256  49  VAL   A CB  
1162 C CG1 A VAL   A 49  ? 0.1746 0.1421 0.1602 -0.0067 0.0185  0.0024  49  VAL   A CG1 
1163 C CG1 B VAL   A 49  ? 0.1215 0.1462 0.1485 0.0151  0.0205  0.0313  49  VAL   A CG1 
1164 C CG2 A VAL   A 49  ? 0.1791 0.1598 0.2111 -0.0419 0.0172  -0.0044 49  VAL   A CG2 
1165 C CG2 B VAL   A 49  ? 0.1325 0.1454 0.1458 0.0107  0.0264  0.0222  49  VAL   A CG2 
1184 N N   A ALA   A 50  ? 0.1241 0.1289 0.1119 -0.0054 -0.0020 0.0043  50  ALA   A N   
1185 N N   B ALA   A 50  ? 0.1290 0.1253 0.1206 0.0007  -0.0008 0.0012  50  ALA   A N   
1186 C CA  A ALA   A 50  ? 0.1165 0.1274 0.1252 -0.0091 -0.0024 0.0060  50  ALA   A CA  
1187 C CA  B ALA   A 50  ? 0.1278 0.1194 0.1269 -0.0041 -0.0183 0.0062  50  ALA   A CA  
1188 C C   A ALA   A 50  ? 0.1214 0.1272 0.1168 -0.0096 0.0050  0.0030  50  ALA   A C   
1189 C C   B ALA   A 50  ? 0.1281 0.1195 0.1156 -0.0006 -0.0132 0.0008  50  ALA   A C   
1190 O O   A ALA   A 50  ? 0.1237 0.1349 0.1313 -0.0062 0.0029  0.0021  50  ALA   A O   
1191 O O   B ALA   A 50  ? 0.1309 0.1251 0.1239 0.0049  -0.0059 -0.0008 50  ALA   A O   
1192 C CB  A ALA   A 50  ? 0.1143 0.1307 0.1130 -0.0048 -0.0035 -0.0091 50  ALA   A CB  
1193 C CB  B ALA   A 50  ? 0.1314 0.1132 0.1387 -0.0054 -0.0209 0.0135  50  ALA   A CB  
1204 N N   A GLY   A 51  ? 0.1284 0.1229 0.1307 -0.0020 -0.0033 0.0111  51  GLY   A N   
1205 N N   B GLY   A 51  ? 0.1239 0.1224 0.1224 0.0030  -0.0201 0.0002  51  GLY   A N   
1206 C CA  A GLY   A 51  ? 0.1447 0.1186 0.1441 -0.0031 -0.0065 0.0096  51  GLY   A CA  
1207 C CA  B GLY   A 51  ? 0.1222 0.1192 0.1127 0.0023  -0.0121 0.0022  51  GLY   A CA  
1208 C C   A GLY   A 51  ? 0.1440 0.1234 0.1467 -0.0003 -0.0016 -0.0019 51  GLY   A C   
1209 C C   B GLY   A 51  ? 0.1194 0.1164 0.1142 0.0087  -0.0009 0.0048  51  GLY   A C   
1210 O O   A GLY   A 51  ? 0.1549 0.1311 0.1552 -0.0070 -0.0061 -0.0047 51  GLY   A O   
1211 O O   B GLY   A 51  ? 0.1180 0.1215 0.1230 0.0075  -0.0023 0.0053  51  GLY   A O   
1218 N N   A ALA   A 52  ? 0.1417 0.1318 0.1328 -0.0008 0.0021  -0.0014 52  ALA   A N   
1219 N N   B ALA   A 52  ? 0.1238 0.1154 0.1121 0.0096  0.0018  -0.0061 52  ALA   A N   
1220 C CA  A ALA   A 52  ? 0.1360 0.1331 0.1433 -0.0006 -0.0024 -0.0033 52  ALA   A CA  
1221 C CA  B ALA   A 52  ? 0.1258 0.1153 0.1232 0.0033  0.0005  0.0030  52  ALA   A CA  
1222 C C   A ALA   A 52  ? 0.1257 0.1376 0.1320 -0.0021 0.0067  -0.0053 52  ALA   A C   
1223 C C   B ALA   A 52  ? 0.1352 0.1193 0.1172 -0.0007 0.0055  -0.0023 52  ALA   A C   
1224 O O   A ALA   A 52  ? 0.1348 0.1440 0.1440 0.0024  0.0072  -0.0095 52  ALA   A O   
1225 O O   B ALA   A 52  ? 0.1476 0.1326 0.1390 0.0013  0.0042  -0.0050 52  ALA   A O   
1226 C CB  A ALA   A 52  ? 0.1384 0.1440 0.1769 0.0004  -0.0056 0.0135  52  ALA   A CB  
1227 C CB  B ALA   A 52  ? 0.1226 0.1179 0.1352 -0.0029 -0.0019 0.0269  52  ALA   A CB  
1238 N N   A LEU   A 53  ? 0.1232 0.1373 0.1290 0.0017  -0.0004 -0.0038 53  LEU   A N   
1239 N N   B LEU   A 53  ? 0.1355 0.1150 0.1149 -0.0063 0.0016  0.0004  53  LEU   A N   
1240 C CA  A LEU   A 53  ? 0.1304 0.1424 0.1231 0.0041  0.0073  -0.0010 53  LEU   A CA  
1241 C CA  B LEU   A 53  ? 0.1429 0.1289 0.1261 -0.0054 0.0055  0.0033  53  LEU   A CA  
1242 C C   A LEU   A 53  ? 0.1327 0.1481 0.1131 0.0087  0.0141  -0.0006 53  LEU   A C   
1243 C C   B LEU   A 53  ? 0.1402 0.1347 0.1199 0.0031  -0.0018 0.0044  53  LEU   A C   
1244 O O   A LEU   A 53  ? 0.1375 0.1584 0.1283 -0.0032 0.0103  -0.0044 53  LEU   A O   
1245 O O   B LEU   A 53  ? 0.1438 0.1344 0.1213 0.0057  -0.0082 -0.0000 53  LEU   A O   
1246 C CB  A LEU   A 53  ? 0.1314 0.1431 0.1344 0.0031  0.0029  0.0016  53  LEU   A CB  
1247 C CB  B LEU   A 53  ? 0.1471 0.1350 0.1367 -0.0054 0.0067  0.0093  53  LEU   A CB  
1248 C CG  A LEU   A 53  ? 0.1457 0.1459 0.1382 -0.0018 0.0086  -0.0010 53  LEU   A CG  
1249 C CG  B LEU   A 53  ? 0.1499 0.1371 0.1304 -0.0075 0.0127  0.0051  53  LEU   A CG  
1250 C CD1 A LEU   A 53  ? 0.1611 0.1592 0.1551 -0.0011 0.0044  0.0008  53  LEU   A CD1 
1251 C CD1 B LEU   A 53  ? 0.1496 0.1419 0.1218 0.0020  0.0115  -0.0015 53  LEU   A CD1 
1252 C CD2 A LEU   A 53  ? 0.1681 0.1493 0.1424 -0.0057 0.0208  -0.0103 53  LEU   A CD2 
1253 C CD2 B LEU   A 53  ? 0.1594 0.1463 0.1520 -0.0147 0.0182  0.0068  53  LEU   A CD2 
1276 N N   A ASN   A 54  ? 0.1256 0.1415 0.1104 -0.0015 0.0030  0.0080  54  ASN   A N   
1277 N N   B ASN   A 54  ? 0.1361 0.1352 0.1215 -0.0013 -0.0025 0.0025  54  ASN   A N   
1278 C CA  A ASN   A 54  ? 0.1246 0.1389 0.1315 -0.0043 -0.0085 0.0022  54  ASN   A CA  
1279 C CA  B ASN   A 54  ? 0.1367 0.1374 0.1306 -0.0043 -0.0019 -0.0087 54  ASN   A CA  
1280 C C   A ASN   A 54  ? 0.1342 0.1406 0.1258 -0.0094 -0.0019 0.0048  54  ASN   A C   
1281 C C   B ASN   A 54  ? 0.1380 0.1381 0.1397 -0.0095 -0.0003 -0.0059 54  ASN   A C   
1282 O O   A ASN   A 54  ? 0.1345 0.1492 0.1169 -0.0092 -0.0004 -0.0034 54  ASN   A O   
1283 O O   B ASN   A 54  ? 0.1392 0.1391 0.1473 -0.0133 -0.0026 -0.0136 54  ASN   A O   
1284 C CB  A ASN   A 54  ? 0.1217 0.1347 0.1398 -0.0060 -0.0104 0.0118  54  ASN   A CB  
1285 C CB  B ASN   A 54  ? 0.1422 0.1386 0.1228 -0.0020 0.0043  -0.0144 54  ASN   A CB  
1286 C CG  A ASN   A 54  ? 0.1224 0.1370 0.1442 -0.0035 0.0014  0.0043  54  ASN   A CG  
1287 C CG  B ASN   A 54  ? 0.1436 0.1419 0.1137 0.0000  0.0077  -0.0265 54  ASN   A CG  
1288 O OD1 A ASN   A 54  ? 0.1171 0.1437 0.1550 -0.0083 -0.0018 0.0115  54  ASN   A OD1 
1289 O OD1 B ASN   A 54  ? 0.1389 0.1381 0.0799 0.0072  0.0062  -0.0341 54  ASN   A OD1 
1290 N ND2 A ASN   A 54  ? 0.1152 0.1315 0.1392 -0.0045 0.0020  0.0082  54  ASN   A ND2 
1291 N ND2 B ASN   A 54  ? 0.1425 0.1480 0.1398 -0.0057 0.0072  -0.0226 54  ASN   A ND2 
1304 N N   . LYS   A 55  ? 0.1369 0.1404 0.1395 -0.0042 0.0000  -0.0057 55  LYS   A N   
1305 C CA  . LYS   A 55  ? 0.1456 0.1503 0.1518 0.0093  -0.0047 -0.0171 55  LYS   A CA  
1306 C C   . LYS   A 55  ? 0.1457 0.1521 0.1598 -0.0005 0.0068  -0.0249 55  LYS   A C   
1307 O O   . LYS   A 55  ? 0.1569 0.1627 0.1569 0.0024  0.0014  -0.0252 55  LYS   A O   
1308 C CB  . LYS   A 55  ? 0.1537 0.1592 0.1769 0.0228  -0.0064 -0.0212 55  LYS   A CB  
1309 C CG  . LYS   A 55  ? 0.1703 0.1901 0.2036 0.0292  -0.0178 -0.0275 55  LYS   A CG  
1310 C CD  . LYS   A 55  ? 0.1866 0.2192 0.2136 0.0387  -0.0147 -0.0258 55  LYS   A CD  
1311 C CE  . LYS   A 55  ? 0.2122 0.2605 0.2268 0.0484  -0.0297 -0.0266 55  LYS   A CE  
1312 N NZ  . LYS   A 55  ? 0.2230 0.2918 0.2001 0.0650  -0.0435 -0.0201 55  LYS   A NZ  
1327 N N   . ALA   A 56  ? 0.1508 0.1596 0.1537 -0.0103 0.0087  -0.0240 56  ALA   A N   
1328 C CA  . ALA   A 56  ? 0.1590 0.1825 0.1436 -0.0146 0.0137  -0.0213 56  ALA   A CA  
1329 C C   . ALA   A 56  ? 0.1635 0.1924 0.1249 -0.0129 0.0101  -0.0239 56  ALA   A C   
1330 O O   . ALA   A 56  ? 0.1650 0.2189 0.1413 -0.0008 0.0137  -0.0189 56  ALA   A O   
1331 C CB  . ALA   A 56  ? 0.1588 0.1996 0.1509 -0.0215 0.0106  -0.0148 56  ALA   A CB  
1337 N N   . THR   A 57  ? 0.1502 0.1722 0.1228 -0.0132 0.0089  -0.0198 57  THR   A N   
1338 C CA  . THR   A 57  ? 0.1536 0.1668 0.1259 -0.0106 0.0035  -0.0121 57  THR   A CA  
1339 C C   . THR   A 57  ? 0.1527 0.1753 0.1340 -0.0065 -0.0020 -0.0218 57  THR   A C   
1340 O O   . THR   A 57  ? 0.1452 0.1803 0.1618 -0.0111 -0.0135 -0.0284 57  THR   A O   
1341 C CB  . THR   A 57  ? 0.1539 0.1728 0.1257 -0.0055 -0.0004 -0.0143 57  THR   A CB  
1342 O OG1 . THR   A 57  ? 0.1410 0.1683 0.1280 -0.0062 0.0028  -0.0116 57  THR   A OG1 
1343 C CG2 . THR   A 57  ? 0.1589 0.1663 0.1247 -0.0116 0.0074  -0.0032 57  THR   A CG2 
1351 N N   . ASN   A 58  ? 0.1519 0.1726 0.1514 -0.0080 0.0087  -0.0331 58  ASN   A N   
1352 C CA  . ASN   A 58  ? 0.1769 0.1650 0.1761 -0.0135 0.0132  -0.0381 58  ASN   A CA  
1353 C C   . ASN   A 58  ? 0.1541 0.1532 0.1757 0.0002  -0.0034 -0.0288 58  ASN   A C   
1354 O O   . ASN   A 58  ? 0.1511 0.1591 0.1934 -0.0127 -0.0043 -0.0337 58  ASN   A O   
1355 C CB  . ASN   A 58  ? 0.2257 0.1850 0.2120 -0.0285 0.0382  -0.0499 58  ASN   A CB  
1356 C CG  . ASN   A 58  ? 0.2819 0.2122 0.2968 -0.0295 0.0466  -0.0431 58  ASN   A CG  
1357 O OD1 . ASN   A 58  ? 0.3081 0.2026 0.3437 0.0065  0.0931  -0.0245 58  ASN   A OD1 
1358 N ND2 . ASN   A 58  ? 0.3052 0.2357 0.3376 -0.0385 0.0300  -0.0632 58  ASN   A ND2 
1365 N N   . ASN   A 59  ? 0.1334 0.1410 0.1694 -0.0057 -0.0100 -0.0203 59  ASN   A N   
1366 C CA  . ASN   A 59  ? 0.1329 0.1360 0.1625 -0.0042 -0.0014 -0.0154 59  ASN   A CA  
1367 C C   . ASN   A 59  ? 0.1367 0.1378 0.1403 -0.0038 -0.0055 -0.0115 59  ASN   A C   
1368 O O   . ASN   A 59  ? 0.1415 0.1415 0.1436 -0.0082 0.0002  0.0025  59  ASN   A O   
1369 C CB  . ASN   A 59  ? 0.1407 0.1326 0.1671 -0.0027 -0.0127 -0.0251 59  ASN   A CB  
1370 C CG  . ASN   A 59  ? 0.1467 0.1415 0.1718 -0.0032 -0.0227 -0.0038 59  ASN   A CG  
1371 O OD1 . ASN   A 59  ? 0.1665 0.1479 0.1550 -0.0131 -0.0166 -0.0027 59  ASN   A OD1 
1372 N ND2 . ASN   A 59  ? 0.1531 0.1463 0.1742 -0.0123 -0.0157 0.0025  59  ASN   A ND2 
1379 N N   . ALA   A 60  ? 0.1322 0.1508 0.1438 -0.0042 -0.0035 -0.0058 60  ALA   A N   
1380 C CA  . ALA   A 60  ? 0.1331 0.1462 0.1521 -0.0066 -0.0080 -0.0055 60  ALA   A CA  
1381 C C   . ALA   A 60  ? 0.1356 0.1386 0.1504 -0.0089 0.0008  -0.0067 60  ALA   A C   
1382 O O   . ALA   A 60  ? 0.1299 0.1408 0.1718 -0.0045 -0.0066 -0.0103 60  ALA   A O   
1383 C CB  . ALA   A 60  ? 0.1483 0.1561 0.1586 -0.0040 -0.0198 -0.0218 60  ALA   A CB  
1389 N N   . MET   A 61  ? 0.1304 0.1367 0.1454 -0.0069 -0.0030 -0.0059 61  MET   A N   
1390 C CA  . MET   A 61  ? 0.1303 0.1345 0.1511 -0.0090 0.0035  -0.0036 61  MET   A CA  
1391 C C   . MET   A 61  ? 0.1285 0.1293 0.1497 -0.0067 -0.0040 -0.0052 61  MET   A C   
1392 O O   . MET   A 61  ? 0.1297 0.1304 0.1552 -0.0044 0.0057  -0.0030 61  MET   A O   
1393 C CB  . MET   A 61  ? 0.1324 0.1323 0.1384 -0.0033 0.0050  -0.0063 61  MET   A CB  
1394 C CG  . MET   A 61  ? 0.1391 0.1416 0.1487 -0.0050 0.0027  -0.0031 61  MET   A CG  
1395 S SD  . MET   A 61  ? 0.1380 0.1414 0.1909 -0.0119 0.0003  -0.0195 61  MET   A SD  
1396 C CE  . MET   A 61  ? 0.1591 0.1537 0.1995 -0.0159 0.0098  -0.0100 61  MET   A CE  
1406 N N   . GLN   A 62  ? 0.1329 0.1260 0.1511 -0.0080 -0.0045 -0.0024 62  GLN   A N   
1407 C CA  . GLN   A 62  ? 0.1354 0.1204 0.1456 -0.0030 0.0038  -0.0023 62  GLN   A CA  
1408 C C   . GLN   A 62  ? 0.1377 0.1219 0.1495 -0.0012 0.0117  0.0015  62  GLN   A C   
1409 O O   . GLN   A 62  ? 0.1404 0.1325 0.1473 -0.0062 0.0060  -0.0023 62  GLN   A O   
1410 C CB  . GLN   A 62  ? 0.1346 0.1258 0.1489 -0.0057 -0.0012 -0.0008 62  GLN   A CB  
1411 C CG  . GLN   A 62  ? 0.1402 0.1279 0.1456 -0.0036 -0.0027 0.0092  62  GLN   A CG  
1412 C CD  . GLN   A 62  ? 0.1453 0.1299 0.1492 -0.0072 0.0082  0.0039  62  GLN   A CD  
1413 O OE1 . GLN   A 62  ? 0.1520 0.1401 0.1534 -0.0038 0.0024  0.0017  62  GLN   A OE1 
1414 N NE2 . GLN   A 62  ? 0.1527 0.1336 0.1559 0.0014  0.0050  -0.0069 62  GLN   A NE2 
1423 N N   . VAL   A 63  ? 0.1306 0.1309 0.1686 -0.0094 0.0158  -0.0195 63  VAL   A N   
1424 C CA  . VAL   A 63  ? 0.1305 0.1381 0.1807 -0.0132 0.0103  -0.0208 63  VAL   A CA  
1425 C C   . VAL   A 63  ? 0.1239 0.1380 0.1724 -0.0102 -0.0015 -0.0147 63  VAL   A C   
1426 O O   . VAL   A 63  ? 0.1267 0.1404 0.1883 -0.0184 -0.0004 -0.0122 63  VAL   A O   
1427 C CB  . VAL   A 63  ? 0.1445 0.1569 0.2214 -0.0116 -0.0015 -0.0440 63  VAL   A CB  
1428 C CG1 . VAL   A 63  ? 0.1610 0.1740 0.2480 -0.0135 -0.0089 -0.0632 63  VAL   A CG1 
1429 C CG2 . VAL   A 63  ? 0.1543 0.1484 0.2250 -0.0078 0.0177  -0.0417 63  VAL   A CG2 
1439 N N   . GLU   A 64  ? 0.1278 0.1433 0.1623 -0.0057 0.0024  -0.0095 64  GLU   A N   
1440 C CA  . GLU   A 64  ? 0.1292 0.1400 0.1666 -0.0104 -0.0067 -0.0012 64  GLU   A CA  
1441 C C   . GLU   A 64  ? 0.1208 0.1374 0.1706 -0.0085 0.0022  0.0051  64  GLU   A C   
1442 O O   . GLU   A 64  ? 0.1283 0.1417 0.1844 -0.0041 0.0010  -0.0016 64  GLU   A O   
1443 C CB  . GLU   A 64  ? 0.1387 0.1463 0.1717 -0.0090 0.0030  -0.0080 64  GLU   A CB  
1444 C CG  . GLU   A 64  ? 0.1446 0.1516 0.1921 -0.0101 0.0066  -0.0028 64  GLU   A CG  
1445 C CD  . GLU   A 64  ? 0.1548 0.1633 0.1930 -0.0240 0.0117  -0.0039 64  GLU   A CD  
1446 O OE1 . GLU   A 64  ? 0.1511 0.1752 0.1950 -0.0244 0.0121  -0.0074 64  GLU   A OE1 
1447 O OE2 . GLU   A 64  ? 0.1770 0.1670 0.1778 -0.0332 -0.0036 0.0004  64  GLU   A OE2 
1454 N N   . SER   A 65  ? 0.1187 0.1380 0.1537 -0.0018 -0.0007 0.0030  65  SER   A N   
1455 C CA  . SER   A 65  ? 0.1289 0.1327 0.1481 -0.0023 0.0009  0.0007  65  SER   A CA  
1456 C C   . SER   A 65  ? 0.1340 0.1425 0.1451 -0.0072 0.0039  -0.0052 65  SER   A C   
1457 O O   . SER   A 65  ? 0.1402 0.1493 0.1720 -0.0039 0.0129  -0.0126 65  SER   A O   
1458 C CB  . SER   A 65  ? 0.1313 0.1349 0.1450 -0.0054 0.0071  0.0051  65  SER   A CB  
1459 O OG  . SER   A 65  ? 0.1298 0.1464 0.1515 -0.0139 0.0007  0.0116  65  SER   A OG  
1465 N N   . ASP   A 66  ? 0.1344 0.1338 0.1602 -0.0070 0.0181  -0.0028 66  ASP   A N   
1466 C CA  . ASP   A 66  ? 0.1417 0.1465 0.1733 -0.0047 0.0117  0.0115  66  ASP   A CA  
1467 C C   . ASP   A 66  ? 0.1391 0.1397 0.1724 -0.0071 0.0157  0.0131  66  ASP   A C   
1468 O O   . ASP   A 66  ? 0.1457 0.1519 0.1918 -0.0041 0.0249  0.0155  66  ASP   A O   
1469 C CB  . ASP   A 66  ? 0.1496 0.1551 0.2135 0.0034  0.0142  0.0326  66  ASP   A CB  
1470 C CG  . ASP   A 66  ? 0.1757 0.1704 0.2633 -0.0010 0.0045  0.0577  66  ASP   A CG  
1471 O OD1 . ASP   A 66  ? 0.1773 0.2008 0.2338 -0.0125 -0.0012 0.0594  66  ASP   A OD1 
1472 O OD2 . ASP   A 66  ? 0.1918 0.1865 0.3648 0.0183  -0.0135 0.0336  66  ASP   A OD2 
1477 N N   . ASP   A 67  ? 0.1308 0.1439 0.1839 -0.0008 0.0100  0.0148  67  ASP   A N   
1478 C CA  . ASP   A 67  ? 0.1327 0.1564 0.2103 -0.0058 0.0079  0.0176  67  ASP   A CA  
1479 C C   . ASP   A 67  ? 0.1346 0.1533 0.1985 -0.0028 0.0116  0.0125  67  ASP   A C   
1480 O O   . ASP   A 67  ? 0.1323 0.1606 0.2207 -0.0028 0.0232  0.0169  67  ASP   A O   
1481 C CB  . ASP   A 67  ? 0.1431 0.1677 0.2375 -0.0105 -0.0133 0.0229  67  ASP   A CB  
1482 C CG  . ASP   A 67  ? 0.1415 0.1793 0.2741 -0.0064 -0.0261 0.0295  67  ASP   A CG  
1483 O OD1 . ASP   A 67  ? 0.1479 0.1922 0.3557 -0.0128 -0.0306 0.0380  67  ASP   A OD1 
1484 O OD2 . ASP   A 67  ? 0.1415 0.1813 0.2547 0.0012  -0.0179 0.0198  67  ASP   A OD2 
1489 N N   . TYR   A 68  ? 0.1368 0.1434 0.1935 -0.0009 0.0214  0.0148  68  TYR   A N   
1490 C CA  . TYR   A 68  ? 0.1482 0.1434 0.1849 -0.0024 0.0227  0.0160  68  TYR   A CA  
1491 C C   . TYR   A 68  ? 0.1378 0.1434 0.1876 -0.0018 0.0234  0.0077  68  TYR   A C   
1492 O O   . TYR   A 68  ? 0.1451 0.1457 0.2050 0.0057  0.0302  0.0033  68  TYR   A O   
1493 C CB  . TYR   A 68  ? 0.1492 0.1378 0.1911 0.0045  0.0391  0.0204  68  TYR   A CB  
1494 C CG  . TYR   A 68  ? 0.1597 0.1551 0.2330 -0.0048 0.0576  0.0244  68  TYR   A CG  
1495 C CD1 . TYR   A 68  ? 0.1728 0.1647 0.2806 -0.0230 0.0538  -0.0223 68  TYR   A CD1 
1496 C CD2 . TYR   A 68  ? 0.1802 0.1598 0.2830 0.0007  0.0679  0.0191  68  TYR   A CD2 
1497 C CE1 . TYR   A 68  ? 0.1803 0.1772 0.3136 -0.0262 0.0590  -0.0280 68  TYR   A CE1 
1498 C CE2 . TYR   A 68  ? 0.1843 0.1662 0.3147 -0.0088 0.0769  -0.0070 68  TYR   A CE2 
1499 C CZ  . TYR   A 68  ? 0.1841 0.1692 0.3348 -0.0278 0.0582  -0.0330 68  TYR   A CZ  
1500 O OH  . TYR   A 68  ? 0.2075 0.1721 0.3643 -0.0234 0.0353  -0.0495 68  TYR   A OH  
1510 N N   . ILE   A 69  ? 0.1326 0.1357 0.1928 -0.0034 0.0262  0.0110  69  ILE   A N   
1511 C CA  . ILE   A 69  ? 0.1442 0.1446 0.1839 -0.0020 0.0291  0.0027  69  ILE   A CA  
1512 C C   . ILE   A 69  ? 0.1470 0.1471 0.1794 0.0005  0.0305  0.0098  69  ILE   A C   
1513 O O   . ILE   A 69  ? 0.1547 0.1547 0.1797 -0.0081 0.0323  0.0137  69  ILE   A O   
1514 C CB  . ILE   A 69  ? 0.1552 0.1692 0.1822 0.0011  0.0221  -0.0026 69  ILE   A CB  
1515 C CG1 . ILE   A 69  ? 0.1552 0.1781 0.1857 0.0059  0.0224  -0.0114 69  ILE   A CG1 
1516 C CG2 . ILE   A 69  ? 0.1718 0.1898 0.2208 0.0123  0.0091  -0.0124 69  ILE   A CG2 
1517 C CD1 . ILE   A 69  ? 0.1533 0.1869 0.2007 -0.0063 0.0290  -0.0168 69  ILE   A CD1 
1529 N N   . ALA   A 70  ? 0.1536 0.1472 0.1993 -0.0098 0.0325  0.0025  70  ALA   A N   
1530 C CA  . ALA   A 70  ? 0.1594 0.1560 0.2289 -0.0211 0.0484  0.0016  70  ALA   A CA  
1531 C C   . ALA   A 70  ? 0.1576 0.1713 0.2336 -0.0135 0.0457  -0.0017 70  ALA   A C   
1532 O O   . ALA   A 70  ? 0.1744 0.2075 0.2417 0.0017  0.0584  0.0171  70  ALA   A O   
1533 C CB  . ALA   A 70  ? 0.1640 0.1522 0.2440 -0.0249 0.0370  0.0054  70  ALA   A CB  
1539 N N   . THR   A 71  ? 0.1530 0.1710 0.2129 -0.0050 0.0334  0.0102  71  THR   A N   
1540 C CA  . THR   A 71  ? 0.1560 0.1860 0.2368 0.0023  0.0244  0.0182  71  THR   A CA  
1541 C C   . THR   A 71  ? 0.1461 0.1788 0.2646 0.0078  0.0377  0.0052  71  THR   A C   
1542 O O   . THR   A 71  ? 0.1495 0.2009 0.3142 0.0022  0.0507  -0.0263 71  THR   A O   
1543 C CB  . THR   A 71  ? 0.1819 0.2113 0.2693 0.0111  -0.0160 0.0283  71  THR   A CB  
1544 O OG1 . THR   A 71  ? 0.2033 0.2263 0.2874 0.0024  -0.0286 0.0110  71  THR   A OG1 
1545 C CG2 . THR   A 71  ? 0.2019 0.2345 0.2964 0.0196  -0.0318 0.0497  71  THR   A CG2 
1553 N N   . ASN   A 72  ? 0.1464 0.1609 0.2394 0.0075  0.0330  0.0175  72  ASN   A N   
1554 C CA  . ASN   A 72  ? 0.1555 0.1576 0.2297 0.0085  0.0458  0.0133  72  ASN   A CA  
1555 C C   . ASN   A 72  ? 0.1719 0.1607 0.2193 0.0053  0.0589  -0.0007 72  ASN   A C   
1556 O O   . ASN   A 72  ? 0.1845 0.1616 0.2613 0.0077  0.0556  -0.0086 72  ASN   A O   
1557 C CB  . ASN   A 72  ? 0.1756 0.1670 0.2306 0.0158  0.0442  0.0035  72  ASN   A CB  
1558 C CG  . ASN   A 72  ? 0.1976 0.1827 0.2420 0.0231  0.0328  0.0171  72  ASN   A CG  
1559 O OD1 . ASN   A 72  ? 0.2146 0.2094 0.2540 0.0233  0.0359  0.0329  72  ASN   A OD1 
1560 N ND2 . ASN   A 72  ? 0.2123 0.1834 0.2440 0.0526  0.0234  0.0147  72  ASN   A ND2 
1567 N N   . GLY   A 73  ? 0.1734 0.1616 0.1939 0.0063  0.0516  0.0012  73  GLY   A N   
1568 C CA  . GLY   A 73  ? 0.1776 0.1597 0.1954 -0.0008 0.0502  0.0132  73  GLY   A CA  
1569 C C   . GLY   A 73  ? 0.1762 0.1501 0.1744 0.0023  0.0553  0.0213  73  GLY   A C   
1570 O O   . GLY   A 73  ? 0.1710 0.1583 0.1904 0.0097  0.0399  0.0205  73  GLY   A O   
1574 N N   . PRO   A 74  ? 0.1843 0.1544 0.1815 -0.0094 0.0562  0.0116  74  PRO   A N   
1575 C CA  . PRO   A 74  ? 0.1831 0.1518 0.1883 -0.0026 0.0490  0.0147  74  PRO   A CA  
1576 C C   . PRO   A 74  ? 0.1732 0.1375 0.1882 -0.0026 0.0311  0.0047  74  PRO   A C   
1577 O O   . PRO   A 74  ? 0.1826 0.1389 0.2054 -0.0051 0.0403  -0.0128 74  PRO   A O   
1578 C CB  . PRO   A 74  ? 0.1943 0.1851 0.2120 0.0003  0.0597  0.0315  74  PRO   A CB  
1579 C CG  . PRO   A 74  ? 0.2183 0.2230 0.2674 -0.0127 0.0461  0.0194  74  PRO   A CG  
1580 C CD  . PRO   A 74  ? 0.2012 0.1957 0.2082 -0.0146 0.0482  0.0037  74  PRO   A CD  
1588 N N   . LEU   A 75  ? 0.1695 0.1265 0.1619 -0.0015 0.0260  -0.0020 75  LEU   A N   
1589 C CA  . LEU   A 75  ? 0.1720 0.1292 0.1467 -0.0019 0.0158  0.0035  75  LEU   A CA  
1590 C C   . LEU   A 75  ? 0.1824 0.1424 0.1451 0.0026  0.0188  0.0112  75  LEU   A C   
1591 O O   . LEU   A 75  ? 0.2074 0.1573 0.1507 0.0087  0.0144  0.0063  75  LEU   A O   
1592 C CB  . LEU   A 75  ? 0.1738 0.1409 0.1418 -0.0128 0.0171  0.0164  75  LEU   A CB  
1593 C CG  . LEU   A 75  ? 0.1873 0.1794 0.1561 -0.0395 0.0190  -0.0014 75  LEU   A CG  
1594 C CD1 . LEU   A 75  ? 0.2011 0.2304 0.1870 -0.0467 0.0196  -0.0201 75  LEU   A CD1 
1595 C CD2 . LEU   A 75  ? 0.2130 0.2182 0.2318 -0.0182 0.0207  -0.0103 75  LEU   A CD2 
1607 N N   . LYS   A 76  ? 0.1774 0.1398 0.1516 -0.0043 0.0104  0.0014  76  LYS   A N   
1608 C CA  . LYS   A 76  ? 0.1702 0.1586 0.1483 -0.0020 0.0115  -0.0117 76  LYS   A CA  
1609 C C   . LYS   A 76  ? 0.1673 0.1435 0.1251 0.0034  0.0113  0.0066  76  LYS   A C   
1610 O O   . LYS   A 76  ? 0.1739 0.1380 0.1380 -0.0004 0.0085  0.0088  76  LYS   A O   
1611 C CB  . LYS   A 76  ? 0.1750 0.1886 0.2064 0.0045  0.0135  -0.0434 76  LYS   A CB  
1612 C CG  . LYS   A 76  ? 0.1839 0.1814 0.2609 0.0108  0.0067  -0.0409 76  LYS   A CG  
1613 C CD  . LYS   A 76  ? 0.1928 0.1790 0.3092 0.0152  0.0040  -0.0416 76  LYS   A CD  
1614 C CE  . LYS   A 76  ? 0.2158 0.1996 0.3687 0.0050  0.0135  -0.0460 76  LYS   A CE  
1615 N NZ  . LYS   A 76  ? 0.2183 0.1946 0.4142 -0.0085 0.0097  -0.0538 76  LYS   A NZ  
1629 N N   . VAL   A 77  ? 0.1749 0.1511 0.1268 0.0022  0.0255  0.0169  77  VAL   A N   
1630 C CA  . VAL   A 77  ? 0.1720 0.1549 0.1365 0.0051  0.0224  0.0118  77  VAL   A CA  
1631 C C   . VAL   A 77  ? 0.1685 0.1479 0.1329 0.0082  0.0153  -0.0027 77  VAL   A C   
1632 O O   . VAL   A 77  ? 0.1759 0.1518 0.1317 0.0107  0.0254  -0.0058 77  VAL   A O   
1633 C CB  . VAL   A 77  ? 0.1851 0.1705 0.1531 0.0050  0.0122  0.0132  77  VAL   A CB  
1634 C CG1 . VAL   A 77  ? 0.1797 0.1906 0.1646 0.0112  0.0007  0.0033  77  VAL   A CG1 
1635 C CG2 . VAL   A 77  ? 0.2081 0.1781 0.1719 0.0036  0.0066  0.0186  77  VAL   A CG2 
1645 N N   . GLY   A 78  ? 0.1677 0.1428 0.1284 0.0071  0.0160  0.0004  78  GLY   A N   
1646 C CA  . GLY   A 78  ? 0.1632 0.1413 0.1455 0.0020  0.0219  0.0034  78  GLY   A CA  
1647 C C   . GLY   A 78  ? 0.1547 0.1294 0.1456 0.0055  0.0220  0.0114  78  GLY   A C   
1648 O O   . GLY   A 78  ? 0.1520 0.1414 0.1646 -0.0008 0.0212  0.0196  78  GLY   A O   
1652 N N   . GLY   A 79  ? 0.1604 0.1303 0.1417 -0.0007 0.0140  0.0064  79  GLY   A N   
1653 C CA  . GLY   A 79  ? 0.1586 0.1345 0.1513 0.0005  0.0199  0.0121  79  GLY   A CA  
1654 C C   . GLY   A 79  ? 0.1388 0.1328 0.1402 -0.0013 0.0117  0.0097  79  GLY   A C   
1655 O O   . GLY   A 79  ? 0.1396 0.1401 0.1438 0.0145  0.0074  0.0007  79  GLY   A O   
1659 N N   . SER   A 80  ? 0.1315 0.1444 0.1627 0.0002  0.0142  0.0019  80  SER   A N   
1660 C CA  . SER   A 80  ? 0.1326 0.1406 0.1492 -0.0008 0.0132  0.0036  80  SER   A CA  
1661 C C   . SER   A 80  ? 0.1273 0.1438 0.1426 -0.0076 0.0091  0.0122  80  SER   A C   
1662 O O   . SER   A 80  ? 0.1272 0.1590 0.1857 0.0028  0.0118  -0.0051 80  SER   A O   
1663 C CB  . SER   A 80  ? 0.1515 0.1372 0.1662 -0.0010 0.0134  0.0115  80  SER   A CB  
1664 O OG  . SER   A 80  ? 0.1721 0.1412 0.2124 0.0026  -0.0069 0.0175  80  SER   A OG  
1670 N N   . CYS   A 81  ? 0.1288 0.1380 0.1412 -0.0027 -0.0026 0.0129  81  CYS   A N   
1671 C CA  . CYS   A 81  ? 0.1281 0.1443 0.1437 -0.0068 -0.0062 0.0184  81  CYS   A CA  
1672 C C   . CYS   A 81  ? 0.1284 0.1415 0.1471 -0.0075 -0.0032 0.0259  81  CYS   A C   
1673 O O   . CYS   A 81  ? 0.1309 0.1700 0.1602 -0.0012 -0.0017 0.0324  81  CYS   A O   
1674 C CB  . CYS   A 81  ? 0.1346 0.1498 0.1613 -0.0150 -0.0045 0.0142  81  CYS   A CB  
1675 S SG  . CYS   A 81  ? 0.1478 0.1389 0.1821 -0.0121 0.0012  0.0138  81  CYS   A SG  
1681 N N   . VAL   A 82  ? 0.1291 0.1464 0.1454 -0.0003 -0.0119 0.0200  82  VAL   A N   
1682 C CA  . VAL   A 82  ? 0.1461 0.1555 0.1432 -0.0004 -0.0116 0.0269  82  VAL   A CA  
1683 C C   . VAL   A 82  ? 0.1399 0.1566 0.1483 -0.0009 -0.0105 0.0214  82  VAL   A C   
1684 O O   . VAL   A 82  ? 0.1383 0.1631 0.1793 -0.0016 -0.0050 0.0052  82  VAL   A O   
1685 C CB  . VAL   A 82  ? 0.1766 0.1653 0.1622 0.0002  -0.0033 0.0333  82  VAL   A CB  
1686 C CG1 . VAL   A 82  ? 0.2003 0.1778 0.1706 0.0051  0.0012  0.0250  82  VAL   A CG1 
1687 C CG2 . VAL   A 82  ? 0.1861 0.1657 0.1971 -0.0130 -0.0141 0.0340  82  VAL   A CG2 
1697 N N   . LEU   A 83  ? 0.1369 0.1535 0.1417 -0.0125 -0.0103 0.0075  83  LEU   A N   
1698 C CA  . LEU   A 83  ? 0.1403 0.1575 0.1431 -0.0161 -0.0106 0.0038  83  LEU   A CA  
1699 C C   . LEU   A 83  ? 0.1455 0.1575 0.1407 -0.0112 -0.0076 0.0053  83  LEU   A C   
1700 O O   . LEU   A 83  ? 0.1539 0.1599 0.1457 -0.0161 -0.0034 0.0135  83  LEU   A O   
1701 C CB  . LEU   A 83  ? 0.1467 0.1627 0.1573 -0.0145 -0.0152 0.0119  83  LEU   A CB  
1702 C CG  . LEU   A 83  ? 0.1596 0.1715 0.1537 -0.0109 0.0023  0.0042  83  LEU   A CG  
1703 C CD1 . LEU   A 83  ? 0.1684 0.1750 0.1634 -0.0290 -0.0022 0.0207  83  LEU   A CD1 
1704 C CD2 . LEU   A 83  ? 0.1568 0.1828 0.1790 -0.0163 0.0181  0.0137  83  LEU   A CD2 
1716 N N   . SER   A 84  ? 0.1591 0.1625 0.1358 -0.0170 -0.0133 0.0103  84  SER   A N   
1717 C CA  . SER   A 84  ? 0.1721 0.1687 0.1275 -0.0175 -0.0150 0.0053  84  SER   A CA  
1718 C C   . SER   A 84  ? 0.1745 0.1644 0.1223 -0.0201 -0.0002 0.0052  84  SER   A C   
1719 O O   . SER   A 84  ? 0.1642 0.1723 0.1305 -0.0144 -0.0050 0.0037  84  SER   A O   
1720 C CB  . SER   A 84  ? 0.1837 0.1890 0.1307 -0.0141 -0.0143 -0.0022 84  SER   A CB  
1721 O OG  . SER   A 84  ? 0.1877 0.2045 0.1444 -0.0130 -0.0192 -0.0141 84  SER   A OG  
1727 N N   . GLY   A 85  ? 0.1883 0.1754 0.1309 -0.0194 0.0046  -0.0012 85  GLY   A N   
1728 C CA  . GLY   A 85  ? 0.1874 0.1806 0.1381 -0.0264 0.0170  -0.0027 85  GLY   A CA  
1729 C C   . GLY   A 85  ? 0.1840 0.1879 0.1181 -0.0214 0.0038  0.0001  85  GLY   A C   
1730 O O   . GLY   A 85  ? 0.1860 0.2016 0.1417 -0.0255 0.0117  -0.0131 85  GLY   A O   
1734 N N   . HIS   A 86  ? 0.1890 0.1778 0.1297 -0.0187 -0.0058 0.0029  86  HIS   A N   
1735 C CA  . HIS   A 86  ? 0.2024 0.1856 0.1184 -0.0225 -0.0035 0.0033  86  HIS   A CA  
1736 C C   . HIS   A 86  ? 0.2270 0.2008 0.1143 -0.0228 -0.0021 -0.0032 86  HIS   A C   
1737 O O   . HIS   A 86  ? 0.2446 0.2299 0.1295 -0.0194 0.0033  -0.0061 86  HIS   A O   
1738 C CB  . HIS   A 86  ? 0.2005 0.1779 0.1362 -0.0161 0.0026  0.0031  86  HIS   A CB  
1739 C CG  . HIS   A 86  ? 0.1931 0.1793 0.1316 -0.0105 0.0051  0.0097  86  HIS   A CG  
1740 N ND1 . HIS   A 86  ? 0.1968 0.1798 0.1779 -0.0208 0.0008  0.0040  86  HIS   A ND1 
1741 C CD2 . HIS   A 86  ? 0.1908 0.1688 0.1366 -0.0026 0.0099  0.0104  86  HIS   A CD2 
1742 C CE1 . HIS   A 86  ? 0.1902 0.1749 0.1835 -0.0162 0.0179  0.0069  86  HIS   A CE1 
1743 N NE2 . HIS   A 86  ? 0.1867 0.1663 0.1500 -0.0050 0.0138  0.0212  86  HIS   A NE2 
1751 N N   . ASN   A 87  ? 0.2417 0.2025 0.1338 -0.0123 0.0151  -0.0119 87  ASN   A N   
1752 C CA  . ASN   A 87  ? 0.2612 0.2175 0.1283 -0.0089 0.0358  -0.0160 87  ASN   A CA  
1753 C C   . ASN   A 87  ? 0.2590 0.2335 0.1742 -0.0152 0.0606  -0.0110 87  ASN   A C   
1754 O O   . ASN   A 87  ? 0.2822 0.2522 0.2330 -0.0265 0.1073  -0.0138 87  ASN   A O   
1755 C CB  . ASN   A 87  ? 0.2788 0.2297 0.1412 0.0007  0.0396  -0.0151 87  ASN   A CB  
1756 C CG  . ASN   A 87  ? 0.2960 0.2475 0.1564 0.0123  0.0582  -0.0084 87  ASN   A CG  
1757 O OD1 . ASN   A 87  ? 0.3145 0.2465 0.1669 0.0332  0.0572  0.0053  87  ASN   A OD1 
1758 N ND2 . ASN   A 87  ? 0.2997 0.2764 0.1685 0.0079  0.0625  -0.0040 87  ASN   A ND2 
1765 N N   . LEU   A 88  ? 0.2295 0.2199 0.1607 -0.0210 0.0295  0.0050  88  LEU   A N   
1766 C CA  . LEU   A 88  ? 0.2088 0.2218 0.1881 -0.0323 0.0250  0.0250  88  LEU   A CA  
1767 C C   . LEU   A 88  ? 0.2026 0.2275 0.1689 -0.0302 0.0330  0.0317  88  LEU   A C   
1768 O O   . LEU   A 88  ? 0.2083 0.2373 0.2070 -0.0281 0.0426  0.0468  88  LEU   A O   
1769 C CB  . LEU   A 88  ? 0.2075 0.2279 0.1997 -0.0386 -0.0082 0.0351  88  LEU   A CB  
1770 C CG  . LEU   A 88  ? 0.2271 0.2423 0.2413 -0.0376 -0.0142 0.0327  88  LEU   A CG  
1771 C CD1 . LEU   A 88  ? 0.2358 0.2449 0.2438 -0.0443 -0.0178 0.0220  88  LEU   A CD1 
1772 C CD2 . LEU   A 88  ? 0.2435 0.2554 0.2892 -0.0271 -0.0058 0.0251  88  LEU   A CD2 
1784 N N   . ALA   A 89  ? 0.2027 0.2184 0.1467 -0.0282 0.0216  0.0048  89  ALA   A N   
1785 C CA  . ALA   A 89  ? 0.2054 0.2179 0.1263 -0.0233 0.0121  0.0106  89  ALA   A CA  
1786 C C   . ALA   A 89  ? 0.2153 0.2194 0.1255 -0.0183 -0.0034 0.0131  89  ALA   A C   
1787 O O   . ALA   A 89  ? 0.2144 0.2153 0.1693 -0.0251 -0.0091 -0.0097 89  ALA   A O   
1788 C CB  . ALA   A 89  ? 0.1949 0.2198 0.1229 -0.0238 0.0046  0.0142  89  ALA   A CB  
1794 N N   . LYS   A 90  ? 0.2258 0.2336 0.1251 -0.0249 -0.0226 0.0207  90  LYS   A N   
1795 C CA  . LYS   A 90  ? 0.2331 0.2474 0.1382 -0.0241 -0.0428 0.0232  90  LYS   A CA  
1796 C C   . LYS   A 90  ? 0.2106 0.2275 0.1536 -0.0233 -0.0411 0.0163  90  LYS   A C   
1797 O O   . LYS   A 90  ? 0.2135 0.2461 0.1800 -0.0240 -0.0382 0.0063  90  LYS   A O   
1798 C CB  . LYS   A 90  ? 0.2611 0.2831 0.1753 -0.0210 -0.0580 0.0477  90  LYS   A CB  
1799 C CG  . LYS   A 90  ? 0.3033 0.3229 0.2991 -0.0226 -0.0566 0.0571  90  LYS   A CG  
1800 C CD  . LYS   A 90  ? 0.3424 0.3577 0.4108 -0.0279 -0.0401 0.0520  90  LYS   A CD  
1801 C CE  . LYS   A 90  ? 0.3795 0.3898 0.4787 -0.0320 -0.0302 0.0465  90  LYS   A CE  
1802 N NZ  . LYS   A 90  ? 0.4255 0.4282 0.5358 -0.0331 -0.0253 0.0463  90  LYS   A NZ  
1816 N N   . HIS   A 91  ? 0.1956 0.2021 0.1238 -0.0188 -0.0341 0.0132  91  HIS   A N   
1817 C CA  . HIS   A 91  ? 0.1807 0.1861 0.1287 -0.0101 -0.0242 0.0094  91  HIS   A CA  
1818 C C   . HIS   A 91  ? 0.1611 0.1712 0.1050 -0.0159 -0.0070 0.0099  91  HIS   A C   
1819 O O   . HIS   A 91  ? 0.1586 0.1861 0.1194 -0.0199 -0.0011 0.0146  91  HIS   A O   
1820 C CB  . HIS   A 91  ? 0.1959 0.2154 0.1869 0.0065  -0.0431 0.0102  91  HIS   A CB  
1821 C CG  . HIS   A 91  ? 0.2436 0.2649 0.2555 0.0147  -0.0632 0.0005  91  HIS   A CG  
1822 N ND1 . HIS   A 91  ? 0.2576 0.2948 0.2993 0.0189  -0.0767 -0.0123 91  HIS   A ND1 
1823 C CD2 . HIS   A 91  ? 0.2726 0.2911 0.2778 0.0227  -0.0892 0.0146  91  HIS   A CD2 
1824 C CE1 . HIS   A 91  ? 0.2755 0.3095 0.3002 0.0263  -0.0830 0.0073  91  HIS   A CE1 
1825 N NE2 . HIS   A 91  ? 0.2856 0.3076 0.2948 0.0316  -0.0994 0.0127  91  HIS   A NE2 
1833 N N   . CYS   A 92  ? 0.1493 0.1646 0.1225 -0.0219 -0.0112 0.0143  92  CYS   A N   
1834 C CA  . CYS   A 92  ? 0.1457 0.1566 0.1266 -0.0129 0.0006  0.0137  92  CYS   A CA  
1835 C C   . CYS   A 92  ? 0.1404 0.1533 0.1243 -0.0164 -0.0009 0.0116  92  CYS   A C   
1836 O O   . CYS   A 92  ? 0.1400 0.1540 0.1443 -0.0193 -0.0058 0.0050  92  CYS   A O   
1837 C CB  . CYS   A 92  ? 0.1495 0.1553 0.1318 -0.0080 -0.0079 0.0101  92  CYS   A CB  
1838 S SG  . CYS   A 92  ? 0.1424 0.1433 0.1456 -0.0112 -0.0054 0.0128  92  CYS   A SG  
1844 N N   . LEU   A 93  ? 0.1363 0.1406 0.1266 -0.0105 0.0020  0.0139  93  LEU   A N   
1845 C CA  . LEU   A 93  ? 0.1295 0.1393 0.1324 -0.0098 -0.0020 0.0138  93  LEU   A CA  
1846 C C   . LEU   A 93  ? 0.1301 0.1309 0.1144 -0.0050 0.0013  0.0057  93  LEU   A C   
1847 O O   . LEU   A 93  ? 0.1249 0.1348 0.1196 -0.0028 0.0011  0.0092  93  LEU   A O   
1848 C CB  . LEU   A 93  ? 0.1372 0.1374 0.1460 -0.0074 -0.0051 0.0195  93  LEU   A CB  
1849 C CG  . LEU   A 93  ? 0.1414 0.1354 0.1519 -0.0044 -0.0005 0.0163  93  LEU   A CG  
1850 C CD1 . LEU   A 93  ? 0.1470 0.1431 0.1840 -0.0015 0.0103  0.0127  93  LEU   A CD1 
1851 C CD2 . LEU   A 93  ? 0.1508 0.1331 0.1700 -0.0109 -0.0026 0.0121  93  LEU   A CD2 
1863 N N   . HIS   A 94  ? 0.1221 0.1234 0.1216 -0.0039 0.0007  0.0152  94  HIS   A N   
1864 C CA  . HIS   A 94  ? 0.1236 0.1241 0.1378 -0.0035 0.0058  0.0152  94  HIS   A CA  
1865 C C   . HIS   A 94  ? 0.1196 0.1223 0.1315 -0.0044 0.0009  0.0086  94  HIS   A C   
1866 O O   . HIS   A 94  ? 0.1246 0.1411 0.1573 -0.0048 -0.0017 -0.0050 94  HIS   A O   
1867 C CB  . HIS   A 94  ? 0.1224 0.1244 0.1376 -0.0055 -0.0029 0.0121  94  HIS   A CB  
1868 C CG  . HIS   A 94  ? 0.1249 0.1255 0.1216 -0.0035 -0.0037 0.0153  94  HIS   A CG  
1869 N ND1 . HIS   A 94  ? 0.1301 0.1254 0.1350 -0.0019 0.0008  0.0111  94  HIS   A ND1 
1870 C CD2 . HIS   A 94  ? 0.1345 0.1369 0.1404 -0.0071 -0.0054 0.0056  94  HIS   A CD2 
1871 C CE1 . HIS   A 94  ? 0.1313 0.1267 0.1410 -0.0118 -0.0114 0.0042  94  HIS   A CE1 
1872 N NE2 . HIS   A 94  ? 0.1347 0.1299 0.1386 -0.0126 -0.0075 0.0012  94  HIS   A NE2 
1880 N N   . VAL   A 95  ? 0.1206 0.1205 0.1166 0.0002  0.0088  0.0038  95  VAL   A N   
1881 C CA  . VAL   A 95  ? 0.1270 0.1254 0.1111 -0.0037 0.0119  0.0007  95  VAL   A CA  
1882 C C   . VAL   A 95  ? 0.1279 0.1247 0.1031 -0.0130 -0.0026 0.0070  95  VAL   A C   
1883 O O   . VAL   A 95  ? 0.1303 0.1346 0.1255 0.0097  0.0080  0.0044  95  VAL   A O   
1884 C CB  . VAL   A 95  ? 0.1338 0.1221 0.1336 -0.0083 0.0059  0.0035  95  VAL   A CB  
1885 C CG1 . VAL   A 95  ? 0.1439 0.1253 0.1407 -0.0097 0.0021  0.0035  95  VAL   A CG1 
1886 C CG2 . VAL   A 95  ? 0.1381 0.1354 0.1355 -0.0089 0.0083  0.0225  95  VAL   A CG2 
1896 N N   . VAL   A 96  ? 0.1367 0.1268 0.1005 -0.0047 0.0037  0.0073  96  VAL   A N   
1897 C CA  . VAL   A 96  ? 0.1446 0.1293 0.1185 -0.0034 0.0111  0.0112  96  VAL   A CA  
1898 C C   . VAL   A 96  ? 0.1448 0.1300 0.1248 0.0009  0.0136  0.0067  96  VAL   A C   
1899 O O   . VAL   A 96  ? 0.1523 0.1413 0.1374 -0.0088 0.0138  -0.0068 96  VAL   A O   
1900 C CB  . VAL   A 96  ? 0.1443 0.1293 0.1389 -0.0045 0.0171  0.0114  96  VAL   A CB  
1901 C CG1 . VAL   A 96  ? 0.1532 0.1314 0.1282 -0.0026 0.0152  0.0039  96  VAL   A CG1 
1902 C CG2 . VAL   A 96  ? 0.1426 0.1385 0.1410 -0.0141 0.0151  0.0115  96  VAL   A CG2 
1912 N N   . GLY   A 97  ? 0.1428 0.1361 0.1254 -0.0030 0.0065  0.0083  97  GLY   A N   
1913 C CA  . GLY   A 97  ? 0.1543 0.1463 0.1189 0.0018  -0.0009 0.0010  97  GLY   A CA  
1914 C C   . GLY   A 97  ? 0.1546 0.1592 0.1140 0.0000  0.0059  0.0059  97  GLY   A C   
1915 O O   . GLY   A 97  ? 0.1690 0.1574 0.1321 -0.0061 0.0008  0.0152  97  GLY   A O   
1919 N N   . PRO   A 98  ? 0.1538 0.1672 0.1027 -0.0027 -0.0001 0.0119  98  PRO   A N   
1920 C CA  . PRO   A 98  ? 0.1647 0.1901 0.1185 -0.0069 0.0047  0.0020  98  PRO   A CA  
1921 C C   . PRO   A 98  ? 0.1686 0.2008 0.1280 -0.0122 0.0008  0.0262  98  PRO   A C   
1922 O O   . PRO   A 98  ? 0.1648 0.1811 0.1406 -0.0077 -0.0017 0.0204  98  PRO   A O   
1923 C CB  . PRO   A 98  ? 0.1811 0.2024 0.0974 0.0003  0.0020  -0.0121 98  PRO   A CB  
1924 C CG  . PRO   A 98  ? 0.1797 0.1908 0.1176 0.0038  0.0032  -0.0190 98  PRO   A CG  
1925 C CD  . PRO   A 98  ? 0.1618 0.1708 0.1217 0.0004  0.0004  -0.0007 98  PRO   A CD  
1933 N N   A ASN   A 99  ? 0.1732 0.2253 0.1314 -0.0145 0.0023  0.0461  99  ASN   A N   
1934 N N   B ASN   A 99  ? 0.1822 0.2093 0.1363 -0.0085 -0.0027 0.0456  99  ASN   A N   
1935 C CA  A ASN   A 99  ? 0.1945 0.2482 0.1280 -0.0240 0.0057  0.0654  99  ASN   A CA  
1936 C CA  B ASN   A 99  ? 0.2046 0.2185 0.1484 -0.0081 -0.0073 0.0607  99  ASN   A CA  
1937 C C   A ASN   A 99  ? 0.2138 0.2888 0.1093 -0.0322 0.0045  0.0727  99  ASN   A C   
1938 C C   B ASN   A 99  ? 0.2204 0.2374 0.1557 -0.0016 -0.0004 0.0604  99  ASN   A C   
1939 O O   A ASN   A 99  ? 0.2267 0.3119 0.1232 -0.0218 -0.0059 0.0645  99  ASN   A O   
1940 O O   B ASN   A 99  ? 0.2231 0.2345 0.1548 0.0190  0.0033  0.0705  99  ASN   A O   
1941 C CB  A ASN   A 99  ? 0.1974 0.2378 0.1714 -0.0281 -0.0096 0.0679  99  ASN   A CB  
1942 C CB  B ASN   A 99  ? 0.2116 0.2141 0.1888 -0.0150 -0.0274 0.0730  99  ASN   A CB  
1943 C CG  A ASN   A 99  ? 0.2011 0.2341 0.2188 -0.0260 -0.0341 0.0449  99  ASN   A CG  
1944 C CG  B ASN   A 99  ? 0.2160 0.2128 0.2207 -0.0191 -0.0390 0.0900  99  ASN   A CG  
1945 O OD1 A ASN   A 99  ? 0.2150 0.2488 0.2256 -0.0125 -0.0435 0.0372  99  ASN   A OD1 
1946 O OD1 B ASN   A 99  ? 0.2245 0.2194 0.2043 -0.0203 -0.0372 0.1114  99  ASN   A OD1 
1947 N ND2 A ASN   A 99  ? 0.2048 0.2265 0.2377 -0.0231 -0.0221 0.0459  99  ASN   A ND2 
1948 N ND2 B ASN   A 99  ? 0.2177 0.2108 0.2380 -0.0119 -0.0448 0.0819  99  ASN   A ND2 
1961 N N   A VAL   A 100 ? 0.2281 0.3116 0.1216 -0.0455 -0.0303 0.0739  100 VAL   A N   
1962 N N   B VAL   A 100 ? 0.2369 0.2600 0.1707 -0.0139 -0.0173 0.0455  100 VAL   A N   
1963 C CA  A VAL   A 100 ? 0.2525 0.3425 0.1595 -0.0502 -0.0438 0.0752  100 VAL   A CA  
1964 C CA  B VAL   A 100 ? 0.2592 0.2862 0.2081 -0.0211 -0.0282 0.0336  100 VAL   A CA  
1965 C C   A VAL   A 100 ? 0.2534 0.3656 0.1538 -0.0567 -0.0468 0.0985  100 VAL   A C   
1966 C C   B VAL   A 100 ? 0.2694 0.3096 0.2262 -0.0310 -0.0325 0.0469  100 VAL   A C   
1967 O O   A VAL   A 100 ? 0.2554 0.3854 0.1794 -0.0536 -0.0271 0.0909  100 VAL   A O   
1968 O O   B VAL   A 100 ? 0.2735 0.3200 0.2453 -0.0309 -0.0278 0.0496  100 VAL   A O   
1969 C CB  A VAL   A 100 ? 0.2726 0.3400 0.1975 -0.0529 -0.0534 0.0647  100 VAL   A CB  
1970 C CB  B VAL   A 100 ? 0.2720 0.2846 0.2276 -0.0218 -0.0353 0.0220  100 VAL   A CB  
1971 C CG1 A VAL   A 100 ? 0.2724 0.3423 0.2331 -0.0587 -0.0458 0.0683  100 VAL   A CG1 
1972 C CG1 B VAL   A 100 ? 0.2749 0.2875 0.2499 -0.0213 -0.0320 0.0197  100 VAL   A CG1 
1973 C CG2 A VAL   A 100 ? 0.2843 0.3374 0.2207 -0.0520 -0.0544 0.0576  100 VAL   A CG2 
1974 C CG2 B VAL   A 100 ? 0.2783 0.2824 0.2395 -0.0249 -0.0355 0.0187  100 VAL   A CG2 
1993 N N   A ASN   A 101 ? 0.2612 0.3640 0.1944 -0.0636 -0.0443 0.1361  101 ASN   A N   
1994 N N   B ASN   A 101 ? 0.2799 0.3200 0.2421 -0.0388 -0.0321 0.0701  101 ASN   A N   
1995 C CA  A ASN   A 101 ? 0.2829 0.3672 0.2255 -0.0690 -0.0374 0.1538  101 ASN   A CA  
1996 C CA  B ASN   A 101 ? 0.2962 0.3309 0.2561 -0.0457 -0.0312 0.0856  101 ASN   A CA  
1997 C C   A ASN   A 101 ? 0.3049 0.3996 0.2512 -0.0645 -0.0050 0.1707  101 ASN   A C   
1998 C C   B ASN   A 101 ? 0.3083 0.3494 0.2725 -0.0546 -0.0185 0.0919  101 ASN   A C   
1999 O O   A ASN   A 101 ? 0.3268 0.4135 0.3020 -0.0590 -0.0046 0.1478  101 ASN   A O   
2000 O O   B ASN   A 101 ? 0.3206 0.3587 0.2759 -0.0488 -0.0244 0.0936  101 ASN   A O   
2001 C CB  A ASN   A 101 ? 0.2801 0.3377 0.2227 -0.0763 -0.0636 0.1461  101 ASN   A CB  
2002 C CB  B ASN   A 101 ? 0.2998 0.3242 0.2585 -0.0416 -0.0403 0.0843  101 ASN   A CB  
2003 C CG  A ASN   A 101 ? 0.2809 0.3171 0.2034 -0.0860 -0.0840 0.1167  101 ASN   A CG  
2004 C CG  B ASN   A 101 ? 0.3032 0.3185 0.2472 -0.0383 -0.0422 0.0720  101 ASN   A CG  
2005 O OD1 A ASN   A 101 ? 0.2768 0.3219 0.2068 -0.0785 -0.0688 0.0714  101 ASN   A OD1 
2006 O OD1 B ASN   A 101 ? 0.3027 0.3188 0.2423 -0.0317 -0.0358 0.0560  101 ASN   A OD1 
2007 N ND2 A ASN   A 101 ? 0.2877 0.3045 0.2061 -0.0984 -0.0990 0.1052  101 ASN   A ND2 
2008 N ND2 B ASN   A 101 ? 0.3081 0.3177 0.2530 -0.0405 -0.0482 0.0690  101 ASN   A ND2 
2021 N N   A LYS   A 102 ? 0.2977 0.4188 0.2748 -0.0706 0.0206  0.1716  102 LYS   A N   
2022 N N   B LYS   A 102 ? 0.3040 0.3581 0.2834 -0.0722 -0.0012 0.0840  102 LYS   A N   
2023 C CA  A LYS   A 102 ? 0.2990 0.4358 0.2748 -0.0768 0.0215  0.1471  102 LYS   A CA  
2024 C CA  B LYS   A 102 ? 0.3067 0.3687 0.2893 -0.0836 0.0096  0.0678  102 LYS   A CA  
2025 C C   A LYS   A 102 ? 0.3000 0.4564 0.2496 -0.0777 0.0174  0.1378  102 LYS   A C   
2026 C C   B LYS   A 102 ? 0.3113 0.3809 0.2898 -0.0851 0.0134  0.0543  102 LYS   A C   
2027 O O   A LYS   A 102 ? 0.3004 0.4726 0.2529 -0.0815 0.0262  0.1262  102 LYS   A O   
2028 O O   B LYS   A 102 ? 0.3117 0.3856 0.2911 -0.0926 0.0161  0.0495  102 LYS   A O   
2029 C CB  A LYS   A 102 ? 0.3042 0.4331 0.3138 -0.0811 0.0098  0.1175  102 LYS   A CB  
2030 C CB  B LYS   A 102 ? 0.3093 0.3688 0.3035 -0.0892 0.0080  0.0560  102 LYS   A CB  
2031 C CG  A LYS   A 102 ? 0.3163 0.4338 0.3329 -0.0809 0.0027  0.0936  102 LYS   A CG  
2032 C CG  B LYS   A 102 ? 0.3173 0.3713 0.3140 -0.0933 0.0061  0.0464  102 LYS   A CG  
2033 C CD  A LYS   A 102 ? 0.3330 0.4388 0.3587 -0.0766 -0.0010 0.0640  102 LYS   A CD  
2034 C CD  B LYS   A 102 ? 0.3281 0.3752 0.3279 -0.0950 0.0066  0.0323  102 LYS   A CD  
2035 C CE  A LYS   A 102 ? 0.3477 0.4432 0.3878 -0.0687 -0.0089 0.0420  102 LYS   A CE  
2036 C CE  B LYS   A 102 ? 0.3375 0.3788 0.3384 -0.0934 0.0085  0.0203  102 LYS   A CE  
2037 N NZ  A LYS   A 102 ? 0.3553 0.4440 0.3928 -0.0650 -0.0152 0.0294  102 LYS   A NZ  
2038 N NZ  B LYS   A 102 ? 0.3427 0.3805 0.3451 -0.0932 0.0105  0.0130  102 LYS   A NZ  
2065 N N   A GLY   A 103 ? 0.3035 0.4645 0.2513 -0.0651 -0.0079 0.1142  103 GLY   A N   
2066 N N   B GLY   A 103 ? 0.3139 0.3872 0.2849 -0.0786 0.0096  0.0422  103 GLY   A N   
2067 C CA  A GLY   A 103 ? 0.3093 0.4677 0.2364 -0.0502 -0.0027 0.0911  103 GLY   A CA  
2068 C CA  B GLY   A 103 ? 0.3095 0.3924 0.2734 -0.0750 0.0105  0.0306  103 GLY   A CA  
2069 C C   A GLY   A 103 ? 0.3104 0.4695 0.2222 -0.0400 0.0102  0.0680  103 GLY   A C   
2070 C C   B GLY   A 103 ? 0.3013 0.3982 0.2763 -0.0713 0.0138  0.0219  103 GLY   A C   
2071 O O   A GLY   A 103 ? 0.3179 0.4771 0.2447 -0.0373 0.0060  0.0623  103 GLY   A O   
2072 O O   B GLY   A 103 ? 0.3039 0.4023 0.2751 -0.0754 0.0092  0.0196  103 GLY   A O   
2079 N N   A GLU   A 104 ? 0.2969 0.4583 0.1677 -0.0354 0.0260  0.0546  104 GLU   A N   
2080 N N   B GLU   A 104 ? 0.2890 0.3990 0.2506 -0.0631 0.0242  0.0181  104 GLU   A N   
2081 C CA  A GLU   A 104 ? 0.2780 0.4406 0.1460 -0.0392 0.0267  0.0417  104 GLU   A CA  
2082 C CA  B GLU   A 104 ? 0.2820 0.4007 0.2471 -0.0548 0.0196  0.0105  104 GLU   A CA  
2083 C C   A GLU   A 104 ? 0.2819 0.4470 0.1344 -0.0474 0.0230  0.0091  104 GLU   A C   
2084 C C   B GLU   A 104 ? 0.2998 0.4118 0.2562 -0.0486 0.0152  -0.0042 104 GLU   A C   
2085 O O   A GLU   A 104 ? 0.2732 0.4530 0.1560 -0.0523 -0.0010 -0.0077 104 GLU   A O   
2086 O O   B GLU   A 104 ? 0.3022 0.4183 0.2667 -0.0482 0.0134  -0.0125 104 GLU   A O   
2087 C CB  A GLU   A 104 ? 0.2498 0.4149 0.1324 -0.0370 0.0247  0.0657  104 GLU   A CB  
2088 C CB  B GLU   A 104 ? 0.2599 0.3916 0.2339 -0.0538 0.0179  0.0147  104 GLU   A CB  
2089 C CG  A GLU   A 104 ? 0.2302 0.3977 0.1333 -0.0341 0.0144  0.0758  104 GLU   A CG  
2090 C CG  B GLU   A 104 ? 0.2425 0.3833 0.2276 -0.0540 0.0153  0.0142  104 GLU   A CG  
2091 C CD  A GLU   A 104 ? 0.2149 0.3830 0.1363 -0.0316 0.0096  0.0879  104 GLU   A CD  
2092 C CD  B GLU   A 104 ? 0.2265 0.3746 0.2173 -0.0579 0.0137  0.0168  104 GLU   A CD  
2093 O OE1 A GLU   A 104 ? 0.2036 0.3726 0.1320 -0.0253 -0.0000 0.0884  104 GLU   A OE1 
2094 O OE1 B GLU   A 104 ? 0.2126 0.3657 0.1949 -0.0632 0.0170  0.0165  104 GLU   A OE1 
2095 O OE2 A GLU   A 104 ? 0.2295 0.3837 0.1544 -0.0377 0.0111  0.1042  104 GLU   A OE2 
2096 O OE2 B GLU   A 104 ? 0.2318 0.3771 0.2432 -0.0564 0.0009  0.0157  104 GLU   A OE2 
2109 N N   A ASP   A 105 ? 0.2989 0.4452 0.1569 -0.0491 0.0330  -0.0168 105 ASP   A N   
2110 N N   B ASP   A 105 ? 0.3162 0.4157 0.2685 -0.0433 0.0111  -0.0162 105 ASP   A N   
2111 C CA  A ASP   A 105 ? 0.3056 0.4477 0.2146 -0.0458 0.0418  -0.0448 105 ASP   A CA  
2112 C CA  B ASP   A 105 ? 0.3274 0.4192 0.2937 -0.0385 0.0108  -0.0312 105 ASP   A CA  
2113 C C   A ASP   A 105 ? 0.2728 0.4261 0.1678 -0.0540 0.0293  -0.0693 105 ASP   A C   
2114 C C   B ASP   A 105 ? 0.3187 0.4121 0.2771 -0.0421 0.0080  -0.0379 105 ASP   A C   
2115 O O   A ASP   A 105 ? 0.2512 0.3872 0.1311 -0.0470 0.0206  -0.0805 105 ASP   A O   
2116 O O   B ASP   A 105 ? 0.3164 0.4131 0.2609 -0.0417 0.0110  -0.0443 105 ASP   A O   
2117 C CB  A ASP   A 105 ? 0.3354 0.4646 0.2930 -0.0323 0.0612  -0.0537 105 ASP   A CB  
2118 C CB  B ASP   A 105 ? 0.3432 0.4289 0.3277 -0.0306 0.0141  -0.0420 105 ASP   A CB  
2119 C CG  A ASP   A 105 ? 0.3546 0.4845 0.3653 -0.0204 0.0667  -0.0662 105 ASP   A CG  
2120 C CG  B ASP   A 105 ? 0.3557 0.4387 0.3601 -0.0246 0.0119  -0.0535 105 ASP   A CG  
2121 O OD1 A ASP   A 105 ? 0.3618 0.4941 0.3850 -0.0180 0.0578  -0.0772 105 ASP   A OD1 
2122 O OD1 B ASP   A 105 ? 0.3569 0.4442 0.3706 -0.0233 0.0080  -0.0608 105 ASP   A OD1 
2123 O OD2 A ASP   A 105 ? 0.3620 0.4922 0.3968 -0.0185 0.0829  -0.0674 105 ASP   A OD2 
2124 O OD2 B ASP   A 105 ? 0.3652 0.4410 0.3766 -0.0229 0.0137  -0.0579 105 ASP   A OD2 
2133 N N   A ILE   A 106 ? 0.2598 0.4207 0.2029 -0.0632 -0.0031 -0.0576 106 ILE   A N   
2134 N N   B ILE   A 106 ? 0.3106 0.4010 0.2767 -0.0465 -0.0016 -0.0394 106 ILE   A N   
2135 C CA  A ILE   A 106 ? 0.2365 0.4025 0.2307 -0.0711 -0.0252 -0.0746 106 ILE   A CA  
2136 C CA  B ILE   A 106 ? 0.2964 0.3845 0.2790 -0.0495 -0.0064 -0.0500 106 ILE   A CA  
2137 C C   A ILE   A 106 ? 0.2196 0.3763 0.2308 -0.0825 -0.0209 -0.1013 106 ILE   A C   
2138 C C   B ILE   A 106 ? 0.2822 0.3586 0.2756 -0.0512 0.0029  -0.0769 106 ILE   A C   
2139 O O   A ILE   A 106 ? 0.1931 0.3628 0.2214 -0.0844 0.0033  -0.0973 106 ILE   A O   
2140 O O   B ILE   A 106 ? 0.2709 0.3463 0.2634 -0.0507 0.0076  -0.0868 106 ILE   A O   
2141 C CB  A ILE   A 106 ? 0.2403 0.4144 0.2669 -0.0572 -0.0441 -0.0475 106 ILE   A CB  
2142 C CB  B ILE   A 106 ? 0.2983 0.3917 0.2893 -0.0463 -0.0192 -0.0325 106 ILE   A CB  
2143 C CG1 A ILE   A 106 ? 0.2306 0.4085 0.2980 -0.0408 -0.0496 -0.0269 106 ILE   A CG1 
2144 C CG1 B ILE   A 106 ? 0.2968 0.3862 0.3054 -0.0413 -0.0225 -0.0202 106 ILE   A CG1 
2145 C CG2 A ILE   A 106 ? 0.2503 0.4236 0.2869 -0.0582 -0.0487 -0.0419 106 ILE   A CG2 
2146 C CG2 B ILE   A 106 ? 0.3013 0.3996 0.2971 -0.0463 -0.0250 -0.0306 106 ILE   A CG2 
2147 C CD1 A ILE   A 106 ? 0.2268 0.4002 0.3177 -0.0253 -0.0402 -0.0116 106 ILE   A CD1 
2148 C CD1 B ILE   A 106 ? 0.2974 0.3807 0.3131 -0.0361 -0.0208 -0.0115 106 ILE   A CD1 
2171 N N   A GLN   A 107 ? 0.2421 0.3649 0.2488 -0.0831 -0.0152 -0.1239 107 GLN   A N   
2172 N N   B GLN   A 107 ? 0.2823 0.3469 0.2956 -0.0508 0.0138  -0.0882 107 GLN   A N   
2173 C CA  A GLN   A 107 ? 0.2707 0.3520 0.3339 -0.0711 0.0176  -0.1105 107 GLN   A CA  
2174 C CA  B GLN   A 107 ? 0.2809 0.3299 0.3263 -0.0447 0.0297  -0.0866 107 GLN   A CA  
2175 C C   A GLN   A 107 ? 0.2533 0.3023 0.3229 -0.0617 0.0480  -0.0833 107 GLN   A C   
2176 C C   B GLN   A 107 ? 0.2506 0.2923 0.3106 -0.0468 0.0474  -0.0765 107 GLN   A C   
2177 O O   A GLN   A 107 ? 0.2674 0.2962 0.3935 -0.0636 0.0590  -0.0844 107 GLN   A O   
2178 O O   B GLN   A 107 ? 0.2504 0.2871 0.3502 -0.0430 0.0579  -0.0827 107 GLN   A O   
2179 C CB  A GLN   A 107 ? 0.3093 0.3851 0.4296 -0.0763 0.0168  -0.1055 107 GLN   A CB  
2180 C CB  B GLN   A 107 ? 0.3063 0.3471 0.3845 -0.0402 0.0204  -0.0810 107 GLN   A CB  
2181 C CG  A GLN   A 107 ? 0.3458 0.4124 0.5282 -0.0734 0.0150  -0.0884 107 GLN   A CG  
2182 C CG  B GLN   A 107 ? 0.3297 0.3609 0.4478 -0.0341 0.0115  -0.0685 107 GLN   A CG  
2183 C CD  A GLN   A 107 ? 0.3751 0.4284 0.6101 -0.0696 0.0136  -0.0727 107 GLN   A CD  
2184 C CD  B GLN   A 107 ? 0.3475 0.3677 0.4996 -0.0274 0.0047  -0.0517 107 GLN   A CD  
2185 O OE1 A GLN   A 107 ? 0.3881 0.4394 0.6429 -0.0708 0.0137  -0.0687 107 GLN   A OE1 
2186 O OE1 B GLN   A 107 ? 0.3558 0.3696 0.5203 -0.0259 0.0014  -0.0437 107 GLN   A OE1 
2187 N NE2 A GLN   A 107 ? 0.3888 0.4305 0.6392 -0.0666 0.0084  -0.0718 107 GLN   A NE2 
2188 N NE2 B GLN   A 107 ? 0.3511 0.3682 0.5113 -0.0244 0.0039  -0.0480 107 GLN   A NE2 
2205 N N   . LEU   A 108 ? 0.2228 0.2576 0.2498 -0.0502 0.0508  -0.0759 108 LEU   A N   
2206 C CA  . LEU   A 108 ? 0.1960 0.1982 0.2226 -0.0199 0.0443  -0.0287 108 LEU   A CA  
2207 C C   . LEU   A 108 ? 0.1764 0.1609 0.2213 -0.0056 0.0381  -0.0019 108 LEU   A C   
2208 O O   . LEU   A 108 ? 0.1697 0.1566 0.2193 -0.0002 0.0375  0.0061  108 LEU   A O   
2209 C CB  . LEU   A 108 ? 0.2012 0.2050 0.1875 -0.0181 0.0412  -0.0132 108 LEU   A CB  
2210 C CG  . LEU   A 108 ? 0.2208 0.2344 0.2168 -0.0178 0.0555  -0.0152 108 LEU   A CG  
2211 C CD1 . LEU   A 108 ? 0.2430 0.2422 0.2171 -0.0315 0.0680  -0.0067 108 LEU   A CD1 
2212 C CD2 . LEU   A 108 ? 0.2221 0.2555 0.2713 -0.0090 0.0549  -0.0117 108 LEU   A CD2 
2225 N N   . LEU   A 109 ? 0.1582 0.1538 0.2031 0.0025  0.0302  0.0117  109 LEU   A N   
2226 C CA  . LEU   A 109 ? 0.1539 0.1425 0.1731 -0.0024 0.0093  0.0100  109 LEU   A CA  
2227 C C   . LEU   A 109 ? 0.1422 0.1354 0.1690 -0.0119 0.0102  0.0056  109 LEU   A C   
2228 O O   . LEU   A 109 ? 0.1511 0.1275 0.1893 -0.0022 -0.0043 0.0002  109 LEU   A O   
2229 C CB  . LEU   A 109 ? 0.1614 0.1499 0.1960 0.0121  0.0049  0.0254  109 LEU   A CB  
2230 C CG  . LEU   A 109 ? 0.1528 0.1583 0.2027 0.0068  0.0055  0.0326  109 LEU   A CG  
2231 C CD1 . LEU   A 109 ? 0.1536 0.1503 0.2086 0.0011  0.0150  0.0099  109 LEU   A CD1 
2232 C CD2 . LEU   A 109 ? 0.1545 0.1713 0.2184 0.0068  0.0014  0.0310  109 LEU   A CD2 
2244 N N   . LYS   A 110 ? 0.1446 0.1386 0.1576 -0.0073 0.0006  0.0031  110 LYS   A N   
2245 C CA  . LYS   A 110 ? 0.1450 0.1335 0.1638 -0.0048 0.0020  0.0025  110 LYS   A CA  
2246 C C   . LYS   A 110 ? 0.1445 0.1301 0.1571 -0.0062 0.0056  -0.0096 110 LYS   A C   
2247 O O   . LYS   A 110 ? 0.1386 0.1328 0.1611 -0.0126 0.0101  -0.0085 110 LYS   A O   
2248 C CB  . LYS   A 110 ? 0.1586 0.1412 0.1950 -0.0073 -0.0108 -0.0041 110 LYS   A CB  
2249 C CG  . LYS   A 110 ? 0.1571 0.1364 0.1972 -0.0104 -0.0110 -0.0039 110 LYS   A CG  
2250 C CD  . LYS   A 110 ? 0.1576 0.1443 0.2156 -0.0108 -0.0051 -0.0073 110 LYS   A CD  
2251 C CE  . LYS   A 110 ? 0.1650 0.1485 0.2332 -0.0171 0.0063  -0.0087 110 LYS   A CE  
2252 N NZ  . LYS   A 110 ? 0.1593 0.1531 0.2445 -0.0221 0.0113  -0.0078 110 LYS   A NZ  
2266 N N   . SER   A 111 ? 0.1454 0.1343 0.1610 -0.0003 0.0027  -0.0043 111 SER   A N   
2267 C CA  . SER   A 111 ? 0.1355 0.1387 0.1717 0.0034  0.0102  0.0072  111 SER   A CA  
2268 C C   . SER   A 111 ? 0.1335 0.1297 0.1646 -0.0063 0.0094  0.0047  111 SER   A C   
2269 O O   . SER   A 111 ? 0.1446 0.1271 0.1706 -0.0050 0.0129  0.0065  111 SER   A O   
2270 C CB  . SER   A 111 ? 0.1579 0.1614 0.1825 0.0036  0.0243  -0.0105 111 SER   A CB  
2271 O OG  . SER   A 111 ? 0.2002 0.1811 0.1815 0.0035  0.0314  -0.0150 111 SER   A OG  
2277 N N   . ALA   A 112 ? 0.1368 0.1259 0.1662 -0.0009 0.0134  0.0026  112 ALA   A N   
2278 C CA  . ALA   A 112 ? 0.1372 0.1257 0.1574 -0.0050 0.0157  0.0036  112 ALA   A CA  
2279 C C   . ALA   A 112 ? 0.1317 0.1182 0.1753 0.0014  0.0106  0.0020  112 ALA   A C   
2280 O O   . ALA   A 112 ? 0.1376 0.1196 0.1731 -0.0109 0.0169  -0.0010 112 ALA   A O   
2281 C CB  . ALA   A 112 ? 0.1496 0.1265 0.1557 -0.0058 0.0132  0.0017  112 ALA   A CB  
2287 N N   . TYR   A 113 ? 0.1199 0.1219 0.1762 -0.0051 0.0133  0.0067  113 TYR   A N   
2288 C CA  . TYR   A 113 ? 0.1239 0.1219 0.1708 -0.0006 0.0153  0.0134  113 TYR   A CA  
2289 C C   . TYR   A 113 ? 0.1203 0.1238 0.1603 -0.0104 0.0110  0.0055  113 TYR   A C   
2290 O O   . TYR   A 113 ? 0.1280 0.1309 0.1680 -0.0084 0.0124  0.0040  113 TYR   A O   
2291 C CB  . TYR   A 113 ? 0.1220 0.1318 0.1726 -0.0073 -0.0052 0.0157  113 TYR   A CB  
2292 C CG  . TYR   A 113 ? 0.1286 0.1353 0.1568 -0.0166 0.0081  0.0173  113 TYR   A CG  
2293 C CD1 . TYR   A 113 ? 0.1267 0.1417 0.1584 -0.0083 0.0023  0.0197  113 TYR   A CD1 
2294 C CD2 . TYR   A 113 ? 0.1346 0.1403 0.1542 -0.0107 0.0091  0.0102  113 TYR   A CD2 
2295 C CE1 . TYR   A 113 ? 0.1292 0.1498 0.1518 -0.0041 0.0064  0.0234  113 TYR   A CE1 
2296 C CE2 . TYR   A 113 ? 0.1294 0.1515 0.1541 -0.0109 -0.0008 0.0175  113 TYR   A CE2 
2297 C CZ  . TYR   A 113 ? 0.1309 0.1514 0.1527 -0.0006 0.0115  0.0255  113 TYR   A CZ  
2298 O OH  . TYR   A 113 ? 0.1296 0.1559 0.1746 0.0044  0.0117  0.0251  113 TYR   A OH  
2308 N N   . GLU   A 114 ? 0.1256 0.1279 0.1676 -0.0036 0.0145  0.0091  114 GLU   A N   
2309 C CA  . GLU   A 114 ? 0.1345 0.1181 0.1686 0.0040  0.0121  0.0115  114 GLU   A CA  
2310 C C   . GLU   A 114 ? 0.1328 0.1265 0.1536 -0.0032 0.0088  0.0069  114 GLU   A C   
2311 O O   . GLU   A 114 ? 0.1384 0.1321 0.1560 -0.0018 0.0056  0.0107  114 GLU   A O   
2312 C CB  . GLU   A 114 ? 0.1329 0.1240 0.1740 -0.0070 0.0086  0.0108  114 GLU   A CB  
2313 C CG  . GLU   A 114 ? 0.1380 0.1245 0.1836 -0.0012 0.0112  -0.0004 114 GLU   A CG  
2314 C CD  . GLU   A 114 ? 0.1435 0.1265 0.1830 -0.0081 0.0049  -0.0016 114 GLU   A CD  
2315 O OE1 . GLU   A 114 ? 0.1482 0.1294 0.1845 -0.0098 0.0126  -0.0101 114 GLU   A OE1 
2316 O OE2 . GLU   A 114 ? 0.1568 0.1369 0.2121 -0.0101 0.0109  -0.0138 114 GLU   A OE2 
2323 N N   . ASN   A 115 ? 0.1344 0.1221 0.1498 -0.0068 0.0077  -0.0006 115 ASN   A N   
2324 C CA  . ASN   A 115 ? 0.1357 0.1317 0.1652 -0.0109 0.0105  0.0046  115 ASN   A CA  
2325 C C   . ASN   A 115 ? 0.1314 0.1281 0.1594 -0.0109 0.0003  0.0079  115 ASN   A C   
2326 O O   . ASN   A 115 ? 0.1346 0.1407 0.1673 -0.0104 0.0063  0.0131  115 ASN   A O   
2327 C CB  . ASN   A 115 ? 0.1431 0.1337 0.1554 -0.0189 0.0099  0.0081  115 ASN   A CB  
2328 C CG  . ASN   A 115 ? 0.1432 0.1532 0.1666 -0.0193 0.0209  0.0101  115 ASN   A CG  
2329 O OD1 . ASN   A 115 ? 0.1411 0.2428 0.2131 -0.0139 0.0282  0.0287  115 ASN   A OD1 
2330 N ND2 . ASN   A 115 ? 0.1487 0.1344 0.1607 -0.0154 0.0292  0.0088  115 ASN   A ND2 
2337 N N   . PHE   A 116 ? 0.1258 0.1290 0.1674 -0.0054 0.0070  0.0133  116 PHE   A N   
2338 C CA  . PHE   A 116 ? 0.1323 0.1350 0.1493 -0.0008 0.0153  0.0113  116 PHE   A CA  
2339 C C   . PHE   A 116 ? 0.1299 0.1405 0.1517 -0.0050 0.0157  0.0166  116 PHE   A C   
2340 O O   . PHE   A 116 ? 0.1371 0.1434 0.1579 -0.0002 0.0146  0.0159  116 PHE   A O   
2341 C CB  . PHE   A 116 ? 0.1310 0.1308 0.1673 -0.0029 0.0117  0.0200  116 PHE   A CB  
2342 C CG  . PHE   A 116 ? 0.1305 0.1279 0.1473 -0.0062 0.0167  0.0072  116 PHE   A CG  
2343 C CD1 . PHE   A 116 ? 0.1354 0.1333 0.1436 -0.0057 0.0154  0.0082  116 PHE   A CD1 
2344 C CD2 . PHE   A 116 ? 0.1384 0.1359 0.1617 -0.0046 0.0177  0.0122  116 PHE   A CD2 
2345 C CE1 . PHE   A 116 ? 0.1316 0.1318 0.1630 -0.0156 0.0087  0.0056  116 PHE   A CE1 
2346 C CE2 . PHE   A 116 ? 0.1304 0.1289 0.1747 -0.0035 0.0175  0.0051  116 PHE   A CE2 
2347 C CZ  . PHE   A 116 ? 0.1369 0.1249 0.1633 -0.0026 0.0062  0.0057  116 PHE   A CZ  
2357 N N   . ASN   A 117 ? 0.1330 0.1341 0.1688 -0.0050 0.0100  0.0188  117 ASN   A N   
2358 C CA  . ASN   A 117 ? 0.1317 0.1361 0.1717 -0.0029 0.0114  0.0173  117 ASN   A CA  
2359 C C   . ASN   A 117 ? 0.1327 0.1437 0.1883 -0.0033 0.0142  0.0248  117 ASN   A C   
2360 O O   . ASN   A 117 ? 0.1427 0.1494 0.2120 -0.0074 -0.0071 0.0348  117 ASN   A O   
2361 C CB  . ASN   A 117 ? 0.1339 0.1426 0.1824 0.0013  0.0142  0.0215  117 ASN   A CB  
2362 C CG  . ASN   A 117 ? 0.1310 0.1396 0.1764 -0.0025 0.0123  0.0280  117 ASN   A CG  
2363 O OD1 . ASN   A 117 ? 0.1304 0.1578 0.1920 -0.0107 0.0163  0.0186  117 ASN   A OD1 
2364 N ND2 . ASN   A 117 ? 0.1312 0.1406 0.1762 -0.0027 0.0096  0.0302  117 ASN   A ND2 
2371 N N   . GLN   A 118 ? 0.1332 0.1411 0.1810 -0.0044 -0.0083 0.0259  118 GLN   A N   
2372 C CA  . GLN   A 118 ? 0.1400 0.1528 0.1872 -0.0031 -0.0037 0.0206  118 GLN   A CA  
2373 C C   . GLN   A 118 ? 0.1439 0.1604 0.1681 -0.0081 -0.0080 0.0257  118 GLN   A C   
2374 O O   . GLN   A 118 ? 0.1420 0.1950 0.1981 0.0031  -0.0168 0.0046  118 GLN   A O   
2375 C CB  . GLN   A 118 ? 0.1337 0.1578 0.2007 -0.0085 0.0072  0.0196  118 GLN   A CB  
2376 C CG  . GLN   A 118 ? 0.1351 0.1581 0.2042 -0.0039 0.0159  0.0249  118 GLN   A CG  
2377 C CD  . GLN   A 118 ? 0.1344 0.1625 0.2175 0.0020  0.0135  0.0208  118 GLN   A CD  
2378 O OE1 . GLN   A 118 ? 0.1388 0.1746 0.2234 0.0088  0.0030  0.0162  118 GLN   A OE1 
2379 N NE2 . GLN   A 118 ? 0.1402 0.1574 0.2240 0.0048  0.0098  0.0253  118 GLN   A NE2 
2388 N N   . HIS   A 119 ? 0.1465 0.1531 0.1641 -0.0021 -0.0039 0.0269  119 HIS   A N   
2389 C CA  . HIS   A 119 ? 0.1565 0.1609 0.1686 -0.0067 -0.0007 0.0262  119 HIS   A CA  
2390 C C   . HIS   A 119 ? 0.1647 0.1674 0.1583 -0.0080 0.0051  0.0340  119 HIS   A C   
2391 O O   . HIS   A 119 ? 0.1644 0.1768 0.1697 -0.0250 -0.0008 0.0328  119 HIS   A O   
2392 C CB  . HIS   A 119 ? 0.1551 0.1595 0.1960 -0.0086 0.0207  0.0307  119 HIS   A CB  
2393 C CG  . HIS   A 119 ? 0.1582 0.1632 0.2425 -0.0001 0.0150  0.0427  119 HIS   A CG  
2394 N ND1 . HIS   A 119 ? 0.1731 0.1799 0.3090 -0.0143 0.0134  0.0277  119 HIS   A ND1 
2395 C CD2 . HIS   A 119 ? 0.1709 0.1759 0.2541 0.0119  0.0285  0.0644  119 HIS   A CD2 
2396 C CE1 . HIS   A 119 ? 0.1773 0.1810 0.3127 -0.0186 0.0272  0.0504  119 HIS   A CE1 
2397 N NE2 . HIS   A 119 ? 0.1863 0.1809 0.3049 0.0022  0.0412  0.0675  119 HIS   A NE2 
2405 N N   . GLU   A 120 ? 0.1717 0.1904 0.1677 -0.0020 0.0003  0.0547  120 GLU   A N   
2406 C CA  . GLU   A 120 ? 0.1962 0.2202 0.2068 0.0092  0.0017  0.0927  120 GLU   A CA  
2407 C C   . GLU   A 120 ? 0.1800 0.2013 0.1728 -0.0066 -0.0014 0.0822  120 GLU   A C   
2408 O O   . GLU   A 120 ? 0.1783 0.1941 0.1916 -0.0112 -0.0055 0.0692  120 GLU   A O   
2409 C CB  . GLU   A 120 ? 0.2660 0.2943 0.2533 0.0370  -0.0019 0.1478  120 GLU   A CB  
2410 C CG  . GLU   A 120 ? 0.3722 0.3776 0.3775 0.0545  -0.0003 0.1571  120 GLU   A CG  
2411 C CD  . GLU   A 120 ? 0.4856 0.4747 0.5133 0.0581  0.0196  0.1375  120 GLU   A CD  
2412 O OE1 . GLU   A 120 ? 0.5129 0.4804 0.5370 0.0595  0.0243  0.1329  120 GLU   A OE1 
2413 O OE2 . GLU   A 120 ? 0.5558 0.5534 0.5746 0.0551  0.0287  0.1289  120 GLU   A OE2 
2420 N N   . VAL   A 121 ? 0.1726 0.2043 0.1522 -0.0114 0.0096  0.0586  121 VAL   A N   
2421 C CA  . VAL   A 121 ? 0.1768 0.2087 0.1461 -0.0086 0.0157  0.0606  121 VAL   A CA  
2422 C C   . VAL   A 121 ? 0.1643 0.1868 0.1322 -0.0176 0.0062  0.0439  121 VAL   A C   
2423 O O   . VAL   A 121 ? 0.1727 0.1905 0.1454 -0.0263 -0.0039 0.0290  121 VAL   A O   
2424 C CB  . VAL   A 121 ? 0.2085 0.2459 0.1881 -0.0028 0.0278  0.0693  121 VAL   A CB  
2425 C CG1 . VAL   A 121 ? 0.2146 0.2584 0.1826 0.0033  0.0395  0.0622  121 VAL   A CG1 
2426 C CG2 . VAL   A 121 ? 0.2308 0.2685 0.2345 -0.0142 0.0194  0.0499  121 VAL   A CG2 
2436 N N   . LEU   A 122 ? 0.1506 0.1724 0.1441 -0.0146 0.0102  0.0405  122 LEU   A N   
2437 C CA  . LEU   A 122 ? 0.1580 0.1570 0.1572 -0.0122 0.0196  0.0378  122 LEU   A CA  
2438 C C   . LEU   A 122 ? 0.1524 0.1538 0.1490 -0.0175 0.0064  0.0324  122 LEU   A C   
2439 O O   . LEU   A 122 ? 0.1537 0.1620 0.1766 -0.0265 0.0051  0.0276  122 LEU   A O   
2440 C CB  . LEU   A 122 ? 0.1812 0.1594 0.1886 -0.0061 0.0156  0.0444  122 LEU   A CB  
2441 C CG  . LEU   A 122 ? 0.1817 0.1640 0.1783 -0.0117 0.0256  0.0211  122 LEU   A CG  
2442 C CD1 . LEU   A 122 ? 0.2075 0.1671 0.1897 -0.0231 0.0232  0.0264  122 LEU   A CD1 
2443 C CD2 . LEU   A 122 ? 0.1781 0.1687 0.1638 -0.0055 0.0359  0.0224  122 LEU   A CD2 
2455 N N   . LEU   A 123 ? 0.1459 0.1534 0.1463 -0.0186 0.0081  0.0259  123 LEU   A N   
2456 C CA  . LEU   A 123 ? 0.1439 0.1542 0.1361 -0.0205 0.0087  0.0207  123 LEU   A CA  
2457 C C   . LEU   A 123 ? 0.1400 0.1482 0.1257 -0.0142 0.0111  0.0202  123 LEU   A C   
2458 O O   . LEU   A 123 ? 0.1382 0.1592 0.1352 -0.0259 0.0037  0.0253  123 LEU   A O   
2459 C CB  . LEU   A 123 ? 0.1588 0.1615 0.1355 -0.0197 0.0162  0.0167  123 LEU   A CB  
2460 C CG  . LEU   A 123 ? 0.1651 0.1772 0.1449 -0.0171 0.0188  0.0034  123 LEU   A CG  
2461 C CD1 . LEU   A 123 ? 0.1711 0.1833 0.1634 -0.0032 0.0111  0.0007  123 LEU   A CD1 
2462 C CD2 . LEU   A 123 ? 0.1740 0.1860 0.1563 -0.0147 0.0107  -0.0080 123 LEU   A CD2 
2474 N N   A ALA   A 124 ? 0.1402 0.1429 0.1249 -0.0183 0.0068  0.0152  124 ALA   A N   
2475 N N   B ALA   A 124 ? 0.1349 0.1413 0.1226 -0.0093 0.0125  0.0119  124 ALA   A N   
2476 C CA  A ALA   A 124 ? 0.1367 0.1442 0.1347 -0.0174 0.0059  0.0252  124 ALA   A CA  
2477 C CA  B ALA   A 124 ? 0.1292 0.1391 0.1316 -0.0041 0.0144  0.0171  124 ALA   A CA  
2478 C C   A ALA   A 124 ? 0.1329 0.1458 0.1380 -0.0161 0.0111  0.0268  124 ALA   A C   
2479 C C   B ALA   A 124 ? 0.1238 0.1380 0.1396 -0.0037 0.0268  0.0152  124 ALA   A C   
2480 O O   A ALA   A 124 ? 0.1384 0.1559 0.1564 -0.0138 0.0103  0.0338  124 ALA   A O   
2481 O O   B ALA   A 124 ? 0.1177 0.1303 0.1515 -0.0034 0.0296  0.0142  124 ALA   A O   
2482 C CB  A ALA   A 124 ? 0.1415 0.1418 0.1665 -0.0187 0.0163  0.0209  124 ALA   A CB  
2483 C CB  B ALA   A 124 ? 0.1323 0.1374 0.1420 0.0006  0.0136  0.0193  124 ALA   A CB  
2494 N N   A PRO   A 125 ? 0.1263 0.1296 0.1265 -0.0075 0.0077  0.0232  125 PRO   A N   
2495 N N   B PRO   A 125 ? 0.1314 0.1417 0.1432 -0.0018 0.0231  0.0192  125 PRO   A N   
2496 C CA  A PRO   A 125 ? 0.1289 0.1277 0.1260 0.0012  0.0026  0.0167  125 PRO   A CA  
2497 C CA  B PRO   A 125 ? 0.1433 0.1439 0.1413 -0.0037 0.0176  0.0094  125 PRO   A CA  
2498 C C   A PRO   A 125 ? 0.1212 0.1377 0.1368 -0.0008 0.0014  0.0186  125 PRO   A C   
2499 C C   B PRO   A 125 ? 0.1435 0.1456 0.1434 -0.0033 0.0125  0.0132  125 PRO   A C   
2500 O O   A PRO   A 125 ? 0.1285 0.1388 0.1466 0.0091  0.0056  0.0126  125 PRO   A O   
2501 O O   B PRO   A 125 ? 0.1459 0.1438 0.1463 -0.0041 0.0128  0.0256  125 PRO   A O   
2502 C CB  A PRO   A 125 ? 0.1344 0.1200 0.1097 -0.0013 0.0145  0.0089  125 PRO   A CB  
2503 C CB  B PRO   A 125 ? 0.1476 0.1435 0.1425 -0.0048 0.0246  0.0027  125 PRO   A CB  
2504 C CG  A PRO   A 125 ? 0.1267 0.1147 0.1269 0.0008  0.0173  0.0211  125 PRO   A CG  
2505 C CG  B PRO   A 125 ? 0.1479 0.1471 0.1566 -0.0059 0.0170  0.0078  125 PRO   A CG  
2506 C CD  A PRO   A 125 ? 0.1264 0.1245 0.1267 -0.0058 0.0182  0.0232  125 PRO   A CD  
2507 C CD  B PRO   A 125 ? 0.1354 0.1459 0.1489 -0.0016 0.0273  0.0152  125 PRO   A CD  
2522 N N   A LEU   A 126 ? 0.1175 0.1392 0.1352 0.0041  0.0106  0.0169  126 LEU   A N   
2523 N N   B LEU   A 126 ? 0.1500 0.1541 0.1523 -0.0044 0.0172  0.0080  126 LEU   A N   
2524 C CA  A LEU   A 126 ? 0.1277 0.1323 0.1404 -0.0054 0.0110  0.0116  126 LEU   A CA  
2525 C CA  B LEU   A 126 ? 0.1461 0.1463 0.1524 -0.0026 0.0230  0.0031  126 LEU   A CA  
2526 C C   A LEU   A 126 ? 0.1359 0.1254 0.1461 -0.0068 0.0011  0.0105  126 LEU   A C   
2527 C C   B LEU   A 126 ? 0.1435 0.1339 0.1586 0.0035  0.0246  -0.0000 126 LEU   A C   
2528 O O   A LEU   A 126 ? 0.1532 0.1221 0.1581 -0.0071 0.0143  0.0048  126 LEU   A O   
2529 O O   B LEU   A 126 ? 0.1614 0.1266 0.1799 -0.0026 0.0413  -0.0019 126 LEU   A O   
2530 C CB  A LEU   A 126 ? 0.1363 0.1322 0.1466 -0.0006 0.0038  0.0081  126 LEU   A CB  
2531 C CB  B LEU   A 126 ? 0.1486 0.1553 0.1723 -0.0116 0.0212  0.0063  126 LEU   A CB  
2532 C CG  A LEU   A 126 ? 0.1404 0.1491 0.1733 -0.0049 0.0013  0.0042  126 LEU   A CG  
2533 C CG  B LEU   A 126 ? 0.1475 0.1533 0.1897 -0.0114 0.0136  0.0073  126 LEU   A CG  
2534 C CD1 A LEU   A 126 ? 0.1460 0.1638 0.2110 -0.0107 -0.0070 0.0067  126 LEU   A CD1 
2535 C CD1 B LEU   A 126 ? 0.1483 0.1530 0.1980 -0.0115 0.0058  -0.0093 126 LEU   A CD1 
2536 C CD2 A LEU   A 126 ? 0.1416 0.1488 0.1642 -0.0147 -0.0061 0.0100  126 LEU   A CD2 
2537 C CD2 B LEU   A 126 ? 0.1458 0.1511 0.2090 -0.0107 -0.0012 0.0211  126 LEU   A CD2 
2560 N N   A LEU   A 127 ? 0.1333 0.1351 0.1343 -0.0018 0.0036  0.0138  127 LEU   A N   
2561 N N   B LEU   A 127 ? 0.1290 0.1327 0.1458 0.0057  0.0120  0.0110  127 LEU   A N   
2562 C CA  A LEU   A 127 ? 0.1328 0.1391 0.1246 -0.0059 0.0010  0.0094  127 LEU   A CA  
2563 C CA  B LEU   A 127 ? 0.1243 0.1385 0.1393 0.0096  0.0024  0.0185  127 LEU   A CA  
2564 C C   A LEU   A 127 ? 0.1348 0.1347 0.1308 -0.0099 -0.0085 0.0069  127 LEU   A C   
2565 C C   B LEU   A 127 ? 0.1296 0.1377 0.1416 0.0093  -0.0092 0.0112  127 LEU   A C   
2566 O O   A LEU   A 127 ? 0.1402 0.1351 0.1117 -0.0167 0.0040  0.0075  127 LEU   A O   
2567 O O   B LEU   A 127 ? 0.1369 0.1469 0.1465 0.0077  -0.0022 0.0164  127 LEU   A O   
2568 C CB  A LEU   A 127 ? 0.1409 0.1423 0.1488 0.0046  0.0084  0.0060  127 LEU   A CB  
2569 C CB  B LEU   A 127 ? 0.1248 0.1493 0.1395 0.0083  0.0008  0.0123  127 LEU   A CB  
2570 C CG  A LEU   A 127 ? 0.1516 0.1445 0.1599 0.0072  -0.0010 0.0055  127 LEU   A CG  
2571 C CG  B LEU   A 127 ? 0.1273 0.1595 0.1460 0.0166  -0.0129 0.0169  127 LEU   A CG  
2572 C CD1 A LEU   A 127 ? 0.1542 0.1373 0.1690 0.0039  0.0053  0.0006  127 LEU   A CD1 
2573 C CD1 B LEU   A 127 ? 0.1319 0.1603 0.1639 0.0181  -0.0019 0.0235  127 LEU   A CD1 
2574 C CD2 A LEU   A 127 ? 0.1633 0.1461 0.1651 0.0214  -0.0034 0.0097  127 LEU   A CD2 
2575 C CD2 B LEU   A 127 ? 0.1327 0.1731 0.1340 0.0204  -0.0257 0.0073  127 LEU   A CD2 
2598 N N   A SER   A 128 ? 0.1425 0.1393 0.1282 -0.0113 0.0035  0.0073  128 SER   A N   
2599 N N   B SER   A 128 ? 0.1342 0.1371 0.1418 0.0036  -0.0101 0.0067  128 SER   A N   
2600 C CA  A SER   A 128 ? 0.1503 0.1427 0.1158 -0.0076 0.0085  0.0147  128 SER   A CA  
2601 C CA  B SER   A 128 ? 0.1382 0.1358 0.1279 0.0055  -0.0119 0.0106  128 SER   A CA  
2602 C C   A SER   A 128 ? 0.1564 0.1541 0.1192 -0.0048 0.0089  0.0159  128 SER   A C   
2603 C C   B SER   A 128 ? 0.1341 0.1381 0.1292 0.0083  -0.0217 0.0116  128 SER   A C   
2604 O O   A SER   A 128 ? 0.1664 0.1691 0.1325 -0.0082 0.0054  0.0132  128 SER   A O   
2605 O O   B SER   A 128 ? 0.1267 0.1370 0.1270 0.0117  -0.0160 0.0068  128 SER   A O   
2606 C CB  A SER   A 128 ? 0.1507 0.1415 0.1218 -0.0143 0.0062  0.0160  128 SER   A CB  
2607 C CB  B SER   A 128 ? 0.1467 0.1423 0.1297 0.0019  -0.0065 0.0129  128 SER   A CB  
2608 O OG  A SER   A 128 ? 0.1500 0.1451 0.1241 -0.0099 0.0010  0.0089  128 SER   A OG  
2609 O OG  B SER   A 128 ? 0.1484 0.1449 0.1217 -0.0006 0.0081  0.0204  128 SER   A OG  
2620 N N   A ALA   A 129 ? 0.1490 0.1599 0.1435 -0.0071 0.0123  0.0204  129 ALA   A N   
2621 N N   B ALA   A 129 ? 0.1308 0.1451 0.1320 0.0084  -0.0268 0.0176  129 ALA   A N   
2622 C CA  A ALA   A 129 ? 0.1437 0.1610 0.1542 -0.0040 0.0097  0.0183  129 ALA   A CA  
2623 C CA  B ALA   A 129 ? 0.1355 0.1547 0.1306 0.0125  -0.0167 0.0256  129 ALA   A CA  
2624 C C   A ALA   A 129 ? 0.1414 0.1566 0.1281 -0.0023 0.0097  -0.0011 129 ALA   A C   
2625 C C   B ALA   A 129 ? 0.1382 0.1639 0.1323 0.0094  -0.0144 0.0197  129 ALA   A C   
2626 O O   A ALA   A 129 ? 0.1437 0.1618 0.1222 0.0008  0.0057  0.0084  129 ALA   A O   
2627 O O   B ALA   A 129 ? 0.1380 0.1710 0.1489 0.0101  -0.0108 0.0254  129 ALA   A O   
2628 C CB  A ALA   A 129 ? 0.1474 0.1728 0.1919 0.0024  0.0091  0.0304  129 ALA   A CB  
2629 C CB  B ALA   A 129 ? 0.1396 0.1619 0.1267 0.0132  -0.0098 0.0178  129 ALA   A CB  
2640 N N   A GLY   A 130 ? 0.1415 0.1561 0.1474 -0.0026 0.0118  0.0004  130 GLY   A N   
2641 N N   B GLY   A 130 ? 0.1399 0.1687 0.1322 0.0059  -0.0177 0.0222  130 GLY   A N   
2642 C CA  A GLY   A 130 ? 0.1541 0.1541 0.1415 0.0003  0.0046  -0.0001 130 GLY   A CA  
2643 C CA  B GLY   A 130 ? 0.1409 0.1666 0.1331 -0.0059 -0.0070 0.0128  130 GLY   A CA  
2644 C C   A GLY   A 130 ? 0.1545 0.1450 0.1173 0.0047  -0.0034 0.0068  130 GLY   A C   
2645 C C   B GLY   A 130 ? 0.1439 0.1664 0.1406 -0.0003 -0.0154 0.0122  130 GLY   A C   
2646 O O   A GLY   A 130 ? 0.1569 0.1419 0.1227 -0.0020 -0.0047 0.0101  130 GLY   A O   
2647 O O   B GLY   A 130 ? 0.1495 0.1674 0.1514 0.0038  -0.0182 0.0217  130 GLY   A O   
2654 N N   A ILE   A 131 ? 0.1608 0.1412 0.1323 -0.0034 -0.0035 0.0115  131 ILE   A N   
2655 N N   B ILE   A 131 ? 0.1417 0.1651 0.1458 -0.0044 -0.0061 0.0137  131 ILE   A N   
2656 C CA  A ILE   A 131 ? 0.1720 0.1484 0.1104 -0.0025 -0.0143 0.0039  131 ILE   A CA  
2657 C CA  B ILE   A 131 ? 0.1459 0.1678 0.1418 -0.0022 -0.0120 0.0206  131 ILE   A CA  
2658 C C   A ILE   A 131 ? 0.1757 0.1484 0.1119 0.0015  -0.0109 0.0132  131 ILE   A C   
2659 C C   B ILE   A 131 ? 0.1381 0.1633 0.1443 -0.0035 -0.0047 0.0263  131 ILE   A C   
2660 O O   A ILE   A 131 ? 0.1806 0.1477 0.1335 0.0038  -0.0096 0.0157  131 ILE   A O   
2661 O O   B ILE   A 131 ? 0.1447 0.1616 0.1454 -0.0057 0.0092  0.0297  131 ILE   A O   
2662 C CB  A ILE   A 131 ? 0.1841 0.1654 0.1386 -0.0073 -0.0133 -0.0119 131 ILE   A CB  
2663 C CB  B ILE   A 131 ? 0.1555 0.1787 0.1531 -0.0017 -0.0129 0.0114  131 ILE   A CB  
2664 C CG1 A ILE   A 131 ? 0.1900 0.2001 0.1611 -0.0143 -0.0209 -0.0261 131 ILE   A CG1 
2665 C CG1 B ILE   A 131 ? 0.1601 0.1927 0.1663 -0.0062 -0.0168 0.0030  131 ILE   A CG1 
2666 C CG2 A ILE   A 131 ? 0.1904 0.1534 0.1749 -0.0026 0.0028  -0.0221 131 ILE   A CG2 
2667 C CG2 B ILE   A 131 ? 0.1597 0.1780 0.1649 0.0014  -0.0055 0.0059  131 ILE   A CG2 
2668 C CD1 A ILE   A 131 ? 0.1986 0.2176 0.2054 -0.0155 -0.0182 -0.0333 131 ILE   A CD1 
2669 C CD1 B ILE   A 131 ? 0.1662 0.1969 0.1837 -0.0088 -0.0077 -0.0056 131 ILE   A CD1 
2692 N N   A PHE   A 132 ? 0.1765 0.1510 0.0952 -0.0027 0.0025  0.0139  132 PHE   A N   
2693 N N   B PHE   A 132 ? 0.1331 0.1609 0.1573 0.0067  -0.0111 0.0124  132 PHE   A N   
2694 C CA  A PHE   A 132 ? 0.1754 0.1588 0.0981 -0.0050 0.0060  0.0049  132 PHE   A CA  
2695 C CA  B PHE   A 132 ? 0.1407 0.1618 0.1637 0.0079  -0.0148 0.0044  132 PHE   A CA  
2696 C C   A PHE   A 132 ? 0.1682 0.1778 0.0931 -0.0037 0.0054  0.0066  132 PHE   A C   
2697 C C   B PHE   A 132 ? 0.1501 0.1682 0.1757 0.0121  -0.0132 0.0035  132 PHE   A C   
2698 O O   A PHE   A 132 ? 0.1750 0.1950 0.1188 -0.0025 0.0022  0.0017  132 PHE   A O   
2699 O O   B PHE   A 132 ? 0.1643 0.1787 0.1956 0.0133  -0.0055 0.0031  132 PHE   A O   
2700 C CB  A PHE   A 132 ? 0.1739 0.1456 0.1087 -0.0011 -0.0004 0.0122  132 PHE   A CB  
2701 C CB  B PHE   A 132 ? 0.1388 0.1602 0.1473 0.0051  -0.0169 0.0133  132 PHE   A CB  
2702 C CG  A PHE   A 132 ? 0.1747 0.1475 0.1076 -0.0028 -0.0061 0.0137  132 PHE   A CG  
2703 C CG  B PHE   A 132 ? 0.1433 0.1604 0.1393 0.0024  -0.0170 0.0079  132 PHE   A CG  
2704 C CD1 A PHE   A 132 ? 0.1798 0.1559 0.1373 -0.0027 -0.0084 0.0014  132 PHE   A CD1 
2705 C CD1 B PHE   A 132 ? 0.1480 0.1662 0.1529 0.0080  -0.0143 0.0016  132 PHE   A CD1 
2706 C CD2 A PHE   A 132 ? 0.1744 0.1598 0.1371 -0.0003 -0.0069 0.0091  132 PHE   A CD2 
2707 C CD2 B PHE   A 132 ? 0.1430 0.1625 0.1413 0.0038  -0.0202 0.0013  132 PHE   A CD2 
2708 C CE1 A PHE   A 132 ? 0.1824 0.1624 0.1381 -0.0003 -0.0110 -0.0044 132 PHE   A CE1 
2709 C CE1 B PHE   A 132 ? 0.1482 0.1684 0.1463 0.0107  -0.0091 -0.0042 132 PHE   A CE1 
2710 C CE2 A PHE   A 132 ? 0.1745 0.1662 0.1543 0.0025  -0.0093 0.0034  132 PHE   A CE2 
2711 C CE2 B PHE   A 132 ? 0.1409 0.1673 0.1398 0.0078  -0.0168 -0.0037 132 PHE   A CE2 
2712 C CZ  A PHE   A 132 ? 0.1766 0.1650 0.1490 -0.0049 -0.0189 0.0020  132 PHE   A CZ  
2713 C CZ  B PHE   A 132 ? 0.1421 0.1669 0.1357 0.0051  -0.0144 -0.0031 132 PHE   A CZ  
2732 N N   A GLY   A 133 ? 0.1669 0.1798 0.0959 -0.0045 -0.0013 0.0054  133 GLY   A N   
2733 N N   B GLY   A 133 ? 0.1506 0.1643 0.1612 0.0108  -0.0171 0.0049  133 GLY   A N   
2734 C CA  A GLY   A 133 ? 0.1790 0.1871 0.1075 -0.0146 -0.0108 0.0066  133 GLY   A CA  
2735 C CA  B GLY   A 133 ? 0.1568 0.1656 0.1454 0.0079  -0.0179 0.0017  133 GLY   A CA  
2736 C C   A GLY   A 133 ? 0.1939 0.1981 0.1320 -0.0190 -0.0260 0.0028  133 GLY   A C   
2737 C C   B GLY   A 133 ? 0.1626 0.1738 0.1488 0.0090  -0.0305 -0.0129 133 GLY   A C   
2738 O O   A GLY   A 133 ? 0.2042 0.2133 0.1467 -0.0176 -0.0279 -0.0111 133 GLY   A O   
2739 O O   B GLY   A 133 ? 0.1610 0.1856 0.1359 0.0163  -0.0326 -0.0361 133 GLY   A O   
2746 N N   A ALA   A 134 ? 0.1939 0.1914 0.1287 -0.0245 -0.0218 0.0075  134 ALA   A N   
2747 N N   B ALA   A 134 ? 0.1676 0.1685 0.1560 0.0045  -0.0229 -0.0108 134 ALA   A N   
2748 C CA  A ALA   A 134 ? 0.1913 0.1891 0.1601 -0.0228 -0.0329 0.0046  134 ALA   A CA  
2749 C CA  B ALA   A 134 ? 0.1693 0.1633 0.1647 -0.0018 -0.0152 -0.0114 134 ALA   A CA  
2750 C C   A ALA   A 134 ? 0.1912 0.1863 0.1743 -0.0177 -0.0415 0.0077  134 ALA   A C   
2751 C C   B ALA   A 134 ? 0.1722 0.1568 0.1683 -0.0014 -0.0136 -0.0069 134 ALA   A C   
2752 O O   A ALA   A 134 ? 0.1978 0.1889 0.2011 -0.0168 -0.0253 0.0034  134 ALA   A O   
2753 O O   B ALA   A 134 ? 0.1743 0.1565 0.1918 -0.0029 0.0061  -0.0006 134 ALA   A O   
2754 C CB  A ALA   A 134 ? 0.1999 0.1938 0.2033 -0.0186 -0.0291 0.0060  134 ALA   A CB  
2755 C CB  B ALA   A 134 ? 0.1730 0.1644 0.1822 -0.0046 -0.0150 -0.0146 134 ALA   A CB  
2766 N N   A ASP   A 135 ? 0.1918 0.1847 0.1902 -0.0134 -0.0442 0.0160  135 ASP   A N   
2767 N N   B ASP   A 135 ? 0.1778 0.1590 0.1713 -0.0032 -0.0228 -0.0060 135 ASP   A N   
2768 C CA  A ASP   A 135 ? 0.1875 0.1873 0.2093 -0.0124 -0.0538 0.0122  135 ASP   A CA  
2769 C CA  B ASP   A 135 ? 0.1794 0.1594 0.1921 -0.0038 -0.0325 -0.0061 135 ASP   A CA  
2770 C C   A ASP   A 135 ? 0.1713 0.1731 0.2035 -0.0076 -0.0357 0.0235  135 ASP   A C   
2771 C C   B ASP   A 135 ? 0.1689 0.1457 0.1882 0.0005  -0.0225 -0.0095 135 ASP   A C   
2772 O O   A ASP   A 135 ? 0.1660 0.1686 0.2132 -0.0117 -0.0261 0.0359  135 ASP   A O   
2773 O O   B ASP   A 135 ? 0.1634 0.1365 0.1931 -0.0030 -0.0200 -0.0043 135 ASP   A O   
2774 C CB  A ASP   A 135 ? 0.2067 0.2154 0.2359 -0.0277 -0.0677 -0.0034 135 ASP   A CB  
2775 C CB  B ASP   A 135 ? 0.1934 0.1784 0.2066 -0.0085 -0.0447 -0.0090 135 ASP   A CB  
2776 C CG  A ASP   A 135 ? 0.2213 0.2373 0.2740 -0.0470 -0.0642 -0.0126 135 ASP   A CG  
2777 C CG  B ASP   A 135 ? 0.2056 0.1977 0.2375 -0.0103 -0.0490 -0.0073 135 ASP   A CG  
2778 O OD1 A ASP   A 135 ? 0.2121 0.2415 0.2848 -0.0584 -0.0717 0.0055  135 ASP   A OD1 
2779 O OD1 B ASP   A 135 ? 0.2099 0.1992 0.2508 -0.0038 -0.0526 -0.0081 135 ASP   A OD1 
2780 O OD2 A ASP   A 135 ? 0.2518 0.2589 0.3202 -0.0475 -0.0394 -0.0210 135 ASP   A OD2 
2781 O OD2 B ASP   A 135 ? 0.2105 0.2119 0.2647 -0.0144 -0.0549 -0.0056 135 ASP   A OD2 
2790 N N   A PRO   A 136 ? 0.1569 0.1586 0.2174 -0.0026 -0.0219 0.0251  136 PRO   A N   
2791 N N   B PRO   A 136 ? 0.1643 0.1388 0.1954 0.0056  -0.0041 -0.0160 136 PRO   A N   
2792 C CA  A PRO   A 136 ? 0.1521 0.1600 0.2266 -0.0096 -0.0088 0.0158  136 PRO   A CA  
2793 C CA  B PRO   A 136 ? 0.1597 0.1448 0.1921 0.0020  0.0016  -0.0279 136 PRO   A CA  
2794 C C   A PRO   A 136 ? 0.1395 0.1623 0.2169 0.0002  -0.0124 0.0144  136 PRO   A C   
2795 C C   B PRO   A 136 ? 0.1467 0.1507 0.1847 0.0040  0.0053  -0.0171 136 PRO   A C   
2796 O O   A PRO   A 136 ? 0.1364 0.1689 0.2074 -0.0036 -0.0119 0.0156  136 PRO   A O   
2797 O O   B PRO   A 136 ? 0.1369 0.1462 0.1601 0.0102  0.0227  -0.0118 136 PRO   A O   
2798 C CB  A PRO   A 136 ? 0.1683 0.1601 0.2489 -0.0047 -0.0075 0.0126  136 PRO   A CB  
2799 C CB  B PRO   A 136 ? 0.1735 0.1435 0.2065 0.0019  -0.0050 -0.0333 136 PRO   A CB  
2800 C CG  A PRO   A 136 ? 0.1757 0.1622 0.2652 0.0002  -0.0104 0.0176  136 PRO   A CG  
2801 C CG  B PRO   A 136 ? 0.1797 0.1431 0.2296 0.0076  -0.0037 -0.0269 136 PRO   A CG  
2802 C CD  A PRO   A 136 ? 0.1668 0.1558 0.2487 0.0024  -0.0148 0.0274  136 PRO   A CD  
2803 C CD  B PRO   A 136 ? 0.1709 0.1365 0.2222 0.0086  0.0007  -0.0167 136 PRO   A CD  
2818 N N   A ILE   A 137 ? 0.1360 0.1564 0.2166 0.0018  -0.0158 0.0106  137 ILE   A N   
2819 N N   B ILE   A 137 ? 0.1446 0.1524 0.1918 0.0018  -0.0027 -0.0178 137 ILE   A N   
2820 C CA  A ILE   A 137 ? 0.1431 0.1572 0.2294 -0.0091 -0.0201 0.0208  137 ILE   A CA  
2821 C CA  B ILE   A 137 ? 0.1450 0.1556 0.1938 0.0035  0.0006  -0.0187 137 ILE   A CA  
2822 C C   A ILE   A 137 ? 0.1503 0.1563 0.2147 -0.0101 -0.0261 0.0223  137 ILE   A C   
2823 C C   B ILE   A 137 ? 0.1405 0.1521 0.1872 -0.0028 0.0067  -0.0189 137 ILE   A C   
2824 O O   A ILE   A 137 ? 0.1575 0.1528 0.2196 -0.0094 -0.0198 0.0288  137 ILE   A O   
2825 O O   B ILE   A 137 ? 0.1337 0.1539 0.1917 0.0007  0.0173  -0.0123 137 ILE   A O   
2826 C CB  A ILE   A 137 ? 0.1486 0.1646 0.2676 -0.0146 -0.0416 0.0210  137 ILE   A CB  
2827 C CB  B ILE   A 137 ? 0.1586 0.1625 0.2281 0.0020  -0.0101 -0.0030 137 ILE   A CB  
2828 C CG1 A ILE   A 137 ? 0.1585 0.1923 0.3167 -0.0143 -0.0426 0.0368  137 ILE   A CG1 
2829 C CG1 B ILE   A 137 ? 0.1674 0.1714 0.2567 0.0084  -0.0334 0.0078  137 ILE   A CG1 
2830 C CG2 A ILE   A 137 ? 0.1606 0.1659 0.2909 -0.0226 -0.0512 0.0165  137 ILE   A CG2 
2831 C CG2 B ILE   A 137 ? 0.1667 0.1564 0.2426 0.0037  -0.0164 0.0008  137 ILE   A CG2 
2832 C CD1 A ILE   A 137 ? 0.1754 0.2090 0.3423 -0.0079 -0.0284 0.0447  137 ILE   A CD1 
2833 C CD1 B ILE   A 137 ? 0.1790 0.1736 0.2729 0.0104  -0.0404 0.0154  137 ILE   A CD1 
2856 N N   A HIS   A 138 ? 0.1505 0.1577 0.1926 -0.0071 -0.0201 0.0134  138 HIS   A N   
2857 N N   B HIS   A 138 ? 0.1436 0.1512 0.1835 -0.0066 0.0122  -0.0175 138 HIS   A N   
2858 C CA  A HIS   A 138 ? 0.1581 0.1640 0.1836 -0.0049 -0.0085 0.0091  138 HIS   A CA  
2859 C CA  B HIS   A 138 ? 0.1454 0.1400 0.1677 -0.0084 0.0010  -0.0156 138 HIS   A CA  
2860 C C   A HIS   A 138 ? 0.1472 0.1625 0.1754 -0.0028 0.0009  0.0149  138 HIS   A C   
2861 C C   B HIS   A 138 ? 0.1408 0.1283 0.1760 -0.0033 -0.0020 -0.0162 138 HIS   A C   
2862 O O   A HIS   A 138 ? 0.1557 0.1640 0.1791 -0.0105 -0.0038 0.0226  138 HIS   A O   
2863 O O   B HIS   A 138 ? 0.1528 0.1297 0.1774 -0.0005 -0.0026 -0.0190 138 HIS   A O   
2864 C CB  A HIS   A 138 ? 0.1793 0.1804 0.1846 -0.0057 -0.0186 -0.0006 138 HIS   A CB  
2865 C CB  B HIS   A 138 ? 0.1547 0.1503 0.1659 -0.0024 -0.0004 -0.0226 138 HIS   A CB  
2866 C CG  A HIS   A 138 ? 0.1980 0.1950 0.1935 -0.0091 -0.0127 -0.0001 138 HIS   A CG  
2867 C CG  B HIS   A 138 ? 0.1630 0.1586 0.1738 -0.0016 -0.0012 -0.0260 138 HIS   A CG  
2868 N ND1 A HIS   A 138 ? 0.2102 0.2071 0.2253 -0.0082 -0.0063 -0.0043 138 HIS   A ND1 
2869 N ND1 B HIS   A 138 ? 0.1678 0.1654 0.1912 0.0056  -0.0008 -0.0307 138 HIS   A ND1 
2870 C CD2 A HIS   A 138 ? 0.2044 0.2006 0.1900 -0.0075 -0.0076 0.0161  138 HIS   A CD2 
2871 C CD2 B HIS   A 138 ? 0.1680 0.1615 0.1861 0.0018  0.0001  -0.0181 138 HIS   A CD2 
2872 C CE1 A HIS   A 138 ? 0.2188 0.2136 0.2365 0.0018  -0.0052 0.0013  138 HIS   A CE1 
2873 C CE1 B HIS   A 138 ? 0.1735 0.1666 0.1984 0.0124  0.0010  -0.0327 138 HIS   A CE1 
2874 N NE2 A HIS   A 138 ? 0.2136 0.2116 0.2095 0.0010  -0.0006 0.0145  138 HIS   A NE2 
2875 N NE2 B HIS   A 138 ? 0.1735 0.1655 0.1951 0.0091  0.0016  -0.0226 138 HIS   A NE2 
2890 N N   A SER   A 139 ? 0.1416 0.1578 0.1638 -0.0007 -0.0012 0.0158  139 SER   A N   
2891 N N   B SER   A 139 ? 0.1353 0.1277 0.1843 -0.0076 0.0019  -0.0060 139 SER   A N   
2892 C CA  A SER   A 139 ? 0.1411 0.1561 0.1646 -0.0030 0.0023  0.0180  139 SER   A CA  
2893 C CA  B SER   A 139 ? 0.1283 0.1358 0.1670 0.0012  0.0041  -0.0045 139 SER   A CA  
2894 C C   A SER   A 139 ? 0.1318 0.1501 0.1841 -0.0034 0.0065  0.0201  139 SER   A C   
2895 C C   B SER   A 139 ? 0.1244 0.1383 0.1643 -0.0027 0.0044  -0.0091 139 SER   A C   
2896 O O   A SER   A 139 ? 0.1273 0.1339 0.1827 -0.0082 0.0047  0.0171  139 SER   A O   
2897 O O   B SER   A 139 ? 0.1229 0.1326 0.1720 -0.0063 -0.0009 -0.0061 139 SER   A O   
2898 C CB  A SER   A 139 ? 0.1361 0.1534 0.1544 -0.0053 0.0092  0.0021  139 SER   A CB  
2899 C CB  B SER   A 139 ? 0.1263 0.1341 0.1493 0.0024  0.0019  -0.0015 139 SER   A CB  
2900 O OG  A SER   A 139 ? 0.1337 0.1480 0.1519 -0.0144 0.0048  0.0087  139 SER   A OG  
2901 O OG  B SER   A 139 ? 0.1271 0.1302 0.1551 0.0007  0.0010  0.0004  139 SER   A OG  
2912 N N   A LEU   A 140 ? 0.1252 0.1660 0.1857 -0.0037 -0.0019 0.0379  140 LEU   A N   
2913 N N   B LEU   A 140 ? 0.1243 0.1537 0.1644 -0.0076 0.0044  0.0081  140 LEU   A N   
2914 C CA  A LEU   A 140 ? 0.1306 0.1636 0.1792 -0.0068 0.0031  0.0341  140 LEU   A CA  
2915 C CA  B LEU   A 140 ? 0.1311 0.1563 0.1580 -0.0099 0.0024  0.0132  140 LEU   A CA  
2916 C C   A LEU   A 140 ? 0.1285 0.1714 0.1834 -0.0137 0.0039  0.0307  140 LEU   A C   
2917 C C   B LEU   A 140 ? 0.1297 0.1655 0.1752 -0.0122 -0.0009 0.0205  140 LEU   A C   
2918 O O   A LEU   A 140 ? 0.1311 0.1757 0.1987 -0.0071 0.0012  0.0311  140 LEU   A O   
2919 O O   B LEU   A 140 ? 0.1309 0.1664 0.1820 -0.0074 -0.0052 0.0229  140 LEU   A O   
2920 C CB  A LEU   A 140 ? 0.1327 0.1675 0.1852 -0.0106 0.0090  0.0356  140 LEU   A CB  
2921 C CB  B LEU   A 140 ? 0.1373 0.1577 0.1581 -0.0119 0.0045  0.0154  140 LEU   A CB  
2922 C CG  A LEU   A 140 ? 0.1307 0.1715 0.2027 -0.0082 0.0117  0.0425  140 LEU   A CG  
2923 C CG  B LEU   A 140 ? 0.1427 0.1581 0.1669 -0.0111 0.0054  0.0252  140 LEU   A CG  
2924 C CD1 A LEU   A 140 ? 0.1320 0.1494 0.2001 -0.0013 0.0057  0.0325  140 LEU   A CD1 
2925 C CD1 B LEU   A 140 ? 0.1449 0.1491 0.1625 -0.0068 0.0065  0.0240  140 LEU   A CD1 
2926 C CD2 A LEU   A 140 ? 0.1366 0.1945 0.2074 -0.0046 0.0156  0.0441  140 LEU   A CD2 
2927 C CD2 B LEU   A 140 ? 0.1457 0.1704 0.1751 -0.0118 0.0117  0.0291  140 LEU   A CD2 
2950 N N   . ARG   A 141 ? 0.1310 0.1724 0.1935 -0.0127 0.0001  0.0253  141 ARG   A N   
2951 C CA  . ARG   A 141 ? 0.1496 0.1830 0.2062 -0.0203 -0.0022 0.0090  141 ARG   A CA  
2952 C C   . ARG   A 141 ? 0.1472 0.1614 0.1918 -0.0169 -0.0080 0.0084  141 ARG   A C   
2953 O O   . ARG   A 141 ? 0.1414 0.1625 0.2036 -0.0174 0.0059  0.0046  141 ARG   A O   
2954 C CB  . ARG   A 141 ? 0.1664 0.2042 0.2430 -0.0239 -0.0004 -0.0009 141 ARG   A CB  
2955 C CG  . ARG   A 141 ? 0.1985 0.2343 0.2760 -0.0282 0.0090  -0.0092 141 ARG   A CG  
2956 C CD  . ARG   A 141 ? 0.2144 0.2527 0.3024 -0.0308 -0.0017 -0.0240 141 ARG   A CD  
2957 N NE  . ARG   A 141 ? 0.1964 0.2624 0.3046 -0.0246 -0.0060 -0.0167 141 ARG   A NE  
2958 C CZ  . ARG   A 141 ? 0.1951 0.2803 0.3112 -0.0286 0.0168  -0.0087 141 ARG   A CZ  
2959 N NH1 . ARG   A 141 ? 0.1912 0.2907 0.3034 -0.0391 0.0521  -0.0283 141 ARG   A NH1 
2960 N NH2 . ARG   A 141 ? 0.1980 0.2891 0.3337 -0.0118 -0.0034 0.0132  141 ARG   A NH2 
2975 N N   . VAL   A 142 ? 0.1419 0.1564 0.1817 -0.0139 -0.0063 0.0041  142 VAL   A N   
2976 C CA  . VAL   A 142 ? 0.1430 0.1561 0.1872 -0.0096 0.0120  0.0112  142 VAL   A CA  
2977 C C   . VAL   A 142 ? 0.1271 0.1539 0.1891 -0.0130 0.0099  0.0096  142 VAL   A C   
2978 O O   . VAL   A 142 ? 0.1350 0.1596 0.1826 0.0002  0.0084  0.0121  142 VAL   A O   
2979 C CB  . VAL   A 142 ? 0.1488 0.1690 0.1762 -0.0057 0.0154  0.0073  142 VAL   A CB  
2980 C CG1 . VAL   A 142 ? 0.1475 0.1693 0.1813 -0.0088 0.0209  0.0083  142 VAL   A CG1 
2981 C CG2 . VAL   A 142 ? 0.1527 0.1829 0.1980 0.0023  0.0091  0.0164  142 VAL   A CG2 
2991 N N   . CYS   A 143 ? 0.1302 0.1542 0.1718 -0.0140 0.0038  0.0107  143 CYS   A N   
2992 C CA  . CYS   A 143 ? 0.1337 0.1547 0.1848 -0.0173 0.0073  0.0124  143 CYS   A CA  
2993 C C   . CYS   A 143 ? 0.1271 0.1512 0.1958 -0.0134 0.0047  0.0242  143 CYS   A C   
2994 O O   . CYS   A 143 ? 0.1295 0.1507 0.1877 -0.0069 0.0014  0.0228  143 CYS   A O   
2995 C CB  . CYS   A 143 ? 0.1369 0.1548 0.1882 -0.0059 0.0169  0.0178  143 CYS   A CB  
2996 S SG  . CYS   A 143 ? 0.1568 0.1586 0.1789 0.0008  0.0122  0.0133  143 CYS   A SG  
3002 N N   . VAL   A 144 ? 0.1267 0.1550 0.2110 -0.0095 0.0091  0.0332  144 VAL   A N   
3003 C CA  . VAL   A 144 ? 0.1358 0.1657 0.2394 -0.0139 0.0182  0.0317  144 VAL   A CA  
3004 C C   . VAL   A 144 ? 0.1346 0.1556 0.2362 -0.0212 -0.0067 0.0232  144 VAL   A C   
3005 O O   . VAL   A 144 ? 0.1470 0.1559 0.2435 -0.0100 -0.0042 0.0229  144 VAL   A O   
3006 C CB  . VAL   A 144 ? 0.1551 0.1922 0.2859 -0.0083 0.0351  0.0331  144 VAL   A CB  
3007 C CG1 . VAL   A 144 ? 0.1706 0.2104 0.3331 -0.0191 0.0157  0.0303  144 VAL   A CG1 
3008 C CG2 . VAL   A 144 ? 0.1396 0.1991 0.2890 -0.0021 0.0363  0.0503  144 VAL   A CG2 
3018 N N   . ASP   A 145 ? 0.1422 0.1531 0.2472 -0.0171 0.0005  0.0093  145 ASP   A N   
3019 C CA  . ASP   A 145 ? 0.1538 0.1607 0.2391 -0.0260 -0.0030 0.0023  145 ASP   A CA  
3020 C C   . ASP   A 145 ? 0.1547 0.1494 0.2194 -0.0141 -0.0030 -0.0070 145 ASP   A C   
3021 O O   . ASP   A 145 ? 0.1647 0.1593 0.2799 -0.0160 -0.0005 -0.0329 145 ASP   A O   
3022 C CB  . ASP   A 145 ? 0.1667 0.1920 0.2697 -0.0423 -0.0210 0.0081  145 ASP   A CB  
3023 C CG  . ASP   A 145 ? 0.1884 0.2369 0.2901 -0.0556 -0.0317 0.0152  145 ASP   A CG  
3024 O OD1 . ASP   A 145 ? 0.1749 0.2473 0.2978 -0.0680 -0.0092 0.0239  145 ASP   A OD1 
3025 O OD2 . ASP   A 145 ? 0.2088 0.2655 0.2988 -0.0650 -0.0616 0.0076  145 ASP   A OD2 
3030 N N   . THR   A 146 ? 0.1367 0.1484 0.2006 -0.0117 0.0049  0.0006  146 THR   A N   
3031 C CA  . THR   A 146 ? 0.1333 0.1434 0.1946 -0.0114 0.0002  0.0001  146 THR   A CA  
3032 C C   . THR   A 146 ? 0.1300 0.1353 0.1957 -0.0068 0.0121  0.0114  146 THR   A C   
3033 O O   . THR   A 146 ? 0.1399 0.1479 0.2068 0.0059  -0.0029 0.0082  146 THR   A O   
3034 C CB  . THR   A 146 ? 0.1356 0.1442 0.1945 -0.0127 0.0067  0.0091  146 THR   A CB  
3035 O OG1 . THR   A 146 ? 0.1354 0.1579 0.1865 -0.0075 -0.0001 0.0042  146 THR   A OG1 
3036 C CG2 . THR   A 146 ? 0.1385 0.1453 0.2152 -0.0153 0.0100  0.0097  146 THR   A CG2 
3044 N N   . VAL   A 147 ? 0.1293 0.1408 0.1841 0.0018  0.0178  0.0086  147 VAL   A N   
3045 C CA  . VAL   A 147 ? 0.1368 0.1413 0.1864 -0.0017 0.0301  0.0216  147 VAL   A CA  
3046 C C   . VAL   A 147 ? 0.1335 0.1400 0.2042 -0.0059 0.0240  0.0301  147 VAL   A C   
3047 O O   . VAL   A 147 ? 0.1382 0.1448 0.2043 -0.0159 0.0128  0.0259  147 VAL   A O   
3048 C CB  . VAL   A 147 ? 0.1477 0.1409 0.1720 -0.0090 0.0177  0.0166  147 VAL   A CB  
3049 C CG1 . VAL   A 147 ? 0.1719 0.1492 0.1918 -0.0084 0.0138  0.0283  147 VAL   A CG1 
3050 C CG2 . VAL   A 147 ? 0.1542 0.1425 0.1671 -0.0097 0.0087  0.0133  147 VAL   A CG2 
3060 N N   . ARG   A 148 ? 0.1354 0.1370 0.2055 -0.0098 0.0214  0.0340  148 ARG   A N   
3061 C CA  . ARG   A 148 ? 0.1431 0.1406 0.1966 -0.0113 0.0157  0.0353  148 ARG   A CA  
3062 C C   . ARG   A 148 ? 0.1564 0.1423 0.2062 -0.0148 0.0137  0.0512  148 ARG   A C   
3063 O O   . ARG   A 148 ? 0.1814 0.1566 0.2207 -0.0188 0.0194  0.0502  148 ARG   A O   
3064 C CB  . ARG   A 148 ? 0.1479 0.1409 0.2059 -0.0010 0.0185  0.0324  148 ARG   A CB  
3065 C CG  . ARG   A 148 ? 0.1653 0.1456 0.2450 -0.0096 0.0363  0.0254  148 ARG   A CG  
3066 C CD  . ARG   A 148 ? 0.1801 0.1481 0.2682 -0.0035 0.0464  0.0369  148 ARG   A CD  
3067 N NE  . ARG   A 148 ? 0.1797 0.1520 0.2747 0.0042  0.0471  0.0400  148 ARG   A NE  
3068 C CZ  . ARG   A 148 ? 0.1746 0.1439 0.2555 -0.0015 0.0441  0.0327  148 ARG   A CZ  
3069 N NH1 . ARG   A 148 ? 0.1811 0.1460 0.2695 -0.0104 0.0426  0.0191  148 ARG   A NH1 
3070 N NH2 . ARG   A 148 ? 0.1699 0.1632 0.2581 0.0044  0.0464  0.0456  148 ARG   A NH2 
3084 N N   . THR   A 149 ? 0.1538 0.1507 0.2045 -0.0185 -0.0018 0.0415  149 THR   A N   
3085 C CA  . THR   A 149 ? 0.1532 0.1583 0.1981 -0.0142 0.0057  0.0406  149 THR   A CA  
3086 C C   . THR   A 149 ? 0.1509 0.1585 0.1789 -0.0165 0.0111  0.0477  149 THR   A C   
3087 O O   . THR   A 149 ? 0.1508 0.1693 0.1963 -0.0205 0.0065  0.0434  149 THR   A O   
3088 C CB  . THR   A 149 ? 0.1538 0.1749 0.1916 -0.0154 0.0075  0.0335  149 THR   A CB  
3089 O OG1 . THR   A 149 ? 0.1533 0.1699 0.1934 -0.0273 0.0061  0.0298  149 THR   A OG1 
3090 C CG2 . THR   A 149 ? 0.1519 0.1835 0.2007 -0.0099 -0.0064 0.0261  149 THR   A CG2 
3098 N N   . ASN   A 150 ? 0.1575 0.1596 0.1782 -0.0073 0.0012  0.0506  150 ASN   A N   
3099 C CA  . ASN   A 150 ? 0.1703 0.1654 0.1792 -0.0091 -0.0002 0.0417  150 ASN   A CA  
3100 C C   . ASN   A 150 ? 0.1495 0.1561 0.1873 -0.0167 -0.0006 0.0360  150 ASN   A C   
3101 O O   . ASN   A 150 ? 0.1576 0.1717 0.2187 -0.0153 -0.0167 0.0350  150 ASN   A O   
3102 C CB  . ASN   A 150 ? 0.2169 0.1888 0.2042 -0.0149 0.0221  0.0600  150 ASN   A CB  
3103 C CG  . ASN   A 150 ? 0.2702 0.2214 0.2679 -0.0166 0.0109  0.0649  150 ASN   A CG  
3104 O OD1 . ASN   A 150 ? 0.2946 0.2302 0.3023 -0.0255 0.0264  0.0776  150 ASN   A OD1 
3105 N ND2 . ASN   A 150 ? 0.3023 0.2478 0.3141 -0.0132 -0.0115 0.0669  150 ASN   A ND2 
3112 N N   . VAL   A 151 ? 0.1475 0.1479 0.1816 -0.0188 0.0015  0.0344  151 VAL   A N   
3113 C CA  . VAL   A 151 ? 0.1527 0.1525 0.1813 -0.0191 0.0032  0.0362  151 VAL   A CA  
3114 C C   . VAL   A 151 ? 0.1446 0.1472 0.1823 -0.0230 0.0118  0.0364  151 VAL   A C   
3115 O O   . VAL   A 151 ? 0.1532 0.1536 0.2161 -0.0170 0.0148  0.0257  151 VAL   A O   
3116 C CB  . VAL   A 151 ? 0.1813 0.1675 0.1658 -0.0070 0.0100  0.0380  151 VAL   A CB  
3117 C CG1 . VAL   A 151 ? 0.1845 0.1883 0.2011 -0.0028 0.0030  0.0270  151 VAL   A CG1 
3118 C CG2 . VAL   A 151 ? 0.1911 0.1683 0.1665 -0.0023 0.0280  0.0320  151 VAL   A CG2 
3128 N N   . TYR   A 152 ? 0.1436 0.1507 0.1737 -0.0218 0.0113  0.0315  152 TYR   A N   
3129 C CA  . TYR   A 152 ? 0.1446 0.1581 0.1572 -0.0196 0.0099  0.0376  152 TYR   A CA  
3130 C C   . TYR   A 152 ? 0.1427 0.1517 0.1560 -0.0162 0.0174  0.0403  152 TYR   A C   
3131 O O   . TYR   A 152 ? 0.1543 0.1470 0.1630 -0.0239 0.0188  0.0334  152 TYR   A O   
3132 C CB  . TYR   A 152 ? 0.1589 0.1619 0.1591 -0.0090 0.0204  0.0354  152 TYR   A CB  
3133 C CG  . TYR   A 152 ? 0.1669 0.1786 0.1586 -0.0138 0.0201  0.0405  152 TYR   A CG  
3134 C CD1 . TYR   A 152 ? 0.1817 0.2022 0.1886 -0.0029 0.0315  0.0517  152 TYR   A CD1 
3135 C CD2 . TYR   A 152 ? 0.1752 0.1886 0.1507 -0.0294 0.0157  0.0300  152 TYR   A CD2 
3136 C CE1 . TYR   A 152 ? 0.2168 0.2142 0.1942 -0.0012 0.0182  0.0651  152 TYR   A CE1 
3137 C CE2 . TYR   A 152 ? 0.2101 0.2034 0.1748 -0.0306 0.0135  0.0459  152 TYR   A CE2 
3138 C CZ  . TYR   A 152 ? 0.2374 0.2078 0.1828 -0.0190 0.0095  0.0727  152 TYR   A CZ  
3139 O OH  . TYR   A 152 ? 0.2694 0.2292 0.2183 -0.0159 0.0147  0.0829  152 TYR   A OH  
3149 N N   A LEU   A 153 ? 0.1354 0.1454 0.1773 -0.0203 0.0245  0.0386  153 LEU   A N   
3150 N N   B LEU   A 153 ? 0.1417 0.1558 0.1572 -0.0106 0.0091  0.0381  153 LEU   A N   
3151 C CA  A LEU   A 153 ? 0.1337 0.1444 0.1880 -0.0130 0.0235  0.0345  153 LEU   A CA  
3152 C CA  B LEU   A 153 ? 0.1395 0.1604 0.1537 -0.0016 0.0051  0.0371  153 LEU   A CA  
3153 C C   A LEU   A 153 ? 0.1412 0.1421 0.1901 -0.0138 0.0419  0.0242  153 LEU   A C   
3154 C C   B LEU   A 153 ? 0.1400 0.1635 0.1479 0.0035  0.0072  0.0371  153 LEU   A C   
3155 O O   A LEU   A 153 ? 0.1495 0.1510 0.2113 -0.0187 0.0502  0.0272  153 LEU   A O   
3156 O O   B LEU   A 153 ? 0.1420 0.1697 0.1600 0.0047  0.0107  0.0374  153 LEU   A O   
3157 C CB  A LEU   A 153 ? 0.1309 0.1380 0.1809 -0.0100 0.0156  0.0313  153 LEU   A CB  
3158 C CB  B LEU   A 153 ? 0.1411 0.1640 0.1564 0.0027  0.0051  0.0345  153 LEU   A CB  
3159 C CG  A LEU   A 153 ? 0.1363 0.1423 0.1742 -0.0085 0.0177  0.0202  153 LEU   A CG  
3160 C CG  B LEU   A 153 ? 0.1461 0.1714 0.1613 0.0023  0.0046  0.0353  153 LEU   A CG  
3161 C CD1 A LEU   A 153 ? 0.1444 0.1393 0.1668 -0.0073 0.0136  0.0177  153 LEU   A CD1 
3162 C CD1 B LEU   A 153 ? 0.1528 0.1705 0.1701 0.0022  0.0041  0.0353  153 LEU   A CD1 
3163 C CD2 A LEU   A 153 ? 0.1369 0.1435 0.1623 -0.0094 0.0258  0.0034  153 LEU   A CD2 
3164 C CD2 B LEU   A 153 ? 0.1465 0.1779 0.1688 -0.0009 0.0012  0.0328  153 LEU   A CD2 
3187 N N   A ALA   A 154 ? 0.1417 0.1337 0.1819 -0.0160 0.0336  0.0210  154 ALA   A N   
3188 N N   B ALA   A 154 ? 0.1408 0.1605 0.1248 -0.0016 0.0029  0.0303  154 ALA   A N   
3189 C CA  A ALA   A 154 ? 0.1574 0.1392 0.1662 -0.0098 0.0273  0.0226  154 ALA   A CA  
3190 C CA  B ALA   A 154 ? 0.1465 0.1621 0.1341 0.0000  0.0039  0.0261  154 ALA   A CA  
3191 C C   A ALA   A 154 ? 0.1419 0.1329 0.1697 -0.0025 0.0227  0.0204  154 ALA   A C   
3192 C C   B ALA   A 154 ? 0.1416 0.1630 0.1280 -0.0056 0.0068  0.0236  154 ALA   A C   
3193 O O   A ALA   A 154 ? 0.1465 0.1443 0.1744 -0.0126 0.0179  0.0123  154 ALA   A O   
3194 O O   B ALA   A 154 ? 0.1437 0.1695 0.1177 -0.0149 0.0155  0.0273  154 ALA   A O   
3195 C CB  A ALA   A 154 ? 0.1687 0.1424 0.1730 0.0050  0.0139  0.0138  154 ALA   A CB  
3196 C CB  B ALA   A 154 ? 0.1469 0.1606 0.1483 0.0057  -0.0043 0.0133  154 ALA   A CB  
3207 N N   A VAL   A 155 ? 0.1317 0.1230 0.1403 0.0032  0.0266  0.0382  155 VAL   A N   
3208 N N   B VAL   A 155 ? 0.1368 0.1571 0.1324 -0.0026 0.0038  0.0310  155 VAL   A N   
3209 C CA  A VAL   A 155 ? 0.1461 0.1376 0.1791 0.0024  0.0193  0.0422  155 VAL   A CA  
3210 C CA  B VAL   A 155 ? 0.1473 0.1676 0.1639 -0.0051 0.0007  0.0356  155 VAL   A CA  
3211 C CA  T VAL   A 155 ? 0.1697 0.1680 0.1737 0.0073  0.0203  0.0375  155 VAL   A CA  
3212 C C   A VAL   A 155 ? 0.1568 0.1495 0.2139 0.0059  0.0185  0.0501  155 VAL   A C   
3213 C C   B VAL   A 155 ? 0.1546 0.1765 0.1888 0.0038  -0.0095 0.0463  155 VAL   A C   
3214 C C   T VAL   A 155 ? 0.1710 0.1650 0.1747 0.0097  0.0291  0.0406  155 VAL   A C   
3215 O O   A VAL   A 155 ? 0.1530 0.1525 0.2206 0.0108  0.0262  0.0428  155 VAL   A O   
3216 O O   B VAL   A 155 ? 0.1510 0.1787 0.1743 0.0130  -0.0131 0.0357  155 VAL   A O   
3217 O O   T VAL   A 155 ? 0.1686 0.1696 0.1678 0.0158  0.0336  0.0357  155 VAL   A O   
3218 C CB  A VAL   A 155 ? 0.1558 0.1470 0.1885 0.0039  -0.0005 0.0381  155 VAL   A CB  
3219 C CB  B VAL   A 155 ? 0.1509 0.1727 0.1673 -0.0045 -0.0044 0.0285  155 VAL   A CB  
3220 C CB  T VAL   A 155 ? 0.1707 0.1723 0.1762 0.0079  0.0047  0.0362  155 VAL   A CB  
3221 C CG1 A VAL   A 155 ? 0.1643 0.1527 0.1985 0.0046  0.0064  0.0293  155 VAL   A CG1 
3222 C CG1 B VAL   A 155 ? 0.1531 0.1788 0.1797 -0.0077 -0.0025 0.0304  155 VAL   A CG1 
3223 C CG1 T VAL   A 155 ? 0.1735 0.1755 0.1842 0.0086  0.0044  0.0349  155 VAL   A CG1 
3224 C CG2 A VAL   A 155 ? 0.1665 0.1550 0.2034 0.0117  -0.0201 0.0290  155 VAL   A CG2 
3225 C CG2 B VAL   A 155 ? 0.1623 0.1754 0.1833 0.0031  -0.0070 0.0159  155 VAL   A CG2 
3226 C CG2 T VAL   A 155 ? 0.1723 0.1744 0.1806 0.0106  -0.0070 0.0313  155 VAL   A CG2 
3252 N N   A PHE   A 156 ? 0.1725 0.1607 0.2557 0.0093  0.0196  0.0599  156 PHE   A N   
3253 N N   B PHE   A 156 ? 0.1660 0.1810 0.2114 0.0026  -0.0074 0.0578  156 PHE   A N   
3254 N N   T PHE   A 156 ? 0.1768 0.1557 0.1828 0.0062  0.0359  0.0482  156 PHE   A N   
3255 C CA  A PHE   A 156 ? 0.1915 0.1763 0.2853 0.0160  0.0149  0.0638  156 PHE   A CA  
3256 C CA  B PHE   A 156 ? 0.1817 0.1856 0.2394 0.0054  -0.0029 0.0598  156 PHE   A CA  
3257 C CA  T PHE   A 156 ? 0.1887 0.1478 0.1824 0.0051  0.0384  0.0596  156 PHE   A CA  
3258 C C   A PHE   A 156 ? 0.1847 0.1863 0.2799 0.0227  0.0333  0.0729  156 PHE   A C   
3259 C C   B PHE   A 156 ? 0.1888 0.1917 0.2301 0.0178  -0.0016 0.0644  156 PHE   A C   
3260 C C   T PHE   A 156 ? 0.1919 0.1608 0.1912 0.0104  0.0406  0.0670  156 PHE   A C   
3261 O O   A PHE   A 156 ? 0.1884 0.1924 0.2826 0.0210  0.0452  0.0678  156 PHE   A O   
3262 O O   B PHE   A 156 ? 0.1929 0.1950 0.2168 0.0219  -0.0090 0.0724  156 PHE   A O   
3263 O O   T PHE   A 156 ? 0.1987 0.1670 0.2014 0.0119  0.0438  0.0562  156 PHE   A O   
3264 C CB  A PHE   A 156 ? 0.2233 0.1897 0.3002 0.0205  -0.0001 0.0717  156 PHE   A CB  
3265 C CB  B PHE   A 156 ? 0.1838 0.1868 0.2533 -0.0046 0.0037  0.0649  156 PHE   A CB  
3266 C CB  T PHE   A 156 ? 0.1975 0.1318 0.1657 0.0033  0.0363  0.0707  156 PHE   A CB  
3267 C CG  A PHE   A 156 ? 0.2598 0.2099 0.3131 0.0324  -0.0152 0.0645  156 PHE   A CG  
3268 C CG  B PHE   A 156 ? 0.1860 0.1914 0.2615 -0.0071 0.0069  0.0592  156 PHE   A CG  
3269 C CG  T PHE   A 156 ? 0.2068 0.1297 0.1555 0.0087  0.0270  0.0726  156 PHE   A CG  
3270 C CD1 A PHE   A 156 ? 0.2779 0.2222 0.3234 0.0359  -0.0163 0.0551  156 PHE   A CD1 
3271 C CD1 B PHE   A 156 ? 0.1887 0.2017 0.2657 -0.0128 0.0195  0.0466  156 PHE   A CD1 
3272 C CD1 T PHE   A 156 ? 0.2078 0.1319 0.1620 0.0067  0.0168  0.0610  156 PHE   A CD1 
3273 C CD2 A PHE   A 156 ? 0.2799 0.2232 0.3254 0.0387  -0.0190 0.0593  156 PHE   A CD2 
3274 C CD2 B PHE   A 156 ? 0.1794 0.1854 0.2574 -0.0172 0.0051  0.0601  156 PHE   A CD2 
3275 C CD2 T PHE   A 156 ? 0.2145 0.1315 0.1612 0.0120  0.0324  0.0733  156 PHE   A CD2 
3276 C CE1 A PHE   A 156 ? 0.2908 0.2298 0.3339 0.0357  -0.0118 0.0418  156 PHE   A CE1 
3277 C CE1 B PHE   A 156 ? 0.1888 0.2050 0.2672 -0.0195 0.0206  0.0353  156 PHE   A CE1 
3278 C CE1 T PHE   A 156 ? 0.2135 0.1367 0.1766 0.0068  0.0139  0.0501  156 PHE   A CE1 
3279 C CE2 A PHE   A 156 ? 0.2934 0.2331 0.3290 0.0389  -0.0212 0.0447  156 PHE   A CE2 
3280 C CE2 B PHE   A 156 ? 0.1802 0.1922 0.2636 -0.0233 0.0043  0.0391  156 PHE   A CE2 
3281 C CE2 T PHE   A 156 ? 0.2198 0.1363 0.1637 0.0090  0.0240  0.0689  156 PHE   A CE2 
3282 C CZ  A PHE   A 156 ? 0.2954 0.2361 0.3356 0.0374  -0.0136 0.0339  156 PHE   A CZ  
3283 C CZ  B PHE   A 156 ? 0.1885 0.2013 0.2684 -0.0217 0.0083  0.0335  156 PHE   A CZ  
3284 C CZ  T PHE   A 156 ? 0.2186 0.1375 0.1743 0.0050  0.0186  0.0564  156 PHE   A CZ  
3312 N N   A ASP   A 157 ? 0.1808 0.1940 0.2837 0.0220  0.0306  0.0898  157 ASP   A N   
3313 N N   B ASP   A 157 ? 0.1911 0.1910 0.2219 0.0247  0.0041  0.0644  157 ASP   A N   
3314 N N   T ASP   A 157 ? 0.1866 0.1730 0.2060 0.0119  0.0365  0.0784  157 ASP   A N   
3315 C CA  A ASP   A 157 ? 0.1865 0.2099 0.2829 0.0281  0.0321  0.0861  157 ASP   A CA  
3316 C CA  B ASP   A 157 ? 0.2032 0.2042 0.2344 0.0294  0.0082  0.0683  157 ASP   A CA  
3317 C CA  T ASP   A 157 ? 0.1880 0.1907 0.2199 0.0210  0.0281  0.0750  157 ASP   A CA  
3318 C C   A ASP   A 157 ? 0.1729 0.2177 0.2966 0.0273  0.0392  0.0929  157 ASP   A C   
3319 C C   B ASP   A 157 ? 0.1992 0.2183 0.2549 0.0320  0.0170  0.0611  157 ASP   A C   
3320 C C   T ASP   A 157 ? 0.1971 0.2085 0.2290 0.0241  0.0295  0.0762  157 ASP   A C   
3321 O O   A ASP   A 157 ? 0.1579 0.2092 0.2782 0.0285  0.0394  0.1007  157 ASP   A O   
3322 O O   B ASP   A 157 ? 0.1985 0.2175 0.2440 0.0332  0.0162  0.0588  157 ASP   A O   
3323 O O   T ASP   A 157 ? 0.1919 0.2058 0.2199 0.0239  0.0264  0.0788  157 ASP   A O   
3324 C CB  A ASP   A 157 ? 0.2039 0.2203 0.2803 0.0353  0.0319  0.0798  157 ASP   A CB  
3325 C CB  B ASP   A 157 ? 0.2178 0.2058 0.2351 0.0295  0.0034  0.0709  157 ASP   A CB  
3326 C CB  T ASP   A 157 ? 0.1820 0.1935 0.2268 0.0289  0.0165  0.0715  157 ASP   A CB  
3327 C CG  A ASP   A 157 ? 0.2229 0.2260 0.2825 0.0453  0.0325  0.0726  157 ASP   A CG  
3328 C CG  B ASP   A 157 ? 0.2333 0.2086 0.2401 0.0319  0.0053  0.0717  157 ASP   A CG  
3329 C CG  T ASP   A 157 ? 0.1789 0.1928 0.2317 0.0367  0.0079  0.0717  157 ASP   A CG  
3330 O OD1 A ASP   A 157 ? 0.2422 0.2307 0.3035 0.0510  0.0267  0.0592  157 ASP   A OD1 
3331 O OD1 B ASP   A 157 ? 0.2463 0.2171 0.2470 0.0387  0.0087  0.0660  157 ASP   A OD1 
3332 O OD1 T ASP   A 157 ? 0.1782 0.1908 0.2393 0.0368  0.0134  0.0629  157 ASP   A OD1 
3333 O OD2 A ASP   A 157 ? 0.2175 0.2242 0.2671 0.0445  0.0355  0.0836  157 ASP   A OD2 
3334 O OD2 B ASP   A 157 ? 0.2325 0.1984 0.2494 0.0313  0.0090  0.0771  157 ASP   A OD2 
3335 O OD2 T ASP   A 157 ? 0.1768 0.1927 0.2175 0.0402  -0.0013 0.0870  157 ASP   A OD2 
3348 N N   A LYS   A 158 ? 0.1775 0.2331 0.3212 0.0331  0.0439  0.0953  158 LYS   A N   
3349 N N   B LYS   A 158 ? 0.2006 0.2301 0.2867 0.0346  0.0320  0.0656  158 LYS   A N   
3350 N N   T LYS   A 158 ? 0.2134 0.2287 0.2489 0.0300  0.0304  0.0706  158 LYS   A N   
3351 C CA  A LYS   A 158 ? 0.1739 0.2501 0.3369 0.0382  0.0594  0.0932  158 LYS   A CA  
3352 C CA  B LYS   A 158 ? 0.1975 0.2409 0.3024 0.0365  0.0428  0.0672  158 LYS   A CA  
3353 C CA  T LYS   A 158 ? 0.2256 0.2476 0.2722 0.0344  0.0303  0.0613  158 LYS   A CA  
3354 C C   A LYS   A 158 ? 0.1577 0.2601 0.3202 0.0357  0.0515  0.1065  158 LYS   A C   
3355 C C   B LYS   A 158 ? 0.1910 0.2459 0.2996 0.0377  0.0240  0.0650  158 LYS   A C   
3356 C C   T LYS   A 158 ? 0.2281 0.2577 0.2716 0.0357  0.0259  0.0604  158 LYS   A C   
3357 O O   A LYS   A 158 ? 0.1489 0.2616 0.3260 0.0276  0.0475  0.1134  158 LYS   A O   
3358 O O   B LYS   A 158 ? 0.1916 0.2511 0.3128 0.0361  0.0316  0.0631  158 LYS   A O   
3359 O O   T LYS   A 158 ? 0.2267 0.2607 0.2747 0.0372  0.0268  0.0612  158 LYS   A O   
3360 C CB  A LYS   A 158 ? 0.1905 0.2622 0.3626 0.0413  0.0789  0.0780  158 LYS   A CB  
3361 C CB  B LYS   A 158 ? 0.2066 0.2472 0.3189 0.0360  0.0680  0.0698  158 LYS   A CB  
3362 C CB  T LYS   A 158 ? 0.2360 0.2548 0.2930 0.0332  0.0374  0.0531  158 LYS   A CB  
3363 C CG  A LYS   A 158 ? 0.2070 0.2751 0.3886 0.0440  0.0896  0.0757  158 LYS   A CG  
3364 C CG  B LYS   A 158 ? 0.2179 0.2553 0.3425 0.0360  0.0766  0.0751  158 LYS   A CG  
3365 C CG  T LYS   A 158 ? 0.2453 0.2618 0.3147 0.0307  0.0412  0.0485  158 LYS   A CG  
3366 C CD  A LYS   A 158 ? 0.2199 0.2864 0.4027 0.0460  0.1060  0.0838  158 LYS   A CD  
3367 C CD  B LYS   A 158 ? 0.2282 0.2640 0.3572 0.0351  0.0910  0.0803  158 LYS   A CD  
3368 C CD  T LYS   A 158 ? 0.2537 0.2681 0.3343 0.0291  0.0450  0.0494  158 LYS   A CD  
3369 C CE  A LYS   A 158 ? 0.2288 0.2921 0.4129 0.0453  0.1154  0.0992  158 LYS   A CE  
3370 C CE  B LYS   A 158 ? 0.2358 0.2704 0.3686 0.0350  0.1027  0.0881  158 LYS   A CE  
3371 C CE  T LYS   A 158 ? 0.2596 0.2716 0.3464 0.0284  0.0467  0.0543  158 LYS   A CE  
3372 N NZ  A LYS   A 158 ? 0.2347 0.2939 0.4169 0.0416  0.1160  0.1083  158 LYS   A NZ  
3373 N NZ  B LYS   A 158 ? 0.2417 0.2732 0.3788 0.0323  0.1063  0.0920  158 LYS   A NZ  
3374 N NZ  T LYS   A 158 ? 0.2642 0.2735 0.3506 0.0287  0.0467  0.0584  158 LYS   A NZ  
3414 N N   A ASN   A 159 ? 0.1674 0.2713 0.3283 0.0389  0.0378  0.1014  159 ASN   A N   
3415 N N   B ASN   A 159 ? 0.1901 0.2434 0.2926 0.0371  -0.0018 0.0578  159 ASN   A N   
3416 N N   T ASN   A 159 ? 0.2353 0.2634 0.2799 0.0303  0.0224  0.0561  159 ASN   A N   
3417 C CA  A ASN   A 159 ? 0.1731 0.2783 0.3215 0.0407  0.0121  0.1123  159 ASN   A CA  
3418 C CA  B ASN   A 159 ? 0.1837 0.2390 0.2702 0.0357  -0.0252 0.0543  159 ASN   A CA  
3419 C CA  T ASN   A 159 ? 0.2422 0.2683 0.2845 0.0218  0.0156  0.0546  159 ASN   A CA  
3420 C C   A ASN   A 159 ? 0.1586 0.2752 0.2893 0.0237  0.0068  0.0999  159 ASN   A C   
3421 C C   B ASN   A 159 ? 0.1724 0.2374 0.2552 0.0348  -0.0162 0.0464  159 ASN   A C   
3422 C C   T ASN   A 159 ? 0.2437 0.2709 0.2731 0.0135  0.0158  0.0439  159 ASN   A C   
3423 O O   A ASN   A 159 ? 0.1521 0.2919 0.2798 0.0205  -0.0132 0.0913  159 ASN   A O   
3424 O O   B ASN   A 159 ? 0.1541 0.2389 0.2349 0.0449  -0.0241 0.0313  159 ASN   A O   
3425 O O   T ASN   A 159 ? 0.2454 0.2756 0.2697 0.0131  0.0100  0.0397  159 ASN   A O   
3426 C CB  A ASN   A 159 ? 0.1946 0.2895 0.3543 0.0488  -0.0038 0.1253  159 ASN   A CB  
3427 C CB  B ASN   A 159 ? 0.1906 0.2402 0.2754 0.0284  -0.0408 0.0525  159 ASN   A CB  
3428 C CB  T ASN   A 159 ? 0.2475 0.2716 0.3030 0.0191  0.0092  0.0610  159 ASN   A CB  
3429 C CG  A ASN   A 159 ? 0.2169 0.3045 0.3884 0.0471  0.0005  0.1195  159 ASN   A CG  
3430 C CG  B ASN   A 159 ? 0.1968 0.2479 0.2940 0.0217  -0.0403 0.0399  159 ASN   A CG  
3431 C CG  T ASN   A 159 ? 0.2527 0.2757 0.3212 0.0177  0.0094  0.0617  159 ASN   A CG  
3432 O OD1 A ASN   A 159 ? 0.2236 0.3132 0.4116 0.0465  0.0197  0.1135  159 ASN   A OD1 
3433 O OD1 B ASN   A 159 ? 0.2027 0.2585 0.3208 0.0266  -0.0344 0.0239  159 ASN   A OD1 
3434 O OD1 T ASN   A 159 ? 0.2540 0.2798 0.3356 0.0181  0.0191  0.0598  159 ASN   A OD1 
3435 N ND2 A ASN   A 159 ? 0.2271 0.3116 0.4079 0.0425  -0.0036 0.1101  159 ASN   A ND2 
3436 N ND2 B ASN   A 159 ? 0.1958 0.2427 0.2904 0.0190  -0.0419 0.0472  159 ASN   A ND2 
3437 N ND2 T ASN   A 159 ? 0.2546 0.2776 0.3286 0.0163  0.0038  0.0598  159 ASN   A ND2 
3456 N N   A LEU   A 160 ? 0.1474 0.2542 0.2635 0.0120  -0.0022 0.0972  160 LEU   A N   
3457 N N   B LEU   A 160 ? 0.1710 0.2295 0.2441 0.0303  -0.0102 0.0414  160 LEU   A N   
3458 N N   T LEU   A 160 ? 0.2417 0.2669 0.2631 0.0071  0.0152  0.0398  160 LEU   A N   
3459 C CA  A LEU   A 160 ? 0.1501 0.2358 0.2386 -0.0034 -0.0004 0.0931  160 LEU   A CA  
3460 C CA  B LEU   A 160 ? 0.1670 0.2184 0.2183 0.0205  -0.0033 0.0442  160 LEU   A CA  
3461 C CA  T LEU   A 160 ? 0.2430 0.2629 0.2524 0.0003  0.0150  0.0384  160 LEU   A CA  
3462 C C   A LEU   A 160 ? 0.1406 0.2225 0.2031 -0.0005 -0.0044 0.0842  160 LEU   A C   
3463 C C   B LEU   A 160 ? 0.1481 0.2085 0.1758 0.0145  0.0134  0.0421  160 LEU   A C   
3464 O O   A LEU   A 160 ? 0.1333 0.2210 0.2029 -0.0073 0.0002  0.0703  160 LEU   A O   
3465 O O   B LEU   A 160 ? 0.1427 0.2150 0.1825 0.0077  0.0141  0.0373  160 LEU   A O   
3466 C CB  A LEU   A 160 ? 0.1608 0.2357 0.2204 -0.0161 0.0063  0.0929  160 LEU   A CB  
3467 C CB  B LEU   A 160 ? 0.1783 0.2177 0.2213 0.0149  0.0029  0.0481  160 LEU   A CB  
3468 C CB  T LEU   A 160 ? 0.2452 0.2603 0.2381 -0.0049 0.0154  0.0378  160 LEU   A CB  
3469 C CG  A LEU   A 160 ? 0.1761 0.2423 0.2237 -0.0236 0.0005  0.0807  160 LEU   A CG  
3470 C CG  B LEU   A 160 ? 0.1878 0.2196 0.2282 0.0029  0.0100  0.0407  160 LEU   A CG  
3471 C CG  T LEU   A 160 ? 0.2489 0.2604 0.2323 -0.0095 0.0157  0.0331  160 LEU   A CG  
3472 C CD1 A LEU   A 160 ? 0.1867 0.2551 0.2326 -0.0242 0.0053  0.0707  160 LEU   A CD1 
3473 C CD1 B LEU   A 160 ? 0.1909 0.2215 0.2301 -0.0057 0.0078  0.0330  160 LEU   A CD1 
3474 C CD1 T LEU   A 160 ? 0.2513 0.2637 0.2320 -0.0109 0.0165  0.0295  160 LEU   A CD1 
3475 C CD2 A LEU   A 160 ? 0.1779 0.2371 0.2252 -0.0270 0.0062  0.0745  160 LEU   A CD2 
3476 C CD2 B LEU   A 160 ? 0.1911 0.2192 0.2216 0.0004  0.0174  0.0397  160 LEU   A CD2 
3477 C CD2 T LEU   A 160 ? 0.2492 0.2577 0.2282 -0.0112 0.0191  0.0310  160 LEU   A CD2 
3510 N N   A TYR   A 161 ? 0.1489 0.2157 0.2188 0.0016  0.0064  0.0755  161 TYR   A N   
3511 N N   B TYR   A 161 ? 0.1446 0.1948 0.1767 0.0119  0.0172  0.0315  161 TYR   A N   
3512 C CA  A TYR   A 161 ? 0.1532 0.2070 0.2089 -0.0003 0.0099  0.0694  161 TYR   A CA  
3513 C CA  B TYR   A 161 ? 0.1413 0.1843 0.1584 0.0089  0.0188  0.0182  161 TYR   A CA  
3514 C C   A TYR   A 161 ? 0.1528 0.2114 0.2131 0.0007  0.0041  0.0621  161 TYR   A C   
3515 C C   B TYR   A 161 ? 0.1396 0.1932 0.1640 0.0097  0.0194  0.0165  161 TYR   A C   
3516 O O   A TYR   A 161 ? 0.1523 0.2067 0.1900 -0.0045 0.0083  0.0498  161 TYR   A O   
3517 O O   B TYR   A 161 ? 0.1338 0.1914 0.1480 0.0053  0.0221  0.0038  161 TYR   A O   
3518 C CB  A TYR   A 161 ? 0.1557 0.1987 0.2200 -0.0042 0.0071  0.0501  161 TYR   A CB  
3519 C CB  B TYR   A 161 ? 0.1437 0.1727 0.1654 0.0068  0.0182  -0.0079 161 TYR   A CB  
3520 C CG  A TYR   A 161 ? 0.1591 0.1921 0.2148 -0.0040 0.0084  0.0222  161 TYR   A CG  
3521 C CG  B TYR   A 161 ? 0.1468 0.1646 0.1643 0.0080  0.0206  -0.0176 161 TYR   A CG  
3522 C CD1 A TYR   A 161 ? 0.1588 0.1861 0.2103 -0.0021 0.0140  0.0086  161 TYR   A CD1 
3523 C CD1 B TYR   A 161 ? 0.1464 0.1571 0.1561 0.0013  0.0303  -0.0181 161 TYR   A CD1 
3524 C CD2 A TYR   A 161 ? 0.1649 0.1925 0.2159 0.0072  -0.0061 0.0000  161 TYR   A CD2 
3525 C CD2 B TYR   A 161 ? 0.1504 0.1656 0.1704 0.0158  0.0185  -0.0155 161 TYR   A CD2 
3526 C CE1 A TYR   A 161 ? 0.1631 0.1788 0.1915 0.0014  0.0067  0.0077  161 TYR   A CE1 
3527 C CE1 B TYR   A 161 ? 0.1580 0.1609 0.1664 0.0017  0.0343  -0.0212 161 TYR   A CE1 
3528 C CE2 A TYR   A 161 ? 0.1679 0.1861 0.1959 -0.0014 -0.0005 0.0091  161 TYR   A CE2 
3529 C CE2 B TYR   A 161 ? 0.1629 0.1699 0.1837 0.0052  0.0291  -0.0121 161 TYR   A CE2 
3530 C CZ  A TYR   A 161 ? 0.1767 0.1848 0.1850 0.0003  -0.0052 0.0152  161 TYR   A CZ  
3531 C CZ  B TYR   A 161 ? 0.1739 0.1734 0.1897 0.0008  0.0315  -0.0192 161 TYR   A CZ  
3532 O OH  A TYR   A 161 ? 0.1938 0.1975 0.1835 -0.0050 -0.0037 0.0287  161 TYR   A OH  
3533 O OH  B TYR   A 161 ? 0.1910 0.1812 0.2190 -0.0061 0.0275  -0.0183 161 TYR   A OH  
3552 N N   A ASP   A 162 ? 0.1532 0.2242 0.2486 0.0008  0.0043  0.0778  162 ASP   A N   
3553 N N   B ASP   A 162 ? 0.1424 0.2062 0.1827 0.0120  0.0257  0.0261  162 ASP   A N   
3554 C CA  A ASP   A 162 ? 0.1547 0.2496 0.2580 -0.0037 0.0155  0.0773  162 ASP   A CA  
3555 C CA  B ASP   A 162 ? 0.1478 0.2269 0.1857 0.0197  0.0370  0.0193  162 ASP   A CA  
3556 C C   A ASP   A 162 ? 0.1473 0.2733 0.2364 -0.0081 0.0181  0.0843  162 ASP   A C   
3557 C C   B ASP   A 162 ? 0.1515 0.2431 0.1845 0.0210  0.0348  0.0203  162 ASP   A C   
3558 O O   A ASP   A 162 ? 0.1470 0.2711 0.2321 -0.0089 0.0196  0.0695  162 ASP   A O   
3559 O O   B ASP   A 162 ? 0.1513 0.2427 0.1918 0.0283  0.0394  0.0109  162 ASP   A O   
3560 C CB  A ASP   A 162 ? 0.1670 0.2594 0.2882 -0.0009 0.0230  0.0607  162 ASP   A CB  
3561 C CB  B ASP   A 162 ? 0.1537 0.2344 0.1962 0.0272  0.0439  0.0174  162 ASP   A CB  
3562 C CG  A ASP   A 162 ? 0.1837 0.2761 0.3114 0.0056  0.0301  0.0446  162 ASP   A CG  
3563 C CG  B ASP   A 162 ? 0.1608 0.2464 0.2145 0.0327  0.0470  0.0224  162 ASP   A CG  
3564 O OD1 A ASP   A 162 ? 0.1871 0.2790 0.3262 -0.0048 0.0351  0.0408  162 ASP   A OD1 
3565 O OD1 B ASP   A 162 ? 0.1676 0.2510 0.2243 0.0196  0.0362  0.0168  162 ASP   A OD1 
3566 O OD2 A ASP   A 162 ? 0.2046 0.2877 0.3310 0.0157  0.0381  0.0284  162 ASP   A OD2 
3567 O OD2 B ASP   A 162 ? 0.1725 0.2525 0.2390 0.0448  0.0560  0.0231  162 ASP   A OD2 
3576 N N   A LYS   A 163 ? 0.1497 0.2981 0.2544 -0.0113 -0.0040 0.0833  163 LYS   A N   
3577 N N   B LYS   A 163 ? 0.1616 0.2623 0.2074 0.0185  0.0199  0.0262  163 LYS   A N   
3578 C CA  A LYS   A 163 ? 0.1637 0.3222 0.2454 -0.0133 0.0035  0.0908  163 LYS   A CA  
3579 C CA  B LYS   A 163 ? 0.1741 0.2815 0.2176 0.0125  0.0084  0.0317  163 LYS   A CA  
3580 C C   A LYS   A 163 ? 0.1518 0.3169 0.2319 -0.0226 0.0148  0.0926  163 LYS   A C   
3581 C C   B LYS   A 163 ? 0.1720 0.2836 0.2125 0.0085  0.0125  0.0310  163 LYS   A C   
3582 O O   A LYS   A 163 ? 0.1518 0.3350 0.2378 -0.0268 0.0135  0.0778  163 LYS   A O   
3583 O O   B LYS   A 163 ? 0.1748 0.2938 0.2188 0.0092  0.0189  0.0215  163 LYS   A O   
3584 C CB  A LYS   A 163 ? 0.2043 0.3501 0.2928 0.0067  -0.0127 0.0889  163 LYS   A CB  
3585 C CB  B LYS   A 163 ? 0.1960 0.2989 0.2602 0.0165  -0.0091 0.0363  163 LYS   A CB  
3586 C CG  A LYS   A 163 ? 0.2411 0.3737 0.3690 0.0115  -0.0150 0.0845  163 LYS   A CG  
3587 C CG  B LYS   A 163 ? 0.2172 0.3149 0.3063 0.0134  -0.0085 0.0388  163 LYS   A CG  
3588 C CD  A LYS   A 163 ? 0.2667 0.3895 0.4377 0.0133  -0.0136 0.0785  163 LYS   A CD  
3589 C CD  B LYS   A 163 ? 0.2328 0.3266 0.3414 0.0095  -0.0049 0.0398  163 LYS   A CD  
3590 C CE  A LYS   A 163 ? 0.2919 0.3995 0.4841 0.0133  -0.0090 0.0786  163 LYS   A CE  
3591 C CE  B LYS   A 163 ? 0.2434 0.3344 0.3761 0.0077  -0.0025 0.0347  163 LYS   A CE  
3592 N NZ  A LYS   A 163 ? 0.3139 0.4057 0.5184 0.0130  -0.0042 0.0798  163 LYS   A NZ  
3593 N NZ  B LYS   A 163 ? 0.2497 0.3382 0.3900 0.0083  0.0000  0.0340  163 LYS   A NZ  
3620 N N   A LEU   A 164 ? 0.1342 0.2919 0.2230 -0.0296 0.0050  0.0907  164 LEU   A N   
3621 N N   B LEU   A 164 ? 0.1621 0.2705 0.2028 0.0024  0.0081  0.0342  164 LEU   A N   
3622 C CA  A LEU   A 164 ? 0.1410 0.2714 0.2197 -0.0312 0.0190  0.0789  164 LEU   A CA  
3623 C CA  B LEU   A 164 ? 0.1623 0.2570 0.2032 -0.0027 0.0172  0.0352  164 LEU   A CA  
3624 C C   A LEU   A 164 ? 0.1496 0.2691 0.2140 -0.0263 0.0180  0.0672  164 LEU   A C   
3625 C C   B LEU   A 164 ? 0.1599 0.2517 0.2019 -0.0053 0.0239  0.0337  164 LEU   A C   
3626 O O   A LEU   A 164 ? 0.1602 0.2799 0.2188 -0.0316 0.0341  0.0510  164 LEU   A O   
3627 O O   B LEU   A 164 ? 0.1654 0.2574 0.2048 -0.0101 0.0332  0.0255  164 LEU   A O   
3628 C CB  A LEU   A 164 ? 0.1404 0.2591 0.2172 -0.0289 0.0258  0.0774  164 LEU   A CB  
3629 C CB  B LEU   A 164 ? 0.1673 0.2506 0.2092 -0.0025 0.0170  0.0343  164 LEU   A CB  
3630 C CG  A LEU   A 164 ? 0.1499 0.2525 0.2266 -0.0178 0.0198  0.0727  164 LEU   A CG  
3631 C CG  B LEU   A 164 ? 0.1762 0.2453 0.2194 0.0034  0.0143  0.0291  164 LEU   A CG  
3632 C CD1 A LEU   A 164 ? 0.1420 0.2443 0.2256 -0.0082 0.0052  0.0808  164 LEU   A CD1 
3633 C CD1 B LEU   A 164 ? 0.1737 0.2442 0.2286 0.0087  0.0137  0.0261  164 LEU   A CD1 
3634 C CD2 A LEU   A 164 ? 0.1683 0.2532 0.2231 -0.0182 0.0442  0.0719  164 LEU   A CD2 
3635 C CD2 B LEU   A 164 ? 0.1847 0.2413 0.2230 -0.0005 0.0191  0.0236  164 LEU   A CD2 
3658 N N   A VAL   A 165 ? 0.1469 0.2592 0.2034 -0.0190 0.0150  0.0737  165 VAL   A N   
3659 N N   B VAL   A 165 ? 0.1513 0.2428 0.1977 -0.0049 0.0237  0.0362  165 VAL   A N   
3660 C CA  A VAL   A 165 ? 0.1558 0.2538 0.2008 -0.0135 0.0085  0.0783  165 VAL   A CA  
3661 C CA  B VAL   A 165 ? 0.1495 0.2379 0.2011 -0.0027 0.0187  0.0360  165 VAL   A CA  
3662 C C   A VAL   A 165 ? 0.1510 0.2587 0.1878 -0.0027 0.0126  0.0807  165 VAL   A C   
3663 C C   B VAL   A 165 ? 0.1415 0.2428 0.1947 -0.0024 0.0232  0.0361  165 VAL   A C   
3664 O O   A VAL   A 165 ? 0.1560 0.2580 0.1751 -0.0054 0.0243  0.0768  165 VAL   A O   
3665 O O   B VAL   A 165 ? 0.1427 0.2417 0.1886 -0.0016 0.0276  0.0331  165 VAL   A O   
3666 C CB  A VAL   A 165 ? 0.1681 0.2474 0.2093 -0.0140 0.0109  0.0682  165 VAL   A CB  
3667 C CB  B VAL   A 165 ? 0.1535 0.2306 0.2028 0.0005  0.0126  0.0304  165 VAL   A CB  
3668 C CG1 A VAL   A 165 ? 0.1728 0.2496 0.2182 -0.0129 0.0124  0.0635  165 VAL   A CG1 
3669 C CG1 B VAL   A 165 ? 0.1550 0.2273 0.1997 0.0042  0.0112  0.0253  165 VAL   A CG1 
3670 C CG2 A VAL   A 165 ? 0.1736 0.2452 0.2194 -0.0103 0.0105  0.0724  165 VAL   A CG2 
3671 C CG2 B VAL   A 165 ? 0.1582 0.2330 0.2167 -0.0059 0.0104  0.0278  165 VAL   A CG2 
3690 N N   A SER   A 166 ? 0.1444 0.2731 0.1973 0.0016  0.0112  0.0670  166 SER   A N   
3691 N N   B SER   A 166 ? 0.1337 0.2530 0.1997 -0.0109 0.0265  0.0282  166 SER   A N   
3692 C CA  A SER   A 166 ? 0.1484 0.2940 0.2081 -0.0018 0.0164  0.0565  166 SER   A CA  
3693 C CA  B SER   A 166 ? 0.1421 0.2675 0.2074 -0.0169 0.0249  0.0179  166 SER   A CA  
3694 C C   A SER   A 166 ? 0.1568 0.3179 0.2094 -0.0055 0.0042  0.0500  166 SER   A C   
3695 C C   B SER   A 166 ? 0.1580 0.2823 0.2017 -0.0225 0.0216  0.0170  166 SER   A C   
3696 O O   A SER   A 166 ? 0.1767 0.3365 0.2342 -0.0251 0.0058  0.0133  166 SER   A O   
3697 O O   B SER   A 166 ? 0.1683 0.2952 0.2089 -0.0306 0.0334  0.0082  166 SER   A O   
3698 C CB  A SER   A 166 ? 0.1545 0.2934 0.2427 -0.0036 0.0133  0.0511  166 SER   A CB  
3699 C CB  B SER   A 166 ? 0.1490 0.2716 0.2371 -0.0175 0.0202  0.0071  166 SER   A CB  
3700 O OG  A SER   A 166 ? 0.1750 0.2953 0.2936 -0.0128 0.0083  0.0601  166 SER   A OG  
3701 O OG  B SER   A 166 ? 0.1738 0.2779 0.2649 -0.0220 0.0230  0.0150  166 SER   A OG  
3712 N N   A SER   A 167 ? 0.1567 0.3204 0.1806 0.0125  0.0025  0.0704  167 SER   A N   
3713 N N   B SER   A 167 ? 0.1695 0.2818 0.1995 -0.0200 0.0195  0.0224  167 SER   A N   
3714 C CA  A SER   A 167 ? 0.1746 0.3238 0.1843 0.0149  0.0002  0.0616  167 SER   A CA  
3715 C CA  B SER   A 167 ? 0.1867 0.2864 0.1950 -0.0147 0.0246  0.0162  167 SER   A CA  
3716 C C   A SER   A 167 ? 0.1796 0.3224 0.1894 0.0257  0.0198  0.0563  167 SER   A C   
3717 C C   B SER   A 167 ? 0.1988 0.2902 0.2009 -0.0077 0.0186  0.0063  167 SER   A C   
3718 O O   A SER   A 167 ? 0.1986 0.3255 0.2112 0.0310  0.0109  0.0545  167 SER   A O   
3719 O O   B SER   A 167 ? 0.2076 0.2956 0.2082 -0.0090 0.0208  0.0063  167 SER   A O   
3720 C CB  A SER   A 167 ? 0.1790 0.3263 0.1972 0.0078  0.0026  0.0518  167 SER   A CB  
3721 C CB  B SER   A 167 ? 0.1932 0.2885 0.1918 -0.0121 0.0365  0.0085  167 SER   A CB  
3722 O OG  A SER   A 167 ? 0.1820 0.3256 0.2225 0.0009  0.0109  0.0453  167 SER   A OG  
3723 O OG  B SER   A 167 ? 0.1989 0.2893 0.1979 -0.0084 0.0474  0.0051  167 SER   A OG  
3734 N N   A PHE   A 168 ? 0.1655 0.3190 0.1963 0.0360  0.0217  0.0465  168 PHE   A N   
3735 N N   B PHE   A 168 ? 0.2041 0.2896 0.2051 0.0004  0.0029  -0.0022 168 PHE   A N   
3736 C CA  A PHE   A 168 ? 0.1576 0.3165 0.2256 0.0335  0.0245  0.0362  168 PHE   A CA  
3737 C CA  B PHE   A 168 ? 0.2147 0.2873 0.2255 0.0020  -0.0064 -0.0104 168 PHE   A CA  
3738 C C   A PHE   A 168 ? 0.1646 0.3398 0.2581 0.0214  0.0665  0.0150  168 PHE   A C   
3739 C C   B PHE   A 168 ? 0.2383 0.3087 0.2810 0.0007  0.0016  -0.0133 168 PHE   A C   
3740 O O   A PHE   A 168 ? 0.1691 0.3495 0.3158 0.0042  0.0647  0.0189  168 PHE   A O   
3741 O O   B PHE   A 168 ? 0.2352 0.3134 0.2999 0.0028  0.0050  -0.0132 168 PHE   A O   
3742 C CB  A PHE   A 168 ? 0.1585 0.2937 0.2287 0.0262  0.0064  0.0506  168 PHE   A CB  
3743 C CB  B PHE   A 168 ? 0.2073 0.2667 0.2069 -0.0053 -0.0183 -0.0144 168 PHE   A CB  
3744 C CG  A PHE   A 168 ? 0.1538 0.2723 0.2326 0.0179  0.0088  0.0671  168 PHE   A CG  
3745 C CG  B PHE   A 168 ? 0.1989 0.2475 0.1927 -0.0090 -0.0261 -0.0141 168 PHE   A CG  
3746 C CD1 A PHE   A 168 ? 0.1580 0.2691 0.2337 0.0054  0.0071  0.0824  168 PHE   A CD1 
3747 C CD1 B PHE   A 168 ? 0.1941 0.2406 0.1933 -0.0095 -0.0318 -0.0097 168 PHE   A CD1 
3748 C CD2 A PHE   A 168 ? 0.1531 0.2644 0.2438 0.0159  0.0291  0.0638  168 PHE   A CD2 
3749 C CD2 B PHE   A 168 ? 0.1992 0.2391 0.1900 -0.0068 -0.0292 -0.0179 168 PHE   A CD2 
3750 C CE1 A PHE   A 168 ? 0.1513 0.2626 0.2369 0.0032  0.0092  0.0833  168 PHE   A CE1 
3751 C CE1 B PHE   A 168 ? 0.1919 0.2401 0.1953 -0.0106 -0.0334 -0.0095 168 PHE   A CE1 
3752 C CE2 A PHE   A 168 ? 0.1576 0.2566 0.2544 0.0117  0.0277  0.0764  168 PHE   A CE2 
3753 C CE2 B PHE   A 168 ? 0.2016 0.2379 0.1977 -0.0065 -0.0338 -0.0129 168 PHE   A CE2 
3754 C CZ  A PHE   A 168 ? 0.1559 0.2575 0.2463 0.0076  0.0236  0.0820  168 PHE   A CZ  
3755 C CZ  B PHE   A 168 ? 0.1991 0.2394 0.2015 -0.0092 -0.0330 -0.0078 168 PHE   A CZ  
3774 N N   A LEU   A 169 ? 0.1957 0.3526 0.2742 0.0191  0.0907  -0.0171 169 LEU   A N   
3775 N N   B LEU   A 169 ? 0.2696 0.3261 0.3311 -0.0034 0.0067  -0.0181 169 LEU   A N   
3776 C CA  A LEU   A 169 ? 0.2367 0.3706 0.3493 0.0228  0.0668  -0.0243 169 LEU   A CA  
3777 C CA  B LEU   A 169 ? 0.3025 0.3472 0.3874 -0.0053 0.0066  -0.0121 169 LEU   A CA  
3778 C C   A LEU   A 169 ? 0.2321 0.3663 0.3637 0.0221  0.0740  -0.0142 169 LEU   A C   
3779 C C   B LEU   A 169 ? 0.3126 0.3528 0.4097 -0.0126 0.0040  -0.0012 169 LEU   A C   
3780 O O   A LEU   A 169 ? 0.2409 0.3680 0.3675 0.0274  0.0726  -0.0139 169 LEU   A O   
3781 O O   B LEU   A 169 ? 0.3279 0.3605 0.4166 -0.0161 0.0018  0.0056  169 LEU   A O   
3782 C CB  A LEU   A 169 ? 0.2792 0.3898 0.3788 0.0198  0.0398  -0.0398 169 LEU   A CB  
3783 C CB  B LEU   A 169 ? 0.3201 0.3615 0.4046 -0.0023 0.0112  -0.0163 169 LEU   A CB  
3784 C CG  A LEU   A 169 ? 0.3133 0.4062 0.4152 0.0123  0.0147  -0.0610 169 LEU   A CG  
3785 C CG  B LEU   A 169 ? 0.3321 0.3740 0.4269 -0.0011 0.0130  -0.0272 169 LEU   A CG  
3786 C CD1 A LEU   A 169 ? 0.3240 0.4090 0.4282 0.0091  0.0032  -0.0653 169 LEU   A CD1 
3787 C CD1 B LEU   A 169 ? 0.3326 0.3774 0.4306 -0.0010 0.0164  -0.0311 169 LEU   A CD1 
3788 C CD2 A LEU   A 169 ? 0.3288 0.4144 0.4176 0.0088  0.0092  -0.0701 169 LEU   A CD2 
3789 C CD2 B LEU   A 169 ? 0.3383 0.3792 0.4328 -0.0004 0.0124  -0.0316 169 LEU   A CD2 
3790 O OXT A LEU   A 169 ? 0.2230 0.3639 0.3492 0.0128  0.0873  -0.0123 169 LEU   A OXT 
3791 O OXT B LEU   A 169 ? 0.3044 0.3504 0.4206 -0.0153 0.0051  -0.0034 169 LEU   A OXT 
3814 N N   A SER   B 1   ? 0.3753 0.3616 0.3833 -0.1017 -0.0635 0.0330  1   SER   B N   
3815 N N   B SER   B 1   ? 0.3329 0.3282 0.3564 -0.0905 -0.0523 0.0096  1   SER   B N   
3816 C CA  A SER   B 1   ? 0.3695 0.3647 0.3923 -0.1092 -0.0635 0.0282  1   SER   B CA  
3817 C CA  B SER   B 1   ? 0.3271 0.3323 0.3596 -0.0952 -0.0546 0.0053  1   SER   B CA  
3818 C C   A SER   B 1   ? 0.3445 0.3649 0.3737 -0.1157 -0.0736 0.0501  1   SER   B C   
3819 C C   B SER   B 1   ? 0.3086 0.3354 0.3481 -0.0987 -0.0674 0.0239  1   SER   B C   
3820 O O   A SER   B 1   ? 0.3543 0.3705 0.3479 -0.1102 -0.0695 0.0478  1   SER   B O   
3821 O O   B SER   B 1   ? 0.3087 0.3368 0.3333 -0.0999 -0.0706 0.0167  1   SER   B O   
3822 C CB  A SER   B 1   ? 0.3841 0.3657 0.3927 -0.1107 -0.0532 0.0104  1   SER   B CB  
3823 C CB  B SER   B 1   ? 0.3360 0.3313 0.3567 -0.0968 -0.0454 -0.0119 1   SER   B CB  
3824 O OG  A SER   B 1   ? 0.3955 0.3717 0.4362 -0.1117 -0.0495 0.0044  1   SER   B OG  
3825 O OG  B SER   B 1   ? 0.3422 0.3334 0.3812 -0.0996 -0.0402 -0.0163 1   SER   B OG  
3840 N N   A MET   B 2   ? 0.3179 0.3588 0.3621 -0.1221 -0.0793 0.0919  2   MET   B N   
3841 N N   B MET   B 2   ? 0.2956 0.3363 0.3368 -0.0971 -0.0752 0.0577  2   MET   B N   
3842 C CA  A MET   B 2   ? 0.3042 0.3603 0.3741 -0.1073 -0.0845 0.1175  2   MET   B CA  
3843 C CA  B MET   B 2   ? 0.2880 0.3372 0.3367 -0.0859 -0.0832 0.0880  2   MET   B CA  
3844 C C   A MET   B 2   ? 0.2741 0.3363 0.3316 -0.0902 -0.1004 0.1425  2   MET   B C   
3845 C C   B MET   B 2   ? 0.2715 0.3277 0.3158 -0.0799 -0.0910 0.1193  2   MET   B C   
3846 O O   A MET   B 2   ? 0.2655 0.3442 0.3294 -0.0870 -0.1137 0.1459  2   MET   B O   
3847 O O   B MET   B 2   ? 0.2752 0.3437 0.3208 -0.0696 -0.0828 0.1154  2   MET   B O   
3848 C CB  A MET   B 2   ? 0.3341 0.3956 0.4557 -0.0951 -0.0649 0.0908  2   MET   B CB  
3849 C CB  B MET   B 2   ? 0.3041 0.3513 0.3727 -0.0736 -0.0746 0.0802  2   MET   B CB  
3850 C CG  A MET   B 2   ? 0.3641 0.4266 0.5273 -0.0769 -0.0457 0.0725  2   MET   B CG  
3851 C CG  B MET   B 2   ? 0.3181 0.3663 0.3984 -0.0590 -0.0671 0.0833  2   MET   B CG  
3852 S SD  A MET   B 2   ? 0.3925 0.4518 0.6101 -0.0591 -0.0354 0.0641  2   MET   B SD  
3853 S SD  B MET   B 2   ? 0.3302 0.3836 0.4113 -0.0465 -0.0680 0.0901  2   MET   B SD  
3854 C CE  A MET   B 2   ? 0.3999 0.4556 0.5979 -0.0537 -0.0296 0.0726  2   MET   B CE  
3855 C CE  B MET   B 2   ? 0.3328 0.3903 0.4262 -0.0441 -0.0639 0.0867  2   MET   B CE  
3874 N N   . VAL   B 3   ? 0.2522 0.2983 0.3013 -0.0879 -0.1034 0.1450  3   VAL   B N   
3875 C CA  . VAL   B 3   ? 0.2358 0.2497 0.3052 -0.0741 -0.0939 0.1259  3   VAL   B CA  
3876 C C   . VAL   B 3   ? 0.2123 0.2333 0.2607 -0.0620 -0.0770 0.0997  3   VAL   B C   
3877 O O   . VAL   B 3   ? 0.2122 0.2517 0.2676 -0.0685 -0.0775 0.1131  3   VAL   B O   
3878 C CB  . VAL   B 3   ? 0.2515 0.2382 0.3695 -0.0747 -0.0831 0.1012  3   VAL   B CB  
3879 C CG1 . VAL   B 3   ? 0.2668 0.2312 0.3836 -0.0756 -0.0810 0.1010  3   VAL   B CG1 
3880 C CG2 . VAL   B 3   ? 0.2445 0.2380 0.3934 -0.0682 -0.0755 0.1080  3   VAL   B CG2 
3891 N N   . ASN   B 4   ? 0.1934 0.1999 0.2232 -0.0506 -0.0590 0.0690  4   ASN   B N   
3892 C CA  . ASN   B 4   ? 0.1936 0.1986 0.1878 -0.0457 -0.0449 0.0262  4   ASN   B CA  
3893 C C   . ASN   B 4   ? 0.2035 0.2181 0.1809 -0.0456 -0.0352 0.0185  4   ASN   B C   
3894 O O   . ASN   B 4   ? 0.2073 0.2244 0.1933 -0.0472 -0.0312 0.0009  4   ASN   B O   
3895 C CB  . ASN   B 4   ? 0.1941 0.1938 0.1753 -0.0364 -0.0432 0.0207  4   ASN   B CB  
3896 C CG  . ASN   B 4   ? 0.1897 0.1794 0.1738 -0.0322 -0.0462 0.0208  4   ASN   B CG  
3897 O OD1 . ASN   B 4   ? 0.1921 0.1693 0.1793 -0.0307 -0.0477 0.0219  4   ASN   B OD1 
3898 N ND2 . ASN   B 4   ? 0.2008 0.1869 0.1789 -0.0147 -0.0325 0.0170  4   ASN   B ND2 
3905 N N   . SER   B 5   ? 0.2180 0.2332 0.1996 -0.0525 -0.0214 0.0339  5   SER   B N   
3906 C CA  . SER   B 5   ? 0.2512 0.2620 0.2274 -0.0429 -0.0055 0.0343  5   SER   B CA  
3907 C C   . SER   B 5   ? 0.2709 0.2636 0.2572 -0.0583 0.0159  0.0347  5   SER   B C   
3908 O O   . SER   B 5   ? 0.2886 0.2592 0.3302 -0.0555 0.0463  0.0194  5   SER   B O   
3909 C CB  . SER   B 5   ? 0.2699 0.2822 0.2624 -0.0283 0.0074  0.0382  5   SER   B CB  
3910 O OG  . SER   B 5   ? 0.3041 0.3110 0.3329 -0.0149 0.0220  0.0315  5   SER   B OG  
3916 N N   . PHE   B 6   ? 0.2823 0.2797 0.2433 -0.0652 0.0251  0.0448  6   PHE   B N   
3917 C CA  . PHE   B 6   ? 0.2873 0.2862 0.2154 -0.0828 0.0275  0.0256  6   PHE   B CA  
3918 C C   . PHE   B 6   ? 0.3459 0.3278 0.2617 -0.0932 0.0557  -0.0023 6   PHE   B C   
3919 O O   . PHE   B 6   ? 0.3622 0.3779 0.3024 -0.0811 0.0396  -0.0214 6   PHE   B O   
3920 C CB  . PHE   B 6   ? 0.2504 0.2608 0.1875 -0.0719 0.0135  0.0231  6   PHE   B CB  
3921 C CG  . PHE   B 6   ? 0.2152 0.2340 0.1788 -0.0617 -0.0012 0.0136  6   PHE   B CG  
3922 C CD1 . PHE   B 6   ? 0.2178 0.2095 0.1557 -0.0520 -0.0140 0.0106  6   PHE   B CD1 
3923 C CD2 . PHE   B 6   ? 0.1895 0.2406 0.1992 -0.0509 -0.0049 0.0372  6   PHE   B CD2 
3924 C CE1 . PHE   B 6   ? 0.2087 0.1986 0.1755 -0.0409 -0.0190 0.0137  6   PHE   B CE1 
3925 C CE2 . PHE   B 6   ? 0.1889 0.2311 0.2386 -0.0337 -0.0055 0.0379  6   PHE   B CE2 
3926 C CZ  . PHE   B 6   ? 0.1950 0.2106 0.2053 -0.0317 -0.0141 0.0160  6   PHE   B CZ  
3936 N N   A SER   B 7   ? 0.3734 0.3113 0.2688 -0.1123 0.0842  -0.0203 7   SER   B N   
3937 N N   B SER   B 7   ? 0.3626 0.3192 0.2810 -0.0962 0.0694  -0.0066 7   SER   B N   
3938 C CA  A SER   B 7   ? 0.3981 0.3115 0.3063 -0.1100 0.1031  -0.0349 7   SER   B CA  
3939 C CA  B SER   B 7   ? 0.3771 0.3184 0.3095 -0.0898 0.0743  -0.0119 7   SER   B CA  
3940 C C   A SER   B 7   ? 0.3983 0.3013 0.2773 -0.1131 0.1113  -0.0349 7   SER   B C   
3941 C C   B SER   B 7   ? 0.3794 0.3081 0.2963 -0.0916 0.0735  -0.0134 7   SER   B C   
3942 O O   A SER   B 7   ? 0.3976 0.2987 0.3009 -0.1155 0.1014  -0.0358 7   SER   B O   
3943 O O   B SER   B 7   ? 0.3785 0.3075 0.3075 -0.0924 0.0682  -0.0113 7   SER   B O   
3944 C CB  A SER   B 7   ? 0.4154 0.3209 0.3676 -0.0994 0.1148  -0.0347 7   SER   B CB  
3945 C CB  B SER   B 7   ? 0.3858 0.3276 0.3409 -0.0798 0.0779  -0.0111 7   SER   B CB  
3946 O OG  A SER   B 7   ? 0.4261 0.3328 0.4093 -0.0929 0.1126  -0.0174 7   SER   B OG  
3947 O OG  B SER   B 7   ? 0.3908 0.3358 0.3741 -0.0725 0.0751  -0.0018 7   SER   B OG  
3958 N N   A GLY   B 8   ? 0.4014 0.2949 0.2741 -0.1021 0.1207  -0.0419 8   GLY   B N   
3959 N N   B GLY   B 8   ? 0.3831 0.2989 0.2924 -0.0883 0.0781  -0.0212 8   GLY   B N   
3960 C CA  A GLY   B 8   ? 0.3922 0.2803 0.2625 -0.0949 0.1261  -0.0532 8   GLY   B CA  
3961 C CA  B GLY   B 8   ? 0.3801 0.2853 0.2802 -0.0868 0.0827  -0.0333 8   GLY   B CA  
3962 C C   A GLY   B 8   ? 0.3773 0.2619 0.2556 -0.0912 0.1126  -0.0558 8   GLY   B C   
3963 C C   B GLY   B 8   ? 0.3731 0.2685 0.2635 -0.0863 0.0810  -0.0429 8   GLY   B C   
3964 O O   A GLY   B 8   ? 0.3786 0.2641 0.2746 -0.0875 0.1202  -0.0625 8   GLY   B O   
3965 O O   B GLY   B 8   ? 0.3750 0.2746 0.2744 -0.0827 0.0801  -0.0457 8   GLY   B O   
3972 N N   . TYR   B 9   ? 0.3670 0.2481 0.2435 -0.0825 0.0825  -0.0498 9   TYR   B N   
3973 C CA  . TYR   B 9   ? 0.3476 0.2161 0.2066 -0.0661 0.0604  -0.0316 9   TYR   B CA  
3974 C C   . TYR   B 9   ? 0.3443 0.2195 0.1900 -0.0625 0.0343  -0.0191 9   TYR   B C   
3975 O O   . TYR   B 9   ? 0.3676 0.2423 0.2446 -0.0715 0.0286  -0.0029 9   TYR   B O   
3976 C CB  . TYR   B 9   ? 0.3404 0.1873 0.2398 -0.0534 0.0572  -0.0262 9   TYR   B CB  
3977 C CG  . TYR   B 9   ? 0.3344 0.1641 0.2327 -0.0585 0.0565  -0.0350 9   TYR   B CG  
3978 C CD1 . TYR   B 9   ? 0.3438 0.1643 0.2632 -0.0776 0.0601  -0.0262 9   TYR   B CD1 
3979 C CD2 . TYR   B 9   ? 0.3190 0.1603 0.2171 -0.0485 0.0562  -0.0446 9   TYR   B CD2 
3980 C CE1 . TYR   B 9   ? 0.3398 0.1715 0.2588 -0.0887 0.0671  -0.0395 9   TYR   B CE1 
3981 C CE2 . TYR   B 9   ? 0.3214 0.1643 0.2332 -0.0575 0.0568  -0.0422 9   TYR   B CE2 
3982 C CZ  . TYR   B 9   ? 0.3291 0.1807 0.2565 -0.0782 0.0651  -0.0568 9   TYR   B CZ  
3983 O OH  . TYR   B 9   ? 0.3202 0.2028 0.2680 -0.0910 0.0758  -0.0771 9   TYR   B OH  
3994 N N   . LEU   B 10  ? 0.3139 0.1939 0.1772 -0.0518 0.0209  -0.0274 10  LEU   B N   
3995 C CA  . LEU   B 10  ? 0.2977 0.1872 0.1855 -0.0590 -0.0070 -0.0282 10  LEU   B CA  
3996 C C   . LEU   B 10  ? 0.2807 0.1885 0.1809 -0.0605 -0.0288 -0.0224 10  LEU   B C   
3997 O O   . LEU   B 10  ? 0.2664 0.1900 0.1875 -0.0531 -0.0264 -0.0193 10  LEU   B O   
3998 C CB  . LEU   B 10  ? 0.3052 0.1835 0.2130 -0.0605 -0.0312 -0.0123 10  LEU   B CB  
3999 C CG  . LEU   B 10  ? 0.3220 0.1908 0.2437 -0.0624 -0.0621 -0.0060 10  LEU   B CG  
4000 C CD1 . LEU   B 10  ? 0.3363 0.2010 0.2781 -0.0588 -0.0599 -0.0072 10  LEU   B CD1 
4001 C CD2 . LEU   B 10  ? 0.3314 0.1988 0.2823 -0.0611 -0.0504 0.0172  10  LEU   B CD2 
4013 N N   . LYS   B 11  ? 0.2996 0.2181 0.1853 -0.0510 -0.0415 -0.0136 11  LYS   B N   
4014 C CA  . LYS   B 11  ? 0.3126 0.2448 0.2265 -0.0422 -0.0667 -0.0239 11  LYS   B CA  
4015 C C   . LYS   B 11  ? 0.2974 0.2236 0.2441 -0.0690 -0.0542 -0.0367 11  LYS   B C   
4016 O O   . LYS   B 11  ? 0.3146 0.2417 0.2951 -0.0857 -0.0379 -0.0784 11  LYS   B O   
4017 C CB  . LYS   B 11  ? 0.3444 0.2999 0.3018 -0.0071 -0.0657 -0.0276 11  LYS   B CB  
4018 C CG  . LYS   B 11  ? 0.3723 0.3366 0.3689 0.0139  -0.0564 -0.0267 11  LYS   B CG  
4019 C CD  . LYS   B 11  ? 0.3958 0.3578 0.4392 0.0177  -0.0449 -0.0284 11  LYS   B CD  
4020 C CE  . LYS   B 11  ? 0.4120 0.3690 0.4925 0.0124  -0.0391 -0.0310 11  LYS   B CE  
4021 N NZ  . LYS   B 11  ? 0.4212 0.3735 0.5169 0.0081  -0.0389 -0.0279 11  LYS   B NZ  
4035 N N   . LEU   B 12  ? 0.2659 0.1988 0.2409 -0.0645 -0.0616 -0.0349 12  LEU   B N   
4036 C CA  . LEU   B 12  ? 0.2451 0.1808 0.2644 -0.0573 -0.0590 -0.0135 12  LEU   B CA  
4037 C C   . LEU   B 12  ? 0.2348 0.1779 0.2715 -0.0592 -0.0678 -0.0133 12  LEU   B C   
4038 O O   . LEU   B 12  ? 0.2382 0.1790 0.2870 -0.0644 -0.0651 -0.0135 12  LEU   B O   
4039 C CB  . LEU   B 12  ? 0.2392 0.1625 0.2505 -0.0469 -0.0474 -0.0095 12  LEU   B CB  
4040 C CG  . LEU   B 12  ? 0.2305 0.1652 0.2555 -0.0412 -0.0328 -0.0071 12  LEU   B CG  
4041 C CD1 . LEU   B 12  ? 0.2367 0.1653 0.2490 -0.0266 -0.0272 0.0156  12  LEU   B CD1 
4042 C CD2 . LEU   B 12  ? 0.2347 0.1694 0.2744 -0.0383 -0.0217 -0.0302 12  LEU   B CD2 
4054 N N   . THR   B 13  ? 0.2282 0.1821 0.2618 -0.0576 -0.0678 -0.0291 13  THR   B N   
4055 C CA  . THR   B 13  ? 0.2287 0.1964 0.2507 -0.0604 -0.0743 -0.0152 13  THR   B CA  
4056 C C   . THR   B 13  ? 0.2531 0.2086 0.2676 -0.0654 -0.0855 -0.0014 13  THR   B C   
4057 O O   . THR   B 13  ? 0.2678 0.2039 0.2973 -0.0644 -0.0489 -0.0051 13  THR   B O   
4058 C CB  . THR   B 13  ? 0.2104 0.1979 0.2431 -0.0541 -0.0696 -0.0087 13  THR   B CB  
4059 O OG1 . THR   B 13  ? 0.2015 0.1876 0.2712 -0.0457 -0.0631 -0.0106 13  THR   B OG1 
4060 C CG2 . THR   B 13  ? 0.2156 0.2062 0.2589 -0.0494 -0.0485 0.0031  13  THR   B CG2 
4068 N N   A ASP   B 14  ? 0.2630 0.2247 0.2781 -0.0703 -0.1185 0.0060  14  ASP   B N   
4069 N N   B ASP   B 14  ? 0.2590 0.2192 0.2808 -0.0645 -0.0963 0.0084  14  ASP   B N   
4070 C CA  A ASP   B 14  ? 0.2763 0.2396 0.2972 -0.0680 -0.1264 0.0270  14  ASP   B CA  
4071 C CA  B ASP   B 14  ? 0.2683 0.2285 0.2934 -0.0604 -0.0943 0.0188  14  ASP   B CA  
4072 C C   A ASP   B 14  ? 0.2703 0.2140 0.2690 -0.0715 -0.1025 0.0283  14  ASP   B C   
4073 C C   B ASP   B 14  ? 0.2589 0.2093 0.2637 -0.0616 -0.0935 0.0214  14  ASP   B C   
4074 O O   A ASP   B 14  ? 0.3022 0.2261 0.2791 -0.0695 -0.0904 0.0384  14  ASP   B O   
4075 O O   B ASP   B 14  ? 0.2764 0.2162 0.2635 -0.0589 -0.0937 0.0262  14  ASP   B O   
4076 C CB  A ASP   B 14  ? 0.2973 0.2771 0.3812 -0.0645 -0.1354 0.0278  14  ASP   B CB  
4077 C CB  B ASP   B 14  ? 0.2877 0.2570 0.3495 -0.0570 -0.0872 0.0200  14  ASP   B CB  
4078 C CG  A ASP   B 14  ? 0.3259 0.3079 0.4654 -0.0557 -0.1166 0.0072  14  ASP   B CG  
4079 C CG  B ASP   B 14  ? 0.3088 0.2830 0.4053 -0.0525 -0.0709 0.0122  14  ASP   B CG  
4080 O OD1 A ASP   B 14  ? 0.3426 0.3169 0.4819 -0.0564 -0.1107 -0.0086 14  ASP   B OD1 
4081 O OD1 B ASP   B 14  ? 0.3208 0.2935 0.4139 -0.0528 -0.0603 0.0071  14  ASP   B OD1 
4082 O OD2 A ASP   B 14  ? 0.3341 0.3254 0.5055 -0.0521 -0.1020 0.0070  14  ASP   B OD2 
4083 O OD2 B ASP   B 14  ? 0.3123 0.2939 0.4268 -0.0529 -0.0662 0.0130  14  ASP   B OD2 
4092 N N   . ASN   B 15  ? 0.2319 0.1889 0.2424 -0.0583 -0.0947 0.0259  15  ASN   B N   
4093 C CA  . ASN   B 15  ? 0.1903 0.1656 0.2335 -0.0397 -0.0614 0.0161  15  ASN   B CA  
4094 C C   . ASN   B 15  ? 0.1758 0.1532 0.2166 -0.0263 -0.0438 0.0073  15  ASN   B C   
4095 O O   . ASN   B 15  ? 0.1713 0.1510 0.2245 -0.0237 -0.0465 -0.0091 15  ASN   B O   
4096 C CB  . ASN   B 15  ? 0.1830 0.1628 0.2569 -0.0178 -0.0521 0.0114  15  ASN   B CB  
4097 C CG  . ASN   B 15  ? 0.1721 0.1613 0.2313 -0.0208 -0.0304 0.0079  15  ASN   B CG  
4098 O OD1 . ASN   B 15  ? 0.1804 0.1862 0.2742 -0.0424 -0.0390 0.0162  15  ASN   B OD1 
4099 N ND2 . ASN   B 15  ? 0.1689 0.1458 0.2240 -0.0120 -0.0079 -0.0090 15  ASN   B ND2 
4107 N N   . VAL   B 16  ? 0.1753 0.1489 0.2219 -0.0335 -0.0503 0.0007  16  VAL   B N   
4108 C CA  . VAL   B 16  ? 0.1717 0.1573 0.1955 -0.0290 -0.0359 -0.0209 16  VAL   B CA  
4109 C C   . VAL   B 16  ? 0.1799 0.1684 0.1911 -0.0356 -0.0361 -0.0161 16  VAL   B C   
4110 O O   . VAL   B 16  ? 0.1854 0.1746 0.2236 -0.0312 -0.0378 -0.0267 16  VAL   B O   
4111 C CB  . VAL   B 16  ? 0.1784 0.1600 0.2126 -0.0153 -0.0286 -0.0202 16  VAL   B CB  
4112 C CG1 . VAL   B 16  ? 0.1892 0.1560 0.2029 -0.0054 -0.0260 -0.0217 16  VAL   B CG1 
4113 C CG2 . VAL   B 16  ? 0.1778 0.1674 0.2392 -0.0130 -0.0351 -0.0242 16  VAL   B CG2 
4123 N N   . TYR   B 17  ? 0.1851 0.1677 0.1831 -0.0351 -0.0402 -0.0130 17  TYR   B N   
4124 C CA  . TYR   B 17  ? 0.1956 0.1790 0.1839 -0.0399 -0.0334 0.0011  17  TYR   B CA  
4125 C C   . TYR   B 17  ? 0.1838 0.1551 0.1828 -0.0424 -0.0243 -0.0074 17  TYR   B C   
4126 O O   . TYR   B 17  ? 0.1783 0.1644 0.1834 -0.0324 -0.0300 -0.0227 17  TYR   B O   
4127 C CB  . TYR   B 17  ? 0.2288 0.2129 0.2073 -0.0256 -0.0395 0.0374  17  TYR   B CB  
4128 C CG  . TYR   B 17  ? 0.2542 0.2612 0.2470 -0.0259 -0.0553 0.0483  17  TYR   B CG  
4129 C CD1 . TYR   B 17  ? 0.2648 0.2737 0.2852 -0.0241 -0.0675 0.0693  17  TYR   B CD1 
4130 C CD2 . TYR   B 17  ? 0.2790 0.2929 0.2816 -0.0188 -0.0659 0.0442  17  TYR   B CD2 
4131 C CE1 . TYR   B 17  ? 0.2825 0.2962 0.2993 -0.0179 -0.0780 0.0543  17  TYR   B CE1 
4132 C CE2 . TYR   B 17  ? 0.2952 0.3077 0.3103 -0.0070 -0.0755 0.0526  17  TYR   B CE2 
4133 C CZ  . TYR   B 17  ? 0.3015 0.3097 0.3167 -0.0052 -0.0814 0.0519  17  TYR   B CZ  
4134 O OH  . TYR   B 17  ? 0.3168 0.3233 0.3435 0.0056  -0.0888 0.0455  17  TYR   B OH  
4144 N N   . ILE   B 18  ? 0.1968 0.1515 0.1832 -0.0392 -0.0181 -0.0091 18  ILE   B N   
4145 C CA  . ILE   B 18  ? 0.2044 0.1498 0.1721 -0.0368 -0.0243 -0.0076 18  ILE   B CA  
4146 C C   . ILE   B 18  ? 0.2172 0.1563 0.1610 -0.0444 -0.0084 -0.0235 18  ILE   B C   
4147 O O   . ILE   B 18  ? 0.2389 0.1705 0.1875 -0.0372 0.0065  -0.0304 18  ILE   B O   
4148 C CB  . ILE   B 18  ? 0.2090 0.1531 0.1761 -0.0376 -0.0253 -0.0138 18  ILE   B CB  
4149 C CG1 . ILE   B 18  ? 0.2046 0.1612 0.1825 -0.0448 -0.0141 -0.0065 18  ILE   B CG1 
4150 C CG2 . ILE   B 18  ? 0.2121 0.1579 0.1970 -0.0387 -0.0244 -0.0033 18  ILE   B CG2 
4151 C CD1 . ILE   B 18  ? 0.2076 0.1861 0.2059 -0.0472 -0.0181 0.0162  18  ILE   B CD1 
4163 N N   . LYS   B 19  ? 0.2173 0.1614 0.1808 -0.0297 0.0264  -0.0304 19  LYS   B N   
4164 C CA  . LYS   B 19  ? 0.2219 0.1621 0.1866 -0.0332 0.0235  -0.0338 19  LYS   B CA  
4165 C C   . LYS   B 19  ? 0.2010 0.1582 0.2102 -0.0318 0.0263  -0.0389 19  LYS   B C   
4166 O O   . LYS   B 19  ? 0.1905 0.1608 0.1976 -0.0164 0.0136  -0.0347 19  LYS   B O   
4167 C CB  . LYS   B 19  ? 0.2435 0.1765 0.2059 -0.0340 0.0305  -0.0214 19  LYS   B CB  
4168 C CG  . LYS   B 19  ? 0.2696 0.1977 0.2327 -0.0469 0.0320  -0.0215 19  LYS   B CG  
4169 C CD  . LYS   B 19  ? 0.2973 0.2315 0.2318 -0.0533 0.0407  -0.0220 19  LYS   B CD  
4170 C CE  . LYS   B 19  ? 0.3166 0.2604 0.2570 -0.0520 0.0447  -0.0193 19  LYS   B CE  
4171 N NZ  . LYS   B 19  ? 0.3323 0.2806 0.2455 -0.0480 0.0436  -0.0116 19  LYS   B NZ  
4185 N N   . ASN   B 20  ? 0.2059 0.1673 0.2385 -0.0272 0.0340  -0.0529 20  ASN   B N   
4186 C CA  . ASN   B 20  ? 0.2034 0.1848 0.2708 -0.0169 0.0371  -0.0733 20  ASN   B CA  
4187 C C   . ASN   B 20  ? 0.2023 0.2015 0.2720 -0.0215 0.0559  -0.0825 20  ASN   B C   
4188 O O   . ASN   B 20  ? 0.2196 0.2375 0.2951 -0.0402 0.0556  -0.0827 20  ASN   B O   
4189 C CB  . ASN   B 20  ? 0.2304 0.1958 0.3023 0.0062  0.0243  -0.0695 20  ASN   B CB  
4190 C CG  . ASN   B 20  ? 0.2551 0.2030 0.3218 0.0383  0.0311  -0.0708 20  ASN   B CG  
4191 O OD1 . ASN   B 20  ? 0.2859 0.2310 0.3483 0.0562  0.0315  -0.0752 20  ASN   B OD1 
4192 N ND2 . ASN   B 20  ? 0.2455 0.1963 0.3136 0.0380  0.0142  -0.0633 20  ASN   B ND2 
4199 N N   . ALA   B 21  ? 0.1987 0.1853 0.2726 -0.0311 0.0560  -0.0561 21  ALA   B N   
4200 C CA  . ALA   B 21  ? 0.2093 0.1950 0.2862 -0.0341 0.0382  -0.0444 21  ALA   B CA  
4201 C C   . ALA   B 21  ? 0.2096 0.1719 0.2701 -0.0235 0.0325  -0.0281 21  ALA   B C   
4202 O O   . ALA   B 21  ? 0.2098 0.1590 0.2689 -0.0299 0.0329  -0.0248 21  ALA   B O   
4203 C CB  . ALA   B 21  ? 0.2324 0.2201 0.2966 -0.0487 0.0413  -0.0342 21  ALA   B CB  
4209 N N   . ASP   B 22  ? 0.2004 0.1684 0.2620 -0.0252 0.0226  -0.0244 22  ASP   B N   
4210 C CA  . ASP   B 22  ? 0.1915 0.1594 0.2620 -0.0075 0.0160  -0.0143 22  ASP   B CA  
4211 C C   . ASP   B 22  ? 0.1875 0.1515 0.2112 -0.0143 0.0099  -0.0078 22  ASP   B C   
4212 O O   . ASP   B 22  ? 0.1894 0.1559 0.2151 -0.0122 0.0069  -0.0022 22  ASP   B O   
4213 C CB  . ASP   B 22  ? 0.1902 0.1712 0.2876 -0.0033 0.0213  -0.0028 22  ASP   B CB  
4214 C CG  . ASP   B 22  ? 0.1925 0.1937 0.3442 -0.0013 0.0008  -0.0039 22  ASP   B CG  
4215 O OD1 . ASP   B 22  ? 0.2070 0.1759 0.3391 0.0031  -0.0146 -0.0068 22  ASP   B OD1 
4216 O OD2 . ASP   B 22  ? 0.2012 0.2266 0.3998 0.0037  -0.0246 -0.0173 22  ASP   B OD2 
4221 N N   . ILE   B 23  ? 0.1841 0.1449 0.1850 -0.0117 0.0098  0.0126  23  ILE   B N   
4222 C CA  . ILE   B 23  ? 0.1744 0.1480 0.1760 -0.0123 -0.0052 0.0060  23  ILE   B CA  
4223 C C   . ILE   B 23  ? 0.1662 0.1518 0.1695 -0.0092 -0.0163 0.0027  23  ILE   B C   
4224 O O   . ILE   B 23  ? 0.1584 0.1527 0.1666 -0.0129 -0.0053 0.0035  23  ILE   B O   
4225 C CB  . ILE   B 23  ? 0.1668 0.1558 0.2018 -0.0187 -0.0052 0.0150  23  ILE   B CB  
4226 C CG1 . ILE   B 23  ? 0.1687 0.1623 0.2181 -0.0165 0.0010  0.0308  23  ILE   B CG1 
4227 C CG2 . ILE   B 23  ? 0.1808 0.1741 0.2187 -0.0196 0.0044  0.0068  23  ILE   B CG2 
4228 C CD1 . ILE   B 23  ? 0.1798 0.1666 0.2217 -0.0147 0.0089  0.0259  23  ILE   B CD1 
4240 N N   . VAL   B 24  ? 0.1723 0.1462 0.1899 -0.0070 -0.0135 0.0036  24  VAL   B N   
4241 C CA  . VAL   B 24  ? 0.1680 0.1527 0.2194 -0.0106 -0.0137 -0.0014 24  VAL   B CA  
4242 C C   . VAL   B 24  ? 0.1670 0.1544 0.2206 -0.0184 -0.0050 0.0062  24  VAL   B C   
4243 O O   . VAL   B 24  ? 0.1611 0.1641 0.2213 -0.0190 -0.0052 0.0119  24  VAL   B O   
4244 C CB  . VAL   B 24  ? 0.1763 0.1775 0.2140 -0.0007 -0.0256 0.0046  24  VAL   B CB  
4245 C CG1 . VAL   B 24  ? 0.1817 0.1848 0.2421 -0.0098 -0.0348 0.0078  24  VAL   B CG1 
4246 C CG2 . VAL   B 24  ? 0.1817 0.2048 0.2107 0.0070  -0.0234 -0.0042 24  VAL   B CG2 
4256 N N   . GLU   B 25  ? 0.1872 0.1616 0.2191 -0.0109 0.0090  0.0101  25  GLU   B N   
4257 C CA  . GLU   B 25  ? 0.1957 0.1857 0.2291 0.0031  0.0240  0.0018  25  GLU   B CA  
4258 C C   . GLU   B 25  ? 0.1935 0.1783 0.2030 -0.0076 0.0117  0.0055  25  GLU   B C   
4259 O O   . GLU   B 25  ? 0.1945 0.1907 0.2228 -0.0083 0.0135  0.0072  25  GLU   B O   
4260 C CB  . GLU   B 25  ? 0.2241 0.2261 0.2757 0.0229  0.0371  0.0002  25  GLU   B CB  
4261 C CG  . GLU   B 25  ? 0.2671 0.2850 0.3862 0.0309  0.0353  0.0047  25  GLU   B CG  
4262 C CD  . GLU   B 25  ? 0.3128 0.3561 0.4810 0.0237  0.0368  -0.0036 25  GLU   B CD  
4263 O OE1 . GLU   B 25  ? 0.3267 0.3911 0.5027 0.0296  0.0410  0.0003  25  GLU   B OE1 
4264 O OE2 . GLU   B 25  ? 0.3239 0.3811 0.5032 0.0156  0.0301  -0.0166 25  GLU   B OE2 
4271 N N   . GLU   B 26  ? 0.1883 0.1695 0.1884 -0.0243 0.0133  0.0005  26  GLU   B N   
4272 C CA  . GLU   B 26  ? 0.1902 0.1873 0.1958 -0.0344 -0.0052 0.0120  26  GLU   B CA  
4273 C C   . GLU   B 26  ? 0.1704 0.1871 0.1813 -0.0235 -0.0020 0.0250  26  GLU   B C   
4274 O O   . GLU   B 26  ? 0.1896 0.2069 0.1934 -0.0228 -0.0068 0.0312  26  GLU   B O   
4275 C CB  . GLU   B 26  ? 0.2243 0.2060 0.1783 -0.0440 0.0015  0.0136  26  GLU   B CB  
4276 C CG  . GLU   B 26  ? 0.2723 0.2425 0.2547 -0.0518 0.0093  -0.0177 26  GLU   B CG  
4277 C CD  . GLU   B 26  ? 0.2978 0.2634 0.2586 -0.0728 0.0221  -0.0510 26  GLU   B CD  
4278 O OE1 . GLU   B 26  ? 0.3111 0.2392 0.2783 -0.0828 0.0564  -0.0413 26  GLU   B OE1 
4279 O OE2 . GLU   B 26  ? 0.3043 0.3138 0.2924 -0.0728 0.0170  -0.0422 26  GLU   B OE2 
4286 N N   . ALA   B 27  ? 0.1581 0.1707 0.1830 -0.0251 0.0001  0.0151  27  ALA   B N   
4287 C CA  . ALA   B 27  ? 0.1627 0.1736 0.1895 -0.0175 0.0054  0.0238  27  ALA   B CA  
4288 C C   . ALA   B 27  ? 0.1649 0.1778 0.2104 -0.0130 0.0142  0.0410  27  ALA   B C   
4289 O O   . ALA   B 27  ? 0.1723 0.1829 0.2239 -0.0017 0.0156  0.0472  27  ALA   B O   
4290 C CB  . ALA   B 27  ? 0.1810 0.1603 0.1928 -0.0188 0.0104  0.0154  27  ALA   B CB  
4296 N N   . LYS   B 28  ? 0.1589 0.1926 0.2542 -0.0192 0.0203  0.0569  28  LYS   B N   
4297 C CA  . LYS   B 28  ? 0.1787 0.2275 0.2905 -0.0050 0.0476  0.0872  28  LYS   B CA  
4298 C C   . LYS   B 28  ? 0.1959 0.2404 0.2689 0.0009  0.0570  0.0771  28  LYS   B C   
4299 O O   . LYS   B 28  ? 0.2205 0.2461 0.2812 -0.0021 0.0608  0.0750  28  LYS   B O   
4300 C CB  . LYS   B 28  ? 0.2007 0.2661 0.3648 0.0136  0.0700  0.1151  28  LYS   B CB  
4301 C CG  . LYS   B 28  ? 0.2259 0.3210 0.3951 0.0288  0.0823  0.1358  28  LYS   B CG  
4302 C CD  . LYS   B 28  ? 0.2733 0.3826 0.4493 0.0364  0.1035  0.1362  28  LYS   B CD  
4303 C CE  . LYS   B 28  ? 0.3385 0.4475 0.5089 0.0426  0.1032  0.1383  28  LYS   B CE  
4304 N NZ  . LYS   B 28  ? 0.3942 0.4891 0.5207 0.0480  0.0976  0.1484  28  LYS   B NZ  
4318 N N   . LYS   B 29  ? 0.2081 0.2623 0.2671 0.0208  0.0603  0.0652  29  LYS   B N   
4319 C CA  . LYS   B 29  ? 0.2517 0.2902 0.2974 0.0248  0.0663  0.0647  29  LYS   B CA  
4320 C C   . LYS   B 29  ? 0.2480 0.2831 0.2574 0.0229  0.0497  0.0759  29  LYS   B C   
4321 O O   . LYS   B 29  ? 0.2688 0.3071 0.2596 0.0284  0.0468  0.0802  29  LYS   B O   
4322 C CB  . LYS   B 29  ? 0.3120 0.3297 0.3704 0.0276  0.0649  0.0463  29  LYS   B CB  
4323 C CG  . LYS   B 29  ? 0.3648 0.3663 0.4628 0.0235  0.0601  0.0381  29  LYS   B CG  
4324 C CD  . LYS   B 29  ? 0.4022 0.3887 0.5323 0.0152  0.0681  0.0329  29  LYS   B CD  
4325 C CE  . LYS   B 29  ? 0.4383 0.4007 0.5696 0.0076  0.0783  0.0269  29  LYS   B CE  
4326 N NZ  . LYS   B 29  ? 0.4698 0.4090 0.6026 0.0051  0.0791  0.0206  29  LYS   B NZ  
4340 N N   . VAL   B 30  ? 0.2235 0.2618 0.2470 0.0048  0.0270  0.0637  30  VAL   B N   
4341 C CA  . VAL   B 30  ? 0.2141 0.2539 0.2678 -0.0100 0.0013  0.0651  30  VAL   B CA  
4342 C C   . VAL   B 30  ? 0.1926 0.2449 0.2462 -0.0137 0.0046  0.0743  30  VAL   B C   
4343 O O   . VAL   B 30  ? 0.2089 0.2637 0.2436 -0.0036 -0.0009 0.0929  30  VAL   B O   
4344 C CB  . VAL   B 30  ? 0.2252 0.2586 0.3207 -0.0224 -0.0214 0.0682  30  VAL   B CB  
4345 C CG1 . VAL   B 30  ? 0.2371 0.2703 0.3187 -0.0200 -0.0093 0.0519  30  VAL   B CG1 
4346 C CG2 . VAL   B 30  ? 0.2381 0.2610 0.3378 -0.0293 -0.0426 0.0672  30  VAL   B CG2 
4356 N N   A LYS   B 31  ? 0.1756 0.2159 0.2596 -0.0273 0.0123  0.0772  31  LYS   B N   
4357 N N   B LYS   B 31  ? 0.1902 0.2289 0.2545 -0.0199 -0.0047 0.0641  31  LYS   B N   
4358 C CA  A LYS   B 31  ? 0.1588 0.2155 0.2901 -0.0362 0.0039  0.0852  31  LYS   B CA  
4359 C CA  B LYS   B 31  ? 0.1899 0.2231 0.2712 -0.0246 -0.0189 0.0575  31  LYS   B CA  
4360 C C   A LYS   B 31  ? 0.1580 0.1896 0.2591 -0.0302 -0.0183 0.0819  31  LYS   B C   
4361 C C   B LYS   B 31  ? 0.1795 0.1957 0.2414 -0.0281 -0.0365 0.0508  31  LYS   B C   
4362 O O   A LYS   B 31  ? 0.1646 0.2018 0.2715 -0.0238 -0.0074 0.0991  31  LYS   B O   
4363 O O   B LYS   B 31  ? 0.1848 0.2011 0.2368 -0.0314 -0.0466 0.0433  31  LYS   B O   
4364 C CB  A LYS   B 31  ? 0.1705 0.2604 0.3417 -0.0265 0.0124  0.0981  31  LYS   B CB  
4365 C CB  B LYS   B 31  ? 0.2085 0.2505 0.3106 -0.0182 -0.0178 0.0558  31  LYS   B CB  
4366 C CG  A LYS   B 31  ? 0.1965 0.3028 0.3789 -0.0203 0.0285  0.0998  31  LYS   B CG  
4367 C CG  B LYS   B 31  ? 0.2298 0.2765 0.3440 -0.0152 -0.0118 0.0464  31  LYS   B CG  
4368 C CD  A LYS   B 31  ? 0.2200 0.3418 0.4210 -0.0138 0.0240  0.0830  31  LYS   B CD  
4369 C CD  B LYS   B 31  ? 0.2471 0.3004 0.3759 -0.0128 -0.0126 0.0323  31  LYS   B CD  
4370 C CE  A LYS   B 31  ? 0.2295 0.3772 0.4614 -0.0083 0.0142  0.0695  31  LYS   B CE  
4371 C CE  B LYS   B 31  ? 0.2580 0.3148 0.4067 -0.0093 -0.0143 0.0241  31  LYS   B CE  
4372 N NZ  A LYS   B 31  ? 0.2439 0.4049 0.4716 -0.0007 0.0048  0.0633  31  LYS   B NZ  
4373 N NZ  B LYS   B 31  ? 0.2675 0.3242 0.4182 -0.0041 -0.0192 0.0196  31  LYS   B NZ  
4400 N N   . PRO   B 32  ? 0.1711 0.1683 0.2127 -0.0287 -0.0395 0.0464  32  PRO   B N   
4401 C CA  . PRO   B 32  ? 0.1811 0.1574 0.1694 -0.0326 -0.0342 0.0326  32  PRO   B CA  
4402 C C   . PRO   B 32  ? 0.1903 0.1476 0.1792 -0.0344 -0.0479 0.0376  32  PRO   B C   
4403 O O   . PRO   B 32  ? 0.1996 0.1537 0.2082 -0.0386 -0.0653 0.0340  32  PRO   B O   
4404 C CB  . PRO   B 32  ? 0.1900 0.1493 0.1704 -0.0311 -0.0282 0.0161  32  PRO   B CB  
4405 C CG  . PRO   B 32  ? 0.2083 0.1459 0.1762 -0.0204 -0.0470 0.0217  32  PRO   B CG  
4406 C CD  . PRO   B 32  ? 0.1927 0.1522 0.2034 -0.0195 -0.0516 0.0332  32  PRO   B CD  
4414 N N   . THR   B 33  ? 0.1939 0.1387 0.1678 -0.0301 -0.0477 0.0180  33  THR   B N   
4415 C CA  . THR   B 33  ? 0.1965 0.1482 0.1570 -0.0337 -0.0403 0.0241  33  THR   B CA  
4416 C C   . THR   B 33  ? 0.2024 0.1404 0.1590 -0.0349 -0.0482 0.0176  33  THR   B C   
4417 O O   . THR   B 33  ? 0.2248 0.1427 0.1684 -0.0459 -0.0521 0.0200  33  THR   B O   
4418 C CB  . THR   B 33  ? 0.2034 0.1542 0.1660 -0.0156 -0.0405 0.0236  33  THR   B CB  
4419 O OG1 . THR   B 33  ? 0.1894 0.1597 0.1679 -0.0174 -0.0379 0.0237  33  THR   B OG1 
4420 C CG2 . THR   B 33  ? 0.2253 0.1530 0.1873 -0.0053 -0.0349 0.0203  33  THR   B CG2 
4428 N N   . VAL   B 34  ? 0.1888 0.1363 0.1473 -0.0330 -0.0440 0.0107  34  VAL   B N   
4429 C CA  . VAL   B 34  ? 0.1760 0.1338 0.1453 -0.0293 -0.0414 0.0064  34  VAL   B CA  
4430 C C   . VAL   B 34  ? 0.1655 0.1309 0.1370 -0.0286 -0.0233 0.0072  34  VAL   B C   
4431 O O   . VAL   B 34  ? 0.1721 0.1335 0.1391 -0.0242 -0.0309 0.0078  34  VAL   B O   
4432 C CB  . VAL   B 34  ? 0.1761 0.1477 0.1718 -0.0098 -0.0332 0.0047  34  VAL   B CB  
4433 C CG1 . VAL   B 34  ? 0.1703 0.1611 0.1688 -0.0031 -0.0178 0.0024  34  VAL   B CG1 
4434 C CG2 . VAL   B 34  ? 0.1825 0.1474 0.1968 -0.0055 -0.0266 0.0094  34  VAL   B CG2 
4444 N N   . VAL   B 35  ? 0.1559 0.1290 0.1258 -0.0253 -0.0170 0.0032  35  VAL   B N   
4445 C CA  . VAL   B 35  ? 0.1463 0.1283 0.1247 -0.0220 -0.0108 0.0012  35  VAL   B CA  
4446 C C   . VAL   B 35  ? 0.1383 0.1213 0.1325 -0.0186 -0.0139 0.0031  35  VAL   B C   
4447 O O   . VAL   B 35  ? 0.1450 0.1284 0.1309 -0.0229 -0.0037 -0.0042 35  VAL   B O   
4448 C CB  . VAL   B 35  ? 0.1495 0.1472 0.1355 -0.0154 -0.0024 0.0023  35  VAL   B CB  
4449 C CG1 . VAL   B 35  ? 0.1443 0.1585 0.1467 -0.0188 -0.0055 0.0074  35  VAL   B CG1 
4450 C CG2 . VAL   B 35  ? 0.1526 0.1448 0.1509 -0.0093 -0.0042 -0.0032 35  VAL   B CG2 
4460 N N   . VAL   B 36  ? 0.1399 0.1270 0.1308 -0.0152 -0.0189 0.0098  36  VAL   B N   
4461 C CA  . VAL   B 36  ? 0.1368 0.1238 0.1220 -0.0131 -0.0105 0.0048  36  VAL   B CA  
4462 C C   . VAL   B 36  ? 0.1347 0.1283 0.1118 -0.0069 -0.0035 0.0074  36  VAL   B C   
4463 O O   . VAL   B 36  ? 0.1378 0.1358 0.1313 -0.0071 -0.0033 -0.0025 36  VAL   B O   
4464 C CB  . VAL   B 36  ? 0.1380 0.1285 0.1279 -0.0157 -0.0072 0.0047  36  VAL   B CB  
4465 C CG1 . VAL   B 36  ? 0.1349 0.1415 0.1407 -0.0193 -0.0038 -0.0031 36  VAL   B CG1 
4466 C CG2 . VAL   B 36  ? 0.1401 0.1335 0.1371 -0.0168 -0.0119 0.0073  36  VAL   B CG2 
4476 N N   . ASN   B 37  ? 0.1317 0.1313 0.1212 -0.0041 -0.0034 0.0028  37  ASN   B N   
4477 C CA  . ASN   B 37  ? 0.1384 0.1291 0.1289 0.0052  -0.0143 0.0048  37  ASN   B CA  
4478 C C   . ASN   B 37  ? 0.1338 0.1283 0.1390 0.0053  -0.0083 0.0035  37  ASN   B C   
4479 O O   . ASN   B 37  ? 0.1427 0.1378 0.1303 0.0007  -0.0015 0.0098  37  ASN   B O   
4480 C CB  . ASN   B 37  ? 0.1393 0.1327 0.1260 -0.0020 -0.0154 0.0090  37  ASN   B CB  
4481 C CG  . ASN   B 37  ? 0.1460 0.1320 0.1391 -0.0012 -0.0125 0.0029  37  ASN   B CG  
4482 O OD1 . ASN   B 37  ? 0.1549 0.1398 0.1393 0.0037  -0.0178 0.0018  37  ASN   B OD1 
4483 N ND2 . ASN   B 37  ? 0.1509 0.1287 0.1407 0.0031  -0.0207 0.0062  37  ASN   B ND2 
4490 N N   . ALA   B 38  ? 0.1436 0.1312 0.1273 0.0040  -0.0041 0.0076  38  ALA   B N   
4491 C CA  . ALA   B 38  ? 0.1553 0.1352 0.1273 0.0037  0.0007  0.0080  38  ALA   B CA  
4492 C C   . ALA   B 38  ? 0.1491 0.1317 0.1232 0.0012  0.0030  0.0116  38  ALA   B C   
4493 O O   . ALA   B 38  ? 0.1593 0.1409 0.1427 0.0039  -0.0054 0.0067  38  ALA   B O   
4494 C CB  . ALA   B 38  ? 0.1762 0.1437 0.1488 -0.0103 0.0044  0.0012  38  ALA   B CB  
4500 N N   . ALA   B 39  ? 0.1525 0.1368 0.1144 0.0042  -0.0092 0.0045  39  ALA   B N   
4501 C CA  . ALA   B 39  ? 0.1595 0.1418 0.1276 0.0054  -0.0092 0.0056  39  ALA   B CA  
4502 C C   . ALA   B 39  ? 0.1596 0.1451 0.1149 0.0083  -0.0092 0.0066  39  ALA   B C   
4503 O O   . ALA   B 39  ? 0.1615 0.1544 0.1349 -0.0001 -0.0062 0.0028  39  ALA   B O   
4504 C CB  . ALA   B 39  ? 0.1612 0.1489 0.1513 -0.0046 -0.0065 0.0024  39  ALA   B CB  
4510 N N   . ASN   B 40  ? 0.1662 0.1690 0.1186 -0.0007 -0.0010 -0.0077 40  ASN   B N   
4511 C CA  . ASN   B 40  ? 0.1667 0.1752 0.1285 0.0000  -0.0006 -0.0079 40  ASN   B CA  
4512 C C   . ASN   B 40  ? 0.1773 0.1806 0.1085 0.0022  -0.0062 0.0019  40  ASN   B C   
4513 O O   . ASN   B 40  ? 0.1727 0.1712 0.1203 0.0160  -0.0054 -0.0022 40  ASN   B O   
4514 C CB  . ASN   B 40  ? 0.1823 0.1727 0.1639 0.0108  -0.0089 0.0042  40  ASN   B CB  
4515 C CG  . ASN   B 40  ? 0.1881 0.1760 0.1869 0.0072  -0.0287 0.0094  40  ASN   B CG  
4516 O OD1 . ASN   B 40  ? 0.1884 0.1687 0.2632 0.0050  -0.0312 0.0174  40  ASN   B OD1 
4517 N ND2 . ASN   B 40  ? 0.1890 0.1756 0.1745 0.0051  -0.0198 0.0126  40  ASN   B ND2 
4524 N N   . VAL   B 41  ? 0.1844 0.1779 0.1215 0.0126  -0.0030 -0.0019 41  VAL   B N   
4525 C CA  . VAL   B 41  ? 0.1919 0.1888 0.1346 0.0136  -0.0037 -0.0064 41  VAL   B CA  
4526 C C   . VAL   B 41  ? 0.1910 0.1867 0.1263 0.0192  -0.0095 -0.0064 41  VAL   B C   
4527 O O   . VAL   B 41  ? 0.1873 0.1827 0.1394 0.0128  -0.0120 -0.0094 41  VAL   B O   
4528 C CB  . VAL   B 41  ? 0.1983 0.2130 0.1450 -0.0000 0.0123  -0.0199 41  VAL   B CB  
4529 C CG1 . VAL   B 41  ? 0.1900 0.2115 0.1613 -0.0034 0.0264  -0.0232 41  VAL   B CG1 
4530 C CG2 . VAL   B 41  ? 0.2078 0.2375 0.1577 -0.0043 0.0091  -0.0257 41  VAL   B CG2 
4540 N N   . TYR   B 42  ? 0.1961 0.1823 0.1240 0.0152  -0.0187 -0.0018 42  TYR   B N   
4541 C CA  . TYR   B 42  ? 0.1996 0.1897 0.1382 0.0196  -0.0352 -0.0167 42  TYR   B CA  
4542 C C   . TYR   B 42  ? 0.1798 0.1749 0.1500 0.0222  -0.0288 -0.0130 42  TYR   B C   
4543 O O   . TYR   B 42  ? 0.1819 0.1803 0.1781 0.0167  -0.0289 -0.0204 42  TYR   B O   
4544 C CB  . TYR   B 42  ? 0.2238 0.2107 0.1642 0.0095  -0.0457 -0.0069 42  TYR   B CB  
4545 C CG  . TYR   B 42  ? 0.2291 0.2230 0.1398 -0.0094 -0.0360 0.0001  42  TYR   B CG  
4546 C CD1 . TYR   B 42  ? 0.2297 0.2186 0.1021 -0.0160 -0.0184 -0.0039 42  TYR   B CD1 
4547 C CD2 . TYR   B 42  ? 0.2410 0.2341 0.1849 -0.0117 -0.0154 0.0096  42  TYR   B CD2 
4548 C CE1 . TYR   B 42  ? 0.2460 0.2219 0.1088 -0.0081 -0.0170 0.0062  42  TYR   B CE1 
4549 C CE2 . TYR   B 42  ? 0.2474 0.2357 0.1654 -0.0043 0.0075  0.0285  42  TYR   B CE2 
4550 C CZ  . TYR   B 42  ? 0.2670 0.2383 0.1671 0.0120  0.0133  0.0093  42  TYR   B CZ  
4551 O OH  . TYR   B 42  ? 0.3079 0.2658 0.2144 0.0329  0.0248  0.0252  42  TYR   B OH  
4561 N N   . LEU   B 43  ? 0.1748 0.1599 0.1329 0.0099  -0.0189 -0.0102 43  LEU   B N   
4562 C CA  . LEU   B 43  ? 0.1753 0.1580 0.1290 0.0034  -0.0219 -0.0072 43  LEU   B CA  
4563 C C   . LEU   B 43  ? 0.1786 0.1588 0.1356 0.0013  -0.0210 -0.0033 43  LEU   B C   
4564 O O   . LEU   B 43  ? 0.1686 0.1607 0.1733 0.0053  -0.0256 0.0068  43  LEU   B O   
4565 C CB  . LEU   B 43  ? 0.1748 0.1540 0.1564 0.0020  -0.0318 -0.0025 43  LEU   B CB  
4566 C CG  . LEU   B 43  ? 0.1805 0.1518 0.1589 0.0018  -0.0343 -0.0053 43  LEU   B CG  
4567 C CD1 . LEU   B 43  ? 0.1822 0.1526 0.2040 0.0009  -0.0517 -0.0078 43  LEU   B CD1 
4568 C CD2 . LEU   B 43  ? 0.1786 0.1512 0.1803 -0.0044 -0.0383 -0.0115 43  LEU   B CD2 
4580 N N   . LYS   B 44  ? 0.1713 0.1594 0.1326 0.0085  -0.0127 -0.0014 44  LYS   B N   
4581 C CA  . LYS   B 44  ? 0.1802 0.1681 0.1475 0.0082  -0.0171 0.0117  44  LYS   B CA  
4582 C C   . LYS   B 44  ? 0.1704 0.1637 0.1522 0.0056  -0.0168 0.0030  44  LYS   B C   
4583 O O   . LYS   B 44  ? 0.1888 0.1657 0.1651 0.0013  -0.0040 0.0045  44  LYS   B O   
4584 C CB  . LYS   B 44  ? 0.2056 0.1904 0.1611 0.0169  -0.0181 0.0066  44  LYS   B CB  
4585 C CG  . LYS   B 44  ? 0.2483 0.2146 0.2064 0.0084  -0.0425 -0.0006 44  LYS   B CG  
4586 C CD  . LYS   B 44  ? 0.2846 0.2346 0.2783 -0.0077 -0.0558 -0.0141 44  LYS   B CD  
4587 C CE  . LYS   B 44  ? 0.3117 0.2621 0.3235 -0.0173 -0.0690 -0.0042 44  LYS   B CE  
4588 N NZ  . LYS   B 44  ? 0.3217 0.2723 0.3508 -0.0192 -0.0873 0.0243  44  LYS   B NZ  
4602 N N   . HIS   B 45  ? 0.1640 0.1639 0.1485 0.0023  -0.0139 0.0106  45  HIS   B N   
4603 C CA  . HIS   B 45  ? 0.1712 0.1583 0.1437 0.0121  -0.0145 -0.0015 45  HIS   B CA  
4604 C C   . HIS   B 45  ? 0.1986 0.1785 0.1719 0.0209  -0.0203 0.0002  45  HIS   B C   
4605 O O   . HIS   B 45  ? 0.2066 0.2034 0.2339 0.0454  -0.0021 0.0043  45  HIS   B O   
4606 C CB  . HIS   B 45  ? 0.1665 0.1649 0.1489 0.0069  -0.0173 -0.0039 45  HIS   B CB  
4607 C CG  . HIS   B 45  ? 0.1636 0.1628 0.1337 -0.0023 -0.0146 -0.0020 45  HIS   B CG  
4608 N ND1 . HIS   B 45  ? 0.1643 0.1542 0.1526 0.0029  -0.0201 -0.0084 45  HIS   B ND1 
4609 C CD2 . HIS   B 45  ? 0.1698 0.1604 0.1598 -0.0079 -0.0209 -0.0057 45  HIS   B CD2 
4610 C CE1 . HIS   B 45  ? 0.1751 0.1472 0.1406 0.0034  -0.0300 -0.0102 45  HIS   B CE1 
4611 N NE2 . HIS   B 45  ? 0.1809 0.1527 0.1469 -0.0014 -0.0210 -0.0075 45  HIS   B NE2 
4619 N N   A GLY   B 46  ? 0.2174 0.1756 0.2164 0.0222  -0.0299 0.0117  46  GLY   B N   
4620 N N   B GLY   B 46  ? 0.2087 0.1811 0.2031 0.0214  -0.0255 0.0118  46  GLY   B N   
4621 C CA  A GLY   B 46  ? 0.2297 0.1894 0.2627 0.0226  -0.0368 0.0190  46  GLY   B CA  
4622 C CA  B GLY   B 46  ? 0.2173 0.1934 0.2314 0.0215  -0.0327 0.0214  46  GLY   B CA  
4623 C C   A GLY   B 46  ? 0.2262 0.2035 0.3130 0.0319  -0.0351 0.0118  46  GLY   B C   
4624 C C   B GLY   B 46  ? 0.2191 0.2075 0.2647 0.0266  -0.0326 0.0260  46  GLY   B C   
4625 O O   A GLY   B 46  ? 0.2377 0.2173 0.4095 0.0420  -0.0222 -0.0171 46  GLY   B O   
4626 O O   B GLY   B 46  ? 0.2271 0.2207 0.2825 0.0349  -0.0330 0.0380  46  GLY   B O   
4633 N N   . GLY   B 47  ? 0.2161 0.2057 0.2731 0.0135  -0.0199 0.0118  47  GLY   B N   
4634 C CA  . GLY   B 47  ? 0.1972 0.1818 0.2313 0.0055  -0.0124 0.0005  47  GLY   B CA  
4635 C C   . GLY   B 47  ? 0.1773 0.1640 0.1892 0.0014  -0.0051 0.0080  47  GLY   B C   
4636 O O   . GLY   B 47  ? 0.1869 0.1520 0.2039 0.0033  -0.0128 0.0131  47  GLY   B O   
4641 N N   . GLY   B 48  ? 0.1627 0.1545 0.1805 0.0021  -0.0146 0.0152  48  GLY   B N   
4642 C CA  . GLY   B 48  ? 0.1625 0.1558 0.1806 -0.0040 -0.0076 0.0077  48  GLY   B CA  
4643 C C   . GLY   B 48  ? 0.1544 0.1483 0.1756 -0.0005 -0.0054 0.0049  48  GLY   B C   
4644 O O   . GLY   B 48  ? 0.1504 0.1471 0.2039 0.0045  -0.0120 0.0024  48  GLY   B O   
4648 N N   . VAL   B 49  ? 0.1615 0.1556 0.1616 0.0098  -0.0044 0.0090  49  VAL   B N   
4649 C CA  . VAL   B 49  ? 0.1584 0.1654 0.1547 0.0115  -0.0133 0.0008  49  VAL   B CA  
4650 C C   . VAL   B 49  ? 0.1492 0.1522 0.1370 0.0088  -0.0076 0.0051  49  VAL   B C   
4651 O O   . VAL   B 49  ? 0.1565 0.1601 0.1587 0.0035  -0.0018 0.0012  49  VAL   B O   
4652 C CB  . VAL   B 49  ? 0.1642 0.1820 0.1838 0.0062  -0.0255 -0.0039 49  VAL   B CB  
4653 C CG1 . VAL   B 49  ? 0.1621 0.1885 0.1831 0.0097  -0.0217 -0.0031 49  VAL   B CG1 
4654 C CG2 . VAL   B 49  ? 0.1790 0.2048 0.2025 -0.0010 -0.0407 -0.0174 49  VAL   B CG2 
4664 N N   . ALA   B 50  ? 0.1479 0.1526 0.1414 0.0004  -0.0055 0.0044  50  ALA   B N   
4665 C CA  . ALA   B 50  ? 0.1484 0.1403 0.1410 0.0029  -0.0093 0.0049  50  ALA   B CA  
4666 C C   . ALA   B 50  ? 0.1540 0.1408 0.1435 0.0054  -0.0041 0.0040  50  ALA   B C   
4667 O O   . ALA   B 50  ? 0.1542 0.1469 0.1397 0.0068  -0.0059 0.0020  50  ALA   B O   
4668 C CB  . ALA   B 50  ? 0.1570 0.1401 0.1522 0.0016  -0.0106 0.0103  50  ALA   B CB  
4674 N N   . GLY   B 51  ? 0.1486 0.1528 0.1638 0.0076  -0.0095 0.0097  51  GLY   B N   
4675 C CA  . GLY   B 51  ? 0.1517 0.1593 0.1776 0.0178  -0.0164 0.0038  51  GLY   B CA  
4676 C C   . GLY   B 51  ? 0.1517 0.1573 0.1598 0.0213  -0.0121 0.0028  51  GLY   B C   
4677 O O   . GLY   B 51  ? 0.1518 0.1696 0.1876 0.0083  -0.0123 -0.0006 51  GLY   B O   
4681 N N   . ALA   B 52  ? 0.1516 0.1563 0.1555 0.0177  -0.0122 0.0068  52  ALA   B N   
4682 C CA  . ALA   B 52  ? 0.1589 0.1609 0.1663 0.0176  -0.0001 -0.0030 52  ALA   B CA  
4683 C C   . ALA   B 52  ? 0.1458 0.1631 0.1625 0.0115  -0.0021 -0.0047 52  ALA   B C   
4684 O O   . ALA   B 52  ? 0.1454 0.1688 0.1789 0.0101  0.0072  0.0069  52  ALA   B O   
4685 C CB  . ALA   B 52  ? 0.1784 0.1676 0.1739 0.0129  -0.0018 -0.0050 52  ALA   B CB  
4691 N N   . LEU   B 53  ? 0.1445 0.1574 0.1486 0.0153  0.0016  0.0052  53  LEU   B N   
4692 C CA  . LEU   B 53  ? 0.1449 0.1628 0.1481 0.0124  -0.0029 0.0063  53  LEU   B CA  
4693 C C   . LEU   B 53  ? 0.1464 0.1536 0.1456 0.0121  0.0031  0.0086  53  LEU   B C   
4694 O O   . LEU   B 53  ? 0.1553 0.1645 0.1594 0.0012  0.0017  0.0121  53  LEU   B O   
4695 C CB  . LEU   B 53  ? 0.1490 0.1701 0.1617 0.0138  -0.0061 0.0141  53  LEU   B CB  
4696 C CG  . LEU   B 53  ? 0.1434 0.1789 0.1636 0.0034  -0.0050 0.0162  53  LEU   B CG  
4697 C CD1 . LEU   B 53  ? 0.1509 0.1989 0.1931 0.0127  -0.0112 0.0034  53  LEU   B CD1 
4698 C CD2 . LEU   B 53  ? 0.1594 0.2067 0.1971 -0.0103 -0.0171 -0.0182 53  LEU   B CD2 
4710 N N   . ASN   B 54  ? 0.1493 0.1489 0.1417 0.0022  -0.0073 0.0091  54  ASN   B N   
4711 C CA  . ASN   B 54  ? 0.1549 0.1598 0.1470 0.0028  -0.0096 0.0005  54  ASN   B CA  
4712 C C   . ASN   B 54  ? 0.1455 0.1649 0.1649 0.0009  -0.0040 0.0026  54  ASN   B C   
4713 O O   . ASN   B 54  ? 0.1455 0.1705 0.1754 -0.0018 0.0007  0.0068  54  ASN   B O   
4714 C CB  . ASN   B 54  ? 0.1607 0.1688 0.1665 -0.0007 -0.0072 -0.0046 54  ASN   B CB  
4715 C CG  . ASN   B 54  ? 0.1584 0.1772 0.1732 0.0010  -0.0165 -0.0067 54  ASN   B CG  
4716 O OD1 . ASN   B 54  ? 0.1572 0.1759 0.1886 -0.0053 -0.0165 -0.0106 54  ASN   B OD1 
4717 N ND2 . ASN   B 54  ? 0.1709 0.1976 0.2030 0.0059  -0.0409 0.0098  54  ASN   B ND2 
4724 N N   . LYS   B 55  ? 0.1468 0.1683 0.1914 0.0118  0.0005  0.0018  55  LYS   B N   
4725 C CA  . LYS   B 55  ? 0.1554 0.1788 0.2067 0.0174  -0.0053 0.0048  55  LYS   B CA  
4726 C C   . LYS   B 55  ? 0.1500 0.1815 0.2020 0.0175  0.0016  -0.0076 55  LYS   B C   
4727 O O   . LYS   B 55  ? 0.1431 0.1955 0.2229 0.0116  0.0032  -0.0086 55  LYS   B O   
4728 C CB  . LYS   B 55  ? 0.1731 0.1884 0.2503 0.0282  -0.0016 0.0188  55  LYS   B CB  
4729 C CG  . LYS   B 55  ? 0.2171 0.2113 0.3281 0.0339  0.0093  0.0412  55  LYS   B CG  
4730 C CD  . LYS   B 55  ? 0.2553 0.2348 0.3859 0.0457  0.0324  0.0569  55  LYS   B CD  
4731 C CE  . LYS   B 55  ? 0.2763 0.2618 0.4525 0.0465  0.0530  0.0493  55  LYS   B CE  
4732 N NZ  . LYS   B 55  ? 0.2829 0.2829 0.4855 0.0432  0.0347  0.0512  55  LYS   B NZ  
4746 N N   . ALA   B 56  ? 0.1516 0.1890 0.1725 0.0089  -0.0057 -0.0023 56  ALA   B N   
4747 C CA  . ALA   B 56  ? 0.1619 0.2083 0.1666 0.0018  -0.0014 -0.0005 56  ALA   B CA  
4748 C C   . ALA   B 56  ? 0.1605 0.2005 0.1700 0.0006  0.0028  0.0095  56  ALA   B C   
4749 O O   . ALA   B 56  ? 0.1744 0.2066 0.1924 0.0026  0.0184  0.0106  56  ALA   B O   
4750 C CB  . ALA   B 56  ? 0.1673 0.2241 0.1841 -0.0043 0.0028  -0.0058 56  ALA   B CB  
4756 N N   . THR   B 57  ? 0.1567 0.1899 0.1831 0.0024  0.0095  0.0050  57  THR   B N   
4757 C CA  . THR   B 57  ? 0.1611 0.1868 0.1762 0.0037  0.0093  0.0171  57  THR   B CA  
4758 C C   . THR   B 57  ? 0.1612 0.1945 0.1983 0.0009  0.0092  0.0178  57  THR   B C   
4759 O O   . THR   B 57  ? 0.1684 0.1997 0.2050 -0.0123 0.0114  0.0146  57  THR   B O   
4760 C CB  . THR   B 57  ? 0.1664 0.1706 0.1552 -0.0011 0.0124  0.0190  57  THR   B CB  
4761 O OG1 . THR   B 57  ? 0.1691 0.1613 0.1813 -0.0081 0.0048  0.0111  57  THR   B OG1 
4762 C CG2 . THR   B 57  ? 0.1625 0.1718 0.1774 -0.0102 0.0071  0.0133  57  THR   B CG2 
4770 N N   . ASN   B 58  ? 0.1475 0.2081 0.2281 -0.0114 -0.0000 0.0055  58  ASN   B N   
4771 C CA  . ASN   B 58  ? 0.1712 0.2494 0.2805 -0.0244 0.0149  0.0161  58  ASN   B CA  
4772 C C   . ASN   B 58  ? 0.1561 0.2270 0.2428 -0.0192 -0.0091 0.0079  58  ASN   B C   
4773 O O   . ASN   B 58  ? 0.1602 0.2355 0.2587 -0.0253 -0.0186 -0.0026 58  ASN   B O   
4774 C CB  . ASN   B 58  ? 0.2497 0.3192 0.4056 -0.0368 0.0438  0.0361  58  ASN   B CB  
4775 C CG  . ASN   B 58  ? 0.3926 0.4150 0.5472 -0.0389 0.0686  0.0523  58  ASN   B CG  
4776 O OD1 . ASN   B 58  ? 0.4370 0.4419 0.5987 -0.0398 0.0782  0.0551  58  ASN   B OD1 
4777 N ND2 . ASN   B 58  ? 0.4740 0.4786 0.5925 -0.0385 0.0819  0.0531  58  ASN   B ND2 
4784 N N   . ASN   B 59  ? 0.1589 0.2120 0.2129 -0.0140 -0.0129 0.0146  59  ASN   B N   
4785 C CA  . ASN   B 59  ? 0.1592 0.2143 0.2036 -0.0140 -0.0190 0.0189  59  ASN   B CA  
4786 C C   . ASN   B 59  ? 0.1493 0.2058 0.1894 -0.0200 -0.0214 0.0044  59  ASN   B C   
4787 O O   . ASN   B 59  ? 0.1575 0.2020 0.1896 -0.0130 -0.0118 0.0053  59  ASN   B O   
4788 C CB  . ASN   B 59  ? 0.1669 0.2344 0.2018 -0.0078 -0.0296 0.0157  59  ASN   B CB  
4789 C CG  . ASN   B 59  ? 0.1808 0.2533 0.2341 -0.0006 -0.0498 0.0105  59  ASN   B CG  
4790 O OD1 . ASN   B 59  ? 0.1829 0.2582 0.2322 0.0041  -0.0383 0.0311  59  ASN   B OD1 
4791 N ND2 . ASN   B 59  ? 0.1862 0.2593 0.2284 -0.0079 -0.0547 0.0030  59  ASN   B ND2 
4798 N N   . ALA   B 60  ? 0.1537 0.1952 0.1928 -0.0195 -0.0085 0.0093  60  ALA   B N   
4799 C CA  . ALA   B 60  ? 0.1630 0.1863 0.1970 -0.0209 -0.0099 0.0185  60  ALA   B CA  
4800 C C   . ALA   B 60  ? 0.1645 0.1746 0.1725 -0.0144 -0.0141 0.0154  60  ALA   B C   
4801 O O   . ALA   B 60  ? 0.1654 0.1757 0.1843 -0.0190 -0.0048 0.0004  60  ALA   B O   
4802 C CB  . ALA   B 60  ? 0.1715 0.1862 0.2279 -0.0200 -0.0060 0.0133  60  ALA   B CB  
4808 N N   . MET   B 61  ? 0.1526 0.1644 0.1669 -0.0125 -0.0079 0.0146  61  MET   B N   
4809 C CA  . MET   B 61  ? 0.1478 0.1580 0.1772 -0.0118 -0.0153 0.0045  61  MET   B CA  
4810 C C   . MET   B 61  ? 0.1565 0.1538 0.1742 -0.0152 -0.0143 0.0101  61  MET   B C   
4811 O O   . MET   B 61  ? 0.1612 0.1521 0.1485 -0.0043 -0.0106 -0.0084 61  MET   B O   
4812 C CB  . MET   B 61  ? 0.1485 0.1629 0.1711 -0.0064 -0.0110 0.0064  61  MET   B CB  
4813 C CG  . MET   B 61  ? 0.1469 0.1588 0.1530 -0.0014 -0.0058 0.0078  61  MET   B CG  
4814 S SD  . MET   B 61  ? 0.1484 0.1562 0.1870 -0.0022 -0.0093 -0.0053 61  MET   B SD  
4815 C CE  . MET   B 61  ? 0.1591 0.1802 0.1927 -0.0031 -0.0011 -0.0244 61  MET   B CE  
4825 N N   . GLN   B 62  ? 0.1538 0.1619 0.1489 -0.0095 -0.0252 0.0057  62  GLN   B N   
4826 C CA  . GLN   B 62  ? 0.1559 0.1653 0.1629 -0.0038 -0.0306 0.0045  62  GLN   B CA  
4827 C C   . GLN   B 62  ? 0.1589 0.1677 0.1760 -0.0093 -0.0340 0.0025  62  GLN   B C   
4828 O O   . GLN   B 62  ? 0.1722 0.1636 0.1795 -0.0088 -0.0395 -0.0048 62  GLN   B O   
4829 C CB  . GLN   B 62  ? 0.1572 0.1710 0.1712 0.0022  -0.0268 0.0050  62  GLN   B CB  
4830 C CG  . GLN   B 62  ? 0.1621 0.1766 0.1676 0.0035  -0.0352 0.0009  62  GLN   B CG  
4831 C CD  . GLN   B 62  ? 0.1612 0.1661 0.1657 0.0045  -0.0356 0.0109  62  GLN   B CD  
4832 O OE1 . GLN   B 62  ? 0.1655 0.1594 0.1791 -0.0021 -0.0250 -0.0038 62  GLN   B OE1 
4833 N NE2 . GLN   B 62  ? 0.1675 0.1660 0.1774 0.0018  -0.0245 -0.0033 62  GLN   B NE2 
4842 N N   . VAL   B 63  ? 0.1633 0.1702 0.1818 -0.0104 -0.0280 -0.0068 63  VAL   B N   
4843 C CA  . VAL   B 63  ? 0.1736 0.1744 0.2115 -0.0166 -0.0352 0.0012  63  VAL   B CA  
4844 C C   . VAL   B 63  ? 0.1748 0.1610 0.1881 -0.0211 -0.0386 -0.0032 63  VAL   B C   
4845 O O   . VAL   B 63  ? 0.1880 0.1627 0.2008 -0.0158 -0.0521 -0.0098 63  VAL   B O   
4846 C CB  . VAL   B 63  ? 0.1809 0.1901 0.2450 -0.0178 -0.0324 -0.0090 63  VAL   B CB  
4847 C CG1 . VAL   B 63  ? 0.1889 0.1934 0.2563 -0.0260 -0.0213 -0.0058 63  VAL   B CG1 
4848 C CG2 . VAL   B 63  ? 0.1743 0.2046 0.2615 -0.0178 -0.0323 -0.0131 63  VAL   B CG2 
4858 N N   . GLU   B 64  ? 0.1717 0.1579 0.1788 -0.0115 -0.0378 0.0016  64  GLU   B N   
4859 C CA  . GLU   B 64  ? 0.1711 0.1514 0.1776 -0.0133 -0.0397 0.0030  64  GLU   B CA  
4860 C C   . GLU   B 64  ? 0.1657 0.1448 0.1799 -0.0077 -0.0396 -0.0127 64  GLU   B C   
4861 O O   . GLU   B 64  ? 0.1744 0.1569 0.1834 -0.0079 -0.0353 -0.0157 64  GLU   B O   
4862 C CB  . GLU   B 64  ? 0.1715 0.1592 0.1812 -0.0162 -0.0355 0.0039  64  GLU   B CB  
4863 C CG  . GLU   B 64  ? 0.1799 0.1650 0.1876 -0.0194 -0.0331 -0.0191 64  GLU   B CG  
4864 C CD  . GLU   B 64  ? 0.1817 0.1809 0.1793 -0.0292 -0.0339 -0.0157 64  GLU   B CD  
4865 O OE1 . GLU   B 64  ? 0.1827 0.1939 0.1904 -0.0301 -0.0216 -0.0291 64  GLU   B OE1 
4866 O OE2 . GLU   B 64  ? 0.1952 0.1872 0.1805 -0.0395 -0.0442 -0.0086 64  GLU   B OE2 
4873 N N   . SER   B 65  ? 0.1715 0.1458 0.1670 -0.0106 -0.0242 -0.0164 65  SER   B N   
4874 C CA  . SER   B 65  ? 0.1684 0.1441 0.1713 0.0011  -0.0327 -0.0123 65  SER   B CA  
4875 C C   . SER   B 65  ? 0.1726 0.1489 0.1758 0.0016  -0.0374 -0.0183 65  SER   B C   
4876 O O   . SER   B 65  ? 0.1694 0.1554 0.1725 0.0006  -0.0316 -0.0200 65  SER   B O   
4877 C CB  . SER   B 65  ? 0.1683 0.1516 0.1659 -0.0043 -0.0238 -0.0139 65  SER   B CB  
4878 O OG  . SER   B 65  ? 0.1686 0.1551 0.1663 -0.0058 -0.0241 -0.0180 65  SER   B OG  
4884 N N   . ASP   B 66  ? 0.1778 0.1555 0.1667 -0.0003 -0.0369 -0.0191 66  ASP   B N   
4885 C CA  . ASP   B 66  ? 0.1834 0.1664 0.1503 0.0041  -0.0379 -0.0086 66  ASP   B CA  
4886 C C   . ASP   B 66  ? 0.1863 0.1684 0.1654 -0.0047 -0.0318 -0.0185 66  ASP   B C   
4887 O O   . ASP   B 66  ? 0.1889 0.1741 0.1836 0.0023  -0.0251 -0.0210 66  ASP   B O   
4888 C CB  . ASP   B 66  ? 0.2002 0.1877 0.1746 0.0098  -0.0498 -0.0105 66  ASP   B CB  
4889 C CG  . ASP   B 66  ? 0.2235 0.2068 0.2103 0.0170  -0.0730 0.0043  66  ASP   B CG  
4890 O OD1 . ASP   B 66  ? 0.2490 0.2041 0.2126 0.0069  -0.0693 0.0163  66  ASP   B OD1 
4891 O OD2 . ASP   B 66  ? 0.2367 0.2299 0.2860 0.0322  -0.0624 0.0027  66  ASP   B OD2 
4896 N N   . ASP   B 67  ? 0.1865 0.1628 0.1685 -0.0018 -0.0330 -0.0160 67  ASP   B N   
4897 C CA  . ASP   B 67  ? 0.2026 0.1608 0.1737 -0.0101 -0.0353 -0.0139 67  ASP   B CA  
4898 C C   . ASP   B 67  ? 0.1930 0.1637 0.1952 -0.0013 -0.0366 -0.0215 67  ASP   B C   
4899 O O   . ASP   B 67  ? 0.1943 0.1714 0.1938 -0.0032 -0.0236 -0.0264 67  ASP   B O   
4900 C CB  . ASP   B 67  ? 0.2293 0.1678 0.1887 -0.0211 -0.0438 -0.0075 67  ASP   B CB  
4901 C CG  . ASP   B 67  ? 0.2704 0.1763 0.1947 -0.0196 -0.0713 -0.0068 67  ASP   B CG  
4902 O OD1 . ASP   B 67  ? 0.2926 0.1833 0.2133 -0.0234 -0.0657 -0.0044 67  ASP   B OD1 
4903 O OD2 . ASP   B 67  ? 0.2878 0.1825 0.2136 -0.0108 -0.0819 0.0018  67  ASP   B OD2 
4908 N N   . TYR   B 68  ? 0.1837 0.1594 0.1749 0.0039  -0.0444 -0.0261 68  TYR   B N   
4909 C CA  . TYR   B 68  ? 0.1863 0.1692 0.1855 0.0049  -0.0498 -0.0304 68  TYR   B CA  
4910 C C   . TYR   B 68  ? 0.1785 0.1677 0.1804 0.0011  -0.0442 -0.0348 68  TYR   B C   
4911 O O   . TYR   B 68  ? 0.1869 0.1749 0.1924 0.0060  -0.0434 -0.0457 68  TYR   B O   
4912 C CB  . TYR   B 68  ? 0.1922 0.1889 0.1948 0.0117  -0.0490 -0.0407 68  TYR   B CB  
4913 C CG  . TYR   B 68  ? 0.2044 0.2078 0.1989 0.0149  -0.0409 -0.0660 68  TYR   B CG  
4914 C CD1 . TYR   B 68  ? 0.2057 0.2119 0.2301 -0.0115 -0.0441 -0.0646 68  TYR   B CD1 
4915 C CD2 . TYR   B 68  ? 0.2081 0.2316 0.2238 0.0269  -0.0612 -0.0600 68  TYR   B CD2 
4916 C CE1 . TYR   B 68  ? 0.2100 0.2272 0.2711 -0.0093 -0.0439 -0.0638 68  TYR   B CE1 
4917 C CE2 . TYR   B 68  ? 0.2089 0.2393 0.2466 0.0204  -0.0537 -0.0706 68  TYR   B CE2 
4918 C CZ  . TYR   B 68  ? 0.2061 0.2426 0.2789 0.0011  -0.0541 -0.0736 68  TYR   B CZ  
4919 O OH  . TYR   B 68  ? 0.1998 0.2584 0.3193 -0.0007 -0.0458 -0.0727 68  TYR   B OH  
4929 N N   . ILE   B 69  ? 0.1824 0.1608 0.1789 0.0023  -0.0414 -0.0261 69  ILE   B N   
4930 C CA  . ILE   B 69  ? 0.1902 0.1640 0.1908 -0.0053 -0.0365 -0.0297 69  ILE   B CA  
4931 C C   . ILE   B 69  ? 0.1825 0.1658 0.1920 0.0005  -0.0409 -0.0194 69  ILE   B C   
4932 O O   . ILE   B 69  ? 0.1920 0.1772 0.1798 0.0014  -0.0281 -0.0304 69  ILE   B O   
4933 C CB  . ILE   B 69  ? 0.2006 0.1667 0.2168 -0.0077 -0.0151 -0.0192 69  ILE   B CB  
4934 C CG1 . ILE   B 69  ? 0.1978 0.1692 0.2158 -0.0081 0.0018  -0.0219 69  ILE   B CG1 
4935 C CG2 . ILE   B 69  ? 0.2172 0.1718 0.2121 -0.0069 -0.0094 -0.0061 69  ILE   B CG2 
4936 C CD1 . ILE   B 69  ? 0.1928 0.1724 0.2267 -0.0200 0.0102  -0.0220 69  ILE   B CD1 
4948 N N   . ALA   B 70  ? 0.1777 0.1642 0.1882 0.0076  -0.0416 -0.0208 70  ALA   B N   
4949 C CA  . ALA   B 70  ? 0.1847 0.1723 0.1739 0.0008  -0.0431 -0.0252 70  ALA   B CA  
4950 C C   . ALA   B 70  ? 0.1901 0.1683 0.1856 -0.0047 -0.0459 -0.0308 70  ALA   B C   
4951 O O   . ALA   B 70  ? 0.1991 0.1665 0.1923 -0.0023 -0.0435 -0.0273 70  ALA   B O   
4952 C CB  . ALA   B 70  ? 0.1866 0.1890 0.1841 -0.0040 -0.0387 -0.0258 70  ALA   B CB  
4958 N N   . THR   B 71  ? 0.2001 0.1666 0.1836 0.0014  -0.0539 -0.0282 71  THR   B N   
4959 C CA  . THR   B 71  ? 0.2189 0.1723 0.2189 0.0081  -0.0627 -0.0261 71  THR   B CA  
4960 C C   . THR   B 71  ? 0.2133 0.1788 0.2365 0.0271  -0.0622 -0.0467 71  THR   B C   
4961 O O   . THR   B 71  ? 0.2217 0.1816 0.2684 0.0255  -0.0630 -0.0559 71  THR   B O   
4962 C CB  . THR   B 71  ? 0.2452 0.1938 0.2408 0.0007  -0.0781 -0.0037 71  THR   B CB  
4963 O OG1 . THR   B 71  ? 0.2634 0.2215 0.2728 -0.0158 -0.0784 0.0164  71  THR   B OG1 
4964 C CG2 . THR   B 71  ? 0.2613 0.1935 0.2691 0.0059  -0.0759 0.0040  71  THR   B CG2 
4972 N N   . ASN   B 72  ? 0.2003 0.1878 0.2282 0.0214  -0.0665 -0.0740 72  ASN   B N   
4973 C CA  . ASN   B 72  ? 0.2019 0.1989 0.2381 0.0255  -0.0622 -0.0775 72  ASN   B CA  
4974 C C   . ASN   B 72  ? 0.2048 0.2088 0.2423 0.0113  -0.0348 -0.0736 72  ASN   B C   
4975 O O   . ASN   B 72  ? 0.2026 0.2236 0.2601 0.0164  -0.0173 -0.0700 72  ASN   B O   
4976 C CB  . ASN   B 72  ? 0.2097 0.2108 0.2387 0.0233  -0.0737 -0.0674 72  ASN   B CB  
4977 C CG  . ASN   B 72  ? 0.2261 0.2233 0.2504 0.0355  -0.0733 -0.0383 72  ASN   B CG  
4978 O OD1 . ASN   B 72  ? 0.2456 0.2406 0.2610 0.0248  -0.0636 -0.0409 72  ASN   B OD1 
4979 N ND2 . ASN   B 72  ? 0.2360 0.2258 0.2949 0.0479  -0.0695 -0.0013 72  ASN   B ND2 
4986 N N   . GLY   B 73  ? 0.2040 0.2056 0.2045 0.0060  -0.0365 -0.0680 73  GLY   B N   
4987 C CA  . GLY   B 73  ? 0.1972 0.2078 0.1944 0.0066  -0.0367 -0.0571 73  GLY   B CA  
4988 C C   . GLY   B 73  ? 0.1906 0.2048 0.1533 0.0113  -0.0329 -0.0613 73  GLY   B C   
4989 O O   . GLY   B 73  ? 0.1860 0.1992 0.1662 0.0142  -0.0288 -0.0433 73  GLY   B O   
4993 N N   . PRO   B 74  ? 0.1881 0.2157 0.1541 0.0038  -0.0288 -0.0402 74  PRO   B N   
4994 C CA  . PRO   B 74  ? 0.1832 0.2139 0.1430 0.0089  -0.0311 -0.0241 74  PRO   B CA  
4995 C C   . PRO   B 74  ? 0.1731 0.1973 0.1475 0.0094  -0.0217 -0.0199 74  PRO   B C   
4996 O O   . PRO   B 74  ? 0.1781 0.2045 0.1825 0.0091  -0.0188 -0.0328 74  PRO   B O   
4997 C CB  . PRO   B 74  ? 0.1957 0.2311 0.1411 0.0070  -0.0204 -0.0220 74  PRO   B CB  
4998 C CG  . PRO   B 74  ? 0.2092 0.2455 0.1604 0.0048  -0.0150 -0.0186 74  PRO   B CG  
4999 C CD  . PRO   B 74  ? 0.2082 0.2369 0.1514 0.0053  -0.0127 -0.0303 74  PRO   B CD  
5007 N N   . LEU   B 75  ? 0.1693 0.1830 0.1373 0.0122  -0.0247 -0.0202 75  LEU   B N   
5008 C CA  . LEU   B 75  ? 0.1723 0.1881 0.1330 0.0068  -0.0142 -0.0086 75  LEU   B CA  
5009 C C   . LEU   B 75  ? 0.1796 0.2014 0.1252 0.0090  -0.0070 -0.0104 75  LEU   B C   
5010 O O   . LEU   B 75  ? 0.1951 0.2167 0.1355 0.0039  -0.0061 -0.0023 75  LEU   B O   
5011 C CB  . LEU   B 75  ? 0.1810 0.1936 0.1287 -0.0065 -0.0236 0.0125  75  LEU   B CB  
5012 C CG  . LEU   B 75  ? 0.2183 0.2090 0.1411 -0.0293 -0.0122 0.0038  75  LEU   B CG  
5013 C CD1 . LEU   B 75  ? 0.2517 0.2207 0.1441 -0.0405 0.0098  -0.0136 75  LEU   B CD1 
5014 C CD2 . LEU   B 75  ? 0.2532 0.2333 0.2373 -0.0196 0.0039  0.0202  75  LEU   B CD2 
5026 N N   . LYS   B 76  ? 0.1806 0.2205 0.1640 0.0057  -0.0083 -0.0060 76  LYS   B N   
5027 C CA  . LYS   B 76  ? 0.1909 0.2289 0.1985 -0.0005 0.0225  -0.0039 76  LYS   B CA  
5028 C C   . LYS   B 76  ? 0.1818 0.2143 0.1492 0.0058  0.0105  0.0139  76  LYS   B C   
5029 O O   . LYS   B 76  ? 0.1764 0.1979 0.1594 0.0014  0.0016  0.0114  76  LYS   B O   
5030 C CB  . LYS   B 76  ? 0.2108 0.2414 0.2708 -0.0015 0.0436  -0.0388 76  LYS   B CB  
5031 C CG  . LYS   B 76  ? 0.2206 0.2615 0.3121 0.0109  0.0279  -0.0455 76  LYS   B CG  
5032 C CD  . LYS   B 76  ? 0.2187 0.2750 0.3417 0.0211  0.0221  -0.0598 76  LYS   B CD  
5033 C CE  . LYS   B 76  ? 0.2217 0.2949 0.4129 0.0196  0.0065  -0.0646 76  LYS   B CE  
5034 N NZ  . LYS   B 76  ? 0.2176 0.3015 0.4310 0.0162  -0.0193 -0.0869 76  LYS   B NZ  
5048 N N   . VAL   B 77  ? 0.1926 0.2217 0.1479 0.0120  0.0057  0.0188  77  VAL   B N   
5049 C CA  . VAL   B 77  ? 0.1918 0.2159 0.1673 0.0183  0.0099  0.0403  77  VAL   B CA  
5050 C C   . VAL   B 77  ? 0.1751 0.1938 0.1597 0.0198  0.0129  0.0324  77  VAL   B C   
5051 O O   . VAL   B 77  ? 0.1732 0.1888 0.1712 0.0271  0.0244  0.0198  77  VAL   B O   
5052 C CB  . VAL   B 77  ? 0.2058 0.2294 0.2069 0.0157  0.0164  0.0543  77  VAL   B CB  
5053 C CG1 . VAL   B 77  ? 0.2068 0.2271 0.2341 0.0099  0.0305  0.0703  77  VAL   B CG1 
5054 C CG2 . VAL   B 77  ? 0.2237 0.2435 0.2306 0.0052  -0.0036 0.0597  77  VAL   B CG2 
5064 N N   . GLY   B 78  ? 0.1668 0.1873 0.1472 0.0104  0.0080  0.0244  78  GLY   B N   
5065 C CA  . GLY   B 78  ? 0.1630 0.1779 0.1510 0.0142  0.0200  0.0173  78  GLY   B CA  
5066 C C   . GLY   B 78  ? 0.1587 0.1684 0.1476 0.0101  0.0201  0.0212  78  GLY   B C   
5067 O O   . GLY   B 78  ? 0.1674 0.1609 0.1624 0.0183  0.0119  0.0202  78  GLY   B O   
5071 N N   . GLY   B 79  ? 0.1507 0.1736 0.1648 0.0067  0.0122  0.0108  79  GLY   B N   
5072 C CA  . GLY   B 79  ? 0.1557 0.1650 0.1679 0.0113  0.0096  0.0105  79  GLY   B CA  
5073 C C   . GLY   B 79  ? 0.1494 0.1516 0.1501 0.0146  0.0061  -0.0008 79  GLY   B C   
5074 O O   . GLY   B 79  ? 0.1522 0.1493 0.1562 0.0130  0.0054  0.0122  79  GLY   B O   
5078 N N   . SER   B 80  ? 0.1464 0.1448 0.1621 0.0055  0.0096  0.0031  80  SER   B N   
5079 C CA  . SER   B 80  ? 0.1464 0.1437 0.1599 0.0034  -0.0001 0.0005  80  SER   B CA  
5080 C C   . SER   B 80  ? 0.1470 0.1467 0.1562 0.0089  -0.0128 -0.0041 80  SER   B C   
5081 O O   . SER   B 80  ? 0.1583 0.1460 0.1840 0.0113  -0.0047 -0.0086 80  SER   B O   
5082 C CB  . SER   B 80  ? 0.1536 0.1492 0.1676 -0.0026 -0.0026 0.0069  80  SER   B CB  
5083 O OG  . SER   B 80  ? 0.1630 0.1631 0.1909 0.0009  -0.0148 0.0111  80  SER   B OG  
5089 N N   . CYS   B 81  ? 0.1476 0.1314 0.1581 0.0002  -0.0081 -0.0043 81  CYS   B N   
5090 C CA  . CYS   B 81  ? 0.1530 0.1281 0.1584 0.0085  -0.0220 -0.0040 81  CYS   B CA  
5091 C C   . CYS   B 81  ? 0.1534 0.1281 0.1407 0.0031  -0.0232 -0.0064 81  CYS   B C   
5092 O O   . CYS   B 81  ? 0.1698 0.1322 0.1531 0.0047  -0.0044 -0.0037 81  CYS   B O   
5093 C CB  . CYS   B 81  ? 0.1714 0.1423 0.1674 0.0043  -0.0181 -0.0050 81  CYS   B CB  
5094 S SG  . CYS   B 81  ? 0.1668 0.1604 0.1702 -0.0032 -0.0284 -0.0099 81  CYS   B SG  
5100 N N   . VAL   B 82  ? 0.1574 0.1288 0.1468 -0.0007 -0.0182 -0.0099 82  VAL   B N   
5101 C CA  . VAL   B 82  ? 0.1618 0.1345 0.1402 -0.0033 -0.0155 -0.0032 82  VAL   B CA  
5102 C C   . VAL   B 82  ? 0.1668 0.1268 0.1543 -0.0023 -0.0184 0.0019  82  VAL   B C   
5103 O O   . VAL   B 82  ? 0.1787 0.1278 0.1890 -0.0045 -0.0166 -0.0140 82  VAL   B O   
5104 C CB  . VAL   B 82  ? 0.1712 0.1551 0.1540 -0.0015 -0.0202 0.0067  82  VAL   B CB  
5105 C CG1 . VAL   B 82  ? 0.1868 0.1665 0.1751 0.0073  -0.0136 0.0126  82  VAL   B CG1 
5106 C CG2 . VAL   B 82  ? 0.1757 0.1719 0.1693 -0.0065 -0.0280 0.0128  82  VAL   B CG2 
5116 N N   . LEU   B 83  ? 0.1514 0.1302 0.1558 -0.0153 -0.0269 0.0004  83  LEU   B N   
5117 C CA  . LEU   B 83  ? 0.1566 0.1332 0.1432 -0.0142 -0.0253 -0.0033 83  LEU   B CA  
5118 C C   . LEU   B 83  ? 0.1550 0.1318 0.1459 -0.0174 -0.0216 0.0000  83  LEU   B C   
5119 O O   . LEU   B 83  ? 0.1551 0.1376 0.1381 -0.0197 -0.0182 0.0077  83  LEU   B O   
5120 C CB  . LEU   B 83  ? 0.1629 0.1486 0.1429 -0.0134 -0.0260 -0.0121 83  LEU   B CB  
5121 C CG  . LEU   B 83  ? 0.1780 0.1686 0.1620 -0.0145 -0.0214 -0.0120 83  LEU   B CG  
5122 C CD1 . LEU   B 83  ? 0.1855 0.1759 0.1624 -0.0078 -0.0262 -0.0064 83  LEU   B CD1 
5123 C CD2 . LEU   B 83  ? 0.1952 0.1771 0.1668 -0.0080 -0.0180 -0.0180 83  LEU   B CD2 
5135 N N   . SER   B 84  ? 0.1614 0.1410 0.1734 -0.0281 -0.0229 0.0060  84  SER   B N   
5136 C CA  . SER   B 84  ? 0.1631 0.1588 0.1544 -0.0317 -0.0165 0.0162  84  SER   B CA  
5137 C C   . SER   B 84  ? 0.1539 0.1789 0.1299 -0.0240 -0.0292 0.0211  84  SER   B C   
5138 O O   . SER   B 84  ? 0.1632 0.1667 0.1275 -0.0214 -0.0174 0.0083  84  SER   B O   
5139 C CB  . SER   B 84  ? 0.1768 0.1627 0.2105 -0.0282 0.0118  0.0138  84  SER   B CB  
5140 O OG  . SER   B 84  ? 0.1729 0.1780 0.2660 -0.0372 0.0082  0.0191  84  SER   B OG  
5146 N N   . GLY   B 85  ? 0.1554 0.1965 0.1370 -0.0282 -0.0236 0.0240  85  GLY   B N   
5147 C CA  . GLY   B 85  ? 0.1576 0.2039 0.1566 -0.0326 -0.0035 -0.0005 85  GLY   B CA  
5148 C C   . GLY   B 85  ? 0.1560 0.1863 0.1465 -0.0384 -0.0051 0.0109  85  GLY   B C   
5149 O O   . GLY   B 85  ? 0.1676 0.1854 0.1514 -0.0532 0.0049  -0.0024 85  GLY   B O   
5153 N N   . HIS   B 86  ? 0.1553 0.1720 0.1511 -0.0314 -0.0219 0.0231  86  HIS   B N   
5154 C CA  . HIS   B 86  ? 0.1540 0.1691 0.1560 -0.0324 -0.0179 0.0233  86  HIS   B CA  
5155 C C   . HIS   B 86  ? 0.1563 0.1818 0.1425 -0.0463 -0.0145 0.0363  86  HIS   B C   
5156 O O   . HIS   B 86  ? 0.1708 0.2001 0.1503 -0.0389 -0.0010 0.0306  86  HIS   B O   
5157 C CB  . HIS   B 86  ? 0.1654 0.1751 0.1634 -0.0204 -0.0211 0.0174  86  HIS   B CB  
5158 C CG  . HIS   B 86  ? 0.1693 0.1778 0.1625 -0.0183 -0.0330 0.0267  86  HIS   B CG  
5159 N ND1 . HIS   B 86  ? 0.1789 0.1984 0.1725 -0.0250 -0.0353 0.0020  86  HIS   B ND1 
5160 C CD2 . HIS   B 86  ? 0.1631 0.1813 0.1699 -0.0121 -0.0317 0.0245  86  HIS   B CD2 
5161 C CE1 . HIS   B 86  ? 0.1826 0.1977 0.1698 -0.0168 -0.0165 -0.0164 86  HIS   B CE1 
5162 N NE2 . HIS   B 86  ? 0.1743 0.1926 0.1604 -0.0024 -0.0215 0.0031  86  HIS   B NE2 
5170 N N   . ASN   B 87  ? 0.1614 0.1839 0.1630 -0.0401 -0.0089 0.0244  87  ASN   B N   
5171 C CA  . ASN   B 87  ? 0.1703 0.2010 0.1670 -0.0320 0.0169  0.0203  87  ASN   B CA  
5172 C C   . ASN   B 87  ? 0.1831 0.1936 0.1575 -0.0305 0.0290  0.0166  87  ASN   B C   
5173 O O   . ASN   B 87  ? 0.2067 0.2008 0.1934 -0.0300 0.0501  0.0110  87  ASN   B O   
5174 C CB  . ASN   B 87  ? 0.1721 0.2328 0.2129 -0.0171 0.0140  0.0111  87  ASN   B CB  
5175 C CG  . ASN   B 87  ? 0.1851 0.2550 0.2161 0.0122  0.0242  0.0351  87  ASN   B CG  
5176 O OD1 . ASN   B 87  ? 0.1785 0.2393 0.2007 0.0114  0.0441  0.0500  87  ASN   B OD1 
5177 N ND2 . ASN   B 87  ? 0.2150 0.2719 0.2590 0.0227  0.0348  0.0426  87  ASN   B ND2 
5184 N N   . LEU   B 88  ? 0.1674 0.1815 0.1349 -0.0313 0.0106  0.0127  88  LEU   B N   
5185 C CA  . LEU   B 88  ? 0.1717 0.1723 0.1455 -0.0303 0.0014  -0.0006 88  LEU   B CA  
5186 C C   . LEU   B 88  ? 0.1725 0.1623 0.1421 -0.0303 -0.0012 0.0063  88  LEU   B C   
5187 O O   . LEU   B 88  ? 0.2018 0.1699 0.1675 -0.0155 -0.0265 -0.0070 88  LEU   B O   
5188 C CB  . LEU   B 88  ? 0.1968 0.1799 0.1552 -0.0351 -0.0090 0.0211  88  LEU   B CB  
5189 C CG  . LEU   B 88  ? 0.2401 0.2161 0.1858 -0.0292 -0.0216 0.0351  88  LEU   B CG  
5190 C CD1 . LEU   B 88  ? 0.2499 0.2483 0.2061 -0.0469 -0.0130 0.0461  88  LEU   B CD1 
5191 C CD2 . LEU   B 88  ? 0.2772 0.2406 0.2467 0.0117  -0.0556 0.0202  88  LEU   B CD2 
5203 N N   . ALA   B 89  ? 0.1643 0.1621 0.1377 -0.0363 0.0151  0.0026  89  ALA   B N   
5204 C CA  . ALA   B 89  ? 0.1630 0.1566 0.1379 -0.0356 0.0060  0.0120  89  ALA   B CA  
5205 C C   . ALA   B 89  ? 0.1718 0.1552 0.1432 -0.0374 0.0171  0.0093  89  ALA   B C   
5206 O O   . ALA   B 89  ? 0.1538 0.1674 0.1722 -0.0412 0.0107  -0.0201 89  ALA   B O   
5207 C CB  . ALA   B 89  ? 0.1596 0.1595 0.1537 -0.0378 -0.0016 0.0224  89  ALA   B CB  
5213 N N   . LYS   B 90  ? 0.2089 0.1444 0.1448 -0.0498 -0.0065 0.0107  90  LYS   B N   
5214 C CA  . LYS   B 90  ? 0.2261 0.1433 0.1269 -0.0460 -0.0142 0.0114  90  LYS   B CA  
5215 C C   . LYS   B 90  ? 0.2083 0.1367 0.1573 -0.0450 -0.0141 -0.0017 90  LYS   B C   
5216 O O   . LYS   B 90  ? 0.2173 0.1568 0.1816 -0.0603 0.0012  0.0002  90  LYS   B O   
5217 C CB  . LYS   B 90  ? 0.2489 0.1534 0.1602 -0.0341 0.0040  0.0210  90  LYS   B CB  
5218 C CG  . LYS   B 90  ? 0.2467 0.1671 0.1728 -0.0287 0.0309  0.0114  90  LYS   B CG  
5219 C CD  . LYS   B 90  ? 0.2678 0.1863 0.2204 -0.0236 0.0436  -0.0195 90  LYS   B CD  
5220 C CE  . LYS   B 90  ? 0.2821 0.2010 0.2838 -0.0258 0.0562  -0.0233 90  LYS   B CE  
5221 N NZ  . LYS   B 90  ? 0.2826 0.1953 0.2721 -0.0315 0.0732  -0.0185 90  LYS   B NZ  
5235 N N   . HIS   B 91  ? 0.1832 0.1279 0.1326 -0.0308 -0.0208 0.0095  91  HIS   B N   
5236 C CA  . HIS   B 91  ? 0.1708 0.1307 0.1355 -0.0258 -0.0232 0.0012  91  HIS   B CA  
5237 C C   . HIS   B 91  ? 0.1596 0.1374 0.1209 -0.0274 -0.0182 -0.0008 91  HIS   B C   
5238 O O   . HIS   B 91  ? 0.1733 0.1411 0.1194 -0.0267 -0.0187 0.0032  91  HIS   B O   
5239 C CB  . HIS   B 91  ? 0.1929 0.1384 0.1596 -0.0065 -0.0097 0.0121  91  HIS   B CB  
5240 C CG  . HIS   B 91  ? 0.2295 0.1585 0.2483 0.0070  0.0187  0.0264  91  HIS   B CG  
5241 N ND1 . HIS   B 91  ? 0.2613 0.1654 0.3147 0.0077  0.0264  0.0234  91  HIS   B ND1 
5242 C CD2 . HIS   B 91  ? 0.2396 0.1912 0.3075 0.0205  0.0130  0.0579  91  HIS   B CD2 
5243 C CE1 . HIS   B 91  ? 0.2621 0.1832 0.3312 0.0237  0.0297  0.0277  91  HIS   B CE1 
5244 N NE2 . HIS   B 91  ? 0.2486 0.1967 0.3431 0.0322  0.0322  0.0628  91  HIS   B NE2 
5252 N N   . CYS   B 92  ? 0.1558 0.1318 0.1321 -0.0247 -0.0174 0.0024  92  CYS   B N   
5253 C CA  . CYS   B 92  ? 0.1485 0.1284 0.1335 -0.0189 -0.0128 -0.0005 92  CYS   B CA  
5254 C C   . CYS   B 92  ? 0.1407 0.1243 0.1273 -0.0144 -0.0074 -0.0014 92  CYS   B C   
5255 O O   . CYS   B 92  ? 0.1515 0.1307 0.1448 -0.0116 -0.0095 0.0009  92  CYS   B O   
5256 C CB  . CYS   B 92  ? 0.1492 0.1406 0.1283 -0.0149 -0.0110 -0.0013 92  CYS   B CB  
5257 S SG  . CYS   B 92  ? 0.1455 0.1397 0.1481 -0.0137 -0.0159 0.0047  92  CYS   B SG  
5263 N N   . LEU   B 93  ? 0.1373 0.1308 0.1201 -0.0110 -0.0067 -0.0020 93  LEU   B N   
5264 C CA  . LEU   B 93  ? 0.1402 0.1305 0.1248 -0.0057 -0.0048 0.0020  93  LEU   B CA  
5265 C C   . LEU   B 93  ? 0.1373 0.1270 0.1122 -0.0037 -0.0043 0.0081  93  LEU   B C   
5266 O O   . LEU   B 93  ? 0.1427 0.1260 0.1309 -0.0084 -0.0077 0.0029  93  LEU   B O   
5267 C CB  . LEU   B 93  ? 0.1416 0.1344 0.1289 0.0009  -0.0069 0.0043  93  LEU   B CB  
5268 C CG  . LEU   B 93  ? 0.1418 0.1458 0.1485 -0.0007 -0.0103 0.0094  93  LEU   B CG  
5269 C CD1 . LEU   B 93  ? 0.1437 0.1513 0.1492 0.0002  -0.0094 -0.0030 93  LEU   B CD1 
5270 C CD2 . LEU   B 93  ? 0.1375 0.1464 0.1624 -0.0002 -0.0080 0.0002  93  LEU   B CD2 
5282 N N   . HIS   B 94  ? 0.1428 0.1252 0.1179 -0.0041 -0.0126 0.0048  94  HIS   B N   
5283 C CA  . HIS   B 94  ? 0.1422 0.1234 0.1228 -0.0033 -0.0047 0.0035  94  HIS   B CA  
5284 C C   . HIS   B 94  ? 0.1382 0.1297 0.1291 -0.0003 -0.0049 0.0029  94  HIS   B C   
5285 O O   . HIS   B 94  ? 0.1408 0.1368 0.1716 -0.0059 0.0058  -0.0066 94  HIS   B O   
5286 C CB  . HIS   B 94  ? 0.1422 0.1299 0.1392 -0.0004 -0.0094 0.0025  94  HIS   B CB  
5287 C CG  . HIS   B 94  ? 0.1423 0.1299 0.1385 -0.0063 -0.0229 0.0055  94  HIS   B CG  
5288 N ND1 . HIS   B 94  ? 0.1396 0.1377 0.1341 -0.0086 -0.0221 0.0035  94  HIS   B ND1 
5289 C CD2 . HIS   B 94  ? 0.1468 0.1311 0.1428 0.0000  -0.0219 0.0019  94  HIS   B CD2 
5290 C CE1 . HIS   B 94  ? 0.1435 0.1331 0.1430 -0.0089 -0.0233 0.0078  94  HIS   B CE1 
5291 N NE2 . HIS   B 94  ? 0.1411 0.1384 0.1488 -0.0132 -0.0166 0.0051  94  HIS   B NE2 
5299 N N   . VAL   B 95  ? 0.1348 0.1245 0.1384 -0.0015 -0.0015 0.0048  95  VAL   B N   
5300 C CA  . VAL   B 95  ? 0.1382 0.1344 0.1350 0.0031  -0.0005 0.0102  95  VAL   B CA  
5301 C C   . VAL   B 95  ? 0.1422 0.1290 0.1456 -0.0030 0.0067  0.0004  95  VAL   B C   
5302 O O   . VAL   B 95  ? 0.1460 0.1284 0.1544 0.0028  0.0045  0.0075  95  VAL   B O   
5303 C CB  . VAL   B 95  ? 0.1425 0.1324 0.1491 -0.0034 -0.0091 0.0064  95  VAL   B CB  
5304 C CG1 . VAL   B 95  ? 0.1477 0.1548 0.1594 -0.0071 -0.0071 0.0139  95  VAL   B CG1 
5305 C CG2 . VAL   B 95  ? 0.1502 0.1252 0.1473 0.0038  -0.0126 0.0014  95  VAL   B CG2 
5315 N N   . VAL   B 96  ? 0.1506 0.1424 0.1321 0.0184  0.0022  0.0119  96  VAL   B N   
5316 C CA  . VAL   B 96  ? 0.1536 0.1551 0.1336 0.0129  -0.0019 0.0170  96  VAL   B CA  
5317 C C   . VAL   B 96  ? 0.1592 0.1564 0.1303 0.0059  0.0088  0.0186  96  VAL   B C   
5318 O O   . VAL   B 96  ? 0.1595 0.1660 0.1568 -0.0023 0.0152  0.0026  96  VAL   B O   
5319 C CB  . VAL   B 96  ? 0.1639 0.1724 0.1313 0.0111  -0.0033 0.0087  96  VAL   B CB  
5320 C CG1 . VAL   B 96  ? 0.1628 0.1873 0.1580 0.0159  0.0068  0.0037  96  VAL   B CG1 
5321 C CG2 . VAL   B 96  ? 0.1733 0.1764 0.1498 0.0079  0.0054  0.0024  96  VAL   B CG2 
5331 N N   . GLY   B 97  ? 0.1650 0.1541 0.1392 -0.0025 -0.0016 0.0190  97  GLY   B N   
5332 C CA  . GLY   B 97  ? 0.1828 0.1555 0.1400 0.0009  -0.0034 0.0185  97  GLY   B CA  
5333 C C   . GLY   B 97  ? 0.1975 0.1622 0.1553 0.0082  -0.0108 0.0115  97  GLY   B C   
5334 O O   . GLY   B 97  ? 0.2076 0.1721 0.1594 0.0036  -0.0063 0.0137  97  GLY   B O   
5338 N N   . PRO   B 98  ? 0.2090 0.1672 0.1642 0.0017  0.0098  0.0268  98  PRO   B N   
5339 C CA  . PRO   B 98  ? 0.2155 0.1859 0.1711 0.0069  0.0246  0.0228  98  PRO   B CA  
5340 C C   . PRO   B 98  ? 0.2218 0.1904 0.1158 0.0191  0.0230  0.0325  98  PRO   B C   
5341 O O   . PRO   B 98  ? 0.2141 0.1935 0.1491 0.0243  0.0268  0.0335  98  PRO   B O   
5342 C CB  . PRO   B 98  ? 0.2055 0.1930 0.1936 0.0062  0.0364  0.0271  98  PRO   B CB  
5343 C CG  . PRO   B 98  ? 0.2020 0.1855 0.1842 0.0039  0.0215  0.0396  98  PRO   B CG  
5344 C CD  . PRO   B 98  ? 0.1963 0.1683 0.1810 0.0010  0.0202  0.0340  98  PRO   B CD  
5352 N N   . ASN   B 99  ? 0.2232 0.2028 0.1477 0.0307  0.0210  0.0115  99  ASN   B N   
5353 C CA  . ASN   B 99  ? 0.2480 0.2092 0.1544 0.0367  0.0139  0.0372  99  ASN   B CA  
5354 C C   . ASN   B 99  ? 0.2809 0.2429 0.1858 0.0292  0.0390  0.0678  99  ASN   B C   
5355 O O   . ASN   B 99  ? 0.2925 0.2529 0.1893 0.0408  0.0406  0.0698  99  ASN   B O   
5356 C CB  . ASN   B 99  ? 0.2556 0.2049 0.1540 0.0394  0.0013  0.0250  99  ASN   B CB  
5357 C CG  . ASN   B 99  ? 0.2601 0.2077 0.1991 0.0376  -0.0042 0.0256  99  ASN   B CG  
5358 O OD1 . ASN   B 99  ? 0.2691 0.2069 0.2356 0.0347  -0.0035 0.0425  99  ASN   B OD1 
5359 N ND2 . ASN   B 99  ? 0.2582 0.2146 0.2166 0.0416  -0.0162 0.0189  99  ASN   B ND2 
5366 N N   A VAL   B 100 ? 0.2996 0.2503 0.2347 0.0161  0.0367  0.0889  100 VAL   B N   
5367 N N   B VAL   B 100 ? 0.3037 0.2552 0.2339 0.0200  0.0298  0.0806  100 VAL   B N   
5368 C CA  A VAL   B 100 ? 0.3324 0.2684 0.2913 0.0060  0.0362  0.1062  100 VAL   B CA  
5369 C CA  B VAL   B 100 ? 0.3338 0.2707 0.2790 0.0137  0.0227  0.0926  100 VAL   B CA  
5370 C C   A VAL   B 100 ? 0.3526 0.2717 0.2827 0.0160  0.0387  0.1207  100 VAL   B C   
5371 C C   B VAL   B 100 ? 0.3525 0.2744 0.2787 0.0211  0.0228  0.1107  100 VAL   B C   
5372 O O   A VAL   B 100 ? 0.3607 0.2797 0.2818 0.0130  0.0542  0.1144  100 VAL   B O   
5373 O O   B VAL   B 100 ? 0.3579 0.2787 0.2740 0.0190  0.0272  0.1064  100 VAL   B O   
5374 C CB  A VAL   B 100 ? 0.3476 0.2869 0.3580 -0.0131 0.0336  0.1166  100 VAL   B CB  
5375 C CB  B VAL   B 100 ? 0.3456 0.2831 0.3237 0.0011  0.0174  0.0911  100 VAL   B CB  
5376 C CG1 A VAL   B 100 ? 0.3578 0.2938 0.3963 -0.0134 0.0343  0.1121  100 VAL   B CG1 
5377 C CG1 B VAL   B 100 ? 0.3519 0.2864 0.3479 -0.0002 0.0175  0.0871  100 VAL   B CG1 
5378 C CG2 A VAL   B 100 ? 0.3486 0.2929 0.3786 -0.0268 0.0367  0.1306  100 VAL   B CG2 
5379 C CG2 B VAL   B 100 ? 0.3479 0.2883 0.3404 -0.0066 0.0160  0.0934  100 VAL   B CG2 
5398 N N   . ASN   B 101 ? 0.3653 0.2778 0.2859 0.0322  0.0162  0.1252  101 ASN   B N   
5399 C CA  . ASN   B 101 ? 0.4029 0.2988 0.2847 0.0504  -0.0047 0.1356  101 ASN   B CA  
5400 C C   . ASN   B 101 ? 0.4431 0.3344 0.2791 0.0557  -0.0173 0.1532  101 ASN   B C   
5401 O O   . ASN   B 101 ? 0.4534 0.3574 0.3197 0.0622  -0.0146 0.1174  101 ASN   B O   
5402 C CB  . ASN   B 101 ? 0.4039 0.2874 0.3116 0.0503  0.0078  0.1204  101 ASN   B CB  
5403 C CG  . ASN   B 101 ? 0.4056 0.2778 0.3239 0.0519  0.0210  0.1159  101 ASN   B CG  
5404 O OD1 . ASN   B 101 ? 0.4110 0.2784 0.3484 0.0386  0.0459  0.1086  101 ASN   B OD1 
5405 N ND2 . ASN   B 101 ? 0.4038 0.2762 0.3078 0.0592  0.0195  0.1009  101 ASN   B ND2 
5413 N N   . LYS   B 102 ? 0.4692 0.3576 0.2983 0.0460  -0.0135 0.1584  102 LYS   B N   
5414 C CA  . LYS   B 102 ? 0.4944 0.3974 0.3160 0.0270  -0.0012 0.1260  102 LYS   B CA  
5415 C C   . LYS   B 102 ? 0.4910 0.4008 0.3041 0.0246  0.0100  0.1296  102 LYS   B C   
5416 O O   . LYS   B 102 ? 0.5006 0.4073 0.3250 0.0266  -0.0099 0.1158  102 LYS   B O   
5417 C CB  . LYS   B 102 ? 0.5210 0.4351 0.3783 0.0099  0.0110  0.0756  102 LYS   B CB  
5418 C CG  . LYS   B 102 ? 0.5468 0.4719 0.4383 -0.0019 0.0257  0.0331  102 LYS   B CG  
5419 C CD  . LYS   B 102 ? 0.5695 0.5024 0.5054 -0.0093 0.0424  0.0048  102 LYS   B CD  
5420 C CE  . LYS   B 102 ? 0.5847 0.5225 0.5559 -0.0129 0.0508  -0.0185 102 LYS   B CE  
5421 N NZ  . LYS   B 102 ? 0.5939 0.5338 0.5895 -0.0127 0.0499  -0.0339 102 LYS   B NZ  
5435 N N   . GLY   B 103 ? 0.4738 0.3958 0.3029 0.0212  0.0366  0.1278  103 GLY   B N   
5436 C CA  . GLY   B 103 ? 0.4542 0.3872 0.3171 0.0229  0.0595  0.1026  103 GLY   B CA  
5437 C C   . GLY   B 103 ? 0.4293 0.3700 0.3069 0.0240  0.0767  0.0819  103 GLY   B C   
5438 O O   . GLY   B 103 ? 0.4382 0.3810 0.3102 0.0309  0.0816  0.0742  103 GLY   B O   
5442 N N   A GLU   B 104 ? 0.4100 0.3512 0.2877 0.0218  0.0909  0.0733  104 GLU   B N   
5443 N N   B GLU   B 104 ? 0.4121 0.3568 0.3057 0.0178  0.0663  0.0671  104 GLU   B N   
5444 C CA  A GLU   B 104 ? 0.3905 0.3343 0.2656 0.0225  0.0965  0.0602  104 GLU   B CA  
5445 C CA  B GLU   B 104 ? 0.3937 0.3433 0.2975 0.0124  0.0554  0.0487  104 GLU   B CA  
5446 C C   A GLU   B 104 ? 0.3950 0.3414 0.2803 0.0055  0.1353  0.0613  104 GLU   B C   
5447 C C   B GLU   B 104 ? 0.3897 0.3437 0.3100 0.0041  0.0700  0.0413  104 GLU   B C   
5448 O O   A GLU   B 104 ? 0.4023 0.3508 0.3056 -0.0033 0.1317  0.0521  104 GLU   B O   
5449 O O   B GLU   B 104 ? 0.3931 0.3472 0.3185 0.0005  0.0691  0.0341  104 GLU   B O   
5450 C CB  A GLU   B 104 ? 0.3694 0.3097 0.2554 0.0410  0.0572  0.0324  104 GLU   B CB  
5451 C CB  B GLU   B 104 ? 0.3807 0.3292 0.2851 0.0150  0.0309  0.0310  104 GLU   B CB  
5452 C CG  A GLU   B 104 ? 0.3511 0.2935 0.2393 0.0565  0.0209  -0.0024 104 GLU   B CG  
5453 C CG  B GLU   B 104 ? 0.3710 0.3197 0.2732 0.0172  0.0093  0.0100  104 GLU   B CG  
5454 C CD  A GLU   B 104 ? 0.3336 0.2790 0.2000 0.0694  -0.0162 -0.0165 104 GLU   B CD  
5455 C CD  B GLU   B 104 ? 0.3648 0.3129 0.2538 0.0177  -0.0103 -0.0008 104 GLU   B CD  
5456 O OE1 A GLU   B 104 ? 0.3125 0.2661 0.1631 0.0823  -0.0029 -0.0094 104 GLU   B OE1 
5457 O OE1 B GLU   B 104 ? 0.3599 0.3085 0.2412 0.0172  -0.0079 0.0010  104 GLU   B OE1 
5458 O OE2 A GLU   B 104 ? 0.3396 0.2859 0.1960 0.0629  -0.0565 -0.0336 104 GLU   B OE2 
5459 O OE2 B GLU   B 104 ? 0.3657 0.3145 0.2535 0.0169  -0.0280 -0.0097 104 GLU   B OE2 
5472 N N   A ASP   B 105 ? 0.3884 0.3412 0.2636 -0.0025 0.1660  0.0688  105 ASP   B N   
5473 N N   B ASP   B 105 ? 0.3808 0.3412 0.3026 -0.0006 0.0818  0.0401  105 ASP   B N   
5474 C CA  A ASP   B 105 ? 0.3909 0.3448 0.2870 -0.0114 0.1842  0.0501  105 ASP   B CA  
5475 C CA  B ASP   B 105 ? 0.3761 0.3400 0.3155 -0.0063 0.0885  0.0283  105 ASP   B CA  
5476 C C   A ASP   B 105 ? 0.3797 0.3223 0.2704 -0.0253 0.1757  0.0401  105 ASP   B C   
5477 C C   B ASP   B 105 ? 0.3694 0.3308 0.3004 -0.0130 0.0852  0.0186  105 ASP   B C   
5478 O O   A ASP   B 105 ? 0.3695 0.3144 0.2665 -0.0234 0.1741  0.0373  105 ASP   B O   
5479 O O   B ASP   B 105 ? 0.3669 0.3275 0.2839 -0.0133 0.0874  0.0175  105 ASP   B O   
5480 C CB  A ASP   B 105 ? 0.4106 0.3723 0.3584 0.0003  0.1835  0.0238  105 ASP   B CB  
5481 C CB  B ASP   B 105 ? 0.3792 0.3488 0.3437 -0.0032 0.0950  0.0221  105 ASP   B CB  
5482 C CG  A ASP   B 105 ? 0.4299 0.3969 0.4316 0.0024  0.1877  0.0091  105 ASP   B CG  
5483 C CG  B ASP   B 105 ? 0.3835 0.3570 0.3799 -0.0047 0.1035  0.0225  105 ASP   B CG  
5484 O OD1 A ASP   B 105 ? 0.4298 0.4007 0.4293 -0.0062 0.2085  0.0156  105 ASP   B OD1 
5485 O OD1 B ASP   B 105 ? 0.3832 0.3616 0.3791 -0.0106 0.1104  0.0236  105 ASP   B OD1 
5486 O OD2 A ASP   B 105 ? 0.4433 0.4124 0.4753 0.0098  0.1703  -0.0062 105 ASP   B OD2 
5487 O OD2 B ASP   B 105 ? 0.3847 0.3593 0.3892 -0.0039 0.1079  0.0262  105 ASP   B OD2 
5496 N N   A ILE   B 106 ? 0.3743 0.3062 0.2814 -0.0379 0.1620  0.0386  106 ILE   B N   
5497 N N   B ILE   B 106 ? 0.3639 0.3247 0.2948 -0.0170 0.0750  0.0131  106 ILE   B N   
5498 C CA  A ILE   B 106 ? 0.3556 0.2821 0.2858 -0.0540 0.1635  0.0333  106 ILE   B CA  
5499 C CA  B ILE   B 106 ? 0.3528 0.3169 0.2967 -0.0207 0.0724  0.0063  106 ILE   B CA  
5500 C C   A ILE   B 106 ? 0.3187 0.2706 0.2705 -0.0499 0.1617  0.0089  106 ILE   B C   
5501 C C   B ILE   B 106 ? 0.3321 0.3117 0.2898 -0.0178 0.0706  -0.0066 106 ILE   B C   
5502 O O   A ILE   B 106 ? 0.3096 0.2459 0.2700 -0.0541 0.1551  -0.0068 106 ILE   B O   
5503 O O   B ILE   B 106 ? 0.3264 0.3033 0.2840 -0.0216 0.0651  -0.0131 106 ILE   B O   
5504 C CB  A ILE   B 106 ? 0.3774 0.2757 0.3224 -0.0649 0.1529  0.0410  106 ILE   B CB  
5505 C CB  B ILE   B 106 ? 0.3619 0.3164 0.3115 -0.0257 0.0714  0.0103  106 ILE   B CB  
5506 C CG1 A ILE   B 106 ? 0.3830 0.2727 0.3315 -0.0514 0.1458  0.0356  106 ILE   B CG1 
5507 C CG1 B ILE   B 106 ? 0.3625 0.3130 0.3156 -0.0216 0.0692  0.0109  106 ILE   B CG1 
5508 C CG2 A ILE   B 106 ? 0.3853 0.2790 0.3487 -0.0786 0.1514  0.0499  106 ILE   B CG2 
5509 C CG2 B ILE   B 106 ? 0.3667 0.3209 0.3247 -0.0302 0.0722  0.0127  106 ILE   B CG2 
5510 C CD1 A ILE   B 106 ? 0.3852 0.2725 0.3342 -0.0411 0.1412  0.0413  106 ILE   B CD1 
5511 C CD1 B ILE   B 106 ? 0.3627 0.3112 0.3205 -0.0178 0.0667  0.0145  106 ILE   B CD1 
5534 N N   A GLN   B 107 ? 0.3013 0.2916 0.2890 -0.0384 0.1558  0.0045  107 GLN   B N   
5535 N N   B GLN   B 107 ? 0.3199 0.3178 0.3027 -0.0115 0.0718  -0.0113 107 GLN   B N   
5536 C CA  A GLN   B 107 ? 0.2892 0.3130 0.3069 -0.0259 0.1397  0.0060  107 GLN   B CA  
5537 C CA  B GLN   B 107 ? 0.3100 0.3230 0.3153 -0.0044 0.0710  -0.0087 107 GLN   B CA  
5538 C C   A GLN   B 107 ? 0.2652 0.2959 0.2812 -0.0118 0.0941  -0.0033 107 GLN   B C   
5539 C C   B GLN   B 107 ? 0.2795 0.3023 0.2813 0.0015  0.0680  -0.0103 107 GLN   B C   
5540 O O   A GLN   B 107 ? 0.2592 0.3020 0.3250 -0.0072 0.0588  -0.0215 107 GLN   B O   
5541 O O   B GLN   B 107 ? 0.2784 0.3088 0.3012 0.0038  0.0534  -0.0218 107 GLN   B O   
5542 C CB  A GLN   B 107 ? 0.3198 0.3561 0.3864 -0.0203 0.1189  0.0041  107 GLN   B CB  
5543 C CB  B GLN   B 107 ? 0.3341 0.3488 0.3750 -0.0023 0.0598  -0.0071 107 GLN   B CB  
5544 C CG  A GLN   B 107 ? 0.3532 0.3949 0.4698 -0.0111 0.0756  0.0007  107 GLN   B CG  
5545 C CG  B GLN   B 107 ? 0.3562 0.3726 0.4333 0.0004  0.0401  -0.0052 107 GLN   B CG  
5546 C CD  A GLN   B 107 ? 0.3765 0.4227 0.5359 -0.0092 0.0498  0.0017  107 GLN   B CD  
5547 C CD  B GLN   B 107 ? 0.3724 0.3910 0.4818 -0.0002 0.0275  -0.0027 107 GLN   B CD  
5548 O OE1 A GLN   B 107 ? 0.3856 0.4352 0.5593 -0.0132 0.0509  -0.0021 107 GLN   B OE1 
5549 O OE1 B GLN   B 107 ? 0.3797 0.3980 0.4991 -0.0035 0.0291  -0.0037 107 GLN   B OE1 
5550 N NE2 A GLN   B 107 ? 0.3840 0.4303 0.5572 -0.0018 0.0366  0.0076  107 GLN   B NE2 
5551 N NE2 B GLN   B 107 ? 0.3771 0.3969 0.4972 0.0037  0.0209  0.0008  107 GLN   B NE2 
5568 N N   . LEU   B 108 ? 0.2506 0.2747 0.2505 0.0084  0.0755  -0.0067 108 LEU   B N   
5569 C CA  . LEU   B 108 ? 0.2332 0.2410 0.2152 0.0212  0.0621  0.0095  108 LEU   B CA  
5570 C C   . LEU   B 108 ? 0.2003 0.2005 0.2080 0.0218  0.0341  0.0206  108 LEU   B C   
5571 O O   . LEU   B 108 ? 0.1991 0.1855 0.1942 0.0277  0.0250  0.0171  108 LEU   B O   
5572 C CB  . LEU   B 108 ? 0.2499 0.2541 0.2061 0.0198  0.0621  0.0193  108 LEU   B CB  
5573 C CG  . LEU   B 108 ? 0.2674 0.2811 0.2234 0.0240  0.0530  -0.0057 108 LEU   B CG  
5574 C CD1 . LEU   B 108 ? 0.2755 0.2904 0.2033 0.0145  0.0533  0.0006  108 LEU   B CD1 
5575 C CD2 . LEU   B 108 ? 0.2836 0.2973 0.2431 0.0354  0.0401  -0.0274 108 LEU   B CD2 
5588 N N   . LEU   B 109 ? 0.1798 0.1799 0.1975 0.0179  0.0283  0.0199  109 LEU   B N   
5589 C CA  . LEU   B 109 ? 0.1686 0.1582 0.2081 0.0103  0.0342  0.0273  109 LEU   B CA  
5590 C C   . LEU   B 109 ? 0.1591 0.1446 0.2097 0.0069  0.0376  0.0155  109 LEU   B C   
5591 O O   . LEU   B 109 ? 0.1580 0.1392 0.2050 0.0064  0.0294  0.0259  109 LEU   B O   
5592 C CB  . LEU   B 109 ? 0.1710 0.1503 0.2147 0.0100  0.0300  0.0364  109 LEU   B CB  
5593 C CG  . LEU   B 109 ? 0.1698 0.1463 0.2185 0.0019  0.0233  0.0265  109 LEU   B CG  
5594 C CD1 . LEU   B 109 ? 0.1661 0.1591 0.2067 0.0157  0.0177  0.0274  109 LEU   B CD1 
5595 C CD2 . LEU   B 109 ? 0.1783 0.1542 0.2185 0.0146  0.0183  0.0230  109 LEU   B CD2 
5607 N N   . LYS   B 110 ? 0.1493 0.1469 0.2142 -0.0024 0.0335  0.0229  110 LYS   B N   
5608 C CA  . LYS   B 110 ? 0.1497 0.1410 0.2014 -0.0021 0.0160  0.0184  110 LYS   B CA  
5609 C C   . LYS   B 110 ? 0.1448 0.1409 0.1946 0.0020  0.0209  0.0134  110 LYS   B C   
5610 O O   . LYS   B 110 ? 0.1401 0.1441 0.1872 0.0004  0.0173  0.0125  110 LYS   B O   
5611 C CB  . LYS   B 110 ? 0.1427 0.1431 0.2328 -0.0034 0.0240  0.0078  110 LYS   B CB  
5612 C CG  . LYS   B 110 ? 0.1452 0.1441 0.2680 -0.0041 0.0064  0.0060  110 LYS   B CG  
5613 C CD  . LYS   B 110 ? 0.1477 0.1444 0.2624 -0.0107 0.0118  0.0090  110 LYS   B CD  
5614 C CE  . LYS   B 110 ? 0.1454 0.1578 0.2693 -0.0025 0.0204  0.0085  110 LYS   B CE  
5615 N NZ  . LYS   B 110 ? 0.1506 0.1668 0.2560 -0.0018 0.0110  0.0034  110 LYS   B NZ  
5629 N N   . SER   B 111 ? 0.1555 0.1388 0.2165 -0.0032 0.0297  0.0128  111 SER   B N   
5630 C CA  . SER   B 111 ? 0.1578 0.1454 0.2011 0.0038  0.0243  0.0158  111 SER   B CA  
5631 C C   . SER   B 111 ? 0.1521 0.1379 0.1897 0.0058  0.0137  0.0091  111 SER   B C   
5632 O O   . SER   B 111 ? 0.1440 0.1395 0.1988 0.0017  0.0090  0.0068  111 SER   B O   
5633 C CB  . SER   B 111 ? 0.1695 0.1671 0.2231 0.0099  0.0362  0.0269  111 SER   B CB  
5634 O OG  . SER   B 111 ? 0.1874 0.2015 0.2173 0.0130  0.0435  0.0218  111 SER   B OG  
5640 N N   . ALA   B 112 ? 0.1431 0.1471 0.1872 0.0090  0.0223  0.0236  112 ALA   B N   
5641 C CA  . ALA   B 112 ? 0.1454 0.1497 0.1710 0.0066  0.0039  0.0106  112 ALA   B CA  
5642 C C   . ALA   B 112 ? 0.1369 0.1366 0.1671 0.0028  0.0015  0.0043  112 ALA   B C   
5643 O O   . ALA   B 112 ? 0.1309 0.1366 0.1899 -0.0019 0.0088  -0.0013 112 ALA   B O   
5644 C CB  . ALA   B 112 ? 0.1501 0.1510 0.1817 0.0140  0.0065  0.0160  112 ALA   B CB  
5650 N N   . TYR   B 113 ? 0.1326 0.1305 0.1878 0.0035  0.0070  0.0061  113 TYR   B N   
5651 C CA  . TYR   B 113 ? 0.1289 0.1300 0.1763 0.0005  0.0092  0.0011  113 TYR   B CA  
5652 C C   . TYR   B 113 ? 0.1244 0.1249 0.1717 -0.0065 0.0086  0.0003  113 TYR   B C   
5653 O O   . TYR   B 113 ? 0.1332 0.1318 0.1625 -0.0073 0.0024  -0.0035 113 TYR   B O   
5654 C CB  . TYR   B 113 ? 0.1350 0.1228 0.1911 -0.0041 0.0122  0.0088  113 TYR   B CB  
5655 C CG  . TYR   B 113 ? 0.1376 0.1244 0.2016 -0.0060 0.0067  0.0071  113 TYR   B CG  
5656 C CD1 . TYR   B 113 ? 0.1415 0.1306 0.2088 -0.0018 0.0157  0.0156  113 TYR   B CD1 
5657 C CD2 . TYR   B 113 ? 0.1470 0.1269 0.1948 -0.0040 0.0034  0.0085  113 TYR   B CD2 
5658 C CE1 . TYR   B 113 ? 0.1397 0.1340 0.2155 -0.0050 0.0164  0.0112  113 TYR   B CE1 
5659 C CE2 . TYR   B 113 ? 0.1473 0.1215 0.2096 0.0006  0.0030  0.0126  113 TYR   B CE2 
5660 C CZ  . TYR   B 113 ? 0.1376 0.1279 0.2186 0.0031  0.0029  0.0144  113 TYR   B CZ  
5661 O OH  . TYR   B 113 ? 0.1441 0.1250 0.2458 0.0095  0.0126  0.0112  113 TYR   B OH  
5671 N N   . GLU   B 114 ? 0.1270 0.1209 0.1791 0.0008  0.0100  0.0077  114 GLU   B N   
5672 C CA  . GLU   B 114 ? 0.1274 0.1197 0.1771 0.0020  0.0030  -0.0034 114 GLU   B CA  
5673 C C   . GLU   B 114 ? 0.1294 0.1248 0.1710 0.0009  0.0093  0.0021  114 GLU   B C   
5674 O O   . GLU   B 114 ? 0.1344 0.1220 0.1781 0.0030  0.0032  0.0071  114 GLU   B O   
5675 C CB  . GLU   B 114 ? 0.1278 0.1313 0.2005 -0.0023 0.0103  0.0041  114 GLU   B CB  
5676 C CG  . GLU   B 114 ? 0.1350 0.1295 0.2003 -0.0016 0.0064  0.0070  114 GLU   B CG  
5677 C CD  . GLU   B 114 ? 0.1295 0.1311 0.2075 -0.0044 0.0032  0.0045  114 GLU   B CD  
5678 O OE1 . GLU   B 114 ? 0.1309 0.1479 0.1936 -0.0096 0.0161  0.0049  114 GLU   B OE1 
5679 O OE2 . GLU   B 114 ? 0.1372 0.1482 0.2262 -0.0167 0.0103  0.0104  114 GLU   B OE2 
5686 N N   . ASN   B 115 ? 0.1298 0.1201 0.1702 0.0023  0.0018  0.0054  115 ASN   B N   
5687 C CA  . ASN   B 115 ? 0.1351 0.1243 0.1573 -0.0055 -0.0064 0.0057  115 ASN   B CA  
5688 C C   . ASN   B 115 ? 0.1318 0.1203 0.1591 -0.0117 -0.0045 -0.0024 115 ASN   B C   
5689 O O   . ASN   B 115 ? 0.1388 0.1251 0.1649 -0.0097 -0.0034 0.0008  115 ASN   B O   
5690 C CB  . ASN   B 115 ? 0.1453 0.1364 0.1716 -0.0091 -0.0014 0.0027  115 ASN   B CB  
5691 C CG  . ASN   B 115 ? 0.1573 0.1418 0.1765 0.0042  -0.0032 -0.0010 115 ASN   B CG  
5692 O OD1 . ASN   B 115 ? 0.2031 0.1551 0.1888 0.0023  0.0121  -0.0105 115 ASN   B OD1 
5693 N ND2 . ASN   B 115 ? 0.1522 0.1531 0.1591 -0.0007 0.0034  0.0018  115 ASN   B ND2 
5700 N N   . PHE   B 116 ? 0.1326 0.1231 0.1499 -0.0054 -0.0002 0.0025  116 PHE   B N   
5701 C CA  . PHE   B 116 ? 0.1369 0.1279 0.1524 -0.0124 -0.0055 0.0009  116 PHE   B CA  
5702 C C   . PHE   B 116 ? 0.1349 0.1146 0.1612 -0.0057 -0.0101 0.0136  116 PHE   B C   
5703 O O   . PHE   B 116 ? 0.1381 0.1232 0.1708 -0.0041 -0.0092 0.0044  116 PHE   B O   
5704 C CB  . PHE   B 116 ? 0.1309 0.1191 0.1562 -0.0044 -0.0082 0.0112  116 PHE   B CB  
5705 C CG  . PHE   B 116 ? 0.1279 0.1226 0.1564 -0.0034 0.0020  0.0088  116 PHE   B CG  
5706 C CD1 . PHE   B 116 ? 0.1383 0.1287 0.1722 0.0025  -0.0066 0.0039  116 PHE   B CD1 
5707 C CD2 . PHE   B 116 ? 0.1271 0.1312 0.1565 -0.0002 0.0032  0.0024  116 PHE   B CD2 
5708 C CE1 . PHE   B 116 ? 0.1406 0.1341 0.1757 -0.0025 -0.0135 0.0030  116 PHE   B CE1 
5709 C CE2 . PHE   B 116 ? 0.1354 0.1319 0.1588 -0.0067 0.0017  0.0050  116 PHE   B CE2 
5710 C CZ  . PHE   B 116 ? 0.1346 0.1327 0.1675 -0.0053 -0.0040 0.0038  116 PHE   B CZ  
5720 N N   . ASN   B 117 ? 0.1304 0.1255 0.1691 -0.0066 -0.0130 0.0034  117 ASN   B N   
5721 C CA  . ASN   B 117 ? 0.1405 0.1278 0.1666 -0.0086 -0.0083 0.0034  117 ASN   B CA  
5722 C C   . ASN   B 117 ? 0.1455 0.1256 0.1940 -0.0026 -0.0115 0.0013  117 ASN   B C   
5723 O O   . ASN   B 117 ? 0.1490 0.1304 0.2087 -0.0050 -0.0246 0.0110  117 ASN   B O   
5724 C CB  . ASN   B 117 ? 0.1385 0.1278 0.1717 -0.0004 -0.0052 -0.0018 117 ASN   B CB  
5725 C CG  . ASN   B 117 ? 0.1365 0.1294 0.1869 0.0015  -0.0078 -0.0044 117 ASN   B CG  
5726 O OD1 . ASN   B 117 ? 0.1564 0.1282 0.2102 -0.0120 0.0057  -0.0069 117 ASN   B OD1 
5727 N ND2 . ASN   B 117 ? 0.1407 0.1290 0.1910 0.0012  -0.0059 -0.0004 117 ASN   B ND2 
5734 N N   . GLN   B 118 ? 0.1393 0.1161 0.1774 -0.0058 -0.0171 -0.0014 118 GLN   B N   
5735 C CA  . GLN   B 118 ? 0.1488 0.1228 0.1936 0.0030  -0.0172 0.0072  118 GLN   B CA  
5736 C C   . GLN   B 118 ? 0.1517 0.1210 0.1954 -0.0020 -0.0129 0.0021  118 GLN   B C   
5737 O O   . GLN   B 118 ? 0.1679 0.1242 0.2238 -0.0092 0.0015  0.0052  118 GLN   B O   
5738 C CB  . GLN   B 118 ? 0.1479 0.1307 0.2085 0.0012  -0.0144 -0.0019 118 GLN   B CB  
5739 C CG  . GLN   B 118 ? 0.1541 0.1327 0.1943 0.0080  0.0015  -0.0115 118 GLN   B CG  
5740 C CD  . GLN   B 118 ? 0.1616 0.1283 0.1971 0.0038  -0.0080 -0.0098 118 GLN   B CD  
5741 O OE1 . GLN   B 118 ? 0.1661 0.1281 0.2098 0.0027  0.0051  0.0056  118 GLN   B OE1 
5742 N NE2 . GLN   B 118 ? 0.1674 0.1320 0.1985 0.0009  -0.0165 -0.0028 118 GLN   B NE2 
5751 N N   . HIS   B 119 ? 0.1533 0.1227 0.1697 -0.0107 -0.0156 0.0103  119 HIS   B N   
5752 C CA  . HIS   B 119 ? 0.1593 0.1344 0.1543 -0.0068 -0.0180 0.0029  119 HIS   B CA  
5753 C C   . HIS   B 119 ? 0.1607 0.1310 0.1565 0.0005  -0.0274 0.0042  119 HIS   B C   
5754 O O   . HIS   B 119 ? 0.1673 0.1315 0.1763 -0.0193 -0.0202 0.0088  119 HIS   B O   
5755 C CB  . HIS   B 119 ? 0.1600 0.1535 0.1641 -0.0016 -0.0222 0.0049  119 HIS   B CB  
5756 C CG  . HIS   B 119 ? 0.1626 0.1753 0.1771 0.0021  -0.0366 -0.0099 119 HIS   B CG  
5757 N ND1 . HIS   B 119 ? 0.1743 0.1929 0.2102 0.0024  -0.0432 -0.0315 119 HIS   B ND1 
5758 C CD2 . HIS   B 119 ? 0.1803 0.1971 0.1873 0.0291  -0.0450 -0.0214 119 HIS   B CD2 
5759 C CE1 . HIS   B 119 ? 0.1933 0.2109 0.2282 0.0161  -0.0522 -0.0473 119 HIS   B CE1 
5760 N NE2 . HIS   B 119 ? 0.1978 0.2213 0.2149 0.0254  -0.0531 -0.0410 119 HIS   B NE2 
5768 N N   . GLU   B 120 ? 0.1821 0.1342 0.1578 -0.0049 -0.0373 0.0145  120 GLU   B N   
5769 C CA  . GLU   B 120 ? 0.2100 0.1537 0.1777 -0.0003 -0.0584 0.0228  120 GLU   B CA  
5770 C C   . GLU   B 120 ? 0.1876 0.1429 0.1669 -0.0127 -0.0417 0.0272  120 GLU   B C   
5771 O O   . GLU   B 120 ? 0.1824 0.1557 0.1709 -0.0108 -0.0338 0.0174  120 GLU   B O   
5772 C CB  . GLU   B 120 ? 0.2760 0.1893 0.2501 0.0186  -0.0955 0.0489  120 GLU   B CB  
5773 C CG  . GLU   B 120 ? 0.3393 0.2565 0.3550 0.0373  -0.1169 0.0775  120 GLU   B CG  
5774 C CD  . GLU   B 120 ? 0.4030 0.3538 0.4729 0.0393  -0.1187 0.0927  120 GLU   B CD  
5775 O OE1 . GLU   B 120 ? 0.4426 0.3883 0.5018 0.0325  -0.1148 0.1070  120 GLU   B OE1 
5776 O OE2 . GLU   B 120 ? 0.4223 0.4106 0.5209 0.0402  -0.1128 0.0789  120 GLU   B OE2 
5783 N N   . VAL   B 121 ? 0.1757 0.1342 0.1655 -0.0163 -0.0245 0.0179  121 VAL   B N   
5784 C CA  . VAL   B 121 ? 0.1673 0.1462 0.1466 -0.0178 -0.0233 0.0122  121 VAL   B CA  
5785 C C   . VAL   B 121 ? 0.1629 0.1403 0.1359 -0.0233 -0.0170 0.0124  121 VAL   B C   
5786 O O   . VAL   B 121 ? 0.1705 0.1337 0.1649 -0.0291 -0.0240 0.0085  121 VAL   B O   
5787 C CB  . VAL   B 121 ? 0.1888 0.1814 0.1533 -0.0068 -0.0243 0.0197  121 VAL   B CB  
5788 C CG1 . VAL   B 121 ? 0.1975 0.1972 0.1846 -0.0141 -0.0272 0.0173  121 VAL   B CG1 
5789 C CG2 . VAL   B 121 ? 0.2146 0.2058 0.1579 0.0053  -0.0174 -0.0023 121 VAL   B CG2 
5799 N N   . LEU   B 122 ? 0.1553 0.1339 0.1410 -0.0191 -0.0192 0.0107  122 LEU   B N   
5800 C CA  . LEU   B 122 ? 0.1505 0.1416 0.1191 -0.0166 -0.0199 0.0127  122 LEU   B CA  
5801 C C   . LEU   B 122 ? 0.1481 0.1325 0.1352 -0.0232 -0.0188 0.0071  122 LEU   B C   
5802 O O   . LEU   B 122 ? 0.1579 0.1323 0.1739 -0.0257 -0.0309 0.0021  122 LEU   B O   
5803 C CB  . LEU   B 122 ? 0.1733 0.1491 0.1726 -0.0040 -0.0318 0.0119  122 LEU   B CB  
5804 C CG  . LEU   B 122 ? 0.1594 0.1546 0.1820 -0.0109 -0.0129 0.0081  122 LEU   B CG  
5805 C CD1 . LEU   B 122 ? 0.1636 0.1772 0.1843 -0.0111 -0.0228 0.0066  122 LEU   B CD1 
5806 C CD2 . LEU   B 122 ? 0.1653 0.1585 0.1509 -0.0080 -0.0105 -0.0012 122 LEU   B CD2 
5818 N N   . LEU   B 123 ? 0.1472 0.1237 0.1316 -0.0217 -0.0138 0.0062  123 LEU   B N   
5819 C CA  . LEU   B 123 ? 0.1521 0.1247 0.1346 -0.0230 -0.0231 0.0030  123 LEU   B CA  
5820 C C   . LEU   B 123 ? 0.1492 0.1264 0.1343 -0.0225 -0.0186 -0.0026 123 LEU   B C   
5821 O O   . LEU   B 123 ? 0.1609 0.1281 0.1328 -0.0257 -0.0154 0.0017  123 LEU   B O   
5822 C CB  . LEU   B 123 ? 0.1593 0.1327 0.1396 -0.0221 -0.0153 -0.0017 123 LEU   B CB  
5823 C CG  . LEU   B 123 ? 0.1591 0.1340 0.1505 -0.0108 -0.0148 0.0142  123 LEU   B CG  
5824 C CD1 . LEU   B 123 ? 0.1745 0.1385 0.1619 -0.0136 -0.0023 0.0023  123 LEU   B CD1 
5825 C CD2 . LEU   B 123 ? 0.1615 0.1473 0.1675 -0.0185 -0.0083 0.0285  123 LEU   B CD2 
5837 N N   . ALA   B 124 ? 0.1468 0.1279 0.1309 -0.0214 -0.0110 -0.0024 124 ALA   B N   
5838 C CA  . ALA   B 124 ? 0.1357 0.1257 0.1454 -0.0184 -0.0153 -0.0086 124 ALA   B CA  
5839 C C   . ALA   B 124 ? 0.1342 0.1309 0.1399 -0.0134 -0.0022 -0.0025 124 ALA   B C   
5840 O O   . ALA   B 124 ? 0.1465 0.1320 0.1445 -0.0144 -0.0127 -0.0000 124 ALA   B O   
5841 C CB  . ALA   B 124 ? 0.1456 0.1296 0.1529 -0.0052 -0.0008 -0.0015 124 ALA   B CB  
5847 N N   . PRO   B 125 ? 0.1468 0.1313 0.1318 -0.0170 -0.0162 0.0078  125 PRO   B N   
5848 C CA  . PRO   B 125 ? 0.1525 0.1307 0.1608 -0.0166 -0.0146 0.0220  125 PRO   B CA  
5849 C C   . PRO   B 125 ? 0.1424 0.1244 0.1735 -0.0105 -0.0129 0.0120  125 PRO   B C   
5850 O O   . PRO   B 125 ? 0.1475 0.1263 0.1797 -0.0108 -0.0070 0.0136  125 PRO   B O   
5851 C CB  . PRO   B 125 ? 0.1532 0.1554 0.1735 -0.0209 -0.0243 0.0367  125 PRO   B CB  
5852 C CG  . PRO   B 125 ? 0.1601 0.1561 0.1564 -0.0302 -0.0245 0.0163  125 PRO   B CG  
5853 C CD  . PRO   B 125 ? 0.1561 0.1428 0.1420 -0.0279 -0.0160 0.0073  125 PRO   B CD  
5861 N N   . LEU   B 126 ? 0.1494 0.1225 0.1856 -0.0164 0.0053  0.0187  126 LEU   B N   
5862 C CA  . LEU   B 126 ? 0.1583 0.1318 0.1874 -0.0070 0.0136  0.0145  126 LEU   B CA  
5863 C C   . LEU   B 126 ? 0.1513 0.1434 0.1992 0.0010  0.0144  0.0197  126 LEU   B C   
5864 O O   . LEU   B 126 ? 0.1706 0.1709 0.2104 0.0182  -0.0043 -0.0001 126 LEU   B O   
5865 C CB  . LEU   B 126 ? 0.1820 0.1367 0.2206 -0.0193 0.0319  0.0129  126 LEU   B CB  
5866 C CG  . LEU   B 126 ? 0.1951 0.1480 0.2327 -0.0286 0.0206  -0.0178 126 LEU   B CG  
5867 C CD1 . LEU   B 126 ? 0.2093 0.1594 0.2816 -0.0264 0.0076  -0.0331 126 LEU   B CD1 
5868 C CD2 . LEU   B 126 ? 0.1931 0.1629 0.2222 -0.0375 0.0226  -0.0194 126 LEU   B CD2 
5880 N N   . LEU   B 127 ? 0.1506 0.1319 0.2070 0.0022  0.0213  0.0137  127 LEU   B N   
5881 C CA  . LEU   B 127 ? 0.1552 0.1400 0.2065 -0.0030 0.0229  0.0234  127 LEU   B CA  
5882 C C   . LEU   B 127 ? 0.1491 0.1372 0.2030 -0.0049 0.0161  0.0247  127 LEU   B C   
5883 O O   . LEU   B 127 ? 0.1512 0.1396 0.1976 -0.0093 0.0048  0.0229  127 LEU   B O   
5884 C CB  . LEU   B 127 ? 0.1703 0.1373 0.2054 -0.0016 0.0182  0.0215  127 LEU   B CB  
5885 C CG  . LEU   B 127 ? 0.1755 0.1389 0.2214 0.0035  0.0251  0.0160  127 LEU   B CG  
5886 C CD1 . LEU   B 127 ? 0.1739 0.1408 0.2313 0.0002  0.0172  0.0128  127 LEU   B CD1 
5887 C CD2 . LEU   B 127 ? 0.1740 0.1467 0.2433 -0.0091 0.0236  0.0326  127 LEU   B CD2 
5899 N N   . SER   B 128 ? 0.1501 0.1410 0.1979 -0.0001 -0.0009 0.0175  128 SER   B N   
5900 C CA  . SER   B 128 ? 0.1651 0.1468 0.1923 0.0098  -0.0093 0.0207  128 SER   B CA  
5901 C C   . SER   B 128 ? 0.1787 0.1498 0.2158 0.0074  -0.0199 0.0216  128 SER   B C   
5902 O O   . SER   B 128 ? 0.1899 0.1546 0.2402 0.0041  -0.0155 0.0375  128 SER   B O   
5903 C CB  . SER   B 128 ? 0.1787 0.1493 0.1966 0.0108  0.0028  0.0262  128 SER   B CB  
5904 O OG  . SER   B 128 ? 0.1788 0.1606 0.1989 0.0091  0.0046  0.0286  128 SER   B OG  
5910 N N   . ALA   B 129 ? 0.1914 0.1480 0.2404 0.0245  -0.0123 0.0071  129 ALA   B N   
5911 C CA  . ALA   B 129 ? 0.2026 0.1583 0.2473 0.0268  -0.0140 -0.0124 129 ALA   B CA  
5912 C C   . ALA   B 129 ? 0.1880 0.1501 0.2417 0.0200  -0.0020 -0.0026 129 ALA   B C   
5913 O O   . ALA   B 129 ? 0.1797 0.1543 0.2429 0.0184  -0.0039 0.0120  129 ALA   B O   
5914 C CB  . ALA   B 129 ? 0.2273 0.1835 0.2882 0.0315  0.0056  -0.0236 129 ALA   B CB  
5920 N N   . GLY   B 130 ? 0.1854 0.1532 0.2376 0.0186  -0.0040 0.0003  130 GLY   B N   
5921 C CA  . GLY   B 130 ? 0.1911 0.1676 0.2468 0.0127  0.0072  -0.0019 130 GLY   B CA  
5922 C C   . GLY   B 130 ? 0.1956 0.1720 0.2456 0.0137  0.0002  0.0080  130 GLY   B C   
5923 O O   . GLY   B 130 ? 0.2075 0.1788 0.2504 0.0167  0.0011  0.0171  130 GLY   B O   
5927 N N   . ILE   B 131 ? 0.1909 0.1840 0.2532 0.0272  0.0050  -0.0049 131 ILE   B N   
5928 C CA  . ILE   B 131 ? 0.2088 0.1963 0.2530 0.0279  -0.0090 0.0065  131 ILE   B CA  
5929 C C   . ILE   B 131 ? 0.2287 0.1871 0.2177 0.0207  -0.0136 0.0166  131 ILE   B C   
5930 O O   . ILE   B 131 ? 0.2606 0.2021 0.2321 0.0247  -0.0300 0.0177  131 ILE   B O   
5931 C CB  . ILE   B 131 ? 0.2018 0.2336 0.2970 0.0230  -0.0182 0.0162  131 ILE   B CB  
5932 C CG1 . ILE   B 131 ? 0.2050 0.2560 0.3242 -0.0039 -0.0127 0.0254  131 ILE   B CG1 
5933 C CG2 . ILE   B 131 ? 0.2048 0.2508 0.3282 0.0303  -0.0156 0.0156  131 ILE   B CG2 
5934 C CD1 . ILE   B 131 ? 0.2196 0.2740 0.3453 -0.0216 -0.0130 0.0344  131 ILE   B CD1 
5946 N N   . PHE   B 132 ? 0.2100 0.1654 0.2063 0.0188  0.0010  0.0221  132 PHE   B N   
5947 C CA  . PHE   B 132 ? 0.2181 0.1683 0.2033 0.0094  0.0238  0.0139  132 PHE   B CA  
5948 C C   . PHE   B 132 ? 0.2363 0.1836 0.2303 0.0100  0.0304  0.0113  132 PHE   B C   
5949 O O   . PHE   B 132 ? 0.2459 0.2050 0.2552 0.0070  0.0417  0.0240  132 PHE   B O   
5950 C CB  . PHE   B 132 ? 0.2068 0.1641 0.1868 0.0122  0.0214  0.0204  132 PHE   B CB  
5951 C CG  . PHE   B 132 ? 0.2036 0.1667 0.1957 0.0131  0.0172  0.0231  132 PHE   B CG  
5952 C CD1 . PHE   B 132 ? 0.2068 0.1645 0.2415 0.0114  0.0156  0.0191  132 PHE   B CD1 
5953 C CD2 . PHE   B 132 ? 0.2045 0.1711 0.1787 0.0211  0.0089  0.0253  132 PHE   B CD2 
5954 C CE1 . PHE   B 132 ? 0.2116 0.1684 0.2501 0.0053  0.0143  0.0211  132 PHE   B CE1 
5955 C CE2 . PHE   B 132 ? 0.2113 0.1716 0.1950 0.0174  0.0012  0.0208  132 PHE   B CE2 
5956 C CZ  . PHE   B 132 ? 0.2139 0.1714 0.2366 0.0076  0.0020  0.0280  132 PHE   B CZ  
5966 N N   . GLY   B 133 ? 0.2348 0.1767 0.2308 -0.0004 0.0150  0.0373  133 GLY   B N   
5967 C CA  . GLY   B 133 ? 0.2394 0.1908 0.2296 -0.0164 0.0103  0.0454  133 GLY   B CA  
5968 C C   . GLY   B 133 ? 0.2453 0.1977 0.2243 -0.0289 0.0141  0.0523  133 GLY   B C   
5969 O O   . GLY   B 133 ? 0.2682 0.2035 0.2651 -0.0416 0.0167  0.0578  133 GLY   B O   
5973 N N   . ALA   B 134 ? 0.2242 0.1952 0.2141 -0.0275 0.0082  0.0388  134 ALA   B N   
5974 C CA  . ALA   B 134 ? 0.2113 0.1924 0.2262 -0.0187 0.0248  0.0251  134 ALA   B CA  
5975 C C   . ALA   B 134 ? 0.2122 0.1813 0.2435 -0.0094 0.0288  0.0394  134 ALA   B C   
5976 O O   . ALA   B 134 ? 0.2172 0.1983 0.2556 0.0014  0.0254  0.0245  134 ALA   B O   
5977 C CB  . ALA   B 134 ? 0.2059 0.1980 0.2468 -0.0088 0.0177  0.0197  134 ALA   B CB  
5983 N N   . ASP   B 135 ? 0.2244 0.1760 0.2519 -0.0155 0.0147  0.0430  135 ASP   B N   
5984 C CA  . ASP   B 135 ? 0.2409 0.1702 0.2674 -0.0124 0.0011  0.0379  135 ASP   B CA  
5985 C C   . ASP   B 135 ? 0.2237 0.1563 0.2491 -0.0021 0.0043  0.0242  135 ASP   B C   
5986 O O   . ASP   B 135 ? 0.2189 0.1503 0.2596 -0.0003 0.0086  0.0264  135 ASP   B O   
5987 C CB  . ASP   B 135 ? 0.2735 0.1799 0.2930 -0.0376 0.0027  0.0363  135 ASP   B CB  
5988 C CG  . ASP   B 135 ? 0.3042 0.1833 0.3463 -0.0586 0.0016  0.0321  135 ASP   B CG  
5989 O OD1 . ASP   B 135 ? 0.3149 0.1637 0.3292 -0.0374 0.0009  0.0338  135 ASP   B OD1 
5990 O OD2 . ASP   B 135 ? 0.3313 0.2241 0.4014 -0.0747 -0.0118 0.0085  135 ASP   B OD2 
5995 N N   . PRO   B 136 ? 0.2211 0.1592 0.2533 0.0134  -0.0169 0.0211  136 PRO   B N   
5996 C CA  . PRO   B 136 ? 0.2040 0.1490 0.2547 0.0138  -0.0106 0.0147  136 PRO   B CA  
5997 C C   . PRO   B 136 ? 0.1843 0.1367 0.2644 0.0093  -0.0038 0.0059  136 PRO   B C   
5998 O O   . PRO   B 136 ? 0.1731 0.1380 0.2382 0.0091  -0.0010 0.0084  136 PRO   B O   
5999 C CB  . PRO   B 136 ? 0.2160 0.1714 0.2698 0.0246  -0.0215 0.0025  136 PRO   B CB  
6000 C CG  . PRO   B 136 ? 0.2348 0.1764 0.2924 0.0354  -0.0196 -0.0000 136 PRO   B CG  
6001 C CD  . PRO   B 136 ? 0.2358 0.1746 0.2656 0.0312  -0.0099 0.0054  136 PRO   B CD  
6009 N N   . ILE   B 137 ? 0.1965 0.1339 0.2862 0.0152  -0.0133 0.0078  137 ILE   B N   
6010 C CA  . ILE   B 137 ? 0.2055 0.1330 0.2877 0.0035  0.0001  0.0092  137 ILE   B CA  
6011 C C   . ILE   B 137 ? 0.1954 0.1375 0.2739 -0.0036 0.0185  0.0138  137 ILE   B C   
6012 O O   . ILE   B 137 ? 0.1821 0.1401 0.2587 -0.0039 0.0128  0.0120  137 ILE   B O   
6013 C CB  . ILE   B 137 ? 0.2371 0.1341 0.3388 -0.0047 -0.0048 0.0075  137 ILE   B CB  
6014 C CG1 . ILE   B 137 ? 0.2664 0.1575 0.3995 0.0032  -0.0020 -0.0049 137 ILE   B CG1 
6015 C CG2 . ILE   B 137 ? 0.2399 0.1387 0.3563 -0.0264 -0.0032 0.0068  137 ILE   B CG2 
6016 C CD1 . ILE   B 137 ? 0.2895 0.1810 0.4462 0.0205  0.0030  -0.0021 137 ILE   B CD1 
6028 N N   . HIS   B 138 ? 0.1998 0.1372 0.2702 -0.0000 0.0250  0.0150  138 HIS   B N   
6029 C CA  . HIS   B 138 ? 0.2071 0.1522 0.2635 -0.0067 0.0289  0.0197  138 HIS   B CA  
6030 C C   . HIS   B 138 ? 0.1871 0.1457 0.2518 -0.0074 0.0256  0.0294  138 HIS   B C   
6031 O O   . HIS   B 138 ? 0.1783 0.1464 0.2793 0.0023  0.0298  0.0352  138 HIS   B O   
6032 C CB  . HIS   B 138 ? 0.2268 0.1625 0.2836 -0.0152 0.0348  0.0128  138 HIS   B CB  
6033 C CG  . HIS   B 138 ? 0.2419 0.1820 0.2734 -0.0189 0.0488  0.0366  138 HIS   B CG  
6034 N ND1 . HIS   B 138 ? 0.2514 0.2017 0.3041 -0.0179 0.0736  0.0300  138 HIS   B ND1 
6035 C CD2 . HIS   B 138 ? 0.2517 0.1961 0.2667 -0.0173 0.0631  0.0379  138 HIS   B CD2 
6036 C CE1 . HIS   B 138 ? 0.2581 0.2063 0.3126 -0.0149 0.0866  0.0303  138 HIS   B CE1 
6037 N NE2 . HIS   B 138 ? 0.2618 0.1981 0.2762 -0.0074 0.0793  0.0260  138 HIS   B NE2 
6045 N N   . SER   B 139 ? 0.1826 0.1330 0.2484 0.0031  0.0155  0.0167  139 SER   B N   
6046 C CA  . SER   B 139 ? 0.1766 0.1281 0.2409 -0.0019 0.0170  0.0058  139 SER   B CA  
6047 C C   . SER   B 139 ? 0.1571 0.1187 0.2360 -0.0055 0.0120  0.0099  139 SER   B C   
6048 O O   . SER   B 139 ? 0.1616 0.1217 0.2314 -0.0013 0.0022  0.0100  139 SER   B O   
6049 C CB  . SER   B 139 ? 0.1852 0.1322 0.2487 -0.0026 0.0090  0.0051  139 SER   B CB  
6050 O OG  . SER   B 139 ? 0.1892 0.1274 0.2310 -0.0026 -0.0007 0.0091  139 SER   B OG  
6056 N N   . LEU   B 140 ? 0.1523 0.1119 0.2260 -0.0073 0.0142  0.0019  140 LEU   B N   
6057 C CA  . LEU   B 140 ? 0.1526 0.1169 0.2349 -0.0004 0.0070  0.0099  140 LEU   B CA  
6058 C C   . LEU   B 140 ? 0.1517 0.1239 0.2342 -0.0040 0.0051  -0.0002 140 LEU   B C   
6059 O O   . LEU   B 140 ? 0.1486 0.1308 0.2303 -0.0020 -0.0002 0.0082  140 LEU   B O   
6060 C CB  . LEU   B 140 ? 0.1512 0.1217 0.2451 -0.0114 0.0142  -0.0055 140 LEU   B CB  
6061 C CG  . LEU   B 140 ? 0.1632 0.1278 0.2292 -0.0149 0.0002  0.0084  140 LEU   B CG  
6062 C CD1 . LEU   B 140 ? 0.1723 0.1357 0.2492 -0.0152 -0.0001 0.0135  140 LEU   B CD1 
6063 C CD2 . LEU   B 140 ? 0.1795 0.1362 0.2431 -0.0164 -0.0061 -0.0043 140 LEU   B CD2 
6075 N N   . ARG   B 141 ? 0.1411 0.1249 0.2487 -0.0044 0.0090  0.0053  141 ARG   B N   
6076 C CA  . ARG   B 141 ? 0.1472 0.1246 0.2809 -0.0082 0.0259  0.0019  141 ARG   B CA  
6077 C C   . ARG   B 141 ? 0.1401 0.1310 0.2779 -0.0111 0.0180  -0.0052 141 ARG   B C   
6078 O O   . ARG   B 141 ? 0.1400 0.1296 0.2761 -0.0100 -0.0016 -0.0067 141 ARG   B O   
6079 C CB  . ARG   B 141 ? 0.1697 0.1385 0.3156 -0.0146 0.0467  0.0048  141 ARG   B CB  
6080 C CG  . ARG   B 141 ? 0.2090 0.1667 0.3461 -0.0215 0.0366  0.0040  141 ARG   B CG  
6081 C CD  . ARG   B 141 ? 0.2537 0.1908 0.3457 -0.0213 0.0161  -0.0177 141 ARG   B CD  
6082 N NE  . ARG   B 141 ? 0.2754 0.1892 0.3546 -0.0428 0.0286  -0.0290 141 ARG   B NE  
6083 C CZ  . ARG   B 141 ? 0.2870 0.1744 0.3355 -0.0383 0.0476  -0.0290 141 ARG   B CZ  
6084 N NH1 . ARG   B 141 ? 0.2964 0.1607 0.3184 -0.0374 0.0499  -0.0287 141 ARG   B NH1 
6085 N NH2 . ARG   B 141 ? 0.2955 0.1828 0.3487 -0.0182 0.0402  -0.0142 141 ARG   B NH2 
6099 N N   . VAL   B 142 ? 0.1471 0.1271 0.2593 -0.0065 0.0219  -0.0082 142 VAL   B N   
6100 C CA  . VAL   B 142 ? 0.1474 0.1262 0.2510 -0.0018 0.0220  -0.0078 142 VAL   B CA  
6101 C C   . VAL   B 142 ? 0.1428 0.1250 0.2494 0.0034  0.0140  -0.0045 142 VAL   B C   
6102 O O   . VAL   B 142 ? 0.1495 0.1226 0.2574 0.0048  0.0104  -0.0032 142 VAL   B O   
6103 C CB  . VAL   B 142 ? 0.1556 0.1357 0.2561 0.0033  0.0217  0.0110  142 VAL   B CB  
6104 C CG1 . VAL   B 142 ? 0.1569 0.1329 0.2562 0.0072  0.0161  0.0049  142 VAL   B CG1 
6105 C CG2 . VAL   B 142 ? 0.1722 0.1391 0.2517 0.0031  0.0245  0.0085  142 VAL   B CG2 
6115 N N   . CYS   B 143 ? 0.1379 0.1275 0.2320 0.0024  0.0076  0.0033  143 CYS   B N   
6116 C CA  . CYS   B 143 ? 0.1353 0.1243 0.2283 -0.0041 0.0040  -0.0013 143 CYS   B CA  
6117 C C   . CYS   B 143 ? 0.1299 0.1264 0.2287 -0.0073 0.0091  -0.0050 143 CYS   B C   
6118 O O   . CYS   B 143 ? 0.1363 0.1300 0.2285 -0.0023 -0.0040 -0.0040 143 CYS   B O   
6119 C CB  . CYS   B 143 ? 0.1423 0.1335 0.2370 -0.0060 0.0019  -0.0009 143 CYS   B CB  
6120 S SG  . CYS   B 143 ? 0.1448 0.1482 0.2289 -0.0045 0.0049  0.0067  143 CYS   B SG  
6126 N N   . VAL   B 144 ? 0.1427 0.1250 0.2435 -0.0063 0.0008  -0.0066 144 VAL   B N   
6127 C CA  . VAL   B 144 ? 0.1527 0.1351 0.2588 -0.0114 -0.0138 -0.0154 144 VAL   B CA  
6128 C C   . VAL   B 144 ? 0.1426 0.1371 0.2741 -0.0113 -0.0140 0.0055  144 VAL   B C   
6129 O O   . VAL   B 144 ? 0.1538 0.1610 0.2979 -0.0050 -0.0149 0.0263  144 VAL   B O   
6130 C CB  . VAL   B 144 ? 0.1818 0.1548 0.3187 -0.0077 -0.0241 -0.0344 144 VAL   B CB  
6131 C CG1 . VAL   B 144 ? 0.2059 0.1880 0.3690 0.0030  -0.0316 -0.0263 144 VAL   B CG1 
6132 C CG2 . VAL   B 144 ? 0.1936 0.1521 0.3054 0.0016  -0.0364 -0.0539 144 VAL   B CG2 
6142 N N   . ASP   B 145 ? 0.1432 0.1301 0.2923 -0.0044 -0.0127 -0.0072 145 ASP   B N   
6143 C CA  . ASP   B 145 ? 0.1425 0.1348 0.3075 -0.0058 0.0018  -0.0075 145 ASP   B CA  
6144 C C   . ASP   B 145 ? 0.1383 0.1396 0.2860 -0.0032 0.0036  -0.0065 145 ASP   B C   
6145 O O   . ASP   B 145 ? 0.1419 0.1550 0.3370 -0.0076 0.0124  -0.0269 145 ASP   B O   
6146 C CB  . ASP   B 145 ? 0.1582 0.1465 0.3542 -0.0190 0.0192  -0.0104 145 ASP   B CB  
6147 C CG  . ASP   B 145 ? 0.1692 0.1487 0.4058 -0.0236 0.0273  -0.0035 145 ASP   B CG  
6148 O OD1 . ASP   B 145 ? 0.1694 0.1518 0.4016 -0.0245 -0.0101 -0.0207 145 ASP   B OD1 
6149 O OD2 . ASP   B 145 ? 0.1972 0.1574 0.4469 -0.0262 0.0540  0.0135  145 ASP   B OD2 
6154 N N   . THR   B 146 ? 0.1317 0.1300 0.2433 -0.0103 -0.0025 0.0053  146 THR   B N   
6155 C CA  . THR   B 146 ? 0.1375 0.1291 0.2203 -0.0142 0.0060  -0.0028 146 THR   B CA  
6156 C C   . THR   B 146 ? 0.1350 0.1273 0.2220 -0.0050 -0.0073 0.0009  146 THR   B C   
6157 O O   . THR   B 146 ? 0.1419 0.1276 0.2317 -0.0044 0.0027  0.0006  146 THR   B O   
6158 C CB  . THR   B 146 ? 0.1447 0.1310 0.2389 -0.0062 0.0216  0.0011  146 THR   B CB  
6159 O OG1 . THR   B 146 ? 0.1500 0.1293 0.2338 -0.0041 0.0170  0.0123  146 THR   B OG1 
6160 C CG2 . THR   B 146 ? 0.1554 0.1336 0.2223 -0.0068 0.0171  -0.0051 146 THR   B CG2 
6168 N N   . VAL   B 147 ? 0.1362 0.1263 0.2153 -0.0026 0.0077  0.0059  147 VAL   B N   
6169 C CA  . VAL   B 147 ? 0.1446 0.1266 0.2052 -0.0095 -0.0020 -0.0035 147 VAL   B CA  
6170 C C   . VAL   B 147 ? 0.1429 0.1230 0.2184 -0.0162 -0.0117 -0.0067 147 VAL   B C   
6171 O O   . VAL   B 147 ? 0.1524 0.1359 0.2217 -0.0157 -0.0317 -0.0072 147 VAL   B O   
6172 C CB  . VAL   B 147 ? 0.1475 0.1409 0.1836 -0.0127 -0.0025 -0.0047 147 VAL   B CB  
6173 C CG1 . VAL   B 147 ? 0.1430 0.1553 0.1915 -0.0128 -0.0012 0.0010  147 VAL   B CG1 
6174 C CG2 . VAL   B 147 ? 0.1498 0.1402 0.1815 -0.0103 0.0032  0.0054  147 VAL   B CG2 
6184 N N   . ARG   B 148 ? 0.1450 0.1257 0.2110 -0.0123 -0.0227 -0.0142 148 ARG   B N   
6185 C CA  . ARG   B 148 ? 0.1477 0.1350 0.2159 -0.0100 -0.0292 -0.0101 148 ARG   B CA  
6186 C C   . ARG   B 148 ? 0.1505 0.1445 0.2038 -0.0129 -0.0350 -0.0046 148 ARG   B C   
6187 O O   . ARG   B 148 ? 0.1704 0.1746 0.2018 -0.0267 -0.0373 0.0011  148 ARG   B O   
6188 C CB  . ARG   B 148 ? 0.1525 0.1463 0.2169 -0.0013 -0.0322 -0.0151 148 ARG   B CB  
6189 C CG  . ARG   B 148 ? 0.1531 0.1588 0.2263 -0.0108 -0.0276 -0.0282 148 ARG   B CG  
6190 C CD  . ARG   B 148 ? 0.1549 0.1745 0.2368 0.0050  -0.0263 -0.0290 148 ARG   B CD  
6191 N NE  . ARG   B 148 ? 0.1638 0.1743 0.2195 0.0221  -0.0267 -0.0301 148 ARG   B NE  
6192 C CZ  . ARG   B 148 ? 0.1557 0.1677 0.1990 0.0181  -0.0202 -0.0178 148 ARG   B CZ  
6193 N NH1 . ARG   B 148 ? 0.1462 0.1774 0.2056 -0.0011 -0.0041 -0.0114 148 ARG   B NH1 
6194 N NH2 . ARG   B 148 ? 0.1760 0.1538 0.2127 0.0171  -0.0179 -0.0198 148 ARG   B NH2 
6208 N N   . THR   B 149 ? 0.1591 0.1354 0.2044 -0.0088 -0.0330 0.0087  149 THR   B N   
6209 C CA  . THR   B 149 ? 0.1619 0.1401 0.1882 -0.0109 -0.0311 0.0124  149 THR   B CA  
6210 C C   . THR   B 149 ? 0.1629 0.1370 0.1772 -0.0097 -0.0290 0.0030  149 THR   B C   
6211 O O   . THR   B 149 ? 0.1610 0.1373 0.1899 -0.0181 -0.0132 0.0037  149 THR   B O   
6212 C CB  . THR   B 149 ? 0.1637 0.1399 0.1897 -0.0146 -0.0308 0.0022  149 THR   B CB  
6213 O OG1 . THR   B 149 ? 0.1647 0.1476 0.1831 -0.0239 -0.0300 0.0009  149 THR   B OG1 
6214 C CG2 . THR   B 149 ? 0.1668 0.1511 0.1947 -0.0107 -0.0192 0.0034  149 THR   B CG2 
6222 N N   . ASN   B 150 ? 0.1709 0.1379 0.1657 -0.0192 -0.0318 -0.0020 150 ASN   B N   
6223 C CA  . ASN   B 150 ? 0.1732 0.1547 0.1659 -0.0222 -0.0283 -0.0098 150 ASN   B CA  
6224 C C   . ASN   B 150 ? 0.1664 0.1479 0.1659 -0.0182 -0.0259 -0.0023 150 ASN   B C   
6225 O O   . ASN   B 150 ? 0.1764 0.1430 0.1797 -0.0285 -0.0435 0.0020  150 ASN   B O   
6226 C CB  . ASN   B 150 ? 0.1928 0.1929 0.1840 -0.0206 -0.0361 0.0005  150 ASN   B CB  
6227 C CG  . ASN   B 150 ? 0.2147 0.2349 0.2149 -0.0181 -0.0453 0.0210  150 ASN   B CG  
6228 O OD1 . ASN   B 150 ? 0.2241 0.2480 0.2312 -0.0295 -0.0645 0.0162  150 ASN   B OD1 
6229 N ND2 . ASN   B 150 ? 0.2262 0.2555 0.2471 -0.0083 -0.0446 0.0688  150 ASN   B ND2 
6236 N N   . VAL   B 151 ? 0.1574 0.1431 0.1668 -0.0243 -0.0276 0.0025  151 VAL   B N   
6237 C CA  . VAL   B 151 ? 0.1621 0.1499 0.1692 -0.0229 -0.0337 0.0022  151 VAL   B CA  
6238 C C   . VAL   B 151 ? 0.1599 0.1374 0.1664 -0.0273 -0.0304 0.0017  151 VAL   B C   
6239 O O   . VAL   B 151 ? 0.1691 0.1495 0.1901 -0.0224 -0.0265 -0.0045 151 VAL   B O   
6240 C CB  . VAL   B 151 ? 0.1782 0.1623 0.1928 -0.0093 -0.0288 0.0134  151 VAL   B CB  
6241 C CG1 . VAL   B 151 ? 0.1882 0.1638 0.2236 -0.0188 -0.0141 0.0048  151 VAL   B CG1 
6242 C CG2 . VAL   B 151 ? 0.1880 0.1779 0.1745 0.0049  -0.0227 0.0209  151 VAL   B CG2 
6252 N N   . TYR   B 152 ? 0.1525 0.1299 0.1610 -0.0243 -0.0234 0.0016  152 TYR   B N   
6253 C CA  . TYR   B 152 ? 0.1635 0.1424 0.1421 -0.0265 -0.0200 -0.0048 152 TYR   B CA  
6254 C C   . TYR   B 152 ? 0.1627 0.1323 0.1300 -0.0214 -0.0139 -0.0104 152 TYR   B C   
6255 O O   . TYR   B 152 ? 0.1675 0.1366 0.1499 -0.0227 -0.0086 -0.0002 152 TYR   B O   
6256 C CB  . TYR   B 152 ? 0.1775 0.1578 0.1529 -0.0227 -0.0169 0.0089  152 TYR   B CB  
6257 C CG  . TYR   B 152 ? 0.1859 0.1709 0.1518 -0.0338 -0.0169 0.0103  152 TYR   B CG  
6258 C CD1 . TYR   B 152 ? 0.1965 0.1816 0.1457 -0.0285 -0.0264 0.0110  152 TYR   B CD1 
6259 C CD2 . TYR   B 152 ? 0.2022 0.1834 0.1445 -0.0348 -0.0075 0.0010  152 TYR   B CD2 
6260 C CE1 . TYR   B 152 ? 0.2110 0.1924 0.1620 -0.0249 -0.0288 0.0207  152 TYR   B CE1 
6261 C CE2 . TYR   B 152 ? 0.2141 0.2018 0.1720 -0.0337 -0.0201 0.0031  152 TYR   B CE2 
6262 C CZ  . TYR   B 152 ? 0.2177 0.2139 0.1533 -0.0320 -0.0487 0.0266  152 TYR   B CZ  
6263 O OH  . TYR   B 152 ? 0.2399 0.2517 0.2005 -0.0213 -0.0531 0.0393  152 TYR   B OH  
6273 N N   . LEU   B 153 ? 0.1659 0.1273 0.1462 -0.0253 -0.0181 -0.0054 153 LEU   B N   
6274 C CA  . LEU   B 153 ? 0.1675 0.1315 0.1422 -0.0193 -0.0078 -0.0070 153 LEU   B CA  
6275 C C   . LEU   B 153 ? 0.1639 0.1308 0.1503 -0.0214 -0.0096 -0.0118 153 LEU   B C   
6276 O O   . LEU   B 153 ? 0.1656 0.1476 0.1682 -0.0112 -0.0134 -0.0255 153 LEU   B O   
6277 C CB  . LEU   B 153 ? 0.1616 0.1263 0.1677 -0.0243 -0.0022 -0.0051 153 LEU   B CB  
6278 C CG  . LEU   B 153 ? 0.1625 0.1410 0.1963 -0.0210 0.0012  0.0026  153 LEU   B CG  
6279 C CD1 . LEU   B 153 ? 0.1625 0.1542 0.2054 -0.0271 0.0052  0.0119  153 LEU   B CD1 
6280 C CD2 . LEU   B 153 ? 0.1638 0.1529 0.1994 -0.0225 0.0068  0.0033  153 LEU   B CD2 
6292 N N   . ALA   B 154 ? 0.1564 0.1294 0.1584 -0.0067 -0.0148 -0.0075 154 ALA   B N   
6293 C CA  . ALA   B 154 ? 0.1659 0.1435 0.1913 -0.0020 -0.0229 -0.0152 154 ALA   B CA  
6294 C C   . ALA   B 154 ? 0.1763 0.1427 0.1976 0.0048  -0.0279 -0.0182 154 ALA   B C   
6295 O O   . ALA   B 154 ? 0.2054 0.1437 0.2054 0.0052  -0.0125 -0.0033 154 ALA   B O   
6296 C CB  . ALA   B 154 ? 0.1574 0.1600 0.2156 -0.0055 -0.0190 -0.0183 154 ALA   B CB  
6302 N N   . VAL   B 155 ? 0.1445 0.1326 0.2180 -0.0006 0.0032  -0.0141 155 VAL   B N   
6303 C CA  . VAL   B 155 ? 0.1442 0.1377 0.2259 0.0017  -0.0077 -0.0101 155 VAL   B CA  
6304 C C   . VAL   B 155 ? 0.1448 0.1400 0.2066 -0.0013 -0.0164 -0.0158 155 VAL   B C   
6305 O O   . VAL   B 155 ? 0.1605 0.1525 0.2468 -0.0015 -0.0153 -0.0323 155 VAL   B O   
6306 C CB  . VAL   B 155 ? 0.1486 0.1457 0.2626 -0.0036 -0.0153 0.0033  155 VAL   B CB  
6307 C CG1 . VAL   B 155 ? 0.1600 0.1466 0.2645 -0.0054 -0.0071 -0.0032 155 VAL   B CG1 
6308 C CG2 . VAL   B 155 ? 0.1454 0.1640 0.2810 -0.0116 -0.0076 0.0296  155 VAL   B CG2 
6318 N N   . PHE   B 156 ? 0.1361 0.1445 0.2219 0.0021  -0.0039 -0.0061 156 PHE   B N   
6319 C CA  . PHE   B 156 ? 0.1414 0.1487 0.2707 0.0105  -0.0055 -0.0026 156 PHE   B CA  
6320 C C   . PHE   B 156 ? 0.1392 0.1572 0.2982 0.0126  -0.0104 -0.0213 156 PHE   B C   
6321 O O   . PHE   B 156 ? 0.1603 0.1728 0.3272 0.0223  -0.0014 -0.0381 156 PHE   B O   
6322 C CB  . PHE   B 156 ? 0.1511 0.1484 0.2682 0.0050  -0.0137 -0.0068 156 PHE   B CB  
6323 C CG  . PHE   B 156 ? 0.1519 0.1645 0.2743 -0.0015 -0.0148 0.0122  156 PHE   B CG  
6324 C CD1 . PHE   B 156 ? 0.1528 0.1936 0.3095 0.0040  0.0013  0.0448  156 PHE   B CD1 
6325 C CD2 . PHE   B 156 ? 0.1535 0.1770 0.2770 0.0099  -0.0169 0.0269  156 PHE   B CD2 
6326 C CE1 . PHE   B 156 ? 0.1552 0.2102 0.3263 0.0010  0.0006  0.0501  156 PHE   B CE1 
6327 C CE2 . PHE   B 156 ? 0.1624 0.2022 0.2954 0.0120  -0.0141 0.0290  156 PHE   B CE2 
6328 C CZ  . PHE   B 156 ? 0.1576 0.2113 0.3224 0.0094  -0.0159 0.0408  156 PHE   B CZ  
6338 N N   . ASP   B 157 ? 0.1412 0.1500 0.3137 0.0130  -0.0327 -0.0087 157 ASP   B N   
6339 C CA  . ASP   B 157 ? 0.1533 0.1603 0.3518 0.0085  -0.0344 -0.0179 157 ASP   B CA  
6340 C C   . ASP   B 157 ? 0.1558 0.1543 0.3482 0.0039  -0.0237 -0.0485 157 ASP   B C   
6341 O O   . ASP   B 157 ? 0.1406 0.1582 0.3371 0.0063  -0.0249 -0.0340 157 ASP   B O   
6342 C CB  . ASP   B 157 ? 0.1757 0.1845 0.3701 0.0038  -0.0543 -0.0054 157 ASP   B CB  
6343 C CG  . ASP   B 157 ? 0.2207 0.2003 0.3990 -0.0001 -0.0382 -0.0089 157 ASP   B CG  
6344 O OD1 . ASP   B 157 ? 0.2261 0.1887 0.4113 0.0066  -0.0163 -0.0036 157 ASP   B OD1 
6345 O OD2 . ASP   B 157 ? 0.2666 0.2141 0.4163 -0.0035 -0.0362 -0.0105 157 ASP   B OD2 
6350 N N   . LYS   B 158 ? 0.1655 0.1792 0.3586 0.0049  -0.0063 -0.0779 158 LYS   B N   
6351 C CA  . LYS   B 158 ? 0.1818 0.2003 0.3737 -0.0000 0.0062  -0.0926 158 LYS   B CA  
6352 C C   . LYS   B 158 ? 0.1824 0.1830 0.3825 -0.0006 0.0025  -0.0849 158 LYS   B C   
6353 O O   . LYS   B 158 ? 0.1806 0.1820 0.3844 -0.0041 0.0024  -0.0884 158 LYS   B O   
6354 C CB  . LYS   B 158 ? 0.2025 0.2398 0.3723 0.0036  0.0055  -0.1159 158 LYS   B CB  
6355 C CG  . LYS   B 158 ? 0.2268 0.2760 0.3771 0.0093  0.0132  -0.1196 158 LYS   B CG  
6356 C CD  . LYS   B 158 ? 0.2483 0.3200 0.3945 0.0098  0.0318  -0.1154 158 LYS   B CD  
6357 C CE  . LYS   B 158 ? 0.2645 0.3627 0.4074 0.0128  0.0315  -0.1148 158 LYS   B CE  
6358 N NZ  . LYS   B 158 ? 0.2580 0.3743 0.4041 0.0102  0.0238  -0.1137 158 LYS   B NZ  
6372 N N   . ASN   B 159 ? 0.1845 0.1711 0.4011 0.0035  -0.0152 -0.0610 159 ASN   B N   
6373 C CA  . ASN   B 159 ? 0.1968 0.1666 0.4190 0.0182  -0.0254 -0.0515 159 ASN   B CA  
6374 C C   . ASN   B 159 ? 0.1757 0.1532 0.4008 0.0129  -0.0425 -0.0510 159 ASN   B C   
6375 O O   . ASN   B 159 ? 0.1731 0.1460 0.4214 0.0018  -0.0554 -0.0283 159 ASN   B O   
6376 C CB  . ASN   B 159 ? 0.2159 0.1803 0.4471 0.0267  -0.0302 -0.0489 159 ASN   B CB  
6377 C CG  . ASN   B 159 ? 0.2392 0.2085 0.4876 0.0259  -0.0469 -0.0572 159 ASN   B CG  
6378 O OD1 . ASN   B 159 ? 0.2452 0.2216 0.4830 0.0379  -0.0533 -0.0613 159 ASN   B OD1 
6379 N ND2 . ASN   B 159 ? 0.2477 0.2184 0.4937 0.0247  -0.0544 -0.0479 159 ASN   B ND2 
6386 N N   . LEU   B 160 ? 0.1583 0.1536 0.3789 0.0071  -0.0414 -0.0366 160 LEU   B N   
6387 C CA  . LEU   B 160 ? 0.1585 0.1569 0.3362 0.0114  -0.0339 -0.0209 160 LEU   B CA  
6388 C C   . LEU   B 160 ? 0.1529 0.1436 0.3188 0.0045  -0.0241 -0.0220 160 LEU   B C   
6389 O O   . LEU   B 160 ? 0.1440 0.1464 0.3116 -0.0014 -0.0249 -0.0216 160 LEU   B O   
6390 C CB  . LEU   B 160 ? 0.1613 0.1645 0.3227 0.0087  -0.0233 -0.0185 160 LEU   B CB  
6391 C CG  . LEU   B 160 ? 0.1589 0.1734 0.3076 0.0042  -0.0254 -0.0079 160 LEU   B CG  
6392 C CD1 . LEU   B 160 ? 0.1727 0.1900 0.3012 -0.0067 -0.0043 -0.0107 160 LEU   B CD1 
6393 C CD2 . LEU   B 160 ? 0.1654 0.1718 0.3109 0.0164  -0.0281 -0.0067 160 LEU   B CD2 
6405 N N   . TYR   B 161 ? 0.1536 0.1483 0.3293 -0.0072 -0.0023 -0.0285 161 TYR   B N   
6406 C CA  . TYR   B 161 ? 0.1640 0.1459 0.3103 -0.0160 0.0168  -0.0368 161 TYR   B CA  
6407 C C   . TYR   B 161 ? 0.1679 0.1493 0.3001 -0.0168 0.0169  -0.0359 161 TYR   B C   
6408 O O   . TYR   B 161 ? 0.1704 0.1545 0.2855 -0.0163 0.0039  -0.0311 161 TYR   B O   
6409 C CB  . TYR   B 161 ? 0.1791 0.1585 0.3269 -0.0242 0.0416  -0.0341 161 TYR   B CB  
6410 C CG  . TYR   B 161 ? 0.2011 0.1602 0.3215 -0.0264 0.0448  -0.0465 161 TYR   B CG  
6411 C CD1 . TYR   B 161 ? 0.2080 0.1578 0.3155 -0.0356 0.0458  -0.0447 161 TYR   B CD1 
6412 C CD2 . TYR   B 161 ? 0.2266 0.1707 0.3109 -0.0257 0.0288  -0.0618 161 TYR   B CD2 
6413 C CE1 . TYR   B 161 ? 0.2301 0.1707 0.3140 -0.0418 0.0425  -0.0408 161 TYR   B CE1 
6414 C CE2 . TYR   B 161 ? 0.2467 0.1879 0.3246 -0.0297 0.0323  -0.0605 161 TYR   B CE2 
6415 C CZ  . TYR   B 161 ? 0.2498 0.1888 0.3176 -0.0417 0.0319  -0.0466 161 TYR   B CZ  
6416 O OH  . TYR   B 161 ? 0.2811 0.2101 0.3281 -0.0394 0.0278  -0.0385 161 TYR   B OH  
6426 N N   . ASP   B 162 ? 0.1741 0.1490 0.3120 -0.0131 0.0023  -0.0512 162 ASP   B N   
6427 C CA  . ASP   B 162 ? 0.1829 0.1563 0.3181 -0.0069 -0.0041 -0.0446 162 ASP   B CA  
6428 C C   . ASP   B 162 ? 0.1716 0.1452 0.3148 -0.0065 -0.0137 -0.0291 162 ASP   B C   
6429 O O   . ASP   B 162 ? 0.1770 0.1514 0.3217 -0.0124 -0.0243 -0.0298 162 ASP   B O   
6430 C CB  . ASP   B 162 ? 0.2000 0.1743 0.3319 0.0020  -0.0052 -0.0711 162 ASP   B CB  
6431 C CG  . ASP   B 162 ? 0.2003 0.2070 0.3678 0.0103  -0.0067 -0.0856 162 ASP   B CG  
6432 O OD1 . ASP   B 162 ? 0.1985 0.2267 0.3474 0.0035  -0.0022 -0.0784 162 ASP   B OD1 
6433 O OD2 . ASP   B 162 ? 0.2065 0.2297 0.4041 0.0276  0.0017  -0.0899 162 ASP   B OD2 
6438 N N   A LYS   B 163 ? 0.1683 0.1313 0.2999 -0.0093 -0.0340 -0.0141 163 LYS   B N   
6439 N N   B LYS   B 163 ? 0.1744 0.1504 0.3082 -0.0085 -0.0212 -0.0149 163 LYS   B N   
6440 C CA  A LYS   B 163 ? 0.1779 0.1425 0.2959 -0.0157 -0.0328 0.0017  163 LYS   B CA  
6441 C CA  B LYS   B 163 ? 0.1860 0.1669 0.3077 -0.0124 -0.0217 -0.0020 163 LYS   B CA  
6442 C C   A LYS   B 163 ? 0.1544 0.1439 0.2823 -0.0167 -0.0303 0.0028  163 LYS   B C   
6443 C C   B LYS   B 163 ? 0.1630 0.1540 0.2880 -0.0151 -0.0229 0.0023  163 LYS   B C   
6444 O O   A LYS   B 163 ? 0.1496 0.1532 0.3058 -0.0225 -0.0263 -0.0030 163 LYS   B O   
6445 O O   B LYS   B 163 ? 0.1611 0.1589 0.3019 -0.0184 -0.0192 0.0040  163 LYS   B O   
6446 C CB  A LYS   B 163 ? 0.2139 0.1653 0.3339 -0.0187 -0.0283 0.0059  163 LYS   B CB  
6447 C CB  B LYS   B 163 ? 0.2216 0.2024 0.3390 -0.0130 -0.0198 0.0022  163 LYS   B CB  
6448 C CG  A LYS   B 163 ? 0.2761 0.2285 0.3890 -0.0228 -0.0148 0.0094  163 LYS   B CG  
6449 C CG  B LYS   B 163 ? 0.2636 0.2480 0.3797 -0.0144 -0.0144 0.0059  163 LYS   B CG  
6450 C CD  A LYS   B 163 ? 0.3417 0.2869 0.4418 -0.0297 -0.0080 0.0016  163 LYS   B CD  
6451 C CD  B LYS   B 163 ? 0.3011 0.2827 0.4203 -0.0176 -0.0108 0.0032  163 LYS   B CD  
6452 C CE  A LYS   B 163 ? 0.3967 0.3317 0.4674 -0.0314 0.0068  -0.0017 163 LYS   B CE  
6453 C CE  B LYS   B 163 ? 0.3345 0.3117 0.4457 -0.0200 -0.0021 0.0011  163 LYS   B CE  
6454 N NZ  A LYS   B 163 ? 0.4274 0.3581 0.4919 -0.0319 0.0128  -0.0111 163 LYS   B NZ  
6455 N NZ  B LYS   B 163 ? 0.3557 0.3422 0.4664 -0.0211 0.0022  -0.0038 163 LYS   B NZ  
6482 N N   . LEU   B 164 ? 0.1483 0.1386 0.2731 -0.0150 -0.0249 0.0026  164 LEU   B N   
6483 C CA  . LEU   B 164 ? 0.1499 0.1392 0.2628 -0.0115 -0.0273 -0.0011 164 LEU   B CA  
6484 C C   . LEU   B 164 ? 0.1512 0.1396 0.2590 -0.0178 -0.0329 0.0008  164 LEU   B C   
6485 O O   . LEU   B 164 ? 0.1529 0.1570 0.2837 -0.0169 -0.0345 -0.0040 164 LEU   B O   
6486 C CB  . LEU   B 164 ? 0.1426 0.1351 0.2402 -0.0091 -0.0225 -0.0002 164 LEU   B CB  
6487 C CG  . LEU   B 164 ? 0.1488 0.1510 0.2416 -0.0084 -0.0138 0.0051  164 LEU   B CG  
6488 C CD1 . LEU   B 164 ? 0.1543 0.1520 0.2467 -0.0161 -0.0275 -0.0017 164 LEU   B CD1 
6489 C CD2 . LEU   B 164 ? 0.1688 0.1891 0.2710 -0.0079 -0.0121 -0.0034 164 LEU   B CD2 
6502 N N   . VAL   B 165 ? 0.1770 0.1448 0.2800 -0.0165 -0.0365 -0.0010 165 VAL   B N   
6503 C CA  . VAL   B 165 ? 0.2119 0.1556 0.2782 -0.0283 -0.0513 -0.0032 165 VAL   B CA  
6504 C C   . VAL   B 165 ? 0.2388 0.1691 0.3003 -0.0360 -0.0787 -0.0035 165 VAL   B C   
6505 O O   . VAL   B 165 ? 0.2632 0.1792 0.3133 -0.0418 -0.0825 0.0097  165 VAL   B O   
6506 C CB  . VAL   B 165 ? 0.2351 0.1672 0.2929 -0.0158 -0.0231 -0.0110 165 VAL   B CB  
6507 C CG1 . VAL   B 165 ? 0.2566 0.1768 0.3230 -0.0201 -0.0108 -0.0143 165 VAL   B CG1 
6508 C CG2 . VAL   B 165 ? 0.2293 0.1722 0.2866 -0.0107 -0.0134 -0.0027 165 VAL   B CG2 
6518 N N   . SER   B 166 ? 0.2382 0.1598 0.3302 -0.0331 -0.0861 -0.0251 166 SER   B N   
6519 C CA  . SER   B 166 ? 0.2302 0.1677 0.3877 -0.0330 -0.0769 -0.0374 166 SER   B CA  
6520 C C   . SER   B 166 ? 0.2174 0.1763 0.4009 -0.0380 -0.0690 -0.0069 166 SER   B C   
6521 O O   . SER   B 166 ? 0.2223 0.1958 0.4300 -0.0491 -0.0677 -0.0276 166 SER   B O   
6522 C CB  . SER   B 166 ? 0.2298 0.1765 0.4109 -0.0277 -0.0712 -0.0569 166 SER   B CB  
6523 O OG  . SER   B 166 ? 0.2182 0.1761 0.4271 -0.0237 -0.0666 -0.0362 166 SER   B OG  
6529 N N   . SER   B 167 ? 0.2002 0.1688 0.3697 -0.0385 -0.0809 0.0372  167 SER   B N   
6530 C CA  . SER   B 167 ? 0.1952 0.1715 0.3533 -0.0373 -0.0582 0.0322  167 SER   B CA  
6531 C C   . SER   B 167 ? 0.1913 0.1795 0.3387 -0.0406 -0.0473 0.0467  167 SER   B C   
6532 O O   . SER   B 167 ? 0.1965 0.1895 0.3265 -0.0460 -0.0346 0.0451  167 SER   B O   
6533 C CB  . SER   B 167 ? 0.1905 0.1809 0.3531 -0.0292 -0.0250 0.0222  167 SER   B CB  
6534 O OG  . SER   B 167 ? 0.1880 0.1827 0.3502 -0.0233 -0.0119 0.0229  167 SER   B OG  
6540 N N   . PHE   B 168 ? 0.1876 0.1728 0.3304 -0.0387 -0.0432 0.0503  168 PHE   B N   
6541 C CA  . PHE   B 168 ? 0.1957 0.1704 0.3011 -0.0416 -0.0410 0.0296  168 PHE   B CA  
6542 C C   . PHE   B 168 ? 0.1788 0.1622 0.2696 -0.0188 -0.0091 0.0155  168 PHE   B C   
6543 O O   . PHE   B 168 ? 0.2105 0.1558 0.2579 0.0028  -0.0154 -0.0019 168 PHE   B O   
6544 C CB  . PHE   B 168 ? 0.2180 0.1786 0.3129 -0.0495 -0.0568 0.0437  168 PHE   B CB  
6545 C CG  . PHE   B 168 ? 0.2483 0.1619 0.3020 -0.0481 -0.0631 0.0193  168 PHE   B CG  
6546 C CD1 . PHE   B 168 ? 0.2832 0.1681 0.3162 -0.0387 -0.0643 0.0166  168 PHE   B CD1 
6547 C CD2 . PHE   B 168 ? 0.2413 0.1549 0.3012 -0.0372 -0.0582 0.0182  168 PHE   B CD2 
6548 C CE1 . PHE   B 168 ? 0.2996 0.1797 0.3140 -0.0264 -0.0580 0.0156  168 PHE   B CE1 
6549 C CE2 . PHE   B 168 ? 0.2672 0.1645 0.3005 -0.0232 -0.0595 0.0197  168 PHE   B CE2 
6550 C CZ  . PHE   B 168 ? 0.2878 0.1720 0.3071 -0.0188 -0.0588 0.0300  168 PHE   B CZ  
6560 N N   . LEU   B 169 ? 0.1782 0.1778 0.2577 -0.0007 0.0035  0.0078  169 LEU   B N   
6561 C CA  . LEU   B 169 ? 0.2040 0.2088 0.2828 -0.0070 0.0080  -0.0223 169 LEU   B CA  
6562 C C   . LEU   B 169 ? 0.2326 0.2344 0.3362 0.0079  -0.0002 -0.0480 169 LEU   B C   
6563 O O   . LEU   B 169 ? 0.2532 0.2581 0.3952 0.0087  -0.0076 -0.0761 169 LEU   B O   
6564 C CB  . LEU   B 169 ? 0.2194 0.2475 0.3095 -0.0084 0.0013  -0.0002 169 LEU   B CB  
6565 C CG  . LEU   B 169 ? 0.2537 0.2889 0.3575 0.0056  -0.0012 0.0075  169 LEU   B CG  
6566 C CD1 . LEU   B 169 ? 0.2664 0.3121 0.3578 0.0097  -0.0083 0.0307  169 LEU   B CD1 
6567 C CD2 . LEU   B 169 ? 0.2470 0.2959 0.3637 0.0159  0.0110  -0.0109 169 LEU   B CD2 
6568 O OXT . LEU   B 169 ? 0.2544 0.2474 0.3273 0.0334  0.0007  -0.0465 169 LEU   B OXT 
6580 C C1  T TFA   C .   ? 0.1091 0.1411 0.1159 0.0000  0.0188  0.0019  201 TFA   A C1  
6581 C C2  T TFA   C .   ? 0.1471 0.1738 0.1544 -0.0165 0.0082  -0.0095 201 TFA   A C2  
6582 O O   T TFA   C .   ? 0.0956 0.1267 0.1103 -0.0005 0.0199  0.0148  201 TFA   A O   
6583 F F1  T TFA   C .   ? 0.1610 0.1879 0.1579 -0.0218 -0.0010 -0.0262 201 TFA   A F1  
6584 F F2  T TFA   C .   ? 0.1596 0.1821 0.1586 -0.0199 0.0081  0.0091  201 TFA   A F2  
6585 F F3  T TFA   C .   ? 0.1611 0.1792 0.1660 -0.0247 0.0217  -0.0171 201 TFA   A F3  
6586 O OXT T TFA   C .   ? 0.1045 0.1360 0.1414 0.0266  0.0274  0.0128  201 TFA   A OXT 
6587 C C1  B TFA   D .   ? 0.1696 0.1463 0.0906 0.0089  0.0043  0.0331  202 TFA   A C1  
6588 C C2  B TFA   D .   ? 0.1712 0.1745 0.1602 0.0057  -0.0010 0.0218  202 TFA   A C2  
6589 O O   B TFA   D .   ? 0.1843 0.1151 0.1192 0.0256  -0.0374 0.0053  202 TFA   A O   
6590 F F1  B TFA   D .   ? 0.1754 0.1748 0.1900 0.0049  -0.0013 0.0167  202 TFA   A F1  
6591 F F2  B TFA   D .   ? 0.1660 0.1754 0.1822 0.0046  0.0071  0.0228  202 TFA   A F2  
6592 F F3  B TFA   D .   ? 0.1722 0.2008 0.1928 0.0110  -0.0289 0.0154  202 TFA   A F3  
6593 O OXT B TFA   D .   ? 0.1730 0.1558 0.1038 0.0091  0.0104  0.0243  202 TFA   A OXT 
6594 N N2  B A1A9L E .   ? 0.1443 0.1511 0.1805 0.0035  -0.0002 0.0252  203 A1A9L A N2  
6595 C C3  B A1A9L E .   ? 0.2005 0.1843 0.1790 0.0031  0.0227  0.0515  203 A1A9L A C3  
6596 C C6  B A1A9L E .   ? 0.2212 0.2085 0.1781 0.0043  0.0154  0.0591  203 A1A9L A C6  
6597 C C9  B A1A9L E .   ? 0.1431 0.1445 0.1795 0.0036  0.0033  0.0335  203 A1A9L A C9  
6598 C C12 B A1A9L E .   ? 0.1045 0.1493 0.1721 0.0117  -0.0016 0.0336  203 A1A9L A C12 
6599 C C1  B A1A9L E .   ? 0.1970 0.1828 0.1992 0.0115  0.0312  0.0246  203 A1A9L A C1  
6600 C C10 B A1A9L E .   ? 0.1207 0.1398 0.1780 0.0045  -0.0083 0.0380  203 A1A9L A C10 
6601 C C11 B A1A9L E .   ? 0.1191 0.1504 0.1723 0.0074  -0.0015 0.0384  203 A1A9L A C11 
6602 C C13 B A1A9L E .   ? 0.1055 0.1482 0.1827 -0.0019 -0.0090 0.0297  203 A1A9L A C13 
6603 C C2  B A1A9L E .   ? 0.1831 0.1743 0.1860 0.0053  0.0262  0.0351  203 A1A9L A C2  
6604 C C4  B A1A9L E .   ? 0.2126 0.1974 0.1832 0.0006  0.0210  0.0541  203 A1A9L A C4  
6605 C C5  B A1A9L E .   ? 0.2186 0.2065 0.1836 0.0003  0.0153  0.0593  203 A1A9L A C5  
6606 C C7  B A1A9L E .   ? 0.2177 0.2022 0.1784 0.0034  0.0241  0.0516  203 A1A9L A C7  
6607 C C8  B A1A9L E .   ? 0.1364 0.1550 0.1689 0.0092  0.0030  0.0300  203 A1A9L A C8  
6608 N N1  B A1A9L E .   ? 0.1506 0.1574 0.1634 0.0039  0.0181  0.0218  203 A1A9L A N1  
6609 N N3  B A1A9L E .   ? 0.1406 0.1429 0.1747 -0.0008 -0.0057 0.0419  203 A1A9L A N3  
6610 N N4  B A1A9L E .   ? 0.1092 0.1374 0.1764 -0.0009 -0.0148 0.0364  203 A1A9L A N4  
6611 O O1  B A1A9L E .   ? 0.2049 0.1880 0.2254 0.0108  0.0372  0.0112  203 A1A9L A O1  
6612 O O2  B A1A9L E .   ? 0.2226 0.2063 0.1958 0.0033  0.0213  0.0513  203 A1A9L A O2  
6631 O O   . HOH   F .   ? 0.2950 0.2552 0.4653 -0.0321 -0.1412 0.0982  301 HOH   A O   
6632 O O   . HOH   F .   ? 0.3331 0.3561 0.1737 -0.0464 0.0490  0.0426  302 HOH   A O   
6633 O O   . HOH   F .   ? 0.4160 0.3296 0.4206 -0.0023 0.1137  -0.0120 303 HOH   A O   
6634 O O   . HOH   F .   ? 0.4364 0.7731 0.5208 -0.1069 0.0904  0.0952  304 HOH   A O   
6635 O O   A HOH   F .   ? 0.2595 0.1847 0.3393 -0.0162 -0.0540 0.0220  305 HOH   A O   
6636 O O   . HOH   F .   ? 0.2595 0.5850 0.5519 0.0149  -0.0428 0.1677  306 HOH   A O   
6637 O O   . HOH   F .   ? 0.5458 0.4580 0.3181 0.1601  -0.1376 0.0294  307 HOH   A O   
6638 O O   . HOH   F .   ? 0.5312 0.5412 0.5251 -0.0991 0.0973  -0.0267 308 HOH   A O   
6639 O O   B HOH   F .   ? 0.2112 0.3126 0.2330 0.1280  0.0638  0.1194  309 HOH   A O   
6640 O O   . HOH   F .   ? 0.5675 0.6633 0.4116 -0.0908 -0.1235 -0.1050 310 HOH   A O   
6641 O O   . HOH   F .   ? 0.6019 0.4322 0.6210 0.0333  -0.0439 -0.0847 311 HOH   A O   
6642 O O   . HOH   F .   ? 0.5495 0.3020 0.4471 -0.0688 0.1341  0.0608  312 HOH   A O   
6643 O O   . HOH   F .   ? 0.2068 0.1940 0.3545 -0.0375 0.0039  -0.0149 313 HOH   A O   
6644 O O   B HOH   F .   ? 0.1879 0.2653 0.2000 -0.0719 0.0026  0.0099  314 HOH   A O   
6645 O O   . HOH   F .   ? 0.2486 0.4886 0.4575 -0.0457 -0.0738 0.1036  315 HOH   A O   
6646 O O   . HOH   F .   ? 0.3021 0.2948 0.2634 -0.0698 0.0111  0.0692  316 HOH   A O   
6647 O O   . HOH   F .   ? 0.5472 0.5378 0.4061 -0.0809 -0.0245 0.2200  317 HOH   A O   
6648 O O   . HOH   F .   ? 0.3657 0.3375 0.3597 -0.0876 0.1467  -0.0429 318 HOH   A O   
6649 O O   . HOH   F .   ? 0.5325 0.5166 0.4344 -0.0599 0.1256  0.2067  319 HOH   A O   
6650 O O   . HOH   F .   ? 0.4683 0.5403 0.5760 0.1730  0.1534  -0.1105 320 HOH   A O   
6651 O O   . HOH   F .   ? 0.5140 0.3511 0.5212 0.0441  0.2153  -0.0894 321 HOH   A O   
6652 O O   . HOH   F .   ? 0.2032 0.2517 0.3622 0.0233  0.0843  -0.0466 322 HOH   A O   
6653 O O   . HOH   F .   ? 0.4598 0.3000 0.3670 -0.0648 -0.1010 -0.0062 323 HOH   A O   
6654 O O   . HOH   F .   ? 0.2019 0.1812 0.2309 -0.0082 -0.0544 -0.0015 324 HOH   A O   
6655 O O   . HOH   F .   ? 0.1781 0.2192 0.1925 -0.0148 0.0086  0.0613  325 HOH   A O   
6656 O O   . HOH   F .   ? 0.6373 0.7259 0.5603 0.0246  -0.1258 -0.0777 326 HOH   A O   
6657 O O   . HOH   F .   ? 0.1990 0.2628 0.2888 0.0147  -0.0387 -0.0322 327 HOH   A O   
6658 O O   . HOH   F .   ? 0.4559 0.5260 0.2596 -0.1346 0.1067  0.0810  328 HOH   A O   
6659 O O   . HOH   F .   ? 0.2993 0.3038 0.3588 -0.0905 0.0092  -0.0378 329 HOH   A O   
6660 O O   . HOH   F .   ? 0.1986 0.3605 0.3566 -0.0342 0.0252  -0.1034 330 HOH   A O   
6661 O O   . HOH   F .   ? 0.7016 0.5581 0.3515 -0.0567 -0.0478 0.0999  331 HOH   A O   
6662 O O   . HOH   F .   ? 0.3424 0.4454 0.2724 0.0044  0.0412  0.0420  332 HOH   A O   
6663 O O   B HOH   F .   ? 0.1505 0.1959 0.1537 0.0109  -0.0315 0.0696  333 HOH   A O   
6664 O O   . HOH   F .   ? 0.1483 0.4291 0.2460 0.0068  0.0150  0.0798  334 HOH   A O   
6665 O O   . HOH   F .   ? 0.8285 0.4926 0.6095 -0.0212 -0.1393 0.1778  335 HOH   A O   
6666 O O   . HOH   F .   ? 0.1635 0.1594 0.2099 -0.0212 0.0084  0.0059  336 HOH   A O   
6667 O O   . HOH   F .   ? 0.5613 0.1919 0.4970 0.0549  0.0305  0.0138  337 HOH   A O   
6668 O O   . HOH   F .   ? 0.2167 0.4512 0.3919 -0.0215 -0.0299 0.1759  338 HOH   A O   
6669 O O   A HOH   F .   ? 0.1563 0.2086 0.1982 0.0341  0.0419  0.0490  339 HOH   A O   
6670 O O   . HOH   F .   ? 0.6200 0.4494 0.5477 0.0595  0.2448  -0.0828 340 HOH   A O   
6671 O O   . HOH   F .   ? 0.2742 0.2349 0.2540 0.0216  0.0411  0.0420  341 HOH   A O   
6672 O O   . HOH   F .   ? 0.6170 0.4655 0.4319 -0.1852 -0.0772 0.2226  342 HOH   A O   
6673 O O   A HOH   F .   ? 0.1953 0.4186 0.3720 -0.0200 0.0625  0.1751  343 HOH   A O   
6674 O O   B HOH   F .   ? 0.1159 0.2125 0.2852 -0.0346 -0.0376 0.0372  344 HOH   A O   
6675 O O   . HOH   F .   ? 0.2543 0.1933 0.2559 -0.0369 0.0139  0.0028  345 HOH   A O   
6676 O O   . HOH   F .   ? 0.1878 0.1713 0.2216 0.0153  -0.0208 0.0247  346 HOH   A O   
6677 O O   . HOH   F .   ? 0.5379 0.2213 0.4744 0.0370  -0.1436 0.0704  347 HOH   A O   
6678 O O   . HOH   F .   ? 0.2587 0.5963 0.5782 0.1391  0.0550  0.1006  348 HOH   A O   
6679 O O   . HOH   F .   ? 0.2160 0.1963 0.4259 0.0147  0.1128  -0.0148 349 HOH   A O   
6680 O O   . HOH   F .   ? 0.6695 0.3864 0.3207 0.0328  0.0315  0.1210  350 HOH   A O   
6681 O O   . HOH   F .   ? 0.2482 0.4074 0.3992 0.0978  -0.0769 -0.0340 351 HOH   A O   
6682 O O   . HOH   F .   ? 0.2525 0.4082 0.3171 -0.0504 0.0408  0.0363  352 HOH   A O   
6683 O O   . HOH   F .   ? 0.2478 0.1853 0.2330 0.0382  -0.0313 -0.0078 353 HOH   A O   
6684 O O   . HOH   F .   ? 0.1477 0.1545 0.1983 -0.0022 -0.0157 0.0061  354 HOH   A O   
6685 O O   . HOH   F .   ? 0.1410 0.1330 0.1331 -0.0013 0.0073  0.0038  355 HOH   A O   
6686 O O   . HOH   F .   ? 0.2946 0.3393 0.4202 -0.0987 -0.0990 -0.0250 356 HOH   A O   
6687 O O   B HOH   F .   ? 0.1501 0.2027 0.1655 0.0130  0.0210  0.0290  357 HOH   A O   
6688 O O   . HOH   F .   ? 0.3675 0.4385 0.3946 0.1673  0.0832  0.0902  358 HOH   A O   
6689 O O   . HOH   F .   ? 0.1646 0.1808 0.2157 0.0032  -0.0215 -0.0411 359 HOH   A O   
6690 O O   . HOH   F .   ? 0.3383 0.3512 0.4673 -0.0645 -0.0893 -0.0927 360 HOH   A O   
6691 O O   . HOH   F .   ? 0.3313 0.3513 0.2297 -0.0778 -0.0257 -0.0703 361 HOH   A O   
6692 O O   A HOH   F .   ? 0.2210 0.3351 0.2608 0.0610  0.0218  0.0071  362 HOH   A O   
6693 O O   . HOH   F .   ? 0.1554 0.2164 0.2332 -0.0034 -0.0058 0.0412  363 HOH   A O   
6694 O O   . HOH   F .   ? 0.1558 0.2066 0.2619 0.0025  -0.0156 0.0085  364 HOH   A O   
6695 O O   . HOH   F .   ? 0.3718 0.6708 0.4901 -0.0215 -0.1660 0.0491  365 HOH   A O   
6696 O O   . HOH   F .   ? 0.1531 0.1395 0.2345 -0.0106 0.0167  -0.0131 366 HOH   A O   
6697 O O   . HOH   F .   ? 0.1517 0.1652 0.1411 -0.0087 -0.0098 -0.0052 367 HOH   A O   
6698 O O   . HOH   F .   ? 0.3987 0.6437 0.5055 0.0100  0.1812  0.0296  368 HOH   A O   
6699 O O   . HOH   F .   ? 0.3562 0.6593 0.3906 -0.0422 -0.0046 0.1086  369 HOH   A O   
6700 O O   . HOH   F .   ? 0.4262 0.2389 0.4407 -0.1204 0.0972  0.0119  370 HOH   A O   
6701 O O   A HOH   F .   ? 0.2282 0.1889 0.2150 -0.0075 0.0028  -0.0185 371 HOH   A O   
6702 O O   . HOH   F .   ? 0.3942 0.2184 0.2228 0.1250  0.0586  0.0176  372 HOH   A O   
6703 O O   . HOH   F .   ? 0.2049 0.2349 0.2261 -0.0305 -0.0495 0.0399  373 HOH   A O   
6704 O O   . HOH   F .   ? 0.1767 0.1688 0.2277 -0.0140 0.0119  0.0257  374 HOH   A O   
6705 O O   . HOH   F .   ? 0.1943 0.2052 0.2319 -0.0355 -0.0016 0.0410  375 HOH   A O   
6706 O O   B HOH   F .   ? 0.3468 0.3021 0.2014 -0.0416 0.0434  0.0545  376 HOH   A O   
6707 O O   . HOH   F .   ? 0.1711 0.2657 0.2867 -0.0112 0.0560  0.0748  377 HOH   A O   
6708 O O   . HOH   F .   ? 0.4272 0.2459 0.4087 -0.1334 0.1337  -0.0365 378 HOH   A O   
6709 O O   . HOH   F .   ? 0.3269 0.2473 0.4592 -0.0612 0.0142  -0.0176 379 HOH   A O   
6710 O O   . HOH   F .   ? 0.5419 0.5180 0.6437 -0.0980 -0.0260 0.1449  380 HOH   A O   
6711 O O   . HOH   F .   ? 0.2126 0.2147 0.2732 -0.0121 -0.0395 0.0686  381 HOH   A O   
6712 O O   . HOH   F .   ? 0.2900 0.3096 0.3411 -0.0887 0.0968  -0.0247 382 HOH   A O   
6713 O O   A HOH   F .   ? 0.2024 0.2156 0.1944 -0.0388 0.0105  0.0684  383 HOH   A O   
6714 O O   B HOH   F .   ? 0.3886 0.3203 0.4257 -0.0733 0.0440  -0.0051 384 HOH   A O   
6715 O O   . HOH   F .   ? 0.2001 0.1965 0.1720 -0.0108 0.0053  0.0141  385 HOH   A O   
6716 O O   . HOH   F .   ? 0.3397 0.4405 0.3909 0.0182  0.0363  0.1425  386 HOH   A O   
6717 O O   . HOH   F .   ? 0.2999 0.3051 0.2035 0.0408  0.0713  0.0085  387 HOH   A O   
6718 O O   A HOH   F .   ? 0.3280 0.2616 0.2779 0.0862  0.0471  0.0895  388 HOH   A O   
6719 O O   . HOH   F .   ? 0.2811 0.5128 0.2822 0.0704  0.0708  0.1944  389 HOH   A O   
6720 O O   . HOH   F .   ? 0.2572 0.2010 0.1843 -0.0530 0.0203  0.0275  390 HOH   A O   
6721 O O   T HOH   F .   ? 0.0823 0.0927 0.2049 -0.0142 0.0207  0.0124  391 HOH   A O   
6722 O O   . HOH   F .   ? 0.3130 0.2725 0.3294 -0.0029 -0.0362 0.0868  392 HOH   A O   
6723 O O   . HOH   F .   ? 0.2539 0.1694 0.2528 -0.0095 0.0246  0.0171  393 HOH   A O   
6724 O O   . HOH   F .   ? 0.3695 0.6942 0.3973 0.1449  0.1061  -0.0359 394 HOH   A O   
6725 O O   B HOH   F .   ? 0.3457 0.5641 0.3616 0.0758  0.0438  -0.0124 395 HOH   A O   
6726 O O   . HOH   F .   ? 0.6362 0.6291 0.4402 0.2271  -0.0622 -0.0479 396 HOH   A O   
6727 O O   . HOH   F .   ? 0.2630 0.3671 0.4258 -0.0348 0.1247  -0.1073 397 HOH   A O   
6728 O O   . HOH   F .   ? 0.2387 0.2690 0.2943 -0.0015 -0.0130 -0.0462 398 HOH   A O   
6729 O O   . HOH   F .   ? 0.5044 0.3160 0.3031 -0.1285 0.0793  0.0436  399 HOH   A O   
6730 O O   B HOH   F .   ? 0.1595 0.1810 0.2047 0.0510  -0.0645 -0.0123 400 HOH   A O   
6731 O O   . HOH   F .   ? 0.2160 0.1699 0.2740 0.0010  -0.0220 0.0037  401 HOH   A O   
6732 O O   . HOH   F .   ? 0.1502 0.1691 0.2922 -0.0104 0.0006  0.0187  402 HOH   A O   
6733 O O   . HOH   F .   ? 0.2958 0.2949 0.2357 -0.0305 -0.0795 0.0411  403 HOH   A O   
6734 O O   . HOH   F .   ? 0.3717 0.6038 0.6018 0.0486  -0.0673 0.2273  404 HOH   A O   
6735 O O   . HOH   F .   ? 0.3315 0.2759 0.2070 -0.0700 -0.0900 0.0233  405 HOH   A O   
6736 O O   . HOH   F .   ? 0.5280 0.3850 0.1923 -0.0791 0.0879  0.0164  406 HOH   A O   
6737 O O   B HOH   F .   ? 0.2730 0.1349 0.2302 -0.0620 -0.0102 -0.0168 407 HOH   A O   
6738 O O   . HOH   F .   ? 0.1890 0.1973 0.3918 0.0327  0.1047  0.1057  408 HOH   A O   
6739 O O   . HOH   F .   ? 0.1967 0.2542 0.3544 -0.0014 -0.0307 0.0189  409 HOH   A O   
6740 O O   . HOH   F .   ? 0.2171 0.2143 0.2523 -0.0140 -0.0320 0.0262  410 HOH   A O   
6741 O O   . HOH   F .   ? 0.5556 0.2613 0.4758 0.0857  -0.0684 -0.0622 411 HOH   A O   
6742 O O   . HOH   F .   ? 0.3079 0.3908 0.7261 -0.0363 0.1500  -0.0469 412 HOH   A O   
6743 O O   . HOH   F .   ? 0.1923 0.1432 0.1604 -0.0246 0.0141  0.0014  413 HOH   A O   
6744 O O   . HOH   F .   ? 0.2766 0.6056 0.1859 -0.0618 0.0531  0.0270  414 HOH   A O   
6745 O O   A HOH   F .   ? 0.2244 0.1998 0.3510 -0.0236 0.0470  -0.0206 415 HOH   A O   
6746 O O   A HOH   F .   ? 0.1365 0.1545 0.1583 0.0075  -0.0360 -0.0002 416 HOH   A O   
6747 O O   . HOH   F .   ? 0.2548 0.2088 0.2780 -0.0586 -0.0017 0.0571  417 HOH   A O   
6748 O O   . HOH   F .   ? 0.7004 0.6116 0.4959 -0.1536 0.0004  0.2635  418 HOH   A O   
6749 O O   . HOH   F .   ? 0.4642 0.5017 0.4107 0.1645  -0.1223 -0.1434 419 HOH   A O   
6750 O O   A HOH   F .   ? 0.1262 0.1535 0.1602 0.0092  -0.0264 -0.0399 420 HOH   A O   
6751 O O   A HOH   F .   ? 0.2041 0.1921 0.2088 0.0053  -0.0058 0.0567  421 HOH   A O   
6752 O O   . HOH   F .   ? 0.3395 0.3443 0.5270 -0.0331 0.1001  -0.0395 422 HOH   A O   
6753 O O   . HOH   F .   ? 0.2160 0.2885 0.2477 -0.0037 -0.0533 0.0388  423 HOH   A O   
6754 O O   . HOH   F .   ? 0.1688 0.2021 0.2751 -0.0073 0.0053  0.0358  424 HOH   A O   
6755 O O   . HOH   F .   ? 0.2115 0.1764 0.1477 -0.0054 0.0229  0.0196  425 HOH   A O   
6756 O O   . HOH   F .   ? 0.3274 0.1431 0.2062 -0.0063 -0.0437 0.0107  426 HOH   A O   
6757 O O   A HOH   F .   ? 0.2280 0.2170 0.2473 0.0319  -0.0795 0.0432  427 HOH   A O   
6758 O O   . HOH   F .   ? 0.6305 0.4222 0.4375 0.1830  -0.0651 0.1321  428 HOH   A O   
6759 O O   . HOH   F .   ? 0.2298 0.2376 0.3100 -0.0205 -0.0077 -0.0136 429 HOH   A O   
6760 O O   . HOH   F .   ? 0.2428 0.4150 0.2462 0.1520  -0.0188 0.0259  430 HOH   A O   
6761 O O   . HOH   F .   ? 0.5703 0.5836 0.5693 -0.1083 -0.1187 -0.1166 431 HOH   A O   
6762 O O   . HOH   F .   ? 0.4631 0.2376 0.5170 -0.1006 -0.2352 0.1146  432 HOH   A O   
6763 O O   . HOH   F .   ? 0.4292 0.6014 0.3389 -0.0803 -0.0223 0.1002  433 HOH   A O   
6764 O O   . HOH   F .   ? 0.5226 0.6522 0.4299 0.0047  0.0822  0.0851  434 HOH   A O   
6765 O O   A HOH   F .   ? 0.2330 0.2465 0.2678 -0.0341 0.0974  -0.0240 435 HOH   A O   
6766 O O   . HOH   F .   ? 0.6200 0.7058 0.4765 0.0979  0.2976  -0.0582 436 HOH   A O   
6767 O O   B HOH   F .   ? 0.2754 0.2672 0.3891 -0.0298 0.0339  0.0070  437 HOH   A O   
6768 O O   . HOH   F .   ? 0.7004 0.7318 0.6460 0.0972  -0.1071 0.0454  438 HOH   A O   
6769 O O   . HOH   F .   ? 0.3255 0.2634 0.2511 -0.0265 -0.0405 0.0250  439 HOH   A O   
6770 O O   B HOH   F .   ? 0.3393 0.3107 0.3978 0.0209  -0.0406 -0.0762 440 HOH   A O   
6771 O O   A HOH   F .   ? 0.2106 0.1482 0.2517 0.0584  -0.0810 -0.0698 441 HOH   A O   
6772 O O   . HOH   F .   ? 0.1899 0.2042 0.5159 -0.0166 -0.0671 0.0501  442 HOH   A O   
6773 O O   . HOH   F .   ? 0.3362 0.2600 0.1805 -0.0500 0.0226  0.0244  443 HOH   A O   
6774 O O   . HOH   F .   ? 0.5142 0.4863 0.4777 0.1301  0.1141  -0.0737 444 HOH   A O   
6775 O O   . HOH   F .   ? 0.5518 0.6724 0.6002 -0.1540 -0.0878 -0.1318 445 HOH   A O   
6776 O O   . HOH   F .   ? 0.4583 0.4229 0.4930 -0.0733 -0.1104 -0.1227 446 HOH   A O   
6777 O O   . HOH   F .   ? 0.6135 0.5078 0.7678 0.0610  -0.1167 0.1912  447 HOH   A O   
6778 O O   . HOH   F .   ? 0.6405 0.7703 0.4338 0.1737  -0.1166 0.1972  448 HOH   A O   
6779 O O   . HOH   F .   ? 0.2561 0.1669 0.2738 -0.0066 0.0023  0.0166  449 HOH   A O   
6780 O O   . HOH   F .   ? 0.3223 0.2933 0.2986 0.1466  -0.0443 -0.0353 450 HOH   A O   
6781 O O   . HOH   F .   ? 0.5964 0.4570 0.4550 0.0110  -0.1571 0.0221  451 HOH   A O   
6782 O O   A HOH   F .   ? 0.3533 0.2743 0.4091 0.0776  0.1037  0.0004  452 HOH   A O   
6783 O O   . HOH   F .   ? 0.2623 0.2095 0.2542 0.0144  0.0205  0.0311  453 HOH   A O   
6784 O O   A HOH   F .   ? 0.6703 0.3363 0.3771 0.0379  0.1467  0.1015  454 HOH   A O   
6785 O O   . HOH   F .   ? 0.7965 0.8903 0.5998 -0.0634 0.0266  -0.0559 455 HOH   A O   
6786 O O   B HOH   F .   ? 0.1526 0.1769 0.3270 0.0123  -0.0547 -0.0722 456 HOH   A O   
6787 O O   A HOH   F .   ? 0.1657 0.1389 0.1648 0.0003  -0.0129 -0.0243 457 HOH   A O   
6788 O O   . HOH   F .   ? 0.2241 0.2815 0.2541 -0.0031 -0.0103 -0.0483 458 HOH   A O   
6789 O O   B HOH   F .   ? 0.3529 0.2780 0.3738 -0.1183 -0.0823 0.0802  459 HOH   A O   
6790 O O   A HOH   F .   ? 0.2793 0.3677 0.4507 -0.0236 0.1277  -0.1413 460 HOH   A O   
6791 O O   A HOH   F .   ? 0.4264 0.5308 0.5023 0.0608  0.0561  0.2156  461 HOH   A O   
6792 O O   . HOH   F .   ? 0.5242 0.3312 0.4720 0.0756  -0.0038 0.1533  462 HOH   A O   
6793 O O   B HOH   F .   ? 0.2450 0.5535 0.2246 -0.0403 -0.0217 0.0035  463 HOH   A O   
6794 O O   . HOH   F .   ? 0.4815 0.4815 0.4931 0.1155  0.0091  0.1379  464 HOH   A O   
6795 O O   . HOH   F .   ? 0.4855 0.3663 0.5420 0.0215  0.0168  0.0478  465 HOH   A O   
6796 O O   . HOH   F .   ? 0.2696 0.3564 0.4728 0.0689  -0.0376 0.1046  466 HOH   A O   
6797 O O   . HOH   F .   ? 0.5652 0.5762 0.4389 -0.0396 0.0365  0.1313  467 HOH   A O   
6798 O O   . HOH   F .   ? 0.7074 0.7602 0.4669 0.0612  0.0092  -0.0561 468 HOH   A O   
6799 O O   . HOH   F .   ? 0.2536 0.2690 0.3710 -0.0328 0.0319  -0.0795 469 HOH   A O   
6800 O O   B HOH   F .   ? 0.3243 0.1212 0.3330 0.0380  0.0834  0.0491  470 HOH   A O   
6801 O O   . HOH   F .   ? 0.3130 0.4752 0.5288 -0.1366 0.0771  -0.1855 471 HOH   A O   
6802 O O   . HOH   F .   ? 0.3486 0.5203 0.5474 0.0779  -0.0796 0.1532  472 HOH   A O   
6803 O O   . HOH   F .   ? 0.3307 0.4311 0.4787 -0.0610 0.0052  -0.0514 473 HOH   A O   
6804 O O   . HOH   F .   ? 0.2679 0.4588 0.4936 0.0699  0.0189  -0.1900 474 HOH   A O   
6805 O O   . HOH   F .   ? 0.2456 0.2729 0.3437 -0.0779 0.0521  -0.0149 475 HOH   A O   
6806 O O   . HOH   F .   ? 0.6435 0.3394 0.6856 0.0879  0.0584  0.2357  476 HOH   A O   
6807 O O   . HOH   F .   ? 0.2725 0.1970 0.2626 0.0340  -0.0767 -0.0301 477 HOH   A O   
6808 O O   A HOH   F .   ? 0.2755 0.2566 0.4951 0.0296  -0.1566 -0.0484 478 HOH   A O   
6809 O O   . HOH   F .   ? 0.4012 0.6414 0.4183 -0.0571 -0.0643 0.2369  479 HOH   A O   
6810 O O   . HOH   F .   ? 0.5878 0.5378 0.4766 0.0779  0.1481  0.0706  480 HOH   A O   
6811 O O   . HOH   F .   ? 0.7326 0.5125 0.6393 0.0791  0.0692  0.1755  481 HOH   A O   
6812 O O   B HOH   F .   ? 0.2903 0.2857 0.3559 0.1174  -0.0109 0.0071  482 HOH   A O   
6813 O O   B HOH   F .   ? 0.3738 0.2700 0.2295 0.1157  -0.0366 -0.0271 483 HOH   A O   
6814 O O   . HOH   F .   ? 0.4014 0.4690 0.3390 -0.0681 -0.0073 -0.0373 484 HOH   A O   
6815 O O   . HOH   F .   ? 0.4029 0.4672 0.2872 -0.0413 0.0039  -0.0336 485 HOH   A O   
6816 O O   . HOH   F .   ? 0.4093 0.5483 0.3893 0.0210  -0.0028 -0.0596 486 HOH   A O   
6817 O O   . HOH   F .   ? 0.4865 0.5168 0.4640 0.1115  -0.0457 -0.0793 487 HOH   A O   
6818 O O   . HOH   F .   ? 0.3411 0.2487 0.4590 0.0276  0.1223  0.0207  488 HOH   A O   
6819 O O   . HOH   F .   ? 0.2477 0.2237 0.2615 0.0370  -0.0027 -0.0017 489 HOH   A O   
6820 O O   . HOH   F .   ? 0.5468 0.5766 0.6785 -0.1746 -0.1230 -0.0339 490 HOH   A O   
6821 O O   . HOH   F .   ? 0.4311 0.2742 0.3753 -0.0596 -0.1763 0.0301  491 HOH   A O   
6822 O O   . HOH   F .   ? 0.4427 0.4960 0.5010 -0.2027 -0.0447 -0.0270 492 HOH   A O   
6823 O O   . HOH   F .   ? 0.6561 0.5344 0.7210 -0.0670 0.0734  -0.0587 493 HOH   A O   
6824 O O   . HOH   F .   ? 0.8034 0.3886 0.3456 -0.0358 -0.1321 0.0324  494 HOH   A O   
6825 O O   . HOH   F .   ? 0.5379 0.3734 0.2795 -0.1615 0.1742  -0.0634 495 HOH   A O   
6826 O O   . HOH   F .   ? 0.5823 0.4517 0.4574 0.0027  -0.0226 -0.1229 496 HOH   A O   
6827 O O   . HOH   F .   ? 0.4156 0.4278 0.4804 -0.0451 0.1762  0.0991  497 HOH   A O   
6828 O O   . HOH   F .   ? 0.5935 0.6534 0.4362 -0.1059 0.1265  0.0844  498 HOH   A O   
6829 O O   . HOH   F .   ? 0.3018 0.5821 0.4283 0.1520  0.1350  0.2562  499 HOH   A O   
6830 O O   . HOH   F .   ? 0.4653 0.6009 0.6333 0.0931  0.1014  -0.1129 500 HOH   A O   
6831 O O   . HOH   F .   ? 0.5694 0.3929 0.4120 0.0086  0.1529  0.0116  501 HOH   A O   
6832 O O   B HOH   F .   ? 0.5740 0.2984 0.4255 -0.0799 0.2022  -0.0207 502 HOH   A O   
6833 O O   . HOH   F .   ? 0.2578 0.2497 0.6995 -0.0056 -0.1222 0.0342  503 HOH   A O   
6834 O O   . HOH   F .   ? 0.5324 0.5256 0.4963 0.0454  -0.0635 0.0362  504 HOH   A O   
6835 O O   . HOH   F .   ? 0.5693 0.5283 0.4120 -0.0641 -0.1163 -0.0472 505 HOH   A O   
6836 O O   . HOH   F .   ? 0.4582 0.3821 0.5057 -0.0115 0.2434  0.0536  506 HOH   A O   
6837 O O   . HOH   F .   ? 0.2688 0.2112 0.6028 0.0022  0.0337  0.0983  507 HOH   A O   
6838 O O   . HOH   F .   ? 0.4107 0.2835 0.4451 -0.0886 0.0010  0.1033  508 HOH   A O   
6839 O O   . HOH   F .   ? 0.2448 0.2924 0.4746 -0.0112 0.0792  -0.0700 509 HOH   A O   
6840 O O   . HOH   F .   ? 0.3815 0.8545 0.5404 -0.1106 -0.0306 0.2418  510 HOH   A O   
6841 O O   . HOH   F .   ? 0.2950 0.4022 0.3590 0.1105  -0.0618 0.0717  511 HOH   A O   
6842 O O   . HOH   F .   ? 0.4789 0.2436 0.4336 -0.1216 0.0256  -0.0061 512 HOH   A O   
6843 O O   . HOH   F .   ? 0.2717 0.4463 0.4676 0.0851  -0.0592 -0.0118 513 HOH   A O   
6844 O O   . HOH   F .   ? 0.6858 0.2555 0.4195 -0.0846 0.0022  0.0463  514 HOH   A O   
6845 O O   . HOH   F .   ? 0.5531 0.2993 0.4232 0.0987  -0.0255 0.0621  515 HOH   A O   
6846 O O   . HOH   F .   ? 0.5482 0.6474 0.4736 0.0970  -0.0713 0.0033  516 HOH   A O   
6847 O O   B HOH   F .   ? 0.1611 0.3245 0.2688 0.0754  0.0418  0.0814  517 HOH   A O   
6848 O O   . HOH   F .   ? 0.4682 0.5085 0.4169 0.0165  -0.1540 0.0510  518 HOH   A O   
6849 O O   . HOH   F .   ? 0.3156 0.4282 0.2984 -0.0264 -0.0292 -0.0987 519 HOH   A O   
6850 O O   . HOH   F .   ? 0.5311 0.6847 0.4505 0.3274  0.0177  0.1173  520 HOH   A O   
6851 O O   . HOH   F .   ? 0.2726 0.7017 0.4935 0.0273  0.0625  -0.0545 521 HOH   A O   
6852 O O   . HOH   F .   ? 0.2818 0.2309 0.4888 0.0308  0.0566  0.0804  522 HOH   A O   
6853 O O   B HOH   F .   ? 0.2399 0.1827 0.3001 -0.0384 -0.0768 0.0770  523 HOH   A O   
6854 O O   B HOH   F .   ? 0.2862 0.1737 0.2687 0.0389  -0.0387 0.0506  524 HOH   A O   
6855 O O   A HOH   F .   ? 0.5313 0.7171 0.4748 0.1770  0.0871  -0.0406 525 HOH   A O   
6856 O O   T HOH   F .   ? 0.0839 0.0868 0.1698 -0.0344 -0.0340 0.0330  526 HOH   A O   
6857 O O   . HOH   F .   ? 0.4567 0.5394 0.3937 -0.0509 -0.0353 -0.1291 527 HOH   A O   
6858 O O   B HOH   F .   ? 0.2530 0.3672 0.2035 0.0570  -0.0247 0.0119  528 HOH   A O   
6859 O O   . HOH   F .   ? 0.4220 0.4637 0.4905 0.1065  0.0582  0.1016  529 HOH   A O   
6860 O O   . HOH   F .   ? 0.4586 0.6782 0.5447 -0.0710 -0.0432 -0.0007 530 HOH   A O   
6861 O O   . HOH   F .   ? 0.3952 0.4805 0.6220 -0.0678 -0.0647 0.1958  531 HOH   A O   
6862 O O   . HOH   G .   ? 0.2542 0.2532 0.3146 0.0193  0.0807  0.0443  201 HOH   B O   
6863 O O   . HOH   G .   ? 0.4262 0.3074 0.3563 -0.0597 0.0168  -0.1108 202 HOH   B O   
6864 O O   . HOH   G .   ? 0.4468 0.4187 0.6120 -0.0058 -0.1310 0.2664  203 HOH   B O   
6865 O O   . HOH   G .   ? 0.6572 0.5238 0.5686 0.1877  0.0586  0.0052  204 HOH   B O   
6866 O O   . HOH   G .   ? 0.4687 0.4954 0.6049 -0.1122 -0.0708 -0.1347 205 HOH   B O   
6867 O O   . HOH   G .   ? 0.3158 0.4444 0.6667 -0.0797 0.0396  -0.0453 206 HOH   B O   
6868 O O   . HOH   G .   ? 0.7528 0.3596 0.4936 0.0507  0.1733  -0.0297 207 HOH   B O   
6869 O O   . HOH   G .   ? 0.3118 0.5006 0.5377 -0.0238 0.1744  -0.1986 208 HOH   B O   
6870 O O   . HOH   G .   ? 0.3444 0.6864 0.3625 0.0770  0.0442  0.2337  209 HOH   B O   
6871 O O   . HOH   G .   ? 0.5045 0.5914 0.4047 0.2861  -0.1356 -0.0308 210 HOH   B O   
6872 O O   . HOH   G .   ? 0.3470 0.5342 0.4666 0.2358  0.0311  -0.0507 211 HOH   B O   
6873 O O   . HOH   G .   ? 0.3027 0.3308 0.6666 0.0755  -0.1091 0.0321  212 HOH   B O   
6874 O O   . HOH   G .   ? 0.5607 0.4430 0.2985 -0.0499 -0.1154 -0.1346 213 HOH   B O   
6875 O O   . HOH   G .   ? 0.1966 0.2263 0.2991 -0.0088 0.0285  -0.0177 214 HOH   B O   
6876 O O   . HOH   G .   ? 0.3470 0.3852 0.5185 0.0575  -0.0165 0.0520  215 HOH   B O   
6877 O O   . HOH   G .   ? 0.2786 0.2478 0.5971 -0.0384 0.0643  -0.0034 216 HOH   B O   
6878 O O   . HOH   G .   ? 0.1687 0.1947 0.2885 -0.0151 -0.0063 0.0160  217 HOH   B O   
6879 O O   . HOH   G .   ? 0.5396 0.3888 0.3666 -0.0225 -0.1286 0.0649  218 HOH   B O   
6880 O O   . HOH   G .   ? 0.4642 0.5401 0.4068 0.2625  -0.0755 0.0067  219 HOH   B O   
6881 O O   . HOH   G .   ? 0.4639 0.2085 0.3122 -0.0070 -0.1060 0.0229  220 HOH   B O   
6882 O O   . HOH   G .   ? 0.3464 0.2160 0.5808 0.0158  0.2228  0.0762  221 HOH   B O   
6883 O O   . HOH   G .   ? 0.2852 0.3853 0.3837 -0.0945 0.0871  -0.0811 222 HOH   B O   
6884 O O   . HOH   G .   ? 0.4692 0.4089 0.3705 0.0192  0.0932  -0.1322 223 HOH   B O   
6885 O O   . HOH   G .   ? 0.3743 0.5165 0.5410 -0.1924 -0.0087 0.0802  224 HOH   B O   
6886 O O   . HOH   G .   ? 0.4160 0.6577 0.3684 0.2123  0.0202  0.0369  225 HOH   B O   
6887 O O   . HOH   G .   ? 0.1692 0.2107 0.2964 -0.0133 -0.0010 -0.0143 226 HOH   B O   
6888 O O   . HOH   G .   ? 0.4720 0.4710 0.6611 0.0046  -0.1612 -0.0779 227 HOH   B O   
6889 O O   . HOH   G .   ? 0.2806 0.2558 0.3261 0.0301  0.0366  -0.0930 228 HOH   B O   
6890 O O   . HOH   G .   ? 0.6205 0.6251 0.3122 0.1381  0.0343  0.0801  229 HOH   B O   
6891 O O   . HOH   G .   ? 0.2171 0.2155 0.4063 -0.0261 -0.0125 -0.0600 230 HOH   B O   
6892 O O   . HOH   G .   ? 0.3900 0.1831 0.2177 0.0079  -0.0969 -0.0028 231 HOH   B O   
6893 O O   . HOH   G .   ? 0.4641 0.2847 0.2911 -0.0836 0.0420  -0.0451 232 HOH   B O   
6894 O O   . HOH   G .   ? 0.5122 0.2973 0.3683 -0.1557 0.0301  0.0107  233 HOH   B O   
6895 O O   . HOH   G .   ? 0.2727 0.1827 0.2738 -0.0272 0.1086  0.0044  234 HOH   B O   
6896 O O   . HOH   G .   ? 0.3282 0.2426 0.3858 -0.0146 0.1389  0.0118  235 HOH   B O   
6897 O O   . HOH   G .   ? 0.7175 0.4818 0.4896 0.1576  0.0172  -0.1141 236 HOH   B O   
6898 O O   . HOH   G .   ? 0.2268 0.3760 0.3317 -0.0428 -0.0672 -0.0676 237 HOH   B O   
6899 O O   . HOH   G .   ? 0.1682 0.1586 0.2549 -0.0107 -0.0013 -0.0153 238 HOH   B O   
6900 O O   . HOH   G .   ? 0.1496 0.1543 0.1681 -0.0149 -0.0063 0.0054  239 HOH   B O   
6901 O O   . HOH   G .   ? 0.2065 0.1374 0.3318 0.0071  -0.0425 -0.0152 240 HOH   B O   
6902 O O   . HOH   G .   ? 0.2146 0.4180 0.2392 -0.0771 -0.0224 0.0551  241 HOH   B O   
6903 O O   . HOH   G .   ? 0.4007 0.2985 0.3992 0.0517  -0.1191 -0.1582 242 HOH   B O   
6904 O O   . HOH   G .   ? 0.3556 0.2983 0.4318 0.0892  -0.0316 -0.0697 243 HOH   B O   
6905 O O   . HOH   G .   ? 0.2179 0.2047 0.2124 -0.0297 -0.0475 0.0143  244 HOH   B O   
6906 O O   . HOH   G .   ? 0.6381 0.2853 0.2701 0.0107  0.1100  0.0072  245 HOH   B O   
6907 O O   . HOH   G .   ? 0.1596 0.1386 0.1541 -0.0018 -0.0051 0.0028  246 HOH   B O   
6908 O O   . HOH   G .   ? 0.2062 0.2226 0.3082 -0.0409 -0.0034 -0.0195 247 HOH   B O   
6909 O O   . HOH   G .   ? 0.3535 0.3235 0.2128 0.0615  0.0596  0.0472  248 HOH   B O   
6910 O O   . HOH   G .   ? 0.2589 0.4183 0.4944 0.1139  -0.0469 -0.0751 249 HOH   B O   
6911 O O   . HOH   G .   ? 0.2862 0.2454 0.3317 0.0784  0.0990  0.0182  250 HOH   B O   
6912 O O   . HOH   G .   ? 0.3180 0.1783 0.6342 -0.0180 -0.1262 -0.0270 251 HOH   B O   
6913 O O   . HOH   G .   ? 0.2577 0.2265 0.1774 0.0047  -0.0238 0.0009  252 HOH   B O   
6914 O O   . HOH   G .   ? 0.5183 0.2981 0.4366 -0.2144 -0.0481 0.0313  253 HOH   B O   
6915 O O   . HOH   G .   ? 0.3147 0.3525 0.2352 0.0461  0.0621  0.0085  254 HOH   B O   
6916 O O   . HOH   G .   ? 0.1694 0.1749 0.3109 -0.0202 -0.0296 0.0235  255 HOH   B O   
6917 O O   . HOH   G .   ? 0.2176 0.1496 0.2134 -0.0261 -0.0343 0.0295  256 HOH   B O   
6918 O O   . HOH   G .   ? 0.1479 0.1761 0.1950 -0.0067 0.0120  0.0056  257 HOH   B O   
6919 O O   . HOH   G .   ? 0.2956 0.5196 0.3049 -0.1184 -0.0294 -0.0756 258 HOH   B O   
6920 O O   . HOH   G .   ? 0.2419 0.2269 0.2616 0.0889  -0.0808 -0.0814 259 HOH   B O   
6921 O O   . HOH   G .   ? 0.2577 0.2048 0.1946 0.0131  -0.0085 -0.0005 260 HOH   B O   
6922 O O   . HOH   G .   ? 0.3247 0.2465 0.3087 -0.0321 0.0268  -0.0471 261 HOH   B O   
6923 O O   . HOH   G .   ? 0.4233 0.3262 0.4413 -0.0312 -0.1025 -0.0386 262 HOH   B O   
6924 O O   . HOH   G .   ? 0.3249 0.1722 0.3743 0.0015  -0.0619 -0.0295 263 HOH   B O   
6925 O O   . HOH   G .   ? 0.1908 0.2788 0.2604 0.0417  0.0417  0.0837  264 HOH   B O   
6926 O O   . HOH   G .   ? 0.2312 0.4408 0.6171 0.0192  0.0205  -0.0941 265 HOH   B O   
6927 O O   . HOH   G .   ? 0.2583 0.2187 0.2885 -0.0603 -0.0038 -0.0088 266 HOH   B O   
6928 O O   . HOH   G .   ? 0.2255 0.3220 0.2217 -0.0386 0.0180  0.0448  267 HOH   B O   
6929 O O   . HOH   G .   ? 0.4111 0.3409 0.2978 0.0443  -0.0021 -0.1189 268 HOH   B O   
6930 O O   . HOH   G .   ? 0.2078 0.1600 0.2240 -0.0272 -0.0204 0.0192  269 HOH   B O   
6931 O O   . HOH   G .   ? 0.1897 0.1810 0.1777 -0.0365 -0.0367 0.0024  270 HOH   B O   
6932 O O   . HOH   G .   ? 0.2652 0.2994 0.2435 -0.0372 -0.0921 0.0153  271 HOH   B O   
6933 O O   . HOH   G .   ? 0.2757 0.3452 0.5226 0.0273  -0.0352 -0.0492 272 HOH   B O   
6934 O O   . HOH   G .   ? 0.2697 0.4188 0.3305 -0.0805 0.0752  -0.1537 273 HOH   B O   
6935 O O   . HOH   G .   ? 0.2441 0.3696 0.4037 0.0307  0.1195  0.0227  274 HOH   B O   
6936 O O   . HOH   G .   ? 0.3217 0.5105 0.3808 -0.0532 -0.0966 0.1234  275 HOH   B O   
6937 O O   . HOH   G .   ? 0.2409 0.3999 0.2236 0.1109  -0.0269 -0.0148 276 HOH   B O   
6938 O O   . HOH   G .   ? 0.2549 0.2565 0.2463 -0.0383 -0.0803 -0.0368 277 HOH   B O   
6939 O O   . HOH   G .   ? 0.1787 0.1475 0.4806 -0.0049 -0.0449 -0.0227 278 HOH   B O   
6940 O O   . HOH   G .   ? 0.2792 0.2149 0.4957 0.0192  0.0807  0.0368  279 HOH   B O   
6941 O O   . HOH   G .   ? 0.1662 0.1610 0.1886 0.0024  0.0010  -0.0021 280 HOH   B O   
6942 O O   . HOH   G .   ? 0.2436 0.6733 0.2502 0.0287  -0.0186 -0.0197 281 HOH   B O   
6943 O O   . HOH   G .   ? 0.5699 0.3872 0.3216 0.2593  0.1222  0.0984  282 HOH   B O   
6944 O O   . HOH   G .   ? 0.3387 0.3607 0.5081 0.0977  -0.0967 -0.1158 283 HOH   B O   
6945 O O   . HOH   G .   ? 0.1684 0.1641 0.3309 -0.0189 0.0170  -0.0083 284 HOH   B O   
6946 O O   . HOH   G .   ? 0.2415 0.4615 0.5175 -0.0570 -0.0690 -0.1694 285 HOH   B O   
6947 O O   . HOH   G .   ? 0.1708 0.3013 0.5132 0.0129  0.0077  -0.1337 286 HOH   B O   
6948 O O   . HOH   G .   ? 0.2658 0.2471 0.3114 0.0307  -0.0825 0.0152  287 HOH   B O   
6949 O O   . HOH   G .   ? 0.2698 0.4657 0.4566 -0.0920 -0.1178 0.0710  288 HOH   B O   
6950 O O   . HOH   G .   ? 0.3807 0.2707 0.2223 0.0310  -0.0953 -0.0029 289 HOH   B O   
6951 O O   . HOH   G .   ? 0.1693 0.2124 0.1690 -0.0129 -0.0231 0.0068  290 HOH   B O   
6952 O O   . HOH   G .   ? 0.3146 0.6823 0.7221 0.0973  -0.0731 -0.1167 291 HOH   B O   
6953 O O   . HOH   G .   ? 0.3642 0.2396 0.4201 -0.0917 -0.2203 0.0936  292 HOH   B O   
6954 O O   . HOH   G .   ? 0.4499 0.4793 0.2262 -0.0140 0.0707  0.0653  293 HOH   B O   
6955 O O   . HOH   G .   ? 0.3614 0.2752 0.2813 -0.0298 0.0065  -0.1244 294 HOH   B O   
6956 O O   . HOH   G .   ? 0.2106 0.1613 0.2303 0.0110  0.0032  0.0077  295 HOH   B O   
6957 O O   . HOH   G .   ? 0.4622 0.3704 0.2363 0.1320  -0.0777 0.0510  296 HOH   B O   
6958 O O   . HOH   G .   ? 0.2999 0.2811 0.5171 -0.0335 -0.0846 0.1167  297 HOH   B O   
6959 O O   . HOH   G .   ? 0.1695 0.2128 0.2864 0.0154  -0.0063 0.0212  298 HOH   B O   
6960 O O   . HOH   G .   ? 0.3761 0.1981 0.3880 0.0802  0.1525  0.0679  299 HOH   B O   
6961 O O   . HOH   G .   ? 0.3809 0.6152 0.2345 -0.0511 -0.0789 0.1368  300 HOH   B O   
6962 O O   . HOH   G .   ? 0.2208 0.1780 0.2607 -0.0309 -0.0160 -0.0043 301 HOH   B O   
6963 O O   . HOH   G .   ? 0.4111 0.5201 0.4978 0.0438  -0.1285 0.0080  302 HOH   B O   
6964 O O   . HOH   G .   ? 0.2025 0.2569 0.5623 0.0212  -0.0213 -0.1052 303 HOH   B O   
6965 O O   . HOH   G .   ? 0.3186 0.3500 0.4200 -0.1181 0.1157  -0.0766 304 HOH   B O   
6966 O O   . HOH   G .   ? 0.1629 0.1527 0.3124 0.0024  -0.0075 0.0059  305 HOH   B O   
6967 O O   . HOH   G .   ? 0.2488 0.1514 0.2718 -0.0090 -0.0169 0.0322  306 HOH   B O   
6968 O O   . HOH   G .   ? 0.2332 0.2379 0.6036 -0.0535 0.0059  0.1222  307 HOH   B O   
6969 O O   . HOH   G .   ? 0.1660 0.1917 0.2943 -0.0196 -0.0171 0.0094  308 HOH   B O   
6970 O O   . HOH   G .   ? 0.3211 0.8145 0.3586 0.1305  -0.0051 0.1280  309 HOH   B O   
6971 O O   . HOH   G .   ? 0.2862 0.2994 0.3670 -0.0644 0.1100  -0.0937 310 HOH   B O   
6972 O O   . HOH   G .   ? 0.4725 0.3069 0.2402 -0.1917 0.0610  -0.0079 311 HOH   B O   
6973 O O   . HOH   G .   ? 0.2275 0.1654 0.3351 0.0413  -0.1053 -0.0081 312 HOH   B O   
6974 O O   . HOH   G .   ? 0.4470 0.3007 0.5207 0.0774  0.2211  0.1642  313 HOH   B O   
6975 O O   . HOH   G .   ? 0.4224 0.4424 0.5082 -0.0587 0.0036  0.1637  314 HOH   B O   
6976 O O   . HOH   G .   ? 0.4338 0.2470 0.2747 0.1683  0.1120  0.0560  315 HOH   B O   
6977 O O   . HOH   G .   ? 0.3555 0.3795 0.7014 -0.0167 -0.0789 0.2291  316 HOH   B O   
6978 O O   . HOH   G .   ? 0.5950 0.5226 0.4974 -0.1135 -0.0265 0.1102  317 HOH   B O   
6979 O O   . HOH   G .   ? 0.6399 0.6119 0.4691 0.3148  -0.0043 -0.0429 318 HOH   B O   
6980 O O   . HOH   G .   ? 0.2077 0.6252 0.5232 -0.0568 0.0188  -0.0012 319 HOH   B O   
6981 O O   . HOH   G .   ? 0.3543 0.4175 0.6258 0.0360  -0.0160 0.0933  320 HOH   B O   
6982 O O   . HOH   G .   ? 0.2373 0.3769 0.4776 -0.0322 -0.0414 -0.0257 321 HOH   B O   
6983 O O   . HOH   G .   ? 0.2313 0.2071 0.1773 -0.0064 0.0220  0.0145  322 HOH   B O   
6984 O O   . HOH   G .   ? 0.1773 0.2988 0.2529 -0.0160 -0.0177 0.0779  323 HOH   B O   
6985 O O   . HOH   G .   ? 0.4980 0.2770 0.2802 0.0221  0.0308  0.0869  324 HOH   B O   
6986 O O   . HOH   G .   ? 0.1711 0.1728 0.2976 -0.0197 -0.0071 -0.0239 325 HOH   B O   
6987 O O   . HOH   G .   ? 0.4921 0.4212 0.2671 0.0470  -0.0489 -0.0543 326 HOH   B O   
6988 O O   . HOH   G .   ? 0.7297 0.2072 0.2827 0.0055  -0.0578 0.0055  327 HOH   B O   
6989 O O   . HOH   G .   ? 0.2834 0.2360 0.2523 0.0124  -0.0144 0.0401  328 HOH   B O   
6990 O O   . HOH   G .   ? 0.2068 0.2062 0.2991 0.0380  0.0521  0.0165  329 HOH   B O   
6991 O O   . HOH   G .   ? 0.2765 0.3566 0.5044 -0.0604 -0.1560 0.1416  330 HOH   B O   
6992 O O   . HOH   G .   ? 0.5627 0.5009 0.6888 0.0725  -0.1049 0.2085  331 HOH   B O   
6993 O O   . HOH   G .   ? 0.6528 0.4338 0.6087 0.1505  0.1524  0.0043  332 HOH   B O   
6994 O O   . HOH   G .   ? 0.4540 0.4973 0.3377 -0.0228 -0.0906 0.0097  333 HOH   B O   
6995 O O   . HOH   G .   ? 0.2474 0.2163 0.5473 -0.0096 -0.0220 0.0270  334 HOH   B O   
6996 O O   . HOH   G .   ? 0.5605 0.3525 0.3490 -0.0106 0.0762  0.1168  335 HOH   B O   
6997 O O   . HOH   G .   ? 0.1662 0.2662 0.2931 0.0119  -0.0217 -0.0624 336 HOH   B O   
6998 O O   . HOH   G .   ? 0.5366 0.4505 0.2360 0.1936  -0.1089 -0.0480 337 HOH   B O   
6999 O O   . HOH   G .   ? 0.1836 0.1520 0.2355 0.0104  -0.0251 0.0086  338 HOH   B O   
7000 O O   . HOH   G .   ? 0.5688 0.4365 0.6574 -0.0631 -0.0685 -0.1256 339 HOH   B O   
7001 O O   . HOH   G .   ? 0.4884 0.3564 0.4128 0.0365  0.0497  -0.1545 340 HOH   B O   
7002 O O   . HOH   G .   ? 0.4150 0.6806 0.3651 -0.0106 -0.0338 0.1585  341 HOH   B O   
7003 O O   . HOH   G .   ? 0.5676 0.3268 0.3166 0.0829  -0.1321 -0.0784 342 HOH   B O   
7004 O O   . HOH   G .   ? 0.2296 0.1938 0.3013 -0.0064 0.0626  -0.0048 343 HOH   B O   
7005 O O   . HOH   G .   ? 0.4140 0.6666 0.3951 -0.0855 -0.1195 -0.0657 344 HOH   B O   
7006 O O   . HOH   G .   ? 0.6923 0.6250 0.3032 0.0003  -0.0598 0.1517  345 HOH   B O   
7007 O O   . HOH   G .   ? 0.2981 0.6093 0.5992 0.0541  -0.1730 -0.0101 346 HOH   B O   
7008 O O   . HOH   G .   ? 0.6011 0.5032 0.5071 -0.1184 0.1289  0.0831  347 HOH   B O   
7009 O O   . HOH   G .   ? 0.4044 0.5725 0.4715 -0.0212 -0.0813 0.0879  348 HOH   B O   
7010 O O   . HOH   G .   ? 0.2688 0.6425 0.3513 0.1794  -0.0505 -0.1546 349 HOH   B O   
7011 O O   . HOH   G .   ? 0.2682 0.2325 0.5172 -0.0109 -0.0904 -0.0580 350 HOH   B O   
7012 O O   . HOH   G .   ? 0.2154 0.3958 0.5353 0.0304  0.0391  0.0189  351 HOH   B O   
7013 O O   . HOH   G .   ? 0.4319 0.6269 0.6427 0.0222  -0.0057 -0.0681 352 HOH   B O   
7014 O O   . HOH   G .   ? 0.4730 0.2803 0.4993 -0.0822 0.1071  0.0602  353 HOH   B O   
7015 O O   . HOH   G .   ? 0.3552 0.4547 0.4653 -0.1479 0.0176  -0.0268 354 HOH   B O   
7016 O O   . HOH   G .   ? 0.3933 0.2331 0.3905 -0.0667 0.0400  -0.1001 355 HOH   B O   
7017 O O   . HOH   G .   ? 0.5569 0.3753 0.3841 0.0757  0.1198  -0.0578 356 HOH   B O   
7018 O O   . HOH   G .   ? 0.3396 0.1826 0.3972 0.0359  -0.1364 -0.0365 357 HOH   B O   
7019 O O   . HOH   G .   ? 0.4095 0.2701 0.3721 -0.0932 -0.0328 -0.0422 358 HOH   B O   
7020 O O   . HOH   G .   ? 0.4646 0.5096 0.5125 0.1754  -0.1407 0.1365  359 HOH   B O   
7021 O O   . HOH   G .   ? 0.5298 0.3623 0.5155 -0.0062 -0.1636 -0.0658 360 HOH   B O   
7022 O O   . HOH   G .   ? 0.5163 0.4193 0.5784 0.0547  0.1285  0.1421  361 HOH   B O   
7023 O O   . HOH   G .   ? 0.4601 0.7212 0.3100 0.2488  0.0513  0.0831  362 HOH   B O   
7024 O O   . HOH   G .   ? 0.2303 0.3570 0.6479 -0.0772 -0.0489 -0.0782 363 HOH   B O   
7025 O O   . HOH   G .   ? 0.4562 0.4469 0.5044 -0.0426 -0.0020 0.0196  364 HOH   B O   
7026 O O   . HOH   G .   ? 0.6710 0.2165 0.3032 -0.0130 -0.0170 0.0522  365 HOH   B O   
7027 O O   . HOH   G .   ? 0.6366 0.4338 0.4592 0.1018  0.0630  0.0589  366 HOH   B O   
7028 O O   . HOH   G .   ? 0.5182 0.5242 0.4464 -0.0284 -0.0603 -0.1023 367 HOH   B O   
7029 O O   . HOH   G .   ? 0.4407 0.5557 0.5430 0.2542  0.1668  0.1780  368 HOH   B O   
7030 O O   . HOH   G .   ? 0.5921 0.5454 0.3301 0.1896  -0.1344 0.0504  369 HOH   B O   
7031 O O   . HOH   G .   ? 0.5732 0.4304 0.5516 0.0839  -0.1360 0.0063  370 HOH   B O   
7032 O O   . HOH   G .   ? 0.5173 0.3192 0.5222 -0.1411 -0.0620 0.0262  371 HOH   B O   
7033 O O   . HOH   G .   ? 0.6279 0.3651 0.3015 -0.1317 -0.0983 -0.0447 372 HOH   B O   
7034 O O   . HOH   G .   ? 0.7937 0.7520 0.5521 0.2369  -0.1414 0.0376  373 HOH   B O   
7035 O O   . HOH   G .   ? 0.2440 0.4584 0.4576 0.0002  -0.0775 -0.0735 374 HOH   B O   
7036 O O   . HOH   G .   ? 0.4572 0.5452 0.4980 -0.1097 -0.0763 0.0690  375 HOH   B O   
7037 O O   . HOH   G .   ? 0.3577 0.3408 0.4464 0.0660  -0.1099 -0.0785 376 HOH   B O   
7038 O O   . HOH   G .   ? 0.3115 0.4712 0.2435 0.0918  -0.0040 0.0015  377 HOH   B O   
7039 O O   . HOH   G .   ? 0.5022 0.6368 0.6108 0.1830  0.0640  0.2635  378 HOH   B O   
7040 O O   . HOH   G .   ? 0.6992 0.3386 0.5690 -0.1060 -0.0743 -0.0116 379 HOH   B O   
7041 O O   . HOH   G .   ? 0.5247 0.6369 0.4106 -0.1287 0.0006  -0.1528 380 HOH   B O   
7042 O O   . HOH   G .   ? 0.4139 0.4243 0.5007 0.1494  -0.0169 -0.0385 381 HOH   B O   
7043 O O   . HOH   G .   ? 0.4696 0.6519 0.5793 0.0129  0.1482  0.1489  382 HOH   B O   
7044 O O   . HOH   G .   ? 0.3098 0.2689 0.3123 -0.0010 0.0085  0.0368  383 HOH   B O   
7045 O O   . HOH   G .   ? 0.4217 0.7799 0.5489 0.0987  0.1896  0.0848  384 HOH   B O   
7046 O O   . HOH   G .   ? 0.5354 0.4708 0.4592 -0.0026 -0.0485 -0.0502 385 HOH   B O   
7047 O O   . HOH   G .   ? 0.2574 0.4230 0.4165 -0.0663 -0.1134 -0.0125 386 HOH   B O   
7048 O O   . HOH   G .   ? 0.4163 0.3597 0.3260 0.0049  0.0351  -0.0161 387 HOH   B O   
7049 O O   . HOH   G .   ? 0.7205 0.3807 0.4318 0.0462  0.0757  -0.1053 388 HOH   B O   
7050 O O   . HOH   G .   ? 0.6018 0.4464 0.4970 -0.0883 0.0356  -0.0212 389 HOH   B O   
7051 O O   . HOH   G .   ? 0.6755 0.5234 0.3693 0.2163  0.0069  0.0741  390 HOH   B O   
7052 O O   . HOH   G .   ? 0.3691 0.2279 0.3392 0.0716  -0.0216 -0.0099 391 HOH   B O   
7053 O O   . HOH   G .   ? 0.3875 0.4484 0.4623 -0.0120 0.0319  0.0359  392 HOH   B O   
7054 O O   . HOH   G .   ? 0.2471 0.4202 0.6788 -0.1197 -0.0793 0.0097  393 HOH   B O   
7055 O O   . HOH   G .   ? 0.4050 0.2320 0.5441 -0.0092 0.1019  0.0626  394 HOH   B O   
7056 O O   . HOH   G .   ? 0.4136 0.6097 0.4029 0.1138  -0.0165 -0.0935 395 HOH   B O   
7057 O O   . HOH   G .   ? 0.4561 0.4591 0.4023 0.0249  0.1009  0.0439  396 HOH   B O   
7058 O O   . HOH   G .   ? 0.3120 0.3752 0.3851 0.0484  0.0026  -0.0565 397 HOH   B O   
7059 O O   . HOH   G .   ? 0.2257 0.2977 0.6298 -0.0571 -0.1284 0.0436  398 HOH   B O   
7060 O O   . HOH   G .   ? 0.5037 0.6035 0.6932 0.1057  -0.1069 0.1936  399 HOH   B O   
7061 O O   . HOH   G .   ? 0.6243 0.4088 0.3159 -0.2318 -0.0447 0.1188  400 HOH   B O   
7062 O O   . HOH   G .   ? 0.5411 0.5154 0.3326 0.1415  -0.0064 -0.0132 401 HOH   B O   
# 
