data_7HEH
# 
_entry.id   7HEH 
# 
_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   7HEH         pdb_00007heh 10.2210/pdb7heh/pdb 
WWPDB D_1001407371 ?            ?                   
# 
_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                        7HEH 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                      18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                                          114.023   1   ? ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                            78.133    1   ? ? ? ? 
4 non-polymer syn '(2R)-3-(3-methylphenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 282.340   1   ? ? ? ? 
5 water       nat water                                                                           18.015    439 ? ? ? ? 
# 
_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 'DIMETHYL SULFOXIDE'                                                            DMS   
4 '(2R)-3-(3-methylphenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1A9U 
5 water                                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A9U non-polymer         . '(2R)-3-(3-methylphenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C16 H18 N4 O'   
282.340 
ALA   'L-peptide linking' y ALANINE                                                                         ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                        ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                      ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                 ? 'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                        ? 'C3 H7 N O2 S'   
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                            ? 'C2 H6 O S'      
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                       ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                 ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                         ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                       ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                           ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                      ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                         ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                          ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                      ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                   ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                         ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                          ? 'C3 H7 N O3'     
105.093 
TFA   non-polymer         . 'trifluoroacetic acid'                                                          ? 'C2 H F3 O2'     
114.023 
THR   'L-peptide linking' y THREONINE                                                                       ? 'C4 H9 N O3'     
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                        ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                          ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 DMS   1   202 301  DMS   DMS A . 
E 4 A1A9U 1   203 201  A1A9U LA1 A . 
F 5 HOH   1   301 36   HOH   HOH A . 
F 5 HOH   2   302 292  HOH   HOH A . 
F 5 HOH   3   303 196  HOH   HOH A . 
F 5 HOH   4   304 493  HOH   HOH A . 
F 5 HOH   5   305 153  HOH   HOH A . 
F 5 HOH   6   306 11   HOH   HOH A . 
F 5 HOH   7   307 625  HOH   HOH A . 
F 5 HOH   8   308 12   HOH   HOH A . 
F 5 HOH   9   309 281  HOH   HOH A . 
F 5 HOH   10  310 109  HOH   HOH A . 
F 5 HOH   11  311 1283 HOH   HOH A . 
F 5 HOH   12  312 209  HOH   HOH A . 
F 5 HOH   13  313 151  HOH   HOH A . 
F 5 HOH   14  314 21   HOH   HOH A . 
F 5 HOH   15  315 236  HOH   HOH A . 
F 5 HOH   16  316 136  HOH   HOH A . 
F 5 HOH   17  317 76   HOH   HOH A . 
F 5 HOH   18  318 229  HOH   HOH A . 
F 5 HOH   19  319 192  HOH   HOH A . 
F 5 HOH   20  320 409  HOH   HOH A . 
F 5 HOH   21  321 964  HOH   HOH A . 
F 5 HOH   22  322 661  HOH   HOH A . 
F 5 HOH   23  323 124  HOH   HOH A . 
F 5 HOH   24  324 33   HOH   HOH A . 
F 5 HOH   25  325 15   HOH   HOH A . 
F 5 HOH   26  326 1295 HOH   HOH A . 
F 5 HOH   27  327 140  HOH   HOH A . 
F 5 HOH   28  328 241  HOH   HOH A . 
F 5 HOH   29  329 86   HOH   HOH A . 
F 5 HOH   30  330 96   HOH   HOH A . 
F 5 HOH   31  331 662  HOH   HOH A . 
F 5 HOH   32  332 939  HOH   HOH A . 
F 5 HOH   33  333 1309 HOH   HOH A . 
F 5 HOH   34  334 26   HOH   HOH A . 
F 5 HOH   35  335 337  HOH   HOH A . 
F 5 HOH   36  336 39   HOH   HOH A . 
F 5 HOH   37  337 7    HOH   HOH A . 
F 5 HOH   38  338 115  HOH   HOH A . 
F 5 HOH   39  339 469  HOH   HOH A . 
F 5 HOH   40  340 56   HOH   HOH A . 
F 5 HOH   41  341 155  HOH   HOH A . 
F 5 HOH   42  342 92   HOH   HOH A . 
F 5 HOH   43  343 42   HOH   HOH A . 
F 5 HOH   44  344 2    HOH   HOH A . 
F 5 HOH   45  345 27   HOH   HOH A . 
F 5 HOH   46  346 320  HOH   HOH A . 
F 5 HOH   47  347 225  HOH   HOH A . 
F 5 HOH   48  348 162  HOH   HOH A . 
F 5 HOH   49  349 165  HOH   HOH A . 
F 5 HOH   50  350 169  HOH   HOH A . 
F 5 HOH   51  351 164  HOH   HOH A . 
F 5 HOH   52  352 81   HOH   HOH A . 
F 5 HOH   53  353 22   HOH   HOH A . 
F 5 HOH   54  354 1300 HOH   HOH A . 
F 5 HOH   55  355 93   HOH   HOH A . 
F 5 HOH   56  356 1290 HOH   HOH A . 
F 5 HOH   57  357 26   HOH   HOH A . 
F 5 HOH   58  358 66   HOH   HOH A . 
F 5 HOH   59  359 186  HOH   HOH A . 
F 5 HOH   60  360 27   HOH   HOH A . 
F 5 HOH   61  361 247  HOH   HOH A . 
F 5 HOH   62  362 102  HOH   HOH A . 
F 5 HOH   63  363 396  HOH   HOH A . 
F 5 HOH   64  364 630  HOH   HOH A . 
F 5 HOH   65  365 159  HOH   HOH A . 
F 5 HOH   66  366 8    HOH   HOH A . 
F 5 HOH   67  367 21   HOH   HOH A . 
F 5 HOH   68  368 354  HOH   HOH A . 
F 5 HOH   69  369 105  HOH   HOH A . 
F 5 HOH   70  370 19   HOH   HOH A . 
F 5 HOH   71  371 78   HOH   HOH A . 
F 5 HOH   72  372 5    HOH   HOH A . 
F 5 HOH   73  373 45   HOH   HOH A . 
F 5 HOH   74  374 138  HOH   HOH A . 
F 5 HOH   75  375 139  HOH   HOH A . 
F 5 HOH   76  376 461  HOH   HOH A . 
F 5 HOH   77  377 366  HOH   HOH A . 
F 5 HOH   78  378 393  HOH   HOH A . 
F 5 HOH   79  379 17   HOH   HOH A . 
F 5 HOH   80  380 18   HOH   HOH A . 
F 5 HOH   81  381 49   HOH   HOH A . 
F 5 HOH   82  382 10   HOH   HOH A . 
F 5 HOH   83  383 46   HOH   HOH A . 
F 5 HOH   84  384 24   HOH   HOH A . 
F 5 HOH   85  385 134  HOH   HOH A . 
F 5 HOH   86  386 35   HOH   HOH A . 
F 5 HOH   87  387 381  HOH   HOH A . 
F 5 HOH   88  388 296  HOH   HOH A . 
F 5 HOH   89  389 351  HOH   HOH A . 
F 5 HOH   90  390 3    HOH   HOH A . 
F 5 HOH   91  391 218  HOH   HOH A . 
F 5 HOH   92  392 5    HOH   HOH A . 
F 5 HOH   93  393 1308 HOH   HOH A . 
F 5 HOH   94  394 24   HOH   HOH A . 
F 5 HOH   95  395 57   HOH   HOH A . 
F 5 HOH   96  396 148  HOH   HOH A . 
F 5 HOH   97  397 154  HOH   HOH A . 
F 5 HOH   98  398 140  HOH   HOH A . 
F 5 HOH   99  399 1279 HOH   HOH A . 
F 5 HOH   100 400 6    HOH   HOH A . 
F 5 HOH   101 401 68   HOH   HOH A . 
F 5 HOH   102 402 1315 HOH   HOH A . 
F 5 HOH   103 403 116  HOH   HOH A . 
F 5 HOH   104 404 85   HOH   HOH A . 
F 5 HOH   105 405 1238 HOH   HOH A . 
F 5 HOH   106 406 405  HOH   HOH A . 
F 5 HOH   107 407 58   HOH   HOH A . 
F 5 HOH   108 408 1310 HOH   HOH A . 
F 5 HOH   109 409 303  HOH   HOH A . 
F 5 HOH   110 410 278  HOH   HOH A . 
F 5 HOH   111 411 199  HOH   HOH A . 
F 5 HOH   112 412 333  HOH   HOH A . 
F 5 HOH   113 413 30   HOH   HOH A . 
F 5 HOH   114 414 121  HOH   HOH A . 
F 5 HOH   115 415 74   HOH   HOH A . 
F 5 HOH   116 416 1289 HOH   HOH A . 
F 5 HOH   117 417 1275 HOH   HOH A . 
F 5 HOH   118 418 12   HOH   HOH A . 
F 5 HOH   119 419 1296 HOH   HOH A . 
F 5 HOH   120 420 67   HOH   HOH A . 
F 5 HOH   121 421 28   HOH   HOH A . 
F 5 HOH   122 422 34   HOH   HOH A . 
F 5 HOH   123 423 29   HOH   HOH A . 
F 5 HOH   124 424 83   HOH   HOH A . 
F 5 HOH   125 425 122  HOH   HOH A . 
F 5 HOH   126 426 195  HOH   HOH A . 
F 5 HOH   127 427 3    HOH   HOH A . 
F 5 HOH   128 428 25   HOH   HOH A . 
F 5 HOH   129 429 1068 HOH   HOH A . 
F 5 HOH   130 430 123  HOH   HOH A . 
F 5 HOH   131 431 125  HOH   HOH A . 
F 5 HOH   132 432 8    HOH   HOH A . 
F 5 HOH   133 433 13   HOH   HOH A . 
F 5 HOH   134 434 51   HOH   HOH A . 
F 5 HOH   135 435 53   HOH   HOH A . 
F 5 HOH   136 436 397  HOH   HOH A . 
F 5 HOH   137 437 95   HOH   HOH A . 
F 5 HOH   138 438 582  HOH   HOH A . 
F 5 HOH   139 439 16   HOH   HOH A . 
F 5 HOH   140 440 1222 HOH   HOH A . 
F 5 HOH   141 441 1313 HOH   HOH A . 
F 5 HOH   142 442 156  HOH   HOH A . 
F 5 HOH   143 443 7    HOH   HOH A . 
F 5 HOH   144 444 952  HOH   HOH A . 
F 5 HOH   145 445 132  HOH   HOH A . 
F 5 HOH   146 446 70   HOH   HOH A . 
F 5 HOH   147 447 4    HOH   HOH A . 
F 5 HOH   148 448 1189 HOH   HOH A . 
F 5 HOH   149 449 212  HOH   HOH A . 
F 5 HOH   150 450 71   HOH   HOH A . 
F 5 HOH   151 451 1    HOH   HOH A . 
F 5 HOH   152 452 188  HOH   HOH A . 
F 5 HOH   153 453 80   HOH   HOH A . 
F 5 HOH   154 454 79   HOH   HOH A . 
F 5 HOH   155 455 944  HOH   HOH A . 
F 5 HOH   156 456 15   HOH   HOH A . 
F 5 HOH   157 457 17   HOH   HOH A . 
F 5 HOH   158 458 1286 HOH   HOH A . 
F 5 HOH   159 459 1301 HOH   HOH A . 
F 5 HOH   160 460 94   HOH   HOH A . 
F 5 HOH   161 461 16   HOH   HOH A . 
F 5 HOH   162 462 40   HOH   HOH A . 
F 5 HOH   163 463 104  HOH   HOH A . 
F 5 HOH   164 464 73   HOH   HOH A . 
F 5 HOH   165 465 330  HOH   HOH A . 
F 5 HOH   166 466 1094 HOH   HOH A . 
F 5 HOH   167 467 97   HOH   HOH A . 
F 5 HOH   168 468 576  HOH   HOH A . 
F 5 HOH   169 469 1134 HOH   HOH A . 
F 5 HOH   170 470 107  HOH   HOH A . 
F 5 HOH   171 471 9    HOH   HOH A . 
F 5 HOH   172 472 509  HOH   HOH A . 
F 5 HOH   173 473 726  HOH   HOH A . 
F 5 HOH   174 474 163  HOH   HOH A . 
F 5 HOH   175 475 1119 HOH   HOH A . 
F 5 HOH   176 476 756  HOH   HOH A . 
F 5 HOH   177 477 801  HOH   HOH A . 
F 5 HOH   178 478 126  HOH   HOH A . 
F 5 HOH   179 479 408  HOH   HOH A . 
F 5 HOH   180 480 556  HOH   HOH A . 
F 5 HOH   181 481 319  HOH   HOH A . 
F 5 HOH   182 482 361  HOH   HOH A . 
F 5 HOH   183 483 342  HOH   HOH A . 
F 5 HOH   184 484 1307 HOH   HOH A . 
F 5 HOH   185 485 280  HOH   HOH A . 
F 5 HOH   186 486 63   HOH   HOH A . 
F 5 HOH   187 487 370  HOH   HOH A . 
F 5 HOH   188 488 1276 HOH   HOH A . 
F 5 HOH   189 489 250  HOH   HOH A . 
F 5 HOH   190 490 1287 HOH   HOH A . 
F 5 HOH   191 491 224  HOH   HOH A . 
F 5 HOH   192 492 25   HOH   HOH A . 
F 5 HOH   193 493 1306 HOH   HOH A . 
F 5 HOH   194 494 267  HOH   HOH A . 
F 5 HOH   195 495 14   HOH   HOH A . 
F 5 HOH   196 496 695  HOH   HOH A . 
F 5 HOH   197 497 202  HOH   HOH A . 
F 5 HOH   198 498 674  HOH   HOH A . 
F 5 HOH   199 499 1284 HOH   HOH A . 
F 5 HOH   200 500 521  HOH   HOH A . 
F 5 HOH   201 501 711  HOH   HOH A . 
F 5 HOH   202 502 919  HOH   HOH A . 
F 5 HOH   203 503 19   HOH   HOH A . 
F 5 HOH   204 504 20   HOH   HOH A . 
F 5 HOH   205 505 315  HOH   HOH A . 
F 5 HOH   206 506 2    HOH   HOH A . 
F 5 HOH   207 507 6    HOH   HOH A . 
F 5 HOH   208 508 309  HOH   HOH A . 
F 5 HOH   209 509 1314 HOH   HOH A . 
F 5 HOH   210 510 318  HOH   HOH A . 
F 5 HOH   211 511 1299 HOH   HOH A . 
F 5 HOH   212 512 331  HOH   HOH A . 
F 5 HOH   213 513 805  HOH   HOH A . 
F 5 HOH   214 514 263  HOH   HOH A . 
F 5 HOH   215 515 135  HOH   HOH A . 
F 5 HOH   216 516 941  HOH   HOH A . 
F 5 HOH   217 517 152  HOH   HOH A . 
F 5 HOH   218 518 356  HOH   HOH A . 
F 5 HOH   219 519 208  HOH   HOH A . 
F 5 HOH   220 520 350  HOH   HOH A . 
F 5 HOH   221 521 1071 HOH   HOH A . 
F 5 HOH   222 522 180  HOH   HOH A . 
F 5 HOH   223 523 23   HOH   HOH A . 
F 5 HOH   224 524 313  HOH   HOH A . 
F 5 HOH   225 525 363  HOH   HOH A . 
F 5 HOH   226 526 371  HOH   HOH A . 
F 5 HOH   227 527 326  HOH   HOH A . 
F 5 HOH   228 528 429  HOH   HOH A . 
F 5 HOH   229 529 185  HOH   HOH A . 
F 5 HOH   230 530 18   HOH   HOH A . 
F 5 HOH   231 531 4    HOH   HOH A . 
F 5 HOH   232 532 376  HOH   HOH A . 
F 5 HOH   233 533 70   HOH   HOH A . 
F 5 HOH   234 534 772  HOH   HOH A . 
F 5 HOH   235 535 1074 HOH   HOH A . 
F 5 HOH   236 536 1292 HOH   HOH A . 
F 5 HOH   237 537 346  HOH   HOH A . 
F 5 HOH   238 538 1078 HOH   HOH A . 
G 5 HOH   1   201 531  HOH   HOH B . 
G 5 HOH   2   202 64   HOH   HOH B . 
G 5 HOH   3   203 358  HOH   HOH B . 
G 5 HOH   4   204 654  HOH   HOH B . 
G 5 HOH   5   205 900  HOH   HOH B . 
G 5 HOH   6   206 549  HOH   HOH B . 
G 5 HOH   7   207 1249 HOH   HOH B . 
G 5 HOH   8   208 364  HOH   HOH B . 
G 5 HOH   9   209 353  HOH   HOH B . 
G 5 HOH   10  210 452  HOH   HOH B . 
G 5 HOH   11  211 743  HOH   HOH B . 
G 5 HOH   12  212 398  HOH   HOH B . 
G 5 HOH   13  213 240  HOH   HOH B . 
G 5 HOH   14  214 758  HOH   HOH B . 
G 5 HOH   15  215 120  HOH   HOH B . 
G 5 HOH   16  216 1140 HOH   HOH B . 
G 5 HOH   17  217 50   HOH   HOH B . 
G 5 HOH   18  218 264  HOH   HOH B . 
G 5 HOH   19  219 131  HOH   HOH B . 
G 5 HOH   20  220 343  HOH   HOH B . 
G 5 HOH   21  221 282  HOH   HOH B . 
G 5 HOH   22  222 1278 HOH   HOH B . 
G 5 HOH   23  223 444  HOH   HOH B . 
G 5 HOH   24  224 166  HOH   HOH B . 
G 5 HOH   25  225 82   HOH   HOH B . 
G 5 HOH   26  226 723  HOH   HOH B . 
G 5 HOH   27  227 75   HOH   HOH B . 
G 5 HOH   28  228 54   HOH   HOH B . 
G 5 HOH   29  229 252  HOH   HOH B . 
G 5 HOH   30  230 332  HOH   HOH B . 
G 5 HOH   31  231 110  HOH   HOH B . 
G 5 HOH   32  232 391  HOH   HOH B . 
G 5 HOH   33  233 60   HOH   HOH B . 
G 5 HOH   34  234 272  HOH   HOH B . 
G 5 HOH   35  235 133  HOH   HOH B . 
G 5 HOH   36  236 128  HOH   HOH B . 
G 5 HOH   37  237 127  HOH   HOH B . 
G 5 HOH   38  238 1    HOH   HOH B . 
G 5 HOH   39  239 276  HOH   HOH B . 
G 5 HOH   40  240 300  HOH   HOH B . 
G 5 HOH   41  241 72   HOH   HOH B . 
G 5 HOH   42  242 205  HOH   HOH B . 
G 5 HOH   43  243 325  HOH   HOH B . 
G 5 HOH   44  244 181  HOH   HOH B . 
G 5 HOH   45  245 232  HOH   HOH B . 
G 5 HOH   46  246 9    HOH   HOH B . 
G 5 HOH   47  247 129  HOH   HOH B . 
G 5 HOH   48  248 231  HOH   HOH B . 
G 5 HOH   49  249 69   HOH   HOH B . 
G 5 HOH   50  250 14   HOH   HOH B . 
G 5 HOH   51  251 1312 HOH   HOH B . 
G 5 HOH   52  252 30   HOH   HOH B . 
G 5 HOH   53  253 62   HOH   HOH B . 
G 5 HOH   54  254 172  HOH   HOH B . 
G 5 HOH   55  255 41   HOH   HOH B . 
G 5 HOH   56  256 31   HOH   HOH B . 
G 5 HOH   57  257 47   HOH   HOH B . 
G 5 HOH   58  258 10   HOH   HOH B . 
G 5 HOH   59  259 52   HOH   HOH B . 
G 5 HOH   60  260 347  HOH   HOH B . 
G 5 HOH   61  261 271  HOH   HOH B . 
G 5 HOH   62  262 143  HOH   HOH B . 
G 5 HOH   63  263 103  HOH   HOH B . 
G 5 HOH   64  264 144  HOH   HOH B . 
G 5 HOH   65  265 11   HOH   HOH B . 
G 5 HOH   66  266 150  HOH   HOH B . 
G 5 HOH   67  267 61   HOH   HOH B . 
G 5 HOH   68  268 242  HOH   HOH B . 
G 5 HOH   69  269 59   HOH   HOH B . 
G 5 HOH   70  270 77   HOH   HOH B . 
G 5 HOH   71  271 20   HOH   HOH B . 
G 5 HOH   72  272 220  HOH   HOH B . 
G 5 HOH   73  273 117  HOH   HOH B . 
G 5 HOH   74  274 43   HOH   HOH B . 
G 5 HOH   75  275 1277 HOH   HOH B . 
G 5 HOH   76  276 221  HOH   HOH B . 
G 5 HOH   77  277 341  HOH   HOH B . 
G 5 HOH   78  278 243  HOH   HOH B . 
G 5 HOH   79  279 1305 HOH   HOH B . 
G 5 HOH   80  280 147  HOH   HOH B . 
G 5 HOH   81  281 84   HOH   HOH B . 
G 5 HOH   82  282 114  HOH   HOH B . 
G 5 HOH   83  283 302  HOH   HOH B . 
G 5 HOH   84  284 416  HOH   HOH B . 
G 5 HOH   85  285 235  HOH   HOH B . 
G 5 HOH   86  286 88   HOH   HOH B . 
G 5 HOH   87  287 175  HOH   HOH B . 
G 5 HOH   88  288 635  HOH   HOH B . 
G 5 HOH   89  289 22   HOH   HOH B . 
G 5 HOH   90  290 99   HOH   HOH B . 
G 5 HOH   91  291 106  HOH   HOH B . 
G 5 HOH   92  292 216  HOH   HOH B . 
G 5 HOH   93  293 137  HOH   HOH B . 
G 5 HOH   94  294 1126 HOH   HOH B . 
G 5 HOH   95  295 387  HOH   HOH B . 
G 5 HOH   96  296 89   HOH   HOH B . 
G 5 HOH   97  297 141  HOH   HOH B . 
G 5 HOH   98  298 13   HOH   HOH B . 
G 5 HOH   99  299 142  HOH   HOH B . 
G 5 HOH   100 300 1066 HOH   HOH B . 
G 5 HOH   101 301 287  HOH   HOH B . 
G 5 HOH   102 302 1106 HOH   HOH B . 
G 5 HOH   103 303 38   HOH   HOH B . 
G 5 HOH   104 304 112  HOH   HOH B . 
G 5 HOH   105 305 316  HOH   HOH B . 
G 5 HOH   106 306 160  HOH   HOH B . 
G 5 HOH   107 307 101  HOH   HOH B . 
G 5 HOH   108 308 197  HOH   HOH B . 
G 5 HOH   109 309 299  HOH   HOH B . 
G 5 HOH   110 310 32   HOH   HOH B . 
G 5 HOH   111 311 91   HOH   HOH B . 
G 5 HOH   112 312 297  HOH   HOH B . 
G 5 HOH   113 313 1274 HOH   HOH B . 
G 5 HOH   114 314 311  HOH   HOH B . 
G 5 HOH   115 315 23   HOH   HOH B . 
G 5 HOH   116 316 161  HOH   HOH B . 
G 5 HOH   117 317 37   HOH   HOH B . 
G 5 HOH   118 318 215  HOH   HOH B . 
G 5 HOH   119 319 118  HOH   HOH B . 
G 5 HOH   120 320 1291 HOH   HOH B . 
G 5 HOH   121 321 170  HOH   HOH B . 
G 5 HOH   122 322 48   HOH   HOH B . 
G 5 HOH   123 323 182  HOH   HOH B . 
G 5 HOH   124 324 334  HOH   HOH B . 
G 5 HOH   125 325 28   HOH   HOH B . 
G 5 HOH   126 326 100  HOH   HOH B . 
G 5 HOH   127 327 44   HOH   HOH B . 
G 5 HOH   128 328 1285 HOH   HOH B . 
G 5 HOH   129 329 704  HOH   HOH B . 
G 5 HOH   130 330 29   HOH   HOH B . 
G 5 HOH   131 331 177  HOH   HOH B . 
G 5 HOH   132 332 1294 HOH   HOH B . 
G 5 HOH   133 333 207  HOH   HOH B . 
G 5 HOH   134 334 98   HOH   HOH B . 
G 5 HOH   135 335 445  HOH   HOH B . 
G 5 HOH   136 336 339  HOH   HOH B . 
G 5 HOH   137 337 55   HOH   HOH B . 
G 5 HOH   138 338 234  HOH   HOH B . 
G 5 HOH   139 339 1293 HOH   HOH B . 
G 5 HOH   140 340 717  HOH   HOH B . 
G 5 HOH   141 341 65   HOH   HOH B . 
G 5 HOH   142 342 619  HOH   HOH B . 
G 5 HOH   143 343 178  HOH   HOH B . 
G 5 HOH   144 344 90   HOH   HOH B . 
G 5 HOH   145 345 960  HOH   HOH B . 
G 5 HOH   146 346 1304 HOH   HOH B . 
G 5 HOH   147 347 335  HOH   HOH B . 
G 5 HOH   148 348 191  HOH   HOH B . 
G 5 HOH   149 349 362  HOH   HOH B . 
G 5 HOH   150 350 463  HOH   HOH B . 
G 5 HOH   151 351 1280 HOH   HOH B . 
G 5 HOH   152 352 623  HOH   HOH B . 
G 5 HOH   153 353 1046 HOH   HOH B . 
G 5 HOH   154 354 304  HOH   HOH B . 
G 5 HOH   155 355 541  HOH   HOH B . 
G 5 HOH   156 356 203  HOH   HOH B . 
G 5 HOH   157 357 290  HOH   HOH B . 
G 5 HOH   158 358 87   HOH   HOH B . 
G 5 HOH   159 359 479  HOH   HOH B . 
G 5 HOH   160 360 1077 HOH   HOH B . 
G 5 HOH   161 361 389  HOH   HOH B . 
G 5 HOH   162 362 718  HOH   HOH B . 
G 5 HOH   163 363 283  HOH   HOH B . 
G 5 HOH   164 364 1072 HOH   HOH B . 
G 5 HOH   165 365 340  HOH   HOH B . 
G 5 HOH   166 366 898  HOH   HOH B . 
G 5 HOH   167 367 1316 HOH   HOH B . 
G 5 HOH   168 368 373  HOH   HOH B . 
G 5 HOH   169 369 615  HOH   HOH B . 
G 5 HOH   170 370 1303 HOH   HOH B . 
G 5 HOH   171 371 291  HOH   HOH B . 
G 5 HOH   172 372 667  HOH   HOH B . 
G 5 HOH   173 373 310  HOH   HOH B . 
G 5 HOH   174 374 190  HOH   HOH B . 
G 5 HOH   175 375 431  HOH   HOH B . 
G 5 HOH   176 376 149  HOH   HOH B . 
G 5 HOH   177 377 1163 HOH   HOH B . 
G 5 HOH   178 378 1000 HOH   HOH B . 
G 5 HOH   179 379 1173 HOH   HOH B . 
G 5 HOH   180 380 183  HOH   HOH B . 
G 5 HOH   181 381 1311 HOH   HOH B . 
G 5 HOH   182 382 418  HOH   HOH B . 
G 5 HOH   183 383 176  HOH   HOH B . 
G 5 HOH   184 384 491  HOH   HOH B . 
G 5 HOH   185 385 424  HOH   HOH B . 
G 5 HOH   186 386 470  HOH   HOH B . 
G 5 HOH   187 387 981  HOH   HOH B . 
G 5 HOH   188 388 248  HOH   HOH B . 
G 5 HOH   189 389 265  HOH   HOH B . 
G 5 HOH   190 390 1298 HOH   HOH B . 
G 5 HOH   191 391 184  HOH   HOH B . 
G 5 HOH   192 392 360  HOH   HOH B . 
G 5 HOH   193 393 355  HOH   HOH B . 
G 5 HOH   194 394 410  HOH   HOH B . 
G 5 HOH   195 395 566  HOH   HOH B . 
G 5 HOH   196 396 792  HOH   HOH B . 
G 5 HOH   197 397 274  HOH   HOH B . 
G 5 HOH   198 398 157  HOH   HOH B . 
G 5 HOH   199 399 314  HOH   HOH B . 
G 5 HOH   200 400 321  HOH   HOH B . 
G 5 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HEH 
_cell.length_a           88.697 
_cell.length_b           88.697 
_cell.length_c           39.659 
_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                         7HEH 
_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          7HEH 
# 
_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   2023-05-24 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HEH 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.350 
_reflns.d_resolution_high            0.980 
_reflns.number_obs                   176265 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.042 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.100 
_reflns.B_iso_Wilson_estimate        11.080 
_reflns.pdbx_redundancy              6.200 
_reflns.pdbx_Rrim_I_all              0.046 
_reflns.pdbx_Rpim_I_all              0.018 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1086557 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 0.980 1.000  ? 27491 8324 ? 0.950 ? ? ? 3.300 ? 0.900  ? ? ? ? ? ? 95.300 1.125 0.579 0.612 
1 2 5.370 44.350 ? 8063  1166 ? 0.025 ? ? ? 6.900 ? 58.000 ? ? ? ? ? ? 99.800 0.027 0.010 0.999 
# 
_refine.entry_id                                 7HEH 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9800 
_refine.ls_d_res_low                             39.6700 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7000 
_refine.ls_number_reflns_obs                     176197 
_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                          0.1429 
_refine.ls_R_factor_R_work                       0.1423 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1538 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8487 
_refine.ls_number_reflns_R_work                  167710 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.2935 
_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                            0.1000 
_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                                62.050 
_refine.B_iso_min                                5.490 
_refine.pdbx_overall_phase_error                 16.3100 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9800 
_refine_hist.d_res_low                        39.6700 
_refine_hist.pdbx_number_atoms_ligand         56 
_refine_hist.number_atoms_solvent             439 
_refine_hist.number_atoms_total               3037 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           20.28 
_refine_hist.pdbx_B_iso_mean_solvent          28.44 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
0.9800 0.9900  30 94.0000  5294 . 0.3702 0.3797 . 276 0.0000 5570 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 98.0000  5461 . 0.3214 0.3260 . 270 0.0000 5731 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 100.0000 5534 . 0.2915 0.2643 . 265 0.0000 5799 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 100.0000 5623 . 0.2468 0.2615 . 256 0.0000 5879 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5532 . 0.2151 0.2162 . 293 0.0000 5825 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5554 . 0.1957 0.1959 . 320 0.0000 5874 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5546 . 0.1788 0.1907 . 303 0.0000 5849 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5588 . 0.1617 0.1784 . 252 0.0000 5840 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5600 . 0.1498 0.1734 . 290 0.0000 5890 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5571 . 0.1423 0.1747 . 296 0.0000 5867 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5612 . 0.1365 0.1539 . 245 0.0000 5857 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5605 . 0.1284 0.1364 . 267 0.0000 5872 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5545 . 0.1210 0.1418 . 285 0.0000 5830 . 'X-RAY DIFFRACTION' 
1.1800 1.2100  30 100.0000 5572 . 0.1162 0.1536 . 312 0.0000 5884 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5659 . 0.1149 0.1323 . 253 0.0000 5912 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5610 . 0.1176 0.1321 . 277 0.0000 5887 . 'X-RAY DIFFRACTION' 
1.2600 1.3000  30 100.0000 5541 . 0.1189 0.1322 . 296 0.0000 5837 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5604 . 0.1212 0.1286 . 301 0.0000 5905 . 'X-RAY DIFFRACTION' 
1.3300 1.3700  30 100.0000 5568 . 0.1253 0.1523 . 297 0.0000 5865 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5658 . 0.1191 0.1489 . 245 0.0000 5903 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5588 . 0.1199 0.1329 . 311 0.0000 5899 . 'X-RAY DIFFRACTION' 
1.4600 1.5200  30 100.0000 5584 . 0.1158 0.1305 . 264 0.0000 5848 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 5640 . 0.1156 0.1222 . 297 0.0000 5937 . 'X-RAY DIFFRACTION' 
1.5900 1.6800  30 100.0000 5589 . 0.1171 0.1375 . 282 0.0000 5871 . 'X-RAY DIFFRACTION' 
1.6800 1.7800  30 100.0000 5642 . 0.1267 0.1405 . 266 0.0000 5908 . 'X-RAY DIFFRACTION' 
1.7800 1.9200  30 100.0000 5579 . 0.1324 0.1350 . 301 0.0000 5880 . 'X-RAY DIFFRACTION' 
1.9200 2.1100  30 100.0000 5698 . 0.1364 0.1393 . 283 0.0000 5981 . 'X-RAY DIFFRACTION' 
2.1100 2.4200  30 100.0000 5584 . 0.1408 0.1372 . 310 0.0000 5894 . 'X-RAY DIFFRACTION' 
2.4200 3.0400  30 100.0000 5725 . 0.1518 0.1683 . 294 0.0000 6019 . 'X-RAY DIFFRACTION' 
3.0500 39.6700 30 100.0000 5804 . 0.1516 0.1668 . 280 0.0000 6084 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEH 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003675' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEH 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HEH A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEH 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 7HEH SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEH MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEH SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEH 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 LEU A 93  ? O LEU A 93  
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                   7HEH 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86 ? ? 55.22 -133.74 
2 1 HIS B 86 ? ? 57.23 -128.30 
# 
_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 536 ? 5.95 . 
2 1 O ? A HOH 537 ? 5.99 . 
3 1 O ? A HOH 538 ? 7.68 . 
4 1 O ? B HOH 401 ? 6.22 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 1 ? A SER 1 
2 1 Y 1 A MET 2 ? A MET 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1A9U N2   N Y N 1   
A1A9U C3   C Y N 2   
A1A9U C6   C Y N 3   
A1A9U C9   C N N 4   
A1A9U C12  C Y N 5   
A1A9U C14  C Y N 6   
A1A9U C1   C N N 7   
A1A9U C10  C Y N 8   
A1A9U C11  C Y N 9   
A1A9U C13  C Y N 10  
A1A9U C15  C Y N 11  
A1A9U C16  C Y N 12  
A1A9U C2   C Y N 13  
A1A9U C4   C Y N 14  
A1A9U C5   C Y N 15  
A1A9U C7   C N N 16  
A1A9U C8   C N R 17  
A1A9U N1   N N N 18  
A1A9U N3   N Y N 19  
A1A9U N4   N Y N 20  
A1A9U O1   O N N 21  
A1A9U H5   H N N 22  
A1A9U H10  H N N 23  
A1A9U H11  H N N 24  
A1A9U H15  H N N 25  
A1A9U H3   H N N 26  
A1A9U H2   H N N 27  
A1A9U H4   H N N 28  
A1A9U H14  H N N 29  
A1A9U H16  H N N 30  
A1A9U H18  H N N 31  
A1A9U H6   H N N 32  
A1A9U H7   H N N 33  
A1A9U H9   H N N 34  
A1A9U H8   H N N 35  
A1A9U H1   H N N 36  
A1A9U H13  H N N 37  
A1A9U H17  H N N 38  
A1A9U H12  H N N 39  
ALA   N    N N N 40  
ALA   CA   C N S 41  
ALA   C    C N N 42  
ALA   O    O N N 43  
ALA   CB   C N N 44  
ALA   OXT  O N N 45  
ALA   H    H N N 46  
ALA   H2   H N N 47  
ALA   HA   H N N 48  
ALA   HB1  H N N 49  
ALA   HB2  H N N 50  
ALA   HB3  H N N 51  
ALA   HXT  H N N 52  
ARG   N    N N N 53  
ARG   CA   C N S 54  
ARG   C    C N N 55  
ARG   O    O N N 56  
ARG   CB   C N N 57  
ARG   CG   C N N 58  
ARG   CD   C N N 59  
ARG   NE   N N N 60  
ARG   CZ   C N N 61  
ARG   NH1  N N N 62  
ARG   NH2  N N N 63  
ARG   OXT  O N N 64  
ARG   H    H N N 65  
ARG   H2   H N N 66  
ARG   HA   H N N 67  
ARG   HB2  H N N 68  
ARG   HB3  H N N 69  
ARG   HG2  H N N 70  
ARG   HG3  H N N 71  
ARG   HD2  H N N 72  
ARG   HD3  H N N 73  
ARG   HE   H N N 74  
ARG   HH11 H N N 75  
ARG   HH12 H N N 76  
ARG   HH21 H N N 77  
ARG   HH22 H N N 78  
ARG   HXT  H N N 79  
ASN   N    N N N 80  
ASN   CA   C N S 81  
ASN   C    C N N 82  
ASN   O    O N N 83  
ASN   CB   C N N 84  
ASN   CG   C N N 85  
ASN   OD1  O N N 86  
ASN   ND2  N N N 87  
ASN   OXT  O N N 88  
ASN   H    H N N 89  
ASN   H2   H N N 90  
ASN   HA   H N N 91  
ASN   HB2  H N N 92  
ASN   HB3  H N N 93  
ASN   HD21 H N N 94  
ASN   HD22 H N N 95  
ASN   HXT  H N N 96  
ASP   N    N N N 97  
ASP   CA   C N S 98  
ASP   C    C N N 99  
ASP   O    O N N 100 
ASP   CB   C N N 101 
ASP   CG   C N N 102 
ASP   OD1  O N N 103 
ASP   OD2  O N N 104 
ASP   OXT  O N N 105 
ASP   H    H N N 106 
ASP   H2   H N N 107 
ASP   HA   H N N 108 
ASP   HB2  H N N 109 
ASP   HB3  H N N 110 
ASP   HD2  H N N 111 
ASP   HXT  H N N 112 
CYS   N    N N N 113 
CYS   CA   C N R 114 
CYS   C    C N N 115 
CYS   O    O N N 116 
CYS   CB   C N N 117 
CYS   SG   S N N 118 
CYS   OXT  O N N 119 
CYS   H    H N N 120 
CYS   H2   H N N 121 
CYS   HA   H N N 122 
CYS   HB2  H N N 123 
CYS   HB3  H N N 124 
CYS   HG   H N N 125 
CYS   HXT  H N N 126 
DMS   S    S N N 127 
DMS   O    O N N 128 
DMS   C1   C N N 129 
DMS   C2   C N N 130 
DMS   H11  H N N 131 
DMS   H12  H N N 132 
DMS   H13  H N N 133 
DMS   H21  H N N 134 
DMS   H22  H N N 135 
DMS   H23  H N N 136 
GLN   N    N N N 137 
GLN   CA   C N S 138 
GLN   C    C N N 139 
GLN   O    O N N 140 
GLN   CB   C N N 141 
GLN   CG   C N N 142 
GLN   CD   C N N 143 
GLN   OE1  O N N 144 
GLN   NE2  N N N 145 
GLN   OXT  O N N 146 
GLN   H    H N N 147 
GLN   H2   H N N 148 
GLN   HA   H N N 149 
GLN   HB2  H N N 150 
GLN   HB3  H N N 151 
GLN   HG2  H N N 152 
GLN   HG3  H N N 153 
GLN   HE21 H N N 154 
GLN   HE22 H N N 155 
GLN   HXT  H N N 156 
GLU   N    N N N 157 
GLU   CA   C N S 158 
GLU   C    C N N 159 
GLU   O    O N N 160 
GLU   CB   C N N 161 
GLU   CG   C N N 162 
GLU   CD   C N N 163 
GLU   OE1  O N N 164 
GLU   OE2  O N N 165 
GLU   OXT  O N N 166 
GLU   H    H N N 167 
GLU   H2   H N N 168 
GLU   HA   H N N 169 
GLU   HB2  H N N 170 
GLU   HB3  H N N 171 
GLU   HG2  H N N 172 
GLU   HG3  H N N 173 
GLU   HE2  H N N 174 
GLU   HXT  H N N 175 
GLY   N    N N N 176 
GLY   CA   C N N 177 
GLY   C    C N N 178 
GLY   O    O N N 179 
GLY   OXT  O N N 180 
GLY   H    H N N 181 
GLY   H2   H N N 182 
GLY   HA2  H N N 183 
GLY   HA3  H N N 184 
GLY   HXT  H N N 185 
HIS   N    N N N 186 
HIS   CA   C N S 187 
HIS   C    C N N 188 
HIS   O    O N N 189 
HIS   CB   C N N 190 
HIS   CG   C Y N 191 
HIS   ND1  N Y N 192 
HIS   CD2  C Y N 193 
HIS   CE1  C Y N 194 
HIS   NE2  N Y N 195 
HIS   OXT  O N N 196 
HIS   H    H N N 197 
HIS   H2   H N N 198 
HIS   HA   H N N 199 
HIS   HB2  H N N 200 
HIS   HB3  H N N 201 
HIS   HD1  H N N 202 
HIS   HD2  H N N 203 
HIS   HE1  H N N 204 
HIS   HE2  H N N 205 
HIS   HXT  H N N 206 
HOH   O    O N N 207 
HOH   H1   H N N 208 
HOH   H2   H N N 209 
ILE   N    N N N 210 
ILE   CA   C N S 211 
ILE   C    C N N 212 
ILE   O    O N N 213 
ILE   CB   C N S 214 
ILE   CG1  C N N 215 
ILE   CG2  C N N 216 
ILE   CD1  C N N 217 
ILE   OXT  O N N 218 
ILE   H    H N N 219 
ILE   H2   H N N 220 
ILE   HA   H N N 221 
ILE   HB   H N N 222 
ILE   HG12 H N N 223 
ILE   HG13 H N N 224 
ILE   HG21 H N N 225 
ILE   HG22 H N N 226 
ILE   HG23 H N N 227 
ILE   HD11 H N N 228 
ILE   HD12 H N N 229 
ILE   HD13 H N N 230 
ILE   HXT  H N N 231 
LEU   N    N N N 232 
LEU   CA   C N S 233 
LEU   C    C N N 234 
LEU   O    O N N 235 
LEU   CB   C N N 236 
LEU   CG   C N N 237 
LEU   CD1  C N N 238 
LEU   CD2  C N N 239 
LEU   OXT  O N N 240 
LEU   H    H N N 241 
LEU   H2   H N N 242 
LEU   HA   H N N 243 
LEU   HB2  H N N 244 
LEU   HB3  H N N 245 
LEU   HG   H N N 246 
LEU   HD11 H N N 247 
LEU   HD12 H N N 248 
LEU   HD13 H N N 249 
LEU   HD21 H N N 250 
LEU   HD22 H N N 251 
LEU   HD23 H N N 252 
LEU   HXT  H N N 253 
LYS   N    N N N 254 
LYS   CA   C N S 255 
LYS   C    C N N 256 
LYS   O    O N N 257 
LYS   CB   C N N 258 
LYS   CG   C N N 259 
LYS   CD   C N N 260 
LYS   CE   C N N 261 
LYS   NZ   N N N 262 
LYS   OXT  O N N 263 
LYS   H    H N N 264 
LYS   H2   H N N 265 
LYS   HA   H N N 266 
LYS   HB2  H N N 267 
LYS   HB3  H N N 268 
LYS   HG2  H N N 269 
LYS   HG3  H N N 270 
LYS   HD2  H N N 271 
LYS   HD3  H N N 272 
LYS   HE2  H N N 273 
LYS   HE3  H N N 274 
LYS   HZ1  H N N 275 
LYS   HZ2  H N N 276 
LYS   HZ3  H N N 277 
LYS   HXT  H N N 278 
MET   N    N N N 279 
MET   CA   C N S 280 
MET   C    C N N 281 
MET   O    O N N 282 
MET   CB   C N N 283 
MET   CG   C N N 284 
MET   SD   S N N 285 
MET   CE   C N N 286 
MET   OXT  O N N 287 
MET   H    H N N 288 
MET   H2   H N N 289 
MET   HA   H N N 290 
MET   HB2  H N N 291 
MET   HB3  H N N 292 
MET   HG2  H N N 293 
MET   HG3  H N N 294 
MET   HE1  H N N 295 
MET   HE2  H N N 296 
MET   HE3  H N N 297 
MET   HXT  H N N 298 
PHE   N    N N N 299 
PHE   CA   C N S 300 
PHE   C    C N N 301 
PHE   O    O N N 302 
PHE   CB   C N N 303 
PHE   CG   C Y N 304 
PHE   CD1  C Y N 305 
PHE   CD2  C Y N 306 
PHE   CE1  C Y N 307 
PHE   CE2  C Y N 308 
PHE   CZ   C Y N 309 
PHE   OXT  O N N 310 
PHE   H    H N N 311 
PHE   H2   H N N 312 
PHE   HA   H N N 313 
PHE   HB2  H N N 314 
PHE   HB3  H N N 315 
PHE   HD1  H N N 316 
PHE   HD2  H N N 317 
PHE   HE1  H N N 318 
PHE   HE2  H N N 319 
PHE   HZ   H N N 320 
PHE   HXT  H N N 321 
PRO   N    N N N 322 
PRO   CA   C N S 323 
PRO   C    C N N 324 
PRO   O    O N N 325 
PRO   CB   C N N 326 
PRO   CG   C N N 327 
PRO   CD   C N N 328 
PRO   OXT  O N N 329 
PRO   H    H N N 330 
PRO   HA   H N N 331 
PRO   HB2  H N N 332 
PRO   HB3  H N N 333 
PRO   HG2  H N N 334 
PRO   HG3  H N N 335 
PRO   HD2  H N N 336 
PRO   HD3  H N N 337 
PRO   HXT  H N N 338 
SER   N    N N N 339 
SER   CA   C N S 340 
SER   C    C N N 341 
SER   O    O N N 342 
SER   CB   C N N 343 
SER   OG   O N N 344 
SER   OXT  O N N 345 
SER   H    H N N 346 
SER   H2   H N N 347 
SER   HA   H N N 348 
SER   HB2  H N N 349 
SER   HB3  H N N 350 
SER   HG   H N N 351 
SER   HXT  H N N 352 
TFA   C1   C N N 353 
TFA   C2   C N N 354 
TFA   O    O N N 355 
TFA   F1   F N N 356 
TFA   F2   F N N 357 
TFA   F3   F N N 358 
TFA   OXT  O N N 359 
TFA   HXT  H N N 360 
THR   N    N N N 361 
THR   CA   C N S 362 
THR   C    C N N 363 
THR   O    O N N 364 
THR   CB   C N R 365 
THR   OG1  O N N 366 
THR   CG2  C N N 367 
THR   OXT  O N N 368 
THR   H    H N N 369 
THR   H2   H N N 370 
THR   HA   H N N 371 
THR   HB   H N N 372 
THR   HG1  H N N 373 
THR   HG21 H N N 374 
THR   HG22 H N N 375 
THR   HG23 H N N 376 
THR   HXT  H N N 377 
TYR   N    N N N 378 
TYR   CA   C N S 379 
TYR   C    C N N 380 
TYR   O    O N N 381 
TYR   CB   C N N 382 
TYR   CG   C Y N 383 
TYR   CD1  C Y N 384 
TYR   CD2  C Y N 385 
TYR   CE1  C Y N 386 
TYR   CE2  C Y N 387 
TYR   CZ   C Y N 388 
TYR   OH   O N N 389 
TYR   OXT  O N N 390 
TYR   H    H N N 391 
TYR   H2   H N N 392 
TYR   HA   H N N 393 
TYR   HB2  H N N 394 
TYR   HB3  H N N 395 
TYR   HD1  H N N 396 
TYR   HD2  H N N 397 
TYR   HE1  H N N 398 
TYR   HE2  H N N 399 
TYR   HH   H N N 400 
TYR   HXT  H N N 401 
VAL   N    N N N 402 
VAL   CA   C N S 403 
VAL   C    C N N 404 
VAL   O    O N N 405 
VAL   CB   C N N 406 
VAL   CG1  C N N 407 
VAL   CG2  C N N 408 
VAL   OXT  O N N 409 
VAL   H    H N N 410 
VAL   H2   H N N 411 
VAL   HA   H N N 412 
VAL   HB   H N N 413 
VAL   HG11 H N N 414 
VAL   HG12 H N N 415 
VAL   HG13 H N N 416 
VAL   HG21 H N N 417 
VAL   HG22 H N N 418 
VAL   HG23 H N N 419 
VAL   HXT  H N N 420 
# 
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 
A1A9U C1  C2   sing N N 1   
A1A9U C3  C2   doub Y N 2   
A1A9U C3  C4   sing Y N 3   
A1A9U C2  C16  sing Y N 4   
A1A9U C4  C5   doub Y N 5   
A1A9U C16 C6   doub Y N 6   
A1A9U C5  C6   sing Y N 7   
A1A9U C6  C7   sing N N 8   
A1A9U C7  C8   sing N N 9   
A1A9U C8  C9   sing N N 10  
A1A9U C8  N1   sing N N 11  
A1A9U O1  C9   sing N N 12  
A1A9U N1  C10  sing N N 13  
A1A9U C10 C13  doub Y N 14  
A1A9U C10 N2   sing Y N 15  
A1A9U C14 C13  sing Y N 16  
A1A9U C14 C15  doub Y N 17  
A1A9U C13 C12  sing Y N 18  
A1A9U N2  C11  doub Y N 19  
A1A9U C15 N4   sing Y N 20  
A1A9U C12 N4   sing Y N 21  
A1A9U C12 N3   doub Y N 22  
A1A9U C11 N3   sing Y N 23  
A1A9U C3  H5   sing N N 24  
A1A9U C9  H10  sing N N 25  
A1A9U C9  H11  sing N N 26  
A1A9U C14 H15  sing N N 27  
A1A9U C1  H3   sing N N 28  
A1A9U C1  H2   sing N N 29  
A1A9U C1  H4   sing N N 30  
A1A9U C11 H14  sing N N 31  
A1A9U C15 H16  sing N N 32  
A1A9U C16 H18  sing N N 33  
A1A9U C4  H6   sing N N 34  
A1A9U C5  H7   sing N N 35  
A1A9U C7  H9   sing N N 36  
A1A9U C7  H8   sing N N 37  
A1A9U C8  H1   sing N N 38  
A1A9U N1  H13  sing N N 39  
A1A9U N4  H17  sing N N 40  
A1A9U O1  H12  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
TFA   C1  C2   sing N N 340 
TFA   C1  O    doub N N 341 
TFA   C1  OXT  sing N N 342 
TFA   C2  F1   sing N N 343 
TFA   C2  F2   sing N N 344 
TFA   C2  F3   sing N N 345 
TFA   OXT HXT  sing N N 346 
THR   N   CA   sing N N 347 
THR   N   H    sing N N 348 
THR   N   H2   sing N N 349 
THR   CA  C    sing N N 350 
THR   CA  CB   sing N N 351 
THR   CA  HA   sing N N 352 
THR   C   O    doub N N 353 
THR   C   OXT  sing N N 354 
THR   CB  OG1  sing N N 355 
THR   CB  CG2  sing N N 356 
THR   CB  HB   sing N N 357 
THR   OG1 HG1  sing N N 358 
THR   CG2 HG21 sing N N 359 
THR   CG2 HG22 sing N N 360 
THR   CG2 HG23 sing N N 361 
THR   OXT HXT  sing N N 362 
TYR   N   CA   sing N N 363 
TYR   N   H    sing N N 364 
TYR   N   H2   sing N N 365 
TYR   CA  C    sing N N 366 
TYR   CA  CB   sing N N 367 
TYR   CA  HA   sing N N 368 
TYR   C   O    doub N N 369 
TYR   C   OXT  sing N N 370 
TYR   CB  CG   sing N N 371 
TYR   CB  HB2  sing N N 372 
TYR   CB  HB3  sing N N 373 
TYR   CG  CD1  doub Y N 374 
TYR   CG  CD2  sing Y N 375 
TYR   CD1 CE1  sing Y N 376 
TYR   CD1 HD1  sing N N 377 
TYR   CD2 CE2  doub Y N 378 
TYR   CD2 HD2  sing N N 379 
TYR   CE1 CZ   doub Y N 380 
TYR   CE1 HE1  sing N N 381 
TYR   CE2 CZ   sing Y N 382 
TYR   CE2 HE2  sing N N 383 
TYR   CZ  OH   sing N N 384 
TYR   OH  HH   sing N N 385 
TYR   OXT HXT  sing N N 386 
VAL   N   CA   sing N N 387 
VAL   N   H    sing N N 388 
VAL   N   H2   sing N N 389 
VAL   CA  C    sing N N 390 
VAL   CA  CB   sing N N 391 
VAL   CA  HA   sing N N 392 
VAL   C   O    doub N N 393 
VAL   C   OXT  sing N N 394 
VAL   CB  CG1  sing N N 395 
VAL   CB  CG2  sing N N 396 
VAL   CB  HB   sing N N 397 
VAL   CG1 HG11 sing N N 398 
VAL   CG1 HG12 sing N N 399 
VAL   CG1 HG13 sing N N 400 
VAL   CG2 HG21 sing N N 401 
VAL   CG2 HG22 sing N N 402 
VAL   CG2 HG23 sing N N 403 
VAL   OXT HXT  sing N N 404 
# 
_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                    7HEH 
_atom_sites.fract_transf_matrix[1][1]   0.011274 
_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]   0.011274 
_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]   0.025215 
_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   ? 19.625 -16.129 22.247  0.40 47.52 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.561 -16.089 22.415  0.60 47.87 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.643 -15.066 22.423  0.40 47.25 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.594 -15.006 22.554  0.60 47.57 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.286 -13.707 22.160  0.40 45.95 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.250 -13.667 22.238  0.60 46.14 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.407 -13.445 22.597  0.40 46.19 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.354 -13.383 22.704  0.60 46.42 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 17.998 -15.127 23.823  0.40 48.02 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 17.956 -15.003 23.959  0.60 48.40 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 16.943 -14.039 23.974  0.40 48.35 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.928 -13.886 24.076  0.60 48.76 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.390 -16.502 24.068  0.40 48.33 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.320 -16.353 24.258  0.60 48.71 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.934 -15.184 21.774  0.40 56.70 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.881 -15.139 21.915  0.60 57.07 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.681 -14.978 24.495  0.40 57.61 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.646 -14.846 24.623  0.60 58.07 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.445 -14.196 24.792  0.40 58.01 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.418 -14.012 24.892  0.60 58.51 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.380 -13.175 24.014  0.40 58.01 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.388 -13.033 24.104  0.60 58.51 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.343 -14.074 23.212  0.40 58.01 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.336 -13.921 23.309  0.60 58.51 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.918 -16.492 24.915  0.40 57.99 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.858 -16.303 25.110  0.60 58.45 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.773 -16.707 23.348  0.40 57.99 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.690 -16.567 23.552  0.60 58.45 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.100 -17.162 24.093  0.40 57.99 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.015 -17.028 24.297  0.60 58.45 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.570 -12.850 21.434  1.00 43.99 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.018 -11.497 21.121  1.00 39.79 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 17.878 -10.519 21.396  1.00 36.24 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.779 -10.911 21.803  1.00 36.26 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.561 -11.387 19.688  1.00 39.01 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.550 -11.799 18.641  1.00 38.19 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.426 -11.298 18.615  1.00 37.85 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 18.948 -12.719 17.767  1.00 37.86 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.798 -13.037 21.105  0.40 52.78 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.832 -13.066 21.049  0.60 52.78 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.746 -11.273 21.717  1.00 47.74 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 19.812 -10.465 19.516  1.00 46.81 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.336 -11.962 19.600  1.00 46.81 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.414 -12.989 17.150  1.00 45.43 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.744 -13.045 17.818  1.00 45.43 ?  4   ASN   A HD22 1 
ATOM   46   N N    A SER   A 1 5   ? 18.143 -9.233  21.167  0.40 34.56 ?  5   SER   A N    1 
ATOM   47   N N    B SER   A 1 5   ? 18.145 -9.234  21.163  0.60 34.44 ?  5   SER   A N    1 
ATOM   48   C CA   A SER   A 1 5   ? 17.222 -8.165  21.535  0.40 32.89 ?  5   SER   A CA   1 
ATOM   49   C CA   B SER   A 1 5   ? 17.228 -8.162  21.530  0.60 32.74 ?  5   SER   A CA   1 
ATOM   50   C C    A SER   A 1 5   ? 16.355 -7.686  20.373  0.40 30.43 ?  5   SER   A C    1 
ATOM   51   C C    B SER   A 1 5   ? 16.375 -7.672  20.364  0.60 30.31 ?  5   SER   A C    1 
ATOM   52   O O    A SER   A 1 5   ? 15.664 -6.672  20.511  0.40 30.60 ?  5   SER   A O    1 
ATOM   53   O O    B SER   A 1 5   ? 15.712 -6.638  20.489  0.60 30.47 ?  5   SER   A O    1 
ATOM   54   C CB   A SER   A 1 5   ? 17.986 -6.986  22.144  0.40 33.45 ?  5   SER   A CB   1 
ATOM   55   C CB   B SER   A 1 5   ? 17.999 -6.994  22.151  0.60 33.29 ?  5   SER   A CB   1 
ATOM   56   O OG   A SER   A 1 5   ? 18.984 -6.508  21.259  0.40 33.85 ?  5   SER   A OG   1 
ATOM   57   O OG   B SER   A 1 5   ? 18.900 -6.421  21.220  0.60 33.70 ?  5   SER   A OG   1 
ATOM   58   H H    A SER   A 1 5   ? 18.863 -8.954  20.789  0.40 41.47 ?  5   SER   A H    1 
ATOM   59   H H    B SER   A 1 5   ? 18.864 -8.959  20.781  0.60 41.32 ?  5   SER   A H    1 
ATOM   60   H HA   A SER   A 1 5   ? 16.627 -8.501  22.221  0.40 39.46 ?  5   SER   A HA   1 
ATOM   61   H HA   B SER   A 1 5   ? 16.626 -8.497  22.210  0.60 39.28 ?  5   SER   A HA   1 
ATOM   62   H HB2  A SER   A 1 5   ? 17.360 -6.266  22.329  0.40 40.14 ?  5   SER   A HB2  1 
ATOM   63   H HB2  B SER   A 1 5   ? 17.367 -6.314  22.435  0.60 39.94 ?  5   SER   A HB2  1 
ATOM   64   H HB3  A SER   A 1 5   ? 18.406 -7.274  22.971  0.40 40.14 ?  5   SER   A HB3  1 
ATOM   65   H HB3  B SER   A 1 5   ? 18.500 -7.317  22.918  0.60 39.94 ?  5   SER   A HB3  1 
ATOM   66   H HG   A SER   A 1 5   ? 19.395 -5.863  21.611  0.40 40.61 ?  5   SER   A HG   1 
ATOM   67   H HG   B SER   A 1 5   ? 19.316 -5.782  21.578  0.60 40.43 ?  5   SER   A HG   1 
ATOM   68   N N    . PHE   A 1 6   ? 16.371 -8.382  19.238  1.00 27.73 ?  6   PHE   A N    1 
ATOM   69   C CA   . PHE   A 1 6   ? 15.480 -8.026  18.139  1.00 23.36 ?  6   PHE   A CA   1 
ATOM   70   C C    . PHE   A 1 6   ? 14.046 -8.396  18.513  1.00 22.62 ?  6   PHE   A C    1 
ATOM   71   O O    . PHE   A 1 6   ? 13.792 -9.490  19.021  1.00 23.62 ?  6   PHE   A O    1 
ATOM   72   C CB   . PHE   A 1 6   ? 15.895 -8.757  16.864  1.00 20.54 ?  6   PHE   A CB   1 
ATOM   73   C CG   . PHE   A 1 6   ? 17.181 -8.245  16.255  1.00 18.94 ?  6   PHE   A CG   1 
ATOM   74   C CD1  . PHE   A 1 6   ? 17.196 -7.071  15.522  1.00 18.44 ?  6   PHE   A CD1  1 
ATOM   75   C CD2  . PHE   A 1 6   ? 18.364 -8.946  16.410  1.00 19.52 ?  6   PHE   A CD2  1 
ATOM   76   C CE1  . PHE   A 1 6   ? 18.368 -6.603  14.958  1.00 18.47 ?  6   PHE   A CE1  1 
ATOM   77   C CE2  . PHE   A 1 6   ? 19.538 -8.485  15.846  1.00 19.67 ?  6   PHE   A CE2  1 
ATOM   78   C CZ   . PHE   A 1 6   ? 19.539 -7.311  15.121  1.00 19.03 ?  6   PHE   A CZ   1 
ATOM   79   H H    A PHE   A 1 6   ? 16.881 -9.058  19.084  0.40 33.26 ?  6   PHE   A H    1 
ATOM   80   H H    B PHE   A 1 6   ? 16.866 -9.071  19.091  0.60 33.26 ?  6   PHE   A H    1 
ATOM   81   H HA   . PHE   A 1 6   ? 15.519 -7.076  17.985  1.00 28.03 ?  6   PHE   A HA   1 
ATOM   82   H HB2  . PHE   A 1 6   ? 16.012 -9.702  17.072  1.00 24.64 ?  6   PHE   A HB2  1 
ATOM   83   H HB3  . PHE   A 1 6   ? 15.188 -8.657  16.208  1.00 24.64 ?  6   PHE   A HB3  1 
ATOM   84   H HD1  . PHE   A 1 6   ? 16.404 -6.595  15.412  1.00 22.11 ?  6   PHE   A HD1  1 
ATOM   85   H HD2  . PHE   A 1 6   ? 18.365 -9.742  16.902  1.00 23.42 ?  6   PHE   A HD2  1 
ATOM   86   H HE1  . PHE   A 1 6   ? 18.366 -5.814  14.469  1.00 22.15 ?  6   PHE   A HE1  1 
ATOM   87   H HE2  . PHE   A 1 6   ? 20.327 -8.963  15.960  1.00 23.60 ?  6   PHE   A HE2  1 
ATOM   88   H HZ   . PHE   A 1 6   ? 20.328 -6.997  14.743  1.00 22.83 ?  6   PHE   A HZ   1 
ATOM   89   N N    A SER   A 1 7   ? 13.107 -7.483  18.259  0.40 22.38 ?  7   SER   A N    1 
ATOM   90   N N    B SER   A 1 7   ? 13.108 -7.483  18.256  0.60 21.71 ?  7   SER   A N    1 
ATOM   91   C CA   A SER   A 1 7   ? 11.736 -7.624  18.736  0.40 22.54 ?  7   SER   A CA   1 
ATOM   92   C CA   B SER   A 1 7   ? 11.743 -7.602  18.754  0.60 21.92 ?  7   SER   A CA   1 
ATOM   93   C C    A SER   A 1 7   ? 10.739 -7.356  17.616  0.40 20.87 ?  7   SER   A C    1 
ATOM   94   C C    B SER   A 1 7   ? 10.731 -7.354  17.642  0.60 20.07 ?  7   SER   A C    1 
ATOM   95   O O    A SER   A 1 7   ? 10.962 -6.487  16.766  0.40 21.02 ?  7   SER   A O    1 
ATOM   96   O O    B SER   A 1 7   ? 10.911 -6.456  16.813  0.60 20.24 ?  7   SER   A O    1 
ATOM   97   C CB   A SER   A 1 7   ? 11.467 -6.662  19.906  0.40 24.16 ?  7   SER   A CB   1 
ATOM   98   C CB   B SER   A 1 7   ? 11.501 -6.596  19.891  0.60 23.97 ?  7   SER   A CB   1 
ATOM   99   O OG   A SER   A 1 7   ? 10.130 -6.773  20.364  0.40 25.32 ?  7   SER   A OG   1 
ATOM   100  O OG   B SER   A 1 7   ? 10.149 -6.608  20.310  0.60 25.56 ?  7   SER   A OG   1 
ATOM   101  H H    A SER   A 1 7   ? 13.245 -6.768  17.801  0.40 26.85 ?  7   SER   A H    1 
ATOM   102  H H    B SER   A 1 7   ? 13.245 -6.777  17.785  0.60 26.05 ?  7   SER   A H    1 
ATOM   103  H HA   A SER   A 1 7   ? 11.594 -8.526  19.054  0.40 27.04 ?  7   SER   A HA   1 
ATOM   104  H HA   B SER   A 1 7   ? 11.599 -8.495  19.103  0.60 26.30 ?  7   SER   A HA   1 
ATOM   105  H HB2  A SER   A 1 7   ? 12.066 -6.881  20.639  0.40 28.99 ?  7   SER   A HB2  1 
ATOM   106  H HB2  B SER   A 1 7   ? 12.074 -6.825  20.642  0.60 28.75 ?  7   SER   A HB2  1 
ATOM   107  H HB3  A SER   A 1 7   ? 11.627 -5.751  19.612  0.40 28.99 ?  7   SER   A HB3  1 
ATOM   108  H HB3  B SER   A 1 7   ? 11.712 -5.705  19.575  0.60 28.75 ?  7   SER   A HB3  1 
ATOM   109  H HG   A SER   A 1 7   ? 9.999  -6.239  21.000  0.40 30.37 ?  7   SER   A HG   1 
ATOM   110  H HG   B SER   A 1 7   ? 10.036 -6.070  20.944  0.60 30.66 ?  7   SER   A HG   1 
ATOM   111  N N    A GLY   A 1 8   ? 9.636  -8.107  17.625  0.40 19.36 ?  8   GLY   A N    1 
ATOM   112  N N    B GLY   A 1 8   ? 9.660  -8.149  17.638  0.60 18.74 ?  8   GLY   A N    1 
ATOM   113  C CA   A GLY   A 1 8   ? 8.542  -7.884  16.702  0.40 18.05 ?  8   GLY   A CA   1 
ATOM   114  C CA   B GLY   A 1 8   ? 8.558  -7.914  16.727  0.60 17.75 ?  8   GLY   A CA   1 
ATOM   115  C C    A GLY   A 1 8   ? 8.739  -8.424  15.304  0.40 16.63 ?  8   GLY   A C    1 
ATOM   116  C C    B GLY   A 1 8   ? 8.777  -8.385  15.310  0.60 16.44 ?  8   GLY   A C    1 
ATOM   117  O O    A GLY   A 1 8   ? 7.962  -8.072  14.410  0.40 16.97 ?  8   GLY   A O    1 
ATOM   118  O O    B GLY   A 1 8   ? 8.068  -7.937  14.406  0.60 16.97 ?  8   GLY   A O    1 
ATOM   119  H H    A GLY   A 1 8   ? 9.503  -8.757  18.173  0.40 23.23 ?  8   GLY   A H    1 
ATOM   120  H H    B GLY   A 1 8   ? 9.557  -8.828  18.156  0.60 22.48 ?  8   GLY   A H    1 
ATOM   121  H HA2  A GLY   A 1 8   ? 7.740  -8.294  17.067  0.40 21.65 ?  8   GLY   A HA2  1 
ATOM   122  H HA2  B GLY   A 1 8   ? 7.770  -8.360  17.075  0.60 21.29 ?  8   GLY   A HA2  1 
ATOM   123  H HA3  A GLY   A 1 8   ? 8.380  -6.929  16.636  0.40 21.65 ?  8   GLY   A HA3  1 
ATOM   124  H HA3  B GLY   A 1 8   ? 8.374  -6.961  16.704  0.60 21.29 ?  8   GLY   A HA3  1 
ATOM   125  N N    . TYR   A 1 9   ? 9.744  -9.267  15.080  1.00 15.50 ?  9   TYR   A N    1 
ATOM   126  C CA   . TYR   A 1 9   ? 10.001 -9.790  13.748  1.00 13.64 ?  9   TYR   A CA   1 
ATOM   127  C C    . TYR   A 1 9   ? 9.145  -11.013 13.449  1.00 12.94 ?  9   TYR   A C    1 
ATOM   128  O O    . TYR   A 1 9   ? 8.873  -11.842 14.326  1.00 14.73 ?  9   TYR   A O    1 
ATOM   129  C CB   . TYR   A 1 9   ? 11.478 -10.170 13.576  1.00 13.88 ?  9   TYR   A CB   1 
ATOM   130  C CG   . TYR   A 1 9   ? 12.393 -8.978  13.407  1.00 14.26 ?  9   TYR   A CG   1 
ATOM   131  C CD1  . TYR   A 1 9   ? 12.724 -8.181  14.489  1.00 14.97 ?  9   TYR   A CD1  1 
ATOM   132  C CD2  . TYR   A 1 9   ? 12.908 -8.635  12.163  1.00 13.75 ?  9   TYR   A CD2  1 
ATOM   133  C CE1  . TYR   A 1 9   ? 13.544 -7.072  14.343  1.00 15.31 ?  9   TYR   A CE1  1 
ATOM   134  C CE2  . TYR   A 1 9   ? 13.729 -7.528  12.005  1.00 13.93 ?  9   TYR   A CE2  1 
ATOM   135  C CZ   . TYR   A 1 9   ? 14.041 -6.747  13.096  1.00 14.92 ?  9   TYR   A CZ   1 
ATOM   136  O OH   . TYR   A 1 9   ? 14.848 -5.644  12.944  1.00 16.18 ?  9   TYR   A OH   1 
ATOM   137  H H    A TYR   A 1 9   ? 10.282 -9.552  15.683  0.40 18.60 ?  9   TYR   A H    1 
ATOM   138  H H    B TYR   A 1 9   ? 10.264 -9.580  15.685  0.60 18.60 ?  9   TYR   A H    1 
ATOM   139  H HA   . TYR   A 1 9   ? 9.797  -9.103  13.091  1.00 16.36 ?  9   TYR   A HA   1 
ATOM   140  H HB2  . TYR   A 1 9   ? 11.774 -10.675 14.350  1.00 16.65 ?  9   TYR   A HB2  1 
ATOM   141  H HB3  . TYR   A 1 9   ? 11.548 -10.714 12.778  1.00 16.65 ?  9   TYR   A HB3  1 
ATOM   142  H HD1  . TYR   A 1 9   ? 12.381 -8.394  15.330  1.00 17.96 ?  9   TYR   A HD1  1 
ATOM   143  H HD2  . TYR   A 1 9   ? 12.695 -9.159  11.421  1.00 16.50 ?  9   TYR   A HD2  1 
ATOM   144  H HE1  . TYR   A 1 9   ? 13.750 -6.551  15.082  1.00 18.36 ?  9   TYR   A HE1  1 
ATOM   145  H HE2  . TYR   A 1 9   ? 14.066 -7.316  11.164  1.00 16.71 ?  9   TYR   A HE2  1 
ATOM   146  H HH   . TYR   A 1 9   ? 14.962 -5.277  13.691  1.00 19.41 ?  9   TYR   A HH   1 
ATOM   147  N N    A LEU   A 1 10  ? 8.701  -11.104 12.202  0.40 12.45 ?  10  LEU   A N    1 
ATOM   148  N N    B LEU   A 1 10  ? 8.738  -11.128 12.188  0.60 12.55 ?  10  LEU   A N    1 
ATOM   149  C CA   A LEU   A 1 10  ? 8.128  -12.333 11.690  0.40 12.12 ?  10  LEU   A CA   1 
ATOM   150  C CA   B LEU   A 1 10  ? 8.118  -12.334 11.663  0.60 12.36 ?  10  LEU   A CA   1 
ATOM   151  C C    A LEU   A 1 10  ? 9.265  -13.267 11.290  0.40 11.84 ?  10  LEU   A C    1 
ATOM   152  C C    B LEU   A 1 10  ? 9.218  -13.288 11.208  0.60 12.24 ?  10  LEU   A C    1 
ATOM   153  O O    A LEU   A 1 10  ? 10.243 -12.843 10.668  0.40 11.55 ?  10  LEU   A O    1 
ATOM   154  O O    B LEU   A 1 10  ? 10.122 -12.892 10.466  0.60 12.38 ?  10  LEU   A O    1 
ATOM   155  C CB   A LEU   A 1 10  ? 7.267  -12.014 10.469  0.40 12.65 ?  10  LEU   A CB   1 
ATOM   156  C CB   B LEU   A 1 10  ? 7.207  -11.964 10.492  0.60 13.30 ?  10  LEU   A CB   1 
ATOM   157  C CG   A LEU   A 1 10  ? 6.564  -13.209 9.830   0.40 13.54 ?  10  LEU   A CG   1 
ATOM   158  C CG   B LEU   A 1 10  ? 6.733  -13.107 9.590   0.60 14.62 ?  10  LEU   A CG   1 
ATOM   159  C CD1  A LEU   A 1 10  ? 5.504  -13.756 10.767  0.40 13.62 ?  10  LEU   A CD1  1 
ATOM   160  C CD1  B LEU   A 1 10  ? 5.822  -14.058 10.348  0.60 15.67 ?  10  LEU   A CD1  1 
ATOM   161  C CD2  A LEU   A 1 10  ? 5.963  -12.825 8.487   0.40 14.32 ?  10  LEU   A CD2  1 
ATOM   162  C CD2  B LEU   A 1 10  ? 6.042  -12.560 8.353   0.60 15.37 ?  10  LEU   A CD2  1 
ATOM   163  H H    A LEU   A 1 10  ? 8.722  -10.454 11.627  0.40 14.93 ?  10  LEU   A H    1 
ATOM   164  H H    B LEU   A 1 10  ? 8.819  -10.496 11.601  0.60 15.05 ?  10  LEU   A H    1 
ATOM   165  H HA   A LEU   A 1 10  ? 7.576  -12.749 12.375  0.40 14.54 ?  10  LEU   A HA   1 
ATOM   166  H HA   B LEU   A 1 10  ? 7.593  -12.760 12.354  0.60 14.83 ?  10  LEU   A HA   1 
ATOM   167  H HB2  A LEU   A 1 10  ? 6.579  -11.379 10.732  0.40 15.17 ?  10  LEU   A HB2  1 
ATOM   168  H HB2  B LEU   A 1 10  ? 6.409  -11.538 10.855  0.60 15.95 ?  10  LEU   A HB2  1 
ATOM   169  H HB3  A LEU   A 1 10  ? 7.834  -11.613 9.794   0.40 15.17 ?  10  LEU   A HB3  1 
ATOM   170  H HB3  B LEU   A 1 10  ? 7.673  -11.330 9.929   0.60 15.95 ?  10  LEU   A HB3  1 
ATOM   171  H HG   A LEU   A 1 10  ? 7.215  -13.911 9.675   0.40 16.24 ?  10  LEU   A HG   1 
ATOM   172  H HG   B LEU   A 1 10  ? 7.502  -13.613 9.292   0.60 17.54 ?  10  LEU   A HG   1 
ATOM   173  H HD11 A LEU   A 1 10  ? 5.051  -14.495 10.332  0.40 16.34 ?  10  LEU   A HD11 1 
ATOM   174  H HD11 B LEU   A 1 10  ? 5.581  -14.794 9.764   0.60 18.80 ?  10  LEU   A HD11 1 
ATOM   175  H HD12 A LEU   A 1 10  ? 5.929  -14.064 11.583  0.40 16.34 ?  10  LEU   A HD12 1 
ATOM   176  H HD12 B LEU   A 1 10  ? 6.293  -14.395 11.127  0.60 18.80 ?  10  LEU   A HD12 1 
ATOM   177  H HD13 A LEU   A 1 10  ? 4.869  -13.052 10.971  0.40 16.34 ?  10  LEU   A HD13 1 
ATOM   178  H HD13 B LEU   A 1 10  ? 5.025  -13.580 10.626  0.60 18.80 ?  10  LEU   A HD13 1 
ATOM   179  H HD21 A LEU   A 1 10  ? 5.527  -13.602 8.106   0.40 17.17 ?  10  LEU   A HD21 1 
ATOM   180  H HD21 B LEU   A 1 10  ? 5.754  -13.307 7.804   0.60 18.44 ?  10  LEU   A HD21 1 
ATOM   181  H HD22 A LEU   A 1 10  ? 5.321  -12.113 8.621   0.40 17.17 ?  10  LEU   A HD22 1 
ATOM   182  H HD22 B LEU   A 1 10  ? 5.276  -12.035 8.627   0.60 18.44 ?  10  LEU   A HD22 1 
ATOM   183  H HD23 A LEU   A 1 10  ? 6.676  -12.524 7.900   0.40 17.17 ?  10  LEU   A HD23 1 
ATOM   184  H HD23 B LEU   A 1 10  ? 6.669  -12.009 7.862   0.60 18.44 ?  10  LEU   A HD23 1 
ATOM   185  N N    . LYS   A 1 11  ? 9.149  -14.536 11.662  1.00 12.17 ?  11  LYS   A N    1 
ATOM   186  C CA   . LYS   A 1 11  ? 10.132 -15.542 11.289  1.00 12.41 ?  11  LYS   A CA   1 
ATOM   187  C C    . LYS   A 1 11  ? 9.773  -16.074 9.907   1.00 12.74 ?  11  LYS   A C    1 
ATOM   188  O O    . LYS   A 1 11  ? 8.663  -16.577 9.708   1.00 14.31 ?  11  LYS   A O    1 
ATOM   189  C CB   . LYS   A 1 11  ? 10.134 -16.657 12.335  1.00 12.56 ?  11  LYS   A CB   1 
ATOM   190  C CG   . LYS   A 1 11  ? 11.170 -17.746 12.141  1.00 12.63 ?  11  LYS   A CG   1 
ATOM   191  C CD   . LYS   A 1 11  ? 11.217 -18.647 13.383  1.00 13.15 ?  11  LYS   A CD   1 
ATOM   192  C CE   . LYS   A 1 11  ? 12.217 -19.787 13.260  1.00 13.52 ?  11  LYS   A CE   1 
ATOM   193  N NZ   . LYS   A 1 11  ? 13.600 -19.301 13.018  1.00 13.48 ?  11  LYS   A NZ   1 
ATOM   194  H H    A LYS   A 1 11  ? 8.488  -14.846 12.121  0.40 14.60 ?  11  LYS   A H    1 
ATOM   195  H H    B LYS   A 1 11  ? 8.537  -14.820 12.197  0.60 14.60 ?  11  LYS   A H    1 
ATOM   196  H HA   . LYS   A 1 11  ? 11.014 -15.135 11.250  1.00 14.88 ?  11  LYS   A HA   1 
ATOM   197  H HB2  . LYS   A 1 11  ? 10.290 -16.251 13.202  1.00 15.07 ?  11  LYS   A HB2  1 
ATOM   198  H HB3  . LYS   A 1 11  ? 9.260  -17.074 12.326  1.00 15.07 ?  11  LYS   A HB3  1 
ATOM   199  H HG2  . LYS   A 1 11  ? 10.931 -18.291 11.374  1.00 15.15 ?  11  LYS   A HG2  1 
ATOM   200  H HG3  . LYS   A 1 11  ? 12.045 -17.348 12.017  1.00 15.15 ?  11  LYS   A HG3  1 
ATOM   201  H HD2  . LYS   A 1 11  ? 11.466 -18.110 14.151  1.00 15.78 ?  11  LYS   A HD2  1 
ATOM   202  H HD3  . LYS   A 1 11  ? 10.337 -19.034 13.523  1.00 15.78 ?  11  LYS   A HD3  1 
ATOM   203  H HE2  . LYS   A 1 11  ? 12.219 -20.299 14.087  1.00 16.22 ?  11  LYS   A HE2  1 
ATOM   204  H HE3  . LYS   A 1 11  ? 11.962 -20.359 12.519  1.00 16.22 ?  11  LYS   A HE3  1 
ATOM   205  H HZ1  . LYS   A 1 11  ? 14.158 -19.990 12.940  1.00 16.16 ?  11  LYS   A HZ1  1 
ATOM   206  H HZ2  . LYS   A 1 11  ? 13.626 -18.824 12.265  1.00 16.16 ?  11  LYS   A HZ2  1 
ATOM   207  H HZ3  . LYS   A 1 11  ? 13.867 -18.787 13.693  1.00 16.16 ?  11  LYS   A HZ3  1 
ATOM   208  N N    . LEU   A 1 12  ? 10.693 -15.961 8.946   1.00 12.00 ?  12  LEU   A N    1 
ATOM   209  C CA   . LEU   A 1 12  ? 10.445 -16.510 7.618   1.00 12.40 ?  12  LEU   A CA   1 
ATOM   210  C C    . LEU   A 1 12  ? 11.011 -17.915 7.462   1.00 12.14 ?  12  LEU   A C    1 
ATOM   211  O O    . LEU   A 1 12  ? 10.364 -18.776 6.857   1.00 12.70 ?  12  LEU   A O    1 
ATOM   212  C CB   . LEU   A 1 12  ? 11.027 -15.603 6.528   1.00 13.00 ?  12  LEU   A CB   1 
ATOM   213  C CG   . LEU   A 1 12  ? 10.387 -14.222 6.365   1.00 13.75 ?  12  LEU   A CG   1 
ATOM   214  C CD1  . LEU   A 1 12  ? 11.102 -13.470 5.259   1.00 14.54 ?  12  LEU   A CD1  1 
ATOM   215  C CD2  . LEU   A 1 12  ? 8.896  -14.327 6.069   1.00 14.56 ?  12  LEU   A CD2  1 
ATOM   216  H H    . LEU   A 1 12  ? 11.461 -15.570 9.034   1.00 14.40 ?  12  LEU   A H    1 
ATOM   217  H HA   . LEU   A 1 12  ? 9.487  -16.565 7.478   1.00 14.87 ?  12  LEU   A HA   1 
ATOM   218  H HB2  . LEU   A 1 12  ? 11.967 -15.467 6.717   1.00 15.60 ?  12  LEU   A HB2  1 
ATOM   219  H HB3  . LEU   A 1 12  ? 10.937 -16.064 5.676   1.00 15.60 ?  12  LEU   A HB3  1 
ATOM   220  H HG   . LEU   A 1 12  ? 10.501 -13.725 7.187   1.00 16.49 ?  12  LEU   A HG   1 
ATOM   221  H HD11 . LEU   A 1 12  ? 10.693 -12.603 5.146   1.00 17.44 ?  12  LEU   A HD11 1 
ATOM   222  H HD12 . LEU   A 1 12  ? 12.040 -13.367 5.501   1.00 17.44 ?  12  LEU   A HD12 1 
ATOM   223  H HD13 . LEU   A 1 12  ? 11.036 -13.981 4.434   1.00 17.44 ?  12  LEU   A HD13 1 
ATOM   224  H HD21 . LEU   A 1 12  ? 8.562  -13.449 5.831   1.00 17.47 ?  12  LEU   A HD21 1 
ATOM   225  H HD22 . LEU   A 1 12  ? 8.764  -14.943 5.332   1.00 17.47 ?  12  LEU   A HD22 1 
ATOM   226  H HD23 . LEU   A 1 12  ? 8.441  -14.653 6.860   1.00 17.47 ?  12  LEU   A HD23 1 
ATOM   227  N N    . THR   A 1 13  ? 12.221 -18.144 7.969   1.00 12.04 ?  13  THR   A N    1 
ATOM   228  C CA   . THR   A 1 13  ? 12.894 -19.431 7.879   1.00 12.43 ?  13  THR   A CA   1 
ATOM   229  C C    . THR   A 1 13  ? 13.650 -19.666 9.181   1.00 12.47 ?  13  THR   A C    1 
ATOM   230  O O    . THR   A 1 13  ? 13.566 -18.885 10.136  1.00 12.49 ?  13  THR   A O    1 
ATOM   231  C CB   . THR   A 1 13  ? 13.868 -19.467 6.693   1.00 13.60 ?  13  THR   A CB   1 
ATOM   232  O OG1  . THR   A 1 13  ? 14.937 -18.557 6.950   1.00 13.69 ?  13  THR   A OG1  1 
ATOM   233  C CG2  . THR   A 1 13  ? 13.189 -19.090 5.384   1.00 14.23 ?  13  THR   A CG2  1 
ATOM   234  H H    . THR   A 1 13  ? 12.692 -17.544 8.368   1.00 14.44 ?  13  THR   A H    1 
ATOM   235  H HA   . THR   A 1 13  ? 12.237 -20.135 7.764   1.00 14.91 ?  13  THR   A HA   1 
ATOM   236  H HB   . THR   A 1 13  ? 14.226 -20.364 6.599   1.00 16.31 ?  13  THR   A HB   1 
ATOM   237  H HG1  . THR   A 1 13  ? 15.485 -18.567 6.303   1.00 16.41 ?  13  THR   A HG1  1 
ATOM   238  H HG21 . THR   A 1 13  ? 13.764 -19.317 4.636   1.00 17.07 ?  13  THR   A HG21 1 
ATOM   239  H HG22 . THR   A 1 13  ? 12.353 -19.575 5.294   1.00 17.07 ?  13  THR   A HG22 1 
ATOM   240  H HG23 . THR   A 1 13  ? 13.005 -18.139 5.366   1.00 17.07 ?  13  THR   A HG23 1 
ATOM   241  N N    . ASP   A 1 14  ? 14.441 -20.737 9.196   1.00 12.85 ?  14  ASP   A N    1 
ATOM   242  C CA   . ASP   A 1 14  ? 15.290 -21.015 10.343  1.00 13.46 ?  14  ASP   A CA   1 
ATOM   243  C C    . ASP   A 1 14  ? 16.128 -19.807 10.743  1.00 12.80 ?  14  ASP   A C    1 
ATOM   244  O O    . ASP   A 1 14  ? 16.356 -19.574 11.934  1.00 14.01 ?  14  ASP   A O    1 
ATOM   245  C CB   . ASP   A 1 14  ? 16.206 -22.187 10.019  1.00 16.16 ?  14  ASP   A CB   1 
ATOM   246  C CG   . ASP   A 1 14  ? 17.122 -22.523 11.164  1.00 20.51 ?  14  ASP   A CG   1 
ATOM   247  O OD1  . ASP   A 1 14  ? 16.610 -22.959 12.216  1.00 21.90 ?  14  ASP   A OD1  1 
ATOM   248  O OD2  . ASP   A 1 14  ? 18.341 -22.335 11.014  1.00 23.23 -1 14  ASP   A OD2  1 
ATOM   249  H H    . ASP   A 1 14  ? 14.499 -21.306 8.559   1.00 15.41 ?  14  ASP   A H    1 
ATOM   250  H HA   . ASP   A 1 14  ? 14.739 -21.266 11.102  1.00 16.14 ?  14  ASP   A HA   1 
ATOM   251  H HB2  . ASP   A 1 14  ? 15.662 -22.974 9.825   1.00 19.39 ?  14  ASP   A HB2  1 
ATOM   252  H HB3  . ASP   A 1 14  ? 16.746 -21.968 9.241   1.00 19.39 ?  14  ASP   A HB3  1 
ATOM   253  N N    . ASN   A 1 15  ? 16.598 -19.021 9.765   1.00 12.04 ?  15  ASN   A N    1 
ATOM   254  C CA   . ASN   A 1 15  ? 17.597 -17.992 10.035  1.00 12.28 ?  15  ASN   A CA   1 
ATOM   255  C C    . ASN   A 1 15  ? 17.238 -16.594 9.547   1.00 12.64 ?  15  ASN   A C    1 
ATOM   256  O O    . ASN   A 1 15  ? 18.017 -15.670 9.799   1.00 14.27 ?  15  ASN   A O    1 
ATOM   257  C CB   . ASN   A 1 15  ? 18.969 -18.397 9.458   1.00 12.10 ?  15  ASN   A CB   1 
ATOM   258  C CG   . ASN   A 1 15  ? 18.958 -18.491 7.947   1.00 12.39 ?  15  ASN   A CG   1 
ATOM   259  O OD1  . ASN   A 1 15  ? 18.224 -19.295 7.370   1.00 13.61 ?  15  ASN   A OD1  1 
ATOM   260  N ND2  . ASN   A 1 15  ? 19.768 -17.658 7.294   1.00 12.90 ?  15  ASN   A ND2  1 
ATOM   261  H H    . ASN   A 1 15  ? 16.346 -19.063 8.946   1.00 14.44 ?  15  ASN   A H    1 
ATOM   262  H HA   . ASN   A 1 15  ? 17.711 -17.927 10.992  1.00 14.73 ?  15  ASN   A HA   1 
ATOM   263  H HB2  . ASN   A 1 15  ? 19.632 -17.729 9.714   1.00 14.51 ?  15  ASN   A HB2  1 
ATOM   264  H HB3  . ASN   A 1 15  ? 19.225 -19.263 9.811   1.00 14.51 ?  15  ASN   A HB3  1 
ATOM   265  H HD21 . ASN   A 1 15  ? 19.800 -17.670 6.434   1.00 15.47 ?  15  ASN   A HD21 1 
ATOM   266  H HD22 . ASN   A 1 15  ? 20.266 -17.100 7.729   1.00 15.47 ?  15  ASN   A HD22 1 
ATOM   267  N N    . VAL   A 1 16  ? 16.103 -16.404 8.868   1.00 12.21 ?  16  VAL   A N    1 
ATOM   268  C CA   . VAL   A 1 16  ? 15.724 -15.114 8.301   1.00 12.16 ?  16  VAL   A CA   1 
ATOM   269  C C    . VAL   A 1 16  ? 14.440 -14.616 8.955   1.00 11.75 ?  16  VAL   A C    1 
ATOM   270  O O    . VAL   A 1 16  ? 13.443 -15.350 9.036   1.00 11.73 ?  16  VAL   A O    1 
ATOM   271  C CB   . VAL   A 1 16  ? 15.579 -15.168 6.769   1.00 12.87 ?  16  VAL   A CB   1 
ATOM   272  C CG1  . VAL   A 1 16  ? 15.177 -13.788 6.219   1.00 13.84 ?  16  VAL   A CG1  1 
ATOM   273  C CG2  . VAL   A 1 16  ? 16.868 -15.653 6.116   1.00 13.93 ?  16  VAL   A CG2  1 
ATOM   274  H H    . VAL   A 1 16  ? 15.528 -17.029 8.720   1.00 14.65 ?  16  VAL   A H    1 
ATOM   275  H HA   . VAL   A 1 16  ? 16.423 -14.475 8.501   1.00 14.59 ?  16  VAL   A HA   1 
ATOM   276  H HB   . VAL   A 1 16  ? 14.880 -15.795 6.540   1.00 15.44 ?  16  VAL   A HB   1 
ATOM   277  H HG11 . VAL   A 1 16  ? 15.273 -13.797 5.253   1.00 16.61 ?  16  VAL   A HG11 1 
ATOM   278  H HG12 . VAL   A 1 16  ? 14.252 -13.614 6.455   1.00 16.61 ?  16  VAL   A HG12 1 
ATOM   279  H HG13 . VAL   A 1 16  ? 15.754 -13.114 6.603   1.00 16.61 ?  16  VAL   A HG13 1 
ATOM   280  H HG21 . VAL   A 1 16  ? 16.806 -15.529 5.154   1.00 16.71 ?  16  VAL   A HG21 1 
ATOM   281  H HG22 . VAL   A 1 16  ? 17.617 -15.142 6.464   1.00 16.71 ?  16  VAL   A HG22 1 
ATOM   282  H HG23 . VAL   A 1 16  ? 16.993 -16.593 6.320   1.00 16.71 ?  16  VAL   A HG23 1 
ATOM   283  N N    A TYR   A 1 17  ? 14.479 -13.370 9.409   0.40 11.41 ?  17  TYR   A N    1 
ATOM   284  N N    B TYR   A 1 17  ? 14.473 -13.350 9.394   0.60 11.58 ?  17  TYR   A N    1 
ATOM   285  C CA   A TYR   A 1 17  ? 13.361 -12.689 10.033  0.40 11.24 ?  17  TYR   A CA   1 
ATOM   286  C CA   B TYR   A 1 17  ? 13.413 -12.670 10.134  0.60 11.51 ?  17  TYR   A CA   1 
ATOM   287  C C    A TYR   A 1 17  ? 13.099 -11.398 9.266   0.40 10.79 ?  17  TYR   A C    1 
ATOM   288  C C    B TYR   A 1 17  ? 13.148 -11.314 9.487   0.60 11.64 ?  17  TYR   A C    1 
ATOM   289  O O    A TYR   A 1 17  ? 14.012 -10.846 8.645   0.40 11.58 ?  17  TYR   A O    1 
ATOM   290  O O    B TYR   A 1 17  ? 14.042 -10.745 8.859   0.60 12.15 ?  17  TYR   A O    1 
ATOM   291  C CB   A TYR   A 1 17  ? 13.710 -12.386 11.495  0.40 11.71 ?  17  TYR   A CB   1 
ATOM   292  C CB   B TYR   A 1 17  ? 13.857 -12.450 11.589  0.60 11.93 ?  17  TYR   A CB   1 
ATOM   293  C CG   A TYR   A 1 17  ? 13.865 -13.636 12.335  0.40 12.33 ?  17  TYR   A CG   1 
ATOM   294  C CG   B TYR   A 1 17  ? 14.092 -13.729 12.353  0.60 12.99 ?  17  TYR   A CG   1 
ATOM   295  C CD1  A TYR   A 1 17  ? 15.032 -14.397 12.298  0.40 13.06 ?  17  TYR   A CD1  1 
ATOM   296  C CD1  B TYR   A 1 17  ? 15.281 -14.441 12.227  0.60 14.15 ?  17  TYR   A CD1  1 
ATOM   297  C CD2  A TYR   A 1 17  ? 12.830 -14.071 13.149  0.40 12.17 ?  17  TYR   A CD2  1 
ATOM   298  C CD2  B TYR   A 1 17  ? 13.113 -14.237 13.193  0.60 13.45 ?  17  TYR   A CD2  1 
ATOM   299  C CE1  A TYR   A 1 17  ? 15.162 -15.557 13.059  0.40 13.07 ?  17  TYR   A CE1  1 
ATOM   300  C CE1  B TYR   A 1 17  ? 15.485 -15.628 12.921  0.60 14.45 ?  17  TYR   A CE1  1 
ATOM   301  C CE2  A TYR   A 1 17  ? 12.947 -15.228 13.910  0.40 12.55 ?  17  TYR   A CE2  1 
ATOM   302  C CE2  B TYR   A 1 17  ? 13.306 -15.423 13.892  0.60 14.27 ?  17  TYR   A CE2  1 
ATOM   303  C CZ   A TYR   A 1 17  ? 14.113 -15.966 13.865  0.40 12.85 ?  17  TYR   A CZ   1 
ATOM   304  C CZ   B TYR   A 1 17  ? 14.495 -16.114 13.754  0.60 14.43 ?  17  TYR   A CZ   1 
ATOM   305  O OH   A TYR   A 1 17  ? 14.220 -17.114 14.625  0.40 13.16 ?  17  TYR   A OH   1 
ATOM   306  O OH   B TYR   A 1 17  ? 14.692 -17.290 14.447  0.60 14.94 ?  17  TYR   A OH   1 
ATOM   307  H H    A TYR   A 1 17  ? 15.187 -12.878 9.361   0.40 13.68 ?  17  TYR   A H    1 
ATOM   308  H H    B TYR   A 1 17  ? 15.154 -12.836 9.258   0.60 13.89 ?  17  TYR   A H    1 
ATOM   309  H HA   A TYR   A 1 17  ? 12.575 -13.261 10.002  0.40 13.48 ?  17  TYR   A HA   1 
ATOM   310  H HA   B TYR   A 1 17  ? 12.598 -13.191 10.118  0.60 13.81 ?  17  TYR   A HA   1 
ATOM   311  H HB2  A TYR   A 1 17  ? 14.545 -11.897 11.525  0.40 14.04 ?  17  TYR   A HB2  1 
ATOM   312  H HB2  B TYR   A 1 17  ? 14.686 -11.950 11.591  0.60 14.31 ?  17  TYR   A HB2  1 
ATOM   313  H HB3  A TYR   A 1 17  ? 12.999 -11.856 11.877  0.40 14.04 ?  17  TYR   A HB3  1 
ATOM   314  H HB3  B TYR   A 1 17  ? 13.169 -11.951 12.052  0.60 14.31 ?  17  TYR   A HB3  1 
ATOM   315  H HD1  A TYR   A 1 17  ? 15.739 -14.125 11.755  0.40 15.66 ?  17  TYR   A HD1  1 
ATOM   316  H HD1  B TYR   A 1 17  ? 15.949 -14.118 11.665  0.60 16.98 ?  17  TYR   A HD1  1 
ATOM   317  H HD2  A TYR   A 1 17  ? 12.038 -13.586 13.184  0.40 14.60 ?  17  TYR   A HD2  1 
ATOM   318  H HD2  B TYR   A 1 17  ? 12.306 -13.778 13.286  0.60 16.13 ?  17  TYR   A HD2  1 
ATOM   319  H HE1  A TYR   A 1 17  ? 15.952 -16.052 13.026  0.40 15.68 ?  17  TYR   A HE1  1 
ATOM   320  H HE1  B TYR   A 1 17  ? 16.286 -16.090 12.829  0.60 17.33 ?  17  TYR   A HE1  1 
ATOM   321  H HE2  A TYR   A 1 17  ? 12.246 -15.506 14.453  0.40 15.05 ?  17  TYR   A HE2  1 
ATOM   322  H HE2  B TYR   A 1 17  ? 12.637 -15.747 14.451  0.60 17.11 ?  17  TYR   A HE2  1 
ATOM   323  H HH   A TYR   A 1 17  ? 13.469 -17.320 14.934  0.40 15.78 ?  17  TYR   A HH   1 
ATOM   324  H HH   B TYR   A 1 17  ? 15.446 -17.604 14.260  0.60 17.92 ?  17  TYR   A HH   1 
ATOM   325  N N    A ILE   A 1 18  ? 11.852 -10.917 9.293   0.40 9.99  ?  18  ILE   A N    1 
ATOM   326  N N    B ILE   A 1 18  ? 11.937 -10.762 9.662   0.60 11.04 ?  18  ILE   A N    1 
ATOM   327  C CA   A ILE   A 1 18  ? 11.472 -9.738  8.519   0.40 9.66  ?  18  ILE   A CA   1 
ATOM   328  C CA   B ILE   A 1 18  ? 11.560 -9.540  8.947   0.60 10.44 ?  18  ILE   A CA   1 
ATOM   329  C C    A ILE   A 1 18  ? 10.480 -8.888  9.304   0.40 10.16 ?  18  ILE   A C    1 
ATOM   330  C C    B ILE   A 1 18  ? 10.615 -8.679  9.782   0.60 10.46 ?  18  ILE   A C    1 
ATOM   331  O O    A ILE   A 1 18  ? 9.673  -9.404  10.082  0.40 10.23 ?  18  ILE   A O    1 
ATOM   332  O O    B ILE   A 1 18  ? 9.776  -9.188  10.531  0.60 10.91 ?  18  ILE   A O    1 
ATOM   333  C CB   A ILE   A 1 18  ? 10.938 -10.136 7.122   0.40 10.01 ?  18  ILE   A CB   1 
ATOM   334  C CB   B ILE   A 1 18  ? 10.962 -9.889  7.566   0.60 10.40 ?  18  ILE   A CB   1 
ATOM   335  C CG1  A ILE   A 1 18  ? 10.930 -8.933  6.181   0.40 9.76  ?  18  ILE   A CG1  1 
ATOM   336  C CG1  B ILE   A 1 18  ? 10.932 -8.664  6.651   0.60 11.34 ?  18  ILE   A CG1  1 
ATOM   337  C CG2  A ILE   A 1 18  ? 9.565  -10.789 7.222   0.40 9.80  ?  18  ILE   A CG2  1 
ATOM   338  C CG2  B ILE   A 1 18  ? 9.594  -10.543 7.719   0.60 11.17 ?  18  ILE   A CG2  1 
ATOM   339  C CD1  A ILE   A 1 18  ? 10.701 -9.314  4.735   0.40 10.75 ?  18  ILE   A CD1  1 
ATOM   340  C CD1  B ILE   A 1 18  ? 10.605 -9.010  5.218   0.60 13.03 ?  18  ILE   A CD1  1 
ATOM   341  H H    A ILE   A 1 18  ? 11.213 -11.266 9.756   0.40 11.98 ?  18  ILE   A H    1 
ATOM   342  H H    B ILE   A 1 18  ? 11.330 -11.076 10.186  0.60 13.24 ?  18  ILE   A H    1 
ATOM   343  H HA   A ILE   A 1 18  ? 12.266 -9.209  8.378   0.40 11.58 ?  18  ILE   A HA   1 
ATOM   344  H HA   B ILE   A 1 18  ? 12.366 -9.017  8.797   0.60 12.51 ?  18  ILE   A HA   1 
ATOM   345  H HB   A ILE   A 1 18  ? 11.546 -10.797 6.747   0.40 12.01 ?  18  ILE   A HB   1 
ATOM   346  H HB   B ILE   A 1 18  ? 11.551 -10.533 7.161   0.60 12.48 ?  18  ILE   A HB   1 
ATOM   347  H HG12 A ILE   A 1 18  ? 10.225 -8.329  6.448   0.40 11.70 ?  18  ILE   A HG12 1 
ATOM   348  H HG12 B ILE   A 1 18  ? 10.268 -8.038  6.971   0.60 13.60 ?  18  ILE   A HG12 1 
ATOM   349  H HG13 A ILE   A 1 18  ? 11.792 -8.487  6.236   0.40 11.70 ?  18  ILE   A HG13 1 
ATOM   350  H HG13 B ILE   A 1 18  ? 11.813 -8.241  6.661   0.60 13.60 ?  18  ILE   A HG13 1 
ATOM   351  H HG21 A ILE   A 1 18  ? 9.340  -11.187 6.365   0.40 11.75 ?  18  ILE   A HG21 1 
ATOM   352  H HG21 B ILE   A 1 18  ? 9.330  -10.912 6.862   0.60 13.40 ?  18  ILE   A HG21 1 
ATOM   353  H HG22 A ILE   A 1 18  ? 9.591  -11.474 7.906   0.40 11.75 ?  18  ILE   A HG22 1 
ATOM   354  H HG22 B ILE   A 1 18  ? 9.656  -11.248 8.379   0.60 13.40 ?  18  ILE   A HG22 1 
ATOM   355  H HG23 A ILE   A 1 18  ? 8.910  -10.113 7.452   0.40 11.75 ?  18  ILE   A HG23 1 
ATOM   356  H HG23 B ILE   A 1 18  ? 8.950  -9.875  8.004   0.60 13.40 ?  18  ILE   A HG23 1 
ATOM   357  H HD11 A ILE   A 1 18  ? 10.778 -8.516  4.186   0.40 12.89 ?  18  ILE   A HD11 1 
ATOM   358  H HD11 B ILE   A 1 18  ? 10.669 -8.210  4.672   0.60 15.62 ?  18  ILE   A HD11 1 
ATOM   359  H HD12 A ILE   A 1 18  ? 11.365 -9.965  4.469   0.40 12.89 ?  18  ILE   A HD12 1 
ATOM   360  H HD12 B ILE   A 1 18  ? 11.235 -9.677  4.898   0.60 15.62 ?  18  ILE   A HD12 1 
ATOM   361  H HD13 A ILE   A 1 18  ? 9.811  -9.689  4.647   0.40 12.89 ?  18  ILE   A HD13 1 
ATOM   362  H HD13 B ILE   A 1 18  ? 9.703  -9.365  5.177   0.60 15.62 ?  18  ILE   A HD13 1 
ATOM   363  N N    A LYS   A 1 19  ? 10.541 -7.573  9.089   0.40 10.13 ?  19  LYS   A N    1 
ATOM   364  N N    B LYS   A 1 19  ? 10.747 -7.354  9.620   0.60 10.67 ?  19  LYS   A N    1 
ATOM   365  C CA   A LYS   A 1 19  ? 9.740  -6.624  9.852   0.40 11.32 ?  19  LYS   A CA   1 
ATOM   366  C CA   B LYS   A 1 19  ? 9.948  -6.375  10.350  0.60 11.90 ?  19  LYS   A CA   1 
ATOM   367  C C    A LYS   A 1 19  ? 9.568  -5.355  9.031   0.40 11.82 ?  19  LYS   A C    1 
ATOM   368  C C    B LYS   A 1 19  ? 9.729  -5.148  9.471   0.60 12.02 ?  19  LYS   A C    1 
ATOM   369  O O    A LYS   A 1 19  ? 10.451 -4.985  8.252   0.40 11.71 ?  19  LYS   A O    1 
ATOM   370  O O    B LYS   A 1 19  ? 10.615 -4.775  8.701   0.60 11.68 ?  19  LYS   A O    1 
ATOM   371  C CB   A LYS   A 1 19  ? 10.451 -6.290  11.170  0.40 12.70 ?  19  LYS   A CB   1 
ATOM   372  C CB   B LYS   A 1 19  ? 10.666 -5.958  11.646  0.60 12.58 ?  19  LYS   A CB   1 
ATOM   373  C CG   A LYS   A 1 19  ? 9.732  -5.333  12.112  0.40 13.72 ?  19  LYS   A CG   1 
ATOM   374  C CG   B LYS   A 1 19  ? 9.884  -5.050  12.574  0.60 14.38 ?  19  LYS   A CG   1 
ATOM   375  C CD   A LYS   A 1 19  ? 10.596 -5.103  13.352  0.40 14.61 ?  19  LYS   A CD   1 
ATOM   376  C CD   B LYS   A 1 19  ? 10.729 -4.688  13.785  0.60 16.05 ?  19  LYS   A CD   1 
ATOM   377  C CE   A LYS   A 1 19  ? 9.967  -4.149  14.355  0.40 15.02 ?  19  LYS   A CE   1 
ATOM   378  C CE   B LYS   A 1 19  ? 9.959  -3.833  14.773  0.60 16.99 ?  19  LYS   A CE   1 
ATOM   379  N NZ   A LYS   A 1 19  ? 10.864 -3.943  15.535  0.40 15.27 ?  19  LYS   A NZ   1 
ATOM   380  N NZ   B LYS   A 1 19  ? 10.794 -3.509  15.957  0.60 17.62 ?  19  LYS   A NZ   1 
ATOM   381  H H    A LYS   A 1 19  ? 11.048 -7.212  8.499   0.40 12.15 ?  19  LYS   A H    1 
ATOM   382  H H    B LYS   A 1 19  ? 11.322 -6.986  9.086   0.60 12.80 ?  19  LYS   A H    1 
ATOM   383  H HA   A LYS   A 1 19  ? 8.870  -7.005  10.046  0.40 13.58 ?  19  LYS   A HA   1 
ATOM   384  H HA   B LYS   A 1 19  ? 9.092  -6.749  10.582  0.60 14.28 ?  19  LYS   A HA   1 
ATOM   385  H HB2  A LYS   A 1 19  ? 10.591 -7.118  11.653  0.40 15.23 ?  19  LYS   A HB2  1 
ATOM   386  H HB2  B LYS   A 1 19  ? 10.883 -6.759  12.154  0.60 15.09 ?  19  LYS   A HB2  1 
ATOM   387  H HB3  A LYS   A 1 19  ? 11.309 -5.894  10.955  0.40 15.23 ?  19  LYS   A HB3  1 
ATOM   388  H HB3  B LYS   A 1 19  ? 11.488 -5.494  11.418  0.60 15.09 ?  19  LYS   A HB3  1 
ATOM   389  H HG2  A LYS   A 1 19  ? 9.589  -4.481  11.670  0.40 16.45 ?  19  LYS   A HG2  1 
ATOM   390  H HG2  B LYS   A 1 19  ? 9.651  -4.232  12.111  0.60 17.24 ?  19  LYS   A HG2  1 
ATOM   391  H HG3  A LYS   A 1 19  ? 8.886  -5.720  12.390  0.40 16.45 ?  19  LYS   A HG3  1 
ATOM   392  H HG3  B LYS   A 1 19  ? 9.088  -5.508  12.885  0.60 17.24 ?  19  LYS   A HG3  1 
ATOM   393  H HD2  A LYS   A 1 19  ? 10.740 -5.953  13.798  0.40 17.52 ?  19  LYS   A HD2  1 
ATOM   394  H HD2  B LYS   A 1 19  ? 11.005 -5.502  14.238  0.60 19.25 ?  19  LYS   A HD2  1 
ATOM   395  H HD3  A LYS   A 1 19  ? 11.448 -4.728  13.076  0.40 17.52 ?  19  LYS   A HD3  1 
ATOM   396  H HD3  B LYS   A 1 19  ? 11.509 -4.188  13.494  0.60 19.25 ?  19  LYS   A HD3  1 
ATOM   397  H HE2  A LYS   A 1 19  ? 9.818  -3.287  13.934  0.40 18.02 ?  19  LYS   A HE2  1 
ATOM   398  H HE2  B LYS   A 1 19  ? 9.699  -3.004  14.344  0.60 20.38 ?  19  LYS   A HE2  1 
ATOM   399  H HE3  A LYS   A 1 19  ? 9.128  -4.518  14.672  0.40 18.02 ?  19  LYS   A HE3  1 
ATOM   400  H HE3  B LYS   A 1 19  ? 9.175  -4.320  15.073  0.60 20.38 ?  19  LYS   A HE3  1 
ATOM   401  H HZ1  A LYS   A 1 19  ? 10.492 -3.370  16.106  0.40 18.31 ?  19  LYS   A HZ1  1 
ATOM   402  H HZ1  B LYS   A 1 19  ? 10.329 -3.009  16.527  0.60 21.14 ?  19  LYS   A HZ1  1 
ATOM   403  H HZ2  A LYS   A 1 19  ? 11.001 -4.718  15.952  0.40 18.31 ?  19  LYS   A HZ2  1 
ATOM   404  H HZ2  B LYS   A 1 19  ? 11.043 -4.259  16.367  0.60 21.14 ?  19  LYS   A HZ2  1 
ATOM   405  H HZ3  A LYS   A 1 19  ? 11.648 -3.616  15.269  0.40 18.31 ?  19  LYS   A HZ3  1 
ATOM   406  H HZ3  B LYS   A 1 19  ? 11.519 -3.062  15.704  0.60 21.14 ?  19  LYS   A HZ3  1 
ATOM   407  N N    A ASN   A 1 20  ? 8.425  -4.689  9.210   0.40 12.56 ?  20  ASN   A N    1 
ATOM   408  N N    B ASN   A 1 20  ? 8.548  -4.530  9.577   0.60 12.75 ?  20  ASN   A N    1 
ATOM   409  C CA   A ASN   A 1 20  ? 8.233  -3.347  8.667   0.40 13.42 ?  20  ASN   A CA   1 
ATOM   410  C CA   B ASN   A 1 20  ? 8.265  -3.242  8.932   0.60 13.46 ?  20  ASN   A CA   1 
ATOM   411  C C    A ASN   A 1 20  ? 8.855  -2.357  9.644   0.40 13.86 ?  20  ASN   A C    1 
ATOM   412  C C    B ASN   A 1 20  ? 8.850  -2.150  9.823   0.60 14.02 ?  20  ASN   A C    1 
ATOM   413  O O    A ASN   A 1 20  ? 8.333  -2.149  10.745  0.40 14.27 ?  20  ASN   A O    1 
ATOM   414  O O    B ASN   A 1 20  ? 8.218  -1.710  10.786  0.60 15.14 ?  20  ASN   A O    1 
ATOM   415  C CB   A ASN   A 1 20  ? 6.749  -3.056  8.455   0.40 13.81 ?  20  ASN   A CB   1 
ATOM   416  C CB   B ASN   A 1 20  ? 6.752  -3.075  8.761   0.60 13.73 ?  20  ASN   A CB   1 
ATOM   417  C CG   A ASN   A 1 20  ? 6.471  -1.582  8.222   0.40 14.95 ?  20  ASN   A CG   1 
ATOM   418  C CG   B ASN   A 1 20  ? 6.343  -1.819  7.959   0.60 13.72 ?  20  ASN   A CG   1 
ATOM   419  O OD1  A ASN   A 1 20  ? 5.584  -1.004  8.847   0.40 16.88 ?  20  ASN   A OD1  1 
ATOM   420  O OD1  B ASN   A 1 20  ? 5.174  -1.388  8.017   0.60 13.24 ?  20  ASN   A OD1  1 
ATOM   421  N ND2  A ASN   A 1 20  ? 7.236  -0.964  7.330   0.40 14.25 ?  20  ASN   A ND2  1 
ATOM   422  N ND2  B ASN   A 1 20  ? 7.283  -1.241  7.208   0.60 14.87 ?  20  ASN   A ND2  1 
ATOM   423  H H    A ASN   A 1 20  ? 7.746  -4.995  9.646   0.40 15.07 ?  20  ASN   A H    1 
ATOM   424  H H    B ASN   A 1 20  ? 7.883  -4.857  10.004  0.60 15.30 ?  20  ASN   A H    1 
ATOM   425  H HA   A ASN   A 1 20  ? 8.683  -3.273  7.817   0.40 16.10 ?  20  ASN   A HA   1 
ATOM   426  H HA   B ASN   A 1 20  ? 8.694  -3.219  8.065   0.60 16.15 ?  20  ASN   A HA   1 
ATOM   427  H HB2  A ASN   A 1 20  ? 6.432  -3.538  7.677   0.40 16.57 ?  20  ASN   A HB2  1 
ATOM   428  H HB2  B ASN   A 1 20  ? 6.403  -3.849  8.300   0.60 16.47 ?  20  ASN   A HB2  1 
ATOM   429  H HB3  A ASN   A 1 20  ? 6.249  -3.338  9.240   0.40 16.57 ?  20  ASN   A HB3  1 
ATOM   430  H HB3  B ASN   A 1 20  ? 6.348  -3.007  9.643   0.60 16.47 ?  20  ASN   A HB3  1 
ATOM   431  H HD21 A ASN   A 1 20  ? 7.115  -0.131  7.166   0.40 17.09 ?  20  ASN   A HD21 1 
ATOM   432  H HD21 B ASN   A 1 20  ? 7.093  -0.545  6.747   0.60 17.84 ?  20  ASN   A HD21 1 
ATOM   433  H HD22 A ASN   A 1 20  ? 7.850  -1.403  6.917   0.40 17.09 ?  20  ASN   A HD22 1 
ATOM   434  H HD22 B ASN   A 1 20  ? 8.080  -1.567  7.177   0.60 17.84 ?  20  ASN   A HD22 1 
ATOM   435  N N    A ALA   A 1 21  ? 9.981  -1.761  9.258   0.40 13.72 ?  21  ALA   A N    1 
ATOM   436  N N    B ALA   A 1 21  ? 10.076 -1.717  9.514   0.60 14.28 ?  21  ALA   A N    1 
ATOM   437  C CA   A ALA   A 1 21  ? 10.692 -0.884  10.173  0.40 13.69 ?  21  ALA   A CA   1 
ATOM   438  C CA   B ALA   A 1 21  ? 10.749 -0.727  10.346  0.60 14.59 ?  21  ALA   A CA   1 
ATOM   439  C C    A ALA   A 1 21  ? 11.653 0.006   9.404   0.40 13.48 ?  21  ALA   A C    1 
ATOM   440  C C    B ALA   A 1 21  ? 11.844 -0.038  9.546   0.60 13.59 ?  21  ALA   A C    1 
ATOM   441  O O    A ALA   A 1 21  ? 12.110 -0.341  8.312   0.40 13.76 ?  21  ALA   A O    1 
ATOM   442  O O    B ALA   A 1 21  ? 12.350 -0.579  8.561   0.60 13.63 ?  21  ALA   A O    1 
ATOM   443  C CB   A ALA   A 1 21  ? 11.470 -1.686  11.219  0.40 13.81 ?  21  ALA   A CB   1 
ATOM   444  C CB   B ALA   A 1 21  ? 11.333 -1.356  11.616  0.60 15.91 ?  21  ALA   A CB   1 
ATOM   445  H H    A ALA   A 1 21  ? 10.344 -1.856  8.484   0.40 16.46 ?  21  ALA   A H    1 
ATOM   446  H H    B ALA   A 1 21  ? 10.541 -1.983  8.835   0.60 17.12 ?  21  ALA   A H    1 
ATOM   447  H HA   A ALA   A 1 21  ? 10.046 -0.320  10.632  0.40 16.42 ?  21  ALA   A HA   1 
ATOM   448  H HA   B ALA   A 1 21  ? 10.107 -0.054  10.614  0.60 17.50 ?  21  ALA   A HA   1 
ATOM   449  H HB1  A ALA   A 1 21  ? 11.913 -1.066  11.816  0.40 16.56 ?  21  ALA   A HB1  1 
ATOM   450  H HB1  B ALA   A 1 21  ? 11.766 -0.667  12.142  0.60 19.08 ?  21  ALA   A HB1  1 
ATOM   451  H HB2  A ALA   A 1 21  ? 10.846 -2.238  11.718  0.40 16.56 ?  21  ALA   A HB2  1 
ATOM   452  H HB2  B ALA   A 1 21  ? 10.612 -1.758  12.129  0.60 19.08 ?  21  ALA   A HB2  1 
ATOM   453  H HB3  A ALA   A 1 21  ? 12.119 -2.242  10.767  0.40 16.56 ?  21  ALA   A HB3  1 
ATOM   454  H HB3  B ALA   A 1 21  ? 11.977 -2.037  11.367  0.60 19.08 ?  21  ALA   A HB3  1 
ATOM   455  N N    A ASP   A 1 22  ? 11.939 1.164   10.000  0.40 13.90 ?  22  ASP   A N    1 
ATOM   456  N N    B ASP   A 1 22  ? 12.179 1.180   9.986   0.60 13.68 ?  22  ASP   A N    1 
ATOM   457  C CA   A ASP   A 1 22  ? 12.987 2.065   9.538   0.40 14.04 ?  22  ASP   A CA   1 
ATOM   458  C CA   B ASP   A 1 22  ? 13.344 1.901   9.485   0.60 13.68 ?  22  ASP   A CA   1 
ATOM   459  C C    A ASP   A 1 22  ? 14.317 1.575   10.098  0.40 13.44 ?  22  ASP   A C    1 
ATOM   460  C C    B ASP   A 1 22  ? 14.599 1.272   10.077  0.60 12.30 ?  22  ASP   A C    1 
ATOM   461  O O    A ASP   A 1 22  ? 14.523 1.585   11.316  0.40 13.65 ?  22  ASP   A O    1 
ATOM   462  O O    B ASP   A 1 22  ? 14.717 1.138   11.299  0.60 12.49 ?  22  ASP   A O    1 
ATOM   463  C CB   A ASP   A 1 22  ? 12.675 3.473   10.042  0.40 14.85 ?  22  ASP   A CB   1 
ATOM   464  C CB   B ASP   A 1 22  ? 13.253 3.367   9.924   0.60 14.90 ?  22  ASP   A CB   1 
ATOM   465  C CG   A ASP   A 1 22  ? 13.709 4.509   9.608   0.40 15.79 ?  22  ASP   A CG   1 
ATOM   466  C CG   B ASP   A 1 22  ? 14.277 4.267   9.245   0.60 15.67 ?  22  ASP   A CG   1 
ATOM   467  O OD1  A ASP   A 1 22  ? 14.823 4.132   9.189   0.40 15.93 ?  22  ASP   A OD1  1 
ATOM   468  O OD1  B ASP   A 1 22  ? 15.283 3.754   8.704   0.60 14.97 ?  22  ASP   A OD1  1 
ATOM   469  O OD2  A ASP   A 1 22  ? 13.406 5.716   9.694   0.40 16.95 -1 22  ASP   A OD2  1 
ATOM   470  O OD2  B ASP   A 1 22  ? 14.073 5.503   9.272   0.60 17.22 -1 22  ASP   A OD2  1 
ATOM   471  H H    A ASP   A 1 22  ? 11.520 1.453   10.692  0.40 16.67 ?  22  ASP   A H    1 
ATOM   472  H H    B ASP   A 1 22  ? 11.734 1.615   10.585  0.60 16.41 ?  22  ASP   A H    1 
ATOM   473  H HA   A ASP   A 1 22  ? 13.027 2.070   8.568   0.40 16.84 ?  22  ASP   A HA   1 
ATOM   474  H HA   B ASP   A 1 22  ? 13.380 1.851   8.516   0.60 16.41 ?  22  ASP   A HA   1 
ATOM   475  H HB2  A ASP   A 1 22  ? 11.810 3.746   9.693   0.40 17.81 ?  22  ASP   A HB2  1 
ATOM   476  H HB2  B ASP   A 1 22  ? 12.374 3.706   9.710   0.60 17.88 ?  22  ASP   A HB2  1 
ATOM   477  H HB3  A ASP   A 1 22  ? 12.638 3.453   11.015  0.40 17.81 ?  22  ASP   A HB3  1 
ATOM   478  H HB3  B ASP   A 1 22  ? 13.408 3.416   10.880  0.60 17.88 ?  22  ASP   A HB3  1 
ATOM   479  N N    A ILE   A 1 23  ? 15.220 1.151   9.210   0.40 13.09 ?  23  ILE   A N    1 
ATOM   480  N N    B ILE   A 1 23  ? 15.534 0.869   9.212   0.60 11.50 ?  23  ILE   A N    1 
ATOM   481  C CA   A ILE   A 1 23  ? 16.474 0.545   9.649   0.40 12.50 ?  23  ILE   A CA   1 
ATOM   482  C CA   B ILE   A 1 23  ? 16.771 0.256   9.689   0.60 11.35 ?  23  ILE   A CA   1 
ATOM   483  C C    A ILE   A 1 23  ? 17.272 1.500   10.528  0.40 12.28 ?  23  ILE   A C    1 
ATOM   484  C C    B ILE   A 1 23  ? 17.508 1.192   10.640  0.60 11.89 ?  23  ILE   A C    1 
ATOM   485  O O    A ILE   A 1 23  ? 18.019 1.063   11.411  0.40 12.67 ?  23  ILE   A O    1 
ATOM   486  O O    B ILE   A 1 23  ? 18.164 0.735   11.586  0.60 12.13 ?  23  ILE   A O    1 
ATOM   487  C CB   A ILE   A 1 23  ? 17.280 0.042   8.432   0.40 12.26 ?  23  ILE   A CB   1 
ATOM   488  C CB   B ILE   A 1 23  ? 17.653 -0.220  8.511   0.60 10.64 ?  23  ILE   A CB   1 
ATOM   489  C CG1  A ILE   A 1 23  ? 18.414 -0.882  8.888   0.40 11.48 ?  23  ILE   A CG1  1 
ATOM   490  C CG1  B ILE   A 1 23  ? 18.746 -1.163  9.025   0.60 11.11 ?  23  ILE   A CG1  1 
ATOM   491  C CG2  A ILE   A 1 23  ? 17.803 1.212   7.605   0.40 12.62 ?  23  ILE   A CG2  1 
ATOM   492  C CG2  B ILE   A 1 23  ? 18.250 0.961   7.747   0.60 10.69 ?  23  ILE   A CG2  1 
ATOM   493  C CD1  A ILE   A 1 23  ? 19.160 -1.548  7.746   0.40 11.23 ?  23  ILE   A CD1  1 
ATOM   494  C CD1  B ILE   A 1 23  ? 19.561 -1.835  7.934   0.60 11.44 ?  23  ILE   A CD1  1 
ATOM   495  H H    A ILE   A 1 23  ? 15.127 1.203   8.360   0.40 15.70 ?  23  ILE   A H    1 
ATOM   496  H H    B ILE   A 1 23  ? 15.474 0.937   8.368   0.60 13.79 ?  23  ILE   A H    1 
ATOM   497  H HA   A ILE   A 1 23  ? 16.265 -0.230  10.191  0.40 14.99 ?  23  ILE   A HA   1 
ATOM   498  H HA   B ILE   A 1 23  ? 16.533 -0.533  10.195  0.60 13.61 ?  23  ILE   A HA   1 
ATOM   499  H HB   A ILE   A 1 23  ? 16.684 -0.475  7.871   0.40 14.70 ?  23  ILE   A HB   1 
ATOM   500  H HB   B ILE   A 1 23  ? 17.092 -0.720  7.896   0.60 12.76 ?  23  ILE   A HB   1 
ATOM   501  H HG12 A ILE   A 1 23  ? 19.057 -0.366  9.397   0.40 13.77 ?  23  ILE   A HG12 1 
ATOM   502  H HG12 B ILE   A 1 23  ? 19.358 -0.657  9.580   0.60 13.32 ?  23  ILE   A HG12 1 
ATOM   503  H HG13 A ILE   A 1 23  ? 18.042 -1.585  9.443   0.40 13.77 ?  23  ILE   A HG13 1 
ATOM   504  H HG13 B ILE   A 1 23  ? 18.329 -1.863  9.551   0.60 13.32 ?  23  ILE   A HG13 1 
ATOM   505  H HG21 A ILE   A 1 23  ? 18.140 0.876   6.759   0.40 15.13 ?  23  ILE   A HG21 1 
ATOM   506  H HG21 B ILE   A 1 23  ? 18.648 0.634   6.920   0.60 12.82 ?  23  ILE   A HG21 1 
ATOM   507  H HG22 A ILE   A 1 23  ? 17.075 1.834   7.445   0.40 15.13 ?  23  ILE   A HG22 1 
ATOM   508  H HG22 B ILE   A 1 23  ? 17.547 1.595   7.542   0.60 12.82 ?  23  ILE   A HG22 1 
ATOM   509  H HG23 A ILE   A 1 23  ? 18.515 1.654   8.092   0.40 15.13 ?  23  ILE   A HG23 1 
ATOM   510  H HG23 B ILE   A 1 23  ? 18.931 1.383   8.292   0.60 12.82 ?  23  ILE   A HG23 1 
ATOM   511  H HD11 A ILE   A 1 23  ? 19.809 -2.169  8.113   0.40 13.47 ?  23  ILE   A HD11 1 
ATOM   512  H HD11 B ILE   A 1 23  ? 20.184 -2.459  8.344   0.60 13.72 ?  23  ILE   A HD11 1 
ATOM   513  H HD12 A ILE   A 1 23  ? 18.525 -2.022  7.188   0.40 13.47 ?  23  ILE   A HD12 1 
ATOM   514  H HD12 B ILE   A 1 23  ? 18.964 -2.310  7.337   0.60 13.72 ?  23  ILE   A HD12 1 
ATOM   515  H HD13 A ILE   A 1 23  ? 19.614 -0.866  7.225   0.40 13.47 ?  23  ILE   A HD13 1 
ATOM   516  H HD13 B ILE   A 1 23  ? 20.053 -1.158  7.442   0.60 13.72 ?  23  ILE   A HD13 1 
ATOM   517  N N    A VAL   A 1 24  ? 17.127 2.811   10.313  0.40 12.31 ?  24  VAL   A N    1 
ATOM   518  N N    B VAL   A 1 24  ? 17.412 2.505   10.412  0.60 12.83 ?  24  VAL   A N    1 
ATOM   519  C CA   A VAL   A 1 24  ? 17.810 3.784   11.165  0.40 13.44 ?  24  VAL   A CA   1 
ATOM   520  C CA   B VAL   A 1 24  ? 18.051 3.475   11.301  0.60 14.07 ?  24  VAL   A CA   1 
ATOM   521  C C    A VAL   A 1 24  ? 17.295 3.693   12.596  0.40 14.41 ?  24  VAL   A C    1 
ATOM   522  C C    B VAL   A 1 24  ? 17.467 3.381   12.706  0.60 14.71 ?  24  VAL   A C    1 
ATOM   523  O O    A VAL   A 1 24  ? 18.073 3.584   13.552  0.40 15.02 ?  24  VAL   A O    1 
ATOM   524  O O    B VAL   A 1 24  ? 18.199 3.412   13.705  0.60 15.25 ?  24  VAL   A O    1 
ATOM   525  C CB   A VAL   A 1 24  ? 17.654 5.205   10.596  0.40 13.92 ?  24  VAL   A CB   1 
ATOM   526  C CB   B VAL   A 1 24  ? 17.908 4.892   10.712  0.60 15.35 ?  24  VAL   A CB   1 
ATOM   527  C CG1  A VAL   A 1 24  ? 18.159 6.236   11.601  0.40 14.33 ?  24  VAL   A CG1  1 
ATOM   528  C CG1  B VAL   A 1 24  ? 18.454 5.932   11.675  0.60 16.40 ?  24  VAL   A CG1  1 
ATOM   529  C CG2  A VAL   A 1 24  ? 18.391 5.332   9.274   0.40 14.21 ?  24  VAL   A CG2  1 
ATOM   530  C CG2  B VAL   A 1 24  ? 18.599 4.973   9.354   0.60 16.10 ?  24  VAL   A CG2  1 
ATOM   531  H H    A VAL   A 1 24  ? 16.644 3.157   9.690   0.40 14.76 ?  24  VAL   A H    1 
ATOM   532  H H    B VAL   A 1 24  ? 16.995 2.852   9.749   0.60 15.38 ?  24  VAL   A H    1 
ATOM   533  H HA   A VAL   A 1 24  ? 18.756 3.577   11.177  0.40 16.12 ?  24  VAL   A HA   1 
ATOM   534  H HA   B VAL   A 1 24  ? 19.000 3.274   11.355  0.60 16.88 ?  24  VAL   A HA   1 
ATOM   535  H HB   A VAL   A 1 24  ? 16.713 5.384   10.432  0.40 16.69 ?  24  VAL   A HB   1 
ATOM   536  H HB   B VAL   A 1 24  ? 16.967 5.078   10.573  0.60 18.41 ?  24  VAL   A HB   1 
ATOM   537  H HG11 A VAL   A 1 24  ? 18.321 7.073   11.139  0.40 17.18 ?  24  VAL   A HG11 1 
ATOM   538  H HG11 B VAL   A 1 24  ? 18.551 6.773   11.202  0.60 19.67 ?  24  VAL   A HG11 1 
ATOM   539  H HG12 A VAL   A 1 24  ? 17.490 6.364   12.291  0.40 17.18 ?  24  VAL   A HG12 1 
ATOM   540  H HG12 B VAL   A 1 24  ? 17.833 6.036   12.411  0.60 19.67 ?  24  VAL   A HG12 1 
ATOM   541  H HG13 A VAL   A 1 24  ? 18.986 5.911   11.993  0.40 17.18 ?  24  VAL   A HG13 1 
ATOM   542  H HG13 B VAL   A 1 24  ? 19.316 5.635   12.002  0.60 19.67 ?  24  VAL   A HG13 1 
ATOM   543  H HG21 A VAL   A 1 24  ? 18.156 6.176   8.860   0.40 17.05 ?  24  VAL   A HG21 1 
ATOM   544  H HG21 B VAL   A 1 24  ? 18.520 5.877   9.011   0.60 19.32 ?  24  VAL   A HG21 1 
ATOM   545  H HG22 A VAL   A 1 24  ? 19.346 5.303   9.442   0.40 17.05 ?  24  VAL   A HG22 1 
ATOM   546  H HG22 B VAL   A 1 24  ? 19.536 4.742   9.461   0.60 19.32 ?  24  VAL   A HG22 1 
ATOM   547  H HG23 A VAL   A 1 24  ? 18.133 4.597   8.695   0.40 17.05 ?  24  VAL   A HG23 1 
ATOM   548  H HG23 B VAL   A 1 24  ? 18.175 4.350   8.741   0.60 19.32 ?  24  VAL   A HG23 1 
ATOM   549  N N    A GLU   A 1 25  ? 15.973 3.750   12.764  0.40 14.89 ?  25  GLU   A N    1 
ATOM   550  N N    B GLU   A 1 25  ? 16.139 3.271   12.803  0.60 15.32 ?  25  GLU   A N    1 
ATOM   551  C CA   A GLU   A 1 25  ? 15.403 3.694   14.105  0.40 15.61 ?  25  GLU   A CA   1 
ATOM   552  C CA   B GLU   A 1 25  ? 15.492 3.168   14.106  0.60 16.68 ?  25  GLU   A CA   1 
ATOM   553  C C    A GLU   A 1 25  ? 15.622 2.334   14.752  0.40 14.70 ?  25  GLU   A C    1 
ATOM   554  C C    B GLU   A 1 25  ? 15.778 1.824   14.767  0.60 16.04 ?  25  GLU   A C    1 
ATOM   555  O O    A GLU   A 1 25  ? 15.805 2.255   15.972  0.40 15.04 ?  25  GLU   A O    1 
ATOM   556  O O    B GLU   A 1 25  ? 16.007 1.765   15.981  0.60 16.46 ?  25  GLU   A O    1 
ATOM   557  C CB   A GLU   A 1 25  ? 13.918 4.053   14.064  0.40 17.63 ?  25  GLU   A CB   1 
ATOM   558  C CB   B GLU   A 1 25  ? 13.990 3.418   13.963  0.60 18.29 ?  25  GLU   A CB   1 
ATOM   559  C CG   A GLU   A 1 25  ? 13.658 5.508   13.693  0.40 19.97 ?  25  GLU   A CG   1 
ATOM   560  C CG   B GLU   A 1 25  ? 13.669 4.845   13.555  0.60 20.78 ?  25  GLU   A CG   1 
ATOM   561  C CD   A GLU   A 1 25  ? 14.460 6.497   14.527  0.40 21.72 ?  25  GLU   A CD   1 
ATOM   562  C CD   B GLU   A 1 25  ? 14.214 5.857   14.542  0.60 22.89 ?  25  GLU   A CD   1 
ATOM   563  O OE1  A GLU   A 1 25  ? 14.611 6.272   15.746  0.40 22.08 ?  25  GLU   A OE1  1 
ATOM   564  O OE1  B GLU   A 1 25  ? 14.016 5.670   15.762  0.60 23.56 ?  25  GLU   A OE1  1 
ATOM   565  O OE2  A GLU   A 1 25  ? 14.953 7.497   13.957  0.40 22.90 -1 25  GLU   A OE2  1 
ATOM   566  O OE2  B GLU   A 1 25  ? 14.861 6.827   14.098  0.60 23.94 -1 25  GLU   A OE2  1 
ATOM   567  H H    A GLU   A 1 25  ? 15.396 3.831   12.129  0.40 17.87 ?  25  GLU   A H    1 
ATOM   568  H H    B GLU   A 1 25  ? 15.603 3.254   12.131  0.60 18.37 ?  25  GLU   A H    1 
ATOM   569  H HA   A GLU   A 1 25  ? 15.853 4.347   14.659  0.40 18.73 ?  25  GLU   A HA   1 
ATOM   570  H HA   B GLU   A 1 25  ? 15.860 3.847   14.683  0.60 20.00 ?  25  GLU   A HA   1 
ATOM   571  H HB2  A GLU   A 1 25  ? 13.476 3.497   13.398  0.40 21.15 ?  25  GLU   A HB2  1 
ATOM   572  H HB2  B GLU   A 1 25  ? 13.634 2.824   13.283  0.60 21.94 ?  25  GLU   A HB2  1 
ATOM   573  H HB3  A GLU   A 1 25  ? 13.527 3.892   14.936  0.40 21.15 ?  25  GLU   A HB3  1 
ATOM   574  H HB3  B GLU   A 1 25  ? 13.561 3.244   14.814  0.60 21.94 ?  25  GLU   A HB3  1 
ATOM   575  H HG2  A GLU   A 1 25  ? 13.907 5.644   12.770  0.40 23.95 ?  25  GLU   A HG2  1 
ATOM   576  H HG2  B GLU   A 1 25  ? 14.071 5.029   12.691  0.60 24.93 ?  25  GLU   A HG2  1 
ATOM   577  H HG3  A GLU   A 1 25  ? 12.717 5.698   13.824  0.40 23.95 ?  25  GLU   A HG3  1 
ATOM   578  H HG3  B GLU   A 1 25  ? 12.706 4.952   13.504  0.60 24.93 ?  25  GLU   A HG3  1 
ATOM   579  N N    A GLU   A 1 26  ? 15.618 1.260   13.959  0.40 14.50 ?  26  GLU   A N    1 
ATOM   580  N N    B GLU   A 1 26  ? 15.783 0.736   13.989  0.60 15.71 ?  26  GLU   A N    1 
ATOM   581  C CA   A GLU   A 1 26  ? 15.904 -0.061  14.510  0.40 14.62 ?  26  GLU   A CA   1 
ATOM   582  C CA   B GLU   A 1 26  ? 16.156 -0.563  14.543  0.60 15.89 ?  26  GLU   A CA   1 
ATOM   583  C C    A GLU   A 1 26  ? 17.328 -0.131  15.040  0.40 14.15 ?  26  GLU   A C    1 
ATOM   584  C C    B GLU   A 1 26  ? 17.575 -0.533  15.090  0.60 15.18 ?  26  GLU   A C    1 
ATOM   585  O O    A GLU   A 1 26  ? 17.571 -0.640  16.140  0.40 14.33 ?  26  GLU   A O    1 
ATOM   586  O O    B GLU   A 1 26  ? 17.841 -1.055  16.179  0.60 15.66 ?  26  GLU   A O    1 
ATOM   587  C CB   A GLU   A 1 26  ? 15.692 -1.133  13.442  0.40 15.61 ?  26  GLU   A CB   1 
ATOM   588  C CB   B GLU   A 1 26  ? 16.023 -1.659  13.479  0.60 17.13 ?  26  GLU   A CB   1 
ATOM   589  C CG   A GLU   A 1 26  ? 14.254 -1.553  13.252  0.40 17.68 ?  26  GLU   A CG   1 
ATOM   590  C CG   B GLU   A 1 26  ? 14.606 -2.091  13.188  0.60 18.52 ?  26  GLU   A CG   1 
ATOM   591  C CD   A GLU   A 1 26  ? 13.745 -2.415  14.389  0.40 19.46 ?  26  GLU   A CD   1 
ATOM   592  C CD   B GLU   A 1 26  ? 13.932 -2.712  14.386  0.60 19.11 ?  26  GLU   A CD   1 
ATOM   593  O OE1  A GLU   A 1 26  ? 14.359 -3.469  14.653  0.40 20.03 ?  26  GLU   A OE1  1 
ATOM   594  O OE1  B GLU   A 1 26  ? 14.335 -3.819  14.824  0.60 19.59 ?  26  GLU   A OE1  1 
ATOM   595  O OE2  A GLU   A 1 26  ? 12.741 -2.028  15.024  0.40 20.61 -1 26  GLU   A OE2  1 
ATOM   596  O OE2  B GLU   A 1 26  ? 12.994 -2.076  14.886  0.60 19.51 -1 26  GLU   A OE2  1 
ATOM   597  H H    A GLU   A 1 26  ? 15.456 1.278   13.113  0.40 17.39 ?  26  GLU   A H    1 
ATOM   598  H H    B GLU   A 1 26  ? 15.587 0.719   13.152  0.60 18.84 ?  26  GLU   A H    1 
ATOM   599  H HA   A GLU   A 1 26  ? 15.296 -0.235  15.241  0.40 17.53 ?  26  GLU   A HA   1 
ATOM   600  H HA   B GLU   A 1 26  ? 15.570 -0.784  15.276  0.60 19.06 ?  26  GLU   A HA   1 
ATOM   601  H HB2  A GLU   A 1 26  ? 16.012 -0.793  12.592  0.40 18.73 ?  26  GLU   A HB2  1 
ATOM   602  H HB2  B GLU   A 1 26  ? 16.400 -1.341  12.646  0.60 20.55 ?  26  GLU   A HB2  1 
ATOM   603  H HB3  A GLU   A 1 26  ? 16.200 -1.919  13.692  0.40 18.73 ?  26  GLU   A HB3  1 
ATOM   604  H HB3  B GLU   A 1 26  ? 16.507 -2.451  13.773  0.60 20.55 ?  26  GLU   A HB3  1 
ATOM   605  H HG2  A GLU   A 1 26  ? 13.696 -0.766  13.219  0.40 21.21 ?  26  GLU   A HG2  1 
ATOM   606  H HG2  B GLU   A 1 26  ? 14.087 -1.319  12.903  0.60 22.22 ?  26  GLU   A HG2  1 
ATOM   607  H HG3  A GLU   A 1 26  ? 14.181 -2.052  12.421  0.40 21.21 ?  26  GLU   A HG3  1 
ATOM   608  H HG3  B GLU   A 1 26  ? 14.601 -2.768  12.498  0.60 22.22 ?  26  GLU   A HG3  1 
ATOM   609  N N    A ALA   A 1 27  ? 18.288 0.381   14.266  0.40 14.06 ?  27  ALA   A N    1 
ATOM   610  N N    B ALA   A 1 27  ? 18.503 0.079   14.352  0.60 14.59 ?  27  ALA   A N    1 
ATOM   611  C CA   A ALA   A 1 27  ? 19.684 0.300   14.678  0.40 14.62 ?  27  ALA   A CA   1 
ATOM   612  C CA   B ALA   A 1 27  ? 19.882 0.151   14.819  0.60 14.95 ?  27  ALA   A CA   1 
ATOM   613  C C    A ALA   A 1 27  ? 19.915 1.049   15.983  0.40 16.12 ?  27  ALA   A C    1 
ATOM   614  C C    B ALA   A 1 27  ? 19.981 0.996   16.082  0.60 16.04 ?  27  ALA   A C    1 
ATOM   615  O O    A ALA   A 1 27  ? 20.600 0.548   16.883  0.40 16.09 ?  27  ALA   A O    1 
ATOM   616  O O    B ALA   A 1 27  ? 20.634 0.603   17.055  0.60 16.32 ?  27  ALA   A O    1 
ATOM   617  C CB   A ALA   A 1 27  ? 20.588 0.843   13.571  0.40 14.21 ?  27  ALA   A CB   1 
ATOM   618  C CB   B ALA   A 1 27  ? 20.787 0.699   13.712  0.60 14.68 ?  27  ALA   A CB   1 
ATOM   619  H H    A ALA   A 1 27  ? 18.154 0.783   13.515  0.40 16.86 ?  27  ALA   A H    1 
ATOM   620  H H    B ALA   A 1 27  ? 18.364 0.451   13.591  0.60 17.50 ?  27  ALA   A H    1 
ATOM   621  H HA   A ALA   A 1 27  ? 19.913 -0.629  14.820  0.40 17.54 ?  27  ALA   A HA   1 
ATOM   622  H HA   B ALA   A 1 27  ? 20.194 -0.742  15.034  0.60 17.94 ?  27  ALA   A HA   1 
ATOM   623  H HB1  A ALA   A 1 27  ? 21.512 0.780   13.858  0.40 17.05 ?  27  ALA   A HB1  1 
ATOM   624  H HB1  B ALA   A 1 27  ? 21.702 0.741   14.039  0.60 17.60 ?  27  ALA   A HB1  1 
ATOM   625  H HB2  A ALA   A 1 27  ? 20.455 0.314   12.767  0.40 17.05 ?  27  ALA   A HB2  1 
ATOM   626  H HB2  B ALA   A 1 27  ? 20.744 0.106   12.943  0.60 17.60 ?  27  ALA   A HB2  1 
ATOM   627  H HB3  A ALA   A 1 27  ? 20.357 1.769   13.397  0.40 17.05 ?  27  ALA   A HB3  1 
ATOM   628  H HB3  B ALA   A 1 27  ? 20.486 1.585   13.462  0.60 17.60 ?  27  ALA   A HB3  1 
ATOM   629  N N    A LYS   A 1 28  ? 19.345 2.250   16.112  0.40 17.70 ?  28  LYS   A N    1 
ATOM   630  N N    B LYS   A 1 28  ? 19.327 2.162   16.091  0.60 17.08 ?  28  LYS   A N    1 
ATOM   631  C CA   A LYS   A 1 28  ? 19.533 3.033   17.328  0.40 19.84 ?  28  LYS   A CA   1 
ATOM   632  C CA   B LYS   A 1 28  ? 19.336 3.006   17.283  0.60 19.18 ?  28  LYS   A CA   1 
ATOM   633  C C    A LYS   A 1 28  ? 18.936 2.351   18.550  0.40 21.24 ?  28  LYS   A C    1 
ATOM   634  C C    B LYS   A 1 28  ? 18.873 2.226   18.506  0.60 20.40 ?  28  LYS   A C    1 
ATOM   635  O O    A LYS   A 1 28  ? 19.374 2.623   19.674  0.40 21.92 ?  28  LYS   A O    1 
ATOM   636  O O    B LYS   A 1 28  ? 19.478 2.318   19.580  0.60 21.76 ?  28  LYS   A O    1 
ATOM   637  C CB   A LYS   A 1 28  ? 18.922 4.426   17.161  0.40 20.72 ?  28  LYS   A CB   1 
ATOM   638  C CB   B LYS   A 1 28  ? 18.444 4.232   17.068  0.60 20.45 ?  28  LYS   A CB   1 
ATOM   639  C CG   A LYS   A 1 28  ? 19.688 5.316   16.198  0.40 21.76 ?  28  LYS   A CG   1 
ATOM   640  C CG   B LYS   A 1 28  ? 19.026 5.308   16.164  0.60 22.22 ?  28  LYS   A CG   1 
ATOM   641  C CD   A LYS   A 1 28  ? 19.200 6.755   16.239  0.40 22.98 ?  28  LYS   A CD   1 
ATOM   642  C CD   B LYS   A 1 28  ? 18.022 6.441   15.992  0.60 24.06 ?  28  LYS   A CD   1 
ATOM   643  C CE   A LYS   A 1 28  ? 17.857 6.912   15.551  0.40 24.03 ?  28  LYS   A CE   1 
ATOM   644  C CE   B LYS   A 1 28  ? 18.545 7.543   15.090  0.60 25.53 ?  28  LYS   A CE   1 
ATOM   645  N NZ   A LYS   A 1 28  ? 17.433 8.337   15.502  0.40 24.66 ?  28  LYS   A NZ   1 
ATOM   646  N NZ   B LYS   A 1 28  ? 17.513 8.598   14.864  0.60 26.56 ?  28  LYS   A NZ   1 
ATOM   647  H H    A LYS   A 1 28  ? 18.853 2.624   15.515  0.40 21.24 ?  28  LYS   A H    1 
ATOM   648  H H    B LYS   A 1 28  ? 18.877 2.477   15.430  0.60 20.49 ?  28  LYS   A H    1 
ATOM   649  H HA   A LYS   A 1 28  ? 20.484 3.144   17.480  0.40 23.81 ?  28  LYS   A HA   1 
ATOM   650  H HA   B LYS   A 1 28  ? 20.236 3.318   17.452  0.60 23.00 ?  28  LYS   A HA   1 
ATOM   651  H HB2  A LYS   A 1 28  ? 18.018 4.332   16.826  0.40 24.86 ?  28  LYS   A HB2  1 
ATOM   652  H HB2  B LYS   A 1 28  ? 17.610 3.945   16.667  0.60 24.54 ?  28  LYS   A HB2  1 
ATOM   653  H HB3  A LYS   A 1 28  ? 18.909 4.866   18.026  0.40 24.86 ?  28  LYS   A HB3  1 
ATOM   654  H HB3  B LYS   A 1 28  ? 18.268 4.645   17.926  0.60 24.54 ?  28  LYS   A HB3  1 
ATOM   655  H HG2  A LYS   A 1 28  ? 20.628 5.309   16.436  0.40 26.11 ?  28  LYS   A HG2  1 
ATOM   656  H HG2  B LYS   A 1 28  ? 19.831 5.672   16.566  0.60 26.65 ?  28  LYS   A HG2  1 
ATOM   657  H HG3  A LYS   A 1 28  ? 19.570 4.983   15.295  0.40 26.11 ?  28  LYS   A HG3  1 
ATOM   658  H HG3  B LYS   A 1 28  ? 19.221 4.935   15.291  0.60 26.65 ?  28  LYS   A HG3  1 
ATOM   659  H HD2  A LYS   A 1 28  ? 19.101 7.033   17.163  0.40 27.57 ?  28  LYS   A HD2  1 
ATOM   660  H HD2  B LYS   A 1 28  ? 17.208 6.088   15.596  0.60 28.86 ?  28  LYS   A HD2  1 
ATOM   661  H HD3  A LYS   A 1 28  ? 19.842 7.323   15.785  0.40 27.57 ?  28  LYS   A HD3  1 
ATOM   662  H HD3  B LYS   A 1 28  ? 17.826 6.829   16.860  0.60 28.86 ?  28  LYS   A HD3  1 
ATOM   663  H HE2  A LYS   A 1 28  ? 17.925 6.584   14.640  0.40 28.83 ?  28  LYS   A HE2  1 
ATOM   664  H HE2  B LYS   A 1 28  ? 19.317 7.958   15.505  0.60 30.63 ?  28  LYS   A HE2  1 
ATOM   665  H HE3  A LYS   A 1 28  ? 17.186 6.411   16.039  0.40 28.83 ?  28  LYS   A HE3  1 
ATOM   666  H HE3  B LYS   A 1 28  ? 18.787 7.167   14.230  0.60 30.63 ?  28  LYS   A HE3  1 
ATOM   667  H HZ1  A LYS   A 1 28  ? 16.646 8.407   15.094  0.40 29.59 ?  28  LYS   A HZ1  1 
ATOM   668  H HZ1  B LYS   A 1 28  ? 17.838 9.234   14.335  0.60 31.87 ?  28  LYS   A HZ1  1 
ATOM   669  H HZ2  A LYS   A 1 28  ? 17.362 8.662   16.328  0.40 29.59 ?  28  LYS   A HZ2  1 
ATOM   670  H HZ2  B LYS   A 1 28  ? 16.792 8.242   14.481  0.60 31.87 ?  28  LYS   A HZ2  1 
ATOM   671  H HZ3  A LYS   A 1 28  ? 18.034 8.819   15.054  0.40 29.59 ?  28  LYS   A HZ3  1 
ATOM   672  H HZ3  B LYS   A 1 28  ? 17.275 8.962   15.642  0.60 31.87 ?  28  LYS   A HZ3  1 
ATOM   673  N N    A LYS   A 1 29  ? 17.944 1.480   18.358  0.40 22.27 ?  29  LYS   A N    1 
ATOM   674  N N    B LYS   A 1 29  ? 17.810 1.433   18.353  0.60 20.80 ?  29  LYS   A N    1 
ATOM   675  C CA   A LYS   A 1 29  ? 17.328 0.777   19.480  0.40 23.61 ?  29  LYS   A CA   1 
ATOM   676  C CA   B LYS   A 1 29  ? 17.228 0.715   19.483  0.60 22.50 ?  29  LYS   A CA   1 
ATOM   677  C C    A LYS   A 1 29  ? 18.133 -0.456  19.879  0.40 22.81 ?  29  LYS   A C    1 
ATOM   678  C C    B LYS   A 1 29  ? 18.072 -0.491  19.881  0.60 22.19 ?  29  LYS   A C    1 
ATOM   679  O O    A LYS   A 1 29  ? 18.432 -0.656  21.062  0.40 23.41 ?  29  LYS   A O    1 
ATOM   680  O O    B LYS   A 1 29  ? 18.336 -0.708  21.070  0.60 22.82 ?  29  LYS   A O    1 
ATOM   681  C CB   A LYS   A 1 29  ? 15.896 0.382   19.113  0.40 26.08 ?  29  LYS   A CB   1 
ATOM   682  C CB   B LYS   A 1 29  ? 15.810 0.263   19.127  0.60 25.30 ?  29  LYS   A CB   1 
ATOM   683  C CG   A LYS   A 1 29  ? 15.124 -0.301  20.232  0.40 28.34 ?  29  LYS   A CG   1 
ATOM   684  C CG   B LYS   A 1 29  ? 15.020 -0.304  20.295  0.60 28.13 ?  29  LYS   A CG   1 
ATOM   685  C CD   A LYS   A 1 29  ? 14.757 0.680   21.334  0.40 30.24 ?  29  LYS   A CD   1 
ATOM   686  C CD   B LYS   A 1 29  ? 14.662 0.781   21.297  0.60 30.50 ?  29  LYS   A CD   1 
ATOM   687  C CE   A LYS   A 1 29  ? 13.877 0.024   22.387  0.40 31.51 ?  29  LYS   A CE   1 
ATOM   688  C CE   B LYS   A 1 29  ? 13.802 0.237   22.424  0.60 32.05 ?  29  LYS   A CE   1 
ATOM   689  N NZ   A LYS   A 1 29  ? 13.421 0.996   23.419  0.40 32.12 ?  29  LYS   A NZ   1 
ATOM   690  N NZ   B LYS   A 1 29  ? 13.442 1.295   23.407  0.60 32.83 ?  29  LYS   A NZ   1 
ATOM   691  H H    A LYS   A 1 29  ? 17.607 1.289   17.590  0.40 26.72 ?  29  LYS   A H    1 
ATOM   692  H H    B LYS   A 1 29  ? 17.411 1.290   17.603  0.60 24.96 ?  29  LYS   A H    1 
ATOM   693  H HA   A LYS   A 1 29  ? 17.291 1.370   20.242  0.40 28.33 ?  29  LYS   A HA   1 
ATOM   694  H HA   B LYS   A 1 29  ? 17.175 1.311   20.244  0.60 27.00 ?  29  LYS   A HA   1 
ATOM   695  H HB2  A LYS   A 1 29  ? 15.407 1.183   18.867  0.40 31.29 ?  29  LYS   A HB2  1 
ATOM   696  H HB2  B LYS   A 1 29  ? 15.318 1.024   18.783  0.60 30.35 ?  29  LYS   A HB2  1 
ATOM   697  H HB3  A LYS   A 1 29  ? 15.923 -0.228  18.359  0.40 31.29 ?  29  LYS   A HB3  1 
ATOM   698  H HB3  B LYS   A 1 29  ? 15.864 -0.427  18.447  0.60 30.35 ?  29  LYS   A HB3  1 
ATOM   699  H HG2  A LYS   A 1 29  ? 14.304 -0.672  19.872  0.40 34.00 ?  29  LYS   A HG2  1 
ATOM   700  H HG2  B LYS   A 1 29  ? 14.196 -0.696  19.964  0.60 33.75 ?  29  LYS   A HG2  1 
ATOM   701  H HG3  A LYS   A 1 29  ? 15.665 -1.007  20.620  0.40 34.00 ?  29  LYS   A HG3  1 
ATOM   702  H HG3  B LYS   A 1 29  ? 15.551 -0.977  20.750  0.60 33.75 ?  29  LYS   A HG3  1 
ATOM   703  H HD2  A LYS   A 1 29  ? 15.566 0.995   21.767  0.40 36.27 ?  29  LYS   A HD2  1 
ATOM   704  H HD2  B LYS   A 1 29  ? 15.475 1.142   21.684  0.60 36.60 ?  29  LYS   A HD2  1 
ATOM   705  H HD3  A LYS   A 1 29  ? 14.268 1.425   20.950  0.40 36.27 ?  29  LYS   A HD3  1 
ATOM   706  H HD3  B LYS   A 1 29  ? 14.166 1.482   20.845  0.60 36.60 ?  29  LYS   A HD3  1 
ATOM   707  H HE2  A LYS   A 1 29  ? 13.092 -0.352  21.957  0.40 37.80 ?  29  LYS   A HE2  1 
ATOM   708  H HE2  B LYS   A 1 29  ? 12.982 -0.125  22.053  0.60 38.45 ?  29  LYS   A HE2  1 
ATOM   709  H HE3  A LYS   A 1 29  ? 14.381 -0.676  22.832  0.40 37.80 ?  29  LYS   A HE3  1 
ATOM   710  H HE3  B LYS   A 1 29  ? 14.292 -0.458  22.892  0.60 38.45 ?  29  LYS   A HE3  1 
ATOM   711  H HZ1  A LYS   A 1 29  ? 12.910 0.584   24.020  0.40 38.54 ?  29  LYS   A HZ1  1 
ATOM   712  H HZ1  B LYS   A 1 29  ? 12.939 0.950   24.055  0.60 39.39 ?  29  LYS   A HZ1  1 
ATOM   713  H HZ2  A LYS   A 1 29  ? 14.124 1.352   23.833  0.40 38.54 ?  29  LYS   A HZ2  1 
ATOM   714  H HZ2  B LYS   A 1 29  ? 14.180 1.640   23.766  0.60 39.39 ?  29  LYS   A HZ2  1 
ATOM   715  H HZ3  A LYS   A 1 29  ? 12.950 1.647   23.036  0.40 38.54 ?  29  LYS   A HZ3  1 
ATOM   716  H HZ3  B LYS   A 1 29  ? 12.987 1.944   23.002  0.60 39.39 ?  29  LYS   A HZ3  1 
ATOM   717  N N    . VAL   A 1 30  ? 18.486 -1.294  18.905  1.00 21.67 ?  30  VAL   A N    1 
ATOM   718  C CA   . VAL   A 1 30  ? 19.147 -2.560  19.205  1.00 21.19 ?  30  VAL   A CA   1 
ATOM   719  C C    . VAL   A 1 30  ? 20.650 -2.404  19.423  1.00 20.60 ?  30  VAL   A C    1 
ATOM   720  O O    . VAL   A 1 30  ? 21.239 -3.142  20.221  1.00 21.13 ?  30  VAL   A O    1 
ATOM   721  C CB   . VAL   A 1 30  ? 18.837 -3.558  18.074  1.00 22.42 ?  30  VAL   A CB   1 
ATOM   722  C CG1  . VAL   A 1 30  ? 19.622 -4.850  18.250  1.00 23.06 ?  30  VAL   A CG1  1 
ATOM   723  C CG2  . VAL   A 1 30  ? 17.343 -3.841  18.016  1.00 23.10 ?  30  VAL   A CG2  1 
ATOM   724  H H    A VAL   A 1 30  ? 18.358 -1.155  18.065  0.40 26.00 ?  30  VAL   A H    1 
ATOM   725  H H    B VAL   A 1 30  ? 18.394 -1.136  18.063  0.60 26.00 ?  30  VAL   A H    1 
ATOM   726  H HA   . VAL   A 1 30  ? 18.765 -2.922  20.019  1.00 25.42 ?  30  VAL   A HA   1 
ATOM   727  H HB   . VAL   A 1 30  ? 19.097 -3.168  17.226  1.00 26.89 ?  30  VAL   A HB   1 
ATOM   728  H HG11 . VAL   A 1 30  ? 19.239 -5.531  17.672  1.00 27.66 ?  30  VAL   A HG11 1 
ATOM   729  H HG12 . VAL   A 1 30  ? 20.547 -4.696  18.008  1.00 27.66 ?  30  VAL   A HG12 1 
ATOM   730  H HG13 . VAL   A 1 30  ? 19.560 -5.133  19.175  1.00 27.66 ?  30  VAL   A HG13 1 
ATOM   731  H HG21 . VAL   A 1 30  ? 17.171 -4.509  17.332  1.00 27.72 ?  30  VAL   A HG21 1 
ATOM   732  H HG22 . VAL   A 1 30  ? 17.050 -4.174  18.880  1.00 27.72 ?  30  VAL   A HG22 1 
ATOM   733  H HG23 . VAL   A 1 30  ? 16.872 -3.021  17.801  1.00 27.72 ?  30  VAL   A HG23 1 
ATOM   734  N N    . LYS   A 1 31  ? 21.285 -1.455  18.745  1.00 19.34 ?  31  LYS   A N    1 
ATOM   735  C CA   . LYS   A 1 31  ? 22.738 -1.345  18.704  1.00 20.07 ?  31  LYS   A CA   1 
ATOM   736  C C    . LYS   A 1 31  ? 23.343 -2.699  18.321  1.00 18.19 ?  31  LYS   A C    1 
ATOM   737  O O    . LYS   A 1 31  ? 24.130 -3.275  19.078  1.00 19.20 ?  31  LYS   A O    1 
ATOM   738  C CB   . LYS   A 1 31  ? 23.314 -0.840  20.020  1.00 24.50 ?  31  LYS   A CB   1 
ATOM   739  C CG   . LYS   A 1 31  ? 22.646 0.426   20.540  1.00 29.87 ?  31  LYS   A CG   1 
ATOM   740  C CD   . LYS   A 1 31  ? 23.669 1.491   20.907  1.00 34.11 ?  31  LYS   A CD   1 
ATOM   741  C CE   . LYS   A 1 31  ? 23.068 2.547   21.823  1.00 36.91 ?  31  LYS   A CE   1 
ATOM   742  N NZ   . LYS   A 1 31  ? 21.843 3.172   21.252  1.00 38.19 ?  31  LYS   A NZ   1 
ATOM   743  H H    . LYS   A 1 31  ? 20.884 -0.848  18.290  1.00 23.20 ?  31  LYS   A H    1 
ATOM   744  H HA   . LYS   A 1 31  ? 22.975 -0.707  18.017  1.00 24.07 ?  31  LYS   A HA   1 
ATOM   745  H HB2  . LYS   A 1 31  ? 23.212 -1.530  20.692  1.00 29.39 ?  31  LYS   A HB2  1 
ATOM   746  H HB3  . LYS   A 1 31  ? 24.258 -0.645  19.891  1.00 29.39 ?  31  LYS   A HB3  1 
ATOM   747  H HG2  . LYS   A 1 31  ? 22.065 0.789   19.853  1.00 35.84 ?  31  LYS   A HG2  1 
ATOM   748  H HG3  . LYS   A 1 31  ? 22.131 0.214   21.335  1.00 35.84 ?  31  LYS   A HG3  1 
ATOM   749  H HD2  . LYS   A 1 31  ? 24.414 1.076   21.369  1.00 40.92 ?  31  LYS   A HD2  1 
ATOM   750  H HD3  . LYS   A 1 31  ? 23.979 1.929   20.098  1.00 40.92 ?  31  LYS   A HD3  1 
ATOM   751  H HE2  . LYS   A 1 31  ? 22.828 2.134   22.667  1.00 44.29 ?  31  LYS   A HE2  1 
ATOM   752  H HE3  . LYS   A 1 31  ? 23.722 3.248   21.970  1.00 44.29 ?  31  LYS   A HE3  1 
ATOM   753  H HZ1  . LYS   A 1 31  ? 21.535 3.798   21.805  1.00 45.82 ?  31  LYS   A HZ1  1 
ATOM   754  H HZ2  . LYS   A 1 31  ? 22.031 3.547   20.467  1.00 45.82 ?  31  LYS   A HZ2  1 
ATOM   755  H HZ3  . LYS   A 1 31  ? 21.213 2.555   21.134  1.00 45.82 ?  31  LYS   A HZ3  1 
ATOM   756  N N    . PRO   A 1 32  ? 22.978 -3.235  17.163  1.00 16.02 ?  32  PRO   A N    1 
ATOM   757  C CA   . PRO   A 1 32  ? 23.447 -4.568  16.791  1.00 16.10 ?  32  PRO   A CA   1 
ATOM   758  C C    . PRO   A 1 32  ? 24.948 -4.575  16.584  1.00 16.18 ?  32  PRO   A C    1 
ATOM   759  O O    . PRO   A 1 32  ? 25.589 -3.538  16.387  1.00 15.99 ?  32  PRO   A O    1 
ATOM   760  C CB   . PRO   A 1 32  ? 22.714 -4.837  15.473  1.00 16.10 ?  32  PRO   A CB   1 
ATOM   761  C CG   . PRO   A 1 32  ? 22.539 -3.470  14.879  1.00 14.80 ?  32  PRO   A CG   1 
ATOM   762  C CD   . PRO   A 1 32  ? 22.254 -2.580  16.062  1.00 15.02 ?  32  PRO   A CD   1 
ATOM   763  H HA   . PRO   A 1 32  ? 23.197 -5.228  17.455  1.00 19.31 ?  32  PRO   A HA   1 
ATOM   764  H HB2  . PRO   A 1 32  ? 23.258 -5.402  14.898  1.00 19.31 ?  32  PRO   A HB2  1 
ATOM   765  H HB3  . PRO   A 1 32  ? 21.854 -5.255  15.651  1.00 19.31 ?  32  PRO   A HB3  1 
ATOM   766  H HG2  . PRO   A 1 32  ? 23.353 -3.206  14.427  1.00 17.76 ?  32  PRO   A HG2  1 
ATOM   767  H HG3  . PRO   A 1 32  ? 21.788 -3.481  14.260  1.00 17.76 ?  32  PRO   A HG3  1 
ATOM   768  H HD2  . PRO   A 1 32  ? 22.609 -1.692  15.894  1.00 18.02 ?  32  PRO   A HD2  1 
ATOM   769  H HD3  . PRO   A 1 32  ? 21.304 -2.558  16.240  1.00 18.02 ?  32  PRO   A HD3  1 
ATOM   770  N N    . THR   A 1 33  ? 25.506 -5.782  16.618  1.00 16.18 ?  33  THR   A N    1 
ATOM   771  C CA   . THR   A 1 33  ? 26.915 -5.941  16.290  1.00 16.37 ?  33  THR   A CA   1 
ATOM   772  C C    . THR   A 1 33  ? 27.202 -5.477  14.868  1.00 14.51 ?  33  THR   A C    1 
ATOM   773  O O    . THR   A 1 33  ? 28.230 -4.836  14.614  1.00 14.75 ?  33  THR   A O    1 
ATOM   774  C CB   . THR   A 1 33  ? 27.320 -7.400  16.485  1.00 17.81 ?  33  THR   A CB   1 
ATOM   775  O OG1  . THR   A 1 33  ? 27.011 -7.798  17.825  1.00 19.51 ?  33  THR   A OG1  1 
ATOM   776  C CG2  . THR   A 1 33  ? 28.807 -7.586  16.232  1.00 18.76 ?  33  THR   A CG2  1 
ATOM   777  H H    . THR   A 1 33  ? 25.098 -6.510  16.825  1.00 19.40 ?  33  THR   A H    1 
ATOM   778  H HA   . THR   A 1 33  ? 27.444 -5.402  16.899  1.00 19.63 ?  33  THR   A HA   1 
ATOM   779  H HB   . THR   A 1 33  ? 26.828 -7.960  15.860  1.00 21.37 ?  33  THR   A HB   1 
ATOM   780  H HG1  . THR   A 1 33  ? 27.430 -7.316  18.371  1.00 23.40 ?  33  THR   A HG1  1 
ATOM   781  H HG21 . THR   A 1 33  ? 29.078 -8.478  16.504  1.00 22.51 ?  33  THR   A HG21 1 
ATOM   782  H HG22 . THR   A 1 33  ? 29.003 -7.472  15.290  1.00 22.51 ?  33  THR   A HG22 1 
ATOM   783  H HG23 . THR   A 1 33  ? 29.312 -6.935  16.744  1.00 22.51 ?  33  THR   A HG23 1 
ATOM   784  N N    . VAL   A 1 34  ? 26.301 -5.781  13.933  1.00 13.42 ?  34  VAL   A N    1 
ATOM   785  C CA   . VAL   A 1 34  ? 26.489 -5.442  12.525  1.00 11.88 ?  34  VAL   A CA   1 
ATOM   786  C C    . VAL   A 1 34  ? 25.190 -4.881  11.962  1.00 11.26 ?  34  VAL   A C    1 
ATOM   787  O O    . VAL   A 1 34  ? 24.149 -5.549  12.004  1.00 11.97 ?  34  VAL   A O    1 
ATOM   788  C CB   . VAL   A 1 34  ? 26.927 -6.654  11.683  1.00 12.51 ?  34  VAL   A CB   1 
ATOM   789  C CG1  . VAL   A 1 34  ? 27.105 -6.244  10.230  1.00 12.96 ?  34  VAL   A CG1  1 
ATOM   790  C CG2  . VAL   A 1 34  ? 28.200 -7.278  12.241  1.00 13.78 ?  34  VAL   A CG2  1 
ATOM   791  H H    . VAL   A 1 34  ? 25.560 -6.188  14.095  1.00 16.10 ?  34  VAL   A H    1 
ATOM   792  H HA   . VAL   A 1 34  ? 27.168 -4.754  12.447  1.00 14.24 ?  34  VAL   A HA   1 
ATOM   793  H HB   . VAL   A 1 34  ? 26.223 -7.322  11.720  1.00 15.00 ?  34  VAL   A HB   1 
ATOM   794  H HG11 . VAL   A 1 34  ? 27.599 -6.938  9.769   1.00 15.54 ?  34  VAL   A HG11 1 
ATOM   795  H HG12 . VAL   A 1 34  ? 26.233 -6.131  9.818   1.00 15.54 ?  34  VAL   A HG12 1 
ATOM   796  H HG13 . VAL   A 1 34  ? 27.598 -5.409  10.196  1.00 15.54 ?  34  VAL   A HG13 1 
ATOM   797  H HG21 . VAL   A 1 34  ? 28.464 -8.014  11.668  1.00 16.53 ?  34  VAL   A HG21 1 
ATOM   798  H HG22 . VAL   A 1 34  ? 28.897 -6.606  12.264  1.00 16.53 ?  34  VAL   A HG22 1 
ATOM   799  H HG23 . VAL   A 1 34  ? 28.025 -7.606  13.139  1.00 16.53 ?  34  VAL   A HG23 1 
ATOM   800  N N    . VAL   A 1 35  ? 25.255 -3.669  11.410  1.00 10.68 ?  35  VAL   A N    1 
ATOM   801  C CA   . VAL   A 1 35  ? 24.222 -3.147  10.525  1.00 10.40 ?  35  VAL   A CA   1 
ATOM   802  C C    . VAL   A 1 35  ? 24.770 -3.149  9.104   1.00 9.61  ?  35  VAL   A C    1 
ATOM   803  O O    . VAL   A 1 35  ? 25.918 -2.749  8.869   1.00 10.14 ?  35  VAL   A O    1 
ATOM   804  C CB   . VAL   A 1 35  ? 23.704 -1.753  10.945  1.00 11.07 ?  35  VAL   A CB   1 
ATOM   805  C CG1  . VAL   A 1 35  ? 24.774 -0.666  10.807  1.00 11.72 ?  35  VAL   A CG1  1 
ATOM   806  C CG2  . VAL   A 1 35  ? 22.458 -1.389  10.141  1.00 11.63 ?  35  VAL   A CG2  1 
ATOM   807  H H    . VAL   A 1 35  ? 25.896 -3.113  11.535  1.00 12.81 ?  35  VAL   A H    1 
ATOM   808  H HA   . VAL   A 1 35  ? 23.457 -3.750  10.544  1.00 12.47 ?  35  VAL   A HA   1 
ATOM   809  H HB   . VAL   A 1 35  ? 23.436 -1.783  11.875  1.00 13.28 ?  35  VAL   A HB   1 
ATOM   810  H HG11 . VAL   A 1 35  ? 24.435 0.164   11.184  1.00 14.06 ?  35  VAL   A HG11 1 
ATOM   811  H HG12 . VAL   A 1 35  ? 25.566 -0.947  11.283  1.00 14.06 ?  35  VAL   A HG12 1 
ATOM   812  H HG13 . VAL   A 1 35  ? 24.977 -0.537  9.866   1.00 14.06 ?  35  VAL   A HG13 1 
ATOM   813  H HG21 . VAL   A 1 35  ? 22.114 -0.537  10.451  1.00 13.95 ?  35  VAL   A HG21 1 
ATOM   814  H HG22 . VAL   A 1 35  ? 22.696 -1.325  9.200   1.00 13.95 ?  35  VAL   A HG22 1 
ATOM   815  H HG23 . VAL   A 1 35  ? 21.789 -2.081  10.264  1.00 13.95 ?  35  VAL   A HG23 1 
ATOM   816  N N    . VAL   A 1 36  ? 23.953 -3.606  8.159   1.00 9.13  ?  36  VAL   A N    1 
ATOM   817  C CA   . VAL   A 1 36  ? 24.331 -3.624  6.752   1.00 8.87  ?  36  VAL   A CA   1 
ATOM   818  C C    . VAL   A 1 36  ? 23.874 -2.333  6.087   1.00 8.85  ?  36  VAL   A C    1 
ATOM   819  O O    . VAL   A 1 36  ? 22.713 -1.924  6.236   1.00 9.46  ?  36  VAL   A O    1 
ATOM   820  C CB   . VAL   A 1 36  ? 23.721 -4.837  6.031   1.00 8.92  ?  36  VAL   A CB   1 
ATOM   821  C CG1  . VAL   A 1 36  ? 23.987 -4.758  4.538   1.00 9.33  ?  36  VAL   A CG1  1 
ATOM   822  C CG2  . VAL   A 1 36  ? 24.258 -6.133  6.613   1.00 9.50  ?  36  VAL   A CG2  1 
ATOM   823  H H    . VAL   A 1 36  ? 23.162 -3.918  8.306   1.00 10.95 ?  36  VAL   A H    1 
ATOM   824  H HA   . VAL   A 1 36  ? 25.301 -3.685  6.679   1.00 10.63 ?  36  VAL   A HA   1 
ATOM   825  H HB   . VAL   A 1 36  ? 22.761 -4.822  6.161   1.00 10.70 ?  36  VAL   A HB   1 
ATOM   826  H HG11 . VAL   A 1 36  ? 23.847 -5.634  4.148   1.00 11.19 ?  36  VAL   A HG11 1 
ATOM   827  H HG12 . VAL   A 1 36  ? 23.377 -4.118  4.136   1.00 11.19 ?  36  VAL   A HG12 1 
ATOM   828  H HG13 . VAL   A 1 36  ? 24.905 -4.477  4.394   1.00 11.19 ?  36  VAL   A HG13 1 
ATOM   829  H HG21 . VAL   A 1 36  ? 23.867 -6.881  6.134   1.00 11.39 ?  36  VAL   A HG21 1 
ATOM   830  H HG22 . VAL   A 1 36  ? 25.223 -6.149  6.518   1.00 11.39 ?  36  VAL   A HG22 1 
ATOM   831  H HG23 . VAL   A 1 36  ? 24.017 -6.183  7.552   1.00 11.39 ?  36  VAL   A HG23 1 
ATOM   832  N N    A ASN   A 1 37  ? 24.769 -1.728  5.307   0.40 8.61  ?  37  ASN   A N    1 
ATOM   833  N N    B ASN   A 1 37  ? 24.801 -1.670  5.399   0.60 8.45  ?  37  ASN   A N    1 
ATOM   834  C CA   A ASN   A 1 37  ? 24.435 -0.591  4.465   0.40 8.53  ?  37  ASN   A CA   1 
ATOM   835  C CA   B ASN   A 1 37  ? 24.472 -0.567  4.514   0.60 8.28  ?  37  ASN   A CA   1 
ATOM   836  C C    A ASN   A 1 37  ? 24.264 -1.032  3.016   0.40 8.88  ?  37  ASN   A C    1 
ATOM   837  C C    B ASN   A 1 37  ? 24.365 -1.071  3.082   0.60 8.13  ?  37  ASN   A C    1 
ATOM   838  O O    A ASN   A 1 37  ? 25.022 -1.869  2.510   0.40 9.27  ?  37  ASN   A O    1 
ATOM   839  O O    B ASN   A 1 37  ? 25.186 -1.878  2.628   0.60 8.57  ?  37  ASN   A O    1 
ATOM   840  C CB   A ASN   A 1 37  ? 25.527 0.473   4.544   0.40 8.59  ?  37  ASN   A CB   1 
ATOM   841  C CB   B ASN   A 1 37  ? 25.527 0.535   4.597   0.60 8.66  ?  37  ASN   A CB   1 
ATOM   842  C CG   A ASN   A 1 37  ? 25.206 1.685   3.710   0.40 8.43  ?  37  ASN   A CG   1 
ATOM   843  C CG   B ASN   A 1 37  ? 25.197 1.713   3.713   0.60 8.94  ?  37  ASN   A CG   1 
ATOM   844  O OD1  A ASN   A 1 37  ? 24.040 2.055   3.565   0.40 8.85  ?  37  ASN   A OD1  1 
ATOM   845  O OD1  B ASN   A 1 37  ? 24.023 2.003   3.465   0.60 9.61  ?  37  ASN   A OD1  1 
ATOM   846  N ND2  A ASN   A 1 37  ? 26.235 2.310   3.152   0.40 8.48  ?  37  ASN   A ND2  1 
ATOM   847  N ND2  B ASN   A 1 37  ? 26.227 2.396   3.229   0.60 9.20  ?  37  ASN   A ND2  1 
ATOM   848  H H    A ASN   A 1 37  ? 25.597 -1.962  5.253   0.40 10.32 ?  37  ASN   A H    1 
ATOM   849  H H    B ASN   A 1 37  ? 25.646 -1.838  5.440   0.60 10.13 ?  37  ASN   A H    1 
ATOM   850  H HA   A ASN   A 1 37  ? 23.604 -0.197  4.768   0.40 10.22 ?  37  ASN   A HA   1 
ATOM   851  H HA   B ASN   A 1 37  ? 23.620 -0.186  4.775   0.60 9.92  ?  37  ASN   A HA   1 
ATOM   852  H HB2  A ASN   A 1 37  ? 25.626 0.760   5.465   0.40 10.30 ?  37  ASN   A HB2  1 
ATOM   853  H HB2  B ASN   A 1 37  ? 25.587 0.854   5.512   0.60 10.39 ?  37  ASN   A HB2  1 
ATOM   854  H HB3  A ASN   A 1 37  ? 26.363 0.096   4.222   0.40 10.30 ?  37  ASN   A HB3  1 
ATOM   855  H HB3  B ASN   A 1 37  ? 26.386 0.177   4.315   0.60 10.39 ?  37  ASN   A HB3  1 
ATOM   856  H HD21 A ASN   A 1 37  ? 26.099 3.003   2.664   0.40 10.17 ?  37  ASN   A HD21 1 
ATOM   857  H HD21 B ASN   A 1 37  ? 26.087 3.076   2.719   0.60 11.03 ?  37  ASN   A HD21 1 
ATOM   858  H HD22 A ASN   A 1 37  ? 27.030 2.023   3.273   0.40 10.17 ?  37  ASN   A HD22 1 
ATOM   859  H HD22 B ASN   A 1 37  ? 27.026 2.166   3.419   0.60 11.03 ?  37  ASN   A HD22 1 
ATOM   860  N N    A ALA   A 1 38  ? 23.261 -0.451  2.352   0.40 8.87  ?  38  ALA   A N    1 
ATOM   861  N N    B ALA   A 1 38  ? 23.339 -0.585  2.379   0.60 8.55  ?  38  ALA   A N    1 
ATOM   862  C CA   A ALA   A 1 38  ? 23.052 -0.613  0.913   0.40 8.52  ?  38  ALA   A CA   1 
ATOM   863  C CA   B ALA   A 1 38  ? 23.171 -0.821  0.946   0.60 8.83  ?  38  ALA   A CA   1 
ATOM   864  C C    A ALA   A 1 38  ? 23.962 0.380   0.187   0.40 8.25  ?  38  ALA   A C    1 
ATOM   865  C C    B ALA   A 1 38  ? 23.976 0.240   0.200   0.60 9.03  ?  38  ALA   A C    1 
ATOM   866  O O    A ALA   A 1 38  ? 23.548 1.462   -0.238  0.40 8.52  ?  38  ALA   A O    1 
ATOM   867  O O    B ALA   A 1 38  ? 23.470 1.290   -0.207  0.60 9.49  ?  38  ALA   A O    1 
ATOM   868  C CB   A ALA   A 1 38  ? 21.583 -0.396  0.566   0.40 8.93  ?  38  ALA   A CB   1 
ATOM   869  C CB   B ALA   A 1 38  ? 21.695 -0.788  0.575   0.60 9.77  ?  38  ALA   A CB   1 
ATOM   870  H H    A ALA   A 1 38  ? 22.677 0.059   2.728   0.40 10.63 ?  38  ALA   A H    1 
ATOM   871  H H    B ALA   A 1 38  ? 22.724 -0.096  2.723   0.60 10.26 ?  38  ALA   A H    1 
ATOM   872  H HA   A ALA   A 1 38  ? 23.301 -1.509  0.649   0.40 10.21 ?  38  ALA   A HA   1 
ATOM   873  H HA   B ALA   A 1 38  ? 23.528 -1.696  0.723   0.60 10.59 ?  38  ALA   A HA   1 
ATOM   874  H HB1  A ALA   A 1 38  ? 21.463 -0.507  -0.389  0.40 10.70 ?  38  ALA   A HB1  1 
ATOM   875  H HB1  B ALA   A 1 38  ? 21.611 -0.933  -0.378  0.60 11.72 ?  38  ALA   A HB1  1 
ATOM   876  H HB2  A ALA   A 1 38  ? 21.046 -1.049  1.045   0.40 10.70 ?  38  ALA   A HB2  1 
ATOM   877  H HB2  B ALA   A 1 38  ? 21.231 -1.486  1.062   0.60 11.72 ?  38  ALA   A HB2  1 
ATOM   878  H HB3  A ALA   A 1 38  ? 21.322 0.501   0.831   0.40 10.70 ?  38  ALA   A HB3  1 
ATOM   879  H HB3  B ALA   A 1 38  ? 21.333 0.081   0.813   0.60 11.72 ?  38  ALA   A HB3  1 
ATOM   880  N N    A ALA   A 1 39  ? 25.230 -0.003  0.049   0.40 7.95  ?  39  ALA   A N    1 
ATOM   881  N N    B ALA   A 1 39  ? 25.264 -0.046  0.033   0.60 9.41  ?  39  ALA   A N    1 
ATOM   882  C CA   A ALA   A 1 39  ? 26.290 0.869   -0.441  0.40 7.91  ?  39  ALA   A CA   1 
ATOM   883  C CA   B ALA   A 1 39  ? 26.239 0.912   -0.456  0.60 9.73  ?  39  ALA   A CA   1 
ATOM   884  C C    A ALA   A 1 39  ? 26.422 0.807   -1.962  0.40 8.52  ?  39  ALA   A C    1 
ATOM   885  C C    B ALA   A 1 39  ? 26.384 0.835   -1.973  0.60 9.34  ?  39  ALA   A C    1 
ATOM   886  O O    A ALA   A 1 39  ? 25.933 -0.117  -2.619  0.40 8.75  ?  39  ALA   A O    1 
ATOM   887  O O    B ALA   A 1 39  ? 25.871 -0.071  -2.637  0.60 10.00 ?  39  ALA   A O    1 
ATOM   888  C CB   A ALA   A 1 39  ? 27.623 0.468   0.203   0.40 7.98  ?  39  ALA   A CB   1 
ATOM   889  C CB   B ALA   A 1 39  ? 27.590 0.650   0.213   0.60 10.82 ?  39  ALA   A CB   1 
ATOM   890  H H    A ALA   A 1 39  ? 25.503 -0.797  0.243   0.40 9.53  ?  39  ALA   A H    1 
ATOM   891  H H    B ALA   A 1 39  ? 25.600 -0.821  0.201   0.60 11.28 ?  39  ALA   A H    1 
ATOM   892  H HA   A ALA   A 1 39  ? 26.090 1.782   -0.188  0.40 9.48  ?  39  ALA   A HA   1 
ATOM   893  H HA   B ALA   A 1 39  ? 25.945 1.805   -0.217  0.60 11.67 ?  39  ALA   A HA   1 
ATOM   894  H HB1  A ALA   A 1 39  ? 28.319 1.058   -0.127  0.40 9.57  ?  39  ALA   A HB1  1 
ATOM   895  H HB1  B ALA   A 1 39  ? 28.230 1.296   -0.117  0.60 12.97 ?  39  ALA   A HB1  1 
ATOM   896  H HB2  A ALA   A 1 39  ? 27.546 0.560   1.169   0.40 9.57  ?  39  ALA   A HB2  1 
ATOM   897  H HB2  B ALA   A 1 39  ? 27.487 0.747   1.175   0.60 12.97 ?  39  ALA   A HB2  1 
ATOM   898  H HB3  A ALA   A 1 39  ? 27.824 -0.449  -0.027  0.40 9.57  ?  39  ALA   A HB3  1 
ATOM   899  H HB3  B ALA   A 1 39  ? 27.877 -0.249  0.000   0.60 12.97 ?  39  ALA   A HB3  1 
ATOM   900  N N    . ASN   A 1 40  ? 27.106 1.814   -2.516  1.00 9.26  ?  40  ASN   A N    1 
ATOM   901  C CA   . ASN   A 1 40  ? 27.633 1.767   -3.875  1.00 9.30  ?  40  ASN   A CA   1 
ATOM   902  C C    . ASN   A 1 40  ? 29.158 1.644   -3.815  1.00 9.24  ?  40  ASN   A C    1 
ATOM   903  O O    . ASN   A 1 40  ? 29.769 1.735   -2.745  1.00 9.26  ?  40  ASN   A O    1 
ATOM   904  C CB   . ASN   A 1 40  ? 27.168 2.958   -4.728  1.00 10.18 ?  40  ASN   A CB   1 
ATOM   905  C CG   . ASN   A 1 40  ? 27.536 4.297   -4.135  1.00 10.85 ?  40  ASN   A CG   1 
ATOM   906  O OD1  . ASN   A 1 40  ? 28.706 4.553   -3.815  1.00 11.80 ?  40  ASN   A OD1  1 
ATOM   907  N ND2  . ASN   A 1 40  ? 26.542 5.175   -4.002  1.00 11.68 ?  40  ASN   A ND2  1 
ATOM   908  H H    A ASN   A 1 40  ? 27.285 2.545   -2.106  0.40 11.11 ?  40  ASN   A H    1 
ATOM   909  H H    B ASN   A 1 40  ? 27.325 2.528   -2.094  0.60 11.11 ?  40  ASN   A H    1 
ATOM   910  H HA   . ASN   A 1 40  ? 27.300 0.958   -4.303  1.00 11.15 ?  40  ASN   A HA   1 
ATOM   911  H HB2  . ASN   A 1 40  ? 27.574 2.890   -5.605  1.00 12.20 ?  40  ASN   A HB2  1 
ATOM   912  H HB3  . ASN   A 1 40  ? 26.201 2.920   -4.812  1.00 12.20 ?  40  ASN   A HB3  1 
ATOM   913  H HD21 . ASN   A 1 40  ? 26.704 5.956   -3.675  1.00 14.00 ?  40  ASN   A HD21 1 
ATOM   914  H HD22 . ASN   A 1 40  ? 25.746 4.964   -4.238  1.00 14.00 ?  40  ASN   A HD22 1 
ATOM   915  N N    . VAL   A 1 41  ? 29.774 1.392   -4.973  1.00 9.62  ?  41  VAL   A N    1 
ATOM   916  C CA   . VAL   A 1 41  ? 31.201 1.073   -4.996  1.00 10.40 ?  41  VAL   A CA   1 
ATOM   917  C C    . VAL   A 1 41  ? 32.067 2.221   -4.521  1.00 10.26 ?  41  VAL   A C    1 
ATOM   918  O O    . VAL   A 1 41  ? 33.210 1.993   -4.103  1.00 10.49 ?  41  VAL   A O    1 
ATOM   919  C CB   . VAL   A 1 41  ? 31.691 0.592   -6.381  1.00 11.09 ?  41  VAL   A CB   1 
ATOM   920  C CG1  . VAL   A 1 41  ? 31.002 -0.705  -6.778  1.00 11.63 ?  41  VAL   A CG1  1 
ATOM   921  C CG2  . VAL   A 1 41  ? 31.533 1.667   -7.450  1.00 12.07 ?  41  VAL   A CG2  1 
ATOM   922  H H    . VAL   A 1 41  ? 29.391 1.390   -5.740  1.00 11.53 ?  41  VAL   A H    1 
ATOM   923  H HA   . VAL   A 1 41  ? 31.353 0.340   -4.376  1.00 12.47 ?  41  VAL   A HA   1 
ATOM   924  H HB   . VAL   A 1 41  ? 32.637 0.388   -6.310  1.00 13.31 ?  41  VAL   A HB   1 
ATOM   925  H HG11 . VAL   A 1 41  ? 31.343 -0.998  -7.636  1.00 13.95 ?  41  VAL   A HG11 1 
ATOM   926  H HG12 . VAL   A 1 41  ? 31.184 -1.383  -6.103  1.00 13.95 ?  41  VAL   A HG12 1 
ATOM   927  H HG13 . VAL   A 1 41  ? 30.046 -0.551  -6.836  1.00 13.95 ?  41  VAL   A HG13 1 
ATOM   928  H HG21 . VAL   A 1 41  ? 31.758 1.283   -8.315  1.00 14.47 ?  41  VAL   A HG21 1 
ATOM   929  H HG22 . VAL   A 1 41  ? 30.621 1.979   -7.451  1.00 14.47 ?  41  VAL   A HG22 1 
ATOM   930  H HG23 . VAL   A 1 41  ? 32.140 2.396   -7.249  1.00 14.47 ?  41  VAL   A HG23 1 
ATOM   931  N N    A TYR   A 1 42  ? 31.563 3.456   -4.602  0.40 10.22 ?  42  TYR   A N    1 
ATOM   932  N N    B TYR   A 1 42  ? 31.570 3.460   -4.599  0.60 10.26 ?  42  TYR   A N    1 
ATOM   933  C CA   A TYR   A 1 42  ? 32.293 4.646   -4.188  0.40 10.18 ?  42  TYR   A CA   1 
ATOM   934  C CA   B TYR   A 1 42  ? 32.321 4.634   -4.170  0.60 10.24 ?  42  TYR   A CA   1 
ATOM   935  C C    A TYR   A 1 42  ? 32.058 5.003   -2.727  0.40 10.25 ?  42  TYR   A C    1 
ATOM   936  C C    B TYR   A 1 42  ? 32.047 5.017   -2.726  0.60 10.33 ?  42  TYR   A C    1 
ATOM   937  O O    A TYR   A 1 42  ? 32.652 5.969   -2.232  0.40 10.66 ?  42  TYR   A O    1 
ATOM   938  O O    B TYR   A 1 42  ? 32.596 6.020   -2.244  0.60 10.76 ?  42  TYR   A O    1 
ATOM   939  C CB   A TYR   A 1 42  ? 31.901 5.836   -5.078  0.40 10.78 ?  42  TYR   A CB   1 
ATOM   940  C CB   B TYR   A 1 42  ? 32.032 5.824   -5.101  0.60 10.94 ?  42  TYR   A CB   1 
ATOM   941  C CG   A TYR   A 1 42  ? 32.032 5.555   -6.562  0.40 11.50 ?  42  TYR   A CG   1 
ATOM   942  C CG   B TYR   A 1 42  ? 32.275 5.495   -6.554  0.60 11.73 ?  42  TYR   A CG   1 
ATOM   943  C CD1  A TYR   A 1 42  ? 33.275 5.339   -7.138  0.40 11.36 ?  42  TYR   A CD1  1 
ATOM   944  C CD1  B TYR   A 1 42  ? 33.559 5.298   -7.035  0.60 11.96 ?  42  TYR   A CD1  1 
ATOM   945  C CD2  A TYR   A 1 42  ? 30.911 5.494   -7.383  0.40 12.55 ?  42  TYR   A CD2  1 
ATOM   946  C CD2  B TYR   A 1 42  ? 31.216 5.336   -7.435  0.60 12.46 ?  42  TYR   A CD2  1 
ATOM   947  C CE1  A TYR   A 1 42  ? 33.403 5.071   -8.490  0.40 11.64 ?  42  TYR   A CE1  1 
ATOM   948  C CE1  B TYR   A 1 42  ? 33.783 4.964   -8.363  0.60 11.98 ?  42  TYR   A CE1  1 
ATOM   949  C CE2  A TYR   A 1 42  ? 31.030 5.233   -8.740  0.40 13.06 ?  42  TYR   A CE2  1 
ATOM   950  C CE2  B TYR   A 1 42  ? 31.430 5.013   -8.761  0.60 12.78 ?  42  TYR   A CE2  1 
ATOM   951  C CZ   A TYR   A 1 42  ? 32.281 5.020   -9.286  0.40 12.73 ?  42  TYR   A CZ   1 
ATOM   952  C CZ   B TYR   A 1 42  ? 32.715 4.830   -9.221  0.60 12.15 ?  42  TYR   A CZ   1 
ATOM   953  O OH   A TYR   A 1 42  ? 32.417 4.759   -10.631 0.40 13.56 ?  42  TYR   A OH   1 
ATOM   954  O OH   B TYR   A 1 42  ? 32.919 4.498   -10.540 0.60 13.42 ?  42  TYR   A OH   1 
ATOM   955  H H    A TYR   A 1 42  ? 30.778 3.628   -4.909  0.40 12.26 ?  42  TYR   A H    1 
ATOM   956  H H    B TYR   A 1 42  ? 30.790 3.645   -4.912  0.60 12.31 ?  42  TYR   A H    1 
ATOM   957  H HA   A TYR   A 1 42  ? 33.241 4.489   -4.313  0.40 12.21 ?  42  TYR   A HA   1 
ATOM   958  H HA   B TYR   A 1 42  ? 33.267 4.440   -4.244  0.60 12.28 ?  42  TYR   A HA   1 
ATOM   959  H HB2  A TYR   A 1 42  ? 30.977 6.072   -4.899  0.40 12.93 ?  42  TYR   A HB2  1 
ATOM   960  H HB2  B TYR   A 1 42  ? 31.103 6.087   -5.003  0.60 13.12 ?  42  TYR   A HB2  1 
ATOM   961  H HB3  A TYR   A 1 42  ? 32.478 6.589   -4.867  0.40 12.93 ?  42  TYR   A HB3  1 
ATOM   962  H HB3  B TYR   A 1 42  ? 32.612 6.564   -4.859  0.60 13.12 ?  42  TYR   A HB3  1 
ATOM   963  H HD1  A TYR   A 1 42  ? 34.037 5.370   -6.607  0.40 13.62 ?  42  TYR   A HD1  1 
ATOM   964  H HD1  B TYR   A 1 42  ? 34.285 5.390   -6.456  0.60 14.35 ?  42  TYR   A HD1  1 
ATOM   965  H HD2  A TYR   A 1 42  ? 30.067 5.637   -7.018  0.40 15.05 ?  42  TYR   A HD2  1 
ATOM   966  H HD2  B TYR   A 1 42  ? 30.346 5.463   -7.130  0.60 14.94 ?  42  TYR   A HD2  1 
ATOM   967  H HE1  A TYR   A 1 42  ? 34.245 4.929   -8.861  0.40 13.96 ?  42  TYR   A HE1  1 
ATOM   968  H HE1  B TYR   A 1 42  ? 34.654 4.848   -8.675  0.60 14.37 ?  42  TYR   A HE1  1 
ATOM   969  H HE2  A TYR   A 1 42  ? 30.271 5.196   -9.279  0.40 15.66 ?  42  TYR   A HE2  1 
ATOM   970  H HE2  B TYR   A 1 42  ? 30.708 4.922   -9.342  0.60 15.33 ?  42  TYR   A HE2  1 
ATOM   971  H HH   A TYR   A 1 42  ? 31.667 4.754   -11.005 0.40 16.26 ?  42  TYR   A HH   1 
ATOM   972  H HH   B TYR   A 1 42  ? 33.737 4.362   -10.678 0.60 16.10 ?  42  TYR   A HH   1 
ATOM   973  N N    . LEU   A 1 43  ? 31.197 4.255   -2.038  1.00 10.03 ?  43  LEU   A N    1 
ATOM   974  C CA   . LEU   A 1 43  ? 30.762 4.591   -0.687  1.00 9.47  ?  43  LEU   A CA   1 
ATOM   975  C C    . LEU   A 1 43  ? 30.289 6.040   -0.594  1.00 9.59  ?  43  LEU   A C    1 
ATOM   976  O O    . LEU   A 1 43  ? 30.553 6.738   0.388   1.00 10.33 ?  43  LEU   A O    1 
ATOM   977  C CB   . LEU   A 1 43  ? 31.815 4.280   0.376   1.00 9.77  ?  43  LEU   A CB   1 
ATOM   978  C CG   . LEU   A 1 43  ? 32.301 2.830   0.470   1.00 10.01 ?  43  LEU   A CG   1 
ATOM   979  C CD1  . LEU   A 1 43  ? 33.350 2.706   1.570   1.00 11.27 ?  43  LEU   A CD1  1 
ATOM   980  C CD2  . LEU   A 1 43  ? 31.159 1.856   0.717   1.00 10.53 ?  43  LEU   A CD2  1 
ATOM   981  H H    A LEU   A 1 43  ? 30.839 3.528   -2.340  0.40 12.03 ?  43  LEU   A H    1 
ATOM   982  H H    B LEU   A 1 43  ? 30.860 3.515   -2.333  0.60 12.03 ?  43  LEU   A H    1 
ATOM   983  H HA   . LEU   A 1 43  ? 29.992 4.038   -0.484  1.00 11.35 ?  43  LEU   A HA   1 
ATOM   984  H HB2  . LEU   A 1 43  ? 32.591 4.833   0.212   1.00 11.72 ?  43  LEU   A HB2  1 
ATOM   985  H HB3  . LEU   A 1 43  ? 31.439 4.505   1.245   1.00 11.72 ?  43  LEU   A HB3  1 
ATOM   986  H HG   . LEU   A 1 43  ? 32.727 2.590   -0.366  1.00 12.01 ?  43  LEU   A HG   1 
ATOM   987  H HD11 . LEU   A 1 43  ? 33.654 1.786   1.617   1.00 13.52 ?  43  LEU   A HD11 1 
ATOM   988  H HD12 . LEU   A 1 43  ? 34.099 3.290   1.364   1.00 13.52 ?  43  LEU   A HD12 1 
ATOM   989  H HD13 . LEU   A 1 43  ? 32.954 2.967   2.418   1.00 13.52 ?  43  LEU   A HD13 1 
ATOM   990  H HD21 . LEU   A 1 43  ? 31.533 0.972   0.858   1.00 12.63 ?  43  LEU   A HD21 1 
ATOM   991  H HD22 . LEU   A 1 43  ? 30.673 2.142   1.504   1.00 12.63 ?  43  LEU   A HD22 1 
ATOM   992  H HD23 . LEU   A 1 43  ? 30.581 1.856   -0.056  1.00 12.63 ?  43  LEU   A HD23 1 
ATOM   993  N N    . LYS   A 1 44  ? 29.556 6.482   -1.620  1.00 9.59  ?  44  LYS   A N    1 
ATOM   994  C CA   . LYS   A 1 44  ? 28.917 7.797   -1.619  1.00 10.15 ?  44  LYS   A CA   1 
ATOM   995  C C    . LYS   A 1 44  ? 27.491 7.606   -1.120  1.00 9.55  ?  44  LYS   A C    1 
ATOM   996  O O    . LYS   A 1 44  ? 26.627 7.086   -1.832  1.00 10.19 ?  44  LYS   A O    1 
ATOM   997  C CB   . LYS   A 1 44  ? 28.960 8.425   -3.006  1.00 12.08 ?  44  LYS   A CB   1 
ATOM   998  C CG   . LYS   A 1 44  ? 30.339 8.897   -3.413  1.00 15.15 ?  44  LYS   A CG   1 
ATOM   999  C CD   . LYS   A 1 44  ? 30.976 9.813   -2.365  1.00 20.61 ?  44  LYS   A CD   1 
ATOM   1000 C CE   . LYS   A 1 44  ? 32.325 10.328  -2.823  1.00 24.20 ?  44  LYS   A CE   1 
ATOM   1001 N NZ   . LYS   A 1 44  ? 33.096 10.957  -1.716  1.00 25.14 ?  44  LYS   A NZ   1 
ATOM   1002 H H    . LYS   A 1 44  ? 29.415 6.031   -2.338  1.00 11.50 ?  44  LYS   A H    1 
ATOM   1003 H HA   . LYS   A 1 44  ? 29.362 8.375   -0.982  1.00 12.17 ?  44  LYS   A HA   1 
ATOM   1004 H HB2  . LYS   A 1 44  ? 28.665 7.769   -3.656  1.00 14.48 ?  44  LYS   A HB2  1 
ATOM   1005 H HB3  . LYS   A 1 44  ? 28.366 9.193   -3.021  1.00 14.48 ?  44  LYS   A HB3  1 
ATOM   1006 H HG2  . LYS   A 1 44  ? 30.915 8.128   -3.536  1.00 18.17 ?  44  LYS   A HG2  1 
ATOM   1007 H HG3  . LYS   A 1 44  ? 30.269 9.398   -4.244  1.00 18.17 ?  44  LYS   A HG3  1 
ATOM   1008 H HD2  . LYS   A 1 44  ? 30.382 10.562  -2.199  1.00 24.73 ?  44  LYS   A HD2  1 
ATOM   1009 H HD3  . LYS   A 1 44  ? 31.115 9.307   -1.547  1.00 24.73 ?  44  LYS   A HD3  1 
ATOM   1010 H HE2  . LYS   A 1 44  ? 32.844 9.585   -3.167  1.00 29.04 ?  44  LYS   A HE2  1 
ATOM   1011 H HE3  . LYS   A 1 44  ? 32.187 10.990  -3.514  1.00 29.04 ?  44  LYS   A HE3  1 
ATOM   1012 H HZ1  . LYS   A 1 44  ? 33.878 11.250  -2.021  1.00 30.16 ?  44  LYS   A HZ1  1 
ATOM   1013 H HZ2  . LYS   A 1 44  ? 32.639 11.648  -1.383  1.00 30.16 ?  44  LYS   A HZ2  1 
ATOM   1014 H HZ3  . LYS   A 1 44  ? 33.238 10.367  -1.067  1.00 30.16 ?  44  LYS   A HZ3  1 
ATOM   1015 N N    . HIS   A 1 45  ? 27.250 7.997   0.128   1.00 9.31  ?  45  HIS   A N    1 
ATOM   1016 C CA   . HIS   A 1 45  ? 26.011 7.650   0.823   1.00 9.75  ?  45  HIS   A CA   1 
ATOM   1017 C C    . HIS   A 1 45  ? 24.996 8.780   0.656   1.00 10.56 ?  45  HIS   A C    1 
ATOM   1018 O O    . HIS   A 1 45  ? 24.694 9.536   1.581   1.00 12.00 ?  45  HIS   A O    1 
ATOM   1019 C CB   . HIS   A 1 45  ? 26.304 7.396   2.291   1.00 9.63  ?  45  HIS   A CB   1 
ATOM   1020 C CG   . HIS   A 1 45  ? 27.410 6.424   2.523   1.00 8.96  ?  45  HIS   A CG   1 
ATOM   1021 N ND1  . HIS   A 1 45  ? 27.403 5.144   2.012   1.00 9.40  ?  45  HIS   A ND1  1 
ATOM   1022 C CD2  . HIS   A 1 45  ? 28.575 6.571   3.197   1.00 9.49  ?  45  HIS   A CD2  1 
ATOM   1023 C CE1  . HIS   A 1 45  ? 28.522 4.542   2.380   1.00 9.21  ?  45  HIS   A CE1  1 
ATOM   1024 N NE2  . HIS   A 1 45  ? 29.249 5.384   3.100   1.00 9.31  ?  45  HIS   A NE2  1 
ATOM   1025 H H    . HIS   A 1 45  ? 27.789 8.475   0.599   1.00 11.16 ?  45  HIS   A H    1 
ATOM   1026 H HA   . HIS   A 1 45  ? 25.637 6.841   0.435   1.00 11.69 ?  45  HIS   A HA   1 
ATOM   1027 H HB2  . HIS   A 1 45  ? 26.547 8.236   2.708   1.00 11.55 ?  45  HIS   A HB2  1 
ATOM   1028 H HB3  . HIS   A 1 45  ? 25.501 7.042   2.710   1.00 11.55 ?  45  HIS   A HB3  1 
ATOM   1029 H HD2  . HIS   A 1 45  ? 28.864 7.339   3.640   1.00 11.38 ?  45  HIS   A HD2  1 
ATOM   1030 H HE1  . HIS   A 1 45  ? 28.752 3.662   2.184   1.00 11.04 ?  45  HIS   A HE1  1 
ATOM   1031 H HE2  . HIS   A 1 45  ? 30.016 5.213   3.448   1.00 11.17 ?  45  HIS   A HE2  1 
ATOM   1032 N N    A GLY   A 1 46  ? 24.418 8.851   -0.541  0.40 11.43 ?  46  GLY   A N    1 
ATOM   1033 N N    B GLY   A 1 46  ? 24.472 8.890   -0.563  0.60 11.84 ?  46  GLY   A N    1 
ATOM   1034 C CA   A GLY   A 1 46  ? 23.563 9.968   -0.893  0.40 11.93 ?  46  GLY   A CA   1 
ATOM   1035 C CA   B GLY   A 1 46  ? 23.692 10.056  -0.933  0.60 12.56 ?  46  GLY   A CA   1 
ATOM   1036 C C    A GLY   A 1 46  ? 22.091 9.794   -0.578  0.40 11.70 ?  46  GLY   A C    1 
ATOM   1037 C C    B GLY   A 1 46  ? 22.207 9.955   -0.655  0.60 12.14 ?  46  GLY   A C    1 
ATOM   1038 O O    A GLY   A 1 46  ? 21.439 10.731  -0.103  0.40 12.32 ?  46  GLY   A O    1 
ATOM   1039 O O    B GLY   A 1 46  ? 21.547 10.966  -0.393  0.60 12.76 ?  46  GLY   A O    1 
ATOM   1040 H H    A GLY   A 1 46  ? 24.500 8.263   -1.163  0.40 13.71 ?  46  GLY   A H    1 
ATOM   1041 H H    B GLY   A 1 46  ? 24.543 8.304   -1.185  0.60 14.21 ?  46  GLY   A H    1 
ATOM   1042 H HA2  A GLY   A 1 46  ? 23.863 10.756  -0.418  0.40 14.31 ?  46  GLY   A HA2  1 
ATOM   1043 H HA2  B GLY   A 1 46  ? 24.037 10.829  -0.456  0.60 15.07 ?  46  GLY   A HA2  1 
ATOM   1044 H HA3  A GLY   A 1 46  ? 23.648 10.141  -1.843  0.40 14.31 ?  46  GLY   A HA3  1 
ATOM   1045 H HA3  B GLY   A 1 46  ? 23.797 10.218  -1.882  0.60 15.07 ?  46  GLY   A HA3  1 
ATOM   1046 N N    A GLY   A 1 47  ? 21.549 8.608   -0.844  0.40 11.44 ?  47  GLY   A N    1 
ATOM   1047 N N    B GLY   A 1 47  ? 21.664 8.746   -0.734  0.60 11.77 ?  47  GLY   A N    1 
ATOM   1048 C CA   A GLY   A 1 47  ? 20.118 8.412   -0.756  0.40 11.28 ?  47  GLY   A CA   1 
ATOM   1049 C CA   B GLY   A 1 47  ? 20.230 8.567   -0.624  0.60 12.25 ?  47  GLY   A CA   1 
ATOM   1050 C C    A GLY   A 1 47  ? 19.769 7.012   -0.308  0.40 10.62 ?  47  GLY   A C    1 
ATOM   1051 C C    B GLY   A 1 47  ? 19.899 7.138   -0.252  0.60 11.91 ?  47  GLY   A C    1 
ATOM   1052 O O    A GLY   A 1 47  ? 20.642 6.186   -0.036  0.40 10.01 ?  47  GLY   A O    1 
ATOM   1053 O O    B GLY   A 1 47  ? 20.782 6.303   -0.045  0.60 11.62 ?  47  GLY   A O    1 
ATOM   1054 H H    A GLY   A 1 47  ? 21.991 7.903   -1.066  0.40 13.72 ?  47  GLY   A H    1 
ATOM   1055 H H    B GLY   A 1 47  ? 22.104 8.025   -0.850  0.60 14.11 ?  47  GLY   A H    1 
ATOM   1056 H HA2  A GLY   A 1 47  ? 19.738 9.030   -0.116  0.40 13.53 ?  47  GLY   A HA2  1 
ATOM   1057 H HA2  B GLY   A 1 47  ? 19.868 9.165   0.052   0.60 14.70 ?  47  GLY   A HA2  1 
ATOM   1058 H HA3  A GLY   A 1 47  ? 19.711 8.569   -1.622  0.40 13.53 ?  47  GLY   A HA3  1 
ATOM   1059 H HA3  B GLY   A 1 47  ? 19.809 8.771   -1.476  0.60 14.70 ?  47  GLY   A HA3  1 
ATOM   1060 N N    A GLY   A 1 48  ? 18.467 6.751   -0.234  0.40 10.71 ?  48  GLY   A N    1 
ATOM   1061 N N    B GLY   A 1 48  ? 18.603 6.857   -0.173  0.60 12.42 ?  48  GLY   A N    1 
ATOM   1062 C CA   A GLY   A 1 48  ? 18.010 5.450   0.211   0.40 10.48 ?  48  GLY   A CA   1 
ATOM   1063 C CA   B GLY   A 1 48  ? 18.173 5.522   0.190   0.60 11.88 ?  48  GLY   A CA   1 
ATOM   1064 C C    A GLY   A 1 48  ? 18.503 5.141   1.607   0.40 9.80  ?  48  GLY   A C    1 
ATOM   1065 C C    B GLY   A 1 48  ? 18.621 5.140   1.588   0.60 10.89 ?  48  GLY   A C    1 
ATOM   1066 O O    A GLY   A 1 48  ? 18.615 6.020   2.470   0.40 10.06 ?  48  GLY   A O    1 
ATOM   1067 O O    B GLY   A 1 48  ? 18.784 5.983   2.480   0.60 11.70 ?  48  GLY   A O    1 
ATOM   1068 H H    A GLY   A 1 48  ? 17.838 7.304   -0.425  0.40 12.85 ?  48  GLY   A H    1 
ATOM   1069 H H    B GLY   A 1 48  ? 17.970 7.414   -0.324  0.60 14.90 ?  48  GLY   A H    1 
ATOM   1070 H HA2  A GLY   A 1 48  ? 17.040 5.426   0.210   0.40 12.57 ?  48  GLY   A HA2  1 
ATOM   1071 H HA2  B GLY   A 1 48  ? 17.207 5.470   0.141   0.60 14.25 ?  48  GLY   A HA2  1 
ATOM   1072 H HA3  A GLY   A 1 48  ? 18.338 4.765   -0.393  0.40 12.57 ?  48  GLY   A HA3  1 
ATOM   1073 H HA3  B GLY   A 1 48  ? 18.550 4.878   -0.430  0.60 14.25 ?  48  GLY   A HA3  1 
ATOM   1074 N N    A VAL   A 1 49  ? 18.805 3.863   1.833   0.40 9.49  ?  49  VAL   A N    1 
ATOM   1075 N N    B VAL   A 1 49  ? 18.829 3.835   1.779   0.60 10.24 ?  49  VAL   A N    1 
ATOM   1076 C CA   A VAL   A 1 49  ? 19.274 3.425   3.143   0.40 9.72  ?  49  VAL   A CA   1 
ATOM   1077 C CA   B VAL   A 1 49  ? 19.348 3.329   3.048   0.60 9.95  ?  49  VAL   A CA   1 
ATOM   1078 C C    A VAL   A 1 49  ? 20.618 4.062   3.480   0.40 8.79  ?  49  VAL   A C    1 
ATOM   1079 C C    B VAL   A 1 49  ? 20.638 4.051   3.418   0.60 9.19  ?  49  VAL   A C    1 
ATOM   1080 O O    A VAL   A 1 49  ? 20.867 4.444   4.629   0.40 8.78  ?  49  VAL   A O    1 
ATOM   1081 O O    B VAL   A 1 49  ? 20.822 4.484   4.560   0.60 9.99  ?  49  VAL   A O    1 
ATOM   1082 C CB   A VAL   A 1 49  ? 19.334 1.887   3.184   0.40 10.53 ?  49  VAL   A CB   1 
ATOM   1083 C CB   B VAL   A 1 49  ? 19.565 1.805   2.964   0.60 9.57  ?  49  VAL   A CB   1 
ATOM   1084 C CG1  A VAL   A 1 49  ? 20.058 1.418   4.430   0.40 11.21 ?  49  VAL   A CG1  1 
ATOM   1085 C CG1  B VAL   A 1 49  ? 20.353 1.311   4.180   0.60 9.26  ?  49  VAL   A CG1  1 
ATOM   1086 C CG2  A VAL   A 1 49  ? 17.925 1.311   3.122   0.40 11.01 ?  49  VAL   A CG2  1 
ATOM   1087 C CG2  B VAL   A 1 49  ? 18.234 1.074   2.824   0.60 10.36 ?  49  VAL   A CG2  1 
ATOM   1088 H H    A VAL   A 1 49  ? 18.742 3.238   1.246   0.40 11.38 ?  49  VAL   A H    1 
ATOM   1089 H H    B VAL   A 1 49  ? 18.694 3.228   1.190   0.60 12.29 ?  49  VAL   A H    1 
ATOM   1090 H HA   A VAL   A 1 49  ? 18.633 3.714   3.809   0.40 11.66 ?  49  VAL   A HA   1 
ATOM   1091 H HA   B VAL   A 1 49  ? 18.702 3.501   3.749   0.60 11.93 ?  49  VAL   A HA   1 
ATOM   1092 H HB   A VAL   A 1 49  ? 19.826 1.571   2.409   0.40 12.63 ?  49  VAL   A HB   1 
ATOM   1093 H HB   B VAL   A 1 49  ? 20.092 1.610   2.176   0.60 11.48 ?  49  VAL   A HB   1 
ATOM   1094 H HG11 A VAL   A 1 49  ? 19.855 0.482   4.571   0.40 13.44 ?  49  VAL   A HG11 1 
ATOM   1095 H HG11 B VAL   A 1 49  ? 20.225 0.354   4.269   0.60 11.10 ?  49  VAL   A HG11 1 
ATOM   1096 H HG12 A VAL   A 1 49  ? 21.011 1.537   4.307   0.40 13.44 ?  49  VAL   A HG12 1 
ATOM   1097 H HG12 B VAL   A 1 49  ? 21.292 1.510   4.055   0.60 11.10 ?  49  VAL   A HG12 1 
ATOM   1098 H HG13 A VAL   A 1 49  ? 19.749 1.942   5.186   0.40 13.44 ?  49  VAL   A HG13 1 
ATOM   1099 H HG13 B VAL   A 1 49  ? 20.019 1.760   4.976   0.60 11.10 ?  49  VAL   A HG13 1 
ATOM   1100 H HG21 A VAL   A 1 49  ? 17.980 0.345   3.156   0.40 13.21 ?  49  VAL   A HG21 1 
ATOM   1101 H HG21 B VAL   A 1 49  ? 18.401 0.120   2.777   0.60 12.43 ?  49  VAL   A HG21 1 
ATOM   1102 H HG22 A VAL   A 1 49  ? 17.417 1.644   3.877   0.40 13.21 ?  49  VAL   A HG22 1 
ATOM   1103 H HG22 B VAL   A 1 49  ? 17.678 1.276   3.593   0.60 12.43 ?  49  VAL   A HG22 1 
ATOM   1104 H HG23 A VAL   A 1 49  ? 17.506 1.591   2.292   0.40 13.21 ?  49  VAL   A HG23 1 
ATOM   1105 H HG23 B VAL   A 1 49  ? 17.795 1.373   2.011   0.60 12.43 ?  49  VAL   A HG23 1 
ATOM   1106 N N    A ALA   A 1 50  ? 21.516 4.156   2.497   0.40 8.60  ?  50  ALA   A N    1 
ATOM   1107 N N    B ALA   A 1 50  ? 21.562 4.160   2.461   0.60 8.90  ?  50  ALA   A N    1 
ATOM   1108 C CA   A ALA   A 1 50  ? 22.844 4.709   2.756   0.40 8.66  ?  50  ALA   A CA   1 
ATOM   1109 C CA   B ALA   A 1 50  ? 22.879 4.722   2.756   0.60 8.77  ?  50  ALA   A CA   1 
ATOM   1110 C C    A ALA   A 1 50  ? 22.758 6.162   3.202   0.40 8.70  ?  50  ALA   A C    1 
ATOM   1111 C C    B ALA   A 1 50  ? 22.773 6.174   3.199   0.60 8.58  ?  50  ALA   A C    1 
ATOM   1112 O O    A ALA   A 1 50  ? 23.386 6.561   4.190   0.40 9.08  ?  50  ALA   A O    1 
ATOM   1113 O O    B ALA   A 1 50  ? 23.414 6.588   4.173   0.60 9.17  ?  50  ALA   A O    1 
ATOM   1114 C CB   A ALA   A 1 50  ? 23.712 4.577   1.504   0.40 8.57  ?  50  ALA   A CB   1 
ATOM   1115 C CB   B ALA   A 1 50  ? 23.776 4.605   1.526   0.60 8.66  ?  50  ALA   A CB   1 
ATOM   1116 H H    A ALA   A 1 50  ? 21.387 3.901   1.686   0.40 10.31 ?  50  ALA   A H    1 
ATOM   1117 H H    B ALA   A 1 50  ? 21.455 3.913   1.644   0.60 10.67 ?  50  ALA   A H    1 
ATOM   1118 H HA   A ALA   A 1 50  ? 23.264 4.212   3.469   0.40 10.39 ?  50  ALA   A HA   1 
ATOM   1119 H HA   B ALA   A 1 50  ? 23.287 4.223   3.477   0.60 10.51 ?  50  ALA   A HA   1 
ATOM   1120 H HB1  A ALA   A 1 50  ? 24.589 4.950   1.688   0.40 10.27 ?  50  ALA   A HB1  1 
ATOM   1121 H HB1  B ALA   A 1 50  ? 24.644 4.987   1.733   0.60 10.39 ?  50  ALA   A HB1  1 
ATOM   1122 H HB2  A ALA   A 1 50  ? 23.792 3.639   1.274   0.40 10.27 ?  50  ALA   A HB2  1 
ATOM   1123 H HB2  B ALA   A 1 50  ? 23.872 3.670   1.293   0.60 10.39 ?  50  ALA   A HB2  1 
ATOM   1124 H HB3  A ALA   A 1 50  ? 23.293 5.063   0.776   0.40 10.27 ?  50  ALA   A HB3  1 
ATOM   1125 H HB3  B ALA   A 1 50  ? 23.369 5.091   0.791   0.60 10.39 ?  50  ALA   A HB3  1 
ATOM   1126 N N    . GLY   A 1 51  ? 21.989 6.973   2.475   1.00 9.07  ?  51  GLY   A N    1 
ATOM   1127 C CA   . GLY   A 1 51  ? 21.823 8.359   2.863   1.00 9.91  ?  51  GLY   A CA   1 
ATOM   1128 C C    . GLY   A 1 51  ? 21.218 8.492   4.244   1.00 9.74  ?  51  GLY   A C    1 
ATOM   1129 O O    . GLY   A 1 51  ? 21.602 9.374   5.016   1.00 10.06 ?  51  GLY   A O    1 
ATOM   1130 H H    A GLY   A 1 51  ? 21.562 6.745   1.762   0.40 10.88 ?  51  GLY   A H    1 
ATOM   1131 H H    B GLY   A 1 51  ? 21.561 6.741   1.764   0.60 10.88 ?  51  GLY   A H    1 
ATOM   1132 H HA2  . GLY   A 1 51  ? 22.686 8.804   2.861   1.00 11.88 ?  51  GLY   A HA2  1 
ATOM   1133 H HA3  . GLY   A 1 51  ? 21.245 8.809   2.226   1.00 11.88 ?  51  GLY   A HA3  1 
ATOM   1134 N N    A ALA   A 1 52  ? 20.233 7.649   4.558   0.40 9.64  ?  52  ALA   A N    1 
ATOM   1135 N N    B ALA   A 1 52  ? 20.273 7.607   4.580   0.60 9.81  ?  52  ALA   A N    1 
ATOM   1136 C CA   A ALA   A 1 52  ? 19.581 7.728   5.861   0.40 10.16 ?  52  ALA   A CA   1 
ATOM   1137 C CA   B ALA   A 1 52  ? 19.627 7.652   5.889   0.60 10.69 ?  52  ALA   A CA   1 
ATOM   1138 C C    A ALA   A 1 52  ? 20.527 7.318   6.985   0.40 9.62  ?  52  ALA   A C    1 
ATOM   1139 C C    B ALA   A 1 52  ? 20.587 7.240   7.006   0.60 10.03 ?  52  ALA   A C    1 
ATOM   1140 O O    A ALA   A 1 52  ? 20.580 7.975   8.032   0.40 10.20 ?  52  ALA   A O    1 
ATOM   1141 O O    B ALA   A 1 52  ? 20.669 7.909   8.042   0.60 10.81 ?  52  ALA   A O    1 
ATOM   1142 C CB   A ALA   A 1 52  ? 18.320 6.865   5.864   0.40 10.94 ?  52  ALA   A CB   1 
ATOM   1143 C CB   B ALA   A 1 52  ? 18.369 6.780   5.882   0.60 12.00 ?  52  ALA   A CB   1 
ATOM   1144 H H    A ALA   A 1 52  ? 19.932 7.029   4.039   0.40 11.56 ?  52  ALA   A H    1 
ATOM   1145 H H    B ALA   A 1 52  ? 20.001 6.966   4.070   0.60 11.77 ?  52  ALA   A H    1 
ATOM   1146 H HA   A ALA   A 1 52  ? 19.310 8.644   6.012   0.40 12.19 ?  52  ALA   A HA   1 
ATOM   1147 H HA   B ALA   A 1 52  ? 19.350 8.557   6.066   0.60 12.83 ?  52  ALA   A HA   1 
ATOM   1148 H HB1  A ALA   A 1 52  ? 17.886 6.946   6.729   0.40 13.12 ?  52  ALA   A HB1  1 
ATOM   1149 H HB1  B ALA   A 1 52  ? 17.948 6.821   6.758   0.60 14.40 ?  52  ALA   A HB1  1 
ATOM   1150 H HB2  A ALA   A 1 52  ? 17.721 7.173   5.166   0.40 13.12 ?  52  ALA   A HB2  1 
ATOM   1151 H HB2  B ALA   A 1 52  ? 17.753 7.117   5.209   0.60 14.40 ?  52  ALA   A HB2  1 
ATOM   1152 H HB3  A ALA   A 1 52  ? 18.566 5.940   5.704   0.40 13.12 ?  52  ALA   A HB3  1 
ATOM   1153 H HB3  B ALA   A 1 52  ? 18.611 5.864   5.677   0.60 14.40 ?  52  ALA   A HB3  1 
ATOM   1154 N N    A LEU   A 1 53  ? 21.273 6.228   6.797   0.40 9.15  ?  53  LEU   A N    1 
ATOM   1155 N N    B LEU   A 1 53  ? 21.309 6.130   6.828   0.60 9.66  ?  53  LEU   A N    1 
ATOM   1156 C CA   A LEU   A 1 53  ? 22.228 5.799   7.816   0.40 9.51  ?  53  LEU   A CA   1 
ATOM   1157 C CA   B LEU   A 1 53  ? 22.300 5.738   7.832   0.60 9.58  ?  53  LEU   A CA   1 
ATOM   1158 C C    A LEU   A 1 53  ? 23.311 6.850   8.023   0.40 9.45  ?  53  LEU   A C    1 
ATOM   1159 C C    B LEU   A 1 53  ? 23.329 6.843   8.028   0.60 9.35  ?  53  LEU   A C    1 
ATOM   1160 O O    A LEU   A 1 53  ? 23.661 7.186   9.159   0.40 10.04 ?  53  LEU   A O    1 
ATOM   1161 O O    B LEU   A 1 53  ? 23.652 7.219   9.160   0.60 10.03 ?  53  LEU   A O    1 
ATOM   1162 C CB   A LEU   A 1 53  ? 22.853 4.456   7.422   0.40 9.97  ?  53  LEU   A CB   1 
ATOM   1163 C CB   B LEU   A 1 53  ? 22.999 4.429   7.433   0.60 9.42  ?  53  LEU   A CB   1 
ATOM   1164 C CG   A LEU   A 1 53  ? 21.925 3.240   7.483   0.40 10.11 ?  53  LEU   A CG   1 
ATOM   1165 C CG   B LEU   A 1 53  ? 22.201 3.125   7.530   0.60 9.65  ?  53  LEU   A CG   1 
ATOM   1166 C CD1  A LEU   A 1 53  ? 22.625 2.012   6.925   0.40 9.82  ?  53  LEU   A CD1  1 
ATOM   1167 C CD1  B LEU   A 1 53  ? 22.967 2.006   6.843   0.60 10.03 ?  53  LEU   A CD1  1 
ATOM   1168 C CD2  A LEU   A 1 53  ? 21.455 2.991   8.907   0.40 10.65 ?  53  LEU   A CD2  1 
ATOM   1169 C CD2  B LEU   A 1 53  ? 21.914 2.745   8.973   0.60 9.96  ?  53  LEU   A CD2  1 
ATOM   1170 H H    A LEU   A 1 53  ? 21.240 5.725   6.099   0.40 10.97 ?  53  LEU   A H    1 
ATOM   1171 H H    B LEU   A 1 53  ? 21.252 5.597   6.151   0.60 11.58 ?  53  LEU   A H    1 
ATOM   1172 H HA   A LEU   A 1 53  ? 21.760 5.680   8.657   0.40 11.40 ?  53  LEU   A HA   1 
ATOM   1173 H HA   B LEU   A 1 53  ? 21.850 5.588   8.679   0.60 11.49 ?  53  LEU   A HA   1 
ATOM   1174 H HB2  A LEU   A 1 53  ? 23.178 4.525   6.510   0.40 11.95 ?  53  LEU   A HB2  1 
ATOM   1175 H HB2  B LEU   A 1 53  ? 23.289 4.514   6.512   0.60 11.29 ?  53  LEU   A HB2  1 
ATOM   1176 H HB3  A LEU   A 1 53  ? 23.597 4.278   8.017   0.40 11.95 ?  53  LEU   A HB3  1 
ATOM   1177 H HB3  B LEU   A 1 53  ? 23.779 4.322   8.002   0.60 11.29 ?  53  LEU   A HB3  1 
ATOM   1178 H HG   A LEU   A 1 53  ? 21.143 3.412   6.932   0.40 12.12 ?  53  LEU   A HG   1 
ATOM   1179 H HG   B LEU   A 1 53  ? 21.356 3.233   7.069   0.60 11.57 ?  53  LEU   A HG   1 
ATOM   1180 H HD11 A LEU   A 1 53  ? 22.021 1.256   6.971   0.40 11.77 ?  53  LEU   A HD11 1 
ATOM   1181 H HD11 B LEU   A 1 53  ? 22.457 1.183   6.916   0.60 12.03 ?  53  LEU   A HD11 1 
ATOM   1182 H HD12 A LEU   A 1 53  ? 22.875 2.182   6.003   0.40 11.77 ?  53  LEU   A HD12 1 
ATOM   1183 H HD12 B LEU   A 1 53  ? 23.093 2.235   5.909   0.60 12.03 ?  53  LEU   A HD12 1 
ATOM   1184 H HD13 A LEU   A 1 53  ? 23.419 1.836   7.455   0.40 11.77 ?  53  LEU   A HD13 1 
ATOM   1185 H HD13 B LEU   A 1 53  ? 23.828 1.900   7.277   0.60 12.03 ?  53  LEU   A HD13 1 
ATOM   1186 H HD21 A LEU   A 1 53  ? 20.962 2.159   8.934   0.40 12.77 ?  53  LEU   A HD21 1 
ATOM   1187 H HD21 B LEU   A 1 53  ? 21.397 1.924   8.987   0.60 11.95 ?  53  LEU   A HD21 1 
ATOM   1188 H HD22 A LEU   A 1 53  ? 22.231 2.937   9.486   0.40 12.77 ?  53  LEU   A HD22 1 
ATOM   1189 H HD22 B LEU   A 1 53  ? 22.754 2.616   9.440   0.60 11.95 ?  53  LEU   A HD22 1 
ATOM   1190 H HD23 A LEU   A 1 53  ? 20.885 3.724   9.186   0.40 12.77 ?  53  LEU   A HD23 1 
ATOM   1191 H HD23 B LEU   A 1 53  ? 21.409 3.459   9.392   0.60 11.95 ?  53  LEU   A HD23 1 
ATOM   1192 N N    . ASN   A 1 54  ? 23.857 7.378   6.931   1.00 8.91  ?  54  ASN   A N    1 
ATOM   1193 C CA   . ASN   A 1 54  ? 24.903 8.380   7.060   1.00 9.24  ?  54  ASN   A CA   1 
ATOM   1194 C C    . ASN   A 1 54  ? 24.395 9.624   7.786   1.00 9.81  ?  54  ASN   A C    1 
ATOM   1195 O O    . ASN   A 1 54  ? 25.082 10.173  8.656   1.00 10.13 ?  54  ASN   A O    1 
ATOM   1196 C CB   . ASN   A 1 54  ? 25.465 8.736   5.696   1.00 9.49  ?  54  ASN   A CB   1 
ATOM   1197 C CG   . ASN   A 1 54  ? 26.480 9.839   5.799   1.00 9.55  ?  54  ASN   A CG   1 
ATOM   1198 O OD1  . ASN   A 1 54  ? 27.484 9.695   6.508   1.00 9.54  ?  54  ASN   A OD1  1 
ATOM   1199 N ND2  . ASN   A 1 54  ? 26.221 10.961  5.143   1.00 10.40 ?  54  ASN   A ND2  1 
ATOM   1200 H H    A ASN   A 1 54  ? 23.636 7.177   6.123   0.40 10.69 ?  54  ASN   A H    1 
ATOM   1201 H H    B ASN   A 1 54  ? 23.634 7.174   6.124   0.60 10.69 ?  54  ASN   A H    1 
ATOM   1202 H HA   . ASN   A 1 54  ? 25.620 8.006   7.588   1.00 11.08 ?  54  ASN   A HA   1 
ATOM   1203 H HB2  . ASN   A 1 54  ? 25.905 7.950   5.321   1.00 11.39 ?  54  ASN   A HB2  1 
ATOM   1204 H HB3  . ASN   A 1 54  ? 24.748 9.025   5.116   1.00 11.39 ?  54  ASN   A HB3  1 
ATOM   1205 H HD21 . ASN   A 1 54  ? 26.772 11.617  5.187   1.00 12.47 ?  54  ASN   A HD21 1 
ATOM   1206 H HD22 . ASN   A 1 54  ? 25.503 11.028  4.675   1.00 12.47 ?  54  ASN   A HD22 1 
ATOM   1207 N N    . LYS   A 1 55  ? 23.186 10.080  7.443   1.00 9.81  ?  55  LYS   A N    1 
ATOM   1208 C CA   . LYS   A 1 55  ? 22.603 11.236  8.117   1.00 10.64 ?  55  LYS   A CA   1 
ATOM   1209 C C    . LYS   A 1 55  ? 22.517 10.997  9.617   1.00 10.70 ?  55  LYS   A C    1 
ATOM   1210 O O    . LYS   A 1 55  ? 22.798 11.896  10.420  1.00 11.26 ?  55  LYS   A O    1 
ATOM   1211 C CB   . LYS   A 1 55  ? 21.229 11.535  7.507   1.00 11.94 ?  55  LYS   A CB   1 
ATOM   1212 C CG   . LYS   A 1 55  ? 20.471 12.701  8.124   1.00 13.82 ?  55  LYS   A CG   1 
ATOM   1213 C CD   . LYS   A 1 55  ? 19.157 12.947  7.367   1.00 15.65 ?  55  LYS   A CD   1 
ATOM   1214 C CE   . LYS   A 1 55  ? 18.287 13.999  8.034   1.00 17.68 ?  55  LYS   A CE   1 
ATOM   1215 N NZ   . LYS   A 1 55  ? 16.957 14.111  7.367   1.00 18.69 ?  55  LYS   A NZ   1 
ATOM   1216 H H    . LYS   A 1 55  ? 22.680 9.733   6.835   1.00 11.76 ?  55  LYS   A H    1 
ATOM   1217 H HA   . LYS   A 1 55  ? 23.170 12.006  7.970   1.00 12.77 ?  55  LYS   A HA   1 
ATOM   1218 H HB2  . LYS   A 1 55  ? 21.347 11.739  6.568   1.00 14.32 ?  55  LYS   A HB2  1 
ATOM   1219 H HB3  . LYS   A 1 55  ? 20.670 10.748  7.601   1.00 14.32 ?  55  LYS   A HB3  1 
ATOM   1220 H HG2  . LYS   A 1 55  ? 20.251 12.494  9.049   1.00 16.58 ?  55  LYS   A HG2  1 
ATOM   1221 H HG3  . LYS   A 1 55  ? 21.008 13.504  8.075   1.00 16.58 ?  55  LYS   A HG3  1 
ATOM   1222 H HD2  . LYS   A 1 55  ? 19.364 13.250  6.468   1.00 18.77 ?  55  LYS   A HD2  1 
ATOM   1223 H HD3  . LYS   A 1 55  ? 18.653 12.117  7.327   1.00 18.77 ?  55  LYS   A HD3  1 
ATOM   1224 H HE2  . LYS   A 1 55  ? 18.141 13.752  8.960   1.00 21.21 ?  55  LYS   A HE2  1 
ATOM   1225 H HE3  . LYS   A 1 55  ? 18.728 14.860  7.979   1.00 21.21 ?  55  LYS   A HE3  1 
ATOM   1226 H HZ1  . LYS   A 1 55  ? 16.399 14.582  7.876   1.00 22.43 ?  55  LYS   A HZ1  1 
ATOM   1227 H HZ2  . LYS   A 1 55  ? 17.042 14.520  6.580   1.00 22.43 ?  55  LYS   A HZ2  1 
ATOM   1228 H HZ3  . LYS   A 1 55  ? 16.610 13.301  7.235   1.00 22.43 ?  55  LYS   A HZ3  1 
ATOM   1229 N N    . ALA   A 1 56  ? 22.124 9.785   10.017  1.00 11.01 ?  56  ALA   A N    1 
ATOM   1230 C CA   . ALA   A 1 56  ? 21.997 9.454   11.431  1.00 11.48 ?  56  ALA   A CA   1 
ATOM   1231 C C    . ALA   A 1 56  ? 23.336 9.471   12.159  1.00 11.49 ?  56  ALA   A C    1 
ATOM   1232 O O    . ALA   A 1 56  ? 23.357 9.636   13.380  1.00 12.95 ?  56  ALA   A O    1 
ATOM   1233 C CB   . ALA   A 1 56  ? 21.301 8.100   11.600  1.00 12.34 ?  56  ALA   A CB   1 
ATOM   1234 H H    . ALA   A 1 56  ? 21.922 9.142   9.486   1.00 13.20 ?  56  ALA   A H    1 
ATOM   1235 H HA   . ALA   A 1 56  ? 21.436 10.115  11.856  1.00 13.77 ?  56  ALA   A HA   1 
ATOM   1236 H HB1  . ALA   A 1 56  ? 21.227 7.894   12.548  1.00 14.80 ?  56  ALA   A HB1  1 
ATOM   1237 H HB2  . ALA   A 1 56  ? 20.415 8.145   11.206  1.00 14.80 ?  56  ALA   A HB2  1 
ATOM   1238 H HB3  . ALA   A 1 56  ? 21.823 7.411   11.157  1.00 14.80 ?  56  ALA   A HB3  1 
ATOM   1239 N N    . THR   A 1 57  ? 24.449 9.295   11.442  1.00 10.53 ?  57  THR   A N    1 
ATOM   1240 C CA   . THR   A 1 57  ? 25.790 9.415   12.020  1.00 10.89 ?  57  THR   A CA   1 
ATOM   1241 C C    . THR   A 1 57  ? 26.348 10.834  11.945  1.00 11.36 ?  57  THR   A C    1 
ATOM   1242 O O    . THR   A 1 57  ? 27.532 11.045  12.242  1.00 11.82 ?  57  THR   A O    1 
ATOM   1243 C CB   . THR   A 1 57  ? 26.800 8.463   11.347  1.00 10.82 ?  57  THR   A CB   1 
ATOM   1244 O OG1  . THR   A 1 57  ? 27.182 8.962   10.051  1.00 10.28 ?  57  THR   A OG1  1 
ATOM   1245 C CG2  . THR   A 1 57  ? 26.266 7.049   11.238  1.00 10.82 ?  57  THR   A CG2  1 
ATOM   1246 H H    . THR   A 1 57  ? 24.455 9.091   10.605  1.00 12.63 ?  57  THR   A H    1 
ATOM   1247 H HA   . THR   A 1 57  ? 25.738 9.155   12.959  1.00 13.06 ?  57  THR   A HA   1 
ATOM   1248 H HB   . THR   A 1 57  ? 27.596 8.419   11.904  1.00 12.98 ?  57  THR   A HB   1 
ATOM   1249 H HG1  . THR   A 1 57  ? 26.502 9.027   9.563   1.00 12.33 ?  57  THR   A HG1  1 
ATOM   1250 H HG21 . THR   A 1 57  ? 26.941 6.464   10.854  1.00 12.97 ?  57  THR   A HG21 1 
ATOM   1251 H HG22 . THR   A 1 57  ? 26.024 6.712   12.114  1.00 12.97 ?  57  THR   A HG22 1 
ATOM   1252 H HG23 . THR   A 1 57  ? 25.481 7.031   10.669  1.00 12.97 ?  57  THR   A HG23 1 
ATOM   1253 N N    . ASN   A 1 58  ? 25.535 11.807  11.544  1.00 11.55 ?  58  ASN   A N    1 
ATOM   1254 C CA   . ASN   A 1 58  ? 26.002 13.185  11.448  1.00 12.53 ?  58  ASN   A CA   1 
ATOM   1255 C C    . ASN   A 1 58  ? 27.151 13.310  10.444  1.00 11.48 ?  58  ASN   A C    1 
ATOM   1256 O O    . ASN   A 1 58  ? 28.053 14.136  10.609  1.00 12.18 ?  58  ASN   A O    1 
ATOM   1257 C CB   . ASN   A 1 58  ? 26.376 13.726  12.842  1.00 15.76 ?  58  ASN   A CB   1 
ATOM   1258 C CG   . ASN   A 1 58  ? 26.743 15.192  12.837  1.00 19.75 ?  58  ASN   A CG   1 
ATOM   1259 O OD1  . ASN   A 1 58  ? 26.123 15.990  12.144  1.00 21.42 ?  58  ASN   A OD1  1 
ATOM   1260 N ND2  . ASN   A 1 58  ? 27.756 15.557  13.620  1.00 21.36 ?  58  ASN   A ND2  1 
ATOM   1261 H H    . ASN   A 1 58  ? 24.712 11.688  11.316  1.00 13.85 ?  58  ASN   A H    1 
ATOM   1262 H HA   . ASN   A 1 58  ? 25.269 13.721  11.119  1.00 15.03 ?  58  ASN   A HA   1 
ATOM   1263 H HB2  . ASN   A 1 58  ? 25.613 13.603  13.442  1.00 18.90 ?  58  ASN   A HB2  1 
ATOM   1264 H HB3  . ASN   A 1 58  ? 27.136 13.238  13.184  1.00 18.90 ?  58  ASN   A HB3  1 
ATOM   1265 H HD21 . ASN   A 1 58  ? 27.984 16.388  13.663  1.00 25.63 ?  58  ASN   A HD21 1 
ATOM   1266 H HD22 . ASN   A 1 58  ? 28.156 14.974  14.096  1.00 25.63 ?  58  ASN   A HD22 1 
ATOM   1267 N N    . ASN   A 1 59  ? 27.121 12.494  9.385   1.00 10.52 ?  59  ASN   A N    1 
ATOM   1268 C CA   . ASN   A 1 59  ? 28.101 12.473  8.290   1.00 10.50 ?  59  ASN   A CA   1 
ATOM   1269 C C    . ASN   A 1 59  ? 29.420 11.794  8.675   1.00 10.10 ?  59  ASN   A C    1 
ATOM   1270 O O    . ASN   A 1 59  ? 30.339 11.744  7.843   1.00 10.02 ?  59  ASN   A O    1 
ATOM   1271 C CB   . ASN   A 1 59  ? 28.386 13.863  7.688   1.00 10.85 ?  59  ASN   A CB   1 
ATOM   1272 C CG   . ASN   A 1 59  ? 28.747 13.803  6.220   1.00 10.83 ?  59  ASN   A CG   1 
ATOM   1273 O OD1  . ASN   A 1 59  ? 28.040 13.188  5.417   1.00 11.09 ?  59  ASN   A OD1  1 
ATOM   1274 N ND2  . ASN   A 1 59  ? 29.840 14.462  5.853   1.00 11.29 ?  59  ASN   A ND2  1 
ATOM   1275 H H    . ASN   A 1 59  ? 26.496 11.914  9.265   1.00 12.61 ?  59  ASN   A H    1 
ATOM   1276 H HA   . ASN   A 1 59  ? 27.720 11.942  7.576   1.00 12.59 ?  59  ASN   A HA   1 
ATOM   1277 H HB2  . ASN   A 1 59  ? 27.592 14.415  7.770   1.00 13.01 ?  59  ASN   A HB2  1 
ATOM   1278 H HB3  . ASN   A 1 59  ? 29.126 14.271  8.158   1.00 13.01 ?  59  ASN   A HB3  1 
ATOM   1279 H HD21 . ASN   A 1 59  ? 30.094 14.461  5.033   1.00 13.53 ?  59  ASN   A HD21 1 
ATOM   1280 H HD22 . ASN   A 1 59  ? 30.312 14.881  6.445   1.00 13.53 ?  59  ASN   A HD22 1 
ATOM   1281 N N    . ALA   A 1 60  ? 29.544 11.243  9.882   1.00 10.10 ?  60  ALA   A N    1 
ATOM   1282 C CA   . ALA   A 1 60  ? 30.783 10.560  10.235  1.00 10.07 ?  60  ALA   A CA   1 
ATOM   1283 C C    . ALA   A 1 60  ? 31.006 9.327   9.364   1.00 10.18 ?  60  ALA   A C    1 
ATOM   1284 O O    . ALA   A 1 60  ? 32.150 9.004   9.031   1.00 10.57 ?  60  ALA   A O    1 
ATOM   1285 C CB   . ALA   A 1 60  ? 30.778 10.193  11.716  1.00 11.15 ?  60  ALA   A CB   1 
ATOM   1286 H H    . ALA   A 1 60  ? 28.938 11.243  10.495  1.00 12.11 ?  60  ALA   A H    1 
ATOM   1287 H HA   . ALA   A 1 60  ? 31.522 11.164  10.081  1.00 12.07 ?  60  ALA   A HA   1 
ATOM   1288 H HB1  . ALA   A 1 60  ? 31.610 9.742   11.932  1.00 13.38 ?  60  ALA   A HB1  1 
ATOM   1289 H HB2  . ALA   A 1 60  ? 30.699 11.006  12.242  1.00 13.38 ?  60  ALA   A HB2  1 
ATOM   1290 H HB3  . ALA   A 1 60  ? 30.027 9.608   11.898  1.00 13.38 ?  60  ALA   A HB3  1 
ATOM   1291 N N    . MET   A 1 61  ? 29.931 8.632   8.980   1.00 9.83  ?  61  MET   A N    1 
ATOM   1292 C CA   . MET   A 1 61  ? 30.064 7.495   8.072   1.00 9.67  ?  61  MET   A CA   1 
ATOM   1293 C C    . MET   A 1 61  ? 30.693 7.924   6.751   1.00 9.44  ?  61  MET   A C    1 
ATOM   1294 O O    . MET   A 1 61  ? 31.583 7.242   6.231   1.00 9.81  ?  61  MET   A O    1 
ATOM   1295 C CB   . MET   A 1 61  ? 28.697 6.838   7.857   1.00 9.53  ?  61  MET   A CB   1 
ATOM   1296 C CG   . MET   A 1 61  ? 28.711 5.684   6.878   1.00 9.96  ?  61  MET   A CG   1 
ATOM   1297 S SD   . MET   A 1 61  ? 27.080 4.933   6.674   1.00 11.07 ?  61  MET   A SD   1 
ATOM   1298 C CE   . MET   A 1 61  ? 26.959 4.029   8.226   1.00 12.21 ?  61  MET   A CE   1 
ATOM   1299 H H    . MET   A 1 61  ? 29.125 8.799   9.228   1.00 11.79 ?  61  MET   A H    1 
ATOM   1300 H HA   . MET   A 1 61  ? 30.640 6.837   8.489   1.00 11.60 ?  61  MET   A HA   1 
ATOM   1301 H HB2  . MET   A 1 61  ? 28.377 6.501   8.708   1.00 11.43 ?  61  MET   A HB2  1 
ATOM   1302 H HB3  . MET   A 1 61  ? 28.081 7.507   7.518   1.00 11.43 ?  61  MET   A HB3  1 
ATOM   1303 H HG2  . MET   A 1 61  ? 28.994 6.003   6.008   1.00 11.94 ?  61  MET   A HG2  1 
ATOM   1304 H HG3  . MET   A 1 61  ? 29.316 5.001   7.200   1.00 11.94 ?  61  MET   A HG3  1 
ATOM   1305 H HE1  . MET   A 1 61  ? 26.124 3.536   8.242   1.00 14.64 ?  61  MET   A HE1  1 
ATOM   1306 H HE2  . MET   A 1 61  ? 27.707 3.413   8.292   1.00 14.64 ?  61  MET   A HE2  1 
ATOM   1307 H HE3  . MET   A 1 61  ? 26.986 4.658   8.965   1.00 14.64 ?  61  MET   A HE3  1 
ATOM   1308 N N    . GLN   A 1 62  ? 30.250 9.057   6.196   1.00 9.48  ?  62  GLN   A N    1 
ATOM   1309 C CA   . GLN   A 1 62  ? 30.815 9.535   4.935   1.00 9.59  ?  62  GLN   A CA   1 
ATOM   1310 C C    . GLN   A 1 62  ? 32.285 9.912   5.081   1.00 9.76  ?  62  GLN   A C    1 
ATOM   1311 O O    . GLN   A 1 62  ? 33.094 9.602   4.200   1.00 9.93  ?  62  GLN   A O    1 
ATOM   1312 C CB   . GLN   A 1 62  ? 30.016 10.722  4.398   1.00 9.92  ?  62  GLN   A CB   1 
ATOM   1313 C CG   . GLN   A 1 62  ? 30.391 11.091  2.966   1.00 9.75  ?  62  GLN   A CG   1 
ATOM   1314 C CD   . GLN   A 1 62  ? 30.064 9.961   2.018   1.00 10.07 ?  62  GLN   A CD   1 
ATOM   1315 O OE1  . GLN   A 1 62  ? 28.886 9.648   1.813   1.00 10.53 ?  62  GLN   A OE1  1 
ATOM   1316 N NE2  . GLN   A 1 62  ? 31.086 9.301   1.480   1.00 10.26 ?  62  GLN   A NE2  1 
ATOM   1317 H H    . GLN   A 1 62  ? 29.627 9.553   6.524   1.00 11.36 ?  62  GLN   A H    1 
ATOM   1318 H HA   . GLN   A 1 62  ? 30.758 8.818   4.285   1.00 11.49 ?  62  GLN   A HA   1 
ATOM   1319 H HB2  . GLN   A 1 62  ? 29.070 10.506  4.414   1.00 11.90 ?  62  GLN   A HB2  1 
ATOM   1320 H HB3  . GLN   A 1 62  ? 30.186 11.498  4.959   1.00 11.90 ?  62  GLN   A HB3  1 
ATOM   1321 H HG2  . GLN   A 1 62  ? 29.886 11.871  2.692   1.00 11.69 ?  62  GLN   A HG2  1 
ATOM   1322 H HG3  . GLN   A 1 62  ? 31.342 11.266  2.916   1.00 11.69 ?  62  GLN   A HG3  1 
ATOM   1323 H HE21 . GLN   A 1 62  ? 31.894 9.539   1.659   1.00 12.30 ?  62  GLN   A HE21 1 
ATOM   1324 H HE22 . GLN   A 1 62  ? 30.941 8.644   0.945   1.00 12.30 ?  62  GLN   A HE22 1 
ATOM   1325 N N    . VAL   A 1 63  ? 32.651 10.591  6.175   1.00 10.36 ?  63  VAL   A N    1 
ATOM   1326 C CA   . VAL   A 1 63  ? 34.043 10.991  6.378   1.00 11.23 ?  63  VAL   A CA   1 
ATOM   1327 C C    . VAL   A 1 63  ? 34.941 9.758   6.431   1.00 10.23 ?  63  VAL   A C    1 
ATOM   1328 O O    . VAL   A 1 63  ? 35.993 9.697   5.777   1.00 10.76 ?  63  VAL   A O    1 
ATOM   1329 C CB   . VAL   A 1 63  ? 34.160 11.860  7.645   1.00 12.49 ?  63  VAL   A CB   1 
ATOM   1330 C CG1  . VAL   A 1 63  ? 35.613 12.105  7.990   1.00 14.54 ?  63  VAL   A CG1  1 
ATOM   1331 C CG2  . VAL   A 1 63  ? 33.426 13.187  7.450   1.00 12.82 ?  63  VAL   A CG2  1 
ATOM   1332 H H    . VAL   A 1 63  ? 32.109 10.822  6.810   1.00 12.42 ?  63  VAL   A H    1 
ATOM   1333 H HA   . VAL   A 1 63  ? 34.313 11.529  5.623   1.00 13.47 ?  63  VAL   A HA   1 
ATOM   1334 H HB   . VAL   A 1 63  ? 33.750 11.394  8.390   1.00 14.98 ?  63  VAL   A HB   1 
ATOM   1335 H HG11 . VAL   A 1 63  ? 35.671 12.845  8.612   1.00 17.44 ?  63  VAL   A HG11 1 
ATOM   1336 H HG12 . VAL   A 1 63  ? 35.987 11.304  8.393   1.00 17.44 ?  63  VAL   A HG12 1 
ATOM   1337 H HG13 . VAL   A 1 63  ? 36.099 12.321  7.175   1.00 17.44 ?  63  VAL   A HG13 1 
ATOM   1338 H HG21 . VAL   A 1 63  ? 33.524 13.721  8.255   1.00 15.38 ?  63  VAL   A HG21 1 
ATOM   1339 H HG22 . VAL   A 1 63  ? 33.815 13.655  6.695   1.00 15.38 ?  63  VAL   A HG22 1 
ATOM   1340 H HG23 . VAL   A 1 63  ? 32.489 13.008  7.283   1.00 15.38 ?  63  VAL   A HG23 1 
ATOM   1341 N N    . GLU   A 1 64  ? 34.521 8.748   7.197   1.00 10.28 ?  64  GLU   A N    1 
ATOM   1342 C CA   . GLU   A 1 64  ? 35.284 7.511   7.294   1.00 10.50 ?  64  GLU   A CA   1 
ATOM   1343 C C    . GLU   A 1 64  ? 35.368 6.822   5.937   1.00 10.02 ?  64  GLU   A C    1 
ATOM   1344 O O    . GLU   A 1 64  ? 36.417 6.279   5.559   1.00 10.30 ?  64  GLU   A O    1 
ATOM   1345 C CB   . GLU   A 1 64  ? 34.600 6.602   8.317   1.00 10.82 ?  64  GLU   A CB   1 
ATOM   1346 C CG   . GLU   A 1 64  ? 35.247 5.248   8.469   1.00 11.36 ?  64  GLU   A CG   1 
ATOM   1347 C CD   . GLU   A 1 64  ? 34.367 4.253   9.198   1.00 11.84 ?  64  GLU   A CD   1 
ATOM   1348 O OE1  . GLU   A 1 64  ? 33.128 4.343   9.066   1.00 12.59 ?  64  GLU   A OE1  1 
ATOM   1349 O OE2  . GLU   A 1 64  ? 34.916 3.359   9.884   1.00 12.55 -1 64  GLU   A OE2  1 
ATOM   1350 H H    . GLU   A 1 64  ? 33.797 8.758   7.665   1.00 12.33 ?  64  GLU   A H    1 
ATOM   1351 H HA   . GLU   A 1 64  ? 36.183 7.712   7.605   1.00 12.60 ?  64  GLU   A HA   1 
ATOM   1352 H HB2  . GLU   A 1 64  ? 34.622 7.045   9.186   1.00 12.98 ?  64  GLU   A HB2  1 
ATOM   1353 H HB3  . GLU   A 1 64  ? 33.679 6.475   8.045   1.00 12.98 ?  64  GLU   A HB3  1 
ATOM   1354 H HG2  . GLU   A 1 64  ? 35.446 4.884   7.589   1.00 13.63 ?  64  GLU   A HG2  1 
ATOM   1355 H HG3  . GLU   A 1 64  ? 36.069 5.350   8.973   1.00 13.63 ?  64  GLU   A HG3  1 
ATOM   1356 N N    . SER   A 1 65  ? 34.249 6.812   5.209   1.00 9.72  ?  65  SER   A N    1 
ATOM   1357 C CA   . SER   A 1 65  ? 34.196 6.159   3.906   1.00 9.78  ?  65  SER   A CA   1 
ATOM   1358 C C    . SER   A 1 65  ? 35.123 6.830   2.901   1.00 10.03 ?  65  SER   A C    1 
ATOM   1359 O O    . SER   A 1 65  ? 35.756 6.153   2.083   1.00 10.52 ?  65  SER   A O    1 
ATOM   1360 C CB   . SER   A 1 65  ? 32.764 6.182   3.374   1.00 9.70  ?  65  SER   A CB   1 
ATOM   1361 O OG   . SER   A 1 65  ? 31.905 5.356   4.152   1.00 10.06 ?  65  SER   A OG   1 
ATOM   1362 H H    . SER   A 1 65  ? 33.510 7.184   5.449   1.00 11.65 ?  65  SER   A H    1 
ATOM   1363 H HA   . SER   A 1 65  ? 34.470 5.235   4.003   1.00 11.73 ?  65  SER   A HA   1 
ATOM   1364 H HB2  . SER   A 1 65  ? 32.431 7.090   3.399   1.00 11.63 ?  65  SER   A HB2  1 
ATOM   1365 H HB3  . SER   A 1 65  ? 32.766 5.854   2.461   1.00 11.63 ?  65  SER   A HB3  1 
ATOM   1366 H HG   . SER   A 1 65  ? 31.892 5.628   4.949   1.00 12.07 ?  65  SER   A HG   1 
ATOM   1367 N N    . ASP   A 1 66  ? 35.200 8.165   2.928   1.00 9.91  ?  66  ASP   A N    1 
ATOM   1368 C CA   . ASP   A 1 66  ? 36.058 8.866   1.981   1.00 10.92 ?  66  ASP   A CA   1 
ATOM   1369 C C    . ASP   A 1 66  ? 37.520 8.503   2.208   1.00 10.80 ?  66  ASP   A C    1 
ATOM   1370 O O    . ASP   A 1 66  ? 38.284 8.331   1.251   1.00 11.44 ?  66  ASP   A O    1 
ATOM   1371 C CB   . ASP   A 1 66  ? 35.848 10.375  2.105   1.00 12.41 ?  66  ASP   A CB   1 
ATOM   1372 C CG   . ASP   A 1 66  ? 34.512 10.847  1.519   1.00 14.22 ?  66  ASP   A CG   1 
ATOM   1373 O OD1  . ASP   A 1 66  ? 33.788 10.058  0.876   1.00 13.98 ?  66  ASP   A OD1  1 
ATOM   1374 O OD2  . ASP   A 1 66  ? 34.212 12.046  1.682   1.00 16.94 -1 66  ASP   A OD2  1 
ATOM   1375 H H    . ASP   A 1 66  ? 34.770 8.673   3.477   1.00 11.88 ?  66  ASP   A H    1 
ATOM   1376 H HA   . ASP   A 1 66  ? 35.814 8.601   1.083   1.00 13.10 ?  66  ASP   A HA   1 
ATOM   1377 H HB2  . ASP   A 1 66  ? 35.867 10.624  3.042   1.00 14.89 ?  66  ASP   A HB2  1 
ATOM   1378 H HB3  . ASP   A 1 66  ? 36.561 10.831  1.627   1.00 14.89 ?  66  ASP   A HB3  1 
ATOM   1379 N N    . ASP   A 1 67  ? 37.924 8.366   3.471   1.00 10.94 ?  67  ASP   A N    1 
ATOM   1380 C CA   . ASP   A 1 67  ? 39.276 7.915   3.762   1.00 11.85 ?  67  ASP   A CA   1 
ATOM   1381 C C    . ASP   A 1 67  ? 39.489 6.481   3.288   1.00 11.56 ?  67  ASP   A C    1 
ATOM   1382 O O    . ASP   A 1 67  ? 40.546 6.161   2.728   1.00 11.92 ?  67  ASP   A O    1 
ATOM   1383 C CB   . ASP   A 1 67  ? 39.553 8.048   5.258   1.00 12.93 ?  67  ASP   A CB   1 
ATOM   1384 C CG   . ASP   A 1 67  ? 40.846 7.376   5.671   1.00 14.34 ?  67  ASP   A CG   1 
ATOM   1385 O OD1  . ASP   A 1 67  ? 41.923 7.995   5.512   1.00 16.84 ?  67  ASP   A OD1  1 
ATOM   1386 O OD2  . ASP   A 1 67  ? 40.786 6.218   6.146   1.00 13.95 -1 67  ASP   A OD2  1 
ATOM   1387 H H    . ASP   A 1 67  ? 37.443 8.526   4.160   1.00 13.12 ?  67  ASP   A H    1 
ATOM   1388 H HA   . ASP   A 1 67  ? 39.905 8.477   3.284   1.00 14.21 ?  67  ASP   A HA   1 
ATOM   1389 H HB2  . ASP   A 1 67  ? 39.618 8.985   5.477   1.00 15.51 ?  67  ASP   A HB2  1 
ATOM   1390 H HB3  . ASP   A 1 67  ? 38.825 7.632   5.745   1.00 15.51 ?  67  ASP   A HB3  1 
ATOM   1391 N N    . TYR   A 1 68  ? 38.493 5.606   3.487   1.00 11.23 ?  68  TYR   A N    1 
ATOM   1392 C CA   . TYR   A 1 68  ? 38.607 4.227   3.009   1.00 11.30 ?  68  TYR   A CA   1 
ATOM   1393 C C    . TYR   A 1 68  ? 38.851 4.181   1.501   1.00 10.87 ?  68  TYR   A C    1 
ATOM   1394 O O    . TYR   A 1 68  ? 39.729 3.448   1.024   1.00 11.44 ?  68  TYR   A O    1 
ATOM   1395 C CB   . TYR   A 1 68  ? 37.351 3.409   3.384   1.00 11.63 ?  68  TYR   A CB   1 
ATOM   1396 C CG   . TYR   A 1 68  ? 37.376 2.024   2.751   1.00 12.90 ?  68  TYR   A CG   1 
ATOM   1397 C CD1  . TYR   A 1 68  ? 36.927 1.833   1.447   1.00 14.06 ?  68  TYR   A CD1  1 
ATOM   1398 C CD2  . TYR   A 1 68  ? 37.915 0.932   3.418   1.00 13.95 ?  68  TYR   A CD2  1 
ATOM   1399 C CE1  . TYR   A 1 68  ? 36.995 0.612   0.827   1.00 15.07 ?  68  TYR   A CE1  1 
ATOM   1400 C CE2  . TYR   A 1 68  ? 37.980 -0.323  2.797   1.00 14.48 ?  68  TYR   A CE2  1 
ATOM   1401 C CZ   . TYR   A 1 68  ? 37.532 -0.454  1.499   1.00 14.99 ?  68  TYR   A CZ   1 
ATOM   1402 O OH   . TYR   A 1 68  ? 37.610 -1.662  0.862   1.00 15.80 ?  68  TYR   A OH   1 
ATOM   1403 H H    . TYR   A 1 68  ? 37.750 5.783   3.886   1.00 13.47 ?  68  TYR   A H    1 
ATOM   1404 H HA   . TYR   A 1 68  ? 39.365 3.810   3.442   1.00 13.55 ?  68  TYR   A HA   1 
ATOM   1405 H HB2  . TYR   A 1 68  ? 37.317 3.298   4.349   1.00 13.95 ?  68  TYR   A HB2  1 
ATOM   1406 H HB3  . TYR   A 1 68  ? 36.558 3.871   3.072   1.00 13.95 ?  68  TYR   A HB3  1 
ATOM   1407 H HD1  . TYR   A 1 68  ? 36.580 2.562   0.980   1.00 16.87 ?  68  TYR   A HD1  1 
ATOM   1408 H HD2  . TYR   A 1 68  ? 38.243 1.034   4.281   1.00 16.74 ?  68  TYR   A HD2  1 
ATOM   1409 H HE1  . TYR   A 1 68  ? 36.685 0.515   -0.045  1.00 18.08 ?  68  TYR   A HE1  1 
ATOM   1410 H HE2  . TYR   A 1 68  ? 38.348 -1.047  3.238   1.00 17.37 ?  68  TYR   A HE2  1 
ATOM   1411 H HH   . TYR   A 1 68  ? 37.942 -2.235  1.381   1.00 18.95 ?  68  TYR   A HH   1 
ATOM   1412 N N    . ILE   A 1 69  ? 38.067 4.945   0.733   1.00 10.67 ?  69  ILE   A N    1 
ATOM   1413 C CA   . ILE   A 1 69  ? 38.202 4.939   -0.723  1.00 10.79 ?  69  ILE   A CA   1 
ATOM   1414 C C    . ILE   A 1 69  ? 39.538 5.546   -1.153  1.00 10.82 ?  69  ILE   A C    1 
ATOM   1415 O O    . ILE   A 1 69  ? 40.182 5.062   -2.093  1.00 11.34 ?  69  ILE   A O    1 
ATOM   1416 C CB   . ILE   A 1 69  ? 37.006 5.657   -1.381  1.00 11.76 ?  69  ILE   A CB   1 
ATOM   1417 C CG1  . ILE   A 1 69  ? 35.693 4.917   -1.112  1.00 12.24 ?  69  ILE   A CG1  1 
ATOM   1418 C CG2  . ILE   A 1 69  ? 37.244 5.842   -2.884  1.00 13.35 ?  69  ILE   A CG2  1 
ATOM   1419 C CD1  . ILE   A 1 69  ? 35.520 3.641   -1.908  1.00 12.69 ?  69  ILE   A CD1  1 
ATOM   1420 H H    . ILE   A 1 69  ? 37.462 5.478   1.032   1.00 12.80 ?  69  ILE   A H    1 
ATOM   1421 H HA   . ILE   A 1 69  ? 38.195 4.022   -1.022  1.00 12.93 ?  69  ILE   A HA   1 
ATOM   1422 H HB   . ILE   A 1 69  ? 36.935 6.537   -0.984  1.00 14.10 ?  69  ILE   A HB   1 
ATOM   1423 H HG12 . ILE   A 1 69  ? 35.658 4.679   -0.171  1.00 14.68 ?  69  ILE   A HG12 1 
ATOM   1424 H HG13 . ILE   A 1 69  ? 34.956 5.503   -1.329  1.00 14.68 ?  69  ILE   A HG13 1 
ATOM   1425 H HG21 . ILE   A 1 69  ? 36.398 6.055   -3.310  1.00 16.02 ?  69  ILE   A HG21 1 
ATOM   1426 H HG22 . ILE   A 1 69  ? 37.869 6.575   -3.018  1.00 16.02 ?  69  ILE   A HG22 1 
ATOM   1427 H HG23 . ILE   A 1 69  ? 37.605 5.025   -3.253  1.00 16.02 ?  69  ILE   A HG23 1 
ATOM   1428 H HD11 . ILE   A 1 69  ? 34.739 3.171   -1.578  1.00 15.22 ?  69  ILE   A HD11 1 
ATOM   1429 H HD12 . ILE   A 1 69  ? 35.395 3.869   -2.844  1.00 15.22 ?  69  ILE   A HD12 1 
ATOM   1430 H HD13 . ILE   A 1 69  ? 36.308 3.089   -1.803  1.00 15.22 ?  69  ILE   A HD13 1 
ATOM   1431 N N    . ALA   A 1 70  ? 39.963 6.627   -0.496  1.00 11.17 ?  70  ALA   A N    1 
ATOM   1432 C CA   . ALA   A 1 70  ? 41.242 7.231   -0.848  1.00 12.21 ?  70  ALA   A CA   1 
ATOM   1433 C C    . ALA   A 1 70  ? 42.382 6.240   -0.685  1.00 12.49 ?  70  ALA   A C    1 
ATOM   1434 O O    . ALA   A 1 70  ? 43.345 6.266   -1.458  1.00 14.31 ?  70  ALA   A O    1 
ATOM   1435 C CB   . ALA   A 1 70  ? 41.490 8.482   -0.002  1.00 13.15 ?  70  ALA   A CB   1 
ATOM   1436 H H    . ALA   A 1 70  ? 39.541 7.017   0.147   1.00 13.39 ?  70  ALA   A H    1 
ATOM   1437 H HA   . ALA   A 1 70  ? 41.212 7.506   -1.776  1.00 14.64 ?  70  ALA   A HA   1 
ATOM   1438 H HB1  . ALA   A 1 70  ? 42.348 8.869   -0.254  1.00 15.78 ?  70  ALA   A HB1  1 
ATOM   1439 H HB2  . ALA   A 1 70  ? 40.782 9.123   -0.161  1.00 15.78 ?  70  ALA   A HB2  1 
ATOM   1440 H HB3  . ALA   A 1 70  ? 41.509 8.233   0.937   1.00 15.78 ?  70  ALA   A HB3  1 
ATOM   1441 N N    . THR   A 1 71  ? 42.282 5.346   0.296   1.00 11.66 ?  71  THR   A N    1 
ATOM   1442 C CA   . THR   A 1 71  ? 43.336 4.373   0.544   1.00 13.35 ?  71  THR   A CA   1 
ATOM   1443 C C    . THR   A 1 71  ? 43.217 3.152   -0.356  1.00 13.23 ?  71  THR   A C    1 
ATOM   1444 O O    . THR   A 1 71  ? 44.228 2.648   -0.861  1.00 15.11 ?  71  THR   A O    1 
ATOM   1445 C CB   . THR   A 1 71  ? 43.274 3.929   2.001   1.00 14.96 ?  71  THR   A CB   1 
ATOM   1446 O OG1  . THR   A 1 71  ? 43.528 5.056   2.846   1.00 16.17 ?  71  THR   A OG1  1 
ATOM   1447 C CG2  . THR   A 1 71  ? 44.286 2.825   2.285   1.00 16.49 ?  71  THR   A CG2  1 
ATOM   1448 H H    . THR   A 1 71  ? 41.608 5.279   0.827   1.00 13.98 ?  71  THR   A H    1 
ATOM   1449 H HA   . THR   A 1 71  ? 44.196 4.784   0.381   1.00 16.02 ?  71  THR   A HA   1 
ATOM   1450 H HB   . THR   A 1 71  ? 42.387 3.574   2.185   1.00 17.95 ?  71  THR   A HB   1 
ATOM   1451 H HG1  . THR   A 1 71  ? 43.488 4.817   3.650   1.00 19.39 ?  71  THR   A HG1  1 
ATOM   1452 H HG21 . THR   A 1 71  ? 44.421 2.745   3.242   1.00 19.78 ?  71  THR   A HG21 1 
ATOM   1453 H HG22 . THR   A 1 71  ? 43.971 1.978   1.938   1.00 19.78 ?  71  THR   A HG22 1 
ATOM   1454 H HG23 . THR   A 1 71  ? 45.137 3.043   1.868   1.00 19.78 ?  71  THR   A HG23 1 
ATOM   1455 N N    . ASN   A 1 72  ? 41.995 2.645   -0.544  1.00 12.35 ?  72  ASN   A N    1 
ATOM   1456 C CA   . ASN   A 1 72  ? 41.776 1.319   -1.110  1.00 12.61 ?  72  ASN   A CA   1 
ATOM   1457 C C    . ASN   A 1 72  ? 41.144 1.306   -2.490  1.00 12.42 ?  72  ASN   A C    1 
ATOM   1458 O O    . ASN   A 1 72  ? 41.149 0.248   -3.137  1.00 13.77 ?  72  ASN   A O    1 
ATOM   1459 C CB   . ASN   A 1 72  ? 40.891 0.489   -0.171  1.00 13.45 ?  72  ASN   A CB   1 
ATOM   1460 C CG   . ASN   A 1 72  ? 41.503 0.334   1.190   1.00 14.59 ?  72  ASN   A CG   1 
ATOM   1461 O OD1  . ASN   A 1 72  ? 41.044 0.934   2.163   1.00 16.07 ?  72  ASN   A OD1  1 
ATOM   1462 N ND2  . ASN   A 1 72  ? 42.552 -0.461  1.272   1.00 14.81 ?  72  ASN   A ND2  1 
ATOM   1463 H H    . ASN   A 1 72  ? 41.265 3.059   -0.347  1.00 14.81 ?  72  ASN   A H    1 
ATOM   1464 H HA   . ASN   A 1 72  ? 42.628 0.871   -1.187  1.00 15.12 ?  72  ASN   A HA   1 
ATOM   1465 H HB2  . ASN   A 1 72  ? 40.035 0.924   -0.071  1.00 16.13 ?  72  ASN   A HB2  1 
ATOM   1466 H HB3  . ASN   A 1 72  ? 40.776 -0.399  -0.552  1.00 16.13 ?  72  ASN   A HB3  1 
ATOM   1467 H HD21 . ASN   A 1 72  ? 42.947 -0.579  2.029   1.00 17.76 ?  72  ASN   A HD21 1 
ATOM   1468 H HD22 . ASN   A 1 72  ? 42.854 -0.860  0.570   1.00 17.76 ?  72  ASN   A HD22 1 
ATOM   1469 N N    . GLY   A 1 73  ? 40.596 2.423   -2.951  1.00 12.27 ?  73  GLY   A N    1 
ATOM   1470 C CA   . GLY   A 1 73  ? 39.859 2.431   -4.188  1.00 12.07 ?  73  GLY   A CA   1 
ATOM   1471 C C    . GLY   A 1 73  ? 38.468 1.850   -4.014  1.00 11.53 ?  73  GLY   A C    1 
ATOM   1472 O O    . GLY   A 1 73  ? 38.084 1.396   -2.932  1.00 11.93 ?  73  GLY   A O    1 
ATOM   1473 H H    . GLY   A 1 73  ? 40.637 3.196   -2.565  1.00 14.72 ?  73  GLY   A H    1 
ATOM   1474 H HA2  . GLY   A 1 73  ? 39.782 3.343   -4.515  1.00 14.47 ?  73  GLY   A HA2  1 
ATOM   1475 H HA3  . GLY   A 1 73  ? 40.337 1.907   -4.855  1.00 14.47 ?  73  GLY   A HA3  1 
ATOM   1476 N N    . PRO   A 1 74  ? 37.690 1.869   -5.093  1.00 11.87 ?  74  PRO   A N    1 
ATOM   1477 C CA   . PRO   A 1 74  ? 36.293 1.443   -5.010  1.00 12.04 ?  74  PRO   A CA   1 
ATOM   1478 C C    . PRO   A 1 74  ? 36.146 -0.043  -4.708  1.00 11.39 ?  74  PRO   A C    1 
ATOM   1479 O O    . PRO   A 1 74  ? 37.011 -0.878  -4.996  1.00 12.07 ?  74  PRO   A O    1 
ATOM   1480 C CB   . PRO   A 1 74  ? 35.742 1.763   -6.404  1.00 13.74 ?  74  PRO   A CB   1 
ATOM   1481 C CG   . PRO   A 1 74  ? 36.702 2.730   -7.006  1.00 16.22 ?  74  PRO   A CG   1 
ATOM   1482 C CD   . PRO   A 1 74  ? 38.037 2.381   -6.430  1.00 13.72 ?  74  PRO   A CD   1 
ATOM   1483 H HA   . PRO   A 1 74  ? 35.816 1.965   -4.338  1.00 14.44 ?  74  PRO   A HA   1 
ATOM   1484 H HB2  . PRO   A 1 74  ? 35.698 0.949   -6.925  1.00 16.48 ?  74  PRO   A HB2  1 
ATOM   1485 H HB3  . PRO   A 1 74  ? 34.862 2.164   -6.317  1.00 16.48 ?  74  PRO   A HB3  1 
ATOM   1486 H HG2  . PRO   A 1 74  ? 36.711 2.624   -7.968  1.00 19.45 ?  74  PRO   A HG2  1 
ATOM   1487 H HG3  . PRO   A 1 74  ? 36.455 3.634   -6.760  1.00 19.45 ?  74  PRO   A HG3  1 
ATOM   1488 H HD2  . PRO   A 1 74  ? 38.470 1.690   -6.958  1.00 16.45 ?  74  PRO   A HD2  1 
ATOM   1489 H HD3  . PRO   A 1 74  ? 38.592 3.177   -6.367  1.00 16.45 ?  74  PRO   A HD3  1 
ATOM   1490 N N    . LEU   A 1 75  ? 34.994 -0.365  -4.127  1.00 10.80 ?  75  LEU   A N    1 
ATOM   1491 C CA   . LEU   A 1 75  ? 34.584 -1.752  -3.981  1.00 10.49 ?  75  LEU   A CA   1 
ATOM   1492 C C    . LEU   A 1 75  ? 34.192 -2.321  -5.341  1.00 11.01 ?  75  LEU   A C    1 
ATOM   1493 O O    . LEU   A 1 75  ? 34.082 -1.603  -6.340  1.00 12.11 ?  75  LEU   A O    1 
ATOM   1494 C CB   . LEU   A 1 75  ? 33.397 -1.867  -3.021  1.00 10.40 ?  75  LEU   A CB   1 
ATOM   1495 C CG   . LEU   A 1 75  ? 33.606 -1.441  -1.568  1.00 12.22 ?  75  LEU   A CG   1 
ATOM   1496 C CD1  . LEU   A 1 75  ? 32.319 -1.621  -0.761  1.00 14.02 ?  75  LEU   A CD1  1 
ATOM   1497 C CD2  . LEU   A 1 75  ? 34.750 -2.165  -0.914  1.00 15.08 ?  75  LEU   A CD2  1 
ATOM   1498 H H    . LEU   A 1 75  ? 34.433 0.206   -3.814  1.00 12.95 ?  75  LEU   A H    1 
ATOM   1499 H HA   . LEU   A 1 75  ? 35.319 -2.271  -3.630  1.00 12.58 ?  75  LEU   A HA   1 
ATOM   1500 H HB2  . LEU   A 1 75  ? 32.673 -1.329  -3.368  1.00 12.47 ?  75  LEU   A HB2  1 
ATOM   1501 H HB3  . LEU   A 1 75  ? 33.120 -2.798  -3.000  1.00 12.47 ?  75  LEU   A HB3  1 
ATOM   1502 H HG   . LEU   A 1 75  ? 33.826 -0.495  -1.558  1.00 14.65 ?  75  LEU   A HG   1 
ATOM   1503 H HD11 . LEU   A 1 75  ? 32.481 -1.338  0.155   1.00 16.82 ?  75  LEU   A HD11 1 
ATOM   1504 H HD12 . LEU   A 1 75  ? 31.624 -1.070  -1.156  1.00 16.82 ?  75  LEU   A HD12 1 
ATOM   1505 H HD13 . LEU   A 1 75  ? 32.061 -2.551  -0.781  1.00 16.82 ?  75  LEU   A HD13 1 
ATOM   1506 H HD21 . LEU   A 1 75  ? 34.806 -1.897  0.018   1.00 18.09 ?  75  LEU   A HD21 1 
ATOM   1507 H HD22 . LEU   A 1 75  ? 34.600 -3.119  -0.976  1.00 18.09 ?  75  LEU   A HD22 1 
ATOM   1508 H HD23 . LEU   A 1 75  ? 35.578 -1.931  -1.370  1.00 18.09 ?  75  LEU   A HD23 1 
ATOM   1509 N N    . LYS   A 1 76  ? 33.995 -3.637  -5.364  1.00 11.46 ?  76  LYS   A N    1 
ATOM   1510 C CA   . LYS   A 1 76  ? 33.388 -4.340  -6.487  1.00 12.33 ?  76  LYS   A CA   1 
ATOM   1511 C C    . LYS   A 1 76  ? 31.873 -4.414  -6.290  1.00 10.97 ?  76  LYS   A C    1 
ATOM   1512 O O    . LYS   A 1 76  ? 31.388 -4.538  -5.166  1.00 10.55 ?  76  LYS   A O    1 
ATOM   1513 C CB   . LYS   A 1 76  ? 33.923 -5.782  -6.565  1.00 14.18 ?  76  LYS   A CB   1 
ATOM   1514 C CG   . LYS   A 1 76  ? 35.433 -5.901  -6.737  1.00 15.64 ?  76  LYS   A CG   1 
ATOM   1515 C CD   . LYS   A 1 76  ? 35.946 -7.310  -6.517  1.00 17.04 ?  76  LYS   A CD   1 
ATOM   1516 C CE   . LYS   A 1 76  ? 37.439 -7.379  -6.751  1.00 19.47 ?  76  LYS   A CE   1 
ATOM   1517 N NZ   . LYS   A 1 76  ? 37.987 -8.721  -6.465  1.00 20.48 ?  76  LYS   A NZ   1 
ATOM   1518 H H    . LYS   A 1 76  ? 34.212 -4.161  -4.714  1.00 13.75 ?  76  LYS   A H    1 
ATOM   1519 H HA   . LYS   A 1 76  ? 33.584 -3.878  -7.319  1.00 14.79 ?  76  LYS   A HA   1 
ATOM   1520 H HB2  . LYS   A 1 76  ? 33.684 -6.240  -5.747  1.00 17.00 ?  76  LYS   A HB2  1 
ATOM   1521 H HB3  . LYS   A 1 76  ? 33.507 -6.220  -7.323  1.00 17.00 ?  76  LYS   A HB3  1 
ATOM   1522 H HG2  . LYS   A 1 76  ? 35.672 -5.631  -7.639  1.00 18.76 ?  76  LYS   A HG2  1 
ATOM   1523 H HG3  . LYS   A 1 76  ? 35.872 -5.318  -6.094  1.00 18.76 ?  76  LYS   A HG3  1 
ATOM   1524 H HD2  . LYS   A 1 76  ? 35.762 -7.579  -5.602  1.00 20.44 ?  76  LYS   A HD2  1 
ATOM   1525 H HD3  . LYS   A 1 76  ? 35.505 -7.912  -7.139  1.00 20.44 ?  76  LYS   A HD3  1 
ATOM   1526 H HE2  . LYS   A 1 76  ? 37.623 -7.167  -7.679  1.00 23.35 ?  76  LYS   A HE2  1 
ATOM   1527 H HE3  . LYS   A 1 76  ? 37.880 -6.741  -6.168  1.00 23.35 ?  76  LYS   A HE3  1 
ATOM   1528 H HZ1  . LYS   A 1 76  ? 38.863 -8.732  -6.612  1.00 24.57 ?  76  LYS   A HZ1  1 
ATOM   1529 H HZ2  . LYS   A 1 76  ? 37.832 -8.940  -5.615  1.00 24.57 ?  76  LYS   A HZ2  1 
ATOM   1530 H HZ3  . LYS   A 1 76  ? 37.598 -9.328  -6.992  1.00 24.57 ?  76  LYS   A HZ3  1 
ATOM   1531 N N    . VAL   A 1 77  ? 31.121 -4.387  -7.395  1.00 10.95 ?  77  VAL   A N    1 
ATOM   1532 C CA   . VAL   A 1 77  ? 29.713 -4.773  -7.308  1.00 11.03 ?  77  VAL   A CA   1 
ATOM   1533 C C    . VAL   A 1 77  ? 29.651 -6.229  -6.869  1.00 10.42 ?  77  VAL   A C    1 
ATOM   1534 O O    . VAL   A 1 77  ? 30.318 -7.095  -7.446  1.00 10.57 ?  77  VAL   A O    1 
ATOM   1535 C CB   . VAL   A 1 77  ? 28.976 -4.535  -8.635  1.00 12.16 ?  77  VAL   A CB   1 
ATOM   1536 C CG1  . VAL   A 1 77  ? 27.507 -4.949  -8.510  1.00 13.24 ?  77  VAL   A CG1  1 
ATOM   1537 C CG2  . VAL   A 1 77  ? 29.076 -3.077  -9.049  1.00 13.69 ?  77  VAL   A CG2  1 
ATOM   1538 H H    . VAL   A 1 77  ? 31.398 -4.153  -8.175  1.00 13.13 ?  77  VAL   A H    1 
ATOM   1539 H HA   . VAL   A 1 77  ? 29.287 -4.236  -6.623  1.00 13.23 ?  77  VAL   A HA   1 
ATOM   1540 H HB   . VAL   A 1 77  ? 29.388 -5.076  -9.326  1.00 14.58 ?  77  VAL   A HB   1 
ATOM   1541 H HG11 . VAL   A 1 77  ? 27.035 -4.674  -9.309  1.00 15.87 ?  77  VAL   A HG11 1 
ATOM   1542 H HG12 . VAL   A 1 77  ? 27.453 -5.911  -8.406  1.00 15.87 ?  77  VAL   A HG12 1 
ATOM   1543 H HG13 . VAL   A 1 77  ? 27.122 -4.510  -7.732  1.00 15.87 ?  77  VAL   A HG13 1 
ATOM   1544 H HG21 . VAL   A 1 77  ? 28.557 -2.944  -9.855  1.00 16.42 ?  77  VAL   A HG21 1 
ATOM   1545 H HG22 . VAL   A 1 77  ? 28.727 -2.522  -8.333  1.00 16.42 ?  77  VAL   A HG22 1 
ATOM   1546 H HG23 . VAL   A 1 77  ? 30.007 -2.856  -9.212  1.00 16.42 ?  77  VAL   A HG23 1 
ATOM   1547 N N    . GLY   A 1 78  ? 28.862 -6.500  -5.827  1.00 10.33 ?  78  GLY   A N    1 
ATOM   1548 C CA   . GLY   A 1 78  ? 28.840 -7.787  -5.164  1.00 10.34 ?  78  GLY   A CA   1 
ATOM   1549 C C    . GLY   A 1 78  ? 29.755 -7.883  -3.962  1.00 9.93  ?  78  GLY   A C    1 
ATOM   1550 O O    . GLY   A 1 78  ? 29.697 -8.892  -3.238  1.00 10.39 ?  78  GLY   A O    1 
ATOM   1551 H H    . GLY   A 1 78  ? 28.307 -5.931  -5.491  1.00 12.39 ?  78  GLY   A H    1 
ATOM   1552 H HA2  . GLY   A 1 78  ? 27.935 -7.973  -4.872  1.00 12.40 ?  78  GLY   A HA2  1 
ATOM   1553 H HA3  . GLY   A 1 78  ? 29.099 -8.471  -5.801  1.00 12.40 ?  78  GLY   A HA3  1 
ATOM   1554 N N    . GLY   A 1 79  ? 30.608 -6.878  -3.740  1.00 9.88  ?  79  GLY   A N    1 
ATOM   1555 C CA   . GLY   A 1 79  ? 31.579 -6.899  -2.671  1.00 10.48 ?  79  GLY   A CA   1 
ATOM   1556 C C    . GLY   A 1 79  ? 31.140 -6.105  -1.449  1.00 9.74  ?  79  GLY   A C    1 
ATOM   1557 O O    . GLY   A 1 79  ? 30.020 -5.606  -1.358  1.00 10.15 ?  79  GLY   A O    1 
ATOM   1558 H H    . GLY   A 1 79  ? 30.635 -6.155  -4.211  1.00 11.85 ?  79  GLY   A H    1 
ATOM   1559 H HA2  . GLY   A 1 79  ? 31.740 -7.819  -2.403  1.00 12.56 ?  79  GLY   A HA2  1 
ATOM   1560 H HA3  . GLY   A 1 79  ? 32.416 -6.527  -2.990  1.00 12.56 ?  79  GLY   A HA3  1 
ATOM   1561 N N    . SER   A 1 80  ? 32.051 -6.023  -0.480  1.00 10.61 ?  80  SER   A N    1 
ATOM   1562 C CA   . SER   A 1 80  ? 31.745 -5.388  0.794   1.00 10.20 ?  80  SER   A CA   1 
ATOM   1563 C C    . SER   A 1 80  ? 33.022 -4.940  1.489   1.00 9.75  ?  80  SER   A C    1 
ATOM   1564 O O    . SER   A 1 80  ? 34.132 -5.378  1.157   1.00 11.33 ?  80  SER   A O    1 
ATOM   1565 C CB   . SER   A 1 80  ? 30.986 -6.347  1.718   1.00 10.93 ?  80  SER   A CB   1 
ATOM   1566 O OG   . SER   A 1 80  ? 31.814 -7.401  2.180   1.00 12.88 ?  80  SER   A OG   1 
ATOM   1567 H H    . SER   A 1 80  ? 32.851 -6.329  -0.536  1.00 12.73 ?  80  SER   A H    1 
ATOM   1568 H HA   . SER   A 1 80  ? 31.189 -4.612  0.624   1.00 12.24 ?  80  SER   A HA   1 
ATOM   1569 H HB2  . SER   A 1 80  ? 30.659 -5.852  2.484   1.00 13.11 ?  80  SER   A HB2  1 
ATOM   1570 H HB3  . SER   A 1 80  ? 30.239 -6.730  1.230   1.00 13.11 ?  80  SER   A HB3  1 
ATOM   1571 H HG   . SER   A 1 80  ? 32.107 -7.841  1.523   1.00 15.45 ?  80  SER   A HG   1 
ATOM   1572 N N    . CYS   A 1 81  ? 32.837 -4.098  2.507   1.00 9.54  ?  81  CYS   A N    1 
ATOM   1573 C CA   . CYS   A 1 81  ? 33.890 -3.819  3.471   1.00 9.80  ?  81  CYS   A CA   1 
ATOM   1574 C C    . CYS   A 1 81  ? 33.250 -3.583  4.832   1.00 9.77  ?  81  CYS   A C    1 
ATOM   1575 O O    . CYS   A 1 81  ? 32.085 -3.185  4.925   1.00 10.67 ?  81  CYS   A O    1 
ATOM   1576 C CB   . CYS   A 1 81  ? 34.763 -2.628  3.052   1.00 10.64 ?  81  CYS   A CB   1 
ATOM   1577 S SG   . CYS   A 1 81  ? 33.876 -1.051  3.068   1.00 10.61 ?  81  CYS   A SG   1 
ATOM   1578 H H    . CYS   A 1 81  ? 32.103 -3.667  2.658   1.00 11.44 ?  81  CYS   A H    1 
ATOM   1579 H HA   . CYS   A 1 81  ? 34.463 -4.597  3.537   1.00 11.75 ?  81  CYS   A HA   1 
ATOM   1580 H HB2  . CYS   A 1 81  ? 35.517 -2.563  3.665   1.00 12.76 ?  81  CYS   A HB2  1 
ATOM   1581 H HB3  . CYS   A 1 81  ? 35.094 -2.785  2.150   1.00 12.76 ?  81  CYS   A HB3  1 
ATOM   1582 H HG   . CYS   A 1 81  ? 34.629 -0.178  2.731   1.00 12.72 ?  81  CYS   A HG   1 
ATOM   1583 N N    . VAL   A 1 82  ? 34.025 -3.839  5.884   1.00 9.96  ?  82  VAL   A N    1 
ATOM   1584 C CA   . VAL   A 1 82  ? 33.599 -3.598  7.257   1.00 10.30 ?  82  VAL   A CA   1 
ATOM   1585 C C    . VAL   A 1 82  ? 34.203 -2.290  7.734   1.00 10.65 ?  82  VAL   A C    1 
ATOM   1586 O O    . VAL   A 1 82  ? 35.428 -2.121  7.723   1.00 11.52 ?  82  VAL   A O    1 
ATOM   1587 C CB   . VAL   A 1 82  ? 34.019 -4.738  8.194   1.00 11.86 ?  82  VAL   A CB   1 
ATOM   1588 C CG1  . VAL   A 1 82  ? 33.558 -4.439  9.611   1.00 13.37 ?  82  VAL   A CG1  1 
ATOM   1589 C CG2  . VAL   A 1 82  ? 33.474 -6.067  7.708   1.00 12.82 ?  82  VAL   A CG2  1 
ATOM   1590 H H    . VAL   A 1 82  ? 34.825 -4.171  5.826   1.00 11.94 ?  82  VAL   A H    1 
ATOM   1591 H HA   . VAL   A 1 82  ? 32.635 -3.514  7.282   1.00 12.36 ?  82  VAL   A HA   1 
ATOM   1592 H HB   . VAL   A 1 82  ? 34.983 -4.792  8.207   1.00 14.22 ?  82  VAL   A HB   1 
ATOM   1593 H HG11 . VAL   A 1 82  ? 33.625 -5.248  10.141  1.00 16.03 ?  82  VAL   A HG11 1 
ATOM   1594 H HG12 . VAL   A 1 82  ? 34.117 -3.746  9.994   1.00 16.03 ?  82  VAL   A HG12 1 
ATOM   1595 H HG13 . VAL   A 1 82  ? 32.631 -4.140  9.589   1.00 16.03 ?  82  VAL   A HG13 1 
ATOM   1596 H HG21 . VAL   A 1 82  ? 33.710 -6.757  8.348   1.00 15.37 ?  82  VAL   A HG21 1 
ATOM   1597 H HG22 . VAL   A 1 82  ? 32.509 -6.006  7.629   1.00 15.37 ?  82  VAL   A HG22 1 
ATOM   1598 H HG23 . VAL   A 1 82  ? 33.865 -6.270  6.844   1.00 15.37 ?  82  VAL   A HG23 1 
ATOM   1599 N N    . LEU   A 1 83  ? 33.351 -1.364  8.159   1.00 10.27 ?  83  LEU   A N    1 
ATOM   1600 C CA   . LEU   A 1 83  ? 33.771 -0.096  8.740   1.00 10.50 ?  83  LEU   A CA   1 
ATOM   1601 C C    . LEU   A 1 83  ? 33.055 0.078   10.077  1.00 10.43 ?  83  LEU   A C    1 
ATOM   1602 O O    . LEU   A 1 83  ? 32.340 -0.818  10.545  1.00 10.73 ?  83  LEU   A O    1 
ATOM   1603 C CB   . LEU   A 1 83  ? 33.519 1.059   7.758   1.00 10.83 ?  83  LEU   A CB   1 
ATOM   1604 C CG   . LEU   A 1 83  ? 34.412 1.056   6.513   1.00 11.38 ?  83  LEU   A CG   1 
ATOM   1605 C CD1  . LEU   A 1 83  ? 33.987 2.117   5.521   1.00 12.70 ?  83  LEU   A CD1  1 
ATOM   1606 C CD2  . LEU   A 1 83  ? 35.883 1.256   6.897   1.00 12.12 ?  83  LEU   A CD2  1 
ATOM   1607 H H    . LEU   A 1 83  ? 32.500 -1.454  8.119   1.00 12.32 ?  83  LEU   A H    1 
ATOM   1608 H HA   . LEU   A 1 83  ? 34.724 -0.130  8.919   1.00 12.59 ?  83  LEU   A HA   1 
ATOM   1609 H HB2  . LEU   A 1 83  ? 32.601 1.013   7.453   1.00 12.99 ?  83  LEU   A HB2  1 
ATOM   1610 H HB3  . LEU   A 1 83  ? 33.667 1.898   8.221   1.00 12.99 ?  83  LEU   A HB3  1 
ATOM   1611 H HG   . LEU   A 1 83  ? 34.342 0.191   6.082   1.00 13.65 ?  83  LEU   A HG   1 
ATOM   1612 H HD11 . LEU   A 1 83  ? 34.575 2.076   4.749   1.00 15.23 ?  83  LEU   A HD11 1 
ATOM   1613 H HD12 . LEU   A 1 83  ? 33.075 1.944   5.254   1.00 15.23 ?  83  LEU   A HD12 1 
ATOM   1614 H HD13 . LEU   A 1 83  ? 34.056 2.987   5.942   1.00 15.23 ?  83  LEU   A HD13 1 
ATOM   1615 H HD21 . LEU   A 1 83  ? 36.402 1.416   6.090   1.00 14.54 ?  83  LEU   A HD21 1 
ATOM   1616 H HD22 . LEU   A 1 83  ? 35.957 2.020   7.490   1.00 14.54 ?  83  LEU   A HD22 1 
ATOM   1617 H HD23 . LEU   A 1 83  ? 36.212 0.459   7.344   1.00 14.54 ?  83  LEU   A HD23 1 
ATOM   1618 N N    . SER   A 1 84  ? 33.273 1.225   10.716  1.00 10.82 ?  84  SER   A N    1 
ATOM   1619 C CA   . SER   A 1 84  ? 32.626 1.476   11.994  1.00 10.85 ?  84  SER   A CA   1 
ATOM   1620 C C    . SER   A 1 84  ? 31.109 1.569   11.841  1.00 11.04 ?  84  SER   A C    1 
ATOM   1621 O O    . SER   A 1 84  ? 30.588 2.040   10.830  1.00 11.26 ?  84  SER   A O    1 
ATOM   1622 C CB   . SER   A 1 84  ? 33.132 2.786   12.586  1.00 11.74 ?  84  SER   A CB   1 
ATOM   1623 O OG   . SER   A 1 84  ? 32.498 3.059   13.819  1.00 12.85 ?  84  SER   A OG   1 
ATOM   1624 H H    . SER   A 1 84  ? 33.780 1.866   10.429  1.00 12.98 ?  84  SER   A H    1 
ATOM   1625 H HA   . SER   A 1 84  ? 32.840 0.755   12.607  1.00 13.01 ?  84  SER   A HA   1 
ATOM   1626 H HB2  . SER   A 1 84  ? 34.090 2.723   12.734  1.00 14.08 ?  84  SER   A HB2  1 
ATOM   1627 H HB3  . SER   A 1 84  ? 32.943 3.510   11.966  1.00 14.08 ?  84  SER   A HB3  1 
ATOM   1628 H HG   . SER   A 1 84  ? 32.779 3.785   14.136  1.00 15.41 ?  84  SER   A HG   1 
ATOM   1629 N N    . GLY   A 1 85  ? 30.399 1.154   12.888  1.00 11.69 ?  85  GLY   A N    1 
ATOM   1630 C CA   . GLY   A 1 85  ? 28.979 1.405   12.986  1.00 12.35 ?  85  GLY   A CA   1 
ATOM   1631 C C    . GLY   A 1 85  ? 28.625 2.716   13.644  1.00 11.96 ?  85  GLY   A C    1 
ATOM   1632 O O    . GLY   A 1 85  ? 27.438 3.032   13.774  1.00 12.65 ?  85  GLY   A O    1 
ATOM   1633 H H    . GLY   A 1 85  ? 30.733 0.723   13.557  1.00 14.02 ?  85  GLY   A H    1 
ATOM   1634 H HA2  . GLY   A 1 85  ? 28.601 1.398   12.095  1.00 14.81 ?  85  GLY   A HA2  1 
ATOM   1635 H HA3  . GLY   A 1 85  ? 28.572 0.689   13.494  1.00 14.81 ?  85  GLY   A HA3  1 
ATOM   1636 N N    . HIS   A 1 86  ? 29.621 3.483   14.076  1.00 11.57 ?  86  HIS   A N    1 
ATOM   1637 C CA   . HIS   A 1 86  ? 29.406 4.811   14.657  1.00 12.19 ?  86  HIS   A CA   1 
ATOM   1638 C C    . HIS   A 1 86  ? 28.430 4.684   15.820  1.00 13.11 ?  86  HIS   A C    1 
ATOM   1639 O O    . HIS   A 1 86  ? 28.603 3.790   16.664  1.00 14.18 ?  86  HIS   A O    1 
ATOM   1640 C CB   . HIS   A 1 86  ? 29.027 5.805   13.565  1.00 12.21 ?  86  HIS   A CB   1 
ATOM   1641 C CG   . HIS   A 1 86  ? 30.074 5.900   12.517  1.00 12.14 ?  86  HIS   A CG   1 
ATOM   1642 N ND1  . HIS   A 1 86  ? 31.175 6.718   12.648  1.00 13.40 ?  86  HIS   A ND1  1 
ATOM   1643 C CD2  . HIS   A 1 86  ? 30.242 5.212   11.366  1.00 11.83 ?  86  HIS   A CD2  1 
ATOM   1644 C CE1  . HIS   A 1 86  ? 31.960 6.552   11.598  1.00 13.01 ?  86  HIS   A CE1  1 
ATOM   1645 N NE2  . HIS   A 1 86  ? 31.425 5.634   10.815  1.00 11.97 ?  86  HIS   A NE2  1 
ATOM   1646 H H    . HIS   A 1 86  ? 30.446 3.255   14.052  1.00 13.88 ?  86  HIS   A H    1 
ATOM   1647 H HA   . HIS   A 1 86  ? 30.248 5.117   15.026  1.00 14.62 ?  86  HIS   A HA   1 
ATOM   1648 H HB2  . HIS   A 1 86  ? 28.199 5.529   13.143  1.00 14.65 ?  86  HIS   A HB2  1 
ATOM   1649 H HB3  . HIS   A 1 86  ? 28.918 6.692   13.956  1.00 14.65 ?  86  HIS   A HB3  1 
ATOM   1650 H HD2  . HIS   A 1 86  ? 29.671 4.559   11.019  1.00 14.18 ?  86  HIS   A HD2  1 
ATOM   1651 H HE1  . HIS   A 1 86  ? 32.756 7.005   11.427  1.00 15.61 ?  86  HIS   A HE1  1 
ATOM   1652 H HE2  . HIS   A 1 86  ? 31.752 5.359   10.060  1.00 14.35 ?  86  HIS   A HE2  1 
ATOM   1653 N N    . ASN   A 1 87  ? 27.432 5.545   15.910  1.00 13.92 ?  87  ASN   A N    1 
ATOM   1654 C CA   . ASN   A 1 87  ? 26.462 5.525   16.988  1.00 15.04 ?  87  ASN   A CA   1 
ATOM   1655 C C    . ASN   A 1 87  ? 25.334 4.534   16.754  1.00 15.92 ?  87  ASN   A C    1 
ATOM   1656 O O    . ASN   A 1 87  ? 24.431 4.452   17.592  1.00 18.25 ?  87  ASN   A O    1 
ATOM   1657 C CB   . ASN   A 1 87  ? 25.866 6.927   17.151  1.00 15.84 ?  87  ASN   A CB   1 
ATOM   1658 C CG   . ASN   A 1 87  ? 25.364 7.508   15.835  1.00 16.55 ?  87  ASN   A CG   1 
ATOM   1659 O OD1  . ASN   A 1 87  ? 26.025 7.414   14.804  1.00 17.37 ?  87  ASN   A OD1  1 
ATOM   1660 N ND2  . ASN   A 1 87  ? 24.193 8.110   15.869  1.00 17.62 ?  87  ASN   A ND2  1 
ATOM   1661 H H    . ASN   A 1 87  ? 27.286 6.166   15.339  1.00 16.70 ?  87  ASN   A H    1 
ATOM   1662 H HA   . ASN   A 1 87  ? 26.901 5.280   17.820  1.00 18.04 ?  87  ASN   A HA   1 
ATOM   1663 H HB2  . ASN   A 1 87  ? 25.114 6.880   17.769  1.00 19.00 ?  87  ASN   A HB2  1 
ATOM   1664 H HB3  . ASN   A 1 87  ? 26.546 7.517   17.506  1.00 19.00 ?  87  ASN   A HB3  1 
ATOM   1665 H HD21 . ASN   A 1 87  ? 23.871 8.449   15.151  1.00 21.14 ?  87  ASN   A HD21 1 
ATOM   1666 H HD22 . ASN   A 1 87  ? 23.759 8.164   16.608  1.00 21.14 ?  87  ASN   A HD22 1 
ATOM   1667 N N    A LEU   A 1 88  ? 25.364 3.781   15.655  0.40 15.22 ?  88  LEU   A N    1 
ATOM   1668 N N    B LEU   A 1 88  ? 25.364 3.776   15.660  0.60 15.01 ?  88  LEU   A N    1 
ATOM   1669 C CA   A LEU   A 1 88  ? 24.252 2.921   15.264  0.40 15.05 ?  88  LEU   A CA   1 
ATOM   1670 C CA   B LEU   A 1 88  ? 24.243 2.919   15.285  0.60 14.85 ?  88  LEU   A CA   1 
ATOM   1671 C C    A LEU   A 1 88  ? 24.471 1.450   15.589  0.40 14.74 ?  88  LEU   A C    1 
ATOM   1672 C C    B LEU   A 1 88  ? 24.468 1.441   15.571  0.60 14.79 ?  88  LEU   A C    1 
ATOM   1673 O O    A LEU   A 1 88  ? 23.499 0.734   15.850  0.40 15.57 ?  88  LEU   A O    1 
ATOM   1674 O O    B LEU   A 1 88  ? 23.494 0.708   15.773  0.60 15.94 ?  88  LEU   A O    1 
ATOM   1675 C CB   A LEU   A 1 88  ? 24.001 3.049   13.757  0.40 15.63 ?  88  LEU   A CB   1 
ATOM   1676 C CB   B LEU   A 1 88  ? 23.942 3.088   13.793  0.60 15.44 ?  88  LEU   A CB   1 
ATOM   1677 C CG   A LEU   A 1 88  ? 23.705 4.447   13.209  0.40 16.79 ?  88  LEU   A CG   1 
ATOM   1678 C CG   B LEU   A 1 88  ? 23.613 4.515   13.351  0.60 16.70 ?  88  LEU   A CG   1 
ATOM   1679 C CD1  A LEU   A 1 88  ? 23.583 4.394   11.697  0.40 17.18 ?  88  LEU   A CD1  1 
ATOM   1680 C CD1  B LEU   A 1 88  ? 23.387 4.564   11.850  0.60 16.63 ?  88  LEU   A CD1  1 
ATOM   1681 C CD2  A LEU   A 1 88  ? 22.438 5.014   13.828  0.40 17.58 ?  88  LEU   A CD2  1 
ATOM   1682 C CD2  B LEU   A 1 88  ? 22.397 5.043   14.098  0.60 17.95 ?  88  LEU   A CD2  1 
ATOM   1683 H H    A LEU   A 1 88  ? 26.034 3.747   15.115  0.40 18.26 ?  88  LEU   A H    1 
ATOM   1684 H H    B LEU   A 1 88  ? 26.029 3.741   15.115  0.60 18.01 ?  88  LEU   A H    1 
ATOM   1685 H HA   A LEU   A 1 88  ? 23.451 3.209   15.724  0.40 18.05 ?  88  LEU   A HA   1 
ATOM   1686 H HA   B LEU   A 1 88  ? 23.458 3.200   15.778  0.60 17.81 ?  88  LEU   A HA   1 
ATOM   1687 H HB2  A LEU   A 1 88  ? 24.786 2.727   13.290  0.40 18.75 ?  88  LEU   A HB2  1 
ATOM   1688 H HB2  B LEU   A 1 88  ? 24.716 2.798   13.286  0.60 18.52 ?  88  LEU   A HB2  1 
ATOM   1689 H HB3  A LEU   A 1 88  ? 23.242 2.492   13.529  0.40 18.75 ?  88  LEU   A HB3  1 
ATOM   1690 H HB3  B LEU   A 1 88  ? 23.180 2.531   13.569  0.60 18.52 ?  88  LEU   A HB3  1 
ATOM   1691 H HG   A LEU   A 1 88  ? 24.439 5.040   13.429  0.40 20.14 ?  88  LEU   A HG   1 
ATOM   1692 H HG   B LEU   A 1 88  ? 24.364 5.091   13.556  0.60 20.04 ?  88  LEU   A HG   1 
ATOM   1693 H HD11 A LEU   A 1 88  ? 23.427 5.290   11.359  0.40 20.61 ?  88  LEU   A HD11 1 
ATOM   1694 H HD11 B LEU   A 1 88  ? 23.183 5.476   11.589  0.60 19.95 ?  88  LEU   A HD11 1 
ATOM   1695 H HD12 A LEU   A 1 88  ? 24.405 4.038   11.326  0.40 20.61 ?  88  LEU   A HD12 1 
ATOM   1696 H HD12 B LEU   A 1 88  ? 24.193 4.265   11.398  0.60 19.95 ?  88  LEU   A HD12 1 
ATOM   1697 H HD13 A LEU   A 1 88  ? 22.837 3.819   11.462  0.40 20.61 ?  88  LEU   A HD13 1 
ATOM   1698 H HD13 B LEU   A 1 88  ? 22.645 3.981   11.621  0.60 19.95 ?  88  LEU   A HD13 1 
ATOM   1699 H HD21 A LEU   A 1 88  ? 22.239 5.868   13.414  0.40 21.08 ?  88  LEU   A HD21 1 
ATOM   1700 H HD21 B LEU   A 1 88  ? 22.118 5.879   13.693  0.60 21.53 ?  88  LEU   A HD21 1 
ATOM   1701 H HD22 A LEU   A 1 88  ? 21.708 4.394   13.676  0.40 21.08 ?  88  LEU   A HD22 1 
ATOM   1702 H HD22 B LEU   A 1 88  ? 21.683 4.391   14.037  0.60 21.53 ?  88  LEU   A HD22 1 
ATOM   1703 H HD23 A LEU   A 1 88  ? 22.579 5.133   14.780  0.40 21.08 ?  88  LEU   A HD23 1 
ATOM   1704 H HD23 B LEU   A 1 88  ? 22.637 5.187   15.026  0.60 21.53 ?  88  LEU   A HD23 1 
ATOM   1705 N N    . ALA   A 1 89  ? 25.718 0.990   15.579  1.00 13.88 ?  89  ALA   A N    1 
ATOM   1706 C CA   . ALA   A 1 89  ? 26.049 -0.423  15.693  1.00 13.36 ?  89  ALA   A CA   1 
ATOM   1707 C C    . ALA   A 1 89  ? 27.536 -0.494  15.993  1.00 13.82 ?  89  ALA   A C    1 
ATOM   1708 O O    . ALA   A 1 89  ? 28.252 0.499   15.858  1.00 14.42 ?  89  ALA   A O    1 
ATOM   1709 C CB   . ALA   A 1 89  ? 25.749 -1.144  14.380  1.00 12.91 ?  89  ALA   A CB   1 
ATOM   1710 H H    A ALA   A 1 89  ? 26.411 1.498   15.501  0.40 16.64 ?  89  ALA   A H    1 
ATOM   1711 H H    B ALA   A 1 89  ? 26.410 1.499   15.502  0.60 16.64 ?  89  ALA   A H    1 
ATOM   1712 H HA   . ALA   A 1 89  ? 25.550 -0.830  16.418  1.00 16.02 ?  89  ALA   A HA   1 
ATOM   1713 H HB1  . ALA   A 1 89  ? 25.996 -2.079  14.472  1.00 15.49 ?  89  ALA   A HB1  1 
ATOM   1714 H HB2  . ALA   A 1 89  ? 24.800 -1.072  14.189  1.00 15.49 ?  89  ALA   A HB2  1 
ATOM   1715 H HB3  . ALA   A 1 89  ? 26.263 -0.735  13.669  1.00 15.49 ?  89  ALA   A HB3  1 
ATOM   1716 N N    . LYS   A 1 90  ? 28.011 -1.674  16.384  1.00 14.33 ?  90  LYS   A N    1 
ATOM   1717 C CA   . LYS   A 1 90  ? 29.455 -1.834  16.518  1.00 15.08 ?  90  LYS   A CA   1 
ATOM   1718 C C    . LYS   A 1 90  ? 30.142 -1.640  15.168  1.00 14.03 ?  90  LYS   A C    1 
ATOM   1719 O O    . LYS   A 1 90  ? 31.071 -0.827  15.037  1.00 14.94 ?  90  LYS   A O    1 
ATOM   1720 C CB   . LYS   A 1 90  ? 29.790 -3.198  17.124  1.00 17.32 ?  90  LYS   A CB   1 
ATOM   1721 C CG   . LYS   A 1 90  ? 31.258 -3.342  17.491  1.00 21.37 ?  90  LYS   A CG   1 
ATOM   1722 C CD   . LYS   A 1 90  ? 31.499 -4.593  18.318  1.00 24.84 ?  90  LYS   A CD   1 
ATOM   1723 C CE   . LYS   A 1 90  ? 32.914 -4.634  18.874  1.00 27.05 ?  90  LYS   A CE   1 
ATOM   1724 N NZ   . LYS   A 1 90  ? 33.930 -4.873  17.816  1.00 28.91 ?  90  LYS   A NZ   1 
ATOM   1725 H H    . LYS   A 1 90  ? 27.540 -2.365  16.573  1.00 17.19 ?  90  LYS   A H    1 
ATOM   1726 H HA   . LYS   A 1 90  ? 29.792 -1.154  17.121  1.00 18.09 ?  90  LYS   A HA   1 
ATOM   1727 H HB2  . LYS   A 1 90  ? 29.265 -3.324  17.932  1.00 20.77 ?  90  LYS   A HB2  1 
ATOM   1728 H HB3  . LYS   A 1 90  ? 29.573 -3.893  16.481  1.00 20.77 ?  90  LYS   A HB3  1 
ATOM   1729 H HG2  . LYS   A 1 90  ? 31.787 -3.406  16.681  1.00 25.64 ?  90  LYS   A HG2  1 
ATOM   1730 H HG3  . LYS   A 1 90  ? 31.534 -2.574  18.015  1.00 25.64 ?  90  LYS   A HG3  1 
ATOM   1731 H HD2  . LYS   A 1 90  ? 30.879 -4.612  19.065  1.00 29.80 ?  90  LYS   A HD2  1 
ATOM   1732 H HD3  . LYS   A 1 90  ? 31.371 -5.378  17.760  1.00 29.80 ?  90  LYS   A HD3  1 
ATOM   1733 H HE2  . LYS   A 1 90  ? 33.113 -3.783  19.296  1.00 32.45 ?  90  LYS   A HE2  1 
ATOM   1734 H HE3  . LYS   A 1 90  ? 32.980 -5.351  19.525  1.00 32.45 ?  90  LYS   A HE3  1 
ATOM   1735 H HZ1  . LYS   A 1 90  ? 34.744 -4.899  18.177  1.00 34.69 ?  90  LYS   A HZ1  1 
ATOM   1736 H HZ2  . LYS   A 1 90  ? 33.770 -5.650  17.411  1.00 34.69 ?  90  LYS   A HZ2  1 
ATOM   1737 H HZ3  . LYS   A 1 90  ? 33.902 -4.220  17.214  1.00 34.69 ?  90  LYS   A HZ3  1 
ATOM   1738 N N    . HIS   A 1 91  ? 29.671 -2.360  14.150  1.00 12.48 ?  91  HIS   A N    1 
ATOM   1739 C CA   . HIS   A 1 91  ? 30.245 -2.341  12.819  1.00 11.79 ?  91  HIS   A CA   1 
ATOM   1740 C C    . HIS   A 1 91  ? 29.159 -2.059  11.798  1.00 10.75 ?  91  HIS   A C    1 
ATOM   1741 O O    . HIS   A 1 91  ? 27.989 -2.403  11.998  1.00 11.20 ?  91  HIS   A O    1 
ATOM   1742 C CB   . HIS   A 1 91  ? 30.828 -3.713  12.456  1.00 14.10 ?  91  HIS   A CB   1 
ATOM   1743 C CG   . HIS   A 1 91  ? 31.813 -4.243  13.449  1.00 18.34 ?  91  HIS   A CG   1 
ATOM   1744 N ND1  . HIS   A 1 91  ? 33.092 -3.744  13.567  1.00 20.54 ?  91  HIS   A ND1  1 
ATOM   1745 C CD2  . HIS   A 1 91  ? 31.714 -5.241  14.359  1.00 19.92 ?  91  HIS   A CD2  1 
ATOM   1746 C CE1  . HIS   A 1 91  ? 33.735 -4.406  14.513  1.00 21.58 ?  91  HIS   A CE1  1 
ATOM   1747 N NE2  . HIS   A 1 91  ? 32.922 -5.323  15.007  1.00 21.40 ?  91  HIS   A NE2  1 
ATOM   1748 H H    . HIS   A 1 91  ? 28.992 -2.894  14.222  1.00 14.97 ?  91  HIS   A H    1 
ATOM   1749 H HA   . HIS   A 1 91  ? 30.935 -1.670  12.758  1.00 14.14 ?  91  HIS   A HA   1 
ATOM   1750 H HB2  . HIS   A 1 91  ? 30.099 -4.355  12.393  1.00 16.91 ?  91  HIS   A HB2  1 
ATOM   1751 H HB3  . HIS   A 1 91  ? 31.274 -3.643  11.599  1.00 16.91 ?  91  HIS   A HB3  1 
ATOM   1752 H HD1  . HIS   A 1 91  ? 33.417 -3.098  13.096  1.00 24.64 ?  91  HIS   A HD1  1 
ATOM   1753 H HD2  . HIS   A 1 91  ? 30.970 -5.772  14.517  1.00 23.89 ?  91  HIS   A HD2  1 
ATOM   1754 H HE1  . HIS   A 1 91  ? 34.614 -4.249  14.778  1.00 25.89 ?  91  HIS   A HE1  1 
ATOM   1755 N N    . CYS   A 1 92  ? 29.566 -1.470  10.679  1.00 10.49 ?  92  CYS   A N    1 
ATOM   1756 C CA   . CYS   A 1 92  ? 28.726 -1.387  9.493   1.00 10.17 ?  92  CYS   A CA   1 
ATOM   1757 C C    . CYS   A 1 92  ? 29.368 -2.206  8.380   1.00 9.85  ?  92  CYS   A C    1 
ATOM   1758 O O    . CYS   A 1 92  ? 30.524 -1.958  8.007   1.00 10.16 ?  92  CYS   A O    1 
ATOM   1759 C CB   . CYS   A 1 92  ? 28.513 0.055   9.030   1.00 10.52 ?  92  CYS   A CB   1 
ATOM   1760 S SG   . CYS   A 1 92  ? 27.494 0.164   7.519   1.00 10.18 ?  92  CYS   A SG   1 
ATOM   1761 H H    . CYS   A 1 92  ? 30.338 -1.100  10.582  1.00 12.58 ?  92  CYS   A H    1 
ATOM   1762 H HA   . CYS   A 1 92  ? 27.859 -1.770  9.689   1.00 12.20 ?  92  CYS   A HA   1 
ATOM   1763 H HB2  . CYS   A 1 92  ? 28.058 0.551   9.732   1.00 12.61 ?  92  CYS   A HB2  1 
ATOM   1764 H HB3  . CYS   A 1 92  ? 29.371 0.462   8.841   1.00 12.61 ?  92  CYS   A HB3  1 
ATOM   1765 H HG   . CYS   A 1 92  ? 27.355 1.317   7.226   1.00 12.20 ?  92  CYS   A HG   1 
ATOM   1766 N N    . LEU   A 1 93  ? 28.628 -3.187  7.871   1.00 9.63  ?  93  LEU   A N    1 
ATOM   1767 C CA   . LEU   A 1 93  ? 29.026 -3.946  6.690   1.00 9.26  ?  93  LEU   A CA   1 
ATOM   1768 C C    . LEU   A 1 93  ? 28.428 -3.249  5.472   1.00 8.74  ?  93  LEU   A C    1 
ATOM   1769 O O    . LEU   A 1 93  ? 27.209 -3.299  5.257   1.00 9.05  ?  93  LEU   A O    1 
ATOM   1770 C CB   . LEU   A 1 93  ? 28.537 -5.387  6.794   1.00 9.79  ?  93  LEU   A CB   1 
ATOM   1771 C CG   . LEU   A 1 93  ? 28.925 -6.290  5.624   1.00 10.05 ?  93  LEU   A CG   1 
ATOM   1772 C CD1  . LEU   A 1 93  ? 30.425 -6.551  5.603   1.00 10.86 ?  93  LEU   A CD1  1 
ATOM   1773 C CD2  . LEU   A 1 93  ? 28.142 -7.607  5.654   1.00 10.66 ?  93  LEU   A CD2  1 
ATOM   1774 H H    . LEU   A 1 93  ? 27.869 -3.427  8.199   1.00 11.55 ?  93  LEU   A H    1 
ATOM   1775 H HA   . LEU   A 1 93  ? 29.988 -3.939  6.613   1.00 11.11 ?  93  LEU   A HA   1 
ATOM   1776 H HB2  . LEU   A 1 93  ? 28.907 -5.771  7.605   1.00 11.74 ?  93  LEU   A HB2  1 
ATOM   1777 H HB3  . LEU   A 1 93  ? 27.570 -5.378  6.852   1.00 11.74 ?  93  LEU   A HB3  1 
ATOM   1778 H HG   . LEU   A 1 93  ? 28.704 -5.840  4.801   1.00 12.05 ?  93  LEU   A HG   1 
ATOM   1779 H HD11 . LEU   A 1 93  ? 30.636 -7.165  4.882   1.00 13.02 ?  93  LEU   A HD11 1 
ATOM   1780 H HD12 . LEU   A 1 93  ? 30.900 -5.714  5.471   1.00 13.02 ?  93  LEU   A HD12 1 
ATOM   1781 H HD13 . LEU   A 1 93  ? 30.698 -6.947  6.454   1.00 13.02 ?  93  LEU   A HD13 1 
ATOM   1782 H HD21 . LEU   A 1 93  ? 28.421 -8.154  4.899   1.00 12.78 ?  93  LEU   A HD21 1 
ATOM   1783 H HD22 . LEU   A 1 93  ? 28.332 -8.073  6.483   1.00 12.78 ?  93  LEU   A HD22 1 
ATOM   1784 H HD23 . LEU   A 1 93  ? 27.196 -7.413  5.589   1.00 12.78 ?  93  LEU   A HD23 1 
ATOM   1785 N N    . HIS   A 1 94  ? 29.280 -2.561  4.705   1.00 8.64  ?  94  HIS   A N    1 
ATOM   1786 C CA   . HIS   A 1 94  ? 28.857 -1.884  3.480   1.00 8.71  ?  94  HIS   A CA   1 
ATOM   1787 C C    . HIS   A 1 94  ? 28.859 -2.913  2.363   1.00 8.68  ?  94  HIS   A C    1 
ATOM   1788 O O    . HIS   A 1 94  ? 29.918 -3.429  2.010   1.00 10.13 ?  94  HIS   A O    1 
ATOM   1789 C CB   . HIS   A 1 94  ? 29.814 -0.739  3.149   1.00 8.68  ?  94  HIS   A CB   1 
ATOM   1790 C CG   . HIS   A 1 94  ? 29.804 0.351   4.169   1.00 8.74  ?  94  HIS   A CG   1 
ATOM   1791 N ND1  . HIS   A 1 94  ? 28.932 1.417   4.116   1.00 8.88  ?  94  HIS   A ND1  1 
ATOM   1792 C CD2  . HIS   A 1 94  ? 30.550 0.519   5.286   1.00 9.22  ?  94  HIS   A CD2  1 
ATOM   1793 C CE1  . HIS   A 1 94  ? 29.145 2.193   5.163   1.00 9.33  ?  94  HIS   A CE1  1 
ATOM   1794 N NE2  . HIS   A 1 94  ? 30.120 1.670   5.889   1.00 9.62  ?  94  HIS   A NE2  1 
ATOM   1795 H H    . HIS   A 1 94  ? 30.121 -2.472  4.870   1.00 10.36 ?  94  HIS   A H    1 
ATOM   1796 H HA   . HIS   A 1 94  ? 27.957 -1.532  3.587   1.00 10.45 ?  94  HIS   A HA   1 
ATOM   1797 H HB2  . HIS   A 1 94  ? 30.712 -1.091  3.093   1.00 10.40 ?  94  HIS   A HB2  1 
ATOM   1798 H HB3  . HIS   A 1 94  ? 29.552 -0.351  2.299   1.00 10.40 ?  94  HIS   A HB3  1 
ATOM   1799 H HD2  . HIS   A 1 94  ? 31.224 -0.041  5.593   1.00 11.06 ?  94  HIS   A HD2  1 
ATOM   1800 H HE1  . HIS   A 1 94  ? 28.679 2.977   5.356   1.00 11.19 ?  94  HIS   A HE1  1 
ATOM   1801 H HE2  . HIS   A 1 94  ? 30.434 2.012   6.613   1.00 11.54 ?  94  HIS   A HE2  1 
ATOM   1802 N N    . VAL   A 1 95  ? 27.682 -3.237  1.822   1.00 8.07  ?  95  VAL   A N    1 
ATOM   1803 C CA   . VAL   A 1 95  ? 27.538 -4.270  0.800   1.00 8.56  ?  95  VAL   A CA   1 
ATOM   1804 C C    . VAL   A 1 95  ? 26.994 -3.628  -0.465  1.00 7.95  ?  95  VAL   A C    1 
ATOM   1805 O O    . VAL   A 1 95  ? 25.996 -2.899  -0.406  1.00 9.04  ?  95  VAL   A O    1 
ATOM   1806 C CB   . VAL   A 1 95  ? 26.601 -5.402  1.260   1.00 9.02  ?  95  VAL   A CB   1 
ATOM   1807 C CG1  . VAL   A 1 95  ? 26.466 -6.446  0.161   1.00 10.10 ?  95  VAL   A CG1  1 
ATOM   1808 C CG2  . VAL   A 1 95  ? 27.109 -6.033  2.546   1.00 9.42  ?  95  VAL   A CG2  1 
ATOM   1809 H H    . VAL   A 1 95  ? 26.935 -2.864  2.036   1.00 9.68  ?  95  VAL   A H    1 
ATOM   1810 H HA   . VAL   A 1 95  ? 28.403 -4.654  0.598   1.00 10.26 ?  95  VAL   A HA   1 
ATOM   1811 H HB   . VAL   A 1 95  ? 25.722 -5.036  1.436   1.00 10.82 ?  95  VAL   A HB   1 
ATOM   1812 H HG11 . VAL   A 1 95  ? 26.063 -7.251  0.534   1.00 12.12 ?  95  VAL   A HG11 1 
ATOM   1813 H HG12 . VAL   A 1 95  ? 25.901 -6.100  -0.547  1.00 12.12 ?  95  VAL   A HG12 1 
ATOM   1814 H HG13 . VAL   A 1 95  ? 27.346 -6.659  -0.190  1.00 12.12 ?  95  VAL   A HG13 1 
ATOM   1815 H HG21 . VAL   A 1 95  ? 26.544 -6.785  2.775   1.00 11.30 ?  95  VAL   A HG21 1 
ATOM   1816 H HG22 . VAL   A 1 95  ? 28.023 -6.331  2.411   1.00 11.30 ?  95  VAL   A HG22 1 
ATOM   1817 H HG23 . VAL   A 1 95  ? 27.080 -5.368  3.253   1.00 11.30 ?  95  VAL   A HG23 1 
ATOM   1818 N N    . VAL   A 1 96  ? 27.614 -3.923  -1.604  1.00 8.42  ?  96  VAL   A N    1 
ATOM   1819 C CA   . VAL   A 1 96  ? 27.202 -3.366  -2.885  1.00 8.81  ?  96  VAL   A CA   1 
ATOM   1820 C C    . VAL   A 1 96  ? 26.389 -4.407  -3.648  1.00 9.11  ?  96  VAL   A C    1 
ATOM   1821 O O    . VAL   A 1 96  ? 26.939 -5.352  -4.223  1.00 10.09 ?  96  VAL   A O    1 
ATOM   1822 C CB   . VAL   A 1 96  ? 28.394 -2.888  -3.715  1.00 9.26  ?  96  VAL   A CB   1 
ATOM   1823 C CG1  . VAL   A 1 96  ? 27.890 -2.252  -4.990  1.00 9.66  ?  96  VAL   A CG1  1 
ATOM   1824 C CG2  . VAL   A 1 96  ? 29.256 -1.914  -2.923  1.00 9.88  ?  96  VAL   A CG2  1 
ATOM   1825 H H    . VAL   A 1 96  ? 28.299 -4.447  -1.659  1.00 10.10 ?  96  VAL   A H    1 
ATOM   1826 H HA   . VAL   A 1 96  ? 26.633 -2.599  -2.726  1.00 10.56 ?  96  VAL   A HA   1 
ATOM   1827 H HB   . VAL   A 1 96  ? 28.944 -3.645  -3.956  1.00 11.11 ?  96  VAL   A HB   1 
ATOM   1828 H HG11 . VAL   A 1 96  ? 28.623 -1.767  -5.411  1.00 11.58 ?  96  VAL   A HG11 1 
ATOM   1829 H HG12 . VAL   A 1 96  ? 27.571 -2.942  -5.587  1.00 11.58 ?  96  VAL   A HG12 1 
ATOM   1830 H HG13 . VAL   A 1 96  ? 27.174 -1.633  -4.776  1.00 11.58 ?  96  VAL   A HG13 1 
ATOM   1831 H HG21 . VAL   A 1 96  ? 29.963 -1.572  -3.494  1.00 11.84 ?  96  VAL   A HG21 1 
ATOM   1832 H HG22 . VAL   A 1 96  ? 28.703 -1.177  -2.610  1.00 11.84 ?  96  VAL   A HG22 1 
ATOM   1833 H HG23 . VAL   A 1 96  ? 29.644 -2.377  -2.162  1.00 11.84 ?  96  VAL   A HG23 1 
ATOM   1834 N N    A GLY   A 1 97  ? 25.071 -4.241  -3.663  0.40 9.36  ?  97  GLY   A N    1 
ATOM   1835 N N    B GLY   A 1 97  ? 25.072 -4.242  -3.670  0.60 9.36  ?  97  GLY   A N    1 
ATOM   1836 C CA   A GLY   A 1 97  ? 24.242 -4.981  -4.578  0.40 9.98  ?  97  GLY   A CA   1 
ATOM   1837 C CA   B GLY   A 1 97  ? 24.249 -4.991  -4.584  0.60 10.20 ?  97  GLY   A CA   1 
ATOM   1838 C C    A GLY   A 1 97  ? 24.252 -4.318  -5.942  0.40 9.98  ?  97  GLY   A C    1 
ATOM   1839 C C    B GLY   A 1 97  ? 24.224 -4.317  -5.943  0.60 10.19 ?  97  GLY   A C    1 
ATOM   1840 O O    A GLY   A 1 97  ? 24.553 -3.127  -6.072  0.40 10.57 ?  97  GLY   A O    1 
ATOM   1841 O O    B GLY   A 1 97  ? 24.496 -3.119  -6.072  0.60 11.00 ?  97  GLY   A O    1 
ATOM   1842 H H    A GLY   A 1 97  ? 24.641 -3.698  -3.149  0.40 11.23 ?  97  GLY   A H    1 
ATOM   1843 H H    B GLY   A 1 97  ? 24.639 -3.693  -3.164  0.60 11.22 ?  97  GLY   A H    1 
ATOM   1844 H HA2  A GLY   A 1 97  ? 24.578 -5.887  -4.655  0.40 11.97 ?  97  GLY   A HA2  1 
ATOM   1845 H HA2  B GLY   A 1 97  ? 24.607 -5.885  -4.679  0.60 12.23 ?  97  GLY   A HA2  1 
ATOM   1846 H HA3  A GLY   A 1 97  ? 23.331 -5.011  -4.245  0.40 11.97 ?  97  GLY   A HA3  1 
ATOM   1847 H HA3  B GLY   A 1 97  ? 23.344 -5.048  -4.238  0.60 12.23 ?  97  GLY   A HA3  1 
ATOM   1848 N N    A PRO   A 1 98  ? 23.927 -5.072  -6.989  0.40 10.24 ?  98  PRO   A N    1 
ATOM   1849 N N    B PRO   A 1 98  ? 23.889 -5.071  -6.987  0.60 10.48 ?  98  PRO   A N    1 
ATOM   1850 C CA   A PRO   A 1 98  ? 23.837 -4.462  -8.321  0.40 11.09 ?  98  PRO   A CA   1 
ATOM   1851 C CA   B PRO   A 1 98  ? 23.765 -4.458  -8.315  0.60 11.47 ?  98  PRO   A CA   1 
ATOM   1852 C C    A PRO   A 1 98  ? 22.714 -3.435  -8.390  0.40 11.24 ?  98  PRO   A C    1 
ATOM   1853 C C    B PRO   A 1 98  ? 22.639 -3.433  -8.358  0.60 11.09 ?  98  PRO   A C    1 
ATOM   1854 O O    A PRO   A 1 98  ? 21.634 -3.624  -7.827  0.40 11.46 ?  98  PRO   A O    1 
ATOM   1855 O O    B PRO   A 1 98  ? 21.561 -3.635  -7.794  0.60 11.30 ?  98  PRO   A O    1 
ATOM   1856 C CB   A PRO   A 1 98  ? 23.558 -5.658  -9.238  0.40 11.38 ?  98  PRO   A CB   1 
ATOM   1857 C CB   B PRO   A 1 98  ? 23.468 -5.654  -9.226  0.60 11.93 ?  98  PRO   A CB   1 
ATOM   1858 C CG   A PRO   A 1 98  ? 22.926 -6.681  -8.344  0.40 11.14 ?  98  PRO   A CG   1 
ATOM   1859 C CG   B PRO   A 1 98  ? 22.826 -6.665  -8.321  0.60 11.63 ?  98  PRO   A CG   1 
ATOM   1860 C CD   A PRO   A 1 98  ? 23.625 -6.515  -7.021  0.40 10.51 ?  98  PRO   A CD   1 
ATOM   1861 C CD   B PRO   A 1 98  ? 23.550 -6.507  -7.004  0.60 10.82 ?  98  PRO   A CD   1 
ATOM   1862 H HA   A PRO   A 1 98  ? 24.682 -4.049  -8.562  0.40 13.29 ?  98  PRO   A HA   1 
ATOM   1863 H HA   B PRO   A 1 98  ? 24.601 -4.041  -8.576  0.60 13.76 ?  98  PRO   A HA   1 
ATOM   1864 H HB2  A PRO   A 1 98  ? 22.946 -5.390  -9.942  0.40 13.64 ?  98  PRO   A HB2  1 
ATOM   1865 H HB2  B PRO   A 1 98  ? 22.859 -5.384  -9.931  0.60 14.30 ?  98  PRO   A HB2  1 
ATOM   1866 H HB3  A PRO   A 1 98  ? 24.388 -5.990  -9.606  0.40 13.64 ?  98  PRO   A HB3  1 
ATOM   1867 H HB3  B PRO   A 1 98  ? 24.296 -5.997  -9.595  0.60 14.30 ?  98  PRO   A HB3  1 
ATOM   1868 H HG2  A PRO   A 1 98  ? 21.975 -6.496  -8.257  0.40 13.36 ?  98  PRO   A HG2  1 
ATOM   1869 H HG2  B PRO   A 1 98  ? 21.881 -6.461  -8.222  0.60 13.95 ?  98  PRO   A HG2  1 
ATOM   1870 H HG3  A PRO   A 1 98  ? 23.073 -7.566  -8.705  0.40 13.36 ?  98  PRO   A HG3  1 
ATOM   1871 H HG3  B PRO   A 1 98  ? 22.953 -7.554  -8.681  0.60 13.95 ?  98  PRO   A HG3  1 
ATOM   1872 H HD2  A PRO   A 1 98  ? 23.033 -6.758  -6.290  0.40 12.60 ?  98  PRO   A HD2  1 
ATOM   1873 H HD2  B PRO   A 1 98  ? 22.961 -6.730  -6.264  0.60 12.97 ?  98  PRO   A HD2  1 
ATOM   1874 H HD3  A PRO   A 1 98  ? 24.446 -7.031  -7.002  0.40 12.60 ?  98  PRO   A HD3  1 
ATOM   1875 H HD3  B PRO   A 1 98  ? 24.358 -7.040  -6.992  0.60 12.97 ?  98  PRO   A HD3  1 
ATOM   1876 N N    A ASN   A 1 99  ? 22.982 -2.334  -9.094  0.40 12.08 ?  99  ASN   A N    1 
ATOM   1877 N N    B ASN   A 1 99  ? 22.902 -2.316  -9.035  0.60 12.27 ?  99  ASN   A N    1 
ATOM   1878 C CA   A ASN   A 1 99  ? 22.008 -1.261  -9.294  0.40 12.89 ?  99  ASN   A CA   1 
ATOM   1879 C CA   B ASN   A 1 99  ? 21.912 -1.266  -9.254  0.60 13.05 ?  99  ASN   A CA   1 
ATOM   1880 C C    A ASN   A 1 99  ? 21.454 -1.396  -10.708 0.40 13.47 ?  99  ASN   A C    1 
ATOM   1881 C C    B ASN   A 1 99  ? 21.388 -1.430  -10.677 0.60 14.25 ?  99  ASN   A C    1 
ATOM   1882 O O    A ASN   A 1 99  ? 22.087 -0.971  -11.681 0.40 13.93 ?  99  ASN   A O    1 
ATOM   1883 O O    B ASN   A 1 99  ? 22.137 -1.264  -11.647 0.60 15.68 ?  99  ASN   A O    1 
ATOM   1884 C CB   A ASN   A 1 99  ? 22.659 0.102   -9.075  0.40 13.55 ?  99  ASN   A CB   1 
ATOM   1885 C CB   B ASN   A 1 99  ? 22.535 0.114   -9.029  0.60 13.26 ?  99  ASN   A CB   1 
ATOM   1886 C CG   A ASN   A 1 99  ? 21.654 1.249   -9.092  0.40 13.64 ?  99  ASN   A CG   1 
ATOM   1887 C CG   B ASN   A 1 99  ? 21.503 1.245   -9.028  0.60 12.98 ?  99  ASN   A CG   1 
ATOM   1888 O OD1  A ASN   A 1 99  ? 20.652 1.201   -9.804  0.40 14.29 ?  99  ASN   A OD1  1 
ATOM   1889 O OD1  B ASN   A 1 99  ? 20.545 1.229   -9.802  0.60 13.78 ?  99  ASN   A OD1  1 
ATOM   1890 N ND2  A ASN   A 1 99  ? 21.927 2.289   -8.307  0.40 14.10 ?  99  ASN   A ND2  1 
ATOM   1891 N ND2  B ASN   A 1 99  ? 21.702 2.229   -8.151  0.60 13.46 ?  99  ASN   A ND2  1 
ATOM   1892 H H    A ASN   A 1 99  ? 23.745 -2.182  -9.463  0.40 14.48 ?  99  ASN   A H    1 
ATOM   1893 H H    B ASN   A 1 99  ? 23.669 -2.136  -9.380  0.60 14.72 ?  99  ASN   A H    1 
ATOM   1894 H HA   A ASN   A 1 99  ? 21.278 -1.364  -8.658  0.40 15.46 ?  99  ASN   A HA   1 
ATOM   1895 H HA   B ASN   A 1 99  ? 21.175 -1.373  -8.629  0.60 15.66 ?  99  ASN   A HA   1 
ATOM   1896 H HB2  A ASN   A 1 99  ? 23.108 0.106   -8.215  0.40 16.25 ?  99  ASN   A HB2  1 
ATOM   1897 H HB2  B ASN   A 1 99  ? 22.992 0.123   -8.170  0.60 15.90 ?  99  ASN   A HB2  1 
ATOM   1898 H HB3  A ASN   A 1 99  ? 23.303 0.256   -9.785  0.40 16.25 ?  99  ASN   A HB3  1 
ATOM   1899 H HB3  B ASN   A 1 99  ? 23.172 0.294   -9.739  0.60 15.90 ?  99  ASN   A HB3  1 
ATOM   1900 H HD21 A ASN   A 1 99  ? 21.393 2.963   -8.280  0.40 16.91 ?  99  ASN   A HD21 1 
ATOM   1901 H HD21 B ASN   A 1 99  ? 21.151 2.887   -8.111  0.60 16.15 ?  99  ASN   A HD21 1 
ATOM   1902 H HD22 A ASN   A 1 99  ? 22.640 2.287   -7.825  0.40 16.91 ?  99  ASN   A HD22 1 
ATOM   1903 H HD22 B ASN   A 1 99  ? 22.385 2.207   -7.626  0.60 16.15 ?  99  ASN   A HD22 1 
ATOM   1904 N N    A VAL   A 1 100 ? 20.257 -1.983  -10.807 0.40 14.34 ?  100 VAL   A N    1 
ATOM   1905 N N    B VAL   A 1 100 ? 20.109 -1.797  -10.791 0.60 14.41 ?  100 VAL   A N    1 
ATOM   1906 C CA   A VAL   A 1 100 ? 19.627 -2.232  -12.101 0.40 16.06 ?  100 VAL   A CA   1 
ATOM   1907 C CA   B VAL   A 1 100 ? 19.489 -1.970  -12.100 0.60 15.52 ?  100 VAL   A CA   1 
ATOM   1908 C C    A VAL   A 1 100 ? 19.529 -0.953  -12.916 0.40 16.72 ?  100 VAL   A C    1 
ATOM   1909 C C    B VAL   A 1 100 ? 19.357 -0.637  -12.823 0.60 14.68 ?  100 VAL   A C    1 
ATOM   1910 O O    A VAL   A 1 100 ? 19.632 -0.983  -14.148 0.40 17.50 ?  100 VAL   A O    1 
ATOM   1911 O O    B VAL   A 1 100 ? 19.424 -0.583  -14.056 0.60 15.64 ?  100 VAL   A O    1 
ATOM   1912 C CB   A VAL   A 1 100 ? 18.247 -2.893  -11.894 0.40 17.41 ?  100 VAL   A CB   1 
ATOM   1913 C CB   B VAL   A 1 100 ? 18.137 -2.696  -11.949 0.60 17.32 ?  100 VAL   A CB   1 
ATOM   1914 C CG1  A VAL   A 1 100 ? 17.524 -3.070  -13.222 0.40 17.79 ?  100 VAL   A CG1  1 
ATOM   1915 C CG1  B VAL   A 1 100 ? 17.433 -2.832  -13.295 0.60 18.12 ?  100 VAL   A CG1  1 
ATOM   1916 C CG2  A VAL   A 1 100 ? 18.405 -4.229  -11.188 0.40 18.15 ?  100 VAL   A CG2  1 
ATOM   1917 C CG2  B VAL   A 1 100 ? 18.348 -4.061  -11.318 0.60 18.04 ?  100 VAL   A CG2  1 
ATOM   1918 H H    A VAL   A 1 100 ? 19.784 -2.237  -10.132 0.40 17.20 ?  100 VAL   A H    1 
ATOM   1919 H H    B VAL   A 1 100 ? 19.585 -1.960  -10.125 0.60 17.28 ?  100 VAL   A H    1 
ATOM   1920 H HA   A VAL   A 1 100 ? 20.176 -2.855  -12.599 0.40 19.27 ?  100 VAL   A HA   1 
ATOM   1921 H HA   B VAL   A 1 100 ? 20.062 -2.530  -12.637 0.60 18.61 ?  100 VAL   A HA   1 
ATOM   1922 H HB   A VAL   A 1 100 ? 17.702 -2.319  -11.333 0.40 20.89 ?  100 VAL   A HB   1 
ATOM   1923 H HB   B VAL   A 1 100 ? 17.561 -2.180  -11.363 0.60 20.78 ?  100 VAL   A HB   1 
ATOM   1924 H HG11 A VAL   A 1 100 ? 16.762 -3.655  -13.090 0.40 21.34 ?  100 VAL   A HG11 1 
ATOM   1925 H HG11 B VAL   A 1 100 ? 16.683 -3.442  -13.198 0.60 21.74 ?  100 VAL   A HG11 1 
ATOM   1926 H HG12 A VAL   A 1 100 ? 17.223 -2.204  -13.540 0.40 21.34 ?  100 VAL   A HG12 1 
ATOM   1927 H HG12 B VAL   A 1 100 ? 17.114 -1.962  -13.579 0.60 21.74 ?  100 VAL   A HG12 1 
ATOM   1928 H HG13 A VAL   A 1 100 ? 18.135 -3.465  -13.864 0.40 21.34 ?  100 VAL   A HG13 1 
ATOM   1929 H HG13 B VAL   A 1 100 ? 18.060 -3.185  -13.946 0.60 21.74 ?  100 VAL   A HG13 1 
ATOM   1930 H HG21 A VAL   A 1 100 ? 17.539 -4.663  -11.137 0.40 21.77 ?  100 VAL   A HG21 1 
ATOM   1931 H HG21 B VAL   A 1 100 ? 17.502 -4.534  -11.296 0.60 21.63 ?  100 VAL   A HG21 1 
ATOM   1932 H HG22 A VAL   A 1 100 ? 19.023 -4.780  -11.692 0.40 21.77 ?  100 VAL   A HG22 1 
ATOM   1933 H HG22 B VAL   A 1 100 ? 18.992 -4.557  -11.847 0.60 21.63 ?  100 VAL   A HG22 1 
ATOM   1934 H HG23 A VAL   A 1 100 ? 18.751 -4.075  -10.295 0.40 21.77 ?  100 VAL   A HG23 1 
ATOM   1935 H HG23 B VAL   A 1 100 ? 18.685 -3.943  -10.415 0.60 21.63 ?  100 VAL   A HG23 1 
ATOM   1936 N N    A ASN   A 1 101 ? 19.328 0.188   -12.252 0.40 17.52 ?  101 ASN   A N    1 
ATOM   1937 N N    B ASN   A 1 101 ? 19.164 0.458   -12.085 0.60 14.63 ?  101 ASN   A N    1 
ATOM   1938 C CA   A ASN   A 1 101 ? 19.270 1.467   -12.950 0.40 18.74 ?  101 ASN   A CA   1 
ATOM   1939 C CA   B ASN   A 1 101 ? 19.069 1.765   -12.725 0.60 15.50 ?  101 ASN   A CA   1 
ATOM   1940 C C    A ASN   A 1 101 ? 20.621 1.891   -13.517 0.40 19.75 ?  101 ASN   A C    1 
ATOM   1941 C C    B ASN   A 1 101 ? 20.411 2.266   -13.245 0.60 17.21 ?  101 ASN   A C    1 
ATOM   1942 O O    A ASN   A 1 101 ? 20.676 2.867   -14.273 0.40 20.40 ?  101 ASN   A O    1 
ATOM   1943 O O    B ASN   A 1 101 ? 20.439 3.275   -13.960 0.60 19.11 ?  101 ASN   A O    1 
ATOM   1944 C CB   A ASN   A 1 101 ? 18.687 2.535   -12.021 0.40 18.83 ?  101 ASN   A CB   1 
ATOM   1945 C CB   B ASN   A 1 101 ? 18.400 2.764   -11.776 0.60 15.73 ?  101 ASN   A CB   1 
ATOM   1946 C CG   A ASN   A 1 101 ? 17.320 2.148   -11.487 0.40 18.84 ?  101 ASN   A CG   1 
ATOM   1947 C CG   B ASN   A 1 101 ? 16.993 2.335   -11.399 0.60 16.13 ?  101 ASN   A CG   1 
ATOM   1948 O OD1  A ASN   A 1 101 ? 16.478 1.629   -12.223 0.40 19.32 ?  101 ASN   A OD1  1 
ATOM   1949 O OD1  B ASN   A 1 101 ? 16.251 1.817   -12.238 0.60 17.13 ?  101 ASN   A OD1  1 
ATOM   1950 N ND2  A ASN   A 1 101 ? 17.097 2.380   -10.199 0.40 18.59 ?  101 ASN   A ND2  1 
ATOM   1951 N ND2  B ASN   A 1 101 ? 16.623 2.526   -10.141 0.60 15.75 ?  101 ASN   A ND2  1 
ATOM   1952 H H    A ASN   A 1 101 ? 19.214 0.243   -11.402 0.40 21.02 ?  101 ASN   A H    1 
ATOM   1953 H H    B ASN   A 1 101 ? 19.070 0.470   -11.230 0.60 17.55 ?  101 ASN   A H    1 
ATOM   1954 H HA   A ASN   A 1 101 ? 18.670 1.382   -13.701 0.40 22.48 ?  101 ASN   A HA   1 
ATOM   1955 H HA   B ASN   A 1 101 ? 18.490 1.684   -13.494 0.60 18.59 ?  101 ASN   A HA   1 
ATOM   1956 H HB2  A ASN   A 1 101 ? 19.276 2.664   -11.263 0.40 22.59 ?  101 ASN   A HB2  1 
ATOM   1957 H HB2  B ASN   A 1 101 ? 18.922 2.837   -10.963 0.60 18.87 ?  101 ASN   A HB2  1 
ATOM   1958 H HB3  A ASN   A 1 101 ? 18.591 3.369   -12.513 0.40 22.59 ?  101 ASN   A HB3  1 
ATOM   1959 H HB3  B ASN   A 1 101 ? 18.344 3.633   -12.213 0.60 18.87 ?  101 ASN   A HB3  1 
ATOM   1960 H HD21 A ASN   A 1 101 ? 16.337 2.178   -9.849  0.40 22.31 ?  101 ASN   A HD21 1 
ATOM   1961 H HD21 B ASN   A 1 101 ? 15.834 2.297   -9.883  0.60 18.89 ?  101 ASN   A HD21 1 
ATOM   1962 H HD22 A ASN   A 1 101 ? 17.712 2.735   -9.715  0.40 22.31 ?  101 ASN   A HD22 1 
ATOM   1963 H HD22 B ASN   A 1 101 ? 17.166 2.892   -9.583  0.60 18.89 ?  101 ASN   A HD22 1 
ATOM   1964 N N    A LYS   A 1 102 ? 21.698 1.179   -13.185 0.40 20.70 ?  102 LYS   A N    1 
ATOM   1965 N N    B LYS   A 1 102 ? 21.511 1.578   -12.918 0.60 18.23 ?  102 LYS   A N    1 
ATOM   1966 C CA   A LYS   A 1 102 ? 22.990 1.352   -13.832 0.40 21.58 ?  102 LYS   A CA   1 
ATOM   1967 C CA   B LYS   A 1 102 ? 22.814 1.808   -13.529 0.60 19.38 ?  102 LYS   A CA   1 
ATOM   1968 C C    A LYS   A 1 102 ? 23.293 0.226   -14.813 0.40 21.78 ?  102 LYS   A C    1 
ATOM   1969 C C    B LYS   A 1 102 ? 23.148 0.788   -14.610 0.60 19.95 ?  102 LYS   A C    1 
ATOM   1970 O O    A LYS   A 1 102 ? 24.402 0.170   -15.352 0.40 22.08 ?  102 LYS   A O    1 
ATOM   1971 O O    B LYS   A 1 102 ? 24.183 0.933   -15.271 0.60 20.43 ?  102 LYS   A O    1 
ATOM   1972 C CB   A LYS   A 1 102 ? 24.108 1.412   -12.785 0.40 22.17 ?  102 LYS   A CB   1 
ATOM   1973 C CB   B LYS   A 1 102 ? 23.920 1.780   -12.463 0.60 20.06 ?  102 LYS   A CB   1 
ATOM   1974 C CG   A LYS   A 1 102 ? 23.990 2.553   -11.788 0.40 22.59 ?  102 LYS   A CG   1 
ATOM   1975 C CG   B LYS   A 1 102 ? 23.856 2.902   -11.443 0.60 20.48 ?  102 LYS   A CG   1 
ATOM   1976 C CD   A LYS   A 1 102 ? 25.136 2.519   -10.786 0.40 23.11 ?  102 LYS   A CD   1 
ATOM   1977 C CD   B LYS   A 1 102 ? 24.969 2.765   -10.409 0.60 21.01 ?  102 LYS   A CD   1 
ATOM   1978 C CE   A LYS   A 1 102 ? 25.050 3.663   -9.789  0.40 23.50 ?  102 LYS   A CE   1 
ATOM   1979 C CE   B LYS   A 1 102 ? 24.917 3.887   -9.382  0.60 21.56 ?  102 LYS   A CE   1 
ATOM   1980 N NZ   A LYS   A 1 102 ? 26.145 3.597   -8.779  0.40 23.81 ?  102 LYS   A NZ   1 
ATOM   1981 N NZ   B LYS   A 1 102 ? 25.919 3.706   -8.293  0.60 21.54 ?  102 LYS   A NZ   1 
ATOM   1982 H H    A LYS   A 1 102 ? 21.698 0.563   -12.583 0.40 24.84 ?  102 LYS   A H    1 
ATOM   1983 H H    B LYS   A 1 102 ? 21.522 0.946   -12.329 0.60 21.87 ?  102 LYS   A H    1 
ATOM   1984 H HA   A LYS   A 1 102 ? 22.986 2.201   -14.308 0.40 25.88 ?  102 LYS   A HA   1 
ATOM   1985 H HA   B LYS   A 1 102 ? 22.823 2.672   -13.948 0.60 23.25 ?  102 LYS   A HA   1 
ATOM   1986 H HB2  A LYS   A 1 102 ? 24.107 0.583   -12.284 0.40 26.60 ?  102 LYS   A HB2  1 
ATOM   1987 H HB2  B LYS   A 1 102 ? 23.866 0.944   -11.976 0.60 24.06 ?  102 LYS   A HB2  1 
ATOM   1988 H HB3  A LYS   A 1 102 ? 24.956 1.513   -13.247 0.40 26.60 ?  102 LYS   A HB3  1 
ATOM   1989 H HB3  B LYS   A 1 102 ? 24.779 1.843   -12.908 0.60 24.06 ?  102 LYS   A HB3  1 
ATOM   1990 H HG2  A LYS   A 1 102 ? 24.022 3.400   -12.261 0.40 27.10 ?  102 LYS   A HG2  1 
ATOM   1991 H HG2  B LYS   A 1 102 ? 23.963 3.753   -11.896 0.60 24.57 ?  102 LYS   A HG2  1 
ATOM   1992 H HG3  A LYS   A 1 102 ? 23.155 2.470   -11.301 0.40 27.10 ?  102 LYS   A HG3  1 
ATOM   1993 H HG3  B LYS   A 1 102 ? 23.004 2.869   -10.982 0.60 24.57 ?  102 LYS   A HG3  1 
ATOM   1994 H HD2  A LYS   A 1 102 ? 25.105 1.684   -10.293 0.40 27.73 ?  102 LYS   A HD2  1 
ATOM   1995 H HD2  B LYS   A 1 102 ? 24.870 1.919   -9.943  0.60 25.21 ?  102 LYS   A HD2  1 
ATOM   1996 H HD3  A LYS   A 1 102 ? 25.979 2.595   -11.262 0.40 27.73 ?  102 LYS   A HD3  1 
ATOM   1997 H HD3  B LYS   A 1 102 ? 25.829 2.802   -10.858 0.60 25.21 ?  102 LYS   A HD3  1 
ATOM   1998 H HE2  A LYS   A 1 102 ? 25.124 4.507   -10.263 0.40 28.19 ?  102 LYS   A HE2  1 
ATOM   1999 H HE2  B LYS   A 1 102 ? 25.100 4.730   -9.825  0.60 25.86 ?  102 LYS   A HE2  1 
ATOM   2000 H HE3  A LYS   A 1 102 ? 24.201 3.616   -9.321  0.40 28.19 ?  102 LYS   A HE3  1 
ATOM   2001 H HE3  B LYS   A 1 102 ? 24.034 3.906   -8.980  0.60 25.86 ?  102 LYS   A HE3  1 
ATOM   2002 H HZ1  A LYS   A 1 102 ? 26.073 4.275   -8.207  0.40 28.56 ?  102 LYS   A HZ1  1 
ATOM   2003 H HZ1  B LYS   A 1 102 ? 25.861 4.377   -7.712  0.60 25.85 ?  102 LYS   A HZ1  1 
ATOM   2004 H HZ2  A LYS   A 1 102 ? 26.096 2.832   -8.327  0.40 28.56 ?  102 LYS   A HZ2  1 
ATOM   2005 H HZ2  B LYS   A 1 102 ? 25.769 2.939   -7.866  0.60 25.85 ?  102 LYS   A HZ2  1 
ATOM   2006 H HZ3  A LYS   A 1 102 ? 26.936 3.643   -9.185  0.40 28.56 ?  102 LYS   A HZ3  1 
ATOM   2007 H HZ3  B LYS   A 1 102 ? 26.740 3.689   -8.635  0.60 25.85 ?  102 LYS   A HZ3  1 
ATOM   2008 N N    A GLY   A 1 103 ? 22.348 -0.686  -15.032 0.40 21.89 ?  103 GLY   A N    1 
ATOM   2009 N N    B GLY   A 1 103 ? 22.308 -0.229  -14.803 0.60 20.68 ?  103 GLY   A N    1 
ATOM   2010 C CA   A GLY   A 1 103 ? 22.545 -1.780  -15.962 0.40 21.73 ?  103 GLY   A CA   1 
ATOM   2011 C CA   B GLY   A 1 103 ? 22.583 -1.274  -15.769 0.60 21.48 ?  103 GLY   A CA   1 
ATOM   2012 C C    A GLY   A 1 103 ? 23.358 -2.940  -15.432 0.40 21.54 ?  103 GLY   A C    1 
ATOM   2013 C C    B GLY   A 1 103 ? 23.457 -2.398  -15.267 0.60 22.15 ?  103 GLY   A C    1 
ATOM   2014 O O    A GLY   A 1 103 ? 23.830 -3.763  -16.223 0.40 22.00 ?  103 GLY   A O    1 
ATOM   2015 O O    B GLY   A 1 103 ? 24.100 -3.069  -16.081 0.60 22.68 ?  103 GLY   A O    1 
ATOM   2016 H H    A GLY   A 1 103 ? 21.581 -0.688  -14.644 0.40 26.27 ?  103 GLY   A H    1 
ATOM   2017 H H    B GLY   A 1 103 ? 21.566 -0.346  -14.374 0.60 24.81 ?  103 GLY   A H    1 
ATOM   2018 H HA2  A GLY   A 1 103 ? 21.679 -2.128  -16.219 0.40 26.07 ?  103 GLY   A HA2  1 
ATOM   2019 H HA2  B GLY   A 1 103 ? 21.741 -1.650  -16.082 0.60 25.76 ?  103 GLY   A HA2  1 
ATOM   2020 H HA3  A GLY   A 1 103 ? 22.975 -1.431  -16.761 0.40 26.07 ?  103 GLY   A HA3  1 
ATOM   2021 H HA3  B GLY   A 1 103 ? 23.038 -0.890  -16.529 0.60 25.76 ?  103 GLY   A HA3  1 
ATOM   2022 N N    A GLU   A 1 104 ? 23.518 -3.051  -14.118 0.40 20.75 ?  104 GLU   A N    1 
ATOM   2023 N N    B GLU   A 1 104 ? 23.507 -2.628  -13.958 0.60 21.87 ?  104 GLU   A N    1 
ATOM   2024 C CA   A GLU   A 1 104 ? 24.421 -4.039  -13.546 0.40 19.93 ?  104 GLU   A CA   1 
ATOM   2025 C CA   B GLU   A 1 104 ? 24.366 -3.654  -13.387 0.60 21.81 ?  104 GLU   A CA   1 
ATOM   2026 C C    A GLU   A 1 104 ? 23.744 -5.403  -13.421 0.40 20.15 ?  104 GLU   A C    1 
ATOM   2027 C C    B GLU   A 1 104 ? 23.653 -5.004  -13.325 0.60 22.82 ?  104 GLU   A C    1 
ATOM   2028 O O    A GLU   A 1 104 ? 22.522 -5.512  -13.292 0.40 20.26 ?  104 GLU   A O    1 
ATOM   2029 O O    B GLU   A 1 104 ? 22.434 -5.083  -13.151 0.60 23.38 ?  104 GLU   A O    1 
ATOM   2030 C CB   A GLU   A 1 104 ? 24.945 -3.550  -12.193 0.40 18.94 ?  104 GLU   A CB   1 
ATOM   2031 C CB   B GLU   A 1 104 ? 24.867 -3.214  -12.008 0.60 20.10 ?  104 GLU   A CB   1 
ATOM   2032 C CG   A GLU   A 1 104 ? 25.767 -2.269  -12.329 0.40 18.65 ?  104 GLU   A CG   1 
ATOM   2033 C CG   B GLU   A 1 104 ? 25.878 -2.067  -12.117 0.60 19.05 ?  104 GLU   A CG   1 
ATOM   2034 C CD   A GLU   A 1 104 ? 26.215 -1.656  -11.019 0.40 18.15 ?  104 GLU   A CD   1 
ATOM   2035 C CD   B GLU   A 1 104 ? 26.096 -1.284  -10.839 0.60 18.05 ?  104 GLU   A CD   1 
ATOM   2036 O OE1  A GLU   A 1 104 ? 25.629 -1.972  -9.965  0.40 17.54 ?  104 GLU   A OE1  1 
ATOM   2037 O OE1  B GLU   A 1 104 ? 25.494 -1.625  -9.801  0.60 16.41 ?  104 GLU   A OE1  1 
ATOM   2038 O OE2  A GLU   A 1 104 ? 27.158 -0.832  -11.060 0.40 18.23 -1 104 GLU   A OE2  1 
ATOM   2039 O OE2  B GLU   A 1 104 ? 26.884 -0.312  -10.887 0.60 18.75 -1 104 GLU   A OE2  1 
ATOM   2040 H H    A GLU   A 1 104 ? 23.107 -2.564  -13.540 0.40 24.89 ?  104 GLU   A H    1 
ATOM   2041 H H    B GLU   A 1 104 ? 23.047 -2.193  -13.371 0.60 26.23 ?  104 GLU   A H    1 
ATOM   2042 H HA   A GLU   A 1 104 ? 25.183 -4.136  -14.140 0.40 23.91 ?  104 GLU   A HA   1 
ATOM   2043 H HA   B GLU   A 1 104 ? 25.135 -3.763  -13.960 0.60 26.16 ?  104 GLU   A HA   1 
ATOM   2044 H HB2  A GLU   A 1 104 ? 24.193 -3.370  -11.611 0.40 22.72 ?  104 GLU   A HB2  1 
ATOM   2045 H HB2  B GLU   A 1 104 ? 24.114 -2.910  -11.477 0.60 24.11 ?  104 GLU   A HB2  1 
ATOM   2046 H HB3  A GLU   A 1 104 ? 25.511 -4.237  -11.812 0.40 22.72 ?  104 GLU   A HB3  1 
ATOM   2047 H HB3  B GLU   A 1 104 ? 25.303 -3.963  -11.572 0.60 24.11 ?  104 GLU   A HB3  1 
ATOM   2048 H HG2  A GLU   A 1 104 ? 26.562 -2.465  -12.844 0.40 22.37 ?  104 GLU   A HG2  1 
ATOM   2049 H HG2  B GLU   A 1 104 ? 26.737 -2.433  -12.370 0.60 22.85 ?  104 GLU   A HG2  1 
ATOM   2050 H HG3  A GLU   A 1 104 ? 25.231 -1.602  -12.779 0.40 22.37 ?  104 GLU   A HG3  1 
ATOM   2051 H HG3  B GLU   A 1 104 ? 25.572 -1.446  -12.796 0.60 22.85 ?  104 GLU   A HG3  1 
ATOM   2052 N N    A ASP   A 1 105 ? 24.565 -6.450  -13.456 0.40 20.89 ?  105 ASP   A N    1 
ATOM   2053 N N    B ASP   A 1 105 ? 24.441 -6.072  -13.474 0.60 23.46 ?  105 ASP   A N    1 
ATOM   2054 C CA   A ASP   A 1 105 ? 24.073 -7.819  -13.569 0.40 22.02 ?  105 ASP   A CA   1 
ATOM   2055 C CA   B ASP   A 1 105 ? 23.911 -7.419  -13.661 0.60 24.45 ?  105 ASP   A CA   1 
ATOM   2056 C C    A ASP   A 1 105 ? 23.379 -8.249  -12.280 0.40 20.79 ?  105 ASP   A C    1 
ATOM   2057 C C    B ASP   A 1 105 ? 23.270 -7.938  -12.378 0.60 22.69 ?  105 ASP   A C    1 
ATOM   2058 O O    A ASP   A 1 105 ? 24.012 -8.331  -11.224 0.40 19.31 ?  105 ASP   A O    1 
ATOM   2059 O O    B ASP   A 1 105 ? 23.928 -8.029  -11.338 0.60 21.00 ?  105 ASP   A O    1 
ATOM   2060 C CB   A ASP   A 1 105 ? 25.248 -8.745  -13.870 0.40 24.25 ?  105 ASP   A CB   1 
ATOM   2061 C CB   B ASP   A 1 105 ? 25.039 -8.349  -14.105 0.60 26.98 ?  105 ASP   A CB   1 
ATOM   2062 C CG   A ASP   A 1 105 ? 24.812 -10.149 -14.237 0.40 26.12 ?  105 ASP   A CG   1 
ATOM   2063 C CG   B ASP   A 1 105 ? 24.700 -9.811  -13.906 0.60 29.00 ?  105 ASP   A CG   1 
ATOM   2064 O OD1  A ASP   A 1 105 ? 23.592 -10.389 -14.321 0.40 26.96 ?  105 ASP   A OD1  1 
ATOM   2065 O OD1  B ASP   A 1 105 ? 23.556 -10.203 -14.213 0.60 29.42 ?  105 ASP   A OD1  1 
ATOM   2066 O OD2  A ASP   A 1 105 ? 25.695 -11.010 -14.447 0.40 26.81 -1 105 ASP   A OD2  1 
ATOM   2067 O OD2  B ASP   A 1 105 ? 25.583 -10.570 -13.456 0.60 30.07 -1 105 ASP   A OD2  1 
ATOM   2068 H H    A ASP   A 1 105 ? 25.422 -6.384  -13.419 0.40 25.07 ?  105 ASP   A H    1 
ATOM   2069 H H    B ASP   A 1 105 ? 25.301 -6.040  -13.474 0.60 28.14 ?  105 ASP   A H    1 
ATOM   2070 H HA   A ASP   A 1 105 ? 23.434 -7.870  -14.296 0.40 26.42 ?  105 ASP   A HA   1 
ATOM   2071 H HA   B ASP   A 1 105 ? 23.238 -7.414  -14.355 0.60 29.33 ?  105 ASP   A HA   1 
ATOM   2072 H HB2  A ASP   A 1 105 ? 25.747 -8.382  -14.617 0.40 29.09 ?  105 ASP   A HB2  1 
ATOM   2073 H HB2  B ASP   A 1 105 ? 25.208 -8.221  -15.051 0.60 32.37 ?  105 ASP   A HB2  1 
ATOM   2074 H HB3  A ASP   A 1 105 ? 25.813 -8.795  -13.084 0.40 29.09 ?  105 ASP   A HB3  1 
ATOM   2075 H HB3  B ASP   A 1 105 ? 25.843 -8.143  -13.597 0.60 32.37 ?  105 ASP   A HB3  1 
ATOM   2076 N N    A ILE   A 1 106 ? 22.080 -8.548  -12.375 0.40 21.25 ?  106 ILE   A N    1 
ATOM   2077 N N    B ILE   A 1 106 ? 21.994 -8.325  -12.469 0.60 22.81 ?  106 ILE   A N    1 
ATOM   2078 C CA   A ILE   A 1 106 ? 21.315 -8.972  -11.207 0.40 21.56 ?  106 ILE   A CA   1 
ATOM   2079 C CA   B ILE   A 1 106 ? 21.244 -8.744  -11.291 0.60 22.15 ?  106 ILE   A CA   1 
ATOM   2080 C C    A ILE   A 1 106 ? 21.846 -10.276 -10.630 0.40 21.45 ?  106 ILE   A C    1 
ATOM   2081 C C    B ILE   A 1 106 ? 21.774 -10.043 -10.698 0.60 20.60 ?  106 ILE   A C    1 
ATOM   2082 O O    A ILE   A 1 106 ? 21.637 -10.556 -9.445  0.40 21.08 ?  106 ILE   A O    1 
ATOM   2083 O O    B ILE   A 1 106 ? 21.547 -10.311 -9.514  0.60 19.58 ?  106 ILE   A O    1 
ATOM   2084 C CB   A ILE   A 1 106 ? 19.807 -9.049  -11.546 0.40 22.57 ?  106 ILE   A CB   1 
ATOM   2085 C CB   B ILE   A 1 106 ? 19.738 -8.844  -11.613 0.60 23.62 ?  106 ILE   A CB   1 
ATOM   2086 C CG1  A ILE   A 1 106 ? 18.965 -9.152  -10.271 0.40 22.96 ?  106 ILE   A CG1  1 
ATOM   2087 C CG1  B ILE   A 1 106 ? 18.912 -8.920  -10.326 0.60 24.30 ?  106 ILE   A CG1  1 
ATOM   2088 C CG2  A ILE   A 1 106 ? 19.519 -10.228 -12.457 0.40 22.95 ?  106 ILE   A CG2  1 
ATOM   2089 C CG2  B ILE   A 1 106 ? 19.455 -10.067 -12.471 0.60 24.17 ?  106 ILE   A CG2  1 
ATOM   2090 C CD1  A ILE   A 1 106 ? 19.032 -7.925  -9.388  0.40 23.14 ?  106 ILE   A CD1  1 
ATOM   2091 C CD1  B ILE   A 1 106 ? 19.198 -7.804  -9.349  0.60 24.83 ?  106 ILE   A CD1  1 
ATOM   2092 H H    A ILE   A 1 106 ? 21.626 -8.506  -13.101 0.40 25.50 ?  106 ILE   A H    1 
ATOM   2093 H H    B ILE   A 1 106 ? 21.548 -8.352  -13.200 0.60 27.36 ?  106 ILE   A H    1 
ATOM   2094 H HA   A ILE   A 1 106 ? 21.421 -8.300  -10.520 0.40 25.86 ?  106 ILE   A HA   1 
ATOM   2095 H HA   B ILE   A 1 106 ? 21.362 -8.062  -10.620 0.60 26.58 ?  106 ILE   A HA   1 
ATOM   2096 H HB   A ILE   A 1 106 ? 19.557 -8.234  -12.011 0.40 27.08 ?  106 ILE   A HB   1 
ATOM   2097 H HB   B ILE   A 1 106 ? 19.471 -8.053  -12.106 0.60 28.34 ?  106 ILE   A HB   1 
ATOM   2098 H HG12 A ILE   A 1 106 ? 18.036 -9.281  -10.520 0.40 27.54 ?  106 ILE   A HG12 1 
ATOM   2099 H HG12 B ILE   A 1 106 ? 17.970 -8.876  -10.557 0.60 29.16 ?  106 ILE   A HG12 1 
ATOM   2100 H HG13 A ILE   A 1 106 ? 19.272 -9.908  -9.749  0.40 27.54 ?  106 ILE   A HG13 1 
ATOM   2101 H HG13 B ILE   A 1 106 ? 19.101 -9.760  -9.881  0.60 29.16 ?  106 ILE   A HG13 1 
ATOM   2102 H HG21 A ILE   A 1 106 ? 18.620 -10.139 -12.810 0.40 27.54 ?  106 ILE   A HG21 1 
ATOM   2103 H HG21 B ILE   A 1 106 ? 18.567 -9.985  -12.852 0.60 28.99 ?  106 ILE   A HG21 1 
ATOM   2104 H HG22 A ILE   A 1 106 ? 20.162 -10.226 -13.182 0.40 27.54 ?  106 ILE   A HG22 1 
ATOM   2105 H HG22 B ILE   A 1 106 ? 20.116 -10.112 -13.178 0.60 28.99 ?  106 ILE   A HG22 1 
ATOM   2106 H HG23 A ILE   A 1 106 ? 19.595 -11.048 -11.947 0.40 27.54 ?  106 ILE   A HG23 1 
ATOM   2107 H HG23 B ILE   A 1 106 ? 19.506 -10.862 -11.918 0.60 28.99 ?  106 ILE   A HG23 1 
ATOM   2108 H HD11 A ILE   A 1 106 ? 18.322 -7.971  -8.730  0.40 27.76 ?  106 ILE   A HD11 1 
ATOM   2109 H HD11 B ILE   A 1 106 ? 18.450 -7.719  -8.743  0.60 29.78 ?  106 ILE   A HD11 1 
ATOM   2110 H HD12 A ILE   A 1 106 ? 19.894 -7.901  -8.942  0.40 27.76 ?  106 ILE   A HD12 1 
ATOM   2111 H HD12 B ILE   A 1 106 ? 20.005 -8.019  -8.853  0.60 29.78 ?  106 ILE   A HD12 1 
ATOM   2112 H HD13 A ILE   A 1 106 ? 18.922 -7.133  -9.938  0.40 27.76 ?  106 ILE   A HD13 1 
ATOM   2113 H HD13 B ILE   A 1 106 ? 19.321 -6.978  -9.843  0.60 29.78 ?  106 ILE   A HD13 1 
ATOM   2114 N N    A GLN   A 1 107 ? 22.542 -11.081 -11.438 0.40 21.90 ?  107 GLN   A N    1 
ATOM   2115 N N    B GLN   A 1 107 ? 22.485 -10.858 -11.482 0.60 21.07 ?  107 GLN   A N    1 
ATOM   2116 C CA   A GLN   A 1 107 ? 23.173 -12.290 -10.921 0.40 22.72 ?  107 GLN   A CA   1 
ATOM   2117 C CA   B GLN   A 1 107 ? 23.029 -12.102 -10.948 0.60 22.29 ?  107 GLN   A CA   1 
ATOM   2118 C C    A GLN   A 1 107 ? 24.159 -11.976 -9.804  0.40 20.63 ?  107 GLN   A C    1 
ATOM   2119 C C    B GLN   A 1 107 ? 24.050 -11.852 -9.848  0.60 20.26 ?  107 GLN   A C    1 
ATOM   2120 O O    A GLN   A 1 107 ? 24.434 -12.842 -8.966  0.40 21.77 ?  107 GLN   A O    1 
ATOM   2121 O O    B GLN   A 1 107 ? 24.299 -12.747 -9.033  0.60 21.99 ?  107 GLN   A O    1 
ATOM   2122 C CB   A GLN   A 1 107 ? 23.882 -13.035 -12.057 0.40 25.42 ?  107 GLN   A CB   1 
ATOM   2123 C CB   B GLN   A 1 107 ? 23.645 -12.945 -12.070 0.60 25.89 ?  107 GLN   A CB   1 
ATOM   2124 C CG   A GLN   A 1 107 ? 23.005 -13.281 -13.281 0.40 28.13 ?  107 GLN   A CG   1 
ATOM   2125 C CG   B GLN   A 1 107 ? 22.686 -13.240 -13.217 0.60 29.38 ?  107 GLN   A CG   1 
ATOM   2126 C CD   A GLN   A 1 107 ? 21.765 -14.088 -12.960 0.40 30.36 ?  107 GLN   A CD   1 
ATOM   2127 C CD   B GLN   A 1 107 ? 21.362 -13.812 -12.746 0.60 32.21 ?  107 GLN   A CD   1 
ATOM   2128 O OE1  A GLN   A 1 107 ? 21.844 -15.145 -12.334 0.40 31.23 ?  107 GLN   A OE1  1 
ATOM   2129 O OE1  B GLN   A 1 107 ? 21.319 -14.651 -11.846 0.60 33.50 ?  107 GLN   A OE1  1 
ATOM   2130 N NE2  A GLN   A 1 107 ? 20.607 -13.589 -13.383 0.40 31.13 ?  107 GLN   A NE2  1 
ATOM   2131 N NE2  B GLN   A 1 107 ? 20.271 -13.351 -13.348 0.60 33.15 ?  107 GLN   A NE2  1 
ATOM   2132 H H    A GLN   A 1 107 ? 22.664 -10.945 -12.278 0.40 26.27 ?  107 GLN   A H    1 
ATOM   2133 H H    B GLN   A 1 107 ? 22.667 -10.714 -12.305 0.60 25.27 ?  107 GLN   A H    1 
ATOM   2134 H HA   A GLN   A 1 107 ? 22.492 -12.876 -10.561 0.40 27.25 ?  107 GLN   A HA   1 
ATOM   2135 H HA   B GLN   A 1 107 ? 22.313 -12.616 -10.552 0.60 26.74 ?  107 GLN   A HA   1 
ATOM   2136 H HB2  A GLN   A 1 107 ? 24.648 -12.516 -12.345 0.40 30.50 ?  107 GLN   A HB2  1 
ATOM   2137 H HB2  B GLN   A 1 107 ? 24.407 -12.474 -12.439 0.60 31.06 ?  107 GLN   A HB2  1 
ATOM   2138 H HB3  A GLN   A 1 107 ? 24.175 -13.901 -11.731 0.40 30.50 ?  107 GLN   A HB3  1 
ATOM   2139 H HB3  B GLN   A 1 107 ? 23.932 -13.798 -11.703 0.60 31.06 ?  107 GLN   A HB3  1 
ATOM   2140 H HG2  A GLN   A 1 107 ? 22.721 -12.430 -13.651 0.40 33.74 ?  107 GLN   A HG2  1 
ATOM   2141 H HG2  B GLN   A 1 107 ? 22.502 -12.417 -13.695 0.60 35.24 ?  107 GLN   A HG2  1 
ATOM   2142 H HG3  A GLN   A 1 107 ? 23.517 -13.772 -13.942 0.40 33.74 ?  107 GLN   A HG3  1 
ATOM   2143 H HG3  B GLN   A 1 107 ? 23.094 -13.887 -13.814 0.60 35.24 ?  107 GLN   A HG3  1 
ATOM   2144 H HE21 A GLN   A 1 107 ? 20.591 -12.846 -13.817 0.40 37.35 ?  107 GLN   A HE21 1 
ATOM   2145 H HE21 B GLN   A 1 107 ? 20.341 -12.763 -13.971 0.60 39.77 ?  107 GLN   A HE21 1 
ATOM   2146 H HE22 A GLN   A 1 107 ? 19.874 -14.009 -13.223 0.40 37.35 ?  107 GLN   A HE22 1 
ATOM   2147 H HE22 B GLN   A 1 107 ? 19.496 -13.644 -13.117 0.60 39.77 ?  107 GLN   A HE22 1 
ATOM   2148 N N    A LEU   A 1 108 ? 24.684 -10.750 -9.764  0.40 17.51 ?  108 LEU   A N    1 
ATOM   2149 N N    B LEU   A 1 108 ? 24.628 -10.652 -9.784  0.60 16.32 ?  108 LEU   A N    1 
ATOM   2150 C CA   A LEU   A 1 108 ? 25.593 -10.339 -8.703  0.40 15.00 ?  108 LEU   A CA   1 
ATOM   2151 C CA   B LEU   A 1 108 ? 25.572 -10.334 -8.722  0.60 14.35 ?  108 LEU   A CA   1 
ATOM   2152 C C    A LEU   A 1 108 ? 24.895 -10.185 -7.359  0.40 13.17 ?  108 LEU   A C    1 
ATOM   2153 C C    B LEU   A 1 108 ? 24.892 -10.177 -7.370  0.60 12.62 ?  108 LEU   A C    1 
ATOM   2154 O O    A LEU   A 1 108 ? 25.580 -10.029 -6.343  0.40 13.07 ?  108 LEU   A O    1 
ATOM   2155 O O    B LEU   A 1 108 ? 25.585 -10.014 -6.363  0.60 12.44 ?  108 LEU   A O    1 
ATOM   2156 C CB   A LEU   A 1 108 ? 26.286 -9.029  -9.094  0.40 14.72 ?  108 LEU   A CB   1 
ATOM   2157 C CB   B LEU   A 1 108 ? 26.363 -9.073  -9.084  0.60 14.73 ?  108 LEU   A CB   1 
ATOM   2158 C CG   A LEU   A 1 108 ? 27.265 -9.149  -10.264 0.40 15.08 ?  108 LEU   A CG   1 
ATOM   2159 C CG   B LEU   A 1 108 ? 27.336 -9.287  -10.248 0.60 16.08 ?  108 LEU   A CG   1 
ATOM   2160 C CD1  A LEU   A 1 108 ? 27.594 -7.782  -10.847 0.40 15.04 ?  108 LEU   A CD1  1 
ATOM   2161 C CD1  B LEU   A 1 108 ? 27.985 -7.979  -10.659 0.60 16.24 ?  108 LEU   A CD1  1 
ATOM   2162 C CD2  A LEU   A 1 108 ? 28.534 -9.853  -9.812  0.40 15.38 ?  108 LEU   A CD2  1 
ATOM   2163 C CD2  B LEU   A 1 108 ? 28.395 -10.318 -9.883  0.60 17.23 ?  108 LEU   A CD2  1 
ATOM   2164 H H    A LEU   A 1 108 ? 24.527 -10.141 -10.344 0.40 21.00 ?  108 LEU   A H    1 
ATOM   2165 H H    B LEU   A 1 108 ? 24.490 -10.015 -10.337 0.60 19.58 ?  108 LEU   A H    1 
ATOM   2166 H HA   A LEU   A 1 108 ? 26.277 -11.014 -8.597  0.40 17.99 ?  108 LEU   A HA   1 
ATOM   2167 H HA   B LEU   A 1 108 ? 26.200 -11.064 -8.636  0.60 17.21 ?  108 LEU   A HA   1 
ATOM   2168 H HB2  A LEU   A 1 108 ? 25.609 -8.382  -9.346  0.40 17.65 ?  108 LEU   A HB2  1 
ATOM   2169 H HB2  B LEU   A 1 108 ? 25.741 -8.373  -9.342  0.60 17.67 ?  108 LEU   A HB2  1 
ATOM   2170 H HB3  A LEU   A 1 108 ? 26.782 -8.701  -8.330  0.40 17.65 ?  108 LEU   A HB3  1 
ATOM   2171 H HB3  B LEU   A 1 108 ? 26.878 -8.790  -8.313  0.60 17.67 ?  108 LEU   A HB3  1 
ATOM   2172 H HG   A LEU   A 1 108 ? 26.859 -9.684  -10.964 0.40 18.09 ?  108 LEU   A HG   1 
ATOM   2173 H HG   B LEU   A 1 108 ? 26.841 -9.627  -11.010 0.60 19.29 ?  108 LEU   A HG   1 
ATOM   2174 H HD11 A LEU   A 1 108 ? 28.174 -7.899  -11.618 0.40 18.04 ?  108 LEU   A HD11 1 
ATOM   2175 H HD11 B LEU   A 1 108 ? 28.583 -8.145  -11.404 0.60 19.48 ?  108 LEU   A HD11 1 
ATOM   2176 H HD12 A LEU   A 1 108 ? 26.771 -7.347  -11.116 0.40 18.04 ?  108 LEU   A HD12 1 
ATOM   2177 H HD12 B LEU   A 1 108 ? 27.293 -7.353  -10.923 0.60 19.48 ?  108 LEU   A HD12 1 
ATOM   2178 H HD13 A LEU   A 1 108 ? 28.045 -7.251  -10.173 0.40 18.04 ?  108 LEU   A HD13 1 
ATOM   2179 H HD13 B LEU   A 1 108 ? 28.483 -7.624  -9.906  0.60 19.48 ?  108 LEU   A HD13 1 
ATOM   2180 H HD21 A LEU   A 1 108 ? 29.169 -9.860  -10.544 0.40 18.45 ?  108 LEU   A HD21 1 
ATOM   2181 H HD21 B LEU   A 1 108 ? 29.132 -10.244 -10.506 0.60 20.67 ?  108 LEU   A HD21 1 
ATOM   2182 H HD22 A LEU   A 1 108 ? 28.905 -9.379  -9.053  0.40 18.45 ?  108 LEU   A HD22 1 
ATOM   2183 H HD22 B LEU   A 1 108 ? 28.703 -10.143 -8.979  0.60 20.67 ?  108 LEU   A HD22 1 
ATOM   2184 H HD23 A LEU   A 1 108 ? 28.315 -10.765 -9.557  0.40 18.45 ?  108 LEU   A HD23 1 
ATOM   2185 H HD23 B LEU   A 1 108 ? 28.004 -11.204 -9.933  0.60 20.67 ?  108 LEU   A HD23 1 
ATOM   2186 N N    . LEU   A 1 109 ? 23.561 -10.227 -7.319  1.00 12.09 ?  109 LEU   A N    1 
ATOM   2187 C CA   . LEU   A 1 109 ? 22.871 -10.098 -6.044  1.00 11.23 ?  109 LEU   A CA   1 
ATOM   2188 C C    . LEU   A 1 109 ? 23.212 -11.252 -5.108  1.00 10.39 ?  109 LEU   A C    1 
ATOM   2189 O O    . LEU   A 1 109 ? 23.349 -11.057 -3.895  1.00 10.72 ?  109 LEU   A O    1 
ATOM   2190 C CB   . LEU   A 1 109 ? 21.368 -10.005 -6.289  1.00 12.01 ?  109 LEU   A CB   1 
ATOM   2191 C CG   . LEU   A 1 109 ? 20.484 -9.723  -5.078  1.00 11.72 ?  109 LEU   A CG   1 
ATOM   2192 C CD1  . LEU   A 1 109 ? 20.938 -8.464  -4.357  1.00 12.02 ?  109 LEU   A CD1  1 
ATOM   2193 C CD2  . LEU   A 1 109 ? 19.028 -9.584  -5.516  1.00 12.66 ?  109 LEU   A CD2  1 
ATOM   2194 H H    A LEU   A 1 109 ? 23.046 -10.325 -7.999  0.40 14.50 ?  109 LEU   A H    1 
ATOM   2195 H H    B LEU   A 1 109 ? 23.043 -10.328 -7.996  0.60 14.50 ?  109 LEU   A H    1 
ATOM   2196 H HA   . LEU   A 1 109 ? 23.156 -9.275  -5.614  1.00 13.47 ?  109 LEU   A HA   1 
ATOM   2197 H HB2  . LEU   A 1 109 ? 21.212 -9.290  -6.928  1.00 14.40 ?  109 LEU   A HB2  1 
ATOM   2198 H HB3  . LEU   A 1 109 ? 21.070 -10.844 -6.668  1.00 14.40 ?  109 LEU   A HB3  1 
ATOM   2199 H HG   . LEU   A 1 109 ? 20.544 -10.462 -4.458  1.00 14.06 ?  109 LEU   A HG   1 
ATOM   2200 H HD11 . LEU   A 1 109 ? 20.250 -8.189  -3.731  1.00 14.41 ?  109 LEU   A HD11 1 
ATOM   2201 H HD12 . LEU   A 1 109 ? 21.764 -8.645  -3.884  1.00 14.41 ?  109 LEU   A HD12 1 
ATOM   2202 H HD13 . LEU   A 1 109 ? 21.083 -7.756  -5.011  1.00 14.41 ?  109 LEU   A HD13 1 
ATOM   2203 H HD21 . LEU   A 1 109 ? 18.500 -9.260  -4.769  1.00 15.18 ?  109 LEU   A HD21 1 
ATOM   2204 H HD22 . LEU   A 1 109 ? 18.975 -8.954  -6.253  1.00 15.18 ?  109 LEU   A HD22 1 
ATOM   2205 H HD23 . LEU   A 1 109 ? 18.699 -10.452 -5.802  1.00 15.18 ?  109 LEU   A HD23 1 
ATOM   2206 N N    . LYS   A 1 110 ? 23.357 -12.468 -5.645  1.00 10.38 ?  110 LYS   A N    1 
ATOM   2207 C CA   . LYS   A 1 110 ? 23.726 -13.587 -4.785  1.00 10.42 ?  110 LYS   A CA   1 
ATOM   2208 C C    . LYS   A 1 110 ? 25.107 -13.368 -4.174  1.00 10.13 ?  110 LYS   A C    1 
ATOM   2209 O O    . LYS   A 1 110 ? 25.298 -13.564 -2.971  1.00 10.03 ?  110 LYS   A O    1 
ATOM   2210 C CB   . LYS   A 1 110 ? 23.655 -14.911 -5.551  1.00 11.16 ?  110 LYS   A CB   1 
ATOM   2211 C CG   . LYS   A 1 110 ? 23.859 -16.129 -4.644  1.00 11.45 ?  110 LYS   A CG   1 
ATOM   2212 C CD   . LYS   A 1 110 ? 23.615 -17.446 -5.355  1.00 11.94 ?  110 LYS   A CD   1 
ATOM   2213 C CE   . LYS   A 1 110 ? 23.724 -18.619 -4.393  1.00 12.86 ?  110 LYS   A CE   1 
ATOM   2214 N NZ   . LYS   A 1 110 ? 22.534 -18.744 -3.507  1.00 13.25 ?  110 LYS   A NZ   1 
ATOM   2215 H H    . LYS   A 1 110 ? 23.240 -12.662 -6.471  1.00 12.45 ?  110 LYS   A H    1 
ATOM   2216 H HA   . LYS   A 1 110 ? 23.084 -13.644 -4.057  1.00 12.50 ?  110 LYS   A HA   1 
ATOM   2217 H HB2  . LYS   A 1 110 ? 22.782 -14.994 -5.968  1.00 13.38 ?  110 LYS   A HB2  1 
ATOM   2218 H HB3  . LYS   A 1 110 ? 24.348 -14.924 -6.228  1.00 13.38 ?  110 LYS   A HB3  1 
ATOM   2219 H HG2  . LYS   A 1 110 ? 24.773 -16.133 -4.318  1.00 13.73 ?  110 LYS   A HG2  1 
ATOM   2220 H HG3  . LYS   A 1 110 ? 23.242 -16.076 -3.898  1.00 13.73 ?  110 LYS   A HG3  1 
ATOM   2221 H HD2  . LYS   A 1 110 ? 22.724 -17.449 -5.734  1.00 14.32 ?  110 LYS   A HD2  1 
ATOM   2222 H HD3  . LYS   A 1 110 ? 24.280 -17.565 -6.052  1.00 14.32 ?  110 LYS   A HD3  1 
ATOM   2223 H HE2  . LYS   A 1 110 ? 23.808 -19.443 -4.899  1.00 15.42 ?  110 LYS   A HE2  1 
ATOM   2224 H HE3  . LYS   A 1 110 ? 24.505 -18.497 -3.828  1.00 15.42 ?  110 LYS   A HE3  1 
ATOM   2225 H HZ1  . LYS   A 1 110 ? 22.629 -19.436 -2.960  1.00 15.89 ?  110 LYS   A HZ1  1 
ATOM   2226 H HZ2  . LYS   A 1 110 ? 22.435 -18.001 -3.025  1.00 15.89 ?  110 LYS   A HZ2  1 
ATOM   2227 H HZ3  . LYS   A 1 110 ? 21.801 -18.863 -4.002  1.00 15.89 ?  110 LYS   A HZ3  1 
ATOM   2228 N N    . SER   A 1 111 ? 26.072 -12.929 -4.986  1.00 10.22 ?  111 SER   A N    1 
ATOM   2229 C CA   . SER   A 1 111 ? 27.401 -12.625 -4.465  1.00 10.48 ?  111 SER   A CA   1 
ATOM   2230 C C    . SER   A 1 111 ? 27.332 -11.579 -3.357  1.00 9.97  ?  111 SER   A C    1 
ATOM   2231 O O    . SER   A 1 111 ? 28.025 -11.689 -2.339  1.00 10.35 ?  111 SER   A O    1 
ATOM   2232 C CB   . SER   A 1 111 ? 28.289 -12.130 -5.604  1.00 11.74 ?  111 SER   A CB   1 
ATOM   2233 O OG   . SER   A 1 111 ? 28.416 -13.127 -6.603  1.00 13.45 ?  111 SER   A OG   1 
ATOM   2234 H H    . SER   A 1 111 ? 25.977 -12.797 -5.829  1.00 12.25 ?  111 SER   A H    1 
ATOM   2235 H HA   . SER   A 1 111 ? 27.794 -13.433 -4.099  1.00 12.57 ?  111 SER   A HA   1 
ATOM   2236 H HB2  . SER   A 1 111 ? 27.882 -11.345 -6.002  1.00 14.08 ?  111 SER   A HB2  1 
ATOM   2237 H HB3  . SER   A 1 111 ? 29.163 -11.909 -5.249  1.00 14.08 ?  111 SER   A HB3  1 
ATOM   2238 H HG   . SER   A 1 111 ? 28.924 -12.846 -7.220  1.00 16.14 ?  111 SER   A HG   1 
ATOM   2239 N N    . ALA   A 1 112 ? 26.496 -10.559 -3.541  1.00 10.06 ?  112 ALA   A N    1 
ATOM   2240 C CA   . ALA   A 1 112 ? 26.342 -9.525  -2.520  1.00 10.17 ?  112 ALA   A CA   1 
ATOM   2241 C C    . ALA   A 1 112 ? 25.860 -10.122 -1.199  1.00 10.07 ?  112 ALA   A C    1 
ATOM   2242 O O    . ALA   A 1 112 ? 26.418 -9.839  -0.131  1.00 10.08 ?  112 ALA   A O    1 
ATOM   2243 C CB   . ALA   A 1 112 ? 25.382 -8.441  -3.015  1.00 10.46 ?  112 ALA   A CB   1 
ATOM   2244 H H    . ALA   A 1 112 ? 26.010 -10.439 -4.238  1.00 12.06 ?  112 ALA   A H    1 
ATOM   2245 H HA   . ALA   A 1 112 ? 27.202 -9.105  -2.358  1.00 12.19 ?  112 ALA   A HA   1 
ATOM   2246 H HB1  . ALA   A 1 112 ? 25.301 -7.748  -2.330  1.00 12.54 ?  112 ALA   A HB1  1 
ATOM   2247 H HB2  . ALA   A 1 112 ? 25.739 -8.046  -3.828  1.00 12.54 ?  112 ALA   A HB2  1 
ATOM   2248 H HB3  . ALA   A 1 112 ? 24.515 -8.831  -3.188  1.00 12.54 ?  112 ALA   A HB3  1 
ATOM   2249 N N    . TYR   A 1 113 ? 24.824 -10.964 -1.249  1.00 9.77  ?  113 TYR   A N    1 
ATOM   2250 C CA   . TYR   A 1 113 ? 24.316 -11.567 -0.018  1.00 9.79  ?  113 TYR   A CA   1 
ATOM   2251 C C    . TYR   A 1 113 ? 25.317 -12.525 0.627   1.00 9.47  ?  113 TYR   A C    1 
ATOM   2252 O O    . TYR   A 1 113 ? 25.278 -12.709 1.847   1.00 9.97  ?  113 TYR   A O    1 
ATOM   2253 C CB   . TYR   A 1 113 ? 22.990 -12.280 -0.278  1.00 10.16 ?  113 TYR   A CB   1 
ATOM   2254 C CG   . TYR   A 1 113 ? 21.776 -11.374 -0.206  1.00 9.92  ?  113 TYR   A CG   1 
ATOM   2255 C CD1  . TYR   A 1 113 ? 21.414 -10.763 0.989   1.00 10.32 ?  113 TYR   A CD1  1 
ATOM   2256 C CD2  . TYR   A 1 113 ? 20.978 -11.156 -1.321  1.00 10.14 ?  113 TYR   A CD2  1 
ATOM   2257 C CE1  . TYR   A 1 113 ? 20.294 -9.949  1.071   1.00 10.45 ?  113 TYR   A CE1  1 
ATOM   2258 C CE2  . TYR   A 1 113 ? 19.841 -10.346 -1.248  1.00 10.54 ?  113 TYR   A CE2  1 
ATOM   2259 C CZ   . TYR   A 1 113 ? 19.512 -9.744  -0.047  1.00 10.28 ?  113 TYR   A CZ   1 
ATOM   2260 O OH   . TYR   A 1 113 ? 18.387 -8.945  0.068   1.00 11.05 ?  113 TYR   A OH   1 
ATOM   2261 H H    . TYR   A 1 113 ? 24.409 -11.194 -1.966  1.00 11.72 ?  113 TYR   A H    1 
ATOM   2262 H HA   . TYR   A 1 113 ? 24.146 -10.860 0.620   1.00 11.75 ?  113 TYR   A HA   1 
ATOM   2263 H HB2  . TYR   A 1 113 ? 23.011 -12.667 -1.167  1.00 12.18 ?  113 TYR   A HB2  1 
ATOM   2264 H HB3  . TYR   A 1 113 ? 22.875 -12.977 0.383   1.00 12.18 ?  113 TYR   A HB3  1 
ATOM   2265 H HD1  . TYR   A 1 113 ? 21.938 -10.901 1.746   1.00 12.38 ?  113 TYR   A HD1  1 
ATOM   2266 H HD2  . TYR   A 1 113 ? 21.195 -11.561 -2.128  1.00 12.16 ?  113 TYR   A HD2  1 
ATOM   2267 H HE1  . TYR   A 1 113 ? 20.071 -9.550  1.882   1.00 12.53 ?  113 TYR   A HE1  1 
ATOM   2268 H HE2  . TYR   A 1 113 ? 19.309 -10.199 -2.000  1.00 12.64 ?  113 TYR   A HE2  1 
ATOM   2269 H HH   . TYR   A 1 113 ? 18.000 -8.893  -0.681  1.00 13.25 ?  113 TYR   A HH   1 
ATOM   2270 N N    . GLU   A 1 114 ? 26.215 -13.140 -0.157  1.00 9.72  ?  114 GLU   A N    1 
ATOM   2271 C CA   . GLU   A 1 114 ? 27.203 -14.048 0.434   1.00 9.90  ?  114 GLU   A CA   1 
ATOM   2272 C C    . GLU   A 1 114 ? 28.058 -13.346 1.484   1.00 10.14 ?  114 GLU   A C    1 
ATOM   2273 O O    . GLU   A 1 114 ? 28.536 -13.984 2.433   1.00 10.03 ?  114 GLU   A O    1 
ATOM   2274 C CB   . GLU   A 1 114 ? 28.073 -14.686 -0.657  1.00 10.07 ?  114 GLU   A CB   1 
ATOM   2275 C CG   . GLU   A 1 114 ? 27.311 -15.746 -1.442  1.00 10.45 ?  114 GLU   A CG   1 
ATOM   2276 C CD   . GLU   A 1 114 ? 28.016 -16.279 -2.684  1.00 10.38 ?  114 GLU   A CD   1 
ATOM   2277 O OE1  . GLU   A 1 114 ? 28.972 -15.648 -3.178  1.00 10.58 ?  114 GLU   A OE1  1 
ATOM   2278 O OE2  . GLU   A 1 114 ? 27.573 -17.345 -3.174  1.00 11.69 -1 114 GLU   A OE2  1 
ATOM   2279 H H    . GLU   A 1 114 ? 26.275 -13.043 -1.016  1.00 11.65 ?  114 GLU   A H    1 
ATOM   2280 H HA   . GLU   A 1 114 ? 26.731 -14.759 0.875   1.00 11.87 ?  114 GLU   A HA   1 
ATOM   2281 H HB2  . GLU   A 1 114 ? 28.362 -14.002 -1.287  1.00 12.07 ?  114 GLU   A HB2  1 
ATOM   2282 H HB3  . GLU   A 1 114 ? 28.842 -15.110 -0.251  1.00 12.07 ?  114 GLU   A HB3  1 
ATOM   2283 H HG2  . GLU   A 1 114 ? 27.139 -16.500 -0.855  1.00 12.54 ?  114 GLU   A HG2  1 
ATOM   2284 H HG3  . GLU   A 1 114 ? 26.462 -15.367 -1.732  1.00 12.54 ?  114 GLU   A HG3  1 
ATOM   2285 N N    . ASN   A 1 115 ? 28.247 -12.030 1.352   1.00 9.72  ?  115 ASN   A N    1 
ATOM   2286 C CA   . ASN   A 1 115 ? 29.024 -11.309 2.354   1.00 10.06 ?  115 ASN   A CA   1 
ATOM   2287 C C    . ASN   A 1 115 ? 28.411 -11.439 3.744   1.00 9.92  ?  115 ASN   A C    1 
ATOM   2288 O O    . ASN   A 1 115 ? 29.125 -11.369 4.751   1.00 10.13 ?  115 ASN   A O    1 
ATOM   2289 C CB   . ASN   A 1 115 ? 29.133 -9.832  1.976   1.00 10.24 ?  115 ASN   A CB   1 
ATOM   2290 C CG   . ASN   A 1 115 ? 29.927 -9.616  0.715   1.00 10.91 ?  115 ASN   A CG   1 
ATOM   2291 O OD1  . ASN   A 1 115 ? 31.145 -9.720  0.726   1.00 14.15 ?  115 ASN   A OD1  1 
ATOM   2292 N ND2  . ASN   A 1 115 ? 29.250 -9.315  -0.375  1.00 10.59 ?  115 ASN   A ND2  1 
ATOM   2293 H H    . ASN   A 1 115 ? 27.943 -11.537 0.711   1.00 11.65 ?  115 ASN   A H    1 
ATOM   2294 H HA   . ASN   A 1 115 ? 29.920 -11.677 2.386   1.00 12.06 ?  115 ASN   A HA   1 
ATOM   2295 H HB2  . ASN   A 1 115 ? 28.244 -9.472  1.842   1.00 12.28 ?  115 ASN   A HB2  1 
ATOM   2296 H HB3  . ASN   A 1 115 ? 29.577 -9.355  2.700   1.00 12.28 ?  115 ASN   A HB3  1 
ATOM   2297 H HD21 . ASN   A 1 115 ? 29.669 -9.181  -1.113  1.00 12.70 ?  115 ASN   A HD21 1 
ATOM   2298 H HD22 . ASN   A 1 115 ? 28.393 -9.277  -0.350  1.00 12.70 ?  115 ASN   A HD22 1 
ATOM   2299 N N    . PHE   A 1 116 ? 27.087 -11.599 3.824   1.00 10.01 ?  116 PHE   A N    1 
ATOM   2300 C CA   . PHE   A 1 116 ? 26.439 -11.693 5.129   1.00 9.72  ?  116 PHE   A CA   1 
ATOM   2301 C C    . PHE   A 1 116 ? 26.916 -12.923 5.899   1.00 10.08 ?  116 PHE   A C    1 
ATOM   2302 O O    . PHE   A 1 116 ? 26.838 -12.945 7.128   1.00 10.50 ?  116 PHE   A O    1 
ATOM   2303 C CB   . PHE   A 1 116 ? 24.911 -11.817 4.996   1.00 10.05 ?  116 PHE   A CB   1 
ATOM   2304 C CG   . PHE   A 1 116 ? 24.155 -10.567 4.539   1.00 9.46  ?  116 PHE   A CG   1 
ATOM   2305 C CD1  . PHE   A 1 116 ? 24.724 -9.550  3.780   1.00 9.71  ?  116 PHE   A CD1  1 
ATOM   2306 C CD2  . PHE   A 1 116 ? 22.801 -10.457 4.865   1.00 10.44 ?  116 PHE   A CD2  1 
ATOM   2307 C CE1  . PHE   A 1 116 ? 23.956 -8.466  3.367   1.00 9.98  ?  116 PHE   A CE1  1 
ATOM   2308 C CE2  . PHE   A 1 116 ? 22.036 -9.385  4.457   1.00 10.45 ?  116 PHE   A CE2  1 
ATOM   2309 C CZ   . PHE   A 1 116 ? 22.604 -8.386  3.709   1.00 9.90  ?  116 PHE   A CZ   1 
ATOM   2310 H H    . PHE   A 1 116 ? 26.551 -11.650 3.147   1.00 12.00 ?  116 PHE   A H    1 
ATOM   2311 H HA   . PHE   A 1 116 ? 26.638 -10.902 5.649   1.00 11.66 ?  116 PHE   A HA   1 
ATOM   2312 H HB2  . PHE   A 1 116 ? 24.717 -12.519 4.353   1.00 12.05 ?  116 PHE   A HB2  1 
ATOM   2313 H HB3  . PHE   A 1 116 ? 24.552 -12.070 5.861   1.00 12.05 ?  116 PHE   A HB3  1 
ATOM   2314 H HD1  . PHE   A 1 116 ? 25.614 -9.605  3.540   1.00 11.64 ?  116 PHE   A HD1  1 
ATOM   2315 H HD2  . PHE   A 1 116 ? 22.398 -11.136 5.360   1.00 12.52 ?  116 PHE   A HD2  1 
ATOM   2316 H HE1  . PHE   A 1 116 ? 24.348 -7.786  2.866   1.00 11.97 ?  116 PHE   A HE1  1 
ATOM   2317 H HE2  . PHE   A 1 116 ? 21.138 -9.339  4.696   1.00 12.54 ?  116 PHE   A HE2  1 
ATOM   2318 H HZ   . PHE   A 1 116 ? 22.098 -7.652  3.448   1.00 11.87 ?  116 PHE   A HZ   1 
ATOM   2319 N N    . ASN   A 1 117 ? 27.347 -13.977 5.197   1.00 10.30 ?  117 ASN   A N    1 
ATOM   2320 C CA   . ASN   A 1 117 ? 27.709 -15.225 5.865   1.00 10.26 ?  117 ASN   A CA   1 
ATOM   2321 C C    . ASN   A 1 117 ? 28.976 -15.113 6.697   1.00 11.04 ?  117 ASN   A C    1 
ATOM   2322 O O    . ASN   A 1 117 ? 29.266 -16.033 7.472   1.00 11.83 ?  117 ASN   A O    1 
ATOM   2323 C CB   . ASN   A 1 117 ? 27.825 -16.348 4.839   1.00 10.62 ?  117 ASN   A CB   1 
ATOM   2324 C CG   . ASN   A 1 117 ? 26.471 -16.734 4.304   1.00 10.38 ?  117 ASN   A CG   1 
ATOM   2325 O OD1  . ASN   A 1 117 ? 25.496 -16.761 5.058   1.00 11.29 ?  117 ASN   A OD1  1 
ATOM   2326 N ND2  . ASN   A 1 117 ? 26.384 -16.997 3.014   1.00 10.41 ?  117 ASN   A ND2  1 
ATOM   2327 H H    . ASN   A 1 117 ? 27.423 -13.997 4.335   1.00 12.36 ?  117 ASN   A H    1 
ATOM   2328 H HA   . ASN   A 1 117 ? 26.984 -15.461 6.464   1.00 12.31 ?  117 ASN   A HA   1 
ATOM   2329 H HB2  . ASN   A 1 117 ? 28.370 -16.049 4.092   1.00 12.73 ?  117 ASN   A HB2  1 
ATOM   2330 H HB3  . ASN   A 1 117 ? 28.218 -17.125 5.256   1.00 12.73 ?  117 ASN   A HB3  1 
ATOM   2331 H HD21 . ASN   A 1 117 ? 25.629 -17.214 2.672   1.00 12.49 ?  117 ASN   A HD21 1 
ATOM   2332 H HD22 . ASN   A 1 117 ? 27.087 -16.954 2.518   1.00 12.49 ?  117 ASN   A HD22 1 
ATOM   2333 N N    . GLN   A 1 118 ? 29.704 -14.004 6.584   1.00 10.85 ?  118 GLN   A N    1 
ATOM   2334 C CA   . GLN   A 1 118 ? 30.883 -13.774 7.403   1.00 11.22 ?  118 GLN   A CA   1 
ATOM   2335 C C    . GLN   A 1 118 ? 30.545 -13.199 8.773   1.00 11.50 ?  118 GLN   A C    1 
ATOM   2336 O O    . GLN   A 1 118 ? 31.463 -12.904 9.548   1.00 13.15 ?  118 GLN   A O    1 
ATOM   2337 C CB   . GLN   A 1 118 ? 31.876 -12.869 6.665   1.00 11.53 ?  118 GLN   A CB   1 
ATOM   2338 C CG   . GLN   A 1 118 ? 32.348 -13.450 5.339   1.00 11.71 ?  118 GLN   A CG   1 
ATOM   2339 C CD   . GLN   A 1 118 ? 33.172 -14.712 5.512   1.00 12.07 ?  118 GLN   A CD   1 
ATOM   2340 O OE1  . GLN   A 1 118 ? 34.037 -14.782 6.397   1.00 12.90 ?  118 GLN   A OE1  1 
ATOM   2341 N NE2  . GLN   A 1 118 ? 32.923 -15.713 4.660   1.00 11.68 ?  118 GLN   A NE2  1 
ATOM   2342 H H    . GLN   A 1 118 ? 29.523 -13.356 6.039   1.00 13.01 ?  118 GLN   A H    1 
ATOM   2343 H HA   . GLN   A 1 118 ? 31.315 -14.628 7.549   1.00 13.45 ?  118 GLN   A HA   1 
ATOM   2344 H HB2  . GLN   A 1 118 ? 31.450 -12.018 6.485   1.00 13.83 ?  118 GLN   A HB2  1 
ATOM   2345 H HB3  . GLN   A 1 118 ? 32.654 -12.738 7.230   1.00 13.83 ?  118 GLN   A HB3  1 
ATOM   2346 H HG2  . GLN   A 1 118 ? 31.580 -13.663 4.788   1.00 14.05 ?  118 GLN   A HG2  1 
ATOM   2347 H HG3  . GLN   A 1 118 ? 32.908 -12.796 4.887   1.00 14.05 ?  118 GLN   A HG3  1 
ATOM   2348 H HE21 . GLN   A 1 118 ? 32.309 -15.624 4.053   1.00 14.01 ?  118 GLN   A HE21 1 
ATOM   2349 H HE22 . GLN   A 1 118 ? 33.358 -16.453 4.710   1.00 14.01 ?  118 GLN   A HE22 1 
ATOM   2350 N N    . HIS   A 1 119 ? 29.259 -13.043 9.091   1.00 11.20 ?  119 HIS   A N    1 
ATOM   2351 C CA   . HIS   A 1 119 ? 28.816 -12.439 10.342  1.00 11.51 ?  119 HIS   A CA   1 
ATOM   2352 C C    . HIS   A 1 119 ? 27.680 -13.263 10.918  1.00 12.02 ?  119 HIS   A C    1 
ATOM   2353 O O    . HIS   A 1 119 ? 26.733 -13.589 10.204  1.00 12.02 ?  119 HIS   A O    1 
ATOM   2354 C CB   . HIS   A 1 119 ? 28.357 -11.006 10.071  1.00 12.42 ?  119 HIS   A CB   1 
ATOM   2355 C CG   . HIS   A 1 119 ? 29.438 -10.189 9.463   1.00 13.77 ?  119 HIS   A CG   1 
ATOM   2356 N ND1  . HIS   A 1 119 ? 30.416 -9.591  10.222  1.00 15.83 ?  119 HIS   A ND1  1 
ATOM   2357 C CD2  . HIS   A 1 119 ? 29.777 -9.984  8.171   1.00 14.51 ?  119 HIS   A CD2  1 
ATOM   2358 C CE1  . HIS   A 1 119 ? 31.285 -9.001  9.422   1.00 16.30 ?  119 HIS   A CE1  1 
ATOM   2359 N NE2  . HIS   A 1 119 ? 30.930 -9.238  8.172   1.00 16.18 ?  119 HIS   A NE2  1 
ATOM   2360 H H    . HIS   A 1 119 ? 28.606 -13.296 8.586   1.00 13.43 ?  119 HIS   A H    1 
ATOM   2361 H HA   . HIS   A 1 119 ? 29.549 -12.427 10.978  1.00 13.81 ?  119 HIS   A HA   1 
ATOM   2362 H HB2  . HIS   A 1 119 ? 27.607 -11.029 9.456   1.00 14.89 ?  119 HIS   A HB2  1 
ATOM   2363 H HB3  . HIS   A 1 119 ? 28.098 -10.597 10.907  1.00 14.89 ?  119 HIS   A HB3  1 
ATOM   2364 H HD1  . HIS   A 1 119 ? 30.446 -9.588  11.080  1.00 18.99 ?  119 HIS   A HD1  1 
ATOM   2365 H HD2  . HIS   A 1 119 ? 29.317 -10.289 7.419   1.00 17.40 ?  119 HIS   A HD2  1 
ATOM   2366 H HE1  . HIS   A 1 119 ? 32.022 -8.504  9.690   1.00 19.55 ?  119 HIS   A HE1  1 
ATOM   2367 N N    . GLU   A 1 120 ? 27.763 -13.580 12.210  1.00 12.70 ?  120 GLU   A N    1 
ATOM   2368 C CA   . GLU   A 1 120 ? 26.805 -14.508 12.804  1.00 15.00 ?  120 GLU   A CA   1 
ATOM   2369 C C    . GLU   A 1 120 ? 25.388 -13.940 12.873  1.00 13.55 ?  120 GLU   A C    1 
ATOM   2370 O O    . GLU   A 1 120 ? 24.413 -14.702 12.761  1.00 13.32 ?  120 GLU   A O    1 
ATOM   2371 C CB   . GLU   A 1 120 ? 27.283 -14.923 14.196  1.00 19.40 ?  120 GLU   A CB   1 
ATOM   2372 C CG   . GLU   A 1 120 ? 28.452 -15.893 14.169  1.00 25.16 ?  120 GLU   A CG   1 
ATOM   2373 C CD   . GLU   A 1 120 ? 28.670 -16.576 15.501  1.00 32.14 ?  120 GLU   A CD   1 
ATOM   2374 O OE1  . GLU   A 1 120 ? 28.106 -16.104 16.512  1.00 33.55 ?  120 GLU   A OE1  1 
ATOM   2375 O OE2  . GLU   A 1 120 ? 29.406 -17.585 15.538  1.00 36.91 -1 120 GLU   A OE2  1 
ATOM   2376 H H    . GLU   A 1 120 ? 28.360 -13.278 12.755  1.00 15.23 ?  120 GLU   A H    1 
ATOM   2377 H HA   . GLU   A 1 120 ? 26.775 -15.309 12.264  1.00 17.99 ?  120 GLU   A HA   1 
ATOM   2378 H HB2  . GLU   A 1 120 ? 27.569 -14.136 14.687  1.00 23.27 ?  120 GLU   A HB2  1 
ATOM   2379 H HB3  . GLU   A 1 120 ? 26.553 -15.357 14.668  1.00 23.27 ?  120 GLU   A HB3  1 
ATOM   2380 H HG2  . GLU   A 1 120 ? 28.290 -16.571 13.491  1.00 30.19 ?  120 GLU   A HG2  1 
ATOM   2381 H HG3  . GLU   A 1 120 ? 29.267 -15.411 13.967  1.00 30.19 ?  120 GLU   A HG3  1 
ATOM   2382 N N    . VAL   A 1 121 ? 25.256 -12.631 13.099  1.00 12.66 ?  121 VAL   A N    1 
ATOM   2383 C CA   . VAL   A 1 121 ? 23.965 -11.958 13.227  1.00 12.72 ?  121 VAL   A CA   1 
ATOM   2384 C C    . VAL   A 1 121 ? 24.081 -10.580 12.583  1.00 11.78 ?  121 VAL   A C    1 
ATOM   2385 O O    . VAL   A 1 121 ? 25.055 -9.859  12.824  1.00 12.34 ?  121 VAL   A O    1 
ATOM   2386 C CB   . VAL   A 1 121 ? 23.544 -11.803 14.707  1.00 15.74 ?  121 VAL   A CB   1 
ATOM   2387 C CG1  . VAL   A 1 121 ? 22.168 -11.151 14.810  1.00 16.27 ?  121 VAL   A CG1  1 
ATOM   2388 C CG2  . VAL   A 1 121 ? 23.556 -13.133 15.431  1.00 17.61 ?  121 VAL   A CG2  1 
ATOM   2389 H H    . VAL   A 1 121 ? 25.926 -12.094 13.182  1.00 15.18 ?  121 VAL   A H    1 
ATOM   2390 H HA   . VAL   A 1 121 ? 23.285 -12.469 12.763  1.00 15.25 ?  121 VAL   A HA   1 
ATOM   2391 H HB   . VAL   A 1 121 ? 24.178 -11.221 15.151  1.00 18.88 ?  121 VAL   A HB   1 
ATOM   2392 H HG11 . VAL   A 1 121 ? 21.861 -11.208 15.729  1.00 19.51 ?  121 VAL   A HG11 1 
ATOM   2393 H HG12 . VAL   A 1 121 ? 22.236 -10.220 14.544  1.00 19.51 ?  121 VAL   A HG12 1 
ATOM   2394 H HG13 . VAL   A 1 121 ? 21.551 -11.619 14.227  1.00 19.51 ?  121 VAL   A HG13 1 
ATOM   2395 H HG21 . VAL   A 1 121 ? 23.212 -13.006 16.334  1.00 21.12 ?  121 VAL   A HG21 1 
ATOM   2396 H HG22 . VAL   A 1 121 ? 22.985 -13.760 14.954  1.00 21.12 ?  121 VAL   A HG22 1 
ATOM   2397 H HG23 . VAL   A 1 121 ? 24.460 -13.471 15.468  1.00 21.12 ?  121 VAL   A HG23 1 
ATOM   2398 N N    . LEU   A 1 122 ? 23.071 -10.191 11.796  1.00 11.20 ?  122 LEU   A N    1 
ATOM   2399 C CA   . LEU   A 1 122 ? 23.075 -8.888  11.139  1.00 10.95 ?  122 LEU   A CA   1 
ATOM   2400 C C    . LEU   A 1 122 ? 21.680 -8.291  11.094  1.00 10.73 ?  122 LEU   A C    1 
ATOM   2401 O O    . LEU   A 1 122 ? 20.690 -9.012  10.956  1.00 11.89 ?  122 LEU   A O    1 
ATOM   2402 C CB   . LEU   A 1 122 ? 23.503 -8.975  9.668   1.00 12.53 ?  122 LEU   A CB   1 
ATOM   2403 C CG   . LEU   A 1 122 ? 24.704 -9.836  9.304   1.00 12.24 ?  122 LEU   A CG   1 
ATOM   2404 C CD1  . LEU   A 1 122 ? 24.294 -11.281 9.074   1.00 13.03 ?  122 LEU   A CD1  1 
ATOM   2405 C CD2  . LEU   A 1 122 ? 25.388 -9.266  8.067   1.00 11.76 ?  122 LEU   A CD2  1 
ATOM   2406 H H    . LEU   A 1 122 ? 22.369 -10.664 11.633  1.00 13.43 ?  122 LEU   A H    1 
ATOM   2407 H HA   . LEU   A 1 122 ? 23.669 -8.277  11.608  1.00 13.14 ?  122 LEU   A HA   1 
ATOM   2408 H HB2  . LEU   A 1 122 ? 22.759 -9.316  9.158   1.00 15.03 ?  122 LEU   A HB2  1 
ATOM   2409 H HB3  . LEU   A 1 122 ? 23.713 -8.076  9.364   1.00 15.03 ?  122 LEU   A HB3  1 
ATOM   2410 H HG   . LEU   A 1 122 ? 25.352 -9.821  10.030  1.00 14.68 ?  122 LEU   A HG   1 
ATOM   2411 H HD11 . LEU   A 1 122 ? 25.066 -11.793 8.788   1.00 15.62 ?  122 LEU   A HD11 1 
ATOM   2412 H HD12 . LEU   A 1 122 ? 23.946 -11.647 9.903   1.00 15.62 ?  122 LEU   A HD12 1 
ATOM   2413 H HD13 . LEU   A 1 122 ? 23.608 -11.308 8.388   1.00 15.62 ?  122 LEU   A HD13 1 
ATOM   2414 H HD21 . LEU   A 1 122 ? 26.125 -9.845  7.810   1.00 14.10 ?  122 LEU   A HD21 1 
ATOM   2415 H HD22 . LEU   A 1 122 ? 24.742 -9.215  7.345   1.00 14.10 ?  122 LEU   A HD22 1 
ATOM   2416 H HD23 . LEU   A 1 122 ? 25.725 -8.378  8.271   1.00 14.10 ?  122 LEU   A HD23 1 
ATOM   2417 N N    A LEU   A 1 123 ? 21.620 -6.961  11.161  0.40 10.79 ?  123 LEU   A N    1 
ATOM   2418 N N    B LEU   A 1 123 ? 21.626 -6.965  11.235  0.60 10.21 ?  123 LEU   A N    1 
ATOM   2419 C CA   A LEU   A 1 123 ? 20.454 -6.182  10.756  0.40 10.53 ?  123 LEU   A CA   1 
ATOM   2420 C CA   B LEU   A 1 123 ? 20.458 -6.153  10.913  0.60 9.80  ?  123 LEU   A CA   1 
ATOM   2421 C C    A LEU   A 1 123 ? 20.713 -5.665  9.347   0.40 9.94  ?  123 LEU   A C    1 
ATOM   2422 C C    B LEU   A 1 123 ? 20.686 -5.604  9.511   0.60 9.47  ?  123 LEU   A C    1 
ATOM   2423 O O    A LEU   A 1 123 ? 21.813 -5.186  9.054   0.40 9.53  ?  123 LEU   A O    1 
ATOM   2424 O O    B LEU   A 1 123 ? 21.695 -4.929  9.276   0.60 9.80  ?  123 LEU   A O    1 
ATOM   2425 C CB   A LEU   A 1 123 ? 20.268 -4.992  11.701  0.40 11.13 ?  123 LEU   A CB   1 
ATOM   2426 C CB   B LEU   A 1 123 ? 20.353 -4.996  11.907  0.60 10.45 ?  123 LEU   A CB   1 
ATOM   2427 C CG   A LEU   A 1 123 ? 19.196 -3.958  11.356  0.40 11.77 ?  123 LEU   A CG   1 
ATOM   2428 C CG   B LEU   A 1 123 ? 19.354 -3.899  11.539  0.60 11.20 ?  123 LEU   A CG   1 
ATOM   2429 C CD1  A LEU   A 1 123 ? 17.816 -4.590  11.352  0.40 12.23 ?  123 LEU   A CD1  1 
ATOM   2430 C CD1  B LEU   A 1 123 ? 17.935 -4.449  11.515  0.60 11.85 ?  123 LEU   A CD1  1 
ATOM   2431 C CD2  A LEU   A 1 123 ? 19.252 -2.794  12.342  0.40 12.05 ?  123 LEU   A CD2  1 
ATOM   2432 C CD2  B LEU   A 1 123 ? 19.468 -2.731  12.499  0.60 11.72 ?  123 LEU   A CD2  1 
ATOM   2433 H H    A LEU   A 1 123 ? 22.270 -6.473  11.443  0.40 12.94 ?  123 LEU   A H    1 
ATOM   2434 H H    B LEU   A 1 123 ? 22.288 -6.492  11.514  0.60 12.24 ?  123 LEU   A H    1 
ATOM   2435 H HA   A LEU   A 1 123 ? 19.656 -6.736  10.762  0.40 12.63 ?  123 LEU   A HA   1 
ATOM   2436 H HA   B LEU   A 1 123 ? 19.644 -6.680  10.933  0.60 11.75 ?  123 LEU   A HA   1 
ATOM   2437 H HB2  A LEU   A 1 123 ? 20.045 -5.338  12.579  0.40 13.35 ?  123 LEU   A HB2  1 
ATOM   2438 H HB2  B LEU   A 1 123 ? 20.079 -5.355  12.770  0.60 12.53 ?  123 LEU   A HB2  1 
ATOM   2439 H HB3  A LEU   A 1 123 ? 21.108 -4.516  11.750  0.40 13.35 ?  123 LEU   A HB3  1 
ATOM   2440 H HB3  B LEU   A 1 123 ? 21.222 -4.578  11.994  0.60 12.53 ?  123 LEU   A HB3  1 
ATOM   2441 H HG   A LEU   A 1 123 ? 19.367 -3.603  10.470  0.40 14.12 ?  123 LEU   A HG   1 
ATOM   2442 H HG   B LEU   A 1 123 ? 19.555 -3.562  10.653  0.60 13.43 ?  123 LEU   A HG   1 
ATOM   2443 H HD11 A LEU   A 1 123 ? 17.151 -3.897  11.217  0.40 14.66 ?  123 LEU   A HD11 1 
ATOM   2444 H HD11 B LEU   A 1 123 ? 17.316 -3.727  11.332  0.60 14.21 ?  123 LEU   A HD11 1 
ATOM   2445 H HD12 A LEU   A 1 123 ? 17.769 -5.238  10.634  0.40 14.66 ?  123 LEU   A HD12 1 
ATOM   2446 H HD12 B LEU   A 1 123 ? 17.869 -5.126  10.820  0.60 14.21 ?  123 LEU   A HD12 1 
ATOM   2447 H HD13 A LEU   A 1 123 ? 17.667 -5.028  12.206  0.40 14.66 ?  123 LEU   A HD13 1 
ATOM   2448 H HD13 B LEU   A 1 123 ? 17.735 -4.846  12.379  0.60 14.21 ?  123 LEU   A HD13 1 
ATOM   2449 H HD21 A LEU   A 1 123 ? 18.567 -2.148  12.110  0.40 14.45 ?  123 LEU   A HD21 1 
ATOM   2450 H HD21 B LEU   A 1 123 ? 18.826 -2.050  12.245  0.60 14.06 ?  123 LEU   A HD21 1 
ATOM   2451 H HD22 A LEU   A 1 123 ? 19.096 -3.133  13.239  0.40 14.45 ?  123 LEU   A HD22 1 
ATOM   2452 H HD22 B LEU   A 1 123 ? 19.279 -3.044  13.398  0.60 14.06 ?  123 LEU   A HD22 1 
ATOM   2453 H HD23 A LEU   A 1 123 ? 20.128 -2.380  12.295  0.40 14.45 ?  123 LEU   A HD23 1 
ATOM   2454 H HD23 B LEU   A 1 123 ? 20.367 -2.374  12.454  0.60 14.06 ?  123 LEU   A HD23 1 
ATOM   2455 N N    A ALA   A 1 124 ? 19.709 -5.747  8.470   0.40 9.70  ?  124 ALA   A N    1 
ATOM   2456 N N    B ALA   A 1 124 ? 19.776 -5.882  8.583   0.60 9.51  ?  124 ALA   A N    1 
ATOM   2457 C CA   A ALA   A 1 124 ? 20.004 -5.519  7.061   0.40 9.52  ?  124 ALA   A CA   1 
ATOM   2458 C CA   B ALA   A 1 124 ? 20.034 -5.575  7.185   0.60 9.58  ?  124 ALA   A CA   1 
ATOM   2459 C C    A ALA   A 1 124 ? 18.755 -5.124  6.289   0.40 9.30  ?  124 ALA   A C    1 
ATOM   2460 C C    B ALA   A 1 124 ? 18.815 -5.012  6.470   0.60 9.18  ?  124 ALA   A C    1 
ATOM   2461 O O    A ALA   A 1 124 ? 17.638 -5.505  6.664   0.40 9.57  ?  124 ALA   A O    1 
ATOM   2462 O O    B ALA   A 1 124 ? 17.670 -5.273  6.861   0.60 9.95  ?  124 ALA   A O    1 
ATOM   2463 C CB   A ALA   A 1 124 ? 20.624 -6.771  6.433   0.40 10.12 ?  124 ALA   A CB   1 
ATOM   2464 C CB   B ALA   A 1 124 ? 20.511 -6.818  6.423   0.60 9.81  ?  124 ALA   A CB   1 
ATOM   2465 H H    A ALA   A 1 124 ? 18.886 -5.911  8.661   0.40 11.63 ?  124 ALA   A H    1 
ATOM   2466 H H    B ALA   A 1 124 ? 19.015 -6.254  8.732   0.60 11.40 ?  124 ALA   A H    1 
ATOM   2467 H HA   A ALA   A 1 124 ? 20.646 -4.801  6.995   0.40 11.42 ?  124 ALA   A HA   1 
ATOM   2468 H HA   B ALA   A 1 124 ? 20.747 -4.918  7.146   0.60 11.48 ?  124 ALA   A HA   1 
ATOM   2469 H HB1  A ALA   A 1 124 ? 20.810 -6.596  5.498   0.40 12.14 ?  124 ALA   A HB1  1 
ATOM   2470 H HB1  B ALA   A 1 124 ? 20.673 -6.585  5.492   0.60 11.76 ?  124 ALA   A HB1  1 
ATOM   2471 H HB2  A ALA   A 1 124 ? 21.451 -6.977  6.900   0.40 12.14 ?  124 ALA   A HB2  1 
ATOM   2472 H HB2  B ALA   A 1 124 ? 21.341 -7.141  6.821   0.60 11.76 ?  124 ALA   A HB2  1 
ATOM   2473 H HB3  A ALA   A 1 124 ? 20.004 -7.509  6.517   0.40 12.14 ?  124 ALA   A HB3  1 
ATOM   2474 H HB3  B ALA   A 1 124 ? 19.834 -7.508  6.475   0.60 11.76 ?  124 ALA   A HB3  1 
ATOM   2475 N N    A PRO   A 1 125 ? 18.924 -4.388  5.183   0.40 9.43  ?  125 PRO   A N    1 
ATOM   2476 N N    B PRO   A 1 125 ? 19.043 -4.261  5.393   0.60 9.09  ?  125 PRO   A N    1 
ATOM   2477 C CA   A PRO   A 1 125 ? 17.834 -4.166  4.236   0.40 9.28  ?  125 PRO   A CA   1 
ATOM   2478 C CA   B PRO   A 1 125 ? 17.978 -3.895  4.465   0.60 9.45  ?  125 PRO   A CA   1 
ATOM   2479 C C    A PRO   A 1 125 ? 17.897 -5.172  3.103   0.40 8.78  ?  125 PRO   A C    1 
ATOM   2480 C C    B PRO   A 1 125 ? 17.900 -4.940  3.358   0.60 9.41  ?  125 PRO   A C    1 
ATOM   2481 O O    A PRO   A 1 125 ? 18.889 -5.893  2.946   0.40 8.78  ?  125 PRO   A O    1 
ATOM   2482 O O    B PRO   A 1 125 ? 18.728 -5.851  3.263   0.60 9.74  ?  125 PRO   A O    1 
ATOM   2483 C CB   A PRO   A 1 125 ? 18.167 -2.776  3.698   0.40 9.72  ?  125 PRO   A CB   1 
ATOM   2484 C CB   B PRO   A 1 125 ? 18.513 -2.582  3.891   0.60 9.62  ?  125 PRO   A CB   1 
ATOM   2485 C CG   A PRO   A 1 125 ? 19.665 -2.818  3.598   0.40 10.22 ?  125 PRO   A CG   1 
ATOM   2486 C CG   B PRO   A 1 125 ? 20.003 -2.881  3.726   0.60 9.14  ?  125 PRO   A CG   1 
ATOM   2487 C CD   A PRO   A 1 125 ? 20.123 -3.619  4.805   0.40 10.04 ?  125 PRO   A CD   1 
ATOM   2488 C CD   B PRO   A 1 125 ? 20.355 -3.772  4.919   0.60 9.48  ?  125 PRO   A CD   1 
ATOM   2489 H HA   A PRO   A 1 125 ? 16.958 -4.178  4.663   0.40 11.13 ?  125 PRO   A HA   1 
ATOM   2490 H HA   B PRO   A 1 125 ? 17.121 -3.770  4.910   0.60 11.33 ?  125 PRO   A HA   1 
ATOM   2491 H HB2  A PRO   A 1 125 ? 17.758 -2.656  2.836   0.40 11.65 ?  125 PRO   A HB2  1 
ATOM   2492 H HB2  B PRO   A 1 125 ? 18.087 -2.393  3.041   0.60 11.54 ?  125 PRO   A HB2  1 
ATOM   2493 H HB3  A PRO   A 1 125 ? 17.881 -2.098  4.320   0.40 11.65 ?  125 PRO   A HB3  1 
ATOM   2494 H HB3  B PRO   A 1 125 ? 18.364 -1.856  4.522   0.60 11.54 ?  125 PRO   A HB3  1 
ATOM   2495 H HG2  A PRO   A 1 125 ? 19.921 -3.263  2.774   0.40 12.25 ?  125 PRO   A HG2  1 
ATOM   2496 H HG2  B PRO   A 1 125 ? 20.149 -3.353  2.889   0.60 10.96 ?  125 PRO   A HG2  1 
ATOM   2497 H HG3  A PRO   A 1 125 ? 20.014 -1.919  3.629   0.40 12.25 ?  125 PRO   A HG3  1 
ATOM   2498 H HG3  B PRO   A 1 125 ? 20.507 -2.055  3.747   0.60 10.96 ?  125 PRO   A HG3  1 
ATOM   2499 H HD2  A PRO   A 1 125 ? 20.847 -4.215  4.564   0.40 12.04 ?  125 PRO   A HD2  1 
ATOM   2500 H HD2  B PRO   A 1 125 ? 20.914 -4.508  4.632   0.60 11.37 ?  125 PRO   A HD2  1 
ATOM   2501 H HD3  A PRO   A 1 125 ? 20.370 -3.027  5.531   0.40 12.04 ?  125 PRO   A HD3  1 
ATOM   2502 H HD3  B PRO   A 1 125 ? 20.790 -3.242  5.608   0.60 11.37 ?  125 PRO   A HD3  1 
ATOM   2503 N N    A LEU   A 1 126 ? 16.851 -5.199  2.285   0.40 8.93  ?  126 LEU   A N    1 
ATOM   2504 N N    B LEU   A 1 126 ? 16.894 -4.769  2.505   0.60 10.16 ?  126 LEU   A N    1 
ATOM   2505 C CA   A LEU   A 1 126 ? 16.866 -6.008  1.077   0.40 9.19  ?  126 LEU   A CA   1 
ATOM   2506 C CA   B LEU   A 1 126 ? 16.728 -5.607  1.322   0.60 10.66 ?  126 LEU   A CA   1 
ATOM   2507 C C    A LEU   A 1 126 ? 17.799 -5.379  0.049   0.40 9.55  ?  126 LEU   A C    1 
ATOM   2508 C C    B LEU   A 1 126 ? 17.630 -5.080  0.208   0.60 10.26 ?  126 LEU   A C    1 
ATOM   2509 O O    A LEU   A 1 126 ? 17.579 -4.247  -0.400  0.40 10.32 ?  126 LEU   A O    1 
ATOM   2510 O O    B LEU   A 1 126 ? 17.360 -4.021  -0.373  0.60 11.21 ?  126 LEU   A O    1 
ATOM   2511 C CB   A LEU   A 1 126 ? 15.454 -6.123  0.520   0.40 9.26  ?  126 LEU   A CB   1 
ATOM   2512 C CB   B LEU   A 1 126 ? 15.262 -5.582  0.900   0.60 13.15 ?  126 LEU   A CB   1 
ATOM   2513 C CG   A LEU   A 1 126 ? 14.539 -7.037  1.336   0.40 10.10 ?  126 LEU   A CG   1 
ATOM   2514 C CG   B LEU   A 1 126 ? 14.754 -6.689  -0.020  0.60 15.24 ?  126 LEU   A CG   1 
ATOM   2515 C CD1  A LEU   A 1 126 ? 13.116 -6.921  0.831   0.40 11.05 ?  126 LEU   A CD1  1 
ATOM   2516 C CD1  B LEU   A 1 126 ? 14.918 -8.051  0.625   0.60 15.72 ?  126 LEU   A CD1  1 
ATOM   2517 C CD2  A LEU   A 1 126 ? 15.025 -8.484  1.270   0.40 9.91  ?  126 LEU   A CD2  1 
ATOM   2518 C CD2  B LEU   A 1 126 ? 13.297 -6.441  -0.364  0.60 15.99 ?  126 LEU   A CD2  1 
ATOM   2519 H H    A LEU   A 1 126 ? 16.135 -4.743  2.400   0.40 10.70 ?  126 LEU   A H    1 
ATOM   2520 H H    B LEU   A 1 126 ? 16.280 -4.166  2.590   0.60 12.19 ?  126 LEU   A H    1 
ATOM   2521 H HA   A LEU   A 1 126 ? 17.192 -6.899  1.282   0.40 11.02 ?  126 LEU   A HA   1 
ATOM   2522 H HA   B LEU   A 1 126 ? 16.982 -6.517  1.532   0.60 12.78 ?  126 LEU   A HA   1 
ATOM   2523 H HB2  A LEU   A 1 126 ? 15.049 -5.240  0.509   0.40 11.11 ?  126 LEU   A HB2  1 
ATOM   2524 H HB2  B LEU   A 1 126 ? 14.721 -5.619  1.703   0.60 15.78 ?  126 LEU   A HB2  1 
ATOM   2525 H HB3  A LEU   A 1 126 ? 15.493 -6.476  -0.382  0.40 11.11 ?  126 LEU   A HB3  1 
ATOM   2526 H HB3  B LEU   A 1 126 ? 15.097 -4.742  0.445   0.60 15.78 ?  126 LEU   A HB3  1 
ATOM   2527 H HG   A LEU   A 1 126 ? 14.551 -6.757  2.264   0.40 12.11 ?  126 LEU   A HG   1 
ATOM   2528 H HG   B LEU   A 1 126 ? 15.265 -6.677  -0.846  0.60 18.28 ?  126 LEU   A HG   1 
ATOM   2529 H HD11 A LEU   A 1 126 ? 12.547 -7.509  1.352   0.40 13.25 ?  126 LEU   A HD11 1 
ATOM   2530 H HD11 B LEU   A 1 126 ? 14.449 -8.710  0.091   0.60 18.85 ?  126 LEU   A HD11 1 
ATOM   2531 H HD12 A LEU   A 1 126 ? 12.821 -6.003  0.926   0.40 13.25 ?  126 LEU   A HD12 1 
ATOM   2532 H HD12 B LEU   A 1 126 ? 15.862 -8.269  0.667   0.60 18.85 ?  126 LEU   A HD12 1 
ATOM   2533 H HD13 A LEU   A 1 126 ? 13.092 -7.182  -0.104  0.40 13.25 ?  126 LEU   A HD13 1 
ATOM   2534 H HD13 B LEU   A 1 126 ? 14.543 -8.022  1.519   0.60 18.85 ?  126 LEU   A HD13 1 
ATOM   2535 H HD21 A LEU   A 1 126 ? 14.327 -9.068  1.601   0.40 11.88 ?  126 LEU   A HD21 1 
ATOM   2536 H HD21 B LEU   A 1 126 ? 12.989 -7.148  -0.952  0.60 19.18 ?  126 LEU   A HD21 1 
ATOM   2537 H HD22 A LEU   A 1 126 ? 15.231 -8.704  0.347   0.40 11.88 ?  126 LEU   A HD22 1 
ATOM   2538 H HD22 B LEU   A 1 126 ? 12.778 -6.440  0.455   0.60 19.18 ?  126 LEU   A HD22 1 
ATOM   2539 H HD23 A LEU   A 1 126 ? 15.821 -8.575  1.816   0.40 11.88 ?  126 LEU   A HD23 1 
ATOM   2540 H HD23 B LEU   A 1 126 ? 13.219 -5.582  -0.808  0.60 19.18 ?  126 LEU   A HD23 1 
ATOM   2541 N N    A LEU   A 1 127 ? 18.838 -6.120  -0.324  0.40 9.81  ?  127 LEU   A N    1 
ATOM   2542 N N    B LEU   A 1 127 ? 18.704 -5.811  -0.094  0.60 9.98  ?  127 LEU   A N    1 
ATOM   2543 C CA   A LEU   A 1 127 ? 19.831 -5.611  -1.255  0.40 9.32  ?  127 LEU   A CA   1 
ATOM   2544 C CA   B LEU   A 1 127 ? 19.680 -5.340  -1.068  0.60 10.10 ?  127 LEU   A CA   1 
ATOM   2545 C C    A LEU   A 1 127 ? 19.222 -5.417  -2.634  0.40 9.28  ?  127 LEU   A C    1 
ATOM   2546 C C    B LEU   A 1 127 ? 19.066 -5.246  -2.458  0.60 9.99  ?  127 LEU   A C    1 
ATOM   2547 O O    A LEU   A 1 127 ? 18.393 -6.209  -3.093  0.40 8.75  ?  127 LEU   A O    1 
ATOM   2548 O O    B LEU   A 1 127 ? 18.220 -6.053  -2.854  0.60 10.75 ?  127 LEU   A O    1 
ATOM   2549 C CB   A LEU   A 1 127 ? 21.001 -6.586  -1.344  0.40 9.64  ?  127 LEU   A CB   1 
ATOM   2550 C CB   B LEU   A 1 127 ? 20.890 -6.277  -1.112  0.60 11.00 ?  127 LEU   A CB   1 
ATOM   2551 C CG   A LEU   A 1 127 ? 21.741 -6.861  -0.037  0.40 9.80  ?  127 LEU   A CG   1 
ATOM   2552 C CG   B LEU   A 1 127 ? 21.765 -6.346  0.145   0.60 11.37 ?  127 LEU   A CG   1 
ATOM   2553 C CD1  A LEU   A 1 127 ? 22.862 -7.838  -0.310  0.40 9.42  ?  127 LEU   A CD1  1 
ATOM   2554 C CD1  B LEU   A 1 127 ? 22.901 -7.334  -0.057  0.60 11.99 ?  127 LEU   A CD1  1 
ATOM   2555 C CD2  A LEU   A 1 127 ? 22.278 -5.575  0.562   0.40 9.98  ?  127 LEU   A CD2  1 
ATOM   2556 C CD2  B LEU   A 1 127 ? 22.315 -4.975  0.531   0.60 11.99 ?  127 LEU   A CD2  1 
ATOM   2557 H H    A LEU   A 1 127 ? 18.993 -6.926  -0.048  0.40 11.76 ?  127 LEU   A H    1 
ATOM   2558 H H    B LEU   A 1 127 ? 18.894 -6.582  0.251   0.60 11.97 ?  127 LEU   A H    1 
ATOM   2559 H HA   A LEU   A 1 127 ? 20.167 -4.759  -0.940  0.40 11.18 ?  127 LEU   A HA   1 
ATOM   2560 H HA   B LEU   A 1 127 ? 19.986 -4.458  -0.811  0.60 12.12 ?  127 LEU   A HA   1 
ATOM   2561 H HB2  A LEU   A 1 127 ? 20.673 -7.439  -1.665  0.40 11.56 ?  127 LEU   A HB2  1 
ATOM   2562 H HB2  B LEU   A 1 127 ? 20.571 -7.177  -1.288  0.60 13.19 ?  127 LEU   A HB2  1 
ATOM   2563 H HB3  A LEU   A 1 127 ? 21.655 -6.234  -1.967  0.40 11.56 ?  127 LEU   A HB3  1 
ATOM   2564 H HB3  B LEU   A 1 127 ? 21.464 -5.997  -1.843  0.60 13.19 ?  127 LEU   A HB3  1 
ATOM   2565 H HG   A LEU   A 1 127 ? 21.130 -7.267  0.604   0.40 11.75 ?  127 LEU   A HG   1 
ATOM   2566 H HG   B LEU   A 1 127 ? 21.225 -6.670  0.882   0.60 13.63 ?  127 LEU   A HG   1 
ATOM   2567 H HD11 A LEU   A 1 127 ? 23.313 -8.047  0.522   0.40 11.30 ?  127 LEU   A HD11 1 
ATOM   2568 H HD11 B LEU   A 1 127 ? 23.444 -7.358  0.749   0.60 14.38 ?  127 LEU   A HD11 1 
ATOM   2569 H HD12 A LEU   A 1 127 ? 22.488 -8.647  -0.696  0.40 11.30 ?  127 LEU   A HD12 1 
ATOM   2570 H HD12 B LEU   A 1 127 ? 22.530 -8.213  -0.230  0.60 14.38 ?  127 LEU   A HD12 1 
ATOM   2571 H HD13 A LEU   A 1 127 ? 23.484 -7.433  -0.934  0.40 11.30 ?  127 LEU   A HD13 1 
ATOM   2572 H HD13 B LEU   A 1 127 ? 23.441 -7.046  -0.809  0.60 14.38 ?  127 LEU   A HD13 1 
ATOM   2573 H HD21 A LEU   A 1 127 ? 22.865 -5.789  1.301   0.40 11.96 ?  127 LEU   A HD21 1 
ATOM   2574 H HD21 B LEU   A 1 127 ? 22.950 -5.083  1.257   0.60 14.38 ?  127 LEU   A HD21 1 
ATOM   2575 H HD22 A LEU   A 1 127 ? 22.769 -5.094  -0.124  0.40 11.96 ?  127 LEU   A HD22 1 
ATOM   2576 H HD22 B LEU   A 1 127 ? 22.758 -4.585  -0.239  0.60 14.38 ?  127 LEU   A HD22 1 
ATOM   2577 H HD23 A LEU   A 1 127 ? 21.534 -5.035  0.873   0.40 11.96 ?  127 LEU   A HD23 1 
ATOM   2578 H HD23 B LEU   A 1 127 ? 21.581 -4.410  0.814   0.60 14.38 ?  127 LEU   A HD23 1 
ATOM   2579 N N    A SER   A 1 128 ? 19.656 -4.353  -3.301  0.40 9.91  ?  128 SER   A N    1 
ATOM   2580 N N    B SER   A 1 128 ? 19.515 -4.237  -3.200  0.60 9.52  ?  128 SER   A N    1 
ATOM   2581 C CA   A SER   A 1 128 ? 19.246 -3.969  -4.644  0.40 10.30 ?  128 SER   A CA   1 
ATOM   2582 C CA   B SER   A 1 128 ? 19.139 -3.957  -4.582  0.60 9.80  ?  128 SER   A CA   1 
ATOM   2583 C C    A SER   A 1 128 ? 17.788 -3.527  -4.728  0.40 10.18 ?  128 SER   A C    1 
ATOM   2584 C C    B SER   A 1 128 ? 17.676 -3.562  -4.757  0.60 9.82  ?  128 SER   A C    1 
ATOM   2585 O O    A SER   A 1 128 ? 17.330 -3.186  -5.821  0.40 10.34 ?  128 SER   A O    1 
ATOM   2586 O O    B SER   A 1 128 ? 17.237 -3.375  -5.895  0.60 11.35 ?  128 SER   A O    1 
ATOM   2587 C CB   A SER   A 1 128 ? 19.569 -5.032  -5.706  0.40 10.64 ?  128 SER   A CB   1 
ATOM   2588 C CB   B SER   A 1 128 ? 19.541 -5.073  -5.554  0.60 9.68  ?  128 SER   A CB   1 
ATOM   2589 O OG   A SER   A 1 128 ? 20.969 -5.284  -5.753  0.40 11.12 ?  128 SER   A OG   1 
ATOM   2590 O OG   B SER   A 1 128 ? 20.959 -5.183  -5.618  0.60 10.33 ?  128 SER   A OG   1 
ATOM   2591 H H    A SER   A 1 128 ? 20.235 -3.808  -2.970  0.40 11.89 ?  128 SER   A H    1 
ATOM   2592 H H    B SER   A 1 128 ? 20.091 -3.669  -2.903  0.60 11.42 ?  128 SER   A H    1 
ATOM   2593 H HA   A SER   A 1 128 ? 19.774 -3.199  -4.879  0.40 12.35 ?  128 SER   A HA   1 
ATOM   2594 H HA   B SER   A 1 128 ? 19.659 -3.186  -4.852  0.60 11.75 ?  128 SER   A HA   1 
ATOM   2595 H HB2  A SER   A 1 128 ? 19.107 -5.855  -5.493  0.40 12.76 ?  128 SER   A HB2  1 
ATOM   2596 H HB2  B SER   A 1 128 ? 19.165 -5.913  -5.252  0.60 11.61 ?  128 SER   A HB2  1 
ATOM   2597 H HB3  A SER   A 1 128 ? 19.280 -4.705  -6.576  0.40 12.76 ?  128 SER   A HB3  1 
ATOM   2598 H HB3  B SER   A 1 128 ? 19.192 -4.858  -6.443  0.60 11.61 ?  128 SER   A HB3  1 
ATOM   2599 H HG   A SER   A 1 128 ? 21.381 -4.574  -5.938  0.40 13.33 ?  128 SER   A HG   1 
ATOM   2600 H HG   B SER   A 1 128 ? 21.287 -4.456  -5.891  0.60 12.39 ?  128 SER   A HG   1 
ATOM   2601 N N    A ALA   A 1 129 ? 17.058 -3.488  -3.612  0.40 11.08 ?  129 ALA   A N    1 
ATOM   2602 N N    B ALA   A 1 129 ? 16.924 -3.398  -3.671  0.60 10.20 ?  129 ALA   A N    1 
ATOM   2603 C CA   A ALA   A 1 129 ? 15.686 -2.994  -3.592  0.40 11.77 ?  129 ALA   A CA   1 
ATOM   2604 C CA   B ALA   A 1 129 ? 15.539 -2.963  -3.753  0.60 10.83 ?  129 ALA   A CA   1 
ATOM   2605 C C    A ALA   A 1 129 ? 15.684 -1.467  -3.568  0.40 11.80 ?  129 ALA   A C    1 
ATOM   2606 C C    B ALA   A 1 129 ? 15.480 -1.433  -3.799  0.60 10.47 ?  129 ALA   A C    1 
ATOM   2607 O O    A ALA   A 1 129 ? 16.728 -0.813  -3.648  0.40 12.19 ?  129 ALA   A O    1 
ATOM   2608 O O    B ALA   A 1 129 ? 16.501 -0.753  -3.916  0.60 10.99 ?  129 ALA   A O    1 
ATOM   2609 C CB   A ALA   A 1 129 ? 14.929 -3.564  -2.394  0.40 12.48 ?  129 ALA   A CB   1 
ATOM   2610 C CB   B ALA   A 1 129 ? 14.725 -3.555  -2.602  0.60 11.36 ?  129 ALA   A CB   1 
ATOM   2611 H H    A ALA   A 1 129 ? 17.337 -3.753  -2.843  0.40 13.29 ?  129 ALA   A H    1 
ATOM   2612 H H    B ALA   A 1 129 ? 17.196 -3.536  -2.865  0.60 12.24 ?  129 ALA   A H    1 
ATOM   2613 H HA   A ALA   A 1 129 ? 15.234 -3.278  -4.399  0.40 14.11 ?  129 ALA   A HA   1 
ATOM   2614 H HA   B ALA   A 1 129 ? 15.158 -3.291  -4.579  0.60 12.98 ?  129 ALA   A HA   1 
ATOM   2615 H HB1  A ALA   A 1 129 ? 14.015 -3.234  -2.413  0.40 14.97 ?  129 ALA   A HB1  1 
ATOM   2616 H HB1  B ALA   A 1 129 ? 13.803 -3.262  -2.682  0.60 13.62 ?  129 ALA   A HB1  1 
ATOM   2617 H HB2  A ALA   A 1 129 ? 14.933 -4.529  -2.447  0.40 14.97 ?  129 ALA   A HB2  1 
ATOM   2618 H HB2  B ALA   A 1 129 ? 14.769 -4.522  -2.650  0.60 13.62 ?  129 ALA   A HB2  1 
ATOM   2619 H HB3  A ALA   A 1 129 ? 15.366 -3.273  -1.577  0.40 14.97 ?  129 ALA   A HB3  1 
ATOM   2620 H HB3  B ALA   A 1 129 ? 15.096 -3.248  -1.759  0.60 13.62 ?  129 ALA   A HB3  1 
ATOM   2621 N N    A GLY   A 1 130 ? 14.495 -0.885  -3.444  0.40 12.01 ?  130 GLY   A N    1 
ATOM   2622 N N    B GLY   A 1 130 ? 14.273 -0.882  -3.718  0.60 10.59 ?  130 GLY   A N    1 
ATOM   2623 C CA   A GLY   A 1 130 ? 14.392 0.563   -3.383  0.40 12.53 ?  130 GLY   A CA   1 
ATOM   2624 C CA   B GLY   A 1 130 ? 14.117 0.563   -3.742  0.60 10.73 ?  130 GLY   A CA   1 
ATOM   2625 C C    A GLY   A 1 130 ? 14.977 1.200   -4.628  0.40 12.44 ?  130 GLY   A C    1 
ATOM   2626 C C    B GLY   A 1 130 ? 14.773 1.177   -4.960  0.60 10.78 ?  130 GLY   A C    1 
ATOM   2627 O O    A GLY   A 1 130 ? 14.720 0.766   -5.756  0.40 12.36 ?  130 GLY   A O    1 
ATOM   2628 O O    B GLY   A 1 130 ? 14.587 0.715   -6.091  0.60 11.15 ?  130 GLY   A O    1 
ATOM   2629 H H    A GLY   A 1 130 ? 13.748 -1.306  -3.392  0.40 14.40 ?  130 GLY   A H    1 
ATOM   2630 H H    B GLY   A 1 130 ? 13.538 -1.320  -3.651  0.60 12.70 ?  130 GLY   A H    1 
ATOM   2631 H HA2  A GLY   A 1 130 ? 13.457 0.817   -3.299  0.40 15.03 ?  130 GLY   A HA2  1 
ATOM   2632 H HA2  B GLY   A 1 130 ? 13.173 0.789   -3.736  0.60 12.87 ?  130 GLY   A HA2  1 
ATOM   2633 H HA3  A GLY   A 1 130 ? 14.873 0.896   -2.610  0.40 15.03 ?  130 GLY   A HA3  1 
ATOM   2634 H HA3  B GLY   A 1 130 ? 14.527 0.951   -2.958  0.60 12.87 ?  130 GLY   A HA3  1 
ATOM   2635 N N    A ILE   A 1 131 ? 15.790 2.241   -4.428  0.40 12.37 ?  131 ILE   A N    1 
ATOM   2636 N N    B ILE   A 1 131 ? 15.561 2.233   -4.735  0.60 10.92 ?  131 ILE   A N    1 
ATOM   2637 C CA   A ILE   A 1 131 ? 16.338 3.004   -5.547  0.40 11.94 ?  131 ILE   A CA   1 
ATOM   2638 C CA   B ILE   A 1 131 ? 16.146 3.010   -5.826  0.60 11.12 ?  131 ILE   A CA   1 
ATOM   2639 C C    A ILE   A 1 131 ? 17.340 2.220   -6.385  0.40 11.58 ?  131 ILE   A C    1 
ATOM   2640 C C    B ILE   A 1 131 ? 17.295 2.273   -6.515  0.60 11.25 ?  131 ILE   A C    1 
ATOM   2641 O O    A ILE   A 1 131 ? 17.700 2.680   -7.475  0.40 12.01 ?  131 ILE   A O    1 
ATOM   2642 O O    B ILE   A 1 131 ? 17.870 2.787   -7.482  0.60 11.70 ?  131 ILE   A O    1 
ATOM   2643 C CB   A ILE   A 1 131 ? 16.937 4.351   -5.086  0.40 12.85 ?  131 ILE   A CB   1 
ATOM   2644 C CB   B ILE   A 1 131 ? 16.550 4.436   -5.391  0.60 11.44 ?  131 ILE   A CB   1 
ATOM   2645 C CG1  A ILE   A 1 131 ? 18.182 4.131   -4.221  0.40 13.54 ?  131 ILE   A CG1  1 
ATOM   2646 C CG1  B ILE   A 1 131 ? 17.738 4.416   -4.418  0.60 11.60 ?  131 ILE   A CG1  1 
ATOM   2647 C CG2  A ILE   A 1 131 ? 15.898 5.168   -4.331  0.40 13.32 ?  131 ILE   A CG2  1 
ATOM   2648 C CG2  B ILE   A 1 131 ? 15.347 5.174   -4.797  0.60 11.28 ?  131 ILE   A CG2  1 
ATOM   2649 C CD1  A ILE   A 1 131 ? 18.833 5.425   -3.744  0.40 14.47 ?  131 ILE   A CD1  1 
ATOM   2650 C CD1  B ILE   A 1 131 ? 18.250 5.807   -4.053  0.60 12.01 ?  131 ILE   A CD1  1 
ATOM   2651 H H    A ILE   A 1 131 ? 16.025 2.526   -3.656  0.40 14.84 ?  131 ILE   A H    1 
ATOM   2652 H H    B ILE   A 1 131 ? 15.761 2.527   -3.949  0.60 13.10 ?  131 ILE   A H    1 
ATOM   2653 H HA   A ILE   A 1 131 ? 15.603 3.221   -6.141  0.40 14.32 ?  131 ILE   A HA   1 
ATOM   2654 H HA   B ILE   A 1 131 ? 15.455 3.121   -6.494  0.60 13.33 ?  131 ILE   A HA   1 
ATOM   2655 H HB   A ILE   A 1 131 ? 17.195 4.853   -5.875  0.40 15.41 ?  131 ILE   A HB   1 
ATOM   2656 H HB   B ILE   A 1 131 ? 16.829 4.917   -6.184  0.60 13.72 ?  131 ILE   A HB   1 
ATOM   2657 H HG12 A ILE   A 1 131 ? 17.931 3.619   -3.439  0.40 16.24 ?  131 ILE   A HG12 1 
ATOM   2658 H HG12 B ILE   A 1 131 ? 17.470 3.972   -3.600  0.60 13.91 ?  131 ILE   A HG12 1 
ATOM   2659 H HG13 A ILE   A 1 131 ? 18.843 3.647   -4.738  0.40 16.24 ?  131 ILE   A HG13 1 
ATOM   2660 H HG13 B ILE   A 1 131 ? 18.476 3.932   -4.827  0.60 13.91 ?  131 ILE   A HG13 1 
ATOM   2661 H HG21 A ILE   A 1 131 ? 16.224 6.075   -4.222  0.40 15.98 ?  131 ILE   A HG21 1 
ATOM   2662 H HG21 B ILE   A 1 131 ? 15.585 6.104   -4.651  0.60 13.53 ?  131 ILE   A HG21 1 
ATOM   2663 H HG22 A ILE   A 1 131 ? 15.072 5.174   -4.839  0.40 15.98 ?  131 ILE   A HG22 1 
ATOM   2664 H HG22 B ILE   A 1 131 ? 14.606 5.120   -5.421  0.60 13.53 ?  131 ILE   A HG22 1 
ATOM   2665 H HG23 A ILE   A 1 131 ? 15.749 4.762   -3.463  0.40 15.98 ?  131 ILE   A HG23 1 
ATOM   2666 H HG23 B ILE   A 1 131 ? 15.103 4.758   -3.957  0.60 13.53 ?  131 ILE   A HG23 1 
ATOM   2667 H HD11 A ILE   A 1 131 ? 19.685 5.217   -3.331  0.40 17.36 ?  131 ILE   A HD11 1 
ATOM   2668 H HD11 B ILE   A 1 131 ? 19.070 5.715   -3.542  0.60 14.41 ?  131 ILE   A HD11 1 
ATOM   2669 H HD12 A ILE   A 1 131 ? 18.970 6.012   -4.506  0.40 17.36 ?  131 ILE   A HD12 1 
ATOM   2670 H HD12 B ILE   A 1 131 ? 18.420 6.302   -4.868  0.60 14.41 ?  131 ILE   A HD12 1 
ATOM   2671 H HD13 A ILE   A 1 131 ? 18.250 5.858   -3.099  0.40 17.36 ?  131 ILE   A HD13 1 
ATOM   2672 H HD13 B ILE   A 1 131 ? 17.577 6.258   -3.522  0.60 14.41 ?  131 ILE   A HD13 1 
ATOM   2673 N N    A PHE   A 1 132 ? 17.801 1.052   -5.924  0.40 10.99 ?  132 PHE   A N    1 
ATOM   2674 N N    B PHE   A 1 132 ? 17.641 1.066   -6.042  0.60 11.13 ?  132 PHE   A N    1 
ATOM   2675 C CA   A PHE   A 1 132 ? 18.670 0.224   -6.753  0.40 10.82 ?  132 PHE   A CA   1 
ATOM   2676 C CA   B PHE   A 1 132 ? 18.538 0.209   -6.812  0.60 11.22 ?  132 PHE   A CA   1 
ATOM   2677 C C    A PHE   A 1 132 ? 17.907 -0.519  -7.850  0.40 11.52 ?  132 PHE   A C    1 
ATOM   2678 C C    B PHE   A 1 132 ? 17.813 -0.557  -7.918  0.60 12.01 ?  132 PHE   A C    1 
ATOM   2679 O O    A PHE   A 1 132 ? 18.542 -1.114  -8.727  0.40 12.47 ?  132 PHE   A O    1 
ATOM   2680 O O    B PHE   A 1 132 ? 18.469 -1.200  -8.744  0.60 12.88 ?  132 PHE   A O    1 
ATOM   2681 C CB   A PHE   A 1 132 ? 19.477 -0.765  -5.900  0.40 9.79  ?  132 PHE   A CB   1 
ATOM   2682 C CB   B PHE   A 1 132 ? 19.277 -0.782  -5.906  0.60 10.81 ?  132 PHE   A CB   1 
ATOM   2683 C CG   A PHE   A 1 132 ? 20.717 -0.178  -5.247  0.40 9.34  ?  132 PHE   A CG   1 
ATOM   2684 C CG   B PHE   A 1 132 ? 20.490 -0.218  -5.205  0.60 10.64 ?  132 PHE   A CG   1 
ATOM   2685 C CD1  A PHE   A 1 132 ? 20.625 0.840   -4.309  0.40 10.34 ?  132 PHE   A CD1  1 
ATOM   2686 C CD1  B PHE   A 1 132 ? 20.377 0.838   -4.318  0.60 11.56 ?  132 PHE   A CD1  1 
ATOM   2687 C CD2  A PHE   A 1 132 ? 21.974 -0.694  -5.534  0.40 9.72  ?  132 PHE   A CD2  1 
ATOM   2688 C CD2  B PHE   A 1 132 ? 21.739 -0.798  -5.385  0.60 11.30 ?  132 PHE   A CD2  1 
ATOM   2689 C CE1  A PHE   A 1 132 ? 21.768 1.349   -3.696  0.40 10.75 ?  132 PHE   A CE1  1 
ATOM   2690 C CE1  B PHE   A 1 132 ? 21.491 1.329   -3.654  0.60 11.75 ?  132 PHE   A CE1  1 
ATOM   2691 C CE2  A PHE   A 1 132 ? 23.117 -0.186  -4.923  0.40 10.57 ?  132 PHE   A CE2  1 
ATOM   2692 C CE2  B PHE   A 1 132 ? 22.854 -0.315  -4.719  0.60 11.45 ?  132 PHE   A CE2  1 
ATOM   2693 C CZ   A PHE   A 1 132 ? 23.008 0.833   -4.003  0.40 10.83 ?  132 PHE   A CZ   1 
ATOM   2694 C CZ   B PHE   A 1 132 ? 22.728 0.751   -3.852  0.60 11.25 ?  132 PHE   A CZ   1 
ATOM   2695 H H    A PHE   A 1 132 ? 17.626 0.726   -5.149  0.40 13.18 ?  132 PHE   A H    1 
ATOM   2696 H H    B PHE   A 1 132 ? 17.385 0.737   -5.285  0.60 13.35 ?  132 PHE   A H    1 
ATOM   2697 H HA   A PHE   A 1 132 ? 19.310 0.804   -7.193  0.40 12.97 ?  132 PHE   A HA   1 
ATOM   2698 H HA   B PHE   A 1 132 ? 19.212 0.773   -7.225  0.60 13.45 ?  132 PHE   A HA   1 
ATOM   2699 H HB2  A PHE   A 1 132 ? 18.908 -1.099  -5.190  0.40 11.74 ?  132 PHE   A HB2  1 
ATOM   2700 H HB2  B PHE   A 1 132 ? 18.667 -1.091  -5.219  0.60 12.97 ?  132 PHE   A HB2  1 
ATOM   2701 H HB3  A PHE   A 1 132 ? 19.765 -1.502  -6.463  0.40 11.74 ?  132 PHE   A HB3  1 
ATOM   2702 H HB3  B PHE   A 1 132 ? 19.574 -1.532  -6.444  0.60 12.97 ?  132 PHE   A HB3  1 
ATOM   2703 H HD1  A PHE   A 1 132 ? 19.795 1.195   -4.092  0.40 12.39 ?  132 PHE   A HD1  1 
ATOM   2704 H HD1  B PHE   A 1 132 ? 19.547 1.232   -4.174  0.60 13.86 ?  132 PHE   A HD1  1 
ATOM   2705 H HD2  A PHE   A 1 132 ? 22.058 -1.386  -6.151  0.40 11.65 ?  132 PHE   A HD2  1 
ATOM   2706 H HD2  B PHE   A 1 132 ? 21.830 -1.520  -5.966  0.60 13.55 ?  132 PHE   A HD2  1 
ATOM   2707 H HE1  A PHE   A 1 132 ? 21.696 2.040   -3.076  0.40 12.90 ?  132 PHE   A HE1  1 
ATOM   2708 H HE1  B PHE   A 1 132 ? 21.404 2.047   -3.070  0.60 14.09 ?  132 PHE   A HE1  1 
ATOM   2709 H HE2  A PHE   A 1 132 ? 23.951 -0.541  -5.136  0.40 12.67 ?  132 PHE   A HE2  1 
ATOM   2710 H HE2  B PHE   A 1 132 ? 23.685 -0.710  -4.866  0.60 13.74 ?  132 PHE   A HE2  1 
ATOM   2711 H HZ   A PHE   A 1 132 ? 23.773 1.176   -3.597  0.40 12.99 ?  132 PHE   A HZ   1 
ATOM   2712 H HZ   B PHE   A 1 132 ? 23.475 1.082   -3.413  0.60 13.49 ?  132 PHE   A HZ   1 
ATOM   2713 N N    A GLY   A 1 133 ? 16.573 -0.511  -7.826  0.40 11.57 ?  133 GLY   A N    1 
ATOM   2714 N N    B GLY   A 1 133 ? 16.485 -0.530  -7.945  0.60 12.57 ?  133 GLY   A N    1 
ATOM   2715 C CA   A GLY   A 1 133 ? 15.785 -0.867  -8.989  0.40 11.83 ?  133 GLY   A CA   1 
ATOM   2716 C CA   B GLY   A 1 133 ? 15.748 -0.902  -9.136  0.60 13.11 ?  133 GLY   A CA   1 
ATOM   2717 C C    A GLY   A 1 133 ? 15.330 -2.310  -9.099  0.40 11.64 ?  133 GLY   A C    1 
ATOM   2718 C C    B GLY   A 1 133 ? 15.494 -2.379  -9.370  0.60 12.99 ?  133 GLY   A C    1 
ATOM   2719 O O    A GLY   A 1 133 ? 14.547 -2.615  -10.007 0.40 12.15 ?  133 GLY   A O    1 
ATOM   2720 O O    B GLY   A 1 133 ? 14.936 -2.717  -10.420 0.60 13.25 ?  133 GLY   A O    1 
ATOM   2721 H H    A GLY   A 1 133 ? 16.099 -0.290  -7.143  0.40 13.87 ?  133 GLY   A H    1 
ATOM   2722 H H    B GLY   A 1 133 ? 15.992 -0.284  -7.284  0.60 15.07 ?  133 GLY   A H    1 
ATOM   2723 H HA2  A GLY   A 1 133 ? 14.987 -0.314  -9.006  0.40 14.19 ?  133 GLY   A HA2  1 
ATOM   2724 H HA2  B GLY   A 1 133 ? 14.886 -0.463  -9.108  0.60 15.72 ?  133 GLY   A HA2  1 
ATOM   2725 H HA3  A GLY   A 1 133 ? 16.295 -0.667  -9.791  0.40 14.19 ?  133 GLY   A HA3  1 
ATOM   2726 H HA3  B GLY   A 1 133 ? 16.227 -0.559  -9.910  0.60 15.72 ?  133 GLY   A HA3  1 
ATOM   2727 N N    A ALA   A 1 134 ? 15.781 -3.210  -8.229  0.40 11.34 ?  134 ALA   A N    1 
ATOM   2728 N N    B ALA   A 1 134 ? 15.871 -3.270  -8.453  0.60 12.66 ?  134 ALA   A N    1 
ATOM   2729 C CA   A ALA   A 1 134 ? 15.400 -4.609  -8.359  0.40 11.43 ?  134 ALA   A CA   1 
ATOM   2730 C CA   B ALA   A 1 134 ? 15.593 -4.687  -8.648  0.60 13.16 ?  134 ALA   A CA   1 
ATOM   2731 C C    A ALA   A 1 134 ? 14.063 -4.880  -7.679  0.40 11.39 ?  134 ALA   A C    1 
ATOM   2732 C C    B ALA   A 1 134 ? 14.234 -5.061  -8.056  0.60 12.72 ?  134 ALA   A C    1 
ATOM   2733 O O    A ALA   A 1 134 ? 13.590 -4.104  -6.846  0.40 12.05 ?  134 ALA   A O    1 
ATOM   2734 O O    B ALA   A 1 134 ? 13.613 -4.295  -7.317  0.60 13.28 ?  134 ALA   A O    1 
ATOM   2735 C CB   A ALA   A 1 134 ? 16.459 -5.530  -7.763  0.40 11.52 ?  134 ALA   A CB   1 
ATOM   2736 C CB   B ALA   A 1 134 ? 16.700 -5.552  -8.045  0.60 14.11 ?  134 ALA   A CB   1 
ATOM   2737 H H    A ALA   A 1 134 ? 16.300 -3.036  -7.565  0.40 13.60 ?  134 ALA   A H    1 
ATOM   2738 H H    B ALA   A 1 134 ? 16.290 -3.081  -7.720  0.60 15.18 ?  134 ALA   A H    1 
ATOM   2739 H HA   A ALA   A 1 134 ? 15.307 -4.817  -9.303  0.40 13.71 ?  134 ALA   A HA   1 
ATOM   2740 H HA   B ALA   A 1 134 ? 15.563 -4.870  -9.599  0.60 15.79 ?  134 ALA   A HA   1 
ATOM   2741 H HB1  A ALA   A 1 134 ? 16.175 -6.447  -7.886  0.40 13.81 ?  134 ALA   A HB1  1 
ATOM   2742 H HB1  B ALA   A 1 134 ? 16.502 -6.483  -8.227  0.60 16.93 ?  134 ALA   A HB1  1 
ATOM   2743 H HB2  A ALA   A 1 134 ? 17.296 -5.372  -8.221  0.40 13.81 ?  134 ALA   A HB2  1 
ATOM   2744 H HB2  B ALA   A 1 134 ? 17.547 -5.308  -8.452  0.60 16.93 ?  134 ALA   A HB2  1 
ATOM   2745 H HB3  A ALA   A 1 134 ? 16.548 -5.330  -6.820  0.40 13.81 ?  134 ALA   A HB3  1 
ATOM   2746 H HB3  B ALA   A 1 134 ? 16.736 -5.399  -7.090  0.60 16.93 ?  134 ALA   A HB3  1 
ATOM   2747 N N    A ASP   A 1 135 ? 13.463 -6.007  -8.050  0.40 11.38 ?  135 ASP   A N    1 
ATOM   2748 N N    B ASP   A 1 135 ? 13.775 -6.262  -8.401  0.60 13.15 ?  135 ASP   A N    1 
ATOM   2749 C CA   A ASP   A 1 135 ? 12.223 -6.464  -7.438  0.40 11.90 ?  135 ASP   A CA   1 
ATOM   2750 C CA   B ASP   A 1 135 ? 12.512 -6.791  -7.889  0.60 13.35 ?  135 ASP   A CA   1 
ATOM   2751 C C    A ASP   A 1 135 ? 12.509 -6.909  -6.008  0.40 11.75 ?  135 ASP   A C    1 
ATOM   2752 C C    B ASP   A 1 135 ? 12.684 -7.186  -6.428  0.60 12.77 ?  135 ASP   A C    1 
ATOM   2753 O O    A ASP   A 1 135 ? 13.277 -7.859  -5.809  0.40 11.47 ?  135 ASP   A O    1 
ATOM   2754 O O    B ASP   A 1 135 ? 13.503 -8.065  -6.129  0.60 12.81 ?  135 ASP   A O    1 
ATOM   2755 C CB   A ASP   A 1 135 ? 11.686 -7.639  -8.250  0.40 13.86 ?  135 ASP   A CB   1 
ATOM   2756 C CB   B ASP   A 1 135 ? 12.125 -8.018  -8.712  0.60 16.06 ?  135 ASP   A CB   1 
ATOM   2757 C CG   A ASP   A 1 135 ? 10.340 -8.139  -7.747  0.40 15.81 ?  135 ASP   A CG   1 
ATOM   2758 C CG   B ASP   A 1 135 ? 10.864 -8.712  -8.199  0.60 18.11 ?  135 ASP   A CG   1 
ATOM   2759 O OD1  A ASP   A 1 135 ? 9.893  -7.688  -6.669  0.40 15.80 ?  135 ASP   A OD1  1 
ATOM   2760 O OD1  B ASP   A 1 135 ? 10.267 -8.255  -7.203  0.60 18.82 ?  135 ASP   A OD1  1 
ATOM   2761 O OD2  A ASP   A 1 135 ? 9.719  -8.972  -8.444  0.40 17.68 -1 135 ASP   A OD2  1 
ATOM   2762 O OD2  B ASP   A 1 135 ? 10.472 -9.731  -8.803  0.60 20.12 -1 135 ASP   A OD2  1 
ATOM   2763 H H    A ASP   A 1 135 ? 13.751 -6.528  -8.666  0.40 13.65 ?  135 ASP   A H    1 
ATOM   2764 H H    B ASP   A 1 135 ? 14.181 -6.795  -8.940  0.60 15.77 ?  135 ASP   A H    1 
ATOM   2765 H HA   A ASP   A 1 135 ? 11.555 -5.753  -7.449  0.40 14.28 ?  135 ASP   A HA   1 
ATOM   2766 H HA   B ASP   A 1 135 ? 11.819 -6.121  -7.977  0.60 16.01 ?  135 ASP   A HA   1 
ATOM   2767 H HB2  A ASP   A 1 135 ? 11.563 -7.360  -9.169  0.40 16.63 ?  135 ASP   A HB2  1 
ATOM   2768 H HB2  B ASP   A 1 135 ? 11.974 -7.746  -9.631  0.60 19.26 ?  135 ASP   A HB2  1 
ATOM   2769 H HB3  A ASP   A 1 135 ? 12.336 -8.363  -8.210  0.40 16.63 ?  135 ASP   A HB3  1 
ATOM   2770 H HB3  B ASP   A 1 135 ? 12.850 -8.664  -8.675  0.60 19.26 ?  135 ASP   A HB3  1 
ATOM   2771 N N    A PRO   A 1 136 ? 11.937 -6.260  -4.991  0.40 11.40 ?  136 PRO   A N    1 
ATOM   2772 N N    B PRO   A 1 136 ? 11.949 -6.578  -5.492  0.60 12.84 ?  136 PRO   A N    1 
ATOM   2773 C CA   A PRO   A 1 136 ? 12.228 -6.674  -3.607  0.40 11.32 ?  136 PRO   A CA   1 
ATOM   2774 C CA   B PRO   A 1 136 ? 12.156 -6.918  -4.074  0.60 12.48 ?  136 PRO   A CA   1 
ATOM   2775 C C    A PRO   A 1 136 ? 11.789 -8.093  -3.283  0.40 10.73 ?  136 PRO   A C    1 
ATOM   2776 C C    B PRO   A 1 136 ? 11.769 -8.342  -3.715  0.60 11.88 ?  136 PRO   A C    1 
ATOM   2777 O O    A PRO   A 1 136 ? 12.378 -8.721  -2.395  0.40 10.38 ?  136 PRO   A O    1 
ATOM   2778 O O    B PRO   A 1 136 ? 12.399 -8.925  -2.825  0.60 11.78 ?  136 PRO   A O    1 
ATOM   2779 C CB   A PRO   A 1 136 ? 11.492 -5.624  -2.762  0.40 11.97 ?  136 PRO   A CB   1 
ATOM   2780 C CB   B PRO   A 1 136 ? 11.300 -5.882  -3.333  0.60 12.99 ?  136 PRO   A CB   1 
ATOM   2781 C CG   A PRO   A 1 136 ? 10.453 -5.064  -3.670  0.40 12.32 ?  136 PRO   A CG   1 
ATOM   2782 C CG   B PRO   A 1 136 ? 10.266 -5.463  -4.334  0.60 13.52 ?  136 PRO   A CG   1 
ATOM   2783 C CD   A PRO   A 1 136 ? 11.041 -5.093  -5.040  0.40 11.79 ?  136 PRO   A CD   1 
ATOM   2784 C CD   B PRO   A 1 136 ? 10.943 -5.517  -5.669  0.60 13.43 ?  136 PRO   A CD   1 
ATOM   2785 H HA   A PRO   A 1 136 ? 13.179 -6.592  -3.435  0.40 13.57 ?  136 PRO   A HA   1 
ATOM   2786 H HA   B PRO   A 1 136 ? 13.087 -6.784  -3.833  0.60 14.97 ?  136 PRO   A HA   1 
ATOM   2787 H HB2  A PRO   A 1 136 ? 11.080 -6.047  -1.994  0.40 14.36 ?  136 PRO   A HB2  1 
ATOM   2788 H HB2  B PRO   A 1 136 ? 10.885 -6.296  -2.558  0.60 15.58 ?  136 PRO   A HB2  1 
ATOM   2789 H HB3  A PRO   A 1 136 ? 12.110 -4.928  -2.484  0.40 14.36 ?  136 PRO   A HB3  1 
ATOM   2790 H HB3  B PRO   A 1 136 ? 11.854 -5.132  -3.066  0.60 15.58 ?  136 PRO   A HB3  1 
ATOM   2791 H HG2  A PRO   A 1 136 ? 9.661  -5.622  -3.639  0.40 14.78 ?  136 PRO   A HG2  1 
ATOM   2792 H HG2  B PRO   A 1 136 ? 9.519  -6.078  -4.306  0.60 16.21 ?  136 PRO   A HG2  1 
ATOM   2793 H HG3  A PRO   A 1 136 ? 10.244 -4.155  -3.411  0.40 14.78 ?  136 PRO   A HG3  1 
ATOM   2794 H HG3  B PRO   A 1 136 ? 9.977  -4.559  -4.138  0.60 16.21 ?  136 PRO   A HG3  1 
ATOM   2795 H HD2  A PRO   A 1 136 ? 10.342 -5.228  -5.704  0.40 14.14 ?  136 PRO   A HD2  1 
ATOM   2796 H HD2  B PRO   A 1 136 ? 10.310 -5.770  -6.361  0.60 16.11 ?  136 PRO   A HD2  1 
ATOM   2797 H HD3  A PRO   A 1 136 ? 11.543 -4.281  -5.217  0.40 14.14 ?  136 PRO   A HD3  1 
ATOM   2798 H HD3  B PRO   A 1 136 ? 11.373 -4.672  -5.873  0.60 16.11 ?  136 PRO   A HD3  1 
ATOM   2799 N N    A ILE   A 1 137 ? 10.764 -8.611  -3.963  0.40 11.10 ?  137 ILE   A N    1 
ATOM   2800 N N    B ILE   A 1 137 ? 10.749 -8.917  -4.359  0.60 11.62 ?  137 ILE   A N    1 
ATOM   2801 C CA   A ILE   A 1 137 ? 10.381 -10.008 -3.775  0.40 11.57 ?  137 ILE   A CA   1 
ATOM   2802 C CA   B ILE   A 1 137 ? 10.412 -10.316 -4.104  0.60 12.39 ?  137 ILE   A CA   1 
ATOM   2803 C C    A ILE   A 1 137 ? 11.528 -10.922 -4.184  0.40 11.20 ?  137 ILE   A C    1 
ATOM   2804 C C    B ILE   A 1 137 ? 11.591 -11.208 -4.456  0.60 12.20 ?  137 ILE   A C    1 
ATOM   2805 O O    A ILE   A 1 137 ? 11.834 -11.910 -3.505  0.40 11.55 ?  137 ILE   A O    1 
ATOM   2806 O O    B ILE   A 1 137 ? 11.924 -12.150 -3.725  0.60 12.61 ?  137 ILE   A O    1 
ATOM   2807 C CB   A ILE   A 1 137 ? 9.088  -10.315 -4.556  0.40 12.05 ?  137 ILE   A CB   1 
ATOM   2808 C CB   B ILE   A 1 137 ? 9.139  -10.717 -4.875  0.60 13.54 ?  137 ILE   A CB   1 
ATOM   2809 C CG1  A ILE   A 1 137 ? 7.934  -9.442  -4.051  0.40 12.86 ?  137 ILE   A CG1  1 
ATOM   2810 C CG1  B ILE   A 1 137 ? 7.917  -9.975  -4.328  0.60 14.60 ?  137 ILE   A CG1  1 
ATOM   2811 C CG2  A ILE   A 1 137 ? 8.724  -11.792 -4.447  0.40 12.06 ?  137 ILE   A CG2  1 
ATOM   2812 C CG2  B ILE   A 1 137 ? 8.922  -12.228 -4.795  0.60 13.91 ?  137 ILE   A CG2  1 
ATOM   2813 C CD1  A ILE   A 1 137 ? 6.661  -9.604  -4.843  0.40 13.90 ?  137 ILE   A CD1  1 
ATOM   2814 C CD1  B ILE   A 1 137 ? 6.667  -10.156 -5.167  0.60 15.61 ?  137 ILE   A CD1  1 
ATOM   2815 H H    A ILE   A 1 137 ? 10.281 -8.174  -4.529  0.40 13.31 ?  137 ILE   A H    1 
ATOM   2816 H H    B ILE   A 1 137 ? 10.246 -8.526  -4.937  0.60 13.94 ?  137 ILE   A H    1 
ATOM   2817 H HA   A ILE   A 1 137 ? 10.200 -10.156 -2.836  0.40 13.88 ?  137 ILE   A HA   1 
ATOM   2818 H HA   B ILE   A 1 137 ? 10.231 -10.430 -3.162  0.60 14.86 ?  137 ILE   A HA   1 
ATOM   2819 H HB   A ILE   A 1 137 ? 9.236  -10.103 -5.490  0.40 14.45 ?  137 ILE   A HB   1 
ATOM   2820 H HB   B ILE   A 1 137 ? 9.248  -10.476 -5.806  0.60 16.24 ?  137 ILE   A HB   1 
ATOM   2821 H HG12 A ILE   A 1 137 ? 7.743  -9.673  -3.129  0.40 15.42 ?  137 ILE   A HG12 1 
ATOM   2822 H HG12 B ILE   A 1 137 ? 7.722  -10.303 -3.435  0.60 17.51 ?  137 ILE   A HG12 1 
ATOM   2823 H HG13 A ILE   A 1 137 ? 8.194  -8.507  -4.107  0.40 15.42 ?  137 ILE   A HG13 1 
ATOM   2824 H HG13 B ILE   A 1 137 ? 8.116  -9.027  -4.293  0.60 17.51 ?  137 ILE   A HG13 1 
ATOM   2825 H HG21 A ILE   A 1 137 ? 7.863  -11.946 -4.863  0.40 14.46 ?  137 ILE   A HG21 1 
ATOM   2826 H HG21 B ILE   A 1 137 ? 8.046  -12.453 -5.147  0.60 16.68 ?  137 ILE   A HG21 1 
ATOM   2827 H HG22 A ILE   A 1 137 ? 9.401  -12.315 -4.900  0.40 14.46 ?  137 ILE   A HG22 1 
ATOM   2828 H HG22 B ILE   A 1 137 ? 9.600  -12.676 -5.323  0.60 16.68 ?  137 ILE   A HG22 1 
ATOM   2829 H HG23 A ILE   A 1 137 ? 8.687  -12.035 -3.510  0.40 14.46 ?  137 ILE   A HG23 1 
ATOM   2830 H HG23 B ILE   A 1 137 ? 8.983  -12.507 -3.869  0.60 16.68 ?  137 ILE   A HG23 1 
ATOM   2831 H HD11 A ILE   A 1 137 ? 5.981  -10.003 -4.275  0.40 16.67 ?  137 ILE   A HD11 1 
ATOM   2832 H HD11 B ILE   A 1 137 ? 5.951  -9.644  -4.766  0.60 18.73 ?  137 ILE   A HD11 1 
ATOM   2833 H HD12 A ILE   A 1 137 ? 6.374  -8.733  -5.147  0.40 16.67 ?  137 ILE   A HD12 1 
ATOM   2834 H HD12 B ILE   A 1 137 ? 6.845  -9.834  -6.066  0.60 18.73 ?  137 ILE   A HD12 1 
ATOM   2835 H HD13 A ILE   A 1 137 ? 6.831  -10.177 -5.609  0.40 16.67 ?  137 ILE   A HD13 1 
ATOM   2836 H HD13 B ILE   A 1 137 ? 6.426  -11.092 -5.190  0.60 18.73 ?  137 ILE   A HD13 1 
ATOM   2837 N N    A HIS   A 1 138 ? 12.186 -10.595 -5.298  0.40 11.29 ?  138 HIS   A N    1 
ATOM   2838 N N    B HIS   A 1 138 ? 12.235 -10.929 -5.588  0.60 11.87 ?  138 HIS   A N    1 
ATOM   2839 C CA   A HIS   A 1 138 ? 13.353 -11.354 -5.735  0.40 11.08 ?  138 HIS   A CA   1 
ATOM   2840 C CA   B HIS   A 1 138 ? 13.415 -11.690 -5.973  0.60 12.44 ?  138 HIS   A CA   1 
ATOM   2841 C C    A HIS   A 1 138 ? 14.511 -11.208 -4.753  0.40 10.82 ?  138 HIS   A C    1 
ATOM   2842 C C    B HIS   A 1 138 ? 14.532 -11.527 -4.951  0.60 11.69 ?  138 HIS   A C    1 
ATOM   2843 O O    A HIS   A 1 138 ? 15.170 -12.197 -4.410  0.40 10.62 ?  138 HIS   A O    1 
ATOM   2844 O O    B HIS   A 1 138 ? 15.204 -12.501 -4.593  0.60 12.10 ?  138 HIS   A O    1 
ATOM   2845 C CB   A HIS   A 1 138 ? 13.756 -10.897 -7.137  0.40 11.23 ?  138 HIS   A CB   1 
ATOM   2846 C CB   B HIS   A 1 138 ? 13.877 -11.259 -7.362  0.60 13.50 ?  138 HIS   A CB   1 
ATOM   2847 C CG   A HIS   A 1 138 ? 15.019 -11.522 -7.637  0.40 11.74 ?  138 HIS   A CG   1 
ATOM   2848 C CG   B HIS   A 1 138 ? 15.173 -11.875 -7.776  0.60 14.53 ?  138 HIS   A CG   1 
ATOM   2849 N ND1  A HIS   A 1 138 ? 15.142 -12.875 -7.864  0.40 12.89 ?  138 HIS   A ND1  1 
ATOM   2850 N ND1  B HIS   A 1 138 ? 15.307 -13.221 -8.044  0.60 15.76 ?  138 HIS   A ND1  1 
ATOM   2851 C CD2  A HIS   A 1 138 ? 16.218 -10.976 -7.950  0.40 12.03 ?  138 HIS   A CD2  1 
ATOM   2852 C CD2  B HIS   A 1 138 ? 16.400 -11.332 -7.948  0.60 14.99 ?  138 HIS   A CD2  1 
ATOM   2853 C CE1  A HIS   A 1 138 ? 16.363 -13.136 -8.298  0.40 13.18 ?  138 HIS   A CE1  1 
ATOM   2854 C CE1  B HIS   A 1 138 ? 16.560 -13.477 -8.375  0.60 16.29 ?  138 HIS   A CE1  1 
ATOM   2855 N NE2  A HIS   A 1 138 ? 17.035 -12.000 -8.360  0.40 12.57 ?  138 HIS   A NE2  1 
ATOM   2856 N NE2  B HIS   A 1 138 ? 17.244 -12.348 -8.325  0.60 15.65 ?  138 HIS   A NE2  1 
ATOM   2857 H H    A HIS   A 1 138 ? 11.975 -9.937  -5.816  0.40 13.55 ?  138 HIS   A H    1 
ATOM   2858 H H    B HIS   A 1 138 ? 12.014 -10.304 -6.144  0.60 14.24 ?  138 HIS   A H    1 
ATOM   2859 H HA   A HIS   A 1 138 ? 13.117 -12.290 -5.784  0.40 13.28 ?  138 HIS   A HA   1 
ATOM   2860 H HA   B HIS   A 1 138 ? 13.182 -12.627 -6.017  0.60 14.92 ?  138 HIS   A HA   1 
ATOM   2861 H HB2  A HIS   A 1 138 ? 13.046 -11.130 -7.759  0.40 13.47 ?  138 HIS   A HB2  1 
ATOM   2862 H HB2  B HIS   A 1 138 ? 13.202 -11.519 -8.013  0.60 16.19 ?  138 HIS   A HB2  1 
ATOM   2863 H HB3  A HIS   A 1 138 ? 13.883 -9.935  -7.133  0.40 13.47 ?  138 HIS   A HB3  1 
ATOM   2864 H HB3  B HIS   A 1 138 ? 13.987 -10.295 -7.375  0.60 16.19 ?  138 HIS   A HB3  1 
ATOM   2865 H HD1  A HIS   A 1 138 ? 14.523 -13.459 -7.744  0.40 15.46 ?  138 HIS   A HD1  1 
ATOM   2866 H HD2  A HIS   A 1 138 ? 16.445 -10.075 -7.900  0.40 14.43 ?  138 HIS   A HD2  1 
ATOM   2867 H HD2  B HIS   A 1 138 ? 16.625 -10.435 -7.836  0.60 17.98 ?  138 HIS   A HD2  1 
ATOM   2868 H HE1  A HIS   A 1 138 ? 16.693 -13.977 -8.520  0.40 15.81 ?  138 HIS   A HE1  1 
ATOM   2869 H HE1  B HIS   A 1 138 ? 16.901 -14.308 -8.603  0.60 19.54 ?  138 HIS   A HE1  1 
ATOM   2870 H HE2  B HIS   A 1 138 ? 18.081 -12.261 -8.495  0.60 18.77 ?  138 HIS   A HE2  1 
ATOM   2871 N N    A SER   A 1 139 ? 14.775 -9.982  -4.292  0.40 10.55 ?  139 SER   A N    1 
ATOM   2872 N N    B SER   A 1 139 ? 14.751 -10.303 -4.469  0.60 11.24 ?  139 SER   A N    1 
ATOM   2873 C CA   A SER   A 1 139 ? 15.839 -9.772  -3.316  0.40 10.77 ?  139 SER   A CA   1 
ATOM   2874 C CA   B SER   A 1 139 ? 15.829 -10.084 -3.513  0.60 10.93 ?  139 SER   A CA   1 
ATOM   2875 C C    A SER   A 1 139 ? 15.629 -10.642 -2.086  0.40 10.66 ?  139 SER   A C    1 
ATOM   2876 C C    B SER   A 1 139 ? 15.600 -10.853 -2.214  0.60 10.62 ?  139 SER   A C    1 
ATOM   2877 O O    A SER   A 1 139 ? 16.591 -11.173 -1.517  0.40 10.33 ?  139 SER   A O    1 
ATOM   2878 O O    B SER   A 1 139 ? 16.532 -11.468 -1.677  0.60 10.12 ?  139 SER   A O    1 
ATOM   2879 C CB   A SER   A 1 139 ? 15.910 -8.292  -2.932  0.40 10.10 ?  139 SER   A CB   1 
ATOM   2880 C CB   B SER   A 1 139 ? 16.007 -8.593  -3.243  0.60 10.26 ?  139 SER   A CB   1 
ATOM   2881 O OG   A SER   A 1 139 ? 16.901 -8.072  -1.940  0.40 10.08 ?  139 SER   A OG   1 
ATOM   2882 O OG   B SER   A 1 139 ? 17.088 -8.408  -2.345  0.60 9.81  ?  139 SER   A OG   1 
ATOM   2883 H H    A SER   A 1 139 ? 14.355 -9.266  -4.515  0.40 12.65 ?  139 SER   A H    1 
ATOM   2884 H H    B SER   A 1 139 ? 14.309 -9.597  -4.690  0.60 13.49 ?  139 SER   A H    1 
ATOM   2885 H HA   A SER   A 1 139 ? 16.688 -10.023 -3.704  0.40 12.92 ?  139 SER   A HA   1 
ATOM   2886 H HA   B SER   A 1 139 ? 16.658 -10.406 -3.906  0.60 13.11 ?  139 SER   A HA   1 
ATOM   2887 H HB2  A SER   A 1 139 ? 16.134 -7.772  -3.721  0.40 12.11 ?  139 SER   A HB2  1 
ATOM   2888 H HB2  B SER   A 1 139 ? 16.202 -8.134  -4.082  0.60 12.30 ?  139 SER   A HB2  1 
ATOM   2889 H HB3  A SER   A 1 139 ? 15.052 -8.009  -2.582  0.40 12.11 ?  139 SER   A HB3  1 
ATOM   2890 H HB3  B SER   A 1 139 ? 15.200 -8.237  -2.849  0.60 12.30 ?  139 SER   A HB3  1 
ATOM   2891 H HG   A SER   A 1 139 ? 16.958 -7.242  -1.764  0.40 12.09 ?  139 SER   A HG   1 
ATOM   2892 H HG   B SER   A 1 139 ? 17.203 -7.593  -2.196  0.60 11.77 ?  139 SER   A HG   1 
ATOM   2893 N N    . LEU   A 1 140 ? 14.372 -10.816 -1.676  1.00 10.88 ?  140 LEU   A N    1 
ATOM   2894 C CA   . LEU   A 1 140 ? 14.087 -11.606 -0.481  1.00 11.00 ?  140 LEU   A CA   1 
ATOM   2895 C C    . LEU   A 1 140 ? 14.353 -13.088 -0.732  1.00 11.17 ?  140 LEU   A C    1 
ATOM   2896 O O    . LEU   A 1 140 ? 14.902 -13.787 0.130   1.00 11.34 ?  140 LEU   A O    1 
ATOM   2897 C CB   . LEU   A 1 140 ? 12.645 -11.366 -0.022  1.00 11.44 ?  140 LEU   A CB   1 
ATOM   2898 C CG   . LEU   A 1 140 ? 12.189 -12.168 1.198   1.00 11.90 ?  140 LEU   A CG   1 
ATOM   2899 C CD1  . LEU   A 1 140 ? 13.096 -11.963 2.407   1.00 12.61 ?  140 LEU   A CD1  1 
ATOM   2900 C CD2  . LEU   A 1 140 ? 10.745 -11.821 1.542   1.00 13.10 ?  140 LEU   A CD2  1 
ATOM   2901 H H    A LEU   A 1 140 ? 13.675 -10.496 -2.070  0.40 13.05 ?  140 LEU   A H    1 
ATOM   2902 H H    B LEU   A 1 140 ? 13.707 -10.354 -1.971  0.60 13.05 ?  140 LEU   A H    1 
ATOM   2903 H HA   . LEU   A 1 140 ? 14.672 -11.322 0.229   1.00 13.20 ?  140 LEU   A HA   1 
ATOM   2904 H HB2  . LEU   A 1 140 ? 12.544 -10.432 0.195   1.00 13.73 ?  140 LEU   A HB2  1 
ATOM   2905 H HB3  . LEU   A 1 140 ? 12.047 -11.599 -0.752  1.00 13.73 ?  140 LEU   A HB3  1 
ATOM   2906 H HG   . LEU   A 1 140 ? 12.206 -13.113 0.978   1.00 14.27 ?  140 LEU   A HG   1 
ATOM   2907 H HD11 . LEU   A 1 140 ? 12.716 -12.432 3.171   1.00 15.12 ?  140 LEU   A HD11 1 
ATOM   2908 H HD12 . LEU   A 1 140 ? 13.973 -12.330 2.205   1.00 15.12 ?  140 LEU   A HD12 1 
ATOM   2909 H HD13 . LEU   A 1 140 ? 13.164 -11.020 2.598   1.00 15.12 ?  140 LEU   A HD13 1 
ATOM   2910 H HD21 . LEU   A 1 140 ? 10.469 -12.337 2.319   1.00 15.71 ?  140 LEU   A HD21 1 
ATOM   2911 H HD22 . LEU   A 1 140 ? 10.683 -10.874 1.737   1.00 15.71 ?  140 LEU   A HD22 1 
ATOM   2912 H HD23 . LEU   A 1 140 ? 10.177 -12.042 0.785   1.00 15.71 ?  140 LEU   A HD23 1 
ATOM   2913 N N    . ARG   A 1 141 ? 13.968 -13.584 -1.910  1.00 11.63 ?  141 ARG   A N    1 
ATOM   2914 C CA   . ARG   A 1 141 ? 14.209 -14.981 -2.254  1.00 12.65 ?  141 ARG   A CA   1 
ATOM   2915 C C    . ARG   A 1 141 ? 15.705 -15.284 -2.277  1.00 12.04 ?  141 ARG   A C    1 
ATOM   2916 O O    . ARG   A 1 141 ? 16.160 -16.290 -1.718  1.00 12.24 ?  141 ARG   A O    1 
ATOM   2917 C CB   . ARG   A 1 141 ? 13.575 -15.269 -3.618  1.00 14.11 ?  141 ARG   A CB   1 
ATOM   2918 C CG   . ARG   A 1 141 ? 13.577 -16.720 -4.049  1.00 16.39 ?  141 ARG   A CG   1 
ATOM   2919 C CD   . ARG   A 1 141 ? 12.537 -17.485 -3.300  1.00 18.75 ?  141 ARG   A CD   1 
ATOM   2920 N NE   . ARG   A 1 141 ? 13.125 -18.217 -2.192  1.00 19.64 ?  141 ARG   A NE   1 
ATOM   2921 C CZ   . ARG   A 1 141 ? 12.422 -18.747 -1.200  1.00 19.73 ?  141 ARG   A CZ   1 
ATOM   2922 N NH1  . ARG   A 1 141 ? 11.132 -18.493 -1.056  1.00 18.99 ?  141 ARG   A NH1  1 
ATOM   2923 N NH2  . ARG   A 1 141 ? 13.029 -19.548 -0.328  1.00 20.65 ?  141 ARG   A NH2  1 
ATOM   2924 H H    . ARG   A 1 141 ? 13.572 -13.134 -2.527  1.00 13.95 ?  141 ARG   A H    1 
ATOM   2925 H HA   . ARG   A 1 141 ? 13.794 -15.557 -1.597  1.00 15.17 ?  141 ARG   A HA   1 
ATOM   2926 H HB2  . ARG   A 1 141 ? 12.654 -14.965 -3.601  1.00 16.93 ?  141 ARG   A HB2  1 
ATOM   2927 H HB3  . ARG   A 1 141 ? 14.063 -14.769 -4.293  1.00 16.93 ?  141 ARG   A HB3  1 
ATOM   2928 H HG2  . ARG   A 1 141 ? 13.379 -16.778 -4.999  1.00 19.66 ?  141 ARG   A HG2  1 
ATOM   2929 H HG3  . ARG   A 1 141 ? 14.445 -17.117 -3.864  1.00 19.66 ?  141 ARG   A HG3  1 
ATOM   2930 H HD2  . ARG   A 1 141 ? 11.878 -16.870 -2.936  1.00 22.49 ?  141 ARG   A HD2  1 
ATOM   2931 H HD3  . ARG   A 1 141 ? 12.103 -18.116 -3.899  1.00 22.49 ?  141 ARG   A HD3  1 
ATOM   2932 H HE   . ARG   A 1 141 ? 13.955 -18.422 -2.243  1.00 23.56 ?  141 ARG   A HE   1 
ATOM   2933 H HH11 . ARG   A 1 141 ? 10.717 -17.991 -1.617  1.00 22.78 ?  141 ARG   A HH11 1 
ATOM   2934 H HH12 . ARG   A 1 141 ? 10.690 -18.846 -0.399  1.00 22.78 ?  141 ARG   A HH12 1 
ATOM   2935 H HH21 . ARG   A 1 141 ? 13.868 -19.716 -0.411  1.00 24.77 ?  141 ARG   A HH21 1 
ATOM   2936 H HH22 . ARG   A 1 141 ? 12.587 -19.886 0.330   1.00 24.77 ?  141 ARG   A HH22 1 
ATOM   2937 N N    . VAL   A 1 142 ? 16.493 -14.419 -2.926  1.00 11.70 ?  142 VAL   A N    1 
ATOM   2938 C CA   . VAL   A 1 142 ? 17.940 -14.624 -2.956  1.00 11.43 ?  142 VAL   A CA   1 
ATOM   2939 C C    . VAL   A 1 142 ? 18.510 -14.592 -1.545  1.00 10.85 ?  142 VAL   A C    1 
ATOM   2940 O O    . VAL   A 1 142 ? 19.369 -15.408 -1.192  1.00 11.21 ?  142 VAL   A O    1 
ATOM   2941 C CB   . VAL   A 1 142 ? 18.637 -13.613 -3.890  1.00 11.96 ?  142 VAL   A CB   1 
ATOM   2942 C CG1  . VAL   A 1 142 ? 20.156 -13.817 -3.850  1.00 11.75 ?  142 VAL   A CG1  1 
ATOM   2943 C CG2  . VAL   A 1 142 ? 18.137 -13.761 -5.315  1.00 13.33 ?  142 VAL   A CG2  1 
ATOM   2944 H H    . VAL   A 1 142 ? 16.222 -13.714 -3.345  1.00 14.03 ?  142 VAL   A H    1 
ATOM   2945 H HA   . VAL   A 1 142 ? 18.115 -15.503 -3.318  1.00 13.71 ?  142 VAL   A HA   1 
ATOM   2946 H HB   . VAL   A 1 142 ? 18.447 -12.706 -3.592  1.00 14.34 ?  142 VAL   A HB   1 
ATOM   2947 H HG11 . VAL   A 1 142 ? 20.559 -13.336 -4.589  1.00 14.09 ?  142 VAL   A HG11 1 
ATOM   2948 H HG12 . VAL   A 1 142 ? 20.500 -13.478 -3.008  1.00 14.09 ?  142 VAL   A HG12 1 
ATOM   2949 H HG13 . VAL   A 1 142 ? 20.345 -14.765 -3.929  1.00 14.09 ?  142 VAL   A HG13 1 
ATOM   2950 H HG21 . VAL   A 1 142 ? 18.557 -13.083 -5.868  1.00 15.98 ?  142 VAL   A HG21 1 
ATOM   2951 H HG22 . VAL   A 1 142 ? 18.378 -14.644 -5.637  1.00 15.98 ?  142 VAL   A HG22 1 
ATOM   2952 H HG23 . VAL   A 1 142 ? 17.178 -13.652 -5.325  1.00 15.98 ?  142 VAL   A HG23 1 
ATOM   2953 N N    . CYS   A 1 143 ? 18.044 -13.658 -0.714  1.00 10.84 ?  143 CYS   A N    1 
ATOM   2954 C CA   . CYS   A 1 143 ? 18.504 -13.597 0.670   1.00 10.85 ?  143 CYS   A CA   1 
ATOM   2955 C C    . CYS   A 1 143 ? 18.287 -14.932 1.379   1.00 11.20 ?  143 CYS   A C    1 
ATOM   2956 O O    . CYS   A 1 143 ? 19.213 -15.515 1.951   1.00 11.13 ?  143 CYS   A O    1 
ATOM   2957 C CB   . CYS   A 1 143 ? 17.768 -12.480 1.404   1.00 11.31 ?  143 CYS   A CB   1 
ATOM   2958 S SG   . CYS   A 1 143 ? 18.263 -12.298 3.126   1.00 12.02 ?  143 CYS   A SG   1 
ATOM   2959 H H    . CYS   A 1 143 ? 17.471 -13.055 -0.927  1.00 13.00 ?  143 CYS   A H    1 
ATOM   2960 H HA   . CYS   A 1 143 ? 19.452 -13.400 0.683   1.00 13.01 ?  143 CYS   A HA   1 
ATOM   2961 H HB2  . CYS   A 1 143 ? 17.937 -11.641 0.952   1.00 13.56 ?  143 CYS   A HB2  1 
ATOM   2962 H HB3  . CYS   A 1 143 ? 16.817 -12.673 1.389   1.00 13.56 ?  143 CYS   A HB3  1 
ATOM   2963 H HG   . CYS   A 1 143 ? 17.717 -11.336 3.584   1.00 14.42 ?  143 CYS   A HG   1 
ATOM   2964 N N    . VAL   A 1 144 ? 17.054 -15.434 1.349   1.00 11.57 ?  144 VAL   A N    1 
ATOM   2965 C CA   . VAL   A 1 144 ? 16.727 -16.661 2.068   1.00 12.75 ?  144 VAL   A CA   1 
ATOM   2966 C C    . VAL   A 1 144 ? 17.515 -17.846 1.535   1.00 12.53 ?  144 VAL   A C    1 
ATOM   2967 O O    . VAL   A 1 144 ? 17.871 -18.760 2.296   1.00 13.00 ?  144 VAL   A O    1 
ATOM   2968 C CB   . VAL   A 1 144 ? 15.202 -16.882 1.984   1.00 16.21 ?  144 VAL   A CB   1 
ATOM   2969 C CG1  . VAL   A 1 144 ? 14.823 -18.301 2.344   1.00 18.68 ?  144 VAL   A CG1  1 
ATOM   2970 C CG2  . VAL   A 1 144 ? 14.475 -15.854 2.860   1.00 15.50 ?  144 VAL   A CG2  1 
ATOM   2971 H H    . VAL   A 1 144 ? 16.391 -15.084 0.915   1.00 13.87 ?  144 VAL   A H    1 
ATOM   2972 H HA   . VAL   A 1 144 ? 16.954 -16.543 2.995   1.00 15.29 ?  144 VAL   A HA   1 
ATOM   2973 H HB   . VAL   A 1 144 ? 14.912 -16.723 1.069   1.00 19.44 ?  144 VAL   A HB   1 
ATOM   2974 H HG11 . VAL   A 1 144 ? 13.870 -18.333 2.536   1.00 22.41 ?  144 VAL   A HG11 1 
ATOM   2975 H HG12 . VAL   A 1 144 ? 15.025 -18.881 1.596   1.00 22.41 ?  144 VAL   A HG12 1 
ATOM   2976 H HG13 . VAL   A 1 144 ? 15.325 -18.570 3.126   1.00 22.41 ?  144 VAL   A HG13 1 
ATOM   2977 H HG21 . VAL   A 1 144 ? 13.517 -16.017 2.823   1.00 18.59 ?  144 VAL   A HG21 1 
ATOM   2978 H HG22 . VAL   A 1 144 ? 14.787 -15.933 3.774   1.00 18.59 ?  144 VAL   A HG22 1 
ATOM   2979 H HG23 . VAL   A 1 144 ? 14.662 -14.956 2.527   1.00 18.59 ?  144 VAL   A HG23 1 
ATOM   2980 N N    . ASP   A 1 145 ? 17.778 -17.870 0.230   1.00 12.78 ?  145 ASP   A N    1 
ATOM   2981 C CA   . ASP   A 1 145 ? 18.478 -18.980 -0.408  1.00 13.55 ?  145 ASP   A CA   1 
ATOM   2982 C C    . ASP   A 1 145 ? 20.000 -18.842 -0.375  1.00 13.48 ?  145 ASP   A C    1 
ATOM   2983 O O    . ASP   A 1 145 ? 20.697 -19.744 -0.853  1.00 15.29 ?  145 ASP   A O    1 
ATOM   2984 C CB   . ASP   A 1 145 ? 18.017 -19.128 -1.862  1.00 15.71 ?  145 ASP   A CB   1 
ATOM   2985 C CG   . ASP   A 1 145 ? 16.560 -19.553 -1.982  1.00 18.07 ?  145 ASP   A CG   1 
ATOM   2986 O OD1  . ASP   A 1 145 ? 15.998 -20.082 -0.999  1.00 18.72 ?  145 ASP   A OD1  1 
ATOM   2987 O OD2  . ASP   A 1 145 ? 15.975 -19.355 -3.066  1.00 19.33 -1 145 ASP   A OD2  1 
ATOM   2988 H H    . ASP   A 1 145 ? 17.548 -17.243 -0.319  1.00 15.32 ?  145 ASP   A H    1 
ATOM   2989 H HA   . ASP   A 1 145 ? 18.246 -19.795 0.059   1.00 16.25 ?  145 ASP   A HA   1 
ATOM   2990 H HB2  . ASP   A 1 145 ? 18.127 -18.278 -2.315  1.00 18.84 ?  145 ASP   A HB2  1 
ATOM   2991 H HB3  . ASP   A 1 145 ? 18.555 -19.808 -2.292  1.00 18.84 ?  145 ASP   A HB3  1 
ATOM   2992 N N    . THR   A 1 146 ? 20.534 -17.746 0.156   1.00 11.56 ?  146 THR   A N    1 
ATOM   2993 C CA   . THR   A 1 146 ? 21.977 -17.515 0.175   1.00 11.11 ?  146 THR   A CA   1 
ATOM   2994 C C    . THR   A 1 146 ? 22.537 -17.330 1.575   1.00 10.91 ?  146 THR   A C    1 
ATOM   2995 O O    . THR   A 1 146 ? 23.616 -17.855 1.882   1.00 11.88 ?  146 THR   A O    1 
ATOM   2996 C CB   . THR   A 1 146 ? 22.307 -16.264 -0.665  1.00 10.96 ?  146 THR   A CB   1 
ATOM   2997 O OG1  . THR   A 1 146 ? 21.773 -16.421 -1.981  1.00 11.32 ?  146 THR   A OG1  1 
ATOM   2998 C CG2  . THR   A 1 146 ? 23.806 -16.032 -0.763  1.00 11.41 ?  146 THR   A CG2  1 
ATOM   2999 H H    . THR   A 1 146 ? 20.080 -17.109 0.511   1.00 13.87 ?  146 THR   A H    1 
ATOM   3000 H HA   . THR   A 1 146 ? 22.430 -18.270 -0.226  1.00 13.33 ?  146 THR   A HA   1 
ATOM   3001 H HB   . THR   A 1 146 ? 21.912 -15.485 -0.251  1.00 13.14 ?  146 THR   A HB   1 
ATOM   3002 H HG1  . THR   A 1 146 ? 20.937 -16.488 -1.943  1.00 13.58 ?  146 THR   A HG1  1 
ATOM   3003 H HG21 . THR   A 1 146 ? 23.992 -15.358 -1.434  1.00 13.69 ?  146 THR   A HG21 1 
ATOM   3004 H HG22 . THR   A 1 146 ? 24.155 -15.736 0.089   1.00 13.69 ?  146 THR   A HG22 1 
ATOM   3005 H HG23 . THR   A 1 146 ? 24.252 -16.858 -1.019  1.00 13.69 ?  146 THR   A HG23 1 
ATOM   3006 N N    . VAL   A 1 147 ? 21.858 -16.554 2.413   1.00 10.86 ?  147 VAL   A N    1 
ATOM   3007 C CA   . VAL   A 1 147 ? 22.351 -16.258 3.750   1.00 11.06 ?  147 VAL   A CA   1 
ATOM   3008 C C    . VAL   A 1 147 ? 22.024 -17.426 4.668   1.00 11.08 ?  147 VAL   A C    1 
ATOM   3009 O O    . VAL   A 1 147 ? 20.879 -17.892 4.718   1.00 12.00 ?  147 VAL   A O    1 
ATOM   3010 C CB   . VAL   A 1 147 ? 21.740 -14.947 4.271   1.00 11.18 ?  147 VAL   A CB   1 
ATOM   3011 C CG1  . VAL   A 1 147 ? 22.286 -14.634 5.648   1.00 12.31 ?  147 VAL   A CG1  1 
ATOM   3012 C CG2  . VAL   A 1 147 ? 22.006 -13.804 3.298   1.00 11.62 ?  147 VAL   A CG2  1 
ATOM   3013 H H    . VAL   A 1 147 ? 21.097 -16.188 2.233   1.00 13.02 ?  147 VAL   A H    1 
ATOM   3014 H HA   . VAL   A 1 147 ? 23.314 -16.152 3.717   1.00 13.26 ?  147 VAL   A HA   1 
ATOM   3015 H HB   . VAL   A 1 147 ? 20.780 -15.053 4.349   1.00 13.41 ?  147 VAL   A HB   1 
ATOM   3016 H HG11 . VAL   A 1 147 ? 22.041 -13.730 5.887   1.00 14.76 ?  147 VAL   A HG11 1 
ATOM   3017 H HG12 . VAL   A 1 147 ? 21.907 -15.260 6.288   1.00 14.76 ?  147 VAL   A HG12 1 
ATOM   3018 H HG13 . VAL   A 1 147 ? 23.252 -14.724 5.631   1.00 14.76 ?  147 VAL   A HG13 1 
ATOM   3019 H HG21 . VAL   A 1 147 ? 21.691 -12.975 3.690   1.00 13.93 ?  147 VAL   A HG21 1 
ATOM   3020 H HG22 . VAL   A 1 147 ? 22.961 -13.749 3.131   1.00 13.93 ?  147 VAL   A HG22 1 
ATOM   3021 H HG23 . VAL   A 1 147 ? 21.535 -13.979 2.469   1.00 13.93 ?  147 VAL   A HG23 1 
ATOM   3022 N N    . ARG   A 1 148 ? 23.045 -17.906 5.382   1.00 11.25 ?  148 ARG   A N    1 
ATOM   3023 C CA   . ARG   A 1 148 ? 22.916 -18.986 6.346   1.00 11.55 ?  148 ARG   A CA   1 
ATOM   3024 C C    . ARG   A 1 148 ? 23.038 -18.514 7.782   1.00 11.86 ?  148 ARG   A C    1 
ATOM   3025 O O    . ARG   A 1 148 ? 22.626 -19.240 8.695   1.00 13.40 ?  148 ARG   A O    1 
ATOM   3026 C CB   . ARG   A 1 148 ? 23.961 -20.079 6.066   1.00 12.20 ?  148 ARG   A CB   1 
ATOM   3027 C CG   . ARG   A 1 148 ? 23.789 -20.731 4.701   1.00 13.27 ?  148 ARG   A CG   1 
ATOM   3028 C CD   . ARG   A 1 148 ? 24.869 -21.762 4.396   1.00 14.00 ?  148 ARG   A CD   1 
ATOM   3029 N NE   . ARG   A 1 148 ? 26.205 -21.176 4.420   1.00 14.20 ?  148 ARG   A NE   1 
ATOM   3030 C CZ   . ARG   A 1 148 ? 26.711 -20.431 3.446   1.00 13.60 ?  148 ARG   A CZ   1 
ATOM   3031 N NH1  . ARG   A 1 148 ? 26.030 -20.191 2.337   1.00 13.88 ?  148 ARG   A NH1  1 
ATOM   3032 N NH2  . ARG   A 1 148 ? 27.931 -19.908 3.590   1.00 14.06 ?  148 ARG   A NH2  1 
ATOM   3033 H H    . ARG   A 1 148 ? 23.854 -17.609 5.307   1.00 13.49 ?  148 ARG   A H    1 
ATOM   3034 H HA   . ARG   A 1 148 ? 22.043 -19.385 6.242   1.00 13.86 ?  148 ARG   A HA   1 
ATOM   3035 H HB2  . ARG   A 1 148 ? 24.848 -19.688 6.101   1.00 14.63 ?  148 ARG   A HB2  1 
ATOM   3036 H HB3  . ARG   A 1 148 ? 23.877 -20.773 6.739   1.00 14.63 ?  148 ARG   A HB3  1 
ATOM   3037 H HG2  . ARG   A 1 148 ? 22.928 -21.175 4.672   1.00 15.92 ?  148 ARG   A HG2  1 
ATOM   3038 H HG3  . ARG   A 1 148 ? 23.828 -20.041 4.018   1.00 15.92 ?  148 ARG   A HG3  1 
ATOM   3039 H HD2  . ARG   A 1 148 ? 24.836 -22.465 5.062   1.00 16.80 ?  148 ARG   A HD2  1 
ATOM   3040 H HD3  . ARG   A 1 148 ? 24.714 -22.133 3.511   1.00 16.80 ?  148 ARG   A HD3  1 
ATOM   3041 H HE   . ARG   A 1 148 ? 26.693 -21.319 5.109   1.00 17.03 ?  148 ARG   A HE   1 
ATOM   3042 H HH11 . ARG   A 1 148 ? 25.241 -20.518 2.232   1.00 16.65 ?  148 ARG   A HH11 1 
ATOM   3043 H HH12 . ARG   A 1 148 ? 26.374 -19.702 1.717   1.00 16.65 ?  148 ARG   A HH12 1 
ATOM   3044 H HH21 . ARG   A 1 148 ? 28.375 -20.051 4.308   1.00 16.86 ?  148 ARG   A HH21 1 
ATOM   3045 H HH22 . ARG   A 1 148 ? 28.264 -19.418 2.965   1.00 16.86 ?  148 ARG   A HH22 1 
ATOM   3046 N N    . THR   A 1 149 ? 23.591 -17.324 7.999   1.00 11.80 ?  149 THR   A N    1 
ATOM   3047 C CA   . THR   A 1 149 ? 23.665 -16.719 9.315   1.00 11.87 ?  149 THR   A CA   1 
ATOM   3048 C C    . THR   A 1 149 ? 22.342 -16.020 9.628   1.00 11.59 ?  149 THR   A C    1 
ATOM   3049 O O    . THR   A 1 149 ? 21.407 -16.009 8.821   1.00 12.24 ?  149 THR   A O    1 
ATOM   3050 C CB   . THR   A 1 149 ? 24.871 -15.789 9.376   1.00 12.39 ?  149 THR   A CB   1 
ATOM   3051 O OG1  . THR   A 1 149 ? 24.760 -14.857 8.299   1.00 12.42 ?  149 THR   A OG1  1 
ATOM   3052 C CG2  . THR   A 1 149 ? 26.173 -16.585 9.253   1.00 12.87 ?  149 THR   A CG2  1 
ATOM   3053 H H    . THR   A 1 149 ? 23.943 -16.837 7.378   1.00 14.15 ?  149 THR   A H    1 
ATOM   3054 H HA   . THR   A 1 149 ? 23.793 -17.418 9.972   1.00 14.24 ?  149 THR   A HA   1 
ATOM   3055 H HB   . THR   A 1 149 ? 24.867 -15.312 10.219  1.00 14.86 ?  149 THR   A HB   1 
ATOM   3056 H HG1  . THR   A 1 149 ? 25.414 -14.330 8.302   1.00 14.90 ?  149 THR   A HG1  1 
ATOM   3057 H HG21 . THR   A 1 149 ? 26.933 -15.986 9.313   1.00 15.44 ?  149 THR   A HG21 1 
ATOM   3058 H HG22 . THR   A 1 149 ? 26.230 -17.241 9.965   1.00 15.44 ?  149 THR   A HG22 1 
ATOM   3059 H HG23 . THR   A 1 149 ? 26.202 -17.046 8.398   1.00 15.44 ?  149 THR   A HG23 1 
ATOM   3060 N N    . ASN   A 1 150 ? 22.226 -15.481 10.836  1.00 12.14 ?  150 ASN   A N    1 
ATOM   3061 C CA   . ASN   A 1 150 ? 20.946 -14.963 11.321  1.00 12.39 ?  150 ASN   A CA   1 
ATOM   3062 C C    . ASN   A 1 150 ? 20.770 -13.521 10.863  1.00 12.08 ?  150 ASN   A C    1 
ATOM   3063 O O    . ASN   A 1 150 ? 21.523 -12.629 11.276  1.00 13.25 ?  150 ASN   A O    1 
ATOM   3064 C CB   . ASN   A 1 150 ? 20.881 -15.079 12.839  1.00 14.76 ?  150 ASN   A CB   1 
ATOM   3065 C CG   . ASN   A 1 150 ? 20.774 -16.516 13.298  1.00 18.97 ?  150 ASN   A CG   1 
ATOM   3066 O OD1  . ASN   A 1 150 ? 20.210 -17.357 12.598  1.00 20.23 ?  150 ASN   A OD1  1 
ATOM   3067 N ND2  . ASN   A 1 150 ? 21.327 -16.812 14.469  1.00 21.26 ?  150 ASN   A ND2  1 
ATOM   3068 H H    . ASN   A 1 150 ? 22.867 -15.413 11.400  1.00 14.55 ?  150 ASN   A H    1 
ATOM   3069 H HA   . ASN   A 1 150 ? 20.220 -15.496 10.951  1.00 14.86 ?  150 ASN   A HA   1 
ATOM   3070 H HB2  . ASN   A 1 150 ? 21.685 -14.702 13.225  1.00 17.70 ?  150 ASN   A HB2  1 
ATOM   3071 H HB3  . ASN   A 1 150 ? 20.099 -14.605 13.165  1.00 17.70 ?  150 ASN   A HB3  1 
ATOM   3072 H HD21 . ASN   A 1 150 ? 21.294 -17.619 14.776  1.00 25.51 ?  150 ASN   A HD21 1 
ATOM   3073 H HD22 . ASN   A 1 150 ? 21.715 -16.198 14.933  1.00 25.51 ?  150 ASN   A HD22 1 
ATOM   3074 N N    . VAL   A 1 151 ? 19.780 -13.290 10.006  1.00 11.48 ?  151 VAL   A N    1 
ATOM   3075 C CA   . VAL   A 1 151 ? 19.569 -11.979 9.407   1.00 11.32 ?  151 VAL   A CA   1 
ATOM   3076 C C    . VAL   A 1 151 ? 18.186 -11.461 9.776   1.00 11.25 ?  151 VAL   A C    1 
ATOM   3077 O O    . VAL   A 1 151 ? 17.179 -12.170 9.633   1.00 12.78 ?  151 VAL   A O    1 
ATOM   3078 C CB   . VAL   A 1 151 ? 19.857 -11.971 7.889   1.00 13.20 ?  151 VAL   A CB   1 
ATOM   3079 C CG1  . VAL   A 1 151 ? 19.043 -13.002 7.144   1.00 14.79 ?  151 VAL   A CG1  1 
ATOM   3080 C CG2  . VAL   A 1 151 ? 19.654 -10.572 7.304   1.00 13.39 ?  151 VAL   A CG2  1 
ATOM   3081 H H    . VAL   A 1 151 ? 19.218 -13.888 9.746   1.00 13.77 ?  151 VAL   A H    1 
ATOM   3082 H HA   . VAL   A 1 151 ? 20.211 -11.370 9.799   1.00 13.58 ?  151 VAL   A HA   1 
ATOM   3083 H HB   . VAL   A 1 151 ? 20.791 -12.199 7.752   1.00 15.83 ?  151 VAL   A HB   1 
ATOM   3084 H HG11 . VAL   A 1 151 ? 19.231 -12.940 6.194   1.00 17.74 ?  151 VAL   A HG11 1 
ATOM   3085 H HG12 . VAL   A 1 151 ? 19.283 -13.890 7.467   1.00 17.74 ?  151 VAL   A HG12 1 
ATOM   3086 H HG13 . VAL   A 1 151 ? 18.099 -12.843 7.304   1.00 17.74 ?  151 VAL   A HG13 1 
ATOM   3087 H HG21 . VAL   A 1 151 ? 19.966 -10.566 6.382   1.00 16.06 ?  151 VAL   A HG21 1 
ATOM   3088 H HG22 . VAL   A 1 151 ? 18.709 -10.350 7.328   1.00 16.06 ?  151 VAL   A HG22 1 
ATOM   3089 H HG23 . VAL   A 1 151 ? 20.160 -9.934  7.826   1.00 16.06 ?  151 VAL   A HG23 1 
ATOM   3090 N N    . TYR   A 1 152 ? 18.170 -10.217 10.269  1.00 11.35 ?  152 TYR   A N    1 
ATOM   3091 C CA   . TYR   A 1 152 ? 16.976 -9.480  10.653  1.00 11.35 ?  152 TYR   A CA   1 
ATOM   3092 C C    . TYR   A 1 152 ? 16.798 -8.383  9.618   1.00 10.72 ?  152 TYR   A C    1 
ATOM   3093 O O    . TYR   A 1 152 ? 17.576 -7.421  9.576   1.00 11.11 ?  152 TYR   A O    1 
ATOM   3094 C CB   . TYR   A 1 152 ? 17.146 -8.934  12.067  1.00 12.17 ?  152 TYR   A CB   1 
ATOM   3095 C CG   . TYR   A 1 152 ? 17.102 -10.058 13.064  1.00 12.84 ?  152 TYR   A CG   1 
ATOM   3096 C CD1  . TYR   A 1 152 ? 18.232 -10.817 13.345  1.00 14.04 ?  152 TYR   A CD1  1 
ATOM   3097 C CD2  . TYR   A 1 152 ? 15.913 -10.408 13.686  1.00 13.07 ?  152 TYR   A CD2  1 
ATOM   3098 C CE1  . TYR   A 1 152 ? 18.186 -11.874 14.232  1.00 15.51 ?  152 TYR   A CE1  1 
ATOM   3099 C CE2  . TYR   A 1 152 ? 15.852 -11.473 14.580  1.00 14.89 ?  152 TYR   A CE2  1 
ATOM   3100 C CZ   . TYR   A 1 152 ? 16.994 -12.200 14.852  1.00 15.45 ?  152 TYR   A CZ   1 
ATOM   3101 O OH   . TYR   A 1 152 ? 16.948 -13.266 15.732  1.00 17.73 ?  152 TYR   A OH   1 
ATOM   3102 H H    . TYR   A 1 152 ? 18.890 -9.749  10.379  1.00 13.62 ?  152 TYR   A H    1 
ATOM   3103 H HA   . TYR   A 1 152 ? 16.206 -10.069 10.629  1.00 13.62 ?  152 TYR   A HA   1 
ATOM   3104 H HB2  . TYR   A 1 152 ? 18.005 -8.494  12.142  1.00 14.60 ?  152 TYR   A HB2  1 
ATOM   3105 H HB3  . TYR   A 1 152 ? 16.426 -8.318  12.264  1.00 14.60 ?  152 TYR   A HB3  1 
ATOM   3106 H HD1  . TYR   A 1 152 ? 19.035 -10.601 12.925  1.00 16.85 ?  152 TYR   A HD1  1 
ATOM   3107 H HD2  . TYR   A 1 152 ? 15.139 -9.919  13.502  1.00 15.67 ?  152 TYR   A HD2  1 
ATOM   3108 H HE1  . TYR   A 1 152 ? 18.955 -12.360 14.412  1.00 18.60 ?  152 TYR   A HE1  1 
ATOM   3109 H HE2  . TYR   A 1 152 ? 15.048 -11.686 14.999  1.00 17.86 ?  152 TYR   A HE2  1 
ATOM   3110 H HH   . TYR   A 1 152 ? 16.171 -13.341 16.042  1.00 21.27 ?  152 TYR   A HH   1 
ATOM   3111 N N    A LEU   A 1 153 ? 15.792 -8.563  8.761   0.40 10.41 ?  153 LEU   A N    1 
ATOM   3112 N N    B LEU   A 1 153 ? 15.781 -8.525  8.782   0.60 10.71 ?  153 LEU   A N    1 
ATOM   3113 C CA   A LEU   A 1 153 ? 15.533 -7.689  7.624   0.40 10.40 ?  153 LEU   A CA   1 
ATOM   3114 C CA   B LEU   A 1 153 ? 15.531 -7.574  7.710   0.60 10.94 ?  153 LEU   A CA   1 
ATOM   3115 C C    A LEU   A 1 153 ? 14.523 -6.613  8.000   0.40 10.07 ?  153 LEU   A C    1 
ATOM   3116 C C    B LEU   A 1 153 ? 14.545 -6.511  8.173   0.60 11.20 ?  153 LEU   A C    1 
ATOM   3117 O O    A LEU   A 1 153 ? 13.457 -6.914  8.551   0.40 10.82 ?  153 LEU   A O    1 
ATOM   3118 O O    B LEU   A 1 153 ? 13.402 -6.825  8.532   0.60 12.29 ?  153 LEU   A O    1 
ATOM   3119 C CB   A LEU   A 1 153 ? 14.978 -8.503  6.452   0.40 10.61 ?  153 LEU   A CB   1 
ATOM   3120 C CB   B LEU   A 1 153 ? 14.974 -8.289  6.484   0.60 11.26 ?  153 LEU   A CB   1 
ATOM   3121 C CG   A LEU   A 1 153 ? 15.935 -9.459  5.736   0.40 10.58 ?  153 LEU   A CG   1 
ATOM   3122 C CG   B LEU   A 1 153 ? 15.872 -9.350  5.856   0.60 11.64 ?  153 LEU   A CG   1 
ATOM   3123 C CD1  A LEU   A 1 153 ? 15.170 -10.404 4.824   0.40 10.79 ?  153 LEU   A CD1  1 
ATOM   3124 C CD1  B LEU   A 1 153 ? 15.081 -10.143 4.827   0.60 12.48 ?  153 LEU   A CD1  1 
ATOM   3125 C CD2  A LEU   A 1 153 ? 16.950 -8.677  4.933   0.40 10.58 ?  153 LEU   A CD2  1 
ATOM   3126 C CD2  B LEU   A 1 153 ? 17.110 -8.728  5.231   0.60 12.19 ?  153 LEU   A CD2  1 
ATOM   3127 H H    A LEU   A 1 153 ? 15.224 -9.211  8.823   0.40 12.48 ?  153 LEU   A H    1 
ATOM   3128 H H    B LEU   A 1 153 ? 15.208 -9.168  8.820   0.60 12.85 ?  153 LEU   A H    1 
ATOM   3129 H HA   A LEU   A 1 153 ? 16.358 -7.271  7.344   0.40 12.47 ?  153 LEU   A HA   1 
ATOM   3130 H HA   B LEU   A 1 153 ? 16.359 -7.137  7.472   0.60 13.12 ?  153 LEU   A HA   1 
ATOM   3131 H HB2  A LEU   A 1 153 ? 14.237 -9.038  6.778   0.40 12.72 ?  153 LEU   A HB2  1 
ATOM   3132 H HB2  B LEU   A 1 153 ? 14.146 -8.720  6.742   0.60 13.51 ?  153 LEU   A HB2  1 
ATOM   3133 H HB3  A LEU   A 1 153 ? 14.651 -7.885  5.780   0.40 12.72 ?  153 LEU   A HB3  1 
ATOM   3134 H HB3  B LEU   A 1 153 ? 14.794 -7.619  5.808   0.60 13.51 ?  153 LEU   A HB3  1 
ATOM   3135 H HG   A LEU   A 1 153 ? 16.410 -9.994  6.394   0.40 12.68 ?  153 LEU   A HG   1 
ATOM   3136 H HG   B LEU   A 1 153 ? 16.166 -9.962  6.553   0.60 13.96 ?  153 LEU   A HG   1 
ATOM   3137 H HD11 A LEU   A 1 153 ? 15.758 -11.125 4.551   0.40 12.95 ?  153 LEU   A HD11 1 
ATOM   3138 H HD11 B LEU   A 1 153 ? 15.652 -10.830 4.454   0.60 14.97 ?  153 LEU   A HD11 1 
ATOM   3139 H HD12 A LEU   A 1 153 ? 14.411 -10.762 5.308   0.40 12.95 ?  153 LEU   A HD12 1 
ATOM   3140 H HD12 B LEU   A 1 153 ? 14.315 -10.547 5.264   0.60 14.97 ?  153 LEU   A HD12 1 
ATOM   3141 H HD13 A LEU   A 1 153 ? 14.866 -9.909  4.048   0.40 12.95 ?  153 LEU   A HD13 1 
ATOM   3142 H HD13 B LEU   A 1 153 ? 14.784 -9.539  4.129   0.60 14.97 ?  153 LEU   A HD13 1 
ATOM   3143 H HD21 A LEU   A 1 153 ? 17.546 -9.298  4.493   0.40 12.68 ?  153 LEU   A HD21 1 
ATOM   3144 H HD21 B LEU   A 1 153 ? 17.646 -9.432  4.837   0.60 14.62 ?  153 LEU   A HD21 1 
ATOM   3145 H HD22 A LEU   A 1 153 ? 16.477 -8.143  4.277   0.40 12.68 ?  153 LEU   A HD22 1 
ATOM   3146 H HD22 B LEU   A 1 153 ? 16.833 -8.097  4.552   0.60 14.62 ?  153 LEU   A HD22 1 
ATOM   3147 H HD23 A LEU   A 1 153 ? 17.446 -8.106  5.536   0.40 12.68 ?  153 LEU   A HD23 1 
ATOM   3148 H HD23 B LEU   A 1 153 ? 17.618 -8.272  5.922   0.60 14.62 ?  153 LEU   A HD23 1 
ATOM   3149 N N    A ALA   A 1 154 ? 14.852 -5.365  7.673   0.40 9.58  ?  154 ALA   A N    1 
ATOM   3150 N N    B ALA   A 1 154 ? 14.987 -5.255  8.147   0.60 10.32 ?  154 ALA   A N    1 
ATOM   3151 C CA   A ALA   A 1 154 ? 13.976 -4.217  7.878   0.40 9.62  ?  154 ALA   A CA   1 
ATOM   3152 C CA   B ALA   A 1 154 ? 14.131 -4.100  8.385   0.60 10.58 ?  154 ALA   A CA   1 
ATOM   3153 C C    A ALA   A 1 154 ? 13.495 -3.722  6.520   0.40 9.26  ?  154 ALA   A C    1 
ATOM   3154 C C    B ALA   A 1 154 ? 13.679 -3.561  7.033   0.60 10.11 ?  154 ALA   A C    1 
ATOM   3155 O O    A ALA   A 1 154 ? 14.305 -3.339  5.669   0.40 10.10 ?  154 ALA   A O    1 
ATOM   3156 O O    B ALA   A 1 154 ? 14.510 -3.164  6.209   0.60 10.16 ?  154 ALA   A O    1 
ATOM   3157 C CB   A ALA   A 1 154 ? 14.712 -3.096  8.612   0.40 10.43 ?  154 ALA   A CB   1 
ATOM   3158 C CB   B ALA   A 1 154 ? 14.889 -3.020  9.158   0.60 10.85 ?  154 ALA   A CB   1 
ATOM   3159 H H    A ALA   A 1 154 ? 15.605 -5.156  7.314   0.40 11.49 ?  154 ALA   A H    1 
ATOM   3160 H H    B ALA   A 1 154 ? 15.811 -5.038  7.990   0.60 12.38 ?  154 ALA   A H    1 
ATOM   3161 H HA   A ALA   A 1 154 ? 13.206 -4.486  8.407   0.40 11.53 ?  154 ALA   A HA   1 
ATOM   3162 H HA   B ALA   A 1 154 ? 13.354 -4.361  8.899   0.60 12.68 ?  154 ALA   A HA   1 
ATOM   3163 H HB1  A ALA   A 1 154 ? 14.103 -2.351  8.735   0.40 12.51 ?  154 ALA   A HB1  1 
ATOM   3164 H HB1  B ALA   A 1 154 ? 14.301 -2.259  9.304   0.60 13.01 ?  154 ALA   A HB1  1 
ATOM   3165 H HB2  A ALA   A 1 154 ? 15.013 -3.425  9.473   0.40 12.51 ?  154 ALA   A HB2  1 
ATOM   3166 H HB2  B ALA   A 1 154 ? 15.178 -3.378  10.012  0.60 13.01 ?  154 ALA   A HB2  1 
ATOM   3167 H HB3  A ALA   A 1 154 ? 15.472 -2.819  8.078   0.40 12.51 ?  154 ALA   A HB3  1 
ATOM   3168 H HB3  B ALA   A 1 154 ? 15.663 -2.739  8.641   0.60 13.01 ?  154 ALA   A HB3  1 
ATOM   3169 N N    A VAL   A 1 155 ? 12.179 -3.735  6.325   0.30 8.12  ?  155 VAL   A N    1 
ATOM   3170 N N    B VAL   A 1 155 ? 12.369 -3.536  6.812   0.60 10.78 ?  155 VAL   A N    1 
ATOM   3171 C CA   A VAL   A 1 155 ? 11.535 -3.246  5.110   0.30 9.54  ?  155 VAL   A CA   1 
ATOM   3172 C CA   B VAL   A 1 155 ? 11.777 -3.027  5.581   0.60 11.61 ?  155 VAL   A CA   1 
ATOM   3173 C CA   T VAL   A 1 155 ? 11.559 -3.256  5.298   0.10 10.58 ?  155 VAL   A CA   1 
ATOM   3174 C C    A VAL   A 1 155 ? 10.845 -1.933  5.460   0.30 10.67 ?  155 VAL   A C    1 
ATOM   3175 C C    B VAL   A 1 155 ? 10.961 -1.791  5.940   0.60 12.67 ?  155 VAL   A C    1 
ATOM   3176 C C    T VAL   A 1 155 ? 10.957 -1.888  5.618   0.10 10.59 ?  155 VAL   A C    1 
ATOM   3177 O O    A VAL   A 1 155 ? 9.902  -1.918  6.259   0.30 11.01 ?  155 VAL   A O    1 
ATOM   3178 O O    B VAL   A 1 155 ? 9.929  -1.893  6.613   0.60 13.24 ?  155 VAL   A O    1 
ATOM   3179 O O    T VAL   A 1 155 ? 10.140 -1.753  6.528   0.10 10.46 ?  155 VAL   A O    1 
ATOM   3180 C CB   A VAL   A 1 155 ? 10.526 -4.272  4.569   0.30 10.11 ?  155 VAL   A CB   1 
ATOM   3181 C CB   B VAL   A 1 155 ? 10.923 -4.095  4.888   0.60 12.18 ?  155 VAL   A CB   1 
ATOM   3182 C CB   T VAL   A 1 155 ? 10.516 -4.238  4.725   0.10 10.76 ?  155 VAL   A CB   1 
ATOM   3183 C CG1  A VAL   A 1 155 ? 9.897  -3.787  3.268   0.30 10.59 ?  155 VAL   A CG1  1 
ATOM   3184 C CG1  B VAL   A 1 155 ? 10.195 -3.500  3.696   0.60 12.47 ?  155 VAL   A CG1  1 
ATOM   3185 C CG1  T VAL   A 1 155 ? 9.849  -3.648  3.494   0.10 10.87 ?  155 VAL   A CG1  1 
ATOM   3186 C CG2  A VAL   A 1 155 ? 11.190 -5.634  4.379   0.30 10.47 ?  155 VAL   A CG2  1 
ATOM   3187 C CG2  B VAL   A 1 155 ? 11.814 -5.264  4.465   0.60 12.77 ?  155 VAL   A CG2  1 
ATOM   3188 C CG2  T VAL   A 1 155 ? 11.170 -5.576  4.393   0.10 10.91 ?  155 VAL   A CG2  1 
ATOM   3189 H H    A VAL   A 1 155 ? 11.618 -4.047  6.902   0.30 9.73  ?  155 VAL   A H    1 
ATOM   3190 H H    B VAL   A 1 155 ? 11.789 -3.807  7.386   0.60 12.93 ?  155 VAL   A H    1 
ATOM   3191 H HA   A VAL   A 1 155 ? 12.206 -3.082  4.428   0.30 11.44 ?  155 VAL   A HA   1 
ATOM   3192 H HA   B VAL   A 1 155 ? 12.483 -2.759  4.973   0.60 13.93 ?  155 VAL   A HA   1 
ATOM   3193 H HB   A VAL   A 1 155 ? 9.814  -4.383  5.219   0.30 12.12 ?  155 VAL   A HB   1 
ATOM   3194 H HB   B VAL   A 1 155 ? 10.261 -4.426  5.518   0.60 14.61 ?  155 VAL   A HB   1 
ATOM   3195 H HB   T VAL   A 1 155 ? 9.831  -4.399  5.393   0.10 12.91 ?  155 VAL   A HB   1 
ATOM   3196 H HG11 A VAL   A 1 155 ? 9.298  -4.471  2.932   0.30 12.70 ?  155 VAL   A HG11 1 
ATOM   3197 H HG11 B VAL   A 1 155 ? 9.843  -4.223  3.154   0.60 14.95 ?  155 VAL   A HG11 1 
ATOM   3198 H HG11 T VAL   A 1 155 ? 9.346  -4.344  3.044   0.10 13.03 ?  155 VAL   A HG11 1 
ATOM   3199 H HG12 A VAL   A 1 155 ? 9.401  -2.972  3.441   0.30 12.70 ?  155 VAL   A HG12 1 
ATOM   3200 H HG12 B VAL   A 1 155 ? 9.465  -2.942  4.012   0.60 14.95 ?  155 VAL   A HG12 1 
ATOM   3201 H HG12 T VAL   A 1 155 ? 9.253  -2.934  3.767   0.10 13.03 ?  155 VAL   A HG12 1 
ATOM   3202 H HG13 A VAL   A 1 155 ? 10.600 -3.617  2.622   0.30 12.70 ?  155 VAL   A HG13 1 
ATOM   3203 H HG13 B VAL   A 1 155 ? 10.817 -2.970  3.177   0.60 14.95 ?  155 VAL   A HG13 1 
ATOM   3204 H HG13 T VAL   A 1 155 ? 10.535 -3.301  2.901   0.10 13.03 ?  155 VAL   A HG13 1 
ATOM   3205 H HG21 A VAL   A 1 155 ? 10.562 -6.234  3.946   0.30 12.56 ?  155 VAL   A HG21 1 
ATOM   3206 H HG21 B VAL   A 1 155 ? 11.271 -5.921  4.007   0.60 15.32 ?  155 VAL   A HG21 1 
ATOM   3207 H HG21 T VAL   A 1 155 ? 10.497 -6.178  4.038   0.10 13.09 ?  155 VAL   A HG21 1 
ATOM   3208 H HG22 A VAL   A 1 155 ? 11.979 -5.526  3.825   0.30 12.56 ?  155 VAL   A HG22 1 
ATOM   3209 H HG22 B VAL   A 1 155 ? 12.507 -4.931  3.874   0.60 15.32 ?  155 VAL   A HG22 1 
ATOM   3210 H HG22 T VAL   A 1 155 ? 11.866 -5.432  3.732   0.10 13.09 ?  155 VAL   A HG22 1 
ATOM   3211 H HG23 A VAL   A 1 155 ? 11.441 -5.989  5.246   0.30 12.56 ?  155 VAL   A HG23 1 
ATOM   3212 H HG23 B VAL   A 1 155 ? 12.215 -5.657  5.257   0.60 15.32 ?  155 VAL   A HG23 1 
ATOM   3213 H HG23 T VAL   A 1 155 ? 11.555 -5.950  5.202   0.10 13.09 ?  155 VAL   A HG23 1 
ATOM   3214 N N    A PHE   A 1 156 ? 11.302 -0.831  4.856   0.30 12.13 ?  156 PHE   A N    1 
ATOM   3215 N N    B PHE   A 1 156 ? 11.422 -0.617  5.495   0.60 12.72 ?  156 PHE   A N    1 
ATOM   3216 N N    T PHE   A 1 156 ? 11.376 -0.873  4.859   0.10 10.91 ?  156 PHE   A N    1 
ATOM   3217 C CA   A PHE   A 1 156 ? 10.806 0.488   5.255   0.30 13.67 ?  156 PHE   A CA   1 
ATOM   3218 C CA   B PHE   A 1 156 ? 10.809 0.642   5.922   0.60 14.19 ?  156 PHE   A CA   1 
ATOM   3219 C CA   T PHE   A 1 156 ? 10.943 0.494   5.138   0.10 11.17 ?  156 PHE   A CA   1 
ATOM   3220 C C    A PHE   A 1 156 ? 9.356  0.704   4.833   0.30 13.87 ?  156 PHE   A C    1 
ATOM   3221 C C    B PHE   A 1 156 ? 9.414  0.832   5.324   0.60 14.03 ?  156 PHE   A C    1 
ATOM   3222 C C    T PHE   A 1 156 ? 9.493  0.722   4.726   0.10 12.01 ?  156 PHE   A C    1 
ATOM   3223 O O    A PHE   A 1 156 ? 8.569  1.296   5.581   0.30 14.15 ?  156 PHE   A O    1 
ATOM   3224 O O    B PHE   A 1 156 ? 8.494  1.279   6.018   0.60 15.08 ?  156 PHE   A O    1 
ATOM   3225 O O    T PHE   A 1 156 ? 8.725  1.352   5.462   0.10 12.12 ?  156 PHE   A O    1 
ATOM   3226 C CB   A PHE   A 1 156 ? 11.702 1.589   4.684   0.30 14.91 ?  156 PHE   A CB   1 
ATOM   3227 C CB   B PHE   A 1 156 ? 11.735 1.802   5.541   0.60 15.79 ?  156 PHE   A CB   1 
ATOM   3228 C CB   T PHE   A 1 156 ? 11.867 1.482   4.423   0.10 10.54 ?  156 PHE   A CB   1 
ATOM   3229 C CG   A PHE   A 1 156 ? 11.251 2.988   5.040   0.30 16.16 ?  156 PHE   A CG   1 
ATOM   3230 C CG   B PHE   A 1 156 ? 11.350 3.135   6.135   0.60 18.31 ?  156 PHE   A CG   1 
ATOM   3231 C CG   T PHE   A 1 156 ? 11.499 2.925   4.637   0.10 10.22 ?  156 PHE   A CG   1 
ATOM   3232 C CD1  A PHE   A 1 156 ? 11.190 3.390   6.368   0.30 16.43 ?  156 PHE   A CD1  1 
ATOM   3233 C CD1  B PHE   A 1 156 ? 10.543 3.230   7.257   0.60 19.48 ?  156 PHE   A CD1  1 
ATOM   3234 C CD1  T PHE   A 1 156 ? 11.820 3.567   5.824   0.10 10.25 ?  156 PHE   A CD1  1 
ATOM   3235 C CD2  A PHE   A 1 156 ? 10.894 3.895   4.054   0.30 16.59 ?  156 PHE   A CD2  1 
ATOM   3236 C CD2  B PHE   A 1 156 ? 11.819 4.304   5.560   0.60 19.60 ?  156 PHE   A CD2  1 
ATOM   3237 C CD2  T PHE   A 1 156 ? 10.840 3.642   3.651   0.10 10.53 ?  156 PHE   A CD2  1 
ATOM   3238 C CE1  A PHE   A 1 156 ? 10.778 4.670   6.702   0.30 17.04 ?  156 PHE   A CE1  1 
ATOM   3239 C CE1  B PHE   A 1 156 ? 10.209 4.465   7.788   0.60 20.36 ?  156 PHE   A CE1  1 
ATOM   3240 C CE1  T PHE   A 1 156 ? 11.484 4.892   6.026   0.10 10.53 ?  156 PHE   A CE1  1 
ATOM   3241 C CE2  A PHE   A 1 156 ? 10.485 5.177   4.384   0.30 16.95 ?  156 PHE   A CE2  1 
ATOM   3242 C CE2  B PHE   A 1 156 ? 11.486 5.537   6.085   0.60 20.42 ?  156 PHE   A CE2  1 
ATOM   3243 C CE2  T PHE   A 1 156 ? 10.505 4.969   3.848   0.10 10.78 ?  156 PHE   A CE2  1 
ATOM   3244 C CZ   A PHE   A 1 156 ? 10.429 5.564   5.709   0.30 17.27 ?  156 PHE   A CZ   1 
ATOM   3245 C CZ   B PHE   A 1 156 ? 10.683 5.617   7.200   0.60 20.53 ?  156 PHE   A CZ   1 
ATOM   3246 C CZ   T PHE   A 1 156 ? 10.829 5.595   5.036   0.10 10.63 ?  156 PHE   A CZ   1 
ATOM   3247 H H    A PHE   A 1 156 ? 11.885 -0.828  4.226   0.30 14.55 ?  156 PHE   A H    1 
ATOM   3248 H H    B PHE   A 1 156 ? 12.098 -0.520  4.963   0.60 15.26 ?  156 PHE   A H    1 
ATOM   3249 H H    T PHE   A 1 156 ? 11.911 -0.952  4.192   0.10 13.09 ?  156 PHE   A H    1 
ATOM   3250 H HA   A PHE   A 1 156 ? 10.846 0.544   6.224   0.30 16.39 ?  156 PHE   A HA   1 
ATOM   3251 H HA   B PHE   A 1 156 ? 10.738 0.633   6.890   0.60 17.02 ?  156 PHE   A HA   1 
ATOM   3252 H HA   T PHE   A 1 156 ? 11.013 0.652   6.093   0.10 13.39 ?  156 PHE   A HA   1 
ATOM   3253 H HB2  A PHE   A 1 156 ? 12.601 1.468   5.029   0.30 17.88 ?  156 PHE   A HB2  1 
ATOM   3254 H HB2  B PHE   A 1 156 ? 12.635 1.602   5.849   0.60 18.95 ?  156 PHE   A HB2  1 
ATOM   3255 H HB2  T PHE   A 1 156 ? 12.771 1.352   4.751   0.10 12.64 ?  156 PHE   A HB2  1 
ATOM   3256 H HB3  A PHE   A 1 156 ? 11.706 1.514   3.719   0.30 17.88 ?  156 PHE   A HB3  1 
ATOM   3257 H HB3  B PHE   A 1 156 ? 11.742 1.905   4.575   0.60 18.95 ?  156 PHE   A HB3  1 
ATOM   3258 H HB3  T PHE   A 1 156 ? 11.833 1.304   3.471   0.10 12.64 ?  156 PHE   A HB3  1 
ATOM   3259 H HD1  A PHE   A 1 156 ? 11.426 2.789   7.043   0.30 19.71 ?  156 PHE   A HD1  1 
ATOM   3260 H HD1  B PHE   A 1 156 ? 10.226 2.455   7.657   0.60 23.37 ?  156 PHE   A HD1  1 
ATOM   3261 H HD1  T PHE   A 1 156 ? 12.260 3.094   6.497   0.10 12.30 ?  156 PHE   A HD1  1 
ATOM   3262 H HD2  A PHE   A 1 156 ? 10.930 3.633   3.164   0.30 19.90 ?  156 PHE   A HD2  1 
ATOM   3263 H HD2  B PHE   A 1 156 ? 12.369 4.266   4.809   0.60 23.51 ?  156 PHE   A HD2  1 
ATOM   3264 H HD2  T PHE   A 1 156 ? 10.620 3.224   2.852   0.10 12.63 ?  156 PHE   A HD2  1 
ATOM   3265 H HE1  A PHE   A 1 156 ? 10.742 4.927   7.596   0.30 20.45 ?  156 PHE   A HE1  1 
ATOM   3266 H HE1  B PHE   A 1 156 ? 9.665  4.512   8.540   0.60 24.43 ?  156 PHE   A HE1  1 
ATOM   3267 H HE1  T PHE   A 1 156 ? 11.702 5.308   6.830   0.10 12.62 ?  156 PHE   A HE1  1 
ATOM   3268 H HE2  A PHE   A 1 156 ? 10.246 5.773   3.715   0.30 20.34 ?  156 PHE   A HE2  1 
ATOM   3269 H HE2  B PHE   A 1 156 ? 11.810 6.315   5.688   0.60 24.50 ?  156 PHE   A HE2  1 
ATOM   3270 H HE2  T PHE   A 1 156 ? 10.060 5.439   3.182   0.10 12.93 ?  156 PHE   A HE2  1 
ATOM   3271 H HZ   A PHE   A 1 156 ? 10.151 6.421   5.934   0.30 20.72 ?  156 PHE   A HZ   1 
ATOM   3272 H HZ   B PHE   A 1 156 ? 10.457 6.446   7.555   0.60 24.63 ?  156 PHE   A HZ   1 
ATOM   3273 H HZ   T PHE   A 1 156 ? 10.600 6.485   5.172   0.10 12.75 ?  156 PHE   A HZ   1 
ATOM   3274 N N    A ASP   A 1 157 ? 8.987  0.253   3.638   0.30 13.94 ?  157 ASP   A N    1 
ATOM   3275 N N    B ASP   A 1 157 ? 9.240  0.507   4.042   0.60 12.93 ?  157 ASP   A N    1 
ATOM   3276 N N    T ASP   A 1 157 ? 9.101  0.224   3.556   0.10 12.60 ?  157 ASP   A N    1 
ATOM   3277 C CA   A ASP   A 1 157 ? 7.653  0.505   3.106   0.30 14.54 ?  157 ASP   A CA   1 
ATOM   3278 C CA   B ASP   A 1 157 ? 7.997  0.805   3.332   0.60 13.25 ?  157 ASP   A CA   1 
ATOM   3279 C CA   T ASP   A 1 157 ? 7.767  0.473   3.023   0.10 13.29 ?  157 ASP   A CA   1 
ATOM   3280 C C    A ASP   A 1 157 ? 6.679  -0.531  3.655   0.30 15.21 ?  157 ASP   A C    1 
ATOM   3281 C C    B ASP   A 1 157 ? 6.913  -0.190  3.735   0.60 13.62 ?  157 ASP   A C    1 
ATOM   3282 C C    T ASP   A 1 157 ? 6.783  -0.523  3.626   0.10 14.09 ?  157 ASP   A C    1 
ATOM   3283 O O    A ASP   A 1 157 ? 6.808  -1.726  3.362   0.30 14.92 ?  157 ASP   A O    1 
ATOM   3284 O O    B ASP   A 1 157 ? 7.058  -1.402  3.527   0.60 14.23 ?  157 ASP   A O    1 
ATOM   3285 O O    T ASP   A 1 157 ? 6.960  -1.738  3.489   0.10 14.01 ?  157 ASP   A O    1 
ATOM   3286 C CB   A ASP   A 1 157 ? 7.697  0.442   1.583   0.30 15.29 ?  157 ASP   A CB   1 
ATOM   3287 C CB   B ASP   A 1 157 ? 8.240  0.758   1.824   0.60 13.45 ?  157 ASP   A CB   1 
ATOM   3288 C CB   T ASP   A 1 157 ? 7.793  0.344   1.503   0.10 13.34 ?  157 ASP   A CB   1 
ATOM   3289 C CG   A ASP   A 1 157 ? 6.441  0.978   0.938   0.30 16.16 ?  157 ASP   A CG   1 
ATOM   3290 C CG   B ASP   A 1 157 ? 7.038  1.209   1.022   0.60 13.77 ?  157 ASP   A CG   1 
ATOM   3291 C CG   T ASP   A 1 157 ? 6.582  0.972   0.843   0.10 13.35 ?  157 ASP   A CG   1 
ATOM   3292 O OD1  A ASP   A 1 157 ? 6.154  2.180   1.106   0.30 17.19 ?  157 ASP   A OD1  1 
ATOM   3293 O OD1  B ASP   A 1 157 ? 6.029  0.466   0.986   0.60 14.60 ?  157 ASP   A OD1  1 
ATOM   3294 O OD1  T ASP   A 1 157 ? 5.482  0.389   0.943   0.10 13.45 ?  157 ASP   A OD1  1 
ATOM   3295 O OD2  A ASP   A 1 157 ? 5.741  0.198   0.256   0.30 16.11 -1 157 ASP   A OD2  1 
ATOM   3296 O OD2  B ASP   A 1 157 ? 7.101  2.315   0.437   0.60 14.78 -1 157 ASP   A OD2  1 
ATOM   3297 O OD2  T ASP   A 1 157 ? 6.724  2.054   0.237   0.10 13.27 -1 157 ASP   A OD2  1 
ATOM   3298 H H    A ASP   A 1 157 ? 9.497  -0.204  3.116   0.30 16.72 ?  157 ASP   A H    1 
ATOM   3299 H H    B ASP   A 1 157 ? 9.844  0.118   3.566   0.60 15.51 ?  157 ASP   A H    1 
ATOM   3300 H H    T ASP   A 1 157 ? 9.594  -0.265  3.050   0.10 15.11 ?  157 ASP   A H    1 
ATOM   3301 H HA   A ASP   A 1 157 ? 7.357  1.387   3.379   0.30 17.44 ?  157 ASP   A HA   1 
ATOM   3302 H HA   B ASP   A 1 157 ? 7.710  1.704   3.571   0.60 15.89 ?  157 ASP   A HA   1 
ATOM   3303 H HA   T ASP   A 1 157 ? 7.484  1.373   3.254   0.10 15.94 ?  157 ASP   A HA   1 
ATOM   3304 H HB2  A ASP   A 1 157 ? 8.452  0.955   1.272   0.30 18.33 ?  157 ASP   A HB2  1 
ATOM   3305 H HB2  B ASP   A 1 157 ? 8.994  1.334   1.608   0.60 16.14 ?  157 ASP   A HB2  1 
ATOM   3306 H HB2  T ASP   A 1 157 ? 8.599  0.762   1.165   0.10 16.00 ?  157 ASP   A HB2  1 
ATOM   3307 H HB3  A ASP   A 1 157 ? 7.788  -0.479  1.312   0.30 18.33 ?  157 ASP   A HB3  1 
ATOM   3308 H HB3  B ASP   A 1 157 ? 8.445  -0.155  1.572   0.60 16.14 ?  157 ASP   A HB3  1 
ATOM   3309 H HB3  T ASP   A 1 157 ? 7.789  -0.596  1.268   0.10 16.00 ?  157 ASP   A HB3  1 
ATOM   3310 N N    A LYS   A 1 158 ? 5.702  -0.075  4.448   0.30 16.61 ?  158 LYS   A N    1 
ATOM   3311 N N    B LYS   A 1 158 ? 5.818  0.329   4.296   0.60 13.84 ?  158 LYS   A N    1 
ATOM   3312 N N    T LYS   A 1 158 ? 5.743  -0.009  4.289   0.10 15.06 ?  158 LYS   A N    1 
ATOM   3313 C CA   A LYS   A 1 158 ? 4.736  -0.998  5.042   0.30 17.92 ?  158 LYS   A CA   1 
ATOM   3314 C CA   B LYS   A 1 158 ? 4.779  -0.541  4.836   0.60 14.54 ?  158 LYS   A CA   1 
ATOM   3315 C CA   T LYS   A 1 158 ? 4.763  -0.889  4.919   0.10 16.10 ?  158 LYS   A CA   1 
ATOM   3316 C C    A LYS   A 1 158 ? 3.954  -1.742  3.966   0.30 18.03 ?  158 LYS   A C    1 
ATOM   3317 C C    B LYS   A 1 158 ? 4.114  -1.353  3.732   0.60 13.96 ?  158 LYS   A C    1 
ATOM   3318 C C    T LYS   A 1 158 ? 3.995  -1.697  3.880   0.10 16.45 ?  158 LYS   A C    1 
ATOM   3319 O O    A LYS   A 1 158 ? 3.718  -2.950  4.083   0.30 18.34 ?  158 LYS   A O    1 
ATOM   3320 O O    B LYS   A 1 158 ? 3.886  -2.559  3.885   0.60 14.89 ?  158 LYS   A O    1 
ATOM   3321 O O    T LYS   A 1 158 ? 3.780  -2.902  4.059   0.10 16.60 ?  158 LYS   A O    1 
ATOM   3322 C CB   A LYS   A 1 158 ? 3.792  -0.245  5.986   0.30 18.98 ?  158 LYS   A CB   1 
ATOM   3323 C CB   B LYS   A 1 158 ? 3.734  0.275   5.599   0.60 16.51 ?  158 LYS   A CB   1 
ATOM   3324 C CB   T LYS   A 1 158 ? 3.808  -0.072  5.794   0.10 16.74 ?  158 LYS   A CB   1 
ATOM   3325 C CG   A LYS   A 1 158 ? 2.542  -1.022  6.407   0.30 20.18 ?  158 LYS   A CG   1 
ATOM   3326 C CG   B LYS   A 1 158 ? 2.521  -0.562  5.993   0.60 18.10 ?  158 LYS   A CG   1 
ATOM   3327 C CG   T LYS   A 1 158 ? 2.580  -0.838  6.280   0.10 17.33 ?  158 LYS   A CG   1 
ATOM   3328 C CD   A LYS   A 1 158 ? 2.874  -2.277  7.207   0.30 21.14 ?  158 LYS   A CD   1 
ATOM   3329 C CD   B LYS   A 1 158 ? 1.406  0.265   6.585   0.60 19.72 ?  158 LYS   A CD   1 
ATOM   3330 C CD   T LYS   A 1 158 ? 2.957  -2.035  7.141   0.10 17.78 ?  158 LYS   A CD   1 
ATOM   3331 C CE   A LYS   A 1 158 ? 1.604  -2.986  7.665   0.30 21.82 ?  158 LYS   A CE   1 
ATOM   3332 C CE   B LYS   A 1 158 ? 0.238  -0.612  7.019   0.60 20.37 ?  158 LYS   A CE   1 
ATOM   3333 C CE   T LYS   A 1 158 ? 1.725  -2.835  7.538   0.10 18.09 ?  158 LYS   A CE   1 
ATOM   3334 N NZ   A LYS   A 1 158 ? 1.886  -4.290  8.327   0.30 22.01 ?  158 LYS   A NZ   1 
ATOM   3335 N NZ   B LYS   A 1 158 ? -0.378 -1.366  5.889   0.60 20.85 ?  158 LYS   A NZ   1 
ATOM   3336 N NZ   T LYS   A 1 158 ? 2.069  -4.047  8.333   0.10 18.13 ?  158 LYS   A NZ   1 
ATOM   3337 H H    A LYS   A 1 158 ? 5.580  0.751   4.654   0.30 19.92 ?  158 LYS   A H    1 
ATOM   3338 H H    B LYS   A 1 158 ? 5.660  1.174   4.364   0.60 16.60 ?  158 LYS   A H    1 
ATOM   3339 H H    T LYS   A 1 158 ? 5.585  0.831   4.384   0.10 18.07 ?  158 LYS   A H    1 
ATOM   3340 H HA   A LYS   A 1 158 ? 5.212  -1.655  5.572   0.30 21.50 ?  158 LYS   A HA   1 
ATOM   3341 H HA   B LYS   A 1 158 ? 5.194  -1.158  5.465   0.60 17.44 ?  158 LYS   A HA   1 
ATOM   3342 H HA   T LYS   A 1 158 ? 5.229  -1.512  5.496   0.10 19.31 ?  158 LYS   A HA   1 
ATOM   3343 H HB2  A LYS   A 1 158 ? 4.278  -0.018  6.798   0.30 22.77 ?  158 LYS   A HB2  1 
ATOM   3344 H HB2  B LYS   A 1 158 ? 4.139  0.627   6.414   0.60 19.80 ?  158 LYS   A HB2  1 
ATOM   3345 H HB2  T LYS   A 1 158 ? 4.290  0.235   6.580   0.10 20.08 ?  158 LYS   A HB2  1 
ATOM   3346 H HB3  A LYS   A 1 158 ? 3.496  0.569   5.550   0.30 22.77 ?  158 LYS   A HB3  1 
ATOM   3347 H HB3  B LYS   A 1 158 ? 3.434  1.006   5.039   0.60 19.80 ?  158 LYS   A HB3  1 
ATOM   3348 H HB3  T LYS   A 1 158 ? 3.494  0.692   5.286   0.10 20.08 ?  158 LYS   A HB3  1 
ATOM   3349 H HG2  A LYS   A 1 158 ? 1.996  -0.452  6.969   0.30 24.21 ?  158 LYS   A HG2  1 
ATOM   3350 H HG2  B LYS   A 1 158 ? 2.162  -1.008  5.211   0.60 21.72 ?  158 LYS   A HG2  1 
ATOM   3351 H HG2  T LYS   A 1 158 ? 2.034  -0.246  6.819   0.10 20.79 ?  158 LYS   A HG2  1 
ATOM   3352 H HG3  A LYS   A 1 158 ? 2.036  -1.285  5.622   0.30 24.21 ?  158 LYS   A HG3  1 
ATOM   3353 H HG3  B LYS   A 1 158 ? 2.801  -1.222  6.650   0.60 21.72 ?  158 LYS   A HG3  1 
ATOM   3354 H HG3  T LYS   A 1 158 ? 2.066  -1.156  5.521   0.10 20.79 ?  158 LYS   A HG3  1 
ATOM   3355 H HD2  A LYS   A 1 158 ? 3.381  -2.889  6.653   0.30 25.36 ?  158 LYS   A HD2  1 
ATOM   3356 H HD2  B LYS   A 1 158 ? 1.739  0.741   7.361   0.60 23.65 ?  158 LYS   A HD2  1 
ATOM   3357 H HD2  T LYS   A 1 158 ? 3.550  -2.619  6.645   0.10 21.33 ?  158 LYS   A HD2  1 
ATOM   3358 H HD3  A LYS   A 1 158 ? 3.385  -2.030  7.994   0.30 25.36 ?  158 LYS   A HD3  1 
ATOM   3359 H HD3  B LYS   A 1 158 ? 1.088  0.894   5.916   0.60 23.65 ?  158 LYS   A HD3  1 
ATOM   3360 H HD3  T LYS   A 1 158 ? 3.391  -1.723  7.951   0.10 21.33 ?  158 LYS   A HD3  1 
ATOM   3361 H HE2  A LYS   A 1 158 ? 1.136  -2.422  8.302   0.30 26.18 ?  158 LYS   A HE2  1 
ATOM   3362 H HE2  B LYS   A 1 158 ? 0.553  -1.256  7.670   0.60 24.43 ?  158 LYS   A HE2  1 
ATOM   3363 H HE2  T LYS   A 1 158 ? 1.142  -2.277  8.076   0.10 21.69 ?  158 LYS   A HE2  1 
ATOM   3364 H HE3  A LYS   A 1 158 ? 1.039  -3.156  6.895   0.30 26.18 ?  158 LYS   A HE3  1 
ATOM   3365 H HE3  B LYS   A 1 158 ? -0.448 -0.050  7.411   0.60 24.43 ?  158 LYS   A HE3  1 
ATOM   3366 H HE3  T LYS   A 1 158 ? 1.261  -3.124  6.735   0.10 21.69 ?  158 LYS   A HE3  1 
ATOM   3367 H HZ1  A LYS   A 1 158 ? 1.124  -4.675  8.581   0.30 26.41 ?  158 LYS   A HZ1  1 
ATOM   3368 H HZ1  B LYS   A 1 158 ? -1.067 -1.846  6.183   0.60 25.01 ?  158 LYS   A HZ1  1 
ATOM   3369 H HZ1  T LYS   A 1 158 ? 1.327  -4.492  8.547   0.10 21.74 ?  158 LYS   A HZ1  1 
ATOM   3370 H HZ2  A LYS   A 1 158 ? 2.310  -4.833  7.763   0.30 26.41 ?  158 LYS   A HZ2  1 
ATOM   3371 H HZ2  B LYS   A 1 158 ? -0.667 -0.799  5.266   0.60 25.01 ?  158 LYS   A HZ2  1 
ATOM   3372 H HZ2  T LYS   A 1 158 ? 2.598  -4.583  7.858   0.10 21.74 ?  158 LYS   A HZ2  1 
ATOM   3373 H HZ3  A LYS   A 1 158 ? 2.397  -4.163  9.045   0.30 26.41 ?  158 LYS   A HZ3  1 
ATOM   3374 H HZ3  B LYS   A 1 158 ? 0.222  -1.914  5.525   0.60 25.01 ?  158 LYS   A HZ3  1 
ATOM   3375 H HZ3  T LYS   A 1 158 ? 2.490  -3.812  9.080   0.10 21.74 ?  158 LYS   A HZ3  1 
ATOM   3376 N N    A ASN   A 1 159 ? 3.534  -1.037  2.915   0.30 17.99 ?  159 ASN   A N    1 
ATOM   3377 N N    B ASN   A 1 159 ? 3.757  -0.705  2.624   0.60 14.12 ?  159 ASN   A N    1 
ATOM   3378 N N    T ASN   A 1 159 ? 3.571  -1.057  2.797   0.10 16.72 ?  159 ASN   A N    1 
ATOM   3379 C CA   A ASN   A 1 159 ? 2.845  -1.708  1.818   0.30 17.66 ?  159 ASN   A CA   1 
ATOM   3380 C CA   B ASN   A 1 159 ? 3.088  -1.434  1.553   0.60 14.78 ?  159 ASN   A CA   1 
ATOM   3381 C CA   T ASN   A 1 159 ? 2.823  -1.743  1.748   0.10 16.85 ?  159 ASN   A CA   1 
ATOM   3382 C C    A ASN   A 1 159 ? 3.739  -2.756  1.168   0.30 17.39 ?  159 ASN   A C    1 
ATOM   3383 C C    B ASN   A 1 159 ? 3.982  -2.533  0.991   0.60 15.27 ?  159 ASN   A C    1 
ATOM   3384 C C    T ASN   A 1 159 ? 3.655  -2.839  1.090   0.10 16.87 ?  159 ASN   A C    1 
ATOM   3385 O O    A ASN   A 1 159 ? 3.268  -3.835  0.792   0.30 17.78 ?  159 ASN   A O    1 
ATOM   3386 O O    B ASN   A 1 159 ? 3.510  -3.632  0.682   0.60 15.30 ?  159 ASN   A O    1 
ATOM   3387 O O    T ASN   A 1 159 ? 3.125  -3.879  0.701   0.10 16.98 ?  159 ASN   A O    1 
ATOM   3388 C CB   A ASN   A 1 159 ? 2.355  -0.685  0.793   0.30 17.59 ?  159 ASN   A CB   1 
ATOM   3389 C CB   B ASN   A 1 159 ? 2.655  -0.468  0.453   0.60 16.34 ?  159 ASN   A CB   1 
ATOM   3390 C CB   T ASN   A 1 159 ? 2.334  -0.745  0.696   0.10 16.99 ?  159 ASN   A CB   1 
ATOM   3391 C CG   A ASN   A 1 159 ? 1.135  0.079   1.271   0.30 17.79 ?  159 ASN   A CG   1 
ATOM   3392 C CG   B ASN   A 1 159 ? 1.418  0.325   0.828   0.60 17.98 ?  159 ASN   A CG   1 
ATOM   3393 C CG   T ASN   A 1 159 ? 1.146  0.069   1.174   0.10 17.17 ?  159 ASN   A CG   1 
ATOM   3394 O OD1  A ASN   A 1 159 ? 0.302  -0.460  2.003   0.30 18.21 ?  159 ASN   A OD1  1 
ATOM   3395 O OD1  B ASN   A 1 159 ? 0.593  -0.128  1.619   0.60 19.13 ?  159 ASN   A OD1  1 
ATOM   3396 O OD1  T ASN   A 1 159 ? 0.321  -0.415  1.950   0.10 17.36 ?  159 ASN   A OD1  1 
ATOM   3397 N ND2  A ASN   A 1 159 ? 1.021  1.337   0.856   0.30 17.63 ?  159 ASN   A ND2  1 
ATOM   3398 N ND2  B ASN   A 1 159 ? 1.285  1.516   0.262   0.60 18.69 ?  159 ASN   A ND2  1 
ATOM   3399 N ND2  T ASN   A 1 159 ? 1.052  1.309   0.711   0.10 17.15 ?  159 ASN   A ND2  1 
ATOM   3400 H H    A ASN   A 1 159 ? 3.627  -0.189  2.823   0.30 21.58 ?  159 ASN   A H    1 
ATOM   3401 H H    B ASN   A 1 159 ? 3.891  0.129   2.479   0.60 16.93 ?  159 ASN   A H    1 
ATOM   3402 H H    T ASN   A 1 159 ? 3.701  -0.222  2.648   0.10 20.06 ?  159 ASN   A H    1 
ATOM   3403 H HA   A ASN   A 1 159 ? 2.068  -2.166  2.174   0.30 21.18 ?  159 ASN   A HA   1 
ATOM   3404 H HA   B ASN   A 1 159 ? 2.292  -1.853  1.915   0.60 17.73 ?  159 ASN   A HA   1 
ATOM   3405 H HA   T ASN   A 1 159 ? 2.045  -2.163  2.144   0.10 20.21 ?  159 ASN   A HA   1 
ATOM   3406 H HB2  A ASN   A 1 159 ? 3.064  -0.047  0.621   0.30 21.10 ?  159 ASN   A HB2  1 
ATOM   3407 H HB2  B ASN   A 1 159 ? 3.372  0.162   0.285   0.60 19.61 ?  159 ASN   A HB2  1 
ATOM   3408 H HB2  T ASN   A 1 159 ? 3.053  -0.130  0.484   0.10 20.39 ?  159 ASN   A HB2  1 
ATOM   3409 H HB3  A ASN   A 1 159 ? 2.116  -1.149  -0.023  0.30 21.10 ?  159 ASN   A HB3  1 
ATOM   3410 H HB3  B ASN   A 1 159 ? 2.459  -0.975  -0.349  0.60 19.61 ?  159 ASN   A HB3  1 
ATOM   3411 H HB3  T ASN   A 1 159 ? 2.065  -1.230  -0.099  0.10 20.39 ?  159 ASN   A HB3  1 
ATOM   3412 H HD21 A ASN   A 1 159 ? 0.350  1.815   1.100   0.30 21.15 ?  159 ASN   A HD21 1 
ATOM   3413 H HD21 B ASN   A 1 159 ? 0.595  1.996   0.441   0.60 22.43 ?  159 ASN   A HD21 1 
ATOM   3414 H HD21 T ASN   A 1 159 ? 0.396  1.810   0.953   0.10 20.57 ?  159 ASN   A HD21 1 
ATOM   3415 H HD22 A ASN   A 1 159 ? 1.624  1.676   0.342   0.30 21.15 ?  159 ASN   A HD22 1 
ATOM   3416 H HD22 B ASN   A 1 159 ? 1.880  1.799   -0.286  0.60 22.43 ?  159 ASN   A HD22 1 
ATOM   3417 H HD22 T ASN   A 1 159 ? 1.647  1.612   0.169   0.10 20.57 ?  159 ASN   A HD22 1 
ATOM   3418 N N    A LEU   A 1 160 ? 5.036  -2.465  1.036   0.30 16.84 ?  160 LEU   A N    1 
ATOM   3419 N N    B LEU   A 1 160 ? 5.278  -2.255  0.853   0.60 15.23 ?  160 LEU   A N    1 
ATOM   3420 N N    T LEU   A 1 160 ? 4.958  -2.607  0.969   0.10 16.81 ?  160 LEU   A N    1 
ATOM   3421 C CA   A LEU   A 1 160 ? 5.948  -3.474  0.510   0.30 16.56 ?  160 LEU   A CA   1 
ATOM   3422 C CA   B LEU   A 1 160 ? 6.205  -3.277  0.374   0.60 16.04 ?  160 LEU   A CA   1 
ATOM   3423 C CA   T LEU   A 1 160 ? 5.851  -3.603  0.388   0.10 16.73 ?  160 LEU   A CA   1 
ATOM   3424 C C    A LEU   A 1 160 ? 6.139  -4.613  1.504   0.30 16.19 ?  160 LEU   A C    1 
ATOM   3425 C C    B LEU   A 1 160 ? 6.271  -4.445  1.347   0.60 15.49 ?  160 LEU   A C    1 
ATOM   3426 O O    A LEU   A 1 160 ? 6.190  -5.785  1.110   0.30 16.21 ?  160 LEU   A O    1 
ATOM   3427 O O    B LEU   A 1 160 ? 6.214  -5.615  0.946   0.60 15.78 ?  160 LEU   A O    1 
ATOM   3428 C CB   A LEU   A 1 160 ? 7.293  -2.849  0.142   0.30 16.47 ?  160 LEU   A CB   1 
ATOM   3429 C CB   B LEU   A 1 160 ? 7.593  -2.667  0.177   0.60 16.92 ?  160 LEU   A CB   1 
ATOM   3430 C CB   T LEU   A 1 160 ? 7.239  -3.009  0.147   0.10 16.64 ?  160 LEU   A CB   1 
ATOM   3431 C CG   A LEU   A 1 160 ? 8.338  -3.866  -0.317  0.30 16.67 ?  160 LEU   A CG   1 
ATOM   3432 C CG   B LEU   A 1 160 ? 8.666  -3.712  -0.135  0.60 18.16 ?  160 LEU   A CG   1 
ATOM   3433 C CG   T LEU   A 1 160 ? 8.315  -4.002  -0.296  0.10 16.56 ?  160 LEU   A CG   1 
ATOM   3434 C CD1  A LEU   A 1 160 ? 7.805  -4.699  -1.471  0.30 16.79 ?  160 LEU   A CD1  1 
ATOM   3435 C CD1  B LEU   A 1 160 ? 8.319  -4.439  -1.424  0.60 18.38 ?  160 LEU   A CD1  1 
ATOM   3436 C CD1  T LEU   A 1 160 ? 7.877  -4.755  -1.540  0.10 16.57 ?  160 LEU   A CD1  1 
ATOM   3437 C CD2  A LEU   A 1 160 ? 9.632  -3.171  -0.700  0.30 16.66 ?  160 LEU   A CD2  1 
ATOM   3438 C CD2  B LEU   A 1 160 ? 10.045 -3.087  -0.211  0.60 18.70 ?  160 LEU   A CD2  1 
ATOM   3439 C CD2  T LEU   A 1 160 ? 9.632  -3.285  -0.537  0.10 16.51 ?  160 LEU   A CD2  1 
ATOM   3440 H H    A LEU   A 1 160 ? 5.401  -1.714  1.242   0.30 20.20 ?  160 LEU   A H    1 
ATOM   3441 H H    B LEU   A 1 160 ? 5.638  -1.493  1.032   0.60 18.27 ?  160 LEU   A H    1 
ATOM   3442 H H    T LEU   A 1 160 ? 5.349  -1.881  1.216   0.10 20.16 ?  160 LEU   A H    1 
ATOM   3443 H HA   A LEU   A 1 160 ? 5.564  -3.846  -0.292  0.30 19.87 ?  160 LEU   A HA   1 
ATOM   3444 H HA   B LEU   A 1 160 ? 5.896  -3.607  -0.479  0.60 19.24 ?  160 LEU   A HA   1 
ATOM   3445 H HB2  A LEU   A 1 160 ? 7.166  -2.192  -0.568  0.30 19.76 ?  160 LEU   A HB2  1 
ATOM   3446 H HB2  B LEU   A 1 160 ? 7.562  -2.034  -0.562  0.60 20.29 ?  160 LEU   A HB2  1 
ATOM   3447 H HB2  T LEU   A 1 160 ? 7.166  -2.321  -0.536  0.10 19.96 ?  160 LEU   A HB2  1 
ATOM   3448 H HB3  A LEU   A 1 160 ? 7.654  -2.423  0.930   0.30 19.76 ?  160 LEU   A HB3  1 
ATOM   3449 H HB3  B LEU   A 1 160 ? 7.852  -2.205  0.991   0.60 20.29 ?  160 LEU   A HB3  1 
ATOM   3450 H HB3  T LEU   A 1 160 ? 7.549  -2.617  0.976   0.10 19.96 ?  160 LEU   A HB3  1 
ATOM   3451 H HG   A LEU   A 1 160 ? 8.541  -4.465  0.419   0.30 20.00 ?  160 LEU   A HG   1 
ATOM   3452 H HG   B LEU   A 1 160 ? 8.691  -4.368  0.578   0.60 21.78 ?  160 LEU   A HG   1 
ATOM   3453 H HG   T LEU   A 1 160 ? 8.456  -4.648  0.414   0.10 19.86 ?  160 LEU   A HG   1 
ATOM   3454 H HD11 A LEU   A 1 160 ? 8.513  -5.274  -1.792  0.30 20.14 ?  160 LEU   A HD11 1 
ATOM   3455 H HD11 B LEU   A 1 160 ? 9.079  -4.976  -1.693  0.60 22.05 ?  160 LEU   A HD11 1 
ATOM   3456 H HD11 T LEU   A 1 160 ? 8.618  -5.292  -1.859  0.10 19.88 ?  160 LEU   A HD11 1 
ATOM   3457 H HD12 A LEU   A 1 160 ? 7.063  -5.240  -1.159  0.30 20.14 ?  160 LEU   A HD12 1 
ATOM   3458 H HD12 B LEU   A 1 160 ? 7.549  -5.010  -1.270  0.60 22.05 ?  160 LEU   A HD12 1 
ATOM   3459 H HD12 T LEU   A 1 160 ? 7.126  -5.326  -1.315  0.10 19.88 ?  160 LEU   A HD12 1 
ATOM   3460 H HD13 A LEU   A 1 160 ? 7.510  -4.105  -2.179  0.30 20.14 ?  160 LEU   A HD13 1 
ATOM   3461 H HD13 B LEU   A 1 160 ? 8.115  -3.785  -2.110  0.60 22.05 ?  160 LEU   A HD13 1 
ATOM   3462 H HD13 T LEU   A 1 160 ? 7.616  -4.114  -2.219  0.10 19.88 ?  160 LEU   A HD13 1 
ATOM   3463 H HD21 A LEU   A 1 160 ? 10.284 -3.839  -0.962  0.30 19.99 ?  160 LEU   A HD21 1 
ATOM   3464 H HD21 B LEU   A 1 160 ? 10.695 -3.784  -0.399  0.60 22.43 ?  160 LEU   A HD21 1 
ATOM   3465 H HD21 T LEU   A 1 160 ? 10.298 -3.934  -0.813  0.10 19.80 ?  160 LEU   A HD21 1 
ATOM   3466 H HD22 A LEU   A 1 160 ? 9.459  -2.567  -1.439  0.30 19.99 ?  160 LEU   A HD22 1 
ATOM   3467 H HD22 B LEU   A 1 160 ? 10.055 -2.425  -0.918  0.60 22.43 ?  160 LEU   A HD22 1 
ATOM   3468 H HD22 T LEU   A 1 160 ? 9.506  -2.622  -1.234  0.10 19.80 ?  160 LEU   A HD22 1 
ATOM   3469 H HD23 A LEU   A 1 160 ? 9.962  -2.671  0.065   0.30 19.99 ?  160 LEU   A HD23 1 
ATOM   3470 H HD23 B LEU   A 1 160 ? 10.249 -2.667  0.640   0.60 22.43 ?  160 LEU   A HD23 1 
ATOM   3471 H HD23 T LEU   A 1 160 ? 9.912  -2.852  0.285   0.10 19.80 ?  160 LEU   A HD23 1 
ATOM   3472 N N    A TYR   A 1 161 ? 6.256  -4.292  2.793   0.40 16.10 ?  161 TYR   A N    1 
ATOM   3473 N N    B TYR   A 1 161 ? 6.413  -4.142  2.635   0.60 15.33 ?  161 TYR   A N    1 
ATOM   3474 C CA   A TYR   A 1 161 ? 6.381  -5.337  3.803   0.40 15.82 ?  161 TYR   A CA   1 
ATOM   3475 C CA   B TYR   A 1 161 ? 6.449  -5.189  3.644   0.60 14.77 ?  161 TYR   A CA   1 
ATOM   3476 C C    A TYR   A 1 161 ? 5.221  -6.320  3.718   0.40 16.28 ?  161 TYR   A C    1 
ATOM   3477 C C    B TYR   A 1 161 ? 5.246  -6.117  3.515   0.60 15.35 ?  161 TYR   A C    1 
ATOM   3478 O O    A TYR   A 1 161 ? 5.421  -7.540  3.724   0.40 16.23 ?  161 TYR   A O    1 
ATOM   3479 O O    B TYR   A 1 161 ? 5.386  -7.346  3.518   0.60 14.76 ?  161 TYR   A O    1 
ATOM   3480 C CB   A TYR   A 1 161 ? 6.458  -4.720  5.200   0.40 15.83 ?  161 TYR   A CB   1 
ATOM   3481 C CB   B TYR   A 1 161 ? 6.503  -4.557  5.034   0.60 15.01 ?  161 TYR   A CB   1 
ATOM   3482 C CG   A TYR   A 1 161 ? 6.378  -5.752  6.300   0.40 15.52 ?  161 TYR   A CG   1 
ATOM   3483 C CG   B TYR   A 1 161 ? 6.398  -5.591  6.108   0.60 14.35 ?  161 TYR   A CG   1 
ATOM   3484 C CD1  A TYR   A 1 161 ? 7.491  -6.493  6.659   0.40 15.81 ?  161 TYR   A CD1  1 
ATOM   3485 C CD1  B TYR   A 1 161 ? 7.507  -6.319  6.501   0.60 14.50 ?  161 TYR   A CD1  1 
ATOM   3486 C CD2  A TYR   A 1 161 ? 5.186  -5.991  6.975   0.40 15.17 ?  161 TYR   A CD2  1 
ATOM   3487 C CD2  B TYR   A 1 161 ? 5.178  -5.872  6.707   0.60 14.25 ?  161 TYR   A CD2  1 
ATOM   3488 C CE1  A TYR   A 1 161 ? 7.423  -7.442  7.657   0.40 15.68 ?  161 TYR   A CE1  1 
ATOM   3489 C CE1  B TYR   A 1 161 ? 7.410  -7.287  7.472   0.60 14.62 ?  161 TYR   A CE1  1 
ATOM   3490 C CE2  A TYR   A 1 161 ? 5.109  -6.941  7.976   0.40 15.10 ?  161 TYR   A CE2  1 
ATOM   3491 C CE2  B TYR   A 1 161 ? 5.072  -6.838  7.675   0.60 14.22 ?  161 TYR   A CE2  1 
ATOM   3492 C CZ   A TYR   A 1 161 ? 6.232  -7.663  8.315   0.40 15.45 ?  161 TYR   A CZ   1 
ATOM   3493 C CZ   B TYR   A 1 161 ? 6.190  -7.542  8.057   0.60 14.78 ?  161 TYR   A CZ   1 
ATOM   3494 O OH   A TYR   A 1 161 ? 6.173  -8.613  9.311   0.40 15.84 ?  161 TYR   A OH   1 
ATOM   3495 O OH   B TYR   A 1 161 ? 6.097  -8.511  9.025   0.60 15.88 ?  161 TYR   A OH   1 
ATOM   3496 H H    A TYR   A 1 161 ? 6.268  -3.489  3.103   0.40 19.31 ?  161 TYR   A H    1 
ATOM   3497 H H    B TYR   A 1 161 ? 6.490  -3.343  2.944   0.60 18.39 ?  161 TYR   A H    1 
ATOM   3498 H HA   A TYR   A 1 161 ? 7.201  -5.829  3.652   0.40 18.97 ?  161 TYR   A HA   1 
ATOM   3499 H HA   B TYR   A 1 161 ? 7.250  -5.718  3.522   0.60 17.71 ?  161 TYR   A HA   1 
ATOM   3500 H HB2  A TYR   A 1 161 ? 7.304  -4.248  5.292   0.40 18.99 ?  161 TYR   A HB2  1 
ATOM   3501 H HB2  B TYR   A 1 161 ? 7.351  -4.094  5.141   0.60 18.00 ?  161 TYR   A HB2  1 
ATOM   3502 H HB3  A TYR   A 1 161 ? 5.721  -4.100  5.316   0.40 18.99 ?  161 TYR   A HB3  1 
ATOM   3503 H HB3  B TYR   A 1 161 ? 5.767  -3.934  5.133   0.60 18.00 ?  161 TYR   A HB3  1 
ATOM   3504 H HD1  A TYR   A 1 161 ? 8.298  -6.350  6.218   0.40 18.96 ?  161 TYR   A HD1  1 
ATOM   3505 H HD1  B TYR   A 1 161 ? 8.331  -6.150  6.104   0.60 17.40 ?  161 TYR   A HD1  1 
ATOM   3506 H HD2  A TYR   A 1 161 ? 4.427  -5.504  6.750   0.40 18.20 ?  161 TYR   A HD2  1 
ATOM   3507 H HD2  B TYR   A 1 161 ? 4.420  -5.397  6.449   0.60 17.09 ?  161 TYR   A HD2  1 
ATOM   3508 H HE1  A TYR   A 1 161 ? 8.178  -7.931  7.884   0.40 18.81 ?  161 TYR   A HE1  1 
ATOM   3509 H HE1  B TYR   A 1 161 ? 8.164  -7.769  7.730   0.60 17.53 ?  161 TYR   A HE1  1 
ATOM   3510 H HE2  A TYR   A 1 161 ? 4.305  -7.087  8.419   0.40 18.12 ?  161 TYR   A HE2  1 
ATOM   3511 H HE2  B TYR   A 1 161 ? 4.249  -7.009  8.069   0.60 17.05 ?  161 TYR   A HE2  1 
ATOM   3512 H HH   A TYR   A 1 161 ? 5.392  -8.639  9.625   0.40 19.00 ?  161 TYR   A HH   1 
ATOM   3513 H HH   B TYR   A 1 161 ? 5.291  -8.586  9.268   0.60 19.05 ?  161 TYR   A HH   1 
ATOM   3514 N N    A ASP   A 1 162 ? 3.993  -5.805  3.631   0.40 16.60 ?  162 ASP   A N    1 
ATOM   3515 N N    B ASP   A 1 162 ? 4.048  -5.539  3.393   0.60 16.17 ?  162 ASP   A N    1 
ATOM   3516 C CA   A ASP   A 1 162 ? 2.834  -6.690  3.575   0.40 16.98 ?  162 ASP   A CA   1 
ATOM   3517 C CA   B ASP   A 1 162 ? 2.845  -6.355  3.247   0.60 16.67 ?  162 ASP   A CA   1 
ATOM   3518 C C    A ASP   A 1 162 ? 2.874  -7.575  2.336   0.40 16.72 ?  162 ASP   A C    1 
ATOM   3519 C C    B ASP   A 1 162 ? 2.921  -7.230  2.001   0.60 16.52 ?  162 ASP   A C    1 
ATOM   3520 O O    A ASP   A 1 162 ? 2.522  -8.759  2.398   0.40 16.94 ?  162 ASP   A O    1 
ATOM   3521 O O    B ASP   A 1 162 ? 2.556  -8.412  2.035   0.60 16.42 ?  162 ASP   A O    1 
ATOM   3522 C CB   A ASP   A 1 162 ? 1.542  -5.872  3.617   0.40 17.64 ?  162 ASP   A CB   1 
ATOM   3523 C CB   B ASP   A 1 162 ? 1.606  -5.459  3.190   0.60 17.78 ?  162 ASP   A CB   1 
ATOM   3524 C CG   A ASP   A 1 162 ? 1.231  -5.341  5.000   0.40 18.49 ?  162 ASP   A CG   1 
ATOM   3525 C CG   B ASP   A 1 162 ? 1.323  -4.752  4.510   0.60 18.41 ?  162 ASP   A CG   1 
ATOM   3526 O OD1  A ASP   A 1 162 ? 1.871  -5.787  5.976   0.40 18.81 ?  162 ASP   A OD1  1 
ATOM   3527 O OD1  B ASP   A 1 162 ? 1.873  -5.168  5.548   0.60 18.95 ?  162 ASP   A OD1  1 
ATOM   3528 O OD2  A ASP   A 1 162 ? 0.340  -4.475  5.106   0.40 19.24 -1 162 ASP   A OD2  1 
ATOM   3529 O OD2  B ASP   A 1 162 ? 0.540  -3.778  4.512   0.60 19.00 -1 162 ASP   A OD2  1 
ATOM   3530 H H    A ASP   A 1 162 ? 3.809  -4.964  3.600   0.40 19.91 ?  162 ASP   A H    1 
ATOM   3531 H H    B ASP   A 1 162 ? 3.907  -4.687  3.390   0.60 19.39 ?  162 ASP   A H    1 
ATOM   3532 H HA   A ASP   A 1 162 ? 2.842  -7.269  4.349   0.40 20.37 ?  162 ASP   A HA   1 
ATOM   3533 H HA   B ASP   A 1 162 ? 2.759  -6.933  4.019   0.60 20.00 ?  162 ASP   A HA   1 
ATOM   3534 H HB2  A ASP   A 1 162 ? 1.623  -5.110  3.024   0.40 21.16 ?  162 ASP   A HB2  1 
ATOM   3535 H HB2  B ASP   A 1 162 ? 1.732  -4.783  2.504   0.60 21.33 ?  162 ASP   A HB2  1 
ATOM   3536 H HB3  A ASP   A 1 162 ? 0.799  -6.432  3.342   0.40 21.16 ?  162 ASP   A HB3  1 
ATOM   3537 H HB3  B ASP   A 1 162 ? 0.830  -6.004  2.976   0.60 21.33 ?  162 ASP   A HB3  1 
ATOM   3538 N N    A LYS   A 1 163 ? 3.307  -7.024  1.200   0.40 16.83 ?  163 LYS   A N    1 
ATOM   3539 N N    B LYS   A 1 163 ? 3.389  -6.662  0.886   0.60 17.09 ?  163 LYS   A N    1 
ATOM   3540 C CA   A LYS   A 1 163 ? 3.385  -7.826  -0.017  0.40 17.45 ?  163 LYS   A CA   1 
ATOM   3541 C CA   B LYS   A 1 163 ? 3.513  -7.437  -0.345  0.60 17.45 ?  163 LYS   A CA   1 
ATOM   3542 C C    A LYS   A 1 163 ? 4.483  -8.880  0.084   0.40 17.03 ?  163 LYS   A C    1 
ATOM   3543 C C    B LYS   A 1 163 ? 4.525  -8.567  -0.190  0.60 16.28 ?  163 LYS   A C    1 
ATOM   3544 O O    A LYS   A 1 163 ? 4.309  -10.014 -0.377  0.40 17.47 ?  163 LYS   A O    1 
ATOM   3545 O O    B LYS   A 1 163 ? 4.313  -9.675  -0.697  0.60 15.68 ?  163 LYS   A O    1 
ATOM   3546 C CB   A LYS   A 1 163 ? 3.614  -6.919  -1.226  0.40 18.96 ?  163 LYS   A CB   1 
ATOM   3547 C CB   B LYS   A 1 163 ? 3.923  -6.521  -1.500  0.60 19.39 ?  163 LYS   A CB   1 
ATOM   3548 C CG   A LYS   A 1 163 ? 3.609  -7.654  -2.555  0.40 20.69 ?  163 LYS   A CG   1 
ATOM   3549 C CG   B LYS   A 1 163 ? 4.025  -7.235  -2.845  0.60 21.96 ?  163 LYS   A CG   1 
ATOM   3550 C CD   A LYS   A 1 163 ? 3.998  -6.731  -3.695  0.40 22.14 ?  163 LYS   A CD   1 
ATOM   3551 C CD   B LYS   A 1 163 ? 4.614  -6.340  -3.929  0.60 24.18 ?  163 LYS   A CD   1 
ATOM   3552 C CE   A LYS   A 1 163 ? 3.873  -7.429  -5.037  0.40 23.30 ?  163 LYS   A CE   1 
ATOM   3553 C CE   B LYS   A 1 163 ? 4.486  -6.982  -5.309  0.60 25.82 ?  163 LYS   A CE   1 
ATOM   3554 N NZ   A LYS   A 1 163 ? 4.511  -6.648  -6.133  0.40 23.79 ?  163 LYS   A NZ   1 
ATOM   3555 N NZ   B LYS   A 1 163 ? 5.197  -6.202  -6.362  0.60 26.81 ?  163 LYS   A NZ   1 
ATOM   3556 H H    A LYS   A 1 163 ? 3.552  -6.203  1.111   0.40 20.19 ?  163 LYS   A H    1 
ATOM   3557 H H    B LYS   A 1 163 ? 3.626  -5.836  0.820   0.60 20.50 ?  163 LYS   A H    1 
ATOM   3558 H HA   A LYS   A 1 163 ? 2.539  -8.281  -0.146  0.40 20.93 ?  163 LYS   A HA   1 
ATOM   3559 H HA   B LYS   A 1 163 ? 2.650  -7.825  -0.560  0.60 20.93 ?  163 LYS   A HA   1 
ATOM   3560 H HB2  A LYS   A 1 163 ? 2.908  -6.251  -1.258  0.40 22.75 ?  163 LYS   A HB2  1 
ATOM   3561 H HB2  B LYS   A 1 163 ? 3.261  -5.814  -1.592  0.60 23.26 ?  163 LYS   A HB2  1 
ATOM   3562 H HB3  A LYS   A 1 163 ? 4.473  -6.482  -1.133  0.40 22.75 ?  163 LYS   A HB3  1 
ATOM   3563 H HB3  B LYS   A 1 163 ? 4.789  -6.134  -1.303  0.60 23.26 ?  163 LYS   A HB3  1 
ATOM   3564 H HG2  A LYS   A 1 163 ? 4.249  -8.382  -2.526  0.40 24.82 ?  163 LYS   A HG2  1 
ATOM   3565 H HG2  B LYS   A 1 163 ? 4.600  -8.012  -2.754  0.60 26.35 ?  163 LYS   A HG2  1 
ATOM   3566 H HG3  A LYS   A 1 163 ? 2.718  -7.996  -2.730  0.40 24.82 ?  163 LYS   A HG3  1 
ATOM   3567 H HG3  B LYS   A 1 163 ? 3.138  -7.509  -3.126  0.60 26.35 ?  163 LYS   A HG3  1 
ATOM   3568 H HD2  A LYS   A 1 163 ? 3.410  -5.959  -3.698  0.40 26.56 ?  163 LYS   A HD2  1 
ATOM   3569 H HD2  B LYS   A 1 163 ? 4.140  -5.496  -3.941  0.60 29.00 ?  163 LYS   A HD2  1 
ATOM   3570 H HD3  A LYS   A 1 163 ? 4.920  -6.450  -3.581  0.40 26.56 ?  163 LYS   A HD3  1 
ATOM   3571 H HD3  B LYS   A 1 163 ? 5.557  -6.197  -3.748  0.60 29.00 ?  163 LYS   A HD3  1 
ATOM   3572 H HE2  A LYS   A 1 163 ? 4.295  -8.300  -4.988  0.40 27.95 ?  163 LYS   A HE2  1 
ATOM   3573 H HE2  B LYS   A 1 163 ? 4.865  -7.874  -5.285  0.60 30.97 ?  163 LYS   A HE2  1 
ATOM   3574 H HE3  A LYS   A 1 163 ? 2.935  -7.529  -5.252  0.40 27.95 ?  163 LYS   A HE3  1 
ATOM   3575 H HE3  B LYS   A 1 163 ? 3.547  -7.029  -5.551  0.60 30.97 ?  163 LYS   A HE3  1 
ATOM   3576 H HZ1  A LYS   A 1 163 ? 4.424  -7.081  -6.906  0.40 28.54 ?  163 LYS   A HZ1  1 
ATOM   3577 H HZ1  B LYS   A 1 163 ? 5.154  -6.632  -7.140  0.60 32.16 ?  163 LYS   A HZ1  1 
ATOM   3578 H HZ2  A LYS   A 1 163 ? 4.124  -5.850  -6.203  0.40 28.54 ?  163 LYS   A HZ2  1 
ATOM   3579 H HZ2  B LYS   A 1 163 ? 4.821  -5.401  -6.452  0.60 32.16 ?  163 LYS   A HZ2  1 
ATOM   3580 H HZ3  A LYS   A 1 163 ? 5.378  -6.534  -5.962  0.40 28.54 ?  163 LYS   A HZ3  1 
ATOM   3581 H HZ3  B LYS   A 1 163 ? 6.051  -6.098  -6.137  0.60 32.16 ?  163 LYS   A HZ3  1 
ATOM   3582 N N    A LEU   A 1 164 ? 5.624  -8.526  0.678   0.40 15.70 ?  164 LEU   A N    1 
ATOM   3583 N N    B LEU   A 1 164 ? 5.641  -8.303  0.493   0.60 15.26 ?  164 LEU   A N    1 
ATOM   3584 C CA   A LEU   A 1 164 ? 6.705  -9.494  0.840   0.40 14.88 ?  164 LEU   A CA   1 
ATOM   3585 C CA   B LEU   A 1 164 ? 6.673  -9.323  0.658   0.60 15.10 ?  164 LEU   A CA   1 
ATOM   3586 C C    A LEU   A 1 164 ? 6.262  -10.673 1.695   0.40 14.98 ?  164 LEU   A C    1 
ATOM   3587 C C    B LEU   A 1 164 ? 6.176  -10.479 1.513   0.60 14.67 ?  164 LEU   A C    1 
ATOM   3588 O O    A LEU   A 1 164 ? 6.561  -11.831 1.378   0.40 14.66 ?  164 LEU   A O    1 
ATOM   3589 O O    B LEU   A 1 164 ? 6.428  -11.648 1.197   0.60 14.66 ?  164 LEU   A O    1 
ATOM   3590 C CB   A LEU   A 1 164 ? 7.916  -8.811  1.468   0.40 14.12 ?  164 LEU   A CB   1 
ATOM   3591 C CB   B LEU   A 1 164 ? 7.910  -8.700  1.295   0.60 15.17 ?  164 LEU   A CB   1 
ATOM   3592 C CG   A LEU   A 1 164 ? 8.683  -7.844  0.570   0.40 14.25 ?  164 LEU   A CG   1 
ATOM   3593 C CG   B LEU   A 1 164 ? 8.752  -7.798  0.397   0.60 15.58 ?  164 LEU   A CG   1 
ATOM   3594 C CD1  A LEU   A 1 164 ? 9.586  -6.975  1.419   0.40 14.30 ?  164 LEU   A CD1  1 
ATOM   3595 C CD1  B LEU   A 1 164 ? 9.768  -7.057  1.240   0.60 15.96 ?  164 LEU   A CD1  1 
ATOM   3596 C CD2  A LEU   A 1 164 ? 9.496  -8.602  -0.464  0.40 14.31 ?  164 LEU   A CD2  1 
ATOM   3597 C CD2  B LEU   A 1 164 ? 9.446  -8.608  -0.686  0.60 15.89 ?  164 LEU   A CD2  1 
ATOM   3598 H H    A LEU   A 1 164 ? 5.792  -7.742  0.990   0.40 18.83 ?  164 LEU   A H    1 
ATOM   3599 H H    B LEU   A 1 164 ? 5.822  -7.545  0.864   0.60 18.31 ?  164 LEU   A H    1 
ATOM   3600 H HA   A LEU   A 1 164 ? 6.963  -9.830  -0.031  0.40 17.85 ?  164 LEU   A HA   1 
ATOM   3601 H HA   B LEU   A 1 164 ? 6.916  -9.670  -0.212  0.60 18.12 ?  164 LEU   A HA   1 
ATOM   3602 H HB2  A LEU   A 1 164 ? 7.618  -8.306  2.240   0.40 16.93 ?  164 LEU   A HB2  1 
ATOM   3603 H HB2  B LEU   A 1 164 ? 7.626  -8.165  2.053   0.60 18.19 ?  164 LEU   A HB2  1 
ATOM   3604 H HB3  A LEU   A 1 164 ? 8.542  -9.494  1.749   0.40 16.93 ?  164 LEU   A HB3  1 
ATOM   3605 H HB3  B LEU   A 1 164 ? 8.485  -9.415  1.603   0.60 18.19 ?  164 LEU   A HB3  1 
ATOM   3606 H HG   A LEU   A 1 164 ? 8.058  -7.266  0.103   0.40 17.09 ?  164 LEU   A HG   1 
ATOM   3607 H HG   B LEU   A 1 164 ? 8.178  -7.143  -0.032  0.60 18.69 ?  164 LEU   A HG   1 
ATOM   3608 H HD11 A LEU   A 1 164 ? 10.029 -6.327  0.850   0.40 17.15 ?  164 LEU   A HD11 1 
ATOM   3609 H HD11 B LEU   A 1 164 ? 10.307 -6.494  0.664   0.60 19.14 ?  164 LEU   A HD11 1 
ATOM   3610 H HD12 A LEU   A 1 164 ? 9.047  -6.521  2.085   0.40 17.15 ?  164 LEU   A HD12 1 
ATOM   3611 H HD12 B LEU   A 1 164 ? 9.300  -6.513  1.893   0.60 19.14 ?  164 LEU   A HD12 1 
ATOM   3612 H HD13 A LEU   A 1 164 ? 10.244 -7.539  1.855   0.40 17.15 ?  164 LEU   A HD13 1 
ATOM   3613 H HD13 B LEU   A 1 164 ? 10.332 -7.705  1.693   0.60 19.14 ?  164 LEU   A HD13 1 
ATOM   3614 H HD21 A LEU   A 1 164 ? 10.004 -7.968  -0.995  0.40 17.17 ?  164 LEU   A HD21 1 
ATOM   3615 H HD21 B LEU   A 1 164 ? 10.053 -8.029  -1.173  0.60 19.06 ?  164 LEU   A HD21 1 
ATOM   3616 H HD22 A LEU   A 1 164 ? 10.100 -9.208  -0.007  0.40 17.17 ?  164 LEU   A HD22 1 
ATOM   3617 H HD22 B LEU   A 1 164 ? 9.941  -9.331  -0.270  0.60 19.06 ?  164 LEU   A HD22 1 
ATOM   3618 H HD23 A LEU   A 1 164 ? 8.893  -9.103  -1.034  0.40 17.17 ?  164 LEU   A HD23 1 
ATOM   3619 H HD23 B LEU   A 1 164 ? 8.778  -8.969  -1.289  0.60 19.06 ?  164 LEU   A HD23 1 
ATOM   3620 N N    A VAL   A 1 165 ? 5.553  -10.398 2.789   0.40 15.14 ?  165 VAL   A N    1 
ATOM   3621 N N    B VAL   A 1 165 ? 5.485  -10.172 2.609   0.60 14.05 ?  165 VAL   A N    1 
ATOM   3622 C CA   A VAL   A 1 165 ? 5.080  -11.468 3.660   0.40 15.39 ?  165 VAL   A CA   1 
ATOM   3623 C CA   B VAL   A 1 165 ? 4.974  -11.227 3.478   0.60 14.05 ?  165 VAL   A CA   1 
ATOM   3624 C C    A VAL   A 1 165 ? 4.039  -12.320 2.943   0.40 15.54 ?  165 VAL   A C    1 
ATOM   3625 C C    B VAL   A 1 165 ? 3.953  -12.076 2.734   0.60 13.71 ?  165 VAL   A C    1 
ATOM   3626 O O    A VAL   A 1 165 ? 4.142  -13.551 2.896   0.40 15.56 ?  165 VAL   A O    1 
ATOM   3627 O O    B VAL   A 1 165 ? 4.025  -13.310 2.730   0.60 13.44 ?  165 VAL   A O    1 
ATOM   3628 C CB   A VAL   A 1 165 ? 4.534  -10.881 4.975   0.40 15.57 ?  165 VAL   A CB   1 
ATOM   3629 C CB   B VAL   A 1 165 ? 4.393  -10.621 4.768   0.60 14.76 ?  165 VAL   A CB   1 
ATOM   3630 C CG1  A VAL   A 1 165 ? 3.784  -11.942 5.765   0.40 15.47 ?  165 VAL   A CG1  1 
ATOM   3631 C CG1  B VAL   A 1 165 ? 3.620  -11.669 5.558   0.60 14.69 ?  165 VAL   A CG1  1 
ATOM   3632 C CG2  A VAL   A 1 165 ? 5.667  -10.285 5.803   0.40 15.80 ?  165 VAL   A CG2  1 
ATOM   3633 C CG2  B VAL   A 1 165 ? 5.508  -10.024 5.612   0.60 15.14 ?  165 VAL   A CG2  1 
ATOM   3634 H H    A VAL   A 1 165 ? 5.339  -9.606  3.047   0.40 18.17 ?  165 VAL   A H    1 
ATOM   3635 H H    B VAL   A 1 165 ? 5.300  -9.372  2.867   0.60 16.86 ?  165 VAL   A H    1 
ATOM   3636 H HA   A VAL   A 1 165 ? 5.830  -12.039 3.888   0.40 18.46 ?  165 VAL   A HA   1 
ATOM   3637 H HA   B VAL   A 1 165 ? 5.708  -11.804 3.732   0.60 16.85 ?  165 VAL   A HA   1 
ATOM   3638 H HB   A VAL   A 1 165 ? 3.912  -10.165 4.769   0.40 18.68 ?  165 VAL   A HB   1 
ATOM   3639 H HB   B VAL   A 1 165 ? 3.779  -9.905  4.538   0.60 17.71 ?  165 VAL   A HB   1 
ATOM   3640 H HG11 A VAL   A 1 165 ? 3.697  -11.648 6.685   0.40 18.56 ?  165 VAL   A HG11 1 
ATOM   3641 H HG11 B VAL   A 1 165 ? 3.504  -11.356 6.470   0.60 17.62 ?  165 VAL   A HG11 1 
ATOM   3642 H HG12 A VAL   A 1 165 ? 2.903  -12.063 5.375   0.40 18.56 ?  165 VAL   A HG12 1 
ATOM   3643 H HG12 B VAL   A 1 165 ? 2.752  -11.803 5.146   0.60 17.62 ?  165 VAL   A HG12 1 
ATOM   3644 H HG13 A VAL   A 1 165 ? 4.282  -12.772 5.729   0.40 18.56 ?  165 VAL   A HG13 1 
ATOM   3645 H HG13 B VAL   A 1 165 ? 4.121  -12.499 5.557   0.60 17.62 ?  165 VAL   A HG13 1 
ATOM   3646 H HG21 A VAL   A 1 165 ? 5.301  -9.919  6.625   0.40 18.95 ?  165 VAL   A HG21 1 
ATOM   3647 H HG21 B VAL   A 1 165 ? 5.129  -9.654  6.424   0.60 18.15 ?  165 VAL   A HG21 1 
ATOM   3648 H HG22 A VAL   A 1 165 ? 6.308  -10.983 6.009   0.40 18.95 ?  165 VAL   A HG22 1 
ATOM   3649 H HG22 B VAL   A 1 165 ? 6.145  -10.723 5.832   0.60 18.15 ?  165 VAL   A HG22 1 
ATOM   3650 H HG23 A VAL   A 1 165 ? 6.096  -9.581  5.292   0.40 18.95 ?  165 VAL   A HG23 1 
ATOM   3651 H HG23 B VAL   A 1 165 ? 5.948  -9.324  5.104   0.60 18.15 ?  165 VAL   A HG23 1 
ATOM   3652 N N    A SER   A 1 166 ? 3.018  -11.675 2.373   0.40 15.56 ?  166 SER   A N    1 
ATOM   3653 N N    B SER   A 1 166 ? 2.998  -11.425 2.071   0.60 13.96 ?  166 SER   A N    1 
ATOM   3654 C CA   A SER   A 1 166 ? 1.920  -12.419 1.763   0.40 15.74 ?  166 SER   A CA   1 
ATOM   3655 C CA   B SER   A 1 166 ? 1.890  -12.162 1.478   0.60 14.90 ?  166 SER   A CA   1 
ATOM   3656 C C    A SER   A 1 166 ? 2.392  -13.287 0.605   0.40 16.13 ?  166 SER   A C    1 
ATOM   3657 C C    B SER   A 1 166 ? 2.320  -13.015 0.293   0.60 14.50 ?  166 SER   A C    1 
ATOM   3658 O O    A SER   A 1 166 ? 1.813  -14.351 0.355   0.40 16.72 ?  166 SER   A O    1 
ATOM   3659 O O    B SER   A 1 166 ? 1.591  -13.945 -0.072  0.60 14.90 ?  166 SER   A O    1 
ATOM   3660 C CB   A SER   A 1 166 ? 0.831  -11.457 1.278   0.40 16.11 ?  166 SER   A CB   1 
ATOM   3661 C CB   B SER   A 1 166 ? 0.782  -11.200 1.049   0.60 16.74 ?  166 SER   A CB   1 
ATOM   3662 O OG   A SER   A 1 166 ? 0.216  -10.761 2.351   0.40 16.40 ?  166 SER   A OG   1 
ATOM   3663 O OG   B SER   A 1 166 ? 1.141  -10.511 -0.131  0.60 18.52 ?  166 SER   A OG   1 
ATOM   3664 H H    A SER   A 1 166 ? 2.938  -10.824 2.337   0.40 18.66 ?  166 SER   A H    1 
ATOM   3665 H H    B SER   A 1 166 ? 2.966  -10.572 1.956   0.60 16.74 ?  166 SER   A H    1 
ATOM   3666 H HA   A SER   A 1 166 ? 1.527  -13.005 2.429   0.40 18.88 ?  166 SER   A HA   1 
ATOM   3667 H HA   B SER   A 1 166 ? 1.516  -12.757 2.143   0.60 17.88 ?  166 SER   A HA   1 
ATOM   3668 H HB2  A SER   A 1 166 ? 1.229  -10.812 0.675   0.40 19.32 ?  166 SER   A HB2  1 
ATOM   3669 H HB2  B SER   A 1 166 ? -0.034 -11.704 0.890   0.60 20.08 ?  166 SER   A HB2  1 
ATOM   3670 H HB3  A SER   A 1 166 ? 0.150  -11.967 0.811   0.40 19.32 ?  166 SER   A HB3  1 
ATOM   3671 H HB3  B SER   A 1 166 ? 0.632  -10.549 1.754   0.60 20.08 ?  166 SER   A HB3  1 
ATOM   3672 H HG   A SER   A 1 166 ? 0.797  -10.313 2.767   0.40 19.67 ?  166 SER   A HG   1 
ATOM   3673 H HG   B SER   A 1 166 ? 0.518  -9.992  -0.365  0.60 22.21 ?  166 SER   A HG   1 
ATOM   3674 N N    A SER   A 1 167 ? 3.433  -12.863 -0.109  0.40 16.71 ?  167 SER   A N    1 
ATOM   3675 N N    B SER   A 1 167 ? 3.471  -12.726 -0.317  0.60 14.74 ?  167 SER   A N    1 
ATOM   3676 C CA   A SER   A 1 167 ? 3.889  -13.566 -1.301  0.40 17.38 ?  167 SER   A CA   1 
ATOM   3677 C CA   B SER   A 1 167 ? 3.936  -13.475 -1.477  0.60 15.74 ?  167 SER   A CA   1 
ATOM   3678 C C    A SER   A 1 167 ? 5.049  -14.515 -1.036  0.40 17.23 ?  167 SER   A C    1 
ATOM   3679 C C    B SER   A 1 167 ? 5.064  -14.449 -1.150  0.60 15.69 ?  167 SER   A C    1 
ATOM   3680 O O    A SER   A 1 167 ? 5.571  -15.110 -1.984  0.40 17.74 ?  167 SER   A O    1 
ATOM   3681 O O    B SER   A 1 167 ? 5.520  -15.172 -2.043  0.60 16.86 ?  167 SER   A O    1 
ATOM   3682 C CB   A SER   A 1 167 ? 4.290  -12.564 -2.390  0.40 18.01 ?  167 SER   A CB   1 
ATOM   3683 C CB   B SER   A 1 167 ? 4.377  -12.517 -2.592  0.60 16.38 ?  167 SER   A CB   1 
ATOM   3684 O OG   A SER   A 1 167 ? 5.378  -11.758 -1.966  0.40 18.40 ?  167 SER   A OG   1 
ATOM   3685 O OG   B SER   A 1 167 ? 5.459  -11.704 -2.165  0.60 16.80 ?  167 SER   A OG   1 
ATOM   3686 H H    A SER   A 1 167 ? 3.897  -12.162 0.082   0.40 20.04 ?  167 SER   A H    1 
ATOM   3687 H H    B SER   A 1 167 ? 4.004  -12.087 -0.071  0.60 17.68 ?  167 SER   A H    1 
ATOM   3688 H HA   A SER   A 1 167 ? 3.152  -14.089 -1.646  0.40 20.85 ?  167 SER   A HA   1 
ATOM   3689 H HA   B SER   A 1 167 ? 3.194  -13.990 -1.820  0.60 18.88 ?  167 SER   A HA   1 
ATOM   3690 H HB2  A SER   A 1 167 ? 4.552  -13.055 -3.186  0.40 21.61 ?  167 SER   A HB2  1 
ATOM   3691 H HB2  B SER   A 1 167 ? 4.658  -13.039 -3.360  0.60 19.65 ?  167 SER   A HB2  1 
ATOM   3692 H HB3  A SER   A 1 167 ? 3.529  -11.997 -2.590  0.40 21.61 ?  167 SER   A HB3  1 
ATOM   3693 H HB3  B SER   A 1 167 ? 3.622  -11.952 -2.842  0.60 19.65 ?  167 SER   A HB3  1 
ATOM   3694 H HG   A SER   A 1 167 ? 5.158  -11.320 -1.284  0.40 22.07 ?  167 SER   A HG   1 
ATOM   3695 H HG   B SER   A 1 167 ? 5.214  -11.229 -1.515  0.60 20.16 ?  167 SER   A HG   1 
ATOM   3696 N N    A PHE   A 1 168 ? 5.466  -14.678 0.217   0.40 16.80 ?  168 PHE   A N    1 
ATOM   3697 N N    B PHE   A 1 168 ? 5.513  -14.499 0.101   0.60 14.80 ?  168 PHE   A N    1 
ATOM   3698 C CA   A PHE   A 1 168 ? 6.637  -15.491 0.509   0.40 16.63 ?  168 PHE   A CA   1 
ATOM   3699 C CA   B PHE   A 1 168 ? 6.685  -15.297 0.436   0.60 14.72 ?  168 PHE   A CA   1 
ATOM   3700 C C    A PHE   A 1 168 ? 6.310  -16.971 0.379   0.40 18.22 ?  168 PHE   A C    1 
ATOM   3701 C C    B PHE   A 1 168 ? 6.344  -16.780 0.447   0.60 14.85 ?  168 PHE   A C    1 
ATOM   3702 O O    A PHE   A 1 168 ? 5.283  -17.438 0.881   0.40 19.12 ?  168 PHE   A O    1 
ATOM   3703 O O    B PHE   A 1 168 ? 5.394  -17.208 1.114   0.60 15.96 ?  168 PHE   A O    1 
ATOM   3704 C CB   A PHE   A 1 168 ? 7.172  -15.212 1.911   0.40 15.47 ?  168 PHE   A CB   1 
ATOM   3705 C CB   B PHE   A 1 168 ? 7.233  -14.898 1.802   0.60 15.03 ?  168 PHE   A CB   1 
ATOM   3706 C CG   A PHE   A 1 168 ? 8.415  -15.988 2.227   0.40 14.12 ?  168 PHE   A CG   1 
ATOM   3707 C CG   B PHE   A 1 168 ? 8.477  -15.645 2.174   0.60 14.99 ?  168 PHE   A CG   1 
ATOM   3708 C CD1  A PHE   A 1 168 ? 9.612  -15.662 1.615   0.40 13.90 ?  168 PHE   A CD1  1 
ATOM   3709 C CD1  B PHE   A 1 168 ? 9.688  -15.282 1.622   0.60 15.49 ?  168 PHE   A CD1  1 
ATOM   3710 C CD2  A PHE   A 1 168 ? 8.389  -17.060 3.105   0.40 13.78 ?  168 PHE   A CD2  1 
ATOM   3711 C CD2  B PHE   A 1 168 ? 8.439  -16.722 3.044   0.60 14.81 ?  168 PHE   A CD2  1 
ATOM   3712 C CE1  A PHE   A 1 168 ? 10.760 -16.380 1.878   0.40 13.25 ?  168 PHE   A CE1  1 
ATOM   3713 C CE1  B PHE   A 1 168 ? 10.841 -15.965 1.939   0.60 15.73 ?  168 PHE   A CE1  1 
ATOM   3714 C CE2  A PHE   A 1 168 ? 9.539  -17.781 3.376   0.40 13.87 ?  168 PHE   A CE2  1 
ATOM   3715 C CE2  B PHE   A 1 168 ? 9.596  -17.412 3.366   0.60 15.43 ?  168 PHE   A CE2  1 
ATOM   3716 C CZ   A PHE   A 1 168 ? 10.727 -17.437 2.762   0.40 13.65 ?  168 PHE   A CZ   1 
ATOM   3717 C CZ   B PHE   A 1 168 ? 10.797 -17.031 2.811   0.60 15.38 ?  168 PHE   A CZ   1 
ATOM   3718 H H    A PHE   A 1 168 ? 5.095  -14.327 0.908   0.40 20.16 ?  168 PHE   A H    1 
ATOM   3719 H H    B PHE   A 1 168 ? 5.161  -14.075 0.766   0.60 17.75 ?  168 PHE   A H    1 
ATOM   3720 H HA   A PHE   A 1 168 ? 7.335  -15.282 -0.127  0.40 19.94 ?  168 PHE   A HA   1 
ATOM   3721 H HA   B PHE   A 1 168 ? 7.375  -15.139 -0.231  0.60 17.65 ?  168 PHE   A HA   1 
ATOM   3722 H HB2  A PHE   A 1 168 ? 7.384  -14.267 1.983   0.40 18.56 ?  168 PHE   A HB2  1 
ATOM   3723 H HB2  B PHE   A 1 168 ? 7.442  -13.948 1.793   0.60 18.03 ?  168 PHE   A HB2  1 
ATOM   3724 H HB3  A PHE   A 1 168 ? 6.494  -15.450 2.562   0.40 18.56 ?  168 PHE   A HB3  1 
ATOM   3725 H HB3  B PHE   A 1 168 ? 6.560  -15.080 2.474   0.60 18.03 ?  168 PHE   A HB3  1 
ATOM   3726 H HD1  A PHE   A 1 168 ? 9.643  -14.951 1.017   0.40 16.67 ?  168 PHE   A HD1  1 
ATOM   3727 H HD1  B PHE   A 1 168 ? 9.728  -14.561 1.032   0.60 18.58 ?  168 PHE   A HD1  1 
ATOM   3728 H HD2  A PHE   A 1 168 ? 7.590  -17.297 3.519   0.40 16.53 ?  168 PHE   A HD2  1 
ATOM   3729 H HD2  B PHE   A 1 168 ? 7.628  -16.979 3.416   0.60 17.76 ?  168 PHE   A HD2  1 
ATOM   3730 H HE1  A PHE   A 1 168 ? 11.562 -16.146 1.463   0.40 15.90 ?  168 PHE   A HE1  1 
ATOM   3731 H HE1  B PHE   A 1 168 ? 11.656 -15.703 1.563   0.60 18.87 ?  168 PHE   A HE1  1 
ATOM   3732 H HE2  A PHE   A 1 168 ? 9.511  -18.498 3.969   0.40 16.64 ?  168 PHE   A HE2  1 
ATOM   3733 H HE2  B PHE   A 1 168 ? 9.560  -18.129 3.953   0.60 18.51 ?  168 PHE   A HE2  1 
ATOM   3734 H HZ   A PHE   A 1 168 ? 11.502 -17.922 2.941   0.40 16.38 ?  168 PHE   A HZ   1 
ATOM   3735 H HZ   B PHE   A 1 168 ? 11.577 -17.489 3.026   0.60 18.45 ?  168 PHE   A HZ   1 
ATOM   3736 N N    A LEU   A 1 169 ? 7.194  -17.709 -0.285  0.40 19.80 ?  169 LEU   A N    1 
ATOM   3737 N N    B LEU   A 1 169 ? 7.135  -17.569 -0.274  0.60 16.13 ?  169 LEU   A N    1 
ATOM   3738 C CA   A LEU   A 1 169 ? 7.008  -19.142 -0.449  0.40 21.59 ?  169 LEU   A CA   1 
ATOM   3739 C CA   B LEU   A 1 169 ? 6.881  -19.000 -0.351  0.60 17.65 ?  169 LEU   A CA   1 
ATOM   3740 C C    A LEU   A 1 169 ? 7.910  -19.909 0.517   0.40 22.04 ?  169 LEU   A C    1 
ATOM   3741 C C    B LEU   A 1 169 ? 7.699  -19.758 0.691   0.60 16.92 ?  169 LEU   A C    1 
ATOM   3742 O O    A LEU   A 1 169 ? 7.451  -20.390 1.554   0.40 22.58 ?  169 LEU   A O    1 
ATOM   3743 O O    B LEU   A 1 169 ? 7.121  -20.467 1.523   0.60 17.27 ?  169 LEU   A O    1 
ATOM   3744 C CB   A LEU   A 1 169 ? 7.307  -19.556 -1.892  0.40 22.79 ?  169 LEU   A CB   1 
ATOM   3745 C CB   B LEU   A 1 169 ? 7.187  -19.531 -1.754  0.60 19.99 ?  169 LEU   A CB   1 
ATOM   3746 C CG   A LEU   A 1 169 ? 6.978  -21.008 -2.247  0.40 23.76 ?  169 LEU   A CG   1 
ATOM   3747 C CG   B LEU   A 1 169 ? 6.983  -21.039 -1.939  0.60 21.62 ?  169 LEU   A CG   1 
ATOM   3748 C CD1  A LEU   A 1 169 ? 5.537  -21.335 -1.892  0.40 24.23 ?  169 LEU   A CD1  1 
ATOM   3749 C CD1  B LEU   A 1 169 ? 5.569  -21.450 -1.551  0.60 22.26 ?  169 LEU   A CD1  1 
ATOM   3750 C CD2  A LEU   A 1 169 ? 7.236  -21.268 -3.724  0.40 24.08 ?  169 LEU   A CD2  1 
ATOM   3751 C CD2  B LEU   A 1 169 ? 7.288  -21.462 -3.369  0.60 22.37 ?  169 LEU   A CD2  1 
ATOM   3752 O OXT  A LEU   A 1 169 ? 9.115  -20.061 0.294   0.40 21.97 -1 169 LEU   A OXT  1 
ATOM   3753 O OXT  B LEU   A 1 169 ? 8.935  -19.674 0.722   0.60 16.88 -1 169 LEU   A OXT  1 
ATOM   3754 H H    A LEU   A 1 169 ? 7.905  -17.400 -0.656  0.40 23.75 ?  169 LEU   A H    1 
ATOM   3755 H H    B LEU   A 1 169 ? 7.815  -17.295 -0.727  0.60 19.35 ?  169 LEU   A H    1 
ATOM   3756 H HA   A LEU   A 1 169 ? 6.082  -19.361 -0.253  0.40 25.90 ?  169 LEU   A HA   1 
ATOM   3757 H HA   B LEU   A 1 169 ? 5.939  -19.155 -0.172  0.60 21.17 ?  169 LEU   A HA   1 
ATOM   3758 H HB2  A LEU   A 1 169 ? 6.793  -18.990 -2.489  0.40 27.34 ?  169 LEU   A HB2  1 
ATOM   3759 H HB2  B LEU   A 1 169 ? 6.608  -19.080 -2.390  0.60 23.98 ?  169 LEU   A HB2  1 
ATOM   3760 H HB3  A LEU   A 1 169 ? 8.253  -19.426 -2.056  0.40 27.34 ?  169 LEU   A HB3  1 
ATOM   3761 H HB3  B LEU   A 1 169 ? 8.112  -19.336 -1.962  0.60 23.98 ?  169 LEU   A HB3  1 
ATOM   3762 H HG   A LEU   A 1 169 ? 7.554  -21.598 -1.736  0.40 28.50 ?  169 LEU   A HG   1 
ATOM   3763 H HG   B LEU   A 1 169 ? 7.596  -21.513 -1.357  0.60 25.94 ?  169 LEU   A HG   1 
ATOM   3764 H HD11 A LEU   A 1 169 ? 5.287  -22.168 -2.320  0.40 29.06 ?  169 LEU   A HD11 1 
ATOM   3765 H HD11 B LEU   A 1 169 ? 5.426  -22.372 -1.815  0.60 26.71 ?  169 LEU   A HD11 1 
ATOM   3766 H HD12 A LEU   A 1 169 ? 5.460  -21.423 -0.928  0.40 29.06 ?  169 LEU   A HD12 1 
ATOM   3767 H HD12 B LEU   A 1 169 ? 5.465  -21.362 -0.591  0.60 26.71 ?  169 LEU   A HD12 1 
ATOM   3768 H HD13 A LEU   A 1 169 ? 4.964  -20.617 -2.206  0.40 29.06 ?  169 LEU   A HD13 1 
ATOM   3769 H HD13 B LEU   A 1 169 ? 4.936  -20.874 -2.008  0.60 26.71 ?  169 LEU   A HD13 1 
ATOM   3770 H HD21 A LEU   A 1 169 ? 7.027  -22.194 -3.923  0.40 28.89 ?  169 LEU   A HD21 1 
ATOM   3771 H HD21 B LEU   A 1 169 ? 7.152  -22.419 -3.451  0.60 26.83 ?  169 LEU   A HD21 1 
ATOM   3772 H HD22 A LEU   A 1 169 ? 6.670  -20.681 -4.250  0.40 28.89 ?  169 LEU   A HD22 1 
ATOM   3773 H HD22 B LEU   A 1 169 ? 6.690  -20.991 -3.971  0.60 26.83 ?  169 LEU   A HD22 1 
ATOM   3774 H HD23 A LEU   A 1 169 ? 8.169  -21.090 -3.918  0.40 28.89 ?  169 LEU   A HD23 1 
ATOM   3775 H HD23 B LEU   A 1 169 ? 8.209  -21.238 -3.573  0.60 26.83 ?  169 LEU   A HD23 1 
ATOM   3776 N N    A SER   B 1 1   ? 50.709 -9.146  -23.659 0.40 27.95 ?  1   SER   B N    1 
ATOM   3777 N N    B SER   B 1 1   ? 50.615 -9.197  -23.762 0.60 26.41 ?  1   SER   B N    1 
ATOM   3778 C CA   A SER   B 1 1   ? 51.248 -10.245 -22.831 0.40 27.49 ?  1   SER   B CA   1 
ATOM   3779 C CA   B SER   B 1 1   ? 51.083 -10.235 -22.822 0.60 25.75 ?  1   SER   B CA   1 
ATOM   3780 C C    A SER   B 1 1   ? 50.190 -11.312 -22.602 0.40 26.52 ?  1   SER   B C    1 
ATOM   3781 C C    B SER   B 1 1   ? 49.989 -11.258 -22.550 0.60 24.13 ?  1   SER   B C    1 
ATOM   3782 O O    A SER   B 1 1   ? 49.005 -11.112 -22.882 0.40 26.68 ?  1   SER   B O    1 
ATOM   3783 O O    B SER   B 1 1   ? 48.829 -11.097 -22.954 0.60 23.45 ?  1   SER   B O    1 
ATOM   3784 C CB   A SER   B 1 1   ? 51.744 -9.712  -21.491 0.40 28.18 ?  1   SER   B CB   1 
ATOM   3785 C CB   B SER   B 1 1   ? 51.541 -9.609  -21.508 0.60 26.98 ?  1   SER   B CB   1 
ATOM   3786 O OG   A SER   B 1 1   ? 50.660 -9.376  -20.646 0.40 28.92 ?  1   SER   B OG   1 
ATOM   3787 O OG   B SER   B 1 1   ? 50.430 -9.340  -20.673 0.60 28.27 ?  1   SER   B OG   1 
ATOM   3788 H H1   A SER   B 1 1   ? 50.332 -9.489  -24.385 0.40 33.53 ?  1   SER   B H1   1 
ATOM   3789 H H1   B SER   B 1 1   ? 50.404 -9.581  -24.534 0.60 31.69 ?  1   SER   B H1   1 
ATOM   3790 H H2   A SER   B 1 1   ? 50.108 -8.696  -23.188 0.40 33.53 ?  1   SER   B H2   1 
ATOM   3791 H H2   B SER   B 1 1   ? 49.906 -8.794  -23.417 0.60 31.69 ?  1   SER   B H2   1 
ATOM   3792 H H3   A SER   B 1 1   ? 51.377 -8.608  -23.891 0.40 33.53 ?  1   SER   B H3   1 
ATOM   3793 H H3   B SER   B 1 1   ? 51.269 -8.608  -23.886 0.60 31.69 ?  1   SER   B H3   1 
ATOM   3794 H HA   A SER   B 1 1   ? 51.991 -10.645 -23.299 0.40 32.98 ?  1   SER   B HA   1 
ATOM   3795 H HA   B SER   B 1 1   ? 51.837 -10.691 -23.222 0.60 30.89 ?  1   SER   B HA   1 
ATOM   3796 H HB2  A SER   B 1 1   ? 52.280 -10.398 -21.066 0.40 33.80 ?  1   SER   B HB2  1 
ATOM   3797 H HB2  B SER   B 1 1   ? 52.142 -10.228 -21.063 0.60 32.37 ?  1   SER   B HB2  1 
ATOM   3798 H HB3  A SER   B 1 1   ? 52.279 -8.918  -21.646 0.40 33.80 ?  1   SER   B HB3  1 
ATOM   3799 H HB3  B SER   B 1 1   ? 52.002 -8.776  -21.695 0.60 32.37 ?  1   SER   B HB3  1 
ATOM   3800 H HG   A SER   B 1 1   ? 50.901 -8.788  -20.097 0.40 34.70 ?  1   SER   B HG   1 
ATOM   3801 H HG   B SER   B 1 1   ? 50.637 -8.752  -20.110 0.60 33.91 ?  1   SER   B HG   1 
ATOM   3802 N N    A MET   B 1 2   ? 50.636 -12.444 -22.072 0.40 25.40 ?  2   MET   B N    1 
ATOM   3803 N N    B MET   B 1 2   ? 50.375 -12.306 -21.835 0.60 23.79 ?  2   MET   B N    1 
ATOM   3804 C CA   A MET   B 1 2   ? 49.803 -13.622 -21.885 0.40 24.39 ?  2   MET   B CA   1 
ATOM   3805 C CA   B MET   B 1 2   ? 49.576 -13.517 -21.688 0.60 23.88 ?  2   MET   B CA   1 
ATOM   3806 C C    A MET   B 1 2   ? 49.562 -13.804 -20.395 0.40 21.24 ?  2   MET   B C    1 
ATOM   3807 C C    B MET   B 1 2   ? 49.332 -13.739 -20.201 0.60 21.79 ?  2   MET   B C    1 
ATOM   3808 O O    A MET   B 1 2   ? 50.514 -13.966 -19.624 0.40 20.47 ?  2   MET   B O    1 
ATOM   3809 O O    B MET   B 1 2   ? 50.225 -14.202 -19.483 0.60 22.30 ?  2   MET   B O    1 
ATOM   3810 C CB   A MET   B 1 2   ? 50.500 -14.845 -22.474 0.40 27.11 ?  2   MET   B CB   1 
ATOM   3811 C CB   B MET   B 1 2   ? 50.343 -14.677 -22.299 0.60 27.04 ?  2   MET   B CB   1 
ATOM   3812 C CG   A MET   B 1 2   ? 49.611 -16.067 -22.604 0.40 29.65 ?  2   MET   B CG   1 
ATOM   3813 C CG   B MET   B 1 2   ? 49.504 -15.853 -22.770 0.60 29.77 ?  2   MET   B CG   1 
ATOM   3814 S SD   A MET   B 1 2   ? 50.406 -17.381 -23.547 0.40 31.73 ?  2   MET   B SD   1 
ATOM   3815 S SD   B MET   B 1 2   ? 50.457 -16.946 -23.839 0.60 32.02 ?  2   MET   B SD   1 
ATOM   3816 C CE   A MET   B 1 2   ? 50.963 -16.428 -24.960 0.40 31.89 ?  2   MET   B CE   1 
ATOM   3817 C CE   B MET   B 1 2   ? 51.397 -15.749 -24.770 0.60 32.31 ?  2   MET   B CE   1 
ATOM   3818 H H    A MET   B 1 2   ? 51.443 -12.556 -21.796 0.40 30.47 ?  2   MET   B H    1 
ATOM   3819 H H    B MET   B 1 2   ? 51.126 -12.348 -21.415 0.60 28.54 ?  2   MET   B H    1 
ATOM   3820 H HA   A MET   B 1 2   ? 48.959 -13.509 -22.342 0.40 29.26 ?  2   MET   B HA   1 
ATOM   3821 H HA   B MET   B 1 2   ? 48.737 -13.425 -22.164 0.60 28.65 ?  2   MET   B HA   1 
ATOM   3822 H HB2  A MET   B 1 2   ? 50.821 -14.593 -23.353 0.40 32.53 ?  2   MET   B HB2  1 
ATOM   3823 H HB2  B MET   B 1 2   ? 50.816 -14.294 -23.046 0.60 32.44 ?  2   MET   B HB2  1 
ATOM   3824 H HB3  A MET   B 1 2   ? 51.251 -15.092 -21.913 0.40 32.53 ?  2   MET   B HB3  1 
ATOM   3825 H HB3  B MET   B 1 2   ? 50.981 -15.030 -21.662 0.60 32.44 ?  2   MET   B HB3  1 
ATOM   3826 H HG2  A MET   B 1 2   ? 49.411 -16.402 -21.715 0.40 35.57 ?  2   MET   B HG2  1 
ATOM   3827 H HG2  B MET   B 1 2   ? 49.203 -16.364 -21.999 0.60 35.72 ?  2   MET   B HG2  1 
ATOM   3828 H HG3  A MET   B 1 2   ? 48.794 -15.823 -23.066 0.40 35.57 ?  2   MET   B HG3  1 
ATOM   3829 H HG3  B MET   B 1 2   ? 48.745 -15.541 -23.277 0.60 35.72 ?  2   MET   B HG3  1 
ATOM   3830 H HE1  A MET   B 1 2   ? 51.101 -17.029 -25.698 0.40 38.26 ?  2   MET   B HE1  1 
ATOM   3831 H HE1  B MET   B 1 2   ? 51.734 -16.182 -25.548 0.60 38.76 ?  2   MET   B HE1  1 
ATOM   3832 H HE2  A MET   B 1 2   ? 50.276 -15.775 -25.181 0.40 38.26 ?  2   MET   B HE2  1 
ATOM   3833 H HE2  B MET   B 1 2   ? 50.811 -15.014 -25.020 0.60 38.76 ?  2   MET   B HE2  1 
ATOM   3834 H HE3  A MET   B 1 2   ? 51.794 -15.964 -24.746 0.40 38.26 ?  2   MET   B HE3  1 
ATOM   3835 H HE3  B MET   B 1 2   ? 52.136 -15.418 -24.225 0.60 38.76 ?  2   MET   B HE3  1 
ATOM   3836 N N    A VAL   B 1 3   ? 48.294 -13.739 -19.990 0.40 19.20 ?  3   VAL   B N    1 
ATOM   3837 N N    B VAL   B 1 3   ? 48.133 -13.396 -19.738 0.60 19.53 ?  3   VAL   B N    1 
ATOM   3838 C CA   A VAL   B 1 3   ? 47.891 -13.991 -18.613 0.40 17.75 ?  3   VAL   B CA   1 
ATOM   3839 C CA   B VAL   B 1 3   ? 47.707 -13.685 -18.375 0.60 18.50 ?  3   VAL   B CA   1 
ATOM   3840 C C    A VAL   B 1 3   ? 46.650 -14.874 -18.626 0.40 16.16 ?  3   VAL   B C    1 
ATOM   3841 C C    B VAL   B 1 3   ? 46.464 -14.560 -18.430 0.60 17.04 ?  3   VAL   B C    1 
ATOM   3842 O O    A VAL   B 1 3   ? 45.962 -15.005 -19.642 0.40 15.54 ?  3   VAL   B O    1 
ATOM   3843 O O    B VAL   B 1 3   ? 45.646 -14.447 -19.348 0.60 17.31 ?  3   VAL   B O    1 
ATOM   3844 C CB   A VAL   B 1 3   ? 47.599 -12.684 -17.843 0.40 18.58 ?  3   VAL   B CB   1 
ATOM   3845 C CB   B VAL   B 1 3   ? 47.479 -12.412 -17.525 0.60 19.07 ?  3   VAL   B CB   1 
ATOM   3846 C CG1  A VAL   B 1 3   ? 48.855 -11.832 -17.734 0.40 18.91 ?  3   VAL   B CG1  1 
ATOM   3847 C CG1  B VAL   B 1 3   ? 48.773 -11.608 -17.414 0.60 19.50 ?  3   VAL   B CG1  1 
ATOM   3848 C CG2  A VAL   B 1 3   ? 46.478 -11.914 -18.523 0.40 18.91 ?  3   VAL   B CG2  1 
ATOM   3849 C CG2  B VAL   B 1 3   ? 46.358 -11.556 -18.096 0.60 19.23 ?  3   VAL   B CG2  1 
ATOM   3850 H H    A VAL   B 1 3   ? 47.641 -13.526 -20.506 0.40 23.04 ?  3   VAL   B H    1 
ATOM   3851 H H    B VAL   B 1 3   ? 47.536 -12.990 -20.211 0.60 23.43 ?  3   VAL   B H    1 
ATOM   3852 H HA   A VAL   B 1 3   ? 48.610 -14.461 -18.154 0.40 21.29 ?  3   VAL   B HA   1 
ATOM   3853 H HA   B VAL   B 1 3   ? 48.391 -14.200 -17.938 0.60 22.19 ?  3   VAL   B HA   1 
ATOM   3854 H HB   A VAL   B 1 3   ? 47.311 -12.912 -16.945 0.40 22.28 ?  3   VAL   B HB   1 
ATOM   3855 H HB   B VAL   B 1 3   ? 47.220 -12.674 -16.627 0.60 22.88 ?  3   VAL   B HB   1 
ATOM   3856 H HG11 A VAL   B 1 3   ? 48.643 -11.029 -17.234 0.40 22.68 ?  3   VAL   B HG11 1 
ATOM   3857 H HG11 B VAL   B 1 3   ? 48.615 -10.825 -16.864 0.60 23.40 ?  3   VAL   B HG11 1 
ATOM   3858 H HG12 A VAL   B 1 3   ? 49.541 -12.339 -17.272 0.40 22.68 ?  3   VAL   B HG12 1 
ATOM   3859 H HG12 B VAL   B 1 3   ? 49.455 -12.166 -17.008 0.60 23.40 ?  3   VAL   B HG12 1 
ATOM   3860 H HG13 A VAL   B 1 3   ? 49.155 -11.600 -18.625 0.40 22.68 ?  3   VAL   B HG13 1 
ATOM   3861 H HG13 B VAL   B 1 3   ? 49.052 -11.337 -18.303 0.60 23.40 ?  3   VAL   B HG13 1 
ATOM   3862 H HG21 A VAL   B 1 3   ? 46.396 -11.046 -18.101 0.40 22.68 ?  3   VAL   B HG21 1 
ATOM   3863 H HG21 B VAL   B 1 3   ? 46.333 -10.709 -17.619 0.60 23.07 ?  3   VAL   B HG21 1 
ATOM   3864 H HG22 A VAL   B 1 3   ? 46.691 -11.807 -19.463 0.40 22.68 ?  3   VAL   B HG22 1 
ATOM   3865 H HG22 B VAL   B 1 3   ? 46.528 -11.399 -19.036 0.60 23.07 ?  3   VAL   B HG22 1 
ATOM   3866 H HG23 A VAL   B 1 3   ? 45.648 -12.409 -18.426 0.40 22.68 ?  3   VAL   B HG23 1 
ATOM   3867 H HG23 B VAL   B 1 3   ? 45.515 -12.021 -17.983 0.60 23.07 ?  3   VAL   B HG23 1 
ATOM   3868 N N    . ASN   B 1 4   ? 46.358 -15.468 -17.468 1.00 15.54 ?  4   ASN   B N    1 
ATOM   3869 C CA   . ASN   B 1 4   ? 45.224 -16.389 -17.353 1.00 14.71 ?  4   ASN   B CA   1 
ATOM   3870 C C    . ASN   B 1 4   ? 45.177 -17.351 -18.539 1.00 15.63 ?  4   ASN   B C    1 
ATOM   3871 O O    . ASN   B 1 4   ? 44.112 -17.614 -19.098 1.00 16.49 ?  4   ASN   B O    1 
ATOM   3872 C CB   . ASN   B 1 4   ? 43.895 -15.642 -17.179 1.00 14.17 ?  4   ASN   B CB   1 
ATOM   3873 C CG   . ASN   B 1 4   ? 43.863 -14.815 -15.914 1.00 13.69 ?  4   ASN   B CG   1 
ATOM   3874 O OD1  . ASN   B 1 4   ? 44.145 -15.318 -14.831 1.00 13.62 ?  4   ASN   B OD1  1 
ATOM   3875 N ND2  . ASN   B 1 4   ? 43.533 -13.536 -16.047 1.00 14.61 ?  4   ASN   B ND2  1 
ATOM   3876 H H    A ASN   B 1 4   ? 46.793 -15.347 -16.741 0.40 18.64 ?  4   ASN   B H    1 
ATOM   3877 H H    B ASN   B 1 4   ? 46.962 -15.591 -16.874 0.60 18.64 ?  4   ASN   B H    1 
ATOM   3878 H HA   . ASN   B 1 4   ? 45.358 -16.918 -16.554 1.00 17.64 ?  4   ASN   B HA   1 
ATOM   3879 H HB2  . ASN   B 1 4   ? 43.750 -15.051 -17.929 1.00 17.00 ?  4   ASN   B HB2  1 
ATOM   3880 H HB3  . ASN   B 1 4   ? 43.173 -16.295 -17.128 1.00 17.00 ?  4   ASN   B HB3  1 
ATOM   3881 H HD21 . ASN   B 1 4   ? 43.508 -13.025 -15.354 1.00 17.52 ?  4   ASN   B HD21 1 
ATOM   3882 H HD22 . ASN   B 1 4   ? 43.347 -13.218 -16.822 1.00 17.52 ?  4   ASN   B HD22 1 
ATOM   3883 N N    . SER   B 1 5   ? 46.338 -17.873 -18.927 1.00 16.77 ?  5   SER   B N    1 
ATOM   3884 C CA   . SER   B 1 5   ? 46.439 -18.791 -20.059 1.00 19.24 ?  5   SER   B CA   1 
ATOM   3885 C C    . SER   B 1 5   ? 46.448 -20.221 -19.531 1.00 20.23 ?  5   SER   B C    1 
ATOM   3886 O O    . SER   B 1 5   ? 47.476 -20.892 -19.470 1.00 22.13 ?  5   SER   B O    1 
ATOM   3887 C CB   . SER   B 1 5   ? 47.688 -18.485 -20.881 1.00 20.96 ?  5   SER   B CB   1 
ATOM   3888 O OG   . SER   B 1 5   ? 48.864 -18.673 -20.111 1.00 23.75 ?  5   SER   B OG   1 
ATOM   3889 H H    . SER   B 1 5   ? 47.083 -17.722 -18.530 1.00 20.11 ?  5   SER   B H    1 
ATOM   3890 H HA   . SER   B 1 5   ? 45.665 -18.683 -20.631 1.00 23.08 ?  5   SER   B HA   1 
ATOM   3891 H HB2  . SER   B 1 5   ? 47.709 -19.072 -21.655 1.00 25.15 ?  5   SER   B HB2  1 
ATOM   3892 H HB3  . SER   B 1 5   ? 47.641 -17.561 -21.171 1.00 25.15 ?  5   SER   B HB3  1 
ATOM   3893 H HG   . SER   B 1 5   ? 48.933 -19.481 -19.886 1.00 28.49 ?  5   SER   B HG   1 
ATOM   3894 N N    . PHE   B 1 6   ? 45.265 -20.665 -19.117 1.00 19.98 ?  6   PHE   B N    1 
ATOM   3895 C CA   . PHE   B 1 6   ? 45.098 -22.009 -18.588 1.00 19.30 ?  6   PHE   B CA   1 
ATOM   3896 C C    . PHE   B 1 6   ? 45.029 -23.001 -19.740 1.00 22.13 ?  6   PHE   B C    1 
ATOM   3897 O O    . PHE   B 1 6   ? 44.345 -22.761 -20.738 1.00 23.86 ?  6   PHE   B O    1 
ATOM   3898 C CB   . PHE   B 1 6   ? 43.811 -22.083 -17.765 1.00 17.61 ?  6   PHE   B CB   1 
ATOM   3899 C CG   . PHE   B 1 6   ? 43.818 -21.208 -16.540 1.00 15.88 ?  6   PHE   B CG   1 
ATOM   3900 C CD1  . PHE   B 1 6   ? 44.318 -21.685 -15.341 1.00 15.04 ?  6   PHE   B CD1  1 
ATOM   3901 C CD2  . PHE   B 1 6   ? 43.322 -19.909 -16.586 1.00 15.47 ?  6   PHE   B CD2  1 
ATOM   3902 C CE1  . PHE   B 1 6   ? 44.320 -20.887 -14.206 1.00 14.51 ?  6   PHE   B CE1  1 
ATOM   3903 C CE2  . PHE   B 1 6   ? 43.331 -19.102 -15.460 1.00 15.94 ?  6   PHE   B CE2  1 
ATOM   3904 C CZ   . PHE   B 1 6   ? 43.829 -19.590 -14.268 1.00 14.85 ?  6   PHE   B CZ   1 
ATOM   3905 H H    . PHE   B 1 6   ? 44.533 -20.208 -19.139 1.00 23.97 ?  6   PHE   B H    1 
ATOM   3906 H HA   . PHE   B 1 6   ? 45.846 -22.240 -18.019 1.00 23.16 ?  6   PHE   B HA   1 
ATOM   3907 H HB2  . PHE   B 1 6   ? 43.066 -21.806 -18.319 1.00 21.12 ?  6   PHE   B HB2  1 
ATOM   3908 H HB3  . PHE   B 1 6   ? 43.678 -22.998 -17.470 1.00 21.12 ?  6   PHE   B HB3  1 
ATOM   3909 H HD1  . PHE   B 1 6   ? 44.655 -22.549 -15.292 1.00 18.04 ?  6   PHE   B HD1  1 
ATOM   3910 H HD2  . PHE   B 1 6   ? 42.983 -19.580 -17.385 1.00 18.56 ?  6   PHE   B HD2  1 
ATOM   3911 H HE1  . PHE   B 1 6   ? 44.668 -21.211 -13.404 1.00 17.40 ?  6   PHE   B HE1  1 
ATOM   3912 H HE2  . PHE   B 1 6   ? 42.993 -18.236 -15.502 1.00 19.12 ?  6   PHE   B HE2  1 
ATOM   3913 H HZ   . PHE   B 1 6   ? 43.835 -19.052 -13.509 1.00 17.82 ?  6   PHE   B HZ   1 
ATOM   3914 N N    A SER   B 1 7   ? 45.740 -24.120 -19.600 0.40 22.58 ?  7   SER   B N    1 
ATOM   3915 N N    B SER   B 1 7   ? 45.750 -24.114 -19.601 0.60 22.26 ?  7   SER   B N    1 
ATOM   3916 C CA   A SER   B 1 7   ? 45.800 -25.126 -20.651 0.40 23.68 ?  7   SER   B CA   1 
ATOM   3917 C CA   B SER   B 1 7   ? 45.840 -25.122 -20.647 0.60 23.59 ?  7   SER   B CA   1 
ATOM   3918 C C    A SER   B 1 7   ? 45.787 -26.521 -20.042 0.40 23.28 ?  7   SER   B C    1 
ATOM   3919 C C    B SER   B 1 7   ? 45.817 -26.511 -20.026 0.60 23.16 ?  7   SER   B C    1 
ATOM   3920 O O    A SER   B 1 7   ? 46.373 -26.752 -18.981 0.40 23.86 ?  7   SER   B O    1 
ATOM   3921 O O    B SER   B 1 7   ? 46.405 -26.737 -18.964 0.60 24.04 ?  7   SER   B O    1 
ATOM   3922 C CB   A SER   B 1 7   ? 47.057 -24.948 -21.515 0.40 25.21 ?  7   SER   B CB   1 
ATOM   3923 C CB   B SER   B 1 7   ? 47.127 -24.949 -21.465 0.60 25.46 ?  7   SER   B CB   1 
ATOM   3924 O OG   A SER   B 1 7   ? 47.022 -25.799 -22.646 0.40 26.32 ?  7   SER   B OG   1 
ATOM   3925 O OG   B SER   B 1 7   ? 47.194 -25.887 -22.524 0.60 26.93 ?  7   SER   B OG   1 
ATOM   3926 H H    A SER   B 1 7   ? 46.200 -24.318 -18.899 0.40 27.08 ?  7   SER   B H    1 
ATOM   3927 H H    B SER   B 1 7   ? 46.203 -24.308 -18.896 0.60 26.71 ?  7   SER   B H    1 
ATOM   3928 H HA   A SER   B 1 7   ? 45.024 -25.041 -21.223 0.40 28.41 ?  7   SER   B HA   1 
ATOM   3929 H HA   B SER   B 1 7   ? 45.082 -25.043 -21.245 0.60 28.30 ?  7   SER   B HA   1 
ATOM   3930 H HB2  A SER   B 1 7   ? 47.102 -24.028 -21.820 0.40 30.24 ?  7   SER   B HB2  1 
ATOM   3931 H HB2  B SER   B 1 7   ? 47.143 -24.054 -21.838 0.60 30.55 ?  7   SER   B HB2  1 
ATOM   3932 H HB3  A SER   B 1 7   ? 47.841 -25.158 -20.982 0.40 30.24 ?  7   SER   B HB3  1 
ATOM   3933 H HB3  B SER   B 1 7   ? 47.891 -25.078 -20.881 0.60 30.55 ?  7   SER   B HB3  1 
ATOM   3934 H HG   A SER   B 1 7   ? 47.718 -25.698 -23.105 0.40 31.57 ?  7   SER   B HG   1 
ATOM   3935 H HG   B SER   B 1 7   ? 47.903 -25.779 -22.961 0.60 32.31 ?  7   SER   B HG   1 
ATOM   3936 N N    A GLY   B 1 8   ? 45.114 -27.446 -20.725 0.40 22.71 ?  8   GLY   B N    1 
ATOM   3937 N N    B GLY   B 1 8   ? 45.136 -27.439 -20.695 0.60 22.72 ?  8   GLY   B N    1 
ATOM   3938 C CA   A GLY   B 1 8   ? 45.085 -28.835 -20.318 0.40 22.08 ?  8   GLY   B CA   1 
ATOM   3939 C CA   B GLY   B 1 8   ? 45.124 -28.820 -20.262 0.60 22.22 ?  8   GLY   B CA   1 
ATOM   3940 C C    A GLY   B 1 8   ? 44.099 -29.174 -19.224 0.40 21.16 ?  8   GLY   B C    1 
ATOM   3941 C C    B GLY   B 1 8   ? 44.156 -29.134 -19.148 0.60 21.24 ?  8   GLY   B C    1 
ATOM   3942 O O    A GLY   B 1 8   ? 44.189 -30.268 -18.653 0.40 21.72 ?  8   GLY   B O    1 
ATOM   3943 O O    B GLY   B 1 8   ? 44.313 -30.165 -18.483 0.60 22.23 ?  8   GLY   B O    1 
ATOM   3944 H H    A GLY   B 1 8   ? 44.665 -27.284 -21.440 0.40 27.24 ?  8   GLY   B H    1 
ATOM   3945 H H    B GLY   B 1 8   ? 44.672 -27.287 -21.402 0.60 27.25 ?  8   GLY   B H    1 
ATOM   3946 H HA2  A GLY   B 1 8   ? 44.867 -29.382 -21.090 0.40 26.49 ?  8   GLY   B HA2  1 
ATOM   3947 H HA2  B GLY   B 1 8   ? 44.900 -29.384 -21.019 0.60 26.65 ?  8   GLY   B HA2  1 
ATOM   3948 H HA3  A GLY   B 1 8   ? 45.967 -29.092 -20.010 0.40 26.49 ?  8   GLY   B HA3  1 
ATOM   3949 H HA3  B GLY   B 1 8   ? 46.010 -29.064 -19.957 0.60 26.65 ?  8   GLY   B HA3  1 
ATOM   3950 N N    . TYR   B 1 9   ? 43.153 -28.289 -18.922 1.00 20.22 ?  9   TYR   B N    1 
ATOM   3951 C CA   . TYR   B 1 9   ? 42.170 -28.547 -17.882 1.00 18.30 ?  9   TYR   B CA   1 
ATOM   3952 C C    . TYR   B 1 9   ? 40.988 -29.331 -18.427 1.00 17.85 ?  9   TYR   B C    1 
ATOM   3953 O O    . TYR   B 1 9   ? 40.601 -29.197 -19.591 1.00 19.59 ?  9   TYR   B O    1 
ATOM   3954 C CB   . TYR   B 1 9   ? 41.665 -27.250 -17.255 1.00 17.99 ?  9   TYR   B CB   1 
ATOM   3955 C CG   . TYR   B 1 9   ? 42.675 -26.625 -16.330 1.00 17.59 ?  9   TYR   B CG   1 
ATOM   3956 C CD1  . TYR   B 1 9   ? 43.783 -25.960 -16.836 1.00 18.36 ?  9   TYR   B CD1  1 
ATOM   3957 C CD2  . TYR   B 1 9   ? 42.538 -26.713 -14.954 1.00 16.77 ?  9   TYR   B CD2  1 
ATOM   3958 C CE1  . TYR   B 1 9   ? 44.728 -25.403 -16.000 1.00 18.58 ?  9   TYR   B CE1  1 
ATOM   3959 C CE2  . TYR   B 1 9   ? 43.477 -26.151 -14.107 1.00 17.11 ?  9   TYR   B CE2  1 
ATOM   3960 C CZ   . TYR   B 1 9   ? 44.569 -25.495 -14.640 1.00 18.26 ?  9   TYR   B CZ   1 
ATOM   3961 O OH   . TYR   B 1 9   ? 45.509 -24.945 -13.808 1.00 18.81 ?  9   TYR   B OH   1 
ATOM   3962 H H    A TYR   B 1 9   ? 43.049 -27.535 -19.320 0.40 24.25 ?  9   TYR   B H    1 
ATOM   3963 H H    B TYR   B 1 9   ? 43.013 -27.566 -19.366 0.60 24.25 ?  9   TYR   B H    1 
ATOM   3964 H HA   . TYR   B 1 9   ? 42.577 -29.075 -17.181 1.00 21.95 ?  9   TYR   B HA   1 
ATOM   3965 H HB2  . TYR   B 1 9   ? 41.462 -26.609 -17.955 1.00 21.58 ?  9   TYR   B HB2  1 
ATOM   3966 H HB3  . TYR   B 1 9   ? 40.874 -27.446 -16.739 1.00 21.58 ?  9   TYR   B HB3  1 
ATOM   3967 H HD1  . TYR   B 1 9   ? 43.895 -25.899 -17.756 1.00 22.02 ?  9   TYR   B HD1  1 
ATOM   3968 H HD2  . TYR   B 1 9   ? 41.801 -27.158 -14.593 1.00 20.12 ?  9   TYR   B HD2  1 
ATOM   3969 H HE1  . TYR   B 1 9   ? 45.461 -24.960 -16.354 1.00 22.28 ?  9   TYR   B HE1  1 
ATOM   3970 H HE2  . TYR   B 1 9   ? 43.366 -26.220 -13.182 1.00 20.52 ?  9   TYR   B HE2  1 
ATOM   3971 H HH   . TYR   B 1 9   ? 46.109 -24.577 -14.261 1.00 22.56 ?  9   TYR   B HH   1 
ATOM   3972 N N    . LEU   B 1 10  ? 40.423 -30.160 -17.561 1.00 16.20 ?  10  LEU   B N    1 
ATOM   3973 C CA   . LEU   B 1 10  ? 39.219 -30.918 -17.850 1.00 16.06 ?  10  LEU   B CA   1 
ATOM   3974 C C    . LEU   B 1 10  ? 38.024 -30.154 -17.293 1.00 15.40 ?  10  LEU   B C    1 
ATOM   3975 O O    . LEU   B 1 10  ? 38.028 -29.743 -16.129 1.00 15.06 ?  10  LEU   B O    1 
ATOM   3976 C CB   . LEU   B 1 10  ? 39.324 -32.295 -17.196 1.00 16.99 ?  10  LEU   B CB   1 
ATOM   3977 C CG   . LEU   B 1 10  ? 38.184 -33.248 -17.521 1.00 18.63 ?  10  LEU   B CG   1 
ATOM   3978 C CD1  . LEU   B 1 10  ? 38.290 -33.756 -18.954 1.00 20.10 ?  10  LEU   B CD1  1 
ATOM   3979 C CD2  . LEU   B 1 10  ? 38.160 -34.401 -16.539 1.00 19.69 ?  10  LEU   B CD2  1 
ATOM   3980 H H    . LEU   B 1 10  ? 40.731 -30.305 -16.768 1.00 19.43 ?  10  LEU   B H    1 
ATOM   3981 H HA   . LEU   B 1 10  ? 39.114 -31.027 -18.806 1.00 19.27 ?  10  LEU   B HA   1 
ATOM   3982 H HB2  . LEU   B 1 10  ? 40.149 -32.717 -17.489 1.00 20.38 ?  10  LEU   B HB2  1 
ATOM   3983 H HB3  . LEU   B 1 10  ? 39.344 -32.183 -16.232 1.00 20.38 ?  10  LEU   B HB3  1 
ATOM   3984 H HG   . LEU   B 1 10  ? 37.344 -32.773 -17.437 1.00 22.35 ?  10  LEU   B HG   1 
ATOM   3985 H HD11 . LEU   B 1 10  ? 37.574 -34.389 -19.117 1.00 24.11 ?  10  LEU   B HD11 1 
ATOM   3986 H HD12 . LEU   B 1 10  ? 38.208 -33.002 -19.561 1.00 24.11 ?  10  LEU   B HD12 1 
ATOM   3987 H HD13 . LEU   B 1 10  ? 39.149 -34.187 -19.074 1.00 24.11 ?  10  LEU   B HD13 1 
ATOM   3988 H HD21 . LEU   B 1 10  ? 37.432 -34.997 -16.773 1.00 23.61 ?  10  LEU   B HD21 1 
ATOM   3989 H HD22 . LEU   B 1 10  ? 39.005 -34.872 -16.587 1.00 23.61 ?  10  LEU   B HD22 1 
ATOM   3990 H HD23 . LEU   B 1 10  ? 38.026 -34.048 -15.646 1.00 23.61 ?  10  LEU   B HD23 1 
ATOM   3991 N N    . LYS   B 1 11  ? 37.003 -29.974 -18.121 1.00 16.37 ?  11  LYS   B N    1 
ATOM   3992 C CA   . LYS   B 1 11  ? 35.807 -29.254 -17.709 1.00 18.00 ?  11  LYS   B CA   1 
ATOM   3993 C C    . LYS   B 1 11  ? 34.914 -30.176 -16.884 1.00 17.51 ?  11  LYS   B C    1 
ATOM   3994 O O    . LYS   B 1 11  ? 34.525 -31.253 -17.350 1.00 19.42 ?  11  LYS   B O    1 
ATOM   3995 C CB   . LYS   B 1 11  ? 35.070 -28.759 -18.952 1.00 21.80 ?  11  LYS   B CB   1 
ATOM   3996 C CG   . LYS   B 1 11  ? 33.902 -27.829 -18.685 1.00 25.39 ?  11  LYS   B CG   1 
ATOM   3997 C CD   . LYS   B 1 11  ? 33.120 -27.576 -19.968 1.00 28.43 ?  11  LYS   B CD   1 
ATOM   3998 C CE   . LYS   B 1 11  ? 32.126 -26.441 -19.809 1.00 30.68 ?  11  LYS   B CE   1 
ATOM   3999 N NZ   . LYS   B 1 11  ? 32.809 -25.126 -19.683 1.00 32.00 ?  11  LYS   B NZ   1 
ATOM   4000 H H    . LYS   B 1 11  ? 36.973 -30.274 -18.929 1.00 19.63 ?  11  LYS   B H    1 
ATOM   4001 H HA   . LYS   B 1 11  ? 36.056 -28.492 -17.167 1.00 21.60 ?  11  LYS   B HA   1 
ATOM   4002 H HB2  . LYS   B 1 11  ? 35.702 -28.279 -19.512 1.00 26.15 ?  11  LYS   B HB2  1 
ATOM   4003 H HB3  . LYS   B 1 11  ? 34.728 -29.526 -19.436 1.00 26.15 ?  11  LYS   B HB3  1 
ATOM   4004 H HG2  . LYS   B 1 11  ? 33.306 -28.237 -18.039 1.00 30.47 ?  11  LYS   B HG2  1 
ATOM   4005 H HG3  . LYS   B 1 11  ? 34.234 -26.981 -18.355 1.00 30.47 ?  11  LYS   B HG3  1 
ATOM   4006 H HD2  . LYS   B 1 11  ? 33.739 -27.340 -20.678 1.00 34.11 ?  11  LYS   B HD2  1 
ATOM   4007 H HD3  . LYS   B 1 11  ? 32.630 -28.379 -20.207 1.00 34.11 ?  11  LYS   B HD3  1 
ATOM   4008 H HE2  . LYS   B 1 11  ? 31.547 -26.411 -20.588 1.00 36.81 ?  11  LYS   B HE2  1 
ATOM   4009 H HE3  . LYS   B 1 11  ? 31.601 -26.594 -19.008 1.00 36.81 ?  11  LYS   B HE3  1 
ATOM   4010 H HZ1  . LYS   B 1 11  ? 32.207 -24.476 -19.611 1.00 38.39 ?  11  LYS   B HZ1  1 
ATOM   4011 H HZ2  . LYS   B 1 11  ? 33.330 -25.122 -18.962 1.00 38.39 ?  11  LYS   B HZ2  1 
ATOM   4012 H HZ3  . LYS   B 1 11  ? 33.312 -24.976 -20.403 1.00 38.39 ?  11  LYS   B HZ3  1 
ATOM   4013 N N    . LEU   B 1 12  ? 34.591 -29.760 -15.658 1.00 16.23 ?  12  LEU   B N    1 
ATOM   4014 C CA   . LEU   B 1 12  ? 33.633 -30.475 -14.820 1.00 16.19 ?  12  LEU   B CA   1 
ATOM   4015 C C    . LEU   B 1 12  ? 32.242 -29.871 -14.909 1.00 16.16 ?  12  LEU   B C    1 
ATOM   4016 O O    . LEU   B 1 12  ? 31.257 -30.594 -15.082 1.00 16.64 ?  12  LEU   B O    1 
ATOM   4017 C CB   . LEU   B 1 12  ? 34.086 -30.489 -13.355 1.00 15.66 ?  12  LEU   B CB   1 
ATOM   4018 C CG   . LEU   B 1 12  ? 35.422 -31.170 -13.066 1.00 15.80 ?  12  LEU   B CG   1 
ATOM   4019 C CD1  . LEU   B 1 12  ? 35.742 -31.123 -11.586 1.00 16.01 ?  12  LEU   B CD1  1 
ATOM   4020 C CD2  . LEU   B 1 12  ? 35.402 -32.610 -13.561 1.00 16.55 ?  12  LEU   B CD2  1 
ATOM   4021 H H    . LEU   B 1 12  ? 34.917 -29.056 -15.288 1.00 19.47 ?  12  LEU   B H    1 
ATOM   4022 H HA   . LEU   B 1 12  ? 33.566 -31.389 -15.127 1.00 19.42 ?  12  LEU   B HA   1 
ATOM   4023 H HB2  . LEU   B 1 12  ? 34.158 -29.571 -13.053 1.00 18.79 ?  12  LEU   B HB2  1 
ATOM   4024 H HB3  . LEU   B 1 12  ? 33.406 -30.947 -12.835 1.00 18.79 ?  12  LEU   B HB3  1 
ATOM   4025 H HG   . LEU   B 1 12  ? 36.124 -30.705 -13.542 1.00 18.95 ?  12  LEU   B HG   1 
ATOM   4026 H HD11 . LEU   B 1 12  ? 36.594 -31.564 -11.433 1.00 19.21 ?  12  LEU   B HD11 1 
ATOM   4027 H HD12 . LEU   B 1 12  ? 35.791 -30.199 -11.303 1.00 19.21 ?  12  LEU   B HD12 1 
ATOM   4028 H HD13 . LEU   B 1 12  ? 35.042 -31.585 -11.095 1.00 19.21 ?  12  LEU   B HD13 1 
ATOM   4029 H HD21 . LEU   B 1 12  ? 36.191 -33.068 -13.236 1.00 19.85 ?  12  LEU   B HD21 1 
ATOM   4030 H HD22 . LEU   B 1 12  ? 34.603 -33.050 -13.225 1.00 19.85 ?  12  LEU   B HD22 1 
ATOM   4031 H HD23 . LEU   B 1 12  ? 35.393 -32.614 -14.532 1.00 19.85 ?  12  LEU   B HD23 1 
ATOM   4032 N N    . THR   B 1 13  ? 32.146 -28.554 -14.782 1.00 15.67 ?  13  THR   B N    1 
ATOM   4033 C CA   . THR   B 1 13  ? 30.919 -27.807 -14.993 1.00 15.76 ?  13  THR   B CA   1 
ATOM   4034 C C    . THR   B 1 13  ? 31.247 -26.604 -15.869 1.00 17.30 ?  13  THR   B C    1 
ATOM   4035 O O    . THR   B 1 13  ? 32.394 -26.402 -16.287 1.00 18.55 ?  13  THR   B O    1 
ATOM   4036 C CB   . THR   B 1 13  ? 30.312 -27.332 -13.669 1.00 15.47 ?  13  THR   B CB   1 
ATOM   4037 O OG1  . THR   B 1 13  ? 31.152 -26.309 -13.122 1.00 15.25 ?  13  THR   B OG1  1 
ATOM   4038 C CG2  . THR   B 1 13  ? 30.190 -28.485 -12.672 1.00 16.04 ?  13  THR   B CG2  1 
ATOM   4039 H H    . THR   B 1 13  ? 32.809 -28.049 -14.567 1.00 18.80 ?  13  THR   B H    1 
ATOM   4040 H HA   . THR   B 1 13  ? 30.267 -28.359 -15.447 1.00 18.90 ?  13  THR   B HA   1 
ATOM   4041 H HB   . THR   B 1 13  ? 29.423 -26.967 -13.827 1.00 18.56 ?  13  THR   B HB   1 
ATOM   4042 H HG1  . THR   B 1 13  ? 30.826 -25.544 -13.288 1.00 18.29 ?  13  THR   B HG1  1 
ATOM   4043 H HG21 . THR   B 1 13  ? 29.698 -28.196 -11.886 1.00 19.24 ?  13  THR   B HG21 1 
ATOM   4044 H HG22 . THR   B 1 13  ? 29.718 -29.225 -13.083 1.00 19.24 ?  13  THR   B HG22 1 
ATOM   4045 H HG23 . THR   B 1 13  ? 31.071 -28.783 -12.400 1.00 19.24 ?  13  THR   B HG23 1 
ATOM   4046 N N    A ASP   B 1 14  ? 30.228 -25.784 -16.129 0.40 17.89 ?  14  ASP   B N    1 
ATOM   4047 N N    B ASP   B 1 14  ? 30.231 -25.780 -16.133 0.60 17.98 ?  14  ASP   B N    1 
ATOM   4048 C CA   A ASP   B 1 14  ? 30.427 -24.616 -16.977 0.40 18.98 ?  14  ASP   B CA   1 
ATOM   4049 C CA   B ASP   B 1 14  ? 30.430 -24.614 -16.989 0.60 19.48 ?  14  ASP   B CA   1 
ATOM   4050 C C    A ASP   B 1 14  ? 31.534 -23.714 -16.445 0.40 17.53 ?  14  ASP   B C    1 
ATOM   4051 C C    B ASP   B 1 14  ? 31.444 -23.628 -16.426 0.60 17.94 ?  14  ASP   B C    1 
ATOM   4052 O O    A ASP   B 1 14  ? 32.220 -23.052 -17.233 0.40 18.12 ?  14  ASP   B O    1 
ATOM   4053 O O    B ASP   B 1 14  ? 31.938 -22.780 -17.177 0.60 18.88 ?  14  ASP   B O    1 
ATOM   4054 C CB   A ASP   B 1 14  ? 29.114 -23.841 -17.124 0.40 21.63 ?  14  ASP   B CB   1 
ATOM   4055 C CB   B ASP   B 1 14  ? 29.108 -23.888 -17.228 0.60 22.71 ?  14  ASP   B CB   1 
ATOM   4056 C CG   A ASP   B 1 14  ? 28.125 -24.526 -18.047 0.40 24.01 ?  14  ASP   B CG   1 
ATOM   4057 C CG   B ASP   B 1 14  ? 28.245 -24.583 -18.261 0.60 25.74 ?  14  ASP   B CG   1 
ATOM   4058 O OD1  A ASP   B 1 14  ? 28.431 -25.617 -18.579 0.40 24.64 ?  14  ASP   B OD1  1 
ATOM   4059 O OD1  B ASP   B 1 14  ? 28.812 -25.231 -19.167 0.60 26.67 ?  14  ASP   B OD1  1 
ATOM   4060 O OD2  A ASP   B 1 14  ? 27.029 -23.959 -18.235 0.40 25.08 -1 14  ASP   B OD2  1 
ATOM   4061 O OD2  B ASP   B 1 14  ? 27.004 -24.485 -18.170 0.60 27.25 -1 14  ASP   B OD2  1 
ATOM   4062 H H    A ASP   B 1 14  ? 29.430 -25.870 -15.819 0.40 21.46 ?  14  ASP   B H    1 
ATOM   4063 H H    B ASP   B 1 14  ? 29.431 -25.869 -15.830 0.60 21.57 ?  14  ASP   B H    1 
ATOM   4064 H HA   A ASP   B 1 14  ? 30.698 -24.902 -17.856 0.40 22.76 ?  14  ASP   B HA   1 
ATOM   4065 H HA   B ASP   B 1 14  ? 30.759 -24.913 -17.848 0.60 23.37 ?  14  ASP   B HA   1 
ATOM   4066 H HB2  A ASP   B 1 14  ? 28.679 -23.771 -16.263 0.40 25.95 ?  14  ASP   B HB2  1 
ATOM   4067 H HB2  B ASP   B 1 14  ? 28.615 -23.842 -16.392 0.60 27.24 ?  14  ASP   B HB2  1 
ATOM   4068 H HB3  A ASP   B 1 14  ? 29.296 -22.958 -17.481 0.40 25.95 ?  14  ASP   B HB3  1 
ATOM   4069 H HB3  B ASP   B 1 14  ? 29.295 -22.986 -17.546 0.60 27.24 ?  14  ASP   B HB3  1 
ATOM   4070 N N    . ASN   B 1 15  ? 31.749 -23.696 -15.127 1.00 15.65 ?  15  ASN   B N    1 
ATOM   4071 C CA   . ASN   B 1 15  ? 32.705 -22.773 -14.519 1.00 13.63 ?  15  ASN   B CA   1 
ATOM   4072 C C    . ASN   B 1 15  ? 33.798 -23.430 -13.682 1.00 12.73 ?  15  ASN   B C    1 
ATOM   4073 O O    . ASN   B 1 15  ? 34.636 -22.699 -13.136 1.00 13.10 ?  15  ASN   B O    1 
ATOM   4074 C CB   . ASN   B 1 15  ? 31.986 -21.719 -13.658 1.00 13.94 ?  15  ASN   B CB   1 
ATOM   4075 C CG   . ASN   B 1 15  ? 31.356 -22.319 -12.424 1.00 13.84 ?  15  ASN   B CG   1 
ATOM   4076 O OD1  . ASN   B 1 15  ? 30.415 -23.112 -12.524 1.00 15.33 ?  15  ASN   B OD1  1 
ATOM   4077 N ND2  . ASN   B 1 15  ? 31.874 -21.973 -11.257 1.00 12.97 ?  15  ASN   B ND2  1 
ATOM   4078 H H    A ASN   B 1 15  ? 31.363 -24.222 -14.564 0.40 18.77 ?  15  ASN   B H    1 
ATOM   4079 H H    B ASN   B 1 15  ? 31.397 -24.253 -14.572 0.60 18.77 ?  15  ASN   B H    1 
ATOM   4080 H HA   . ASN   B 1 15  ? 33.156 -22.291 -15.222 1.00 16.34 ?  15  ASN   B HA   1 
ATOM   4081 H HB2  . ASN   B 1 15  ? 32.633 -21.048 -13.371 1.00 16.72 ?  15  ASN   B HB2  1 
ATOM   4082 H HB3  . ASN   B 1 15  ? 31.286 -21.299 -14.179 1.00 16.72 ?  15  ASN   B HB3  1 
ATOM   4083 H HD21 . ASN   B 1 15  ? 31.547 -22.291 -10.525 1.00 15.56 ?  15  ASN   B HD21 1 
ATOM   4084 H HD22 . ASN   B 1 15  ? 32.535 -21.419 -11.219 1.00 15.56 ?  15  ASN   B HD22 1 
ATOM   4085 N N    . VAL   B 1 16  ? 33.824 -24.758 -13.557 1.00 12.84 ?  16  VAL   B N    1 
ATOM   4086 C CA   . VAL   B 1 16  ? 34.820 -25.451 -12.745 1.00 12.36 ?  16  VAL   B CA   1 
ATOM   4087 C C    . VAL   B 1 16  ? 35.617 -26.388 -13.634 1.00 12.43 ?  16  VAL   B C    1 
ATOM   4088 O O    . VAL   B 1 16  ? 35.043 -27.262 -14.301 1.00 13.75 ?  16  VAL   B O    1 
ATOM   4089 C CB   . VAL   B 1 16  ? 34.188 -26.214 -11.566 1.00 13.16 ?  16  VAL   B CB   1 
ATOM   4090 C CG1  . VAL   B 1 16  ? 35.273 -26.929 -10.759 1.00 13.11 ?  16  VAL   B CG1  1 
ATOM   4091 C CG2  . VAL   B 1 16  ? 33.386 -25.255 -10.682 1.00 13.66 ?  16  VAL   B CG2  1 
ATOM   4092 H H    . VAL   B 1 16  ? 33.264 -25.290 -13.943 1.00 15.40 ?  16  VAL   B H    1 
ATOM   4093 H HA   . VAL   B 1 16  ? 35.434 -24.795 -12.377 1.00 14.82 ?  16  VAL   B HA   1 
ATOM   4094 H HB   . VAL   B 1 16  ? 33.582 -26.884 -11.915 1.00 15.78 ?  16  VAL   B HB   1 
ATOM   4095 H HG11 . VAL   B 1 16  ? 34.889 -27.233 -9.922  1.00 15.73 ?  16  VAL   B HG11 1 
ATOM   4096 H HG12 . VAL   B 1 16  ? 35.603 -27.685 -11.266 1.00 15.73 ?  16  VAL   B HG12 1 
ATOM   4097 H HG13 . VAL   B 1 16  ? 35.996 -26.305 -10.581 1.00 15.73 ?  16  VAL   B HG13 1 
ATOM   4098 H HG21 . VAL   B 1 16  ? 33.042 -25.747 -9.920  1.00 16.39 ?  16  VAL   B HG21 1 
ATOM   4099 H HG22 . VAL   B 1 16  ? 33.966 -24.540 -10.382 1.00 16.39 ?  16  VAL   B HG22 1 
ATOM   4100 H HG23 . VAL   B 1 16  ? 32.650 -24.891 -11.200 1.00 16.39 ?  16  VAL   B HG23 1 
ATOM   4101 N N    . TYR   B 1 17  ? 36.945 -26.227 -13.593 1.00 12.46 ?  17  TYR   B N    1 
ATOM   4102 C CA   . TYR   B 1 17  ? 37.896 -26.972 -14.403 1.00 12.87 ?  17  TYR   B CA   1 
ATOM   4103 C C    . TYR   B 1 17  ? 38.945 -27.580 -13.483 1.00 12.39 ?  17  TYR   B C    1 
ATOM   4104 O O    . TYR   B 1 17  ? 39.212 -27.052 -12.398 1.00 12.70 ?  17  TYR   B O    1 
ATOM   4105 C CB   . TYR   B 1 17  ? 38.603 -26.031 -15.393 1.00 15.10 ?  17  TYR   B CB   1 
ATOM   4106 C CG   . TYR   B 1 17  ? 37.672 -25.261 -16.298 1.00 18.16 ?  17  TYR   B CG   1 
ATOM   4107 C CD1  . TYR   B 1 17  ? 37.064 -24.084 -15.873 1.00 19.25 ?  17  TYR   B CD1  1 
ATOM   4108 C CD2  . TYR   B 1 17  ? 37.408 -25.708 -17.584 1.00 20.10 ?  17  TYR   B CD2  1 
ATOM   4109 C CE1  . TYR   B 1 17  ? 36.211 -23.379 -16.708 1.00 20.49 ?  17  TYR   B CE1  1 
ATOM   4110 C CE2  . TYR   B 1 17  ? 36.561 -25.012 -18.425 1.00 21.29 ?  17  TYR   B CE2  1 
ATOM   4111 C CZ   . TYR   B 1 17  ? 35.964 -23.852 -17.981 1.00 21.56 ?  17  TYR   B CZ   1 
ATOM   4112 O OH   . TYR   B 1 17  ? 35.123 -23.159 -18.819 1.00 23.07 ?  17  TYR   B OH   1 
ATOM   4113 H H    . TYR   B 1 17  ? 37.339 -25.657 -13.072 1.00 14.95 ?  17  TYR   B H    1 
ATOM   4114 H HA   . TYR   B 1 17  ? 37.445 -27.676 -14.893 1.00 15.43 ?  17  TYR   B HA   1 
ATOM   4115 H HB2  . TYR   B 1 17  ? 39.133 -25.390 -14.895 1.00 18.11 ?  17  TYR   B HB2  1 
ATOM   4116 H HB3  . TYR   B 1 17  ? 39.180 -26.561 -15.961 1.00 18.11 ?  17  TYR   B HB3  1 
ATOM   4117 H HD1  . TYR   B 1 17  ? 37.231 -23.768 -15.016 1.00 23.09 ?  17  TYR   B HD1  1 
ATOM   4118 H HD2  . TYR   B 1 17  ? 37.805 -26.490 -17.889 1.00 24.11 ?  17  TYR   B HD2  1 
ATOM   4119 H HE1  . TYR   B 1 17  ? 35.807 -22.592 -16.412 1.00 24.58 ?  17  TYR   B HE1  1 
ATOM   4120 H HE2  . TYR   B 1 17  ? 36.388 -25.325 -19.285 1.00 25.54 ?  17  TYR   B HE2  1 
ATOM   4121 H HH   . TYR   B 1 17  ? 35.057 -23.550 -19.559 1.00 27.67 ?  17  TYR   B HH   1 
ATOM   4122 N N    . ILE   B 1 18  ? 39.566 -28.678 -13.916 1.00 12.61 ?  18  ILE   B N    1 
ATOM   4123 C CA   . ILE   B 1 18  ? 40.493 -29.398 -13.051 1.00 12.46 ?  18  ILE   B CA   1 
ATOM   4124 C C    . ILE   B 1 18  ? 41.659 -29.946 -13.865 1.00 12.58 ?  18  ILE   B C    1 
ATOM   4125 O O    . ILE   B 1 18  ? 41.499 -30.354 -15.021 1.00 14.14 ?  18  ILE   B O    1 
ATOM   4126 C CB   . ILE   B 1 18  ? 39.737 -30.493 -12.255 1.00 12.92 ?  18  ILE   B CB   1 
ATOM   4127 C CG1  . ILE   B 1 18  ? 40.591 -31.040 -11.108 1.00 13.24 ?  18  ILE   B CG1  1 
ATOM   4128 C CG2  . ILE   B 1 18  ? 39.235 -31.604 -13.189 1.00 13.39 ?  18  ILE   B CG2  1 
ATOM   4129 C CD1  . ILE   B 1 18  ? 39.774 -31.824 -10.081 1.00 14.81 ?  18  ILE   B CD1  1 
ATOM   4130 H H    . ILE   B 1 18  ? 39.472 -29.023 -14.701 1.00 15.12 ?  18  ILE   B H    1 
ATOM   4131 H HA   . ILE   B 1 18  ? 40.855 -28.778 -12.402 1.00 14.95 ?  18  ILE   B HA   1 
ATOM   4132 H HB   . ILE   B 1 18  ? 38.954 -30.081 -11.859 1.00 15.49 ?  18  ILE   B HB   1 
ATOM   4133 H HG12 . ILE   B 1 18  ? 41.265 -31.634 -11.468 1.00 15.88 ?  18  ILE   B HG12 1 
ATOM   4134 H HG13 . ILE   B 1 18  ? 41.011 -30.297 -10.648 1.00 15.88 ?  18  ILE   B HG13 1 
ATOM   4135 H HG21 . ILE   B 1 18  ? 38.649 -32.194 -12.689 1.00 16.07 ?  18  ILE   B HG21 1 
ATOM   4136 H HG22 . ILE   B 1 18  ? 38.747 -31.197 -13.922 1.00 16.07 ?  18  ILE   B HG22 1 
ATOM   4137 H HG23 . ILE   B 1 18  ? 39.994 -32.098 -13.528 1.00 16.07 ?  18  ILE   B HG23 1 
ATOM   4138 H HD11 . ILE   B 1 18  ? 40.362 -32.115 -9.366  1.00 17.77 ?  18  ILE   B HD11 1 
ATOM   4139 H HD12 . ILE   B 1 18  ? 39.079 -31.249 -9.723  1.00 17.77 ?  18  ILE   B HD12 1 
ATOM   4140 H HD13 . ILE   B 1 18  ? 39.375 -32.594 -10.515 1.00 17.77 ?  18  ILE   B HD13 1 
ATOM   4141 N N    . LYS   B 1 19  ? 42.840 -29.975 -13.241 1.00 13.00 ?  19  LYS   B N    1 
ATOM   4142 C CA   . LYS   B 1 19  ? 44.055 -30.454 -13.886 1.00 13.62 ?  19  LYS   B CA   1 
ATOM   4143 C C    . LYS   B 1 19  ? 44.942 -31.137 -12.857 1.00 13.65 ?  19  LYS   B C    1 
ATOM   4144 O O    . LYS   B 1 19  ? 45.016 -30.704 -11.706 1.00 13.32 ?  19  LYS   B O    1 
ATOM   4145 C CB   . LYS   B 1 19  ? 44.833 -29.292 -14.516 1.00 15.17 ?  19  LYS   B CB   1 
ATOM   4146 C CG   . LYS   B 1 19  ? 46.053 -29.708 -15.330 1.00 16.56 ?  19  LYS   B CG   1 
ATOM   4147 C CD   . LYS   B 1 19  ? 46.819 -28.480 -15.807 1.00 18.09 ?  19  LYS   B CD   1 
ATOM   4148 C CE   . LYS   B 1 19  ? 47.941 -28.838 -16.764 1.00 19.98 ?  19  LYS   B CE   1 
ATOM   4149 N NZ   . LYS   B 1 19  ? 48.681 -27.629 -17.220 1.00 21.21 ?  19  LYS   B NZ   1 
ATOM   4150 H H    . LYS   B 1 19  ? 42.957 -29.709 -12.424 1.00 15.59 ?  19  LYS   B H    1 
ATOM   4151 H HA   . LYS   B 1 19  ? 43.824 -31.095 -14.572 1.00 16.34 ?  19  LYS   B HA   1 
ATOM   4152 H HB2  . LYS   B 1 19  ? 44.234 -28.814 -15.106 1.00 18.19 ?  19  LYS   B HB2  1 
ATOM   4153 H HB3  . LYS   B 1 19  ? 45.134 -28.703 -13.805 1.00 18.19 ?  19  LYS   B HB3  1 
ATOM   4154 H HG2  . LYS   B 1 19  ? 46.641 -30.248 -14.779 1.00 19.86 ?  19  LYS   B HG2  1 
ATOM   4155 H HG3  . LYS   B 1 19  ? 45.759 -30.212 -16.107 1.00 19.86 ?  19  LYS   B HG3  1 
ATOM   4156 H HD2  . LYS   B 1 19  ? 46.207 -27.882 -16.262 1.00 21.70 ?  19  LYS   B HD2  1 
ATOM   4157 H HD3  . LYS   B 1 19  ? 47.208 -28.034 -15.036 1.00 21.70 ?  19  LYS   B HD3  1 
ATOM   4158 H HE2  . LYS   B 1 19  ? 48.566 -29.429 -16.315 1.00 23.97 ?  19  LYS   B HE2  1 
ATOM   4159 H HE3  . LYS   B 1 19  ? 47.564 -29.279 -17.543 1.00 23.97 ?  19  LYS   B HE3  1 
ATOM   4160 H HZ1  . LYS   B 1 19  ? 49.284 -27.857 -17.833 1.00 25.45 ?  19  LYS   B HZ1  1 
ATOM   4161 H HZ2  . LYS   B 1 19  ? 48.113 -27.043 -17.576 1.00 25.45 ?  19  LYS   B HZ2  1 
ATOM   4162 H HZ3  . LYS   B 1 19  ? 49.095 -27.250 -16.531 1.00 25.45 ?  19  LYS   B HZ3  1 
ATOM   4163 N N    . ASN   B 1 20  ? 45.630 -32.191 -13.285 1.00 14.78 ?  20  ASN   B N    1 
ATOM   4164 C CA   . ASN   B 1 20  ? 46.657 -32.818 -12.462 1.00 15.52 ?  20  ASN   B CA   1 
ATOM   4165 C C    . ASN   B 1 20  ? 47.925 -31.993 -12.652 1.00 15.68 ?  20  ASN   B C    1 
ATOM   4166 O O    . ASN   B 1 20  ? 48.574 -32.070 -13.702 1.00 17.81 ?  20  ASN   B O    1 
ATOM   4167 C CB   . ASN   B 1 20  ? 46.837 -34.269 -12.894 1.00 16.78 ?  20  ASN   B CB   1 
ATOM   4168 C CG   . ASN   B 1 20  ? 48.002 -34.957 -12.215 1.00 18.20 ?  20  ASN   B CG   1 
ATOM   4169 O OD1  . ASN   B 1 20  ? 48.684 -35.788 -12.826 1.00 20.68 ?  20  ASN   B OD1  1 
ATOM   4170 N ND2  . ASN   B 1 20  ? 48.232 -34.639 -10.951 1.00 17.93 ?  20  ASN   B ND2  1 
ATOM   4171 H H    . ASN   B 1 20  ? 45.526 -32.558 -14.056 1.00 17.73 ?  20  ASN   B H    1 
ATOM   4172 H HA   . ASN   B 1 20  ? 46.385 -32.794 -11.530 1.00 18.62 ?  20  ASN   B HA   1 
ATOM   4173 H HB2  . ASN   B 1 20  ? 46.035 -34.764 -12.672 1.00 20.13 ?  20  ASN   B HB2  1 
ATOM   4174 H HB3  . ASN   B 1 20  ? 46.990 -34.292 -13.850 1.00 20.13 ?  20  ASN   B HB3  1 
ATOM   4175 H HD21 . ASN   B 1 20  ? 48.887 -34.996 -10.530 1.00 21.50 ?  20  ASN   B HD21 1 
ATOM   4176 H HD22 . ASN   B 1 20  ? 47.730 -34.060 -10.549 1.00 21.50 ?  20  ASN   B HD22 1 
ATOM   4177 N N    . ALA   B 1 21  ? 48.272 -31.179 -11.650 1.00 15.11 ?  21  ALA   B N    1 
ATOM   4178 C CA   . ALA   B 1 21  ? 49.390 -30.259 -11.795 1.00 16.25 ?  21  ALA   B CA   1 
ATOM   4179 C C    . ALA   B 1 21  ? 49.839 -29.760 -10.431 1.00 15.36 ?  21  ALA   B C    1 
ATOM   4180 O O    . ALA   B 1 21  ? 49.090 -29.794 -9.450  1.00 15.66 ?  21  ALA   B O    1 
ATOM   4181 C CB   . ALA   B 1 21  ? 49.015 -29.080 -12.694 1.00 18.07 ?  21  ALA   B CB   1 
ATOM   4182 H H    . ALA   B 1 21  ? 47.878 -31.142 -10.882 1.00 18.13 ?  21  ALA   B H    1 
ATOM   4183 H HA   . ALA   B 1 21  ? 50.134 -30.730 -12.202 1.00 19.50 ?  21  ALA   B HA   1 
ATOM   4184 H HB1  . ALA   B 1 21  ? 49.802 -28.537 -12.835 1.00 21.68 ?  21  ALA   B HB1  1 
ATOM   4185 H HB2  . ALA   B 1 21  ? 48.694 -29.428 -13.541 1.00 21.68 ?  21  ALA   B HB2  1 
ATOM   4186 H HB3  . ALA   B 1 21  ? 48.318 -28.564 -12.263 1.00 21.68 ?  21  ALA   B HB3  1 
ATOM   4187 N N    . ASP   B 1 22  ? 51.097 -29.313 -10.401 1.00 14.98 ?  22  ASP   B N    1 
ATOM   4188 C CA   . ASP   B 1 22  ? 51.702 -28.606 -9.279  1.00 14.30 ?  22  ASP   B CA   1 
ATOM   4189 C C    . ASP   B 1 22  ? 51.284 -27.138 -9.373  1.00 13.26 ?  22  ASP   B C    1 
ATOM   4190 O O    . ASP   B 1 22  ? 51.594 -26.464 -10.361 1.00 13.47 ?  22  ASP   B O    1 
ATOM   4191 C CB   . ASP   B 1 22  ? 53.220 -28.777 -9.433  1.00 15.85 ?  22  ASP   B CB   1 
ATOM   4192 C CG   . ASP   B 1 22  ? 54.045 -28.021 -8.401  1.00 17.28 ?  22  ASP   B CG   1 
ATOM   4193 O OD1  . ASP   B 1 22  ? 53.671 -26.910 -7.993  1.00 17.31 ?  22  ASP   B OD1  1 
ATOM   4194 O OD2  . ASP   B 1 22  ? 55.124 -28.532 -8.024  1.00 19.44 -1 22  ASP   B OD2  1 
ATOM   4195 H H    . ASP   B 1 22  ? 51.647 -29.416 -11.057 1.00 17.97 ?  22  ASP   B H    1 
ATOM   4196 H HA   . ASP   B 1 22  ? 51.414 -28.986 -8.432  1.00 17.15 ?  22  ASP   B HA   1 
ATOM   4197 H HB2  . ASP   B 1 22  ? 53.446 -29.714 -9.351  1.00 19.02 ?  22  ASP   B HB2  1 
ATOM   4198 H HB3  . ASP   B 1 22  ? 53.486 -28.446 -10.304 1.00 19.02 ?  22  ASP   B HB3  1 
ATOM   4199 N N    . ILE   B 1 23  ? 50.564 -26.647 -8.358  1.00 12.40 ?  23  ILE   B N    1 
ATOM   4200 C CA   . ILE   B 1 23  ? 49.971 -25.307 -8.428  1.00 11.87 ?  23  ILE   B CA   1 
ATOM   4201 C C    . ILE   B 1 23  ? 51.024 -24.216 -8.568  1.00 11.55 ?  23  ILE   B C    1 
ATOM   4202 O O    . ILE   B 1 23  ? 50.756 -23.178 -9.183  1.00 11.34 ?  23  ILE   B O    1 
ATOM   4203 C CB   . ILE   B 1 23  ? 49.027 -25.066 -7.234  1.00 12.55 ?  23  ILE   B CB   1 
ATOM   4204 C CG1  . ILE   B 1 23  ? 48.179 -23.807 -7.449  1.00 13.18 ?  23  ILE   B CG1  1 
ATOM   4205 C CG2  . ILE   B 1 23  ? 49.797 -25.024 -5.927  1.00 13.72 ?  23  ILE   B CG2  1 
ATOM   4206 C CD1  . ILE   B 1 23  ? 47.068 -23.646 -6.428  1.00 14.01 ?  23  ILE   B CD1  1 
ATOM   4207 H H    . ILE   B 1 23  ? 50.411 -27.067 -7.624  1.00 14.87 ?  23  ILE   B H    1 
ATOM   4208 H HA   . ILE   B 1 23  ? 49.428 -25.272 -9.229  1.00 14.23 ?  23  ILE   B HA   1 
ATOM   4209 H HB   . ILE   B 1 23  ? 48.415 -25.823 -7.194  1.00 15.05 ?  23  ILE   B HB   1 
ATOM   4210 H HG12 . ILE   B 1 23  ? 48.757 -23.029 -7.387  1.00 15.80 ?  23  ILE   B HG12 1 
ATOM   4211 H HG13 . ILE   B 1 23  ? 47.775 -23.844 -8.332  1.00 15.80 ?  23  ILE   B HG13 1 
ATOM   4212 H HG21 . ILE   B 1 23  ? 49.167 -25.022 -5.191  1.00 16.45 ?  23  ILE   B HG21 1 
ATOM   4213 H HG22 . ILE   B 1 23  ? 50.368 -25.805 -5.873  1.00 16.45 ?  23  ILE   B HG22 1 
ATOM   4214 H HG23 . ILE   B 1 23  ? 50.335 -24.218 -5.907  1.00 16.45 ?  23  ILE   B HG23 1 
ATOM   4215 H HD11 . ILE   B 1 23  ? 46.528 -22.877 -6.668  1.00 16.81 ?  23  ILE   B HD11 1 
ATOM   4216 H HD12 . ILE   B 1 23  ? 46.519 -24.449 -6.434  1.00 16.81 ?  23  ILE   B HD12 1 
ATOM   4217 H HD13 . ILE   B 1 23  ? 47.459 -23.520 -5.552  1.00 16.81 ?  23  ILE   B HD13 1 
ATOM   4218 N N    . VAL   B 1 24  ? 52.221 -24.413 -8.007  1.00 11.73 ?  24  VAL   B N    1 
ATOM   4219 C CA   . VAL   B 1 24  ? 53.300 -23.438 -8.179  1.00 12.68 ?  24  VAL   B CA   1 
ATOM   4220 C C    . VAL   B 1 24  ? 53.756 -23.393 -9.632  1.00 12.96 ?  24  VAL   B C    1 
ATOM   4221 O O    . VAL   B 1 24  ? 53.906 -22.317 -10.226 1.00 13.23 ?  24  VAL   B O    1 
ATOM   4222 C CB   . VAL   B 1 24  ? 54.474 -23.759 -7.235  1.00 13.59 ?  24  VAL   B CB   1 
ATOM   4223 C CG1  . VAL   B 1 24  ? 55.692 -22.891 -7.575  1.00 14.71 ?  24  VAL   B CG1  1 
ATOM   4224 C CG2  . VAL   B 1 24  ? 54.067 -23.565 -5.791  1.00 14.97 ?  24  VAL   B CG2  1 
ATOM   4225 H H    . VAL   B 1 24  ? 52.429 -25.092 -7.521  1.00 14.06 ?  24  VAL   B H    1 
ATOM   4226 H HA   . VAL   B 1 24  ? 52.970 -22.560 -7.945  1.00 15.21 ?  24  VAL   B HA   1 
ATOM   4227 H HB   . VAL   B 1 24  ? 54.731 -24.690 -7.347  1.00 16.30 ?  24  VAL   B HB   1 
ATOM   4228 H HG11 . VAL   B 1 24  ? 56.274 -22.848 -6.800  1.00 17.64 ?  24  VAL   B HG11 1 
ATOM   4229 H HG12 . VAL   B 1 24  ? 56.165 -23.296 -8.319  1.00 17.64 ?  24  VAL   B HG12 1 
ATOM   4230 H HG13 . VAL   B 1 24  ? 55.389 -22.002 -7.812  1.00 17.64 ?  24  VAL   B HG13 1 
ATOM   4231 H HG21 . VAL   B 1 24  ? 54.805 -23.817 -5.216  1.00 17.96 ?  24  VAL   B HG21 1 
ATOM   4232 H HG22 . VAL   B 1 24  ? 53.841 -22.632 -5.652  1.00 17.96 ?  24  VAL   B HG22 1 
ATOM   4233 H HG23 . VAL   B 1 24  ? 53.296 -24.123 -5.603  1.00 17.96 ?  24  VAL   B HG23 1 
ATOM   4234 N N    . GLU   B 1 25  ? 54.008 -24.564 -10.222 1.00 14.20 ?  25  GLU   B N    1 
ATOM   4235 C CA   . GLU   B 1 25  ? 54.405 -24.599 -11.624 1.00 15.50 ?  25  GLU   B CA   1 
ATOM   4236 C C    . GLU   B 1 25  ? 53.301 -24.059 -12.516 1.00 14.49 ?  25  GLU   B C    1 
ATOM   4237 O O    . GLU   B 1 25  ? 53.571 -23.344 -13.488 1.00 15.10 ?  25  GLU   B O    1 
ATOM   4238 C CB   . GLU   B 1 25  ? 54.794 -26.020 -12.023 1.00 18.48 ?  25  GLU   B CB   1 
ATOM   4239 C CG   . GLU   B 1 25  ? 56.072 -26.479 -11.351 1.00 22.91 ?  25  GLU   B CG   1 
ATOM   4240 C CD   . GLU   B 1 25  ? 57.203 -25.465 -11.470 1.00 27.08 ?  25  GLU   B CD   1 
ATOM   4241 O OE1  . GLU   B 1 25  ? 57.575 -25.115 -12.611 1.00 28.63 ?  25  GLU   B OE1  1 
ATOM   4242 O OE2  . GLU   B 1 25  ? 57.709 -24.998 -10.422 1.00 28.55 -1 25  GLU   B OE2  1 
ATOM   4243 H H    . GLU   B 1 25  ? 53.950 -25.336 -9.842  1.00 17.03 ?  25  GLU   B H    1 
ATOM   4244 H HA   . GLU   B 1 25  ? 55.164 -24.015 -11.748 1.00 18.60 ?  25  GLU   B HA   1 
ATOM   4245 H HB2  . GLU   B 1 25  ? 54.082 -26.629 -11.763 1.00 22.17 ?  25  GLU   B HB2  1 
ATOM   4246 H HB3  . GLU   B 1 25  ? 54.924 -26.056 -12.984 1.00 22.17 ?  25  GLU   B HB3  1 
ATOM   4247 H HG2  . GLU   B 1 25  ? 55.902 -26.614 -10.411 1.00 27.49 ?  25  GLU   B HG2  1 
ATOM   4248 H HG3  . GLU   B 1 25  ? 56.366 -27.301 -11.769 1.00 27.49 ?  25  GLU   B HG3  1 
ATOM   4249 N N    . GLU   B 1 26  ? 52.048 -24.373 -12.187 1.00 13.33 ?  26  GLU   B N    1 
ATOM   4250 C CA   . GLU   B 1 26  ? 50.922 -23.837 -12.943 1.00 13.66 ?  26  GLU   B CA   1 
ATOM   4251 C C    . GLU   B 1 26  ? 50.883 -22.319 -12.864 1.00 13.21 ?  26  GLU   B C    1 
ATOM   4252 O O    . GLU   B 1 26  ? 50.691 -21.641 -13.878 1.00 14.24 ?  26  GLU   B O    1 
ATOM   4253 C CB   . GLU   B 1 26  ? 49.609 -24.417 -12.416 1.00 15.35 ?  26  GLU   B CB   1 
ATOM   4254 C CG   . GLU   B 1 26  ? 49.200 -25.725 -13.045 1.00 18.71 ?  26  GLU   B CG   1 
ATOM   4255 C CD   . GLU   B 1 26  ? 48.989 -25.633 -14.544 1.00 20.56 ?  26  GLU   B CD   1 
ATOM   4256 O OE1  . GLU   B 1 26  ? 48.058 -24.932 -14.997 1.00 20.58 ?  26  GLU   B OE1  1 
ATOM   4257 O OE2  . GLU   B 1 26  ? 49.754 -26.284 -15.268 1.00 22.22 -1 26  GLU   B OE2  1 
ATOM   4258 H H    . GLU   B 1 26  ? 51.824 -24.901 -11.540 1.00 15.99 ?  26  GLU   B H    1 
ATOM   4259 H HA   . GLU   B 1 26  ? 51.015 -24.088 -13.873 1.00 16.39 ?  26  GLU   B HA   1 
ATOM   4260 H HB2  . GLU   B 1 26  ? 49.695 -24.570 -11.460 1.00 18.41 ?  26  GLU   B HB2  1 
ATOM   4261 H HB3  . GLU   B 1 26  ? 48.897 -23.776 -12.577 1.00 18.41 ?  26  GLU   B HB3  1 
ATOM   4262 H HG2  . GLU   B 1 26  ? 49.898 -26.371 -12.893 1.00 22.44 ?  26  GLU   B HG2  1 
ATOM   4263 H HG3  . GLU   B 1 26  ? 48.367 -26.020 -12.649 1.00 22.44 ?  26  GLU   B HG3  1 
ATOM   4264 N N    . ALA   B 1 27  ? 51.036 -21.768 -11.658 1.00 12.58 ?  27  ALA   B N    1 
ATOM   4265 C CA   . ALA   B 1 27  ? 50.994 -20.319 -11.510 1.00 12.83 ?  27  ALA   B CA   1 
ATOM   4266 C C    . ALA   B 1 27  ? 52.071 -19.656 -12.357 1.00 13.75 ?  27  ALA   B C    1 
ATOM   4267 O O    . ALA   B 1 27  ? 51.817 -18.650 -13.035 1.00 14.41 ?  27  ALA   B O    1 
ATOM   4268 C CB   . ALA   B 1 27  ? 51.145 -19.939 -10.038 1.00 12.85 ?  27  ALA   B CB   1 
ATOM   4269 H H    . ALA   B 1 27  ? 51.160 -22.206 -10.926 1.00 15.09 ?  27  ALA   B H    1 
ATOM   4270 H HA   . ALA   B 1 27  ? 50.138 -19.995 -11.815 1.00 15.39 ?  27  ALA   B HA   1 
ATOM   4271 H HB1  . ALA   B 1 27  ? 51.108 -18.973 -9.956  1.00 15.41 ?  27  ALA   B HB1  1 
ATOM   4272 H HB2  . ALA   B 1 27  ? 50.414 -20.339 -9.536  1.00 15.41 ?  27  ALA   B HB2  1 
ATOM   4273 H HB3  . ALA   B 1 27  ? 51.992 -20.269 -9.707  1.00 15.41 ?  27  ALA   B HB3  1 
ATOM   4274 N N    . LYS   B 1 28  ? 53.283 -20.210 -12.343 1.00 14.80 ?  28  LYS   B N    1 
ATOM   4275 C CA   . LYS   B 1 28  ? 54.364 -19.602 -13.108 1.00 17.09 ?  28  LYS   B CA   1 
ATOM   4276 C C    . LYS   B 1 28  ? 54.106 -19.678 -14.606 1.00 17.63 ?  28  LYS   B C    1 
ATOM   4277 O O    . LYS   B 1 28  ? 54.528 -18.783 -15.346 1.00 18.69 ?  28  LYS   B O    1 
ATOM   4278 C CB   . LYS   B 1 28  ? 55.716 -20.216 -12.723 1.00 19.76 ?  28  LYS   B CB   1 
ATOM   4279 C CG   . LYS   B 1 28  ? 56.120 -19.888 -11.290 1.00 22.96 ?  28  LYS   B CG   1 
ATOM   4280 C CD   . LYS   B 1 28  ? 57.536 -20.334 -10.948 1.00 26.31 ?  28  LYS   B CD   1 
ATOM   4281 C CE   . LYS   B 1 28  ? 57.601 -21.806 -10.607 1.00 29.01 ?  28  LYS   B CE   1 
ATOM   4282 N NZ   . LYS   B 1 28  ? 58.953 -22.192 -10.105 1.00 32.33 ?  28  LYS   B NZ   1 
ATOM   4283 H H    . LYS   B 1 28  ? 53.505 -20.919 -11.908 1.00 17.75 ?  28  LYS   B H    1 
ATOM   4284 H HA   . LYS   B 1 28  ? 54.409 -18.661 -12.882 1.00 20.50 ?  28  LYS   B HA   1 
ATOM   4285 H HB2  . LYS   B 1 28  ? 55.668 -21.179 -12.806 1.00 23.71 ?  28  LYS   B HB2  1 
ATOM   4286 H HB3  . LYS   B 1 28  ? 56.407 -19.865 -13.312 1.00 23.71 ?  28  LYS   B HB3  1 
ATOM   4287 H HG2  . LYS   B 1 28  ? 56.067 -18.927 -11.163 1.00 27.54 ?  28  LYS   B HG2  1 
ATOM   4288 H HG3  . LYS   B 1 28  ? 55.508 -20.335 -10.685 1.00 27.54 ?  28  LYS   B HG3  1 
ATOM   4289 H HD2  . LYS   B 1 28  ? 58.112 -20.172 -11.712 1.00 31.56 ?  28  LYS   B HD2  1 
ATOM   4290 H HD3  . LYS   B 1 28  ? 57.848 -19.829 -10.181 1.00 31.56 ?  28  LYS   B HD3  1 
ATOM   4291 H HE2  . LYS   B 1 28  ? 56.951 -22.003 -9.915  1.00 34.81 ?  28  LYS   B HE2  1 
ATOM   4292 H HE3  . LYS   B 1 28  ? 57.412 -22.329 -11.402 1.00 34.81 ?  28  LYS   B HE3  1 
ATOM   4293 H HZ1  . LYS   B 1 28  ? 58.970 -23.060 -9.910  1.00 38.79 ?  28  LYS   B HZ1  1 
ATOM   4294 H HZ2  . LYS   B 1 28  ? 59.569 -22.023 -10.725 1.00 38.79 ?  28  LYS   B HZ2  1 
ATOM   4295 H HZ3  . LYS   B 1 28  ? 59.149 -21.728 -9.370  1.00 38.79 ?  28  LYS   B HZ3  1 
ATOM   4296 N N    . LYS   B 1 29  ? 53.398 -20.708 -15.070 1.00 18.32 ?  29  LYS   B N    1 
ATOM   4297 C CA   . LYS   B 1 29  ? 53.117 -20.833 -16.496 1.00 21.33 ?  29  LYS   B CA   1 
ATOM   4298 C C    . LYS   B 1 29  ? 51.877 -20.055 -16.927 1.00 20.35 ?  29  LYS   B C    1 
ATOM   4299 O O    . LYS   B 1 29  ? 51.894 -19.400 -17.975 1.00 21.43 ?  29  LYS   B O    1 
ATOM   4300 C CB   . LYS   B 1 29  ? 52.969 -22.308 -16.875 1.00 25.80 ?  29  LYS   B CB   1 
ATOM   4301 C CG   . LYS   B 1 29  ? 52.847 -22.553 -18.368 1.00 29.34 ?  29  LYS   B CG   1 
ATOM   4302 C CD   . LYS   B 1 29  ? 53.095 -24.013 -18.710 1.00 32.08 ?  29  LYS   B CD   1 
ATOM   4303 C CE   . LYS   B 1 29  ? 52.003 -24.918 -18.159 1.00 33.92 ?  29  LYS   B CE   1 
ATOM   4304 N NZ   . LYS   B 1 29  ? 52.255 -26.348 -18.496 1.00 34.88 ?  29  LYS   B NZ   1 
ATOM   4305 H H    . LYS   B 1 29  ? 53.074 -21.344 -14.580 1.00 21.98 ?  29  LYS   B H    1 
ATOM   4306 H HA   . LYS   B 1 29  ? 53.869 -20.478 -16.989 1.00 25.58 ?  29  LYS   B HA   1 
ATOM   4307 H HB2  . LYS   B 1 29  ? 53.753 -22.788 -16.562 1.00 30.96 ?  29  LYS   B HB2  1 
ATOM   4308 H HB3  . LYS   B 1 29  ? 52.176 -22.662 -16.452 1.00 30.96 ?  29  LYS   B HB3  1 
ATOM   4309 H HG2  . LYS   B 1 29  ? 51.952 -22.320 -18.659 1.00 35.19 ?  29  LYS   B HG2  1 
ATOM   4310 H HG3  . LYS   B 1 29  ? 53.504 -22.015 -18.838 1.00 35.19 ?  29  LYS   B HG3  1 
ATOM   4311 H HD2  . LYS   B 1 29  ? 53.116 -24.115 -19.674 1.00 38.49 ?  29  LYS   B HD2  1 
ATOM   4312 H HD3  . LYS   B 1 29  ? 53.942 -24.290 -18.326 1.00 38.49 ?  29  LYS   B HD3  1 
ATOM   4313 H HE2  . LYS   B 1 29  ? 51.974 -24.836 -17.193 1.00 40.70 ?  29  LYS   B HE2  1 
ATOM   4314 H HE3  . LYS   B 1 29  ? 51.150 -24.661 -18.544 1.00 40.70 ?  29  LYS   B HE3  1 
ATOM   4315 H HZ1  . LYS   B 1 29  ? 51.606 -26.859 -18.165 1.00 41.85 ?  29  LYS   B HZ1  1 
ATOM   4316 H HZ2  . LYS   B 1 29  ? 52.283 -26.453 -19.379 1.00 41.85 ?  29  LYS   B HZ2  1 
ATOM   4317 H HZ3  . LYS   B 1 29  ? 53.033 -26.610 -18.150 1.00 41.85 ?  29  LYS   B HZ3  1 
ATOM   4318 N N    . VAL   B 1 30  ? 50.802 -20.124 -16.135 1.00 18.91 ?  30  VAL   B N    1 
ATOM   4319 C CA   . VAL   B 1 30  ? 49.514 -19.523 -16.494 1.00 19.24 ?  30  VAL   B CA   1 
ATOM   4320 C C    . VAL   B 1 30  ? 49.520 -18.008 -16.335 1.00 18.64 ?  30  VAL   B C    1 
ATOM   4321 O O    . VAL   B 1 30  ? 48.781 -17.299 -17.034 1.00 19.47 ?  30  VAL   B O    1 
ATOM   4322 C CB   . VAL   B 1 30  ? 48.409 -20.143 -15.615 1.00 19.61 ?  30  VAL   B CB   1 
ATOM   4323 C CG1  . VAL   B 1 30  ? 47.113 -19.347 -15.712 1.00 19.82 ?  30  VAL   B CG1  1 
ATOM   4324 C CG2  . VAL   B 1 30  ? 48.177 -21.596 -15.994 1.00 20.30 ?  30  VAL   B CG2  1 
ATOM   4325 H H    . VAL   B 1 30  ? 50.778 -20.543 -15.375 1.00 22.68 ?  30  VAL   B H    1 
ATOM   4326 H HA   . VAL   B 1 30  ? 49.307 -19.741 -17.417 1.00 23.08 ?  30  VAL   B HA   1 
ATOM   4327 H HB   . VAL   B 1 30  ? 48.694 -20.128 -14.687 1.00 23.52 ?  30  VAL   B HB   1 
ATOM   4328 H HG11 . VAL   B 1 30  ? 46.370 -19.933 -15.490 1.00 23.78 ?  30  VAL   B HG11 1 
ATOM   4329 H HG12 . VAL   B 1 30  ? 47.141 -18.608 -15.086 1.00 23.78 ?  30  VAL   B HG12 1 
ATOM   4330 H HG13 . VAL   B 1 30  ? 47.004 -19.023 -16.616 1.00 23.78 ?  30  VAL   B HG13 1 
ATOM   4331 H HG21 . VAL   B 1 30  ? 47.488 -21.969 -15.419 1.00 24.35 ?  30  VAL   B HG21 1 
ATOM   4332 H HG22 . VAL   B 1 30  ? 47.891 -21.637 -16.920 1.00 24.35 ?  30  VAL   B HG22 1 
ATOM   4333 H HG23 . VAL   B 1 30  ? 49.004 -22.087 -15.878 1.00 24.35 ?  30  VAL   B HG23 1 
ATOM   4334 N N    . LYS   B 1 31  ? 50.287 -17.504 -15.381 1.00 18.48 ?  31  LYS   B N    1 
ATOM   4335 C CA   . LYS   B 1 31  ? 50.311 -16.095 -15.014 1.00 18.91 ?  31  LYS   B CA   1 
ATOM   4336 C C    . LYS   B 1 31  ? 48.905 -15.632 -14.633 1.00 16.67 ?  31  LYS   B C    1 
ATOM   4337 O O    . LYS   B 1 31  ? 48.357 -14.711 -15.256 1.00 17.63 ?  31  LYS   B O    1 
ATOM   4338 C CB   . LYS   B 1 31  ? 50.939 -15.274 -16.143 1.00 22.37 ?  31  LYS   B CB   1 
ATOM   4339 C CG   . LYS   B 1 31  ? 52.346 -15.758 -16.511 1.00 25.66 ?  31  LYS   B CG   1 
ATOM   4340 C CD   . LYS   B 1 31  ? 52.929 -14.993 -17.679 1.00 28.01 ?  31  LYS   B CD   1 
ATOM   4341 C CE   . LYS   B 1 31  ? 54.395 -15.327 -17.861 1.00 29.68 ?  31  LYS   B CE   1 
ATOM   4342 N NZ   . LYS   B 1 31  ? 55.181 -14.988 -16.642 1.00 31.85 ?  31  LYS   B NZ   1 
ATOM   4343 H H    . LYS   B 1 31  ? 50.819 -17.990 -14.918 1.00 22.17 ?  31  LYS   B H    1 
ATOM   4344 H HA   . LYS   B 1 31  ? 50.864 -16.007 -14.232 1.00 22.68 ?  31  LYS   B HA   1 
ATOM   4345 H HB2  . LYS   B 1 31  ? 50.381 -15.341 -16.933 1.00 26.84 ?  31  LYS   B HB2  1 
ATOM   4346 H HB3  . LYS   B 1 31  ? 51.002 -14.354 -15.853 1.00 26.84 ?  31  LYS   B HB3  1 
ATOM   4347 H HG2  . LYS   B 1 31  ? 52.924 -15.641 -15.742 1.00 30.78 ?  31  LYS   B HG2  1 
ATOM   4348 H HG3  . LYS   B 1 31  ? 52.305 -16.698 -16.755 1.00 30.78 ?  31  LYS   B HG3  1 
ATOM   4349 H HD2  . LYS   B 1 31  ? 52.453 -15.239 -18.489 1.00 33.60 ?  31  LYS   B HD2  1 
ATOM   4350 H HD3  . LYS   B 1 31  ? 52.845 -14.044 -17.511 1.00 33.60 ?  31  LYS   B HD3  1 
ATOM   4351 H HE2  . LYS   B 1 31  ? 54.491 -16.278 -18.031 1.00 35.61 ?  31  LYS   B HE2  1 
ATOM   4352 H HE3  . LYS   B 1 31  ? 54.749 -14.816 -18.605 1.00 35.61 ?  31  LYS   B HE3  1 
ATOM   4353 H HZ1  . LYS   B 1 31  ? 56.052 -15.043 -16.816 1.00 38.21 ?  31  LYS   B HZ1  1 
ATOM   4354 H HZ2  . LYS   B 1 31  ? 54.991 -14.159 -16.378 1.00 38.21 ?  31  LYS   B HZ2  1 
ATOM   4355 H HZ3  . LYS   B 1 31  ? 54.982 -15.553 -15.983 1.00 38.21 ?  31  LYS   B HZ3  1 
ATOM   4356 N N    . PRO   B 1 32  ? 48.293 -16.244 -13.610 1.00 14.02 ?  32  PRO   B N    1 
ATOM   4357 C CA   . PRO   B 1 32  ? 46.911 -15.892 -13.263 1.00 12.85 ?  32  PRO   B CA   1 
ATOM   4358 C C    . PRO   B 1 32  ? 46.822 -14.548 -12.561 1.00 12.98 ?  32  PRO   B C    1 
ATOM   4359 O O    . PRO   B 1 32  ? 47.741 -14.119 -11.856 1.00 14.15 ?  32  PRO   B O    1 
ATOM   4360 C CB   . PRO   B 1 32  ? 46.506 -17.018 -12.306 1.00 12.72 ?  32  PRO   B CB   1 
ATOM   4361 C CG   . PRO   B 1 32  ? 47.788 -17.361 -11.612 1.00 13.44 ?  32  PRO   B CG   1 
ATOM   4362 C CD   . PRO   B 1 32  ? 48.855 -17.234 -12.666 1.00 13.85 ?  32  PRO   B CD   1 
ATOM   4363 H HA   . PRO   B 1 32  ? 46.339 -15.898 -14.047 1.00 15.41 ?  32  PRO   B HA   1 
ATOM   4364 H HB2  . PRO   B 1 32  ? 45.838 -16.698 -11.675 1.00 15.26 ?  32  PRO   B HB2  1 
ATOM   4365 H HB3  . PRO   B 1 32  ? 46.165 -17.777 -12.810 1.00 15.26 ?  32  PRO   B HB3  1 
ATOM   4366 H HG2  . PRO   B 1 32  ? 47.944 -16.737 -10.883 1.00 16.12 ?  32  PRO   B HG2  1 
ATOM   4367 H HG3  . PRO   B 1 32  ? 47.748 -18.272 -11.276 1.00 16.12 ?  32  PRO   B HG3  1 
ATOM   4368 H HD2  . PRO   B 1 32  ? 49.674 -16.889 -12.270 1.00 16.61 ?  32  PRO   B HD2  1 
ATOM   4369 H HD3  . PRO   B 1 32  ? 48.998 -18.080 -13.104 1.00 16.61 ?  32  PRO   B HD3  1 
ATOM   4370 N N    . THR   B 1 33  ? 45.672 -13.894 -12.739 1.00 12.22 ?  33  THR   B N    1 
ATOM   4371 C CA   . THR   B 1 33  ? 45.368 -12.719 -11.933 1.00 12.48 ?  33  THR   B CA   1 
ATOM   4372 C C    . THR   B 1 33  ? 45.315 -13.072 -10.453 1.00 12.01 ?  33  THR   B C    1 
ATOM   4373 O O    . THR   B 1 33  ? 45.779 -12.297 -9.605  1.00 13.13 ?  33  THR   B O    1 
ATOM   4374 C CB   . THR   B 1 33  ? 44.044 -12.103 -12.396 1.00 13.20 ?  33  THR   B CB   1 
ATOM   4375 O OG1  . THR   B 1 33  ? 44.108 -11.833 -13.799 1.00 13.21 ?  33  THR   B OG1  1 
ATOM   4376 C CG2  . THR   B 1 33  ? 43.734 -10.811 -11.641 1.00 13.90 ?  33  THR   B CG2  1 
ATOM   4377 H H    . THR   B 1 33  ? 45.058 -14.110 -13.307 1.00 14.66 ?  33  THR   B H    1 
ATOM   4378 H HA   . THR   B 1 33  ? 46.058 -12.058 -12.056 1.00 14.97 ?  33  THR   B HA   1 
ATOM   4379 H HB   . THR   B 1 33  ? 43.318 -12.732 -12.232 1.00 15.83 ?  33  THR   B HB   1 
ATOM   4380 H HG1  . THR   B 1 33  ? 43.394 -11.483 -14.066 1.00 15.85 ?  33  THR   B HG1  1 
ATOM   4381 H HG21 . THR   B 1 33  ? 42.970 -10.370 -12.042 1.00 16.67 ?  33  THR   B HG21 1 
ATOM   4382 H HG22 . THR   B 1 33  ? 43.532 -11.011 -10.714 1.00 16.67 ?  33  THR   B HG22 1 
ATOM   4383 H HG23 . THR   B 1 33  ? 44.499 -10.219 -11.680 1.00 16.67 ?  33  THR   B HG23 1 
ATOM   4384 N N    . VAL   B 1 34  ? 44.770 -14.245 -10.120 1.00 11.41 ?  34  VAL   B N    1 
ATOM   4385 C CA   . VAL   B 1 34  ? 44.576 -14.646 -8.729  1.00 10.84 ?  34  VAL   B CA   1 
ATOM   4386 C C    . VAL   B 1 34  ? 45.014 -16.094 -8.566  1.00 10.29 ?  34  VAL   B C    1 
ATOM   4387 O O    . VAL   B 1 34  ? 44.503 -16.982 -9.259  1.00 10.71 ?  34  VAL   B O    1 
ATOM   4388 C CB   . VAL   B 1 34  ? 43.108 -14.513 -8.281  1.00 11.85 ?  34  VAL   B CB   1 
ATOM   4389 C CG1  . VAL   B 1 34  ? 42.946 -14.968 -6.834  1.00 12.28 ?  34  VAL   B CG1  1 
ATOM   4390 C CG2  . VAL   B 1 34  ? 42.593 -13.092 -8.478  1.00 12.88 ?  34  VAL   B CG2  1 
ATOM   4391 H H    . VAL   B 1 34  ? 44.504 -14.835 -10.689 1.00 13.68 ?  34  VAL   B H    1 
ATOM   4392 H HA   . VAL   B 1 34  ? 45.130 -14.094 -8.153  1.00 13.00 ?  34  VAL   B HA   1 
ATOM   4393 H HB   . VAL   B 1 34  ? 42.567 -15.095 -8.832  1.00 14.22 ?  34  VAL   B HB   1 
ATOM   4394 H HG11 . VAL   B 1 34  ? 42.085 -14.659 -6.502  1.00 14.73 ?  34  VAL   B HG11 1 
ATOM   4395 H HG12 . VAL   B 1 34  ? 42.980 -15.937 -6.797  1.00 14.73 ?  34  VAL   B HG12 1 
ATOM   4396 H HG13 . VAL   B 1 34  ? 43.658 -14.588 -6.297  1.00 14.73 ?  34  VAL   B HG13 1 
ATOM   4397 H HG21 . VAL   B 1 34  ? 41.677 -13.041 -8.160  1.00 15.45 ?  34  VAL   B HG21 1 
ATOM   4398 H HG22 . VAL   B 1 34  ? 43.151 -12.477 -7.979  1.00 15.45 ?  34  VAL   B HG22 1 
ATOM   4399 H HG23 . VAL   B 1 34  ? 42.623 -12.873 -9.425  1.00 15.45 ?  34  VAL   B HG23 1 
ATOM   4400 N N    . VAL   B 1 35  ? 45.928 -16.339 -7.629  1.00 9.83  ?  35  VAL   B N    1 
ATOM   4401 C CA   . VAL   B 1 35  ? 46.169 -17.680 -7.106  1.00 9.44  ?  35  VAL   B CA   1 
ATOM   4402 C C    . VAL   B 1 35  ? 45.623 -17.735 -5.687  1.00 9.29  ?  35  VAL   B C    1 
ATOM   4403 O O    . VAL   B 1 35  ? 45.840 -16.811 -4.895  1.00 9.76  ?  35  VAL   B O    1 
ATOM   4404 C CB   . VAL   B 1 35  ? 47.652 -18.097 -7.182  1.00 10.07 ?  35  VAL   B CB   1 
ATOM   4405 C CG1  . VAL   B 1 35  ? 48.546 -17.250 -6.267  1.00 10.72 ?  35  VAL   B CG1  1 
ATOM   4406 C CG2  . VAL   B 1 35  ? 47.797 -19.595 -6.852  1.00 10.68 ?  35  VAL   B CG2  1 
ATOM   4407 H H    . VAL   B 1 35  ? 46.435 -15.735 -7.280  1.00 11.78 ?  35  VAL   B H    1 
ATOM   4408 H HA   . VAL   B 1 35  ? 45.657 -18.312 -7.638  1.00 11.32 ?  35  VAL   B HA   1 
ATOM   4409 H HB   . VAL   B 1 35  ? 47.958 -17.977 -8.091  1.00 12.07 ?  35  VAL   B HB   1 
ATOM   4410 H HG11 . VAL   B 1 35  ? 49.471 -17.485 -6.431  1.00 12.85 ?  35  VAL   B HG11 1 
ATOM   4411 H HG12 . VAL   B 1 35  ? 48.395 -16.317 -6.464  1.00 12.85 ?  35  VAL   B HG12 1 
ATOM   4412 H HG13 . VAL   B 1 35  ? 48.316 -17.438 -5.341  1.00 12.85 ?  35  VAL   B HG13 1 
ATOM   4413 H HG21 . VAL   B 1 35  ? 48.724 -19.855 -6.951  1.00 12.81 ?  35  VAL   B HG21 1 
ATOM   4414 H HG22 . VAL   B 1 35  ? 47.506 -19.752 -5.937  1.00 12.81 ?  35  VAL   B HG22 1 
ATOM   4415 H HG23 . VAL   B 1 35  ? 47.243 -20.113 -7.462  1.00 12.81 ?  35  VAL   B HG23 1 
ATOM   4416 N N    . VAL   B 1 36  ? 44.900 -18.812 -5.369  1.00 9.08  ?  36  VAL   B N    1 
ATOM   4417 C CA   . VAL   B 1 36  ? 44.355 -19.016 -4.036  1.00 8.82  ?  36  VAL   B CA   1 
ATOM   4418 C C    . VAL   B 1 36  ? 45.361 -19.781 -3.185  1.00 8.88  ?  36  VAL   B C    1 
ATOM   4419 O O    . VAL   B 1 36  ? 45.905 -20.807 -3.613  1.00 9.68  ?  36  VAL   B O    1 
ATOM   4420 C CB   . VAL   B 1 36  ? 43.018 -19.774 -4.110  1.00 9.24  ?  36  VAL   B CB   1 
ATOM   4421 C CG1  . VAL   B 1 36  ? 42.521 -20.141 -2.718  1.00 9.78  ?  36  VAL   B CG1  1 
ATOM   4422 C CG2  . VAL   B 1 36  ? 41.989 -18.945 -4.851  1.00 9.92  ?  36  VAL   B CG2  1 
ATOM   4423 H H    . VAL   B 1 36  ? 44.714 -19.451 -5.920  1.00 10.89 ?  36  VAL   B H    1 
ATOM   4424 H HA   . VAL   B 1 36  ? 44.191 -18.156 -3.620  1.00 10.57 ?  36  VAL   B HA   1 
ATOM   4425 H HB   . VAL   B 1 36  ? 43.147 -20.598 -4.604  1.00 11.08 ?  36  VAL   B HB   1 
ATOM   4426 H HG11 . VAL   B 1 36  ? 41.581 -20.368 -2.771  1.00 11.72 ?  36  VAL   B HG11 1 
ATOM   4427 H HG12 . VAL   B 1 36  ? 43.029 -20.891 -2.385  1.00 11.72 ?  36  VAL   B HG12 1 
ATOM   4428 H HG13 . VAL   B 1 36  ? 42.638 -19.370 -2.134  1.00 11.72 ?  36  VAL   B HG13 1 
ATOM   4429 H HG21 . VAL   B 1 36  ? 41.147 -19.422 -4.866  1.00 11.89 ?  36  VAL   B HG21 1 
ATOM   4430 H HG22 . VAL   B 1 36  ? 41.881 -18.095 -4.395  1.00 11.89 ?  36  VAL   B HG22 1 
ATOM   4431 H HG23 . VAL   B 1 36  ? 42.301 -18.793 -5.759  1.00 11.89 ?  36  VAL   B HG23 1 
ATOM   4432 N N    . ASN   B 1 37  ? 45.584 -19.289 -1.967  1.00 9.27  ?  37  ASN   B N    1 
ATOM   4433 C CA   . ASN   B 1 37  ? 46.339 -20.004 -0.954  1.00 9.33  ?  37  ASN   B CA   1 
ATOM   4434 C C    . ASN   B 1 37  ? 45.392 -20.681 0.029   1.00 9.30  ?  37  ASN   B C    1 
ATOM   4435 O O    . ASN   B 1 37  ? 44.380 -20.106 0.440   1.00 9.68  ?  37  ASN   B O    1 
ATOM   4436 C CB   . ASN   B 1 37  ? 47.266 -19.055 -0.193  1.00 9.50  ?  37  ASN   B CB   1 
ATOM   4437 C CG   . ASN   B 1 37  ? 48.119 -19.776 0.821   1.00 9.92  ?  37  ASN   B CG   1 
ATOM   4438 O OD1  . ASN   B 1 37  ? 48.460 -20.950 0.640   1.00 10.34 ?  37  ASN   B OD1  1 
ATOM   4439 N ND2  . ASN   B 1 37  ? 48.467 -19.082 1.897   1.00 9.93  ?  37  ASN   B ND2  1 
ATOM   4440 H H    . ASN   B 1 37  ? 45.295 -18.522 -1.699  1.00 11.12 ?  37  ASN   B H    1 
ATOM   4441 H HA   . ASN   B 1 37  ? 46.880 -20.690 -1.374  1.00 11.19 ?  37  ASN   B HA   1 
ATOM   4442 H HB2  . ASN   B 1 37  ? 47.857 -18.621 -0.824  1.00 11.40 ?  37  ASN   B HB2  1 
ATOM   4443 H HB3  . ASN   B 1 37  ? 46.731 -18.398 0.277   1.00 11.40 ?  37  ASN   B HB3  1 
ATOM   4444 H HD21 . ASN   B 1 37  ? 48.956 -19.446 2.502   1.00 11.91 ?  37  ASN   B HD21 1 
ATOM   4445 H HD22 . ASN   B 1 37  ? 48.213 -18.271 1.986   1.00 11.91 ?  37  ASN   B HD22 1 
ATOM   4446 N N    . ALA   B 1 38  ? 45.746 -21.912 0.406   1.00 9.48  ?  38  ALA   B N    1 
ATOM   4447 C CA   . ALA   B 1 38  ? 45.087 -22.666 1.476   1.00 9.97  ?  38  ALA   B CA   1 
ATOM   4448 C C    . ALA   B 1 38  ? 45.668 -22.178 2.805   1.00 9.96  ?  38  ALA   B C    1 
ATOM   4449 O O    . ALA   B 1 38  ? 46.568 -22.783 3.395   1.00 10.73 ?  38  ALA   B O    1 
ATOM   4450 C CB   . ALA   B 1 38  ? 45.316 -24.158 1.271   1.00 10.91 ?  38  ALA   B CB   1 
ATOM   4451 H H    . ALA   B 1 38  ? 46.397 -22.343 0.050   1.00 11.37 ?  38  ALA   B H    1 
ATOM   4452 H HA   . ALA   B 1 38  ? 44.134 -22.487 1.466   1.00 11.96 ?  38  ALA   B HA   1 
ATOM   4453 H HB1  . ALA   B 1 38  ? 44.871 -24.647 1.983   1.00 13.08 ?  38  ALA   B HB1  1 
ATOM   4454 H HB2  . ALA   B 1 38  ? 44.943 -24.419 0.413   1.00 13.08 ?  38  ALA   B HB2  1 
ATOM   4455 H HB3  . ALA   B 1 38  ? 46.266 -24.340 1.289   1.00 13.08 ?  38  ALA   B HB3  1 
ATOM   4456 N N    . ALA   B 1 39  ? 45.156 -21.035 3.265   1.00 9.72  ?  39  ALA   B N    1 
ATOM   4457 C CA   . ALA   B 1 39  ? 45.701 -20.299 4.397   1.00 10.01 ?  39  ALA   B CA   1 
ATOM   4458 C C    . ALA   B 1 39  ? 45.080 -20.741 5.721   1.00 10.16 ?  39  ALA   B C    1 
ATOM   4459 O O    . ALA   B 1 39  ? 44.050 -21.414 5.767   1.00 10.84 ?  39  ALA   B O    1 
ATOM   4460 C CB   . ALA   B 1 39  ? 45.466 -18.798 4.200   1.00 11.00 ?  39  ALA   B CB   1 
ATOM   4461 H H    . ALA   B 1 39  ? 44.466 -20.657 2.917   1.00 11.65 ?  39  ALA   B H    1 
ATOM   4462 H HA   . ALA   B 1 39  ? 46.651 -20.452 4.448   1.00 12.00 ?  39  ALA   B HA   1 
ATOM   4463 H HB1  . ALA   B 1 39  ? 45.832 -18.319 4.959   1.00 13.19 ?  39  ALA   B HB1  1 
ATOM   4464 H HB2  . ALA   B 1 39  ? 45.914 -18.515 3.385   1.00 13.19 ?  39  ALA   B HB2  1 
ATOM   4465 H HB3  . ALA   B 1 39  ? 44.514 -18.629 4.127   1.00 13.19 ?  39  ALA   B HB3  1 
ATOM   4466 N N    . ASN   B 1 40  ? 45.718 -20.321 6.811   1.00 10.79 ?  40  ASN   B N    1 
ATOM   4467 C CA   . ASN   B 1 40  ? 45.153 -20.374 8.152   1.00 11.80 ?  40  ASN   B CA   1 
ATOM   4468 C C    . ASN   B 1 40  ? 44.977 -18.948 8.682   1.00 11.57 ?  40  ASN   B C    1 
ATOM   4469 O O    . ASN   B 1 40  ? 45.389 -17.969 8.052   1.00 11.25 ?  40  ASN   B O    1 
ATOM   4470 C CB   . ASN   B 1 40  ? 45.997 -21.259 9.085   1.00 12.32 ?  40  ASN   B CB   1 
ATOM   4471 C CG   . ASN   B 1 40  ? 47.449 -20.846 9.129   1.00 13.32 ?  40  ASN   B CG   1 
ATOM   4472 O OD1  . ASN   B 1 40  ? 47.764 -19.666 9.211   1.00 15.32 ?  40  ASN   B OD1  1 
ATOM   4473 N ND2  . ASN   B 1 40  ? 48.343 -21.816 9.079   1.00 13.86 ?  40  ASN   B ND2  1 
ATOM   4474 H H    . ASN   B 1 40  ? 46.511 -19.999 6.795   1.00 12.94 ?  40  ASN   B H    1 
ATOM   4475 H HA   . ASN   B 1 40  ? 44.267 -20.768 8.102   1.00 14.15 ?  40  ASN   B HA   1 
ATOM   4476 H HB2  . ASN   B 1 40  ? 45.637 -21.199 9.986   1.00 14.77 ?  40  ASN   B HB2  1 
ATOM   4477 H HB3  . ASN   B 1 40  ? 45.953 -22.175 8.772   1.00 14.77 ?  40  ASN   B HB3  1 
ATOM   4478 H HD21 . ASN   B 1 40  ? 49.181 -21.629 9.107   1.00 16.62 ?  40  ASN   B HD21 1 
ATOM   4479 H HD22 . ASN   B 1 40  ? 48.085 -22.635 9.026   1.00 16.62 ?  40  ASN   B HD22 1 
ATOM   4480 N N    . VAL   B 1 41  ? 44.320 -18.819 9.839   1.00 11.71 ?  41  VAL   B N    1 
ATOM   4481 C CA   . VAL   B 1 41  ? 43.864 -17.498 10.282  1.00 12.27 ?  41  VAL   B CA   1 
ATOM   4482 C C    . VAL   B 1 41  ? 45.019 -16.551 10.591  1.00 12.22 ?  41  VAL   B C    1 
ATOM   4483 O O    . VAL   B 1 41  ? 44.844 -15.328 10.518  1.00 12.68 ?  41  VAL   B O    1 
ATOM   4484 C CB   . VAL   B 1 41  ? 42.880 -17.569 11.468  1.00 13.81 ?  41  VAL   B CB   1 
ATOM   4485 C CG1  . VAL   B 1 41  ? 41.581 -18.254 11.059  1.00 14.09 ?  41  VAL   B CG1  1 
ATOM   4486 C CG2  . VAL   B 1 41  ? 43.515 -18.249 12.667  1.00 15.02 ?  41  VAL   B CG2  1 
ATOM   4487 H H    . VAL   B 1 41  ? 44.125 -19.463 10.369  1.00 14.04 ?  41  VAL   B H    1 
ATOM   4488 H HA   . VAL   B 1 41  ? 43.374 -17.094 9.550   1.00 14.72 ?  41  VAL   B HA   1 
ATOM   4489 H HB   . VAL   B 1 41  ? 42.653 -16.664 11.737  1.00 16.56 ?  41  VAL   B HB   1 
ATOM   4490 H HG11 . VAL   B 1 41  ? 40.976 -18.264 11.818  1.00 16.91 ?  41  VAL   B HG11 1 
ATOM   4491 H HG12 . VAL   B 1 41  ? 41.183 -17.762 10.325  1.00 16.91 ?  41  VAL   B HG12 1 
ATOM   4492 H HG13 . VAL   B 1 41  ? 41.779 -19.162 10.782  1.00 16.91 ?  41  VAL   B HG13 1 
ATOM   4493 H HG21 . VAL   B 1 41  ? 42.869 -18.290 13.388  1.00 18.02 ?  41  VAL   B HG21 1 
ATOM   4494 H HG22 . VAL   B 1 41  ? 43.784 -19.148 12.414  1.00 18.02 ?  41  VAL   B HG22 1 
ATOM   4495 H HG23 . VAL   B 1 41  ? 44.291 -17.740 12.946  1.00 18.02 ?  41  VAL   B HG23 1 
ATOM   4496 N N    . TYR   B 1 42  ? 46.187 -17.071 10.974  1.00 12.40 ?  42  TYR   B N    1 
ATOM   4497 C CA   . TYR   B 1 42  ? 47.344 -16.223 11.240  1.00 13.21 ?  42  TYR   B CA   1 
ATOM   4498 C C    . TYR   B 1 42  ? 48.305 -16.142 10.057  1.00 12.39 ?  42  TYR   B C    1 
ATOM   4499 O O    . TYR   B 1 42  ? 49.395 -15.572 10.188  1.00 13.35 ?  42  TYR   B O    1 
ATOM   4500 C CB   . TYR   B 1 42  ? 48.051 -16.631 12.542  1.00 15.05 ?  42  TYR   B CB   1 
ATOM   4501 C CG   . TYR   B 1 42  ? 47.431 -15.971 13.772  1.00 16.01 ?  42  TYR   B CG   1 
ATOM   4502 C CD1  . TYR   B 1 42  ? 47.643 -14.621 14.037  1.00 15.55 ?  42  TYR   B CD1  1 
ATOM   4503 C CD2  . TYR   B 1 42  ? 46.632 -16.683 14.650  1.00 17.90 ?  42  TYR   B CD2  1 
ATOM   4504 C CE1  . TYR   B 1 42  ? 47.079 -14.002 15.137  1.00 16.79 ?  42  TYR   B CE1  1 
ATOM   4505 C CE2  . TYR   B 1 42  ? 46.068 -16.074 15.760  1.00 18.11 ?  42  TYR   B CE2  1 
ATOM   4506 C CZ   . TYR   B 1 42  ? 46.291 -14.732 15.998  1.00 18.50 ?  42  TYR   B CZ   1 
ATOM   4507 O OH   . TYR   B 1 42  ? 45.733 -14.116 17.099  1.00 21.19 ?  42  TYR   B OH   1 
ATOM   4508 H H    . TYR   B 1 42  ? 46.330 -17.915 11.080  1.00 14.87 ?  42  TYR   B H    1 
ATOM   4509 H HA   . TYR   B 1 42  ? 47.016 -15.325 11.383  1.00 15.85 ?  42  TYR   B HA   1 
ATOM   4510 H HB2  . TYR   B 1 42  ? 47.987 -17.590 12.654  1.00 18.05 ?  42  TYR   B HB2  1 
ATOM   4511 H HB3  . TYR   B 1 42  ? 48.982 -16.361 12.493  1.00 18.05 ?  42  TYR   B HB3  1 
ATOM   4512 H HD1  . TYR   B 1 42  ? 48.176 -14.122 13.451  1.00 18.65 ?  42  TYR   B HD1  1 
ATOM   4513 H HD2  . TYR   B 1 42  ? 46.474 -17.588 14.490  1.00 21.48 ?  42  TYR   B HD2  1 
ATOM   4514 H HE1  . TYR   B 1 42  ? 47.239 -13.100 15.294  1.00 20.14 ?  42  TYR   B HE1  1 
ATOM   4515 H HE2  . TYR   B 1 42  ? 45.534 -16.567 16.338  1.00 21.73 ?  42  TYR   B HE2  1 
ATOM   4516 H HH   . TYR   B 1 42  ? 45.960 -13.310 17.113  1.00 25.42 ?  42  TYR   B HH   1 
ATOM   4517 N N    . LEU   B 1 43  ? 47.906 -16.657 8.897   1.00 11.35 ?  43  LEU   B N    1 
ATOM   4518 C CA   . LEU   B 1 43  ? 48.716 -16.586 7.685   1.00 11.39 ?  43  LEU   B CA   1 
ATOM   4519 C C    . LEU   B 1 43  ? 50.127 -17.098 7.941   1.00 11.25 ?  43  LEU   B C    1 
ATOM   4520 O O    . LEU   B 1 43  ? 51.109 -16.506 7.492   1.00 12.03 ?  43  LEU   B O    1 
ATOM   4521 C CB   . LEU   B 1 43  ? 48.737 -15.181 7.079   1.00 11.65 ?  43  LEU   B CB   1 
ATOM   4522 C CG   . LEU   B 1 43  ? 47.379 -14.570 6.707   1.00 11.76 ?  43  LEU   B CG   1 
ATOM   4523 C CD1  . LEU   B 1 43  ? 47.604 -13.177 6.132   1.00 12.66 ?  43  LEU   B CD1  1 
ATOM   4524 C CD2  . LEU   B 1 43  ? 46.609 -15.450 5.728   1.00 11.86 ?  43  LEU   B CD2  1 
ATOM   4525 H H    . LEU   B 1 43  ? 47.156 -17.065 8.783   1.00 13.61 ?  43  LEU   B H    1 
ATOM   4526 H HA   . LEU   B 1 43  ? 48.314 -17.175 7.023   1.00 13.66 ?  43  LEU   B HA   1 
ATOM   4527 H HB2  . LEU   B 1 43  ? 49.156 -14.585 7.716   1.00 13.97 ?  43  LEU   B HB2  1 
ATOM   4528 H HB3  . LEU   B 1 43  ? 49.266 -15.213 6.268   1.00 13.97 ?  43  LEU   B HB3  1 
ATOM   4529 H HG   . LEU   B 1 43  ? 46.846 -14.477 7.510   1.00 14.10 ?  43  LEU   B HG   1 
ATOM   4530 H HD11 . LEU   B 1 43  ? 46.745 -12.789 5.898   1.00 15.19 ?  43  LEU   B HD11 1 
ATOM   4531 H HD12 . LEU   B 1 43  ? 48.042 -12.626 6.801   1.00 15.19 ?  43  LEU   B HD12 1 
ATOM   4532 H HD13 . LEU   B 1 43  ? 48.163 -13.245 5.343   1.00 15.19 ?  43  LEU   B HD13 1 
ATOM   4533 H HD21 . LEU   B 1 43  ? 45.803 -14.983 5.450   1.00 14.23 ?  43  LEU   B HD21 1 
ATOM   4534 H HD22 . LEU   B 1 43  ? 47.167 -15.631 4.956   1.00 14.23 ?  43  LEU   B HD22 1 
ATOM   4535 H HD23 . LEU   B 1 43  ? 46.372 -16.281 6.168   1.00 14.23 ?  43  LEU   B HD23 1 
ATOM   4536 N N    . LYS   B 1 44  ? 50.225 -18.224 8.655   1.00 11.22 ?  44  LYS   B N    1 
ATOM   4537 C CA   . LYS   B 1 44  ? 51.492 -18.901 8.897   1.00 11.87 ?  44  LYS   B CA   1 
ATOM   4538 C C    . LYS   B 1 44  ? 51.615 -20.015 7.866   1.00 11.53 ?  44  LYS   B C    1 
ATOM   4539 O O    . LYS   B 1 44  ? 50.919 -21.033 7.949   1.00 12.56 ?  44  LYS   B O    1 
ATOM   4540 C CB   . LYS   B 1 44  ? 51.555 -19.424 10.332  1.00 13.92 ?  44  LYS   B CB   1 
ATOM   4541 C CG   . LYS   B 1 44  ? 51.724 -18.309 11.364  1.00 16.72 ?  44  LYS   B CG   1 
ATOM   4542 C CD   . LYS   B 1 44  ? 52.934 -17.443 11.004  1.00 19.53 ?  44  LYS   B CD   1 
ATOM   4543 C CE   . LYS   B 1 44  ? 53.337 -16.495 12.106  1.00 22.04 ?  44  LYS   B CE   1 
ATOM   4544 N NZ   . LYS   B 1 44  ? 54.571 -15.733 11.775  1.00 23.05 ?  44  LYS   B NZ   1 
ATOM   4545 H H    . LYS   B 1 44  ? 49.551 -18.616 9.018   1.00 13.45 ?  44  LYS   B H    1 
ATOM   4546 H HA   . LYS   B 1 44  ? 52.222 -18.282 8.741   1.00 14.24 ?  44  LYS   B HA   1 
ATOM   4547 H HB2  . LYS   B 1 44  ? 50.725 -19.888 10.535  1.00 16.70 ?  44  LYS   B HB2  1 
ATOM   4548 H HB3  . LYS   B 1 44  ? 52.304 -20.026 10.419  1.00 16.70 ?  44  LYS   B HB3  1 
ATOM   4549 H HG2  . LYS   B 1 44  ? 50.933 -17.750 11.376  1.00 20.06 ?  44  LYS   B HG2  1 
ATOM   4550 H HG3  . LYS   B 1 44  ? 51.876 -18.703 12.242  1.00 20.06 ?  44  LYS   B HG3  1 
ATOM   4551 H HD2  . LYS   B 1 44  ? 53.686 -18.029 10.800  1.00 23.43 ?  44  LYS   B HD2  1 
ATOM   4552 H HD3  . LYS   B 1 44  ? 52.714 -16.907 10.227  1.00 23.43 ?  44  LYS   B HD3  1 
ATOM   4553 H HE2  . LYS   B 1 44  ? 52.623 -15.856 12.232  1.00 26.44 ?  44  LYS   B HE2  1 
ATOM   4554 H HE3  . LYS   B 1 44  ? 53.496 -16.999 12.919  1.00 26.44 ?  44  LYS   B HE3  1 
ATOM   4555 H HZ1  . LYS   B 1 44  ? 54.775 -15.182 12.444  1.00 27.66 ?  44  LYS   B HZ1  1 
ATOM   4556 H HZ2  . LYS   B 1 44  ? 55.251 -16.291 11.642  1.00 27.66 ?  44  LYS   B HZ2  1 
ATOM   4557 H HZ3  . LYS   B 1 44  ? 54.443 -15.253 11.035  1.00 27.66 ?  44  LYS   B HZ3  1 
ATOM   4558 N N    . HIS   B 1 45  ? 52.472 -19.793 6.870   1.00 11.46 ?  45  HIS   B N    1 
ATOM   4559 C CA   . HIS   B 1 45  ? 52.500 -20.622 5.666   1.00 11.46 ?  45  HIS   B CA   1 
ATOM   4560 C C    . HIS   B 1 45  ? 53.517 -21.749 5.828   1.00 13.44 ?  45  HIS   B C    1 
ATOM   4561 O O    . HIS   B 1 45  ? 54.576 -21.770 5.209   1.00 15.60 ?  45  HIS   B O    1 
ATOM   4562 C CB   . HIS   B 1 45  ? 52.812 -19.763 4.453   1.00 11.37 ?  45  HIS   B CB   1 
ATOM   4563 C CG   . HIS   B 1 45  ? 51.935 -18.563 4.340   1.00 11.35 ?  45  HIS   B CG   1 
ATOM   4564 N ND1  . HIS   B 1 45  ? 50.558 -18.645 4.286   1.00 11.26 ?  45  HIS   B ND1  1 
ATOM   4565 C CD2  . HIS   B 1 45  ? 52.245 -17.246 4.283   1.00 12.27 ?  45  HIS   B CD2  1 
ATOM   4566 C CE1  . HIS   B 1 45  ? 50.063 -17.423 4.190   1.00 11.31 ?  45  HIS   B CE1  1 
ATOM   4567 N NE2  . HIS   B 1 45  ? 51.064 -16.557 4.178   1.00 11.71 ?  45  HIS   B NE2  1 
ATOM   4568 H H    . HIS   B 1 45  ? 53.051 -19.155 6.866   1.00 13.74 ?  45  HIS   B H    1 
ATOM   4569 H HA   . HIS   B 1 45  ? 51.621 -21.018 5.536   1.00 13.74 ?  45  HIS   B HA   1 
ATOM   4570 H HB2  . HIS   B 1 45  ? 53.729 -19.458 4.511   1.00 13.64 ?  45  HIS   B HB2  1 
ATOM   4571 H HB3  . HIS   B 1 45  ? 52.691 -20.299 3.650   1.00 13.64 ?  45  HIS   B HB3  1 
ATOM   4572 H HD2  . HIS   B 1 45  ? 53.096 -16.878 4.307   1.00 14.71 ?  45  HIS   B HD2  1 
ATOM   4573 H HE1  . HIS   B 1 45  ? 49.158 -17.212 4.124   1.00 13.56 ?  45  HIS   B HE1  1 
ATOM   4574 H HE2  . HIS   B 1 45  ? 50.980 -15.703 4.135   1.00 14.04 ?  45  HIS   B HE2  1 
ATOM   4575 N N    A GLY   B 1 46  ? 53.152 -22.716 6.667   0.40 14.59 ?  46  GLY   B N    1 
ATOM   4576 N N    B GLY   B 1 46  ? 53.162 -22.704 6.681   0.60 14.59 ?  46  GLY   B N    1 
ATOM   4577 C CA   A GLY   B 1 46  ? 54.069 -23.772 7.056   0.40 15.80 ?  46  GLY   B CA   1 
ATOM   4578 C CA   B GLY   B 1 46  ? 54.077 -23.772 7.028   0.60 15.94 ?  46  GLY   B CA   1 
ATOM   4579 C C    A GLY   B 1 46  ? 54.133 -24.986 6.148   0.40 16.93 ?  46  GLY   B C    1 
ATOM   4580 C C    B GLY   B 1 46  ? 54.122 -24.923 6.043   0.60 17.24 ?  46  GLY   B C    1 
ATOM   4581 O O    A GLY   B 1 46  ? 55.222 -25.411 5.747   0.40 18.69 ?  46  GLY   B O    1 
ATOM   4582 O O    B GLY   B 1 46  ? 55.172 -25.226 5.465   0.60 19.42 ?  46  GLY   B O    1 
ATOM   4583 H H    A GLY   B 1 46  ? 52.374 -22.771 7.034   0.40 17.50 ?  46  GLY   B H    1 
ATOM   4584 H H    B GLY   B 1 46  ? 52.396 -22.745 7.078   0.60 17.51 ?  46  GLY   B H    1 
ATOM   4585 H HA2  A GLY   B 1 46  ? 54.960 -23.398 7.114   0.40 18.95 ?  46  GLY   B HA2  1 
ATOM   4586 H HA2  B GLY   B 1 46  ? 54.970 -23.405 7.103   0.60 19.12 ?  46  GLY   B HA2  1 
ATOM   4587 H HA3  A GLY   B 1 46  ? 53.819 -24.085 7.939   0.40 18.95 ?  46  GLY   B HA3  1 
ATOM   4588 H HA3  B GLY   B 1 46  ? 53.825 -24.128 7.895   0.60 19.12 ?  46  GLY   B HA3  1 
ATOM   4589 N N    . GLY   B 1 47  ? 52.981 -25.575 5.832   1.00 16.77 ?  47  GLY   B N    1 
ATOM   4590 C CA   . GLY   B 1 47  ? 52.934 -26.840 5.129   1.00 14.84 ?  47  GLY   B CA   1 
ATOM   4591 C C    . GLY   B 1 47  ? 52.009 -26.819 3.928   1.00 12.48 ?  47  GLY   B C    1 
ATOM   4592 O O    . GLY   B 1 47  ? 51.356 -25.816 3.635   1.00 12.72 ?  47  GLY   B O    1 
ATOM   4593 H H    A GLY   B 1 47  ? 52.206 -25.261 6.034   0.40 20.11 ?  47  GLY   B H    1 
ATOM   4594 H H    B GLY   B 1 47  ? 52.211 -25.299 6.100   0.60 20.11 ?  47  GLY   B H    1 
ATOM   4595 H HA2  . GLY   B 1 47  ? 53.823 -27.079 4.821   1.00 17.80 ?  47  GLY   B HA2  1 
ATOM   4596 H HA3  . GLY   B 1 47  ? 52.631 -27.534 5.740   1.00 17.80 ?  47  GLY   B HA3  1 
ATOM   4597 N N    . GLY   B 1 48  ? 51.964 -27.957 3.238   1.00 11.99 ?  48  GLY   B N    1 
ATOM   4598 C CA   . GLY   B 1 48  ? 51.038 -28.108 2.133   1.00 11.80 ?  48  GLY   B CA   1 
ATOM   4599 C C    . GLY   B 1 48  ? 51.176 -27.001 1.113   1.00 11.18 ?  48  GLY   B C    1 
ATOM   4600 O O    . GLY   B 1 48  ? 52.275 -26.536 0.803   1.00 11.88 ?  48  GLY   B O    1 
ATOM   4601 H H    . GLY   B 1 48  ? 52.463 -28.637 3.386   1.00 14.38 ?  48  GLY   B H    1 
ATOM   4602 H HA2  . GLY   B 1 48  ? 51.199 -28.957 1.692   1.00 14.16 ?  48  GLY   B HA2  1 
ATOM   4603 H HA3  . GLY   B 1 48  ? 50.129 -28.103 2.469   1.00 14.16 ?  48  GLY   B HA3  1 
ATOM   4604 N N    . VAL   B 1 49  ? 50.032 -26.567 0.583   1.00 11.10 ?  49  VAL   B N    1 
ATOM   4605 C CA   . VAL   B 1 49  ? 50.010 -25.541 -0.458  1.00 11.34 ?  49  VAL   B CA   1 
ATOM   4606 C C    . VAL   B 1 49  ? 50.665 -24.253 0.028   1.00 10.31 ?  49  VAL   B C    1 
ATOM   4607 O O    . VAL   B 1 49  ? 51.451 -23.630 -0.693  1.00 10.90 ?  49  VAL   B O    1 
ATOM   4608 C CB   . VAL   B 1 49  ? 48.563 -25.289 -0.927  1.00 12.46 ?  49  VAL   B CB   1 
ATOM   4609 C CG1  . VAL   B 1 49  ? 48.491 -24.055 -1.817  1.00 12.72 ?  49  VAL   B CG1  1 
ATOM   4610 C CG2  . VAL   B 1 49  ? 48.007 -26.514 -1.658  1.00 13.71 ?  49  VAL   B CG2  1 
ATOM   4611 H H    . VAL   B 1 49  ? 49.248 -26.847 0.812   1.00 13.31 ?  49  VAL   B H    1 
ATOM   4612 H HA   . VAL   B 1 49  ? 50.511 -25.860 -1.223  1.00 13.60 ?  49  VAL   B HA   1 
ATOM   4613 H HB   . VAL   B 1 49  ? 48.001 -25.129 -0.153  1.00 14.94 ?  49  VAL   B HB   1 
ATOM   4614 H HG11 . VAL   B 1 49  ? 47.661 -24.075 -2.319  1.00 15.26 ?  49  VAL   B HG11 1 
ATOM   4615 H HG12 . VAL   B 1 49  ? 48.517 -23.260 -1.259  1.00 15.26 ?  49  VAL   B HG12 1 
ATOM   4616 H HG13 . VAL   B 1 49  ? 49.244 -24.060 -2.426  1.00 15.26 ?  49  VAL   B HG13 1 
ATOM   4617 H HG21 . VAL   B 1 49  ? 47.095 -26.330 -1.942  1.00 16.44 ?  49  VAL   B HG21 1 
ATOM   4618 H HG22 . VAL   B 1 49  ? 48.560 -26.698 -2.435  1.00 16.44 ?  49  VAL   B HG22 1 
ATOM   4619 H HG23 . VAL   B 1 49  ? 48.018 -27.274 -1.058  1.00 16.44 ?  49  VAL   B HG23 1 
ATOM   4620 N N    . ALA   B 1 50  ? 50.322 -23.809 1.237   1.00 10.34 ?  50  ALA   B N    1 
ATOM   4621 C CA   . ALA   B 1 50  ? 50.839 -22.530 1.715   1.00 10.52 ?  50  ALA   B CA   1 
ATOM   4622 C C    . ALA   B 1 50  ? 52.358 -22.556 1.820   1.00 10.73 ?  50  ALA   B C    1 
ATOM   4623 O O    . ALA   B 1 50  ? 53.036 -21.587 1.453   1.00 10.51 ?  50  ALA   B O    1 
ATOM   4624 C CB   . ALA   B 1 50  ? 50.212 -22.175 3.060   1.00 10.65 ?  50  ALA   B CB   1 
ATOM   4625 H H    . ALA   B 1 50  ? 49.801 -24.217 1.786   1.00 12.40 ?  50  ALA   B H    1 
ATOM   4626 H HA   . ALA   B 1 50  ? 50.603 -21.835 1.085   1.00 12.61 ?  50  ALA   B HA   1 
ATOM   4627 H HB1  . ALA   B 1 50  ? 50.564 -21.323 3.363   1.00 12.77 ?  50  ALA   B HB1  1 
ATOM   4628 H HB2  . ALA   B 1 50  ? 49.246 -22.110 2.951   1.00 12.77 ?  50  ALA   B HB2  1 
ATOM   4629 H HB3  . ALA   B 1 50  ? 50.422 -22.869 3.704   1.00 12.77 ?  50  ALA   B HB3  1 
ATOM   4630 N N    . GLY   B 1 51  ? 52.909 -23.647 2.343   1.00 10.98 ?  51  GLY   B N    1 
ATOM   4631 C CA   . GLY   B 1 51  ? 54.354 -23.754 2.416   1.00 11.60 ?  51  GLY   B CA   1 
ATOM   4632 C C    . GLY   B 1 51  ? 55.005 -23.702 1.049   1.00 11.58 ?  51  GLY   B C    1 
ATOM   4633 O O    . GLY   B 1 51  ? 56.047 -23.064 0.871   1.00 12.34 ?  51  GLY   B O    1 
ATOM   4634 H H    . GLY   B 1 51  ? 52.481 -24.328 2.651   1.00 13.16 ?  51  GLY   B H    1 
ATOM   4635 H HA2  . GLY   B 1 51  ? 54.707 -23.022 2.950   1.00 13.92 ?  51  GLY   B HA2  1 
ATOM   4636 H HA3  . GLY   B 1 51  ? 54.600 -24.589 2.845   1.00 13.92 ?  51  GLY   B HA3  1 
ATOM   4637 N N    . ALA   B 1 52  ? 54.402 -24.367 0.064   1.00 11.32 ?  52  ALA   B N    1 
ATOM   4638 C CA   . ALA   B 1 52  ? 54.958 -24.373 -1.283  1.00 11.51 ?  52  ALA   B CA   1 
ATOM   4639 C C    . ALA   B 1 52  ? 54.875 -22.994 -1.934  1.00 10.94 ?  52  ALA   B C    1 
ATOM   4640 O O    . ALA   B 1 52  ? 55.842 -22.540 -2.563  1.00 11.53 ?  52  ALA   B O    1 
ATOM   4641 C CB   . ALA   B 1 52  ? 54.253 -25.424 -2.136  1.00 12.04 ?  52  ALA   B CB   1 
ATOM   4642 H H    . ALA   B 1 52  ? 53.675 -24.820 0.154   1.00 13.58 ?  52  ALA   B H    1 
ATOM   4643 H HA   . ALA   B 1 52  ? 55.893 -24.617 -1.228  1.00 13.80 ?  52  ALA   B HA   1 
ATOM   4644 H HB1  . ALA   B 1 52  ? 54.637 -25.414 -3.027  1.00 14.44 ?  52  ALA   B HB1  1 
ATOM   4645 H HB2  . ALA   B 1 52  ? 54.385 -26.298 -1.732  1.00 14.44 ?  52  ALA   B HB2  1 
ATOM   4646 H HB3  . ALA   B 1 52  ? 53.308 -25.218 -2.179  1.00 14.44 ?  52  ALA   B HB3  1 
ATOM   4647 N N    . LEU   B 1 53  ? 53.731 -22.317 -1.810  1.00 10.43 ?  53  LEU   B N    1 
ATOM   4648 C CA   . LEU   B 1 53  ? 53.619 -20.979 -2.377  1.00 10.73 ?  53  LEU   B CA   1 
ATOM   4649 C C    . LEU   B 1 53  ? 54.625 -20.037 -1.730  1.00 10.69 ?  53  LEU   B C    1 
ATOM   4650 O O    . LEU   B 1 53  ? 55.323 -19.283 -2.416  1.00 11.18 ?  53  LEU   B O    1 
ATOM   4651 C CB   . LEU   B 1 53  ? 52.195 -20.443 -2.205  1.00 11.11 ?  53  LEU   B CB   1 
ATOM   4652 C CG   . LEU   B 1 53  ? 51.065 -21.169 -2.948  1.00 11.81 ?  53  LEU   B CG   1 
ATOM   4653 C CD1  . LEU   B 1 53  ? 49.719 -20.568 -2.583  1.00 13.11 ?  53  LEU   B CD1  1 
ATOM   4654 C CD2  . LEU   B 1 53  ? 51.261 -21.129 -4.456  1.00 13.50 ?  53  LEU   B CD2  1 
ATOM   4655 H H    . LEU   B 1 53  ? 53.025 -22.600 -1.408  1.00 12.51 ?  53  LEU   B H    1 
ATOM   4656 H HA   . LEU   B 1 53  ? 53.815 -21.019 -3.327  1.00 12.87 ?  53  LEU   B HA   1 
ATOM   4657 H HB2  . LEU   B 1 53  ? 51.975 -20.471 -1.263  1.00 13.33 ?  53  LEU   B HB2  1 
ATOM   4658 H HB3  . LEU   B 1 53  ? 52.181 -19.522 -2.508  1.00 13.33 ?  53  LEU   B HB3  1 
ATOM   4659 H HG   . LEU   B 1 53  ? 51.051 -22.097 -2.672  1.00 14.16 ?  53  LEU   B HG   1 
ATOM   4660 H HD11 . LEU   B 1 53  ? 49.016 -21.042 -3.058  1.00 15.72 ?  53  LEU   B HD11 1 
ATOM   4661 H HD12 . LEU   B 1 53  ? 49.580 -20.655 -1.623  1.00 15.72 ?  53  LEU   B HD12 1 
ATOM   4662 H HD13 . LEU   B 1 53  ? 49.708 -19.630 -2.831  1.00 15.72 ?  53  LEU   B HD13 1 
ATOM   4663 H HD21 . LEU   B 1 53  ? 50.588 -21.684 -4.877  1.00 16.20 ?  53  LEU   B HD21 1 
ATOM   4664 H HD22 . LEU   B 1 53  ? 51.169 -20.213 -4.763  1.00 16.20 ?  53  LEU   B HD22 1 
ATOM   4665 H HD23 . LEU   B 1 53  ? 52.145 -21.465 -4.671  1.00 16.20 ?  53  LEU   B HD23 1 
ATOM   4666 N N    . ASN   B 1 54  ? 54.714 -20.066 -0.403  1.00 10.41 ?  54  ASN   B N    1 
ATOM   4667 C CA   . ASN   B 1 54  ? 55.626 -19.155 0.269   1.00 11.16 ?  54  ASN   B CA   1 
ATOM   4668 C C    . ASN   B 1 54  ? 57.070 -19.430 -0.132  1.00 11.84 ?  54  ASN   B C    1 
ATOM   4669 O O    . ASN   B 1 54  ? 57.844 -18.493 -0.368  1.00 11.77 ?  54  ASN   B O    1 
ATOM   4670 C CB   . ASN   B 1 54  ? 55.472 -19.243 1.779   1.00 12.16 ?  54  ASN   B CB   1 
ATOM   4671 C CG   . ASN   B 1 54  ? 56.446 -18.331 2.491   1.00 12.37 ?  54  ASN   B CG   1 
ATOM   4672 O OD1  . ASN   B 1 54  ? 56.461 -17.117 2.254   1.00 12.14 ?  54  ASN   B OD1  1 
ATOM   4673 N ND2  . ASN   B 1 54  ? 57.295 -18.907 3.331   1.00 13.64 ?  54  ASN   B ND2  1 
ATOM   4674 H H    . ASN   B 1 54  ? 54.271 -20.588 0.112   1.00 12.49 ?  54  ASN   B H    1 
ATOM   4675 H HA   . ASN   B 1 54  ? 55.415 -18.248 -0.000  1.00 13.38 ?  54  ASN   B HA   1 
ATOM   4676 H HB2  . ASN   B 1 54  ? 54.573 -18.974 2.022   1.00 14.59 ?  54  ASN   B HB2  1 
ATOM   4677 H HB3  . ASN   B 1 54  ? 55.643 -20.151 2.065   1.00 14.59 ?  54  ASN   B HB3  1 
ATOM   4678 H HD21 . ASN   B 1 54  ? 57.876 -18.432 3.754   1.00 16.35 ?  54  ASN   B HD21 1 
ATOM   4679 H HD22 . ASN   B 1 54  ? 57.267 -19.759 3.457   1.00 16.35 ?  54  ASN   B HD22 1 
ATOM   4680 N N    . LYS   B 1 55  ? 57.459 -20.707 -0.198  1.00 12.12 ?  55  LYS   B N    1 
ATOM   4681 C CA   . LYS   B 1 55  ? 58.815 -21.046 -0.618  1.00 13.28 ?  55  LYS   B CA   1 
ATOM   4682 C C    . LYS   B 1 55  ? 59.112 -20.503 -2.009  1.00 12.88 ?  55  LYS   B C    1 
ATOM   4683 O O    . LYS   B 1 55  ? 60.210 -19.995 -2.262  1.00 13.16 ?  55  LYS   B O    1 
ATOM   4684 C CB   . LYS   B 1 55  ? 59.004 -22.564 -0.572  1.00 14.69 ?  55  LYS   B CB   1 
ATOM   4685 C CG   . LYS   B 1 55  ? 60.372 -23.039 -1.027  1.00 18.31 ?  55  LYS   B CG   1 
ATOM   4686 C CD   . LYS   B 1 55  ? 60.536 -24.535 -0.823  1.00 21.40 ?  55  LYS   B CD   1 
ATOM   4687 C CE   . LYS   B 1 55  ? 60.639 -24.894 0.656   1.00 24.18 ?  55  LYS   B CE   1 
ATOM   4688 N NZ   . LYS   B 1 55  ? 61.010 -26.314 0.861   1.00 25.68 ?  55  LYS   B NZ   1 
ATOM   4689 H H    . LYS   B 1 55  ? 56.959 -21.382 -0.013  1.00 14.54 ?  55  LYS   B H    1 
ATOM   4690 H HA   . LYS   B 1 55  ? 59.443 -20.645 0.002   1.00 15.92 ?  55  LYS   B HA   1 
ATOM   4691 H HB2  . LYS   B 1 55  ? 58.874 -22.857 0.344   1.00 17.63 ?  55  LYS   B HB2  1 
ATOM   4692 H HB3  . LYS   B 1 55  ? 58.341 -22.976 -1.145  1.00 17.63 ?  55  LYS   B HB3  1 
ATOM   4693 H HG2  . LYS   B 1 55  ? 60.480 -22.850 -1.972  1.00 21.97 ?  55  LYS   B HG2  1 
ATOM   4694 H HG3  . LYS   B 1 55  ? 61.058 -22.584 -0.513  1.00 21.97 ?  55  LYS   B HG3  1 
ATOM   4695 H HD2  . LYS   B 1 55  ? 59.768 -24.999 -1.192  1.00 25.67 ?  55  LYS   B HD2  1 
ATOM   4696 H HD3  . LYS   B 1 55  ? 61.350 -24.834 -1.261  1.00 25.67 ?  55  LYS   B HD3  1 
ATOM   4697 H HE2  . LYS   B 1 55  ? 61.317 -24.333 1.069   1.00 29.01 ?  55  LYS   B HE2  1 
ATOM   4698 H HE3  . LYS   B 1 55  ? 59.778 -24.738 1.080   1.00 29.01 ?  55  LYS   B HE3  1 
ATOM   4699 H HZ1  . LYS   B 1 55  ? 61.025 -26.500 1.731   1.00 30.80 ?  55  LYS   B HZ1  1 
ATOM   4700 H HZ2  . LYS   B 1 55  ? 60.415 -26.841 0.461   1.00 30.80 ?  55  LYS   B HZ2  1 
ATOM   4701 H HZ3  . LYS   B 1 55  ? 61.814 -26.469 0.516   1.00 30.80 ?  55  LYS   B HZ3  1 
ATOM   4702 N N    . ALA   B 1 56  ? 58.142 -20.592 -2.924  1.00 12.53 ?  56  ALA   B N    1 
ATOM   4703 C CA   . ALA   B 1 56  ? 58.360 -20.084 -4.274  1.00 13.18 ?  56  ALA   B CA   1 
ATOM   4704 C C    . ALA   B 1 56  ? 58.634 -18.588 -4.269  1.00 12.92 ?  56  ALA   B C    1 
ATOM   4705 O O    . ALA   B 1 56  ? 59.358 -18.085 -5.142  1.00 13.74 ?  56  ALA   B O    1 
ATOM   4706 C CB   . ALA   B 1 56  ? 57.167 -20.424 -5.168  1.00 13.91 ?  56  ALA   B CB   1 
ATOM   4707 H H    . ALA   B 1 56  ? 57.360 -20.931 -2.788  1.00 15.03 ?  56  ALA   B H    1 
ATOM   4708 H HA   . ALA   B 1 56  ? 59.140 -20.518 -4.645  1.00 15.81 ?  56  ALA   B HA   1 
ATOM   4709 H HB1  . ALA   B 1 56  ? 57.337 -20.085 -6.065  1.00 16.68 ?  56  ALA   B HB1  1 
ATOM   4710 H HB2  . ALA   B 1 56  ? 57.061 -21.389 -5.199  1.00 16.68 ?  56  ALA   B HB2  1 
ATOM   4711 H HB3  . ALA   B 1 56  ? 56.368 -20.014 -4.807  1.00 16.68 ?  56  ALA   B HB3  1 
ATOM   4712 N N    . THR   B 1 57  ? 58.071 -17.862 -3.300  1.00 12.61 ?  57  THR   B N    1 
ATOM   4713 C CA   . THR   B 1 57  ? 58.299 -16.427 -3.177  1.00 12.78 ?  57  THR   B CA   1 
ATOM   4714 C C    . THR   B 1 57  ? 59.550 -16.097 -2.371  1.00 13.56 ?  57  THR   B C    1 
ATOM   4715 O O    . THR   B 1 57  ? 59.785 -14.920 -2.068  1.00 13.92 ?  57  THR   B O    1 
ATOM   4716 C CB   . THR   B 1 57  ? 57.099 -15.706 -2.539  1.00 12.10 ?  57  THR   B CB   1 
ATOM   4717 O OG1  . THR   B 1 57  ? 57.081 -15.924 -1.121  1.00 12.20 ?  57  THR   B OG1  1 
ATOM   4718 C CG2  . THR   B 1 57  ? 55.788 -16.131 -3.163  1.00 12.14 ?  57  THR   B CG2  1 
ATOM   4719 H H    . THR   B 1 57  ? 57.538 -18.182 -2.699  1.00 15.12 ?  57  THR   B H    1 
ATOM   4720 H HA   . THR   B 1 57  ? 58.414 -16.061 -4.067  1.00 15.33 ?  57  THR   B HA   1 
ATOM   4721 H HB   . THR   B 1 57  ? 57.195 -14.755 -2.699  1.00 14.52 ?  57  THR   B HB   1 
ATOM   4722 H HG1  . THR   B 1 57  ? 57.016 -16.748 -0.958  1.00 14.63 ?  57  THR   B HG1  1 
ATOM   4723 H HG21 . THR   B 1 57  ? 55.065 -15.576 -2.835  1.00 14.57 ?  57  THR   B HG21 1 
ATOM   4724 H HG22 . THR   B 1 57  ? 55.836 -16.056 -4.127  1.00 14.57 ?  57  THR   B HG22 1 
ATOM   4725 H HG23 . THR   B 1 57  ? 55.596 -17.058 -2.934  1.00 14.57 ?  57  THR   B HG23 1 
ATOM   4726 N N    . ASN   B 1 58  ? 60.350 -17.100 -2.012  1.00 14.23 ?  58  ASN   B N    1 
ATOM   4727 C CA   . ASN   B 1 58  ? 61.548 -16.887 -1.205  1.00 16.48 ?  58  ASN   B CA   1 
ATOM   4728 C C    . ASN   B 1 58  ? 61.210 -16.173 0.104   1.00 14.96 ?  58  ASN   B C    1 
ATOM   4729 O O    . ASN   B 1 58  ? 61.949 -15.299 0.567   1.00 15.65 ?  58  ASN   B O    1 
ATOM   4730 C CB   . ASN   B 1 58  ? 62.637 -16.147 -1.988  1.00 21.43 ?  58  ASN   B CB   1 
ATOM   4731 C CG   . ASN   B 1 58  ? 63.998 -16.251 -1.329  1.00 29.10 ?  58  ASN   B CG   1 
ATOM   4732 O OD1  . ASN   B 1 58  ? 64.324 -17.264 -0.712  1.00 30.95 ?  58  ASN   B OD1  1 
ATOM   4733 N ND2  . ASN   B 1 58  ? 64.799 -15.199 -1.453  1.00 34.25 ?  58  ASN   B ND2  1 
ATOM   4734 H H    . ASN   B 1 58  ? 60.216 -17.927 -2.225  1.00 17.07 ?  58  ASN   B H    1 
ATOM   4735 H HA   . ASN   B 1 58  ? 61.908 -17.757 -0.975  1.00 19.77 ?  58  ASN   B HA   1 
ATOM   4736 H HB2  . ASN   B 1 58  ? 62.703 -16.530 -2.880  1.00 25.71 ?  58  ASN   B HB2  1 
ATOM   4737 H HB3  . ASN   B 1 58  ? 62.406 -15.209 -2.047  1.00 25.71 ?  58  ASN   B HB3  1 
ATOM   4738 H HD21 . ASN   B 1 58  ? 65.583 -15.210 -1.098  1.00 41.09 ?  58  ASN   B HD21 1 
ATOM   4739 H HD22 . ASN   B 1 58  ? 64.534 -14.508 -1.888  1.00 41.09 ?  58  ASN   B HD22 1 
ATOM   4740 N N    . ASN   B 1 59  ? 60.081 -16.556 0.709   1.00 14.06 ?  59  ASN   B N    1 
ATOM   4741 C CA   . ASN   B 1 59  ? 59.603 -16.088 2.014   1.00 13.75 ?  59  ASN   B CA   1 
ATOM   4742 C C    . ASN   B 1 59  ? 59.004 -14.684 1.962   1.00 13.12 ?  59  ASN   B C    1 
ATOM   4743 O O    . ASN   B 1 59  ? 58.574 -14.179 3.007   1.00 13.41 ?  59  ASN   B O    1 
ATOM   4744 C CB   . ASN   B 1 59  ? 60.675 -16.148 3.117   1.00 14.81 ?  59  ASN   B CB   1 
ATOM   4745 C CG   . ASN   B 1 59  ? 60.086 -16.326 4.501   1.00 15.97 ?  59  ASN   B CG   1 
ATOM   4746 O OD1  . ASN   B 1 59  ? 59.265 -17.217 4.728   1.00 16.22 ?  59  ASN   B OD1  1 
ATOM   4747 N ND2  . ASN   B 1 59  ? 60.502 -15.478 5.438   1.00 16.76 ?  59  ASN   B ND2  1 
ATOM   4748 H H    . ASN   B 1 59  ? 59.540 -17.131 0.360   1.00 16.86 ?  59  ASN   B H    1 
ATOM   4749 H HA   . ASN   B 1 59  ? 58.896 -16.687 2.295   1.00 16.49 ?  59  ASN   B HA   1 
ATOM   4750 H HB2  . ASN   B 1 59  ? 61.268 -16.900 2.954   1.00 17.77 ?  59  ASN   B HB2  1 
ATOM   4751 H HB3  . ASN   B 1 59  ? 61.182 -15.322 3.120   1.00 17.77 ?  59  ASN   B HB3  1 
ATOM   4752 H HD21 . ASN   B 1 59  ? 60.198 -15.536 6.243   1.00 20.10 ?  59  ASN   B HD21 1 
ATOM   4753 H HD22 . ASN   B 1 59  ? 61.077 -14.869 5.243   1.00 20.10 ?  59  ASN   B HD22 1 
ATOM   4754 N N    . ALA   B 1 60  ? 58.939 -14.041 0.792   1.00 12.85 ?  60  ALA   B N    1 
ATOM   4755 C CA   . ALA   B 1 60  ? 58.347 -12.708 0.722   1.00 13.09 ?  60  ALA   B CA   1 
ATOM   4756 C C    . ALA   B 1 60  ? 56.878 -12.737 1.121   1.00 12.25 ?  60  ALA   B C    1 
ATOM   4757 O O    . ALA   B 1 60  ? 56.374 -11.787 1.735   1.00 12.51 ?  60  ALA   B O    1 
ATOM   4758 C CB   . ALA   B 1 60  ? 58.517 -12.129 -0.683  1.00 14.23 ?  60  ALA   B CB   1 
ATOM   4759 H H    . ALA   B 1 60  ? 59.226 -14.357 0.044   1.00 15.41 ?  60  ALA   B H    1 
ATOM   4760 H HA   . ALA   B 1 60  ? 58.810 -12.132 1.345   1.00 15.71 ?  60  ALA   B HA   1 
ATOM   4761 H HB1  . ALA   B 1 60  ? 58.120 -11.247 -0.706  1.00 17.07 ?  60  ALA   B HB1  1 
ATOM   4762 H HB2  . ALA   B 1 60  ? 59.465 -12.073 -0.887  1.00 17.07 ?  60  ALA   B HB2  1 
ATOM   4763 H HB3  . ALA   B 1 60  ? 58.077 -12.712 -1.321  1.00 17.07 ?  60  ALA   B HB3  1 
ATOM   4764 N N    . MET   B 1 61  ? 56.170 -13.815 0.774   1.00 11.80 ?  61  MET   B N    1 
ATOM   4765 C CA   . MET   B 1 61  ? 54.774 -13.937 1.173   1.00 11.49 ?  61  MET   B CA   1 
ATOM   4766 C C    . MET   B 1 61  ? 54.636 -13.950 2.696   1.00 11.49 ?  61  MET   B C    1 
ATOM   4767 O O    . MET   B 1 61  ? 53.737 -13.306 3.250   1.00 11.40 ?  61  MET   B O    1 
ATOM   4768 C CB   . MET   B 1 61  ? 54.191 -15.204 0.544   1.00 11.54 ?  61  MET   B CB   1 
ATOM   4769 C CG   . MET   B 1 61  ? 52.751 -15.502 0.951   1.00 11.27 ?  61  MET   B CG   1 
ATOM   4770 S SD   . MET   B 1 61  ? 52.118 -17.004 0.172   1.00 11.66 ?  61  MET   B SD   1 
ATOM   4771 C CE   . MET   B 1 61  ? 51.855 -16.400 -1.497  1.00 12.76 ?  61  MET   B CE   1 
ATOM   4772 H H    . MET   B 1 61  ? 56.473 -14.483 0.316   1.00 14.15 ?  61  MET   B H    1 
ATOM   4773 H HA   . MET   B 1 61  ? 54.282 -13.184 0.816   1.00 13.78 ?  61  MET   B HA   1 
ATOM   4774 H HB2  . MET   B 1 61  ? 54.207 -15.112 -0.423  1.00 13.84 ?  61  MET   B HB2  1 
ATOM   4775 H HB3  . MET   B 1 61  ? 54.733 -15.964 0.807   1.00 13.84 ?  61  MET   B HB3  1 
ATOM   4776 H HG2  . MET   B 1 61  ? 52.706 -15.626 1.915   1.00 13.51 ?  61  MET   B HG2  1 
ATOM   4777 H HG3  . MET   B 1 61  ? 52.182 -14.760 0.688   1.00 13.51 ?  61  MET   B HG3  1 
ATOM   4778 H HE1  . MET   B 1 61  ? 51.475 -17.112 -2.035  1.00 15.31 ?  61  MET   B HE1  1 
ATOM   4779 H HE2  . MET   B 1 61  ? 51.239 -15.646 -1.470  1.00 15.31 ?  61  MET   B HE2  1 
ATOM   4780 H HE3  . MET   B 1 61  ? 52.702 -16.116 -1.872  1.00 15.31 ?  61  MET   B HE3  1 
ATOM   4781 N N    . GLN   B 1 62  ? 55.519 -14.672 3.393   1.00 11.50 ?  62  GLN   B N    1 
ATOM   4782 C CA   . GLN   B 1 62  ? 55.414 -14.737 4.849   1.00 11.89 ?  62  GLN   B CA   1 
ATOM   4783 C C    . GLN   B 1 62  ? 55.694 -13.382 5.489   1.00 11.83 ?  62  GLN   B C    1 
ATOM   4784 O O    . GLN   B 1 62  ? 55.008 -12.982 6.436   1.00 12.42 ?  62  GLN   B O    1 
ATOM   4785 C CB   . GLN   B 1 62  ? 56.365 -15.796 5.410   1.00 12.20 ?  62  GLN   B CB   1 
ATOM   4786 C CG   . GLN   B 1 62  ? 56.148 -16.064 6.889   1.00 12.41 ?  62  GLN   B CG   1 
ATOM   4787 C CD   . GLN   B 1 62  ? 54.775 -16.650 7.137   1.00 11.93 ?  62  GLN   B CD   1 
ATOM   4788 O OE1  . GLN   B 1 62  ? 54.517 -17.799 6.784   1.00 12.35 ?  62  GLN   B OE1  1 
ATOM   4789 N NE2  . GLN   B 1 62  ? 53.866 -15.849 7.691   1.00 11.97 ?  62  GLN   B NE2  1 
ATOM   4790 H H    . GLN   B 1 62  ? 56.166 -15.126 3.052   1.00 13.80 ?  62  GLN   B H    1 
ATOM   4791 H HA   . GLN   B 1 62  ? 54.506 -14.994 5.079   1.00 14.26 ?  62  GLN   B HA   1 
ATOM   4792 H HB2  . GLN   B 1 62  ? 56.232 -16.630 4.931   1.00 14.63 ?  62  GLN   B HB2  1 
ATOM   4793 H HB3  . GLN   B 1 62  ? 57.280 -15.491 5.290   1.00 14.63 ?  62  GLN   B HB3  1 
ATOM   4794 H HG2  . GLN   B 1 62  ? 56.811 -16.700 7.196   1.00 14.88 ?  62  GLN   B HG2  1 
ATOM   4795 H HG3  . GLN   B 1 62  ? 56.224 -15.232 7.381   1.00 14.88 ?  62  GLN   B HG3  1 
ATOM   4796 H HE21 . GLN   B 1 62  ? 54.078 -15.042 7.907   1.00 14.35 ?  62  GLN   B HE21 1 
ATOM   4797 H HE22 . GLN   B 1 62  ? 53.070 -16.137 7.837   1.00 14.35 ?  62  GLN   B HE22 1 
ATOM   4798 N N    . VAL   B 1 63  ? 56.710 -12.667 5.000   1.00 12.66 ?  63  VAL   B N    1 
ATOM   4799 C CA   . VAL   B 1 63  ? 57.015 -11.352 5.556   1.00 13.30 ?  63  VAL   B CA   1 
ATOM   4800 C C    . VAL   B 1 63  ? 55.823 -10.417 5.378   1.00 12.76 ?  63  VAL   B C    1 
ATOM   4801 O O    . VAL   B 1 63  ? 55.410 -9.714  6.310   1.00 13.33 ?  63  VAL   B O    1 
ATOM   4802 C CB   . VAL   B 1 63  ? 58.304 -10.792 4.931   1.00 14.73 ?  63  VAL   B CB   1 
ATOM   4803 C CG1  . VAL   B 1 63  ? 58.527 -9.357  5.376   1.00 15.54 ?  63  VAL   B CG1  1 
ATOM   4804 C CG2  . VAL   B 1 63  ? 59.491 -11.665 5.331   1.00 15.37 ?  63  VAL   B CG2  1 
ATOM   4805 H H    . VAL   B 1 63  ? 57.222 -12.917 4.350   1.00 15.19 ?  63  VAL   B H    1 
ATOM   4806 H HA   . VAL   B 1 63  ? 57.171 -11.454 6.505   1.00 15.96 ?  63  VAL   B HA   1 
ATOM   4807 H HB   . VAL   B 1 63  ? 58.234 -10.810 3.965   1.00 17.66 ?  63  VAL   B HB   1 
ATOM   4808 H HG11 . VAL   B 1 63  ? 59.446 -9.111  5.193   1.00 18.64 ?  63  VAL   B HG11 1 
ATOM   4809 H HG12 . VAL   B 1 63  ? 57.924 -8.779  4.887   1.00 18.64 ?  63  VAL   B HG12 1 
ATOM   4810 H HG13 . VAL   B 1 63  ? 58.352 -9.295  6.329   1.00 18.64 ?  63  VAL   B HG13 1 
ATOM   4811 H HG21 . VAL   B 1 63  ? 60.302 -11.292 4.949   1.00 18.44 ?  63  VAL   B HG21 1 
ATOM   4812 H HG22 . VAL   B 1 63  ? 59.561 -11.678 6.301   1.00 18.44 ?  63  VAL   B HG22 1 
ATOM   4813 H HG23 . VAL   B 1 63  ? 59.353 -12.565 4.999   1.00 18.44 ?  63  VAL   B HG23 1 
ATOM   4814 N N    . GLU   B 1 64  ? 55.249 -10.403 4.172   1.00 12.48 ?  64  GLU   B N    1 
ATOM   4815 C CA   . GLU   B 1 64  ? 54.084 -9.566  3.900   1.00 12.15 ?  64  GLU   B CA   1 
ATOM   4816 C C    . GLU   B 1 64  ? 52.904 -9.967  4.779   1.00 11.61 ?  64  GLU   B C    1 
ATOM   4817 O O    . GLU   B 1 64  ? 52.169 -9.107  5.293   1.00 11.93 ?  64  GLU   B O    1 
ATOM   4818 C CB   . GLU   B 1 64  ? 53.720 -9.721  2.422   1.00 12.68 ?  64  GLU   B CB   1 
ATOM   4819 C CG   . GLU   B 1 64  ? 52.465 -8.979  1.985   1.00 12.97 ?  64  GLU   B CG   1 
ATOM   4820 C CD   . GLU   B 1 64  ? 51.926 -9.479  0.652   1.00 13.40 ?  64  GLU   B CD   1 
ATOM   4821 O OE1  . GLU   B 1 64  ? 52.112 -10.683 0.335   1.00 13.62 ?  64  GLU   B OE1  1 
ATOM   4822 O OE2  . GLU   B 1 64  ? 51.310 -8.662  -0.076  1.00 13.96 -1 64  GLU   B OE2  1 
ATOM   4823 H H    . GLU   B 1 64  ? 55.522 -10.864 3.494   1.00 14.97 ?  64  GLU   B H    1 
ATOM   4824 H HA   . GLU   B 1 64  ? 54.302 -8.637  4.069   1.00 14.57 ?  64  GLU   B HA   1 
ATOM   4825 H HB2  . GLU   B 1 64  ? 54.454 -9.387  1.881   1.00 15.21 ?  64  GLU   B HB2  1 
ATOM   4826 H HB3  . GLU   B 1 64  ? 53.580 -10.661 2.235   1.00 15.21 ?  64  GLU   B HB3  1 
ATOM   4827 H HG2  . GLU   B 1 64  ? 51.767 -9.095  2.650   1.00 15.56 ?  64  GLU   B HG2  1 
ATOM   4828 H HG3  . GLU   B 1 64  ? 52.676 -8.035  1.892   1.00 15.56 ?  64  GLU   B HG3  1 
ATOM   4829 N N    . SER   B 1 65  ? 52.715 -11.275 4.957   1.00 11.57 ?  65  SER   B N    1 
ATOM   4830 C CA   . SER   B 1 65  ? 51.611 -11.788 5.756   1.00 11.82 ?  65  SER   B CA   1 
ATOM   4831 C C    . SER   B 1 65  ? 51.747 -11.393 7.222   1.00 11.76 ?  65  SER   B C    1 
ATOM   4832 O O    . SER   B 1 65  ? 50.754 -11.018 7.861   1.00 12.22 ?  65  SER   B O    1 
ATOM   4833 C CB   . SER   B 1 65  ? 51.547 -13.306 5.618   1.00 11.79 ?  65  SER   B CB   1 
ATOM   4834 O OG   . SER   B 1 65  ? 51.191 -13.700 4.298   1.00 11.95 ?  65  SER   B OG   1 
ATOM   4835 H H    . SER   B 1 65  ? 53.216 -11.891 4.617   1.00 13.88 ?  65  SER   B H    1 
ATOM   4836 H HA   . SER   B 1 65  ? 50.777 -11.422 5.419   1.00 14.18 ?  65  SER   B HA   1 
ATOM   4837 H HB2  . SER   B 1 65  ? 52.409 -13.683 5.832   1.00 14.14 ?  65  SER   B HB2  1 
ATOM   4838 H HB3  . SER   B 1 65  ? 50.873 -13.648 6.233   1.00 14.14 ?  65  SER   B HB3  1 
ATOM   4839 H HG   . SER   B 1 65  ? 51.758 -13.408 3.747   1.00 14.34 ?  65  SER   B HG   1 
ATOM   4840 N N    . ASP   B 1 66  ? 52.957 -11.495 7.784   1.00 12.09 ?  66  ASP   B N    1 
ATOM   4841 C CA   . ASP   B 1 66  ? 53.150 -11.109 9.180   1.00 12.35 ?  66  ASP   B CA   1 
ATOM   4842 C C    . ASP   B 1 66  ? 52.840 -9.632  9.386   1.00 12.71 ?  66  ASP   B C    1 
ATOM   4843 O O    . ASP   B 1 66  ? 52.265 -9.247  10.412  1.00 12.97 ?  66  ASP   B O    1 
ATOM   4844 C CB   . ASP   B 1 66  ? 54.578 -11.424 9.633   1.00 13.50 ?  66  ASP   B CB   1 
ATOM   4845 C CG   . ASP   B 1 66  ? 54.842 -12.916 9.785   1.00 15.20 ?  66  ASP   B CG   1 
ATOM   4846 O OD1  . ASP   B 1 66  ? 53.890 -13.724 9.723   1.00 16.37 ?  66  ASP   B OD1  1 
ATOM   4847 O OD2  . ASP   B 1 66  ? 56.020 -13.283 9.980   1.00 18.25 -1 66  ASP   B OD2  1 
ATOM   4848 H H    . ASP   B 1 66  ? 53.661 -11.790 7.390   1.00 14.50 ?  66  ASP   B H    1 
ATOM   4849 H HA   . ASP   B 1 66  ? 52.543 -11.616 9.738   1.00 14.81 ?  66  ASP   B HA   1 
ATOM   4850 H HB2  . ASP   B 1 66  ? 55.203 -11.079 8.979   1.00 16.19 ?  66  ASP   B HB2  1 
ATOM   4851 H HB3  . ASP   B 1 66  ? 54.736 -11.004 10.496  1.00 16.19 ?  66  ASP   B HB3  1 
ATOM   4852 N N    . ASP   B 1 67  ? 53.218 -8.785  8.424   1.00 12.27 ?  67  ASP   B N    1 
ATOM   4853 C CA   . ASP   B 1 67  ? 52.870 -7.375  8.519   1.00 12.94 ?  67  ASP   B CA   1 
ATOM   4854 C C    . ASP   B 1 67  ? 51.358 -7.174  8.442   1.00 13.17 ?  67  ASP   B C    1 
ATOM   4855 O O    . ASP   B 1 67  ? 50.795 -6.370  9.194   1.00 13.72 ?  67  ASP   B O    1 
ATOM   4856 C CB   . ASP   B 1 67  ? 53.581 -6.590  7.426   1.00 14.42 ?  67  ASP   B CB   1 
ATOM   4857 C CG   . ASP   B 1 67  ? 53.147 -5.147  7.395   1.00 15.76 ?  67  ASP   B CG   1 
ATOM   4858 O OD1  . ASP   B 1 67  ? 53.625 -4.342  8.225   1.00 16.79 ?  67  ASP   B OD1  1 
ATOM   4859 O OD2  . ASP   B 1 67  ? 52.285 -4.841  6.558   1.00 16.57 -1 67  ASP   B OD2  1 
ATOM   4860 H H    . ASP   B 1 67  ? 53.681 -8.998  7.728   1.00 14.72 ?  67  ASP   B H    1 
ATOM   4861 H HA   . ASP   B 1 67  ? 53.172 -7.033  9.373   1.00 15.52 ?  67  ASP   B HA   1 
ATOM   4862 H HB2  . ASP   B 1 67  ? 54.538 -6.612  7.588   1.00 17.30 ?  67  ASP   B HB2  1 
ATOM   4863 H HB3  . ASP   B 1 67  ? 53.386 -6.996  6.562   1.00 17.30 ?  67  ASP   B HB3  1 
ATOM   4864 N N    . TYR   B 1 68  ? 50.680 -7.909  7.555   1.00 12.70 ?  68  TYR   B N    1 
ATOM   4865 C CA   . TYR   B 1 68  ? 49.224 -7.820  7.482   1.00 13.78 ?  68  TYR   B CA   1 
ATOM   4866 C C    . TYR   B 1 68  ? 48.585 -8.162  8.824   1.00 13.15 ?  68  TYR   B C    1 
ATOM   4867 O O    . TYR   B 1 68  ? 47.659 -7.474  9.273   1.00 13.77 ?  68  TYR   B O    1 
ATOM   4868 C CB   . TYR   B 1 68  ? 48.685 -8.737  6.376   1.00 14.42 ?  68  TYR   B CB   1 
ATOM   4869 C CG   . TYR   B 1 68  ? 47.181 -8.891  6.435   1.00 15.18 ?  68  TYR   B CG   1 
ATOM   4870 C CD1  . TYR   B 1 68  ? 46.595 -9.849  7.260   1.00 16.13 ?  68  TYR   B CD1  1 
ATOM   4871 C CD2  . TYR   B 1 68  ? 46.350 -8.061  5.709   1.00 16.10 ?  68  TYR   B CD2  1 
ATOM   4872 C CE1  . TYR   B 1 68  ? 45.231 -9.974  7.354   1.00 17.10 ?  68  TYR   B CE1  1 
ATOM   4873 C CE2  . TYR   B 1 68  ? 44.970 -8.190  5.786   1.00 16.61 ?  68  TYR   B CE2  1 
ATOM   4874 C CZ   . TYR   B 1 68  ? 44.430 -9.143  6.613   1.00 16.87 ?  68  TYR   B CZ   1 
ATOM   4875 O OH   . TYR   B 1 68  ? 43.068 -9.262  6.704   1.00 18.11 ?  68  TYR   B OH   1 
ATOM   4876 H H    . TYR   B 1 68  ? 51.034 -8.465  6.999   1.00 15.23 ?  68  TYR   B H    1 
ATOM   4877 H HA   . TYR   B 1 68  ? 48.979 -6.913  7.263   1.00 16.52 ?  68  TYR   B HA   1 
ATOM   4878 H HB2  . TYR   B 1 68  ? 48.908 -8.357  5.515   1.00 17.29 ?  68  TYR   B HB2  1 
ATOM   4879 H HB3  . TYR   B 1 68  ? 49.078 -9.617  6.469   1.00 17.29 ?  68  TYR   B HB3  1 
ATOM   4880 H HD1  . TYR   B 1 68  ? 47.137 -10.414 7.767   1.00 19.35 ?  68  TYR   B HD1  1 
ATOM   4881 H HD2  . TYR   B 1 68  ? 46.718 -7.409  5.164   1.00 19.32 ?  68  TYR   B HD2  1 
ATOM   4882 H HE1  . TYR   B 1 68  ? 44.851 -10.630 7.902   1.00 20.51 ?  68  TYR   B HE1  1 
ATOM   4883 H HE2  . TYR   B 1 68  ? 44.414 -7.627  5.299   1.00 19.92 ?  68  TYR   B HE2  1 
ATOM   4884 H HH   . TYR   B 1 68  ? 42.681 -8.705  6.199   1.00 21.73 ?  68  TYR   B HH   1 
ATOM   4885 N N    . ILE   B 1 69  ? 49.058 -9.235  9.469   1.00 12.86 ?  69  ILE   B N    1 
ATOM   4886 C CA   . ILE   B 1 69  ? 48.500 -9.667  10.748  1.00 13.56 ?  69  ILE   B CA   1 
ATOM   4887 C C    . ILE   B 1 69  ? 48.757 -8.627  11.831  1.00 13.18 ?  69  ILE   B C    1 
ATOM   4888 O O    . ILE   B 1 69  ? 47.887 -8.349  12.663  1.00 13.66 ?  69  ILE   B O    1 
ATOM   4889 C CB   . ILE   B 1 69  ? 49.072 -11.047 11.132  1.00 14.65 ?  69  ILE   B CB   1 
ATOM   4890 C CG1  . ILE   B 1 69  ? 48.545 -12.139 10.196  1.00 15.06 ?  69  ILE   B CG1  1 
ATOM   4891 C CG2  . ILE   B 1 69  ? 48.770 -11.378 12.587  1.00 15.85 ?  69  ILE   B CG2  1 
ATOM   4892 C CD1  . ILE   B 1 69  ? 47.069 -12.442 10.358  1.00 15.42 ?  69  ILE   B CD1  1 
ATOM   4893 H H    . ILE   B 1 69  ? 49.706 -9.723  9.191   1.00 15.43 ?  69  ILE   B H    1 
ATOM   4894 H HA   . ILE   B 1 69  ? 47.542 -9.760  10.655  1.00 16.26 ?  69  ILE   B HA   1 
ATOM   4895 H HB   . ILE   B 1 69  ? 50.039 -11.007 11.032  1.00 17.57 ?  69  ILE   B HB   1 
ATOM   4896 H HG12 . ILE   B 1 69  ? 48.692 -11.855 9.280   1.00 18.07 ?  69  ILE   B HG12 1 
ATOM   4897 H HG13 . ILE   B 1 69  ? 49.038 -12.957 10.368  1.00 18.07 ?  69  ILE   B HG13 1 
ATOM   4898 H HG21 . ILE   B 1 69  ? 48.913 -12.328 12.726  1.00 19.02 ?  69  ILE   B HG21 1 
ATOM   4899 H HG22 . ILE   B 1 69  ? 49.366 -10.871 13.161  1.00 19.02 ?  69  ILE   B HG22 1 
ATOM   4900 H HG23 . ILE   B 1 69  ? 47.848 -11.152 12.777  1.00 19.02 ?  69  ILE   B HG23 1 
ATOM   4901 H HD11 . ILE   B 1 69  ? 46.827 -13.138 9.731   1.00 18.49 ?  69  ILE   B HD11 1 
ATOM   4902 H HD12 . ILE   B 1 69  ? 46.905 -12.744 11.265  1.00 18.49 ?  69  ILE   B HD12 1 
ATOM   4903 H HD13 . ILE   B 1 69  ? 46.557 -11.640 10.176  1.00 18.49 ?  69  ILE   B HD13 1 
ATOM   4904 N N    . ALA   B 1 70  ? 49.952 -8.045  11.852  1.00 12.84 ?  70  ALA   B N    1 
ATOM   4905 C CA   . ALA   B 1 70  ? 50.236 -7.011  12.842  1.00 12.86 ?  70  ALA   B CA   1 
ATOM   4906 C C    . ALA   B 1 70  ? 49.247 -5.860  12.728  1.00 13.30 ?  70  ALA   B C    1 
ATOM   4907 O O    . ALA   B 1 70  ? 48.807 -5.303  13.741  1.00 13.48 ?  70  ALA   B O    1 
ATOM   4908 C CB   . ALA   B 1 70  ? 51.668 -6.505  12.668  1.00 13.52 ?  70  ALA   B CB   1 
ATOM   4909 H H    . ALA   B 1 70  ? 50.597 -8.226  11.322  1.00 15.40 ?  70  ALA   B H    1 
ATOM   4910 H HA   . ALA   B 1 70  ? 50.156 -7.387  13.731  1.00 15.43 ?  70  ALA   B HA   1 
ATOM   4911 H HB1  . ALA   B 1 70  ? 51.856 -5.843  13.352  1.00 16.21 ?  70  ALA   B HB1  1 
ATOM   4912 H HB2  . ALA   B 1 70  ? 52.279 -7.253  12.757  1.00 16.21 ?  70  ALA   B HB2  1 
ATOM   4913 H HB3  . ALA   B 1 70  ? 51.759 -6.107  11.788  1.00 16.21 ?  70  ALA   B HB3  1 
ATOM   4914 N N    . THR   B 1 71  ? 48.872 -5.496  11.503  1.00 13.63 ?  71  THR   B N    1 
ATOM   4915 C CA   . THR   B 1 71  ? 47.991 -4.354  11.292  1.00 14.66 ?  71  THR   B CA   1 
ATOM   4916 C C    . THR   B 1 71  ? 46.522 -4.710  11.495  1.00 15.31 ?  71  THR   B C    1 
ATOM   4917 O O    . THR   B 1 71  ? 45.748 -3.885  12.003  1.00 16.45 ?  71  THR   B O    1 
ATOM   4918 C CB   . THR   B 1 71  ? 48.216 -3.786  9.889   1.00 16.38 ?  71  THR   B CB   1 
ATOM   4919 O OG1  . THR   B 1 71  ? 49.547 -3.266  9.795   1.00 18.25 ?  71  THR   B OG1  1 
ATOM   4920 C CG2  . THR   B 1 71  ? 47.207 -2.686  9.567   1.00 17.53 ?  71  THR   B CG2  1 
ATOM   4921 H H    . THR   B 1 71  ? 49.112 -5.894  10.782  1.00 16.34 ?  71  THR   B H    1 
ATOM   4922 H HA   . THR   B 1 71  ? 48.212 -3.661  11.926  1.00 17.59 ?  71  THR   B HA   1 
ATOM   4923 H HB   . THR   B 1 71  ? 48.109 -4.490  9.229   1.00 19.65 ?  71  THR   B HB   1 
ATOM   4924 H HG1  . THR   B 1 71  ? 49.679 -2.936  9.031   1.00 21.89 ?  71  THR   B HG1  1 
ATOM   4925 H HG21 . THR   B 1 71  ? 47.515 -2.164  8.807   1.00 21.03 ?  71  THR   B HG21 1 
ATOM   4926 H HG22 . THR   B 1 71  ? 46.345 -3.071  9.353   1.00 21.03 ?  71  THR   B HG22 1 
ATOM   4927 H HG23 . THR   B 1 71  ? 47.111 -2.093  10.331  1.00 21.03 ?  71  THR   B HG23 1 
ATOM   4928 N N    . ASN   B 1 72  ? 46.119 -5.923  11.105  1.00 15.03 ?  72  ASN   B N    1 
ATOM   4929 C CA   . ASN   B 1 72  ? 44.713 -6.280  10.980  1.00 15.40 ?  72  ASN   B CA   1 
ATOM   4930 C C    . ASN   B 1 72  ? 44.247 -7.384  11.917  1.00 16.06 ?  72  ASN   B C    1 
ATOM   4931 O O    . ASN   B 1 72  ? 43.031 -7.552  12.083  1.00 17.02 ?  72  ASN   B O    1 
ATOM   4932 C CB   . ASN   B 1 72  ? 44.403 -6.697  9.534   1.00 16.46 ?  72  ASN   B CB   1 
ATOM   4933 C CG   . ASN   B 1 72  ? 44.689 -5.591  8.546   1.00 17.47 ?  72  ASN   B CG   1 
ATOM   4934 O OD1  . ASN   B 1 72  ? 45.695 -5.611  7.831   1.00 18.31 ?  72  ASN   B OD1  1 
ATOM   4935 N ND2  . ASN   B 1 72  ? 43.823 -4.595  8.526   1.00 18.58 ?  72  ASN   B ND2  1 
ATOM   4936 H H    . ASN   B 1 72  ? 46.656 -6.569  10.905  1.00 18.03 ?  72  ASN   B H    1 
ATOM   4937 H HA   . ASN   B 1 72  ? 44.182 -5.495  11.174  1.00 18.48 ?  72  ASN   B HA   1 
ATOM   4938 H HB2  . ASN   B 1 72  ? 44.953 -7.460  9.297   1.00 19.74 ?  72  ASN   B HB2  1 
ATOM   4939 H HB3  . ASN   B 1 72  ? 43.464 -6.929  9.467   1.00 19.74 ?  72  ASN   B HB3  1 
ATOM   4940 H HD21 . ASN   B 1 72  ? 43.933 -3.934  7.985   1.00 22.28 ?  72  ASN   B HD21 1 
ATOM   4941 H HD22 . ASN   B 1 72  ? 43.134 -4.607  9.046   1.00 22.28 ?  72  ASN   B HD22 1 
ATOM   4942 N N    . GLY   B 1 73  ? 45.155 -8.133  12.536  1.00 15.55 ?  73  GLY   B N    1 
ATOM   4943 C CA   . GLY   B 1 73  ? 44.762 -9.273  13.327  1.00 14.91 ?  73  GLY   B CA   1 
ATOM   4944 C C    . GLY   B 1 73  ? 44.384 -10.452 12.456  1.00 13.52 ?  73  GLY   B C    1 
ATOM   4945 O O    . GLY   B 1 73  ? 44.370 -10.367 11.225  1.00 13.41 ?  73  GLY   B O    1 
ATOM   4946 H H    . GLY   B 1 73  ? 46.008 -7.995  12.511  1.00 18.65 ?  73  GLY   B H    1 
ATOM   4947 H HA2  . GLY   B 1 73  ? 45.494 -9.535  13.907  1.00 17.89 ?  73  GLY   B HA2  1 
ATOM   4948 H HA3  . GLY   B 1 73  ? 43.999 -9.038  13.878  1.00 17.89 ?  73  GLY   B HA3  1 
ATOM   4949 N N    . PRO   B 1 74  ? 44.067 -11.577 13.090  1.00 14.04 ?  74  PRO   B N    1 
ATOM   4950 C CA   . PRO   B 1 74  ? 43.819 -12.808 12.340  1.00 13.41 ?  74  PRO   B CA   1 
ATOM   4951 C C    . PRO   B 1 74  ? 42.521 -12.748 11.549  1.00 12.67 ?  74  PRO   B C    1 
ATOM   4952 O O    . PRO   B 1 74  ? 41.580 -12.013 11.868  1.00 13.80 ?  74  PRO   B O    1 
ATOM   4953 C CB   . PRO   B 1 74  ? 43.742 -13.876 13.438  1.00 14.32 ?  74  PRO   B CB   1 
ATOM   4954 C CG   . PRO   B 1 74  ? 43.312 -13.137 14.654  1.00 15.88 ?  74  PRO   B CG   1 
ATOM   4955 C CD   . PRO   B 1 74  ? 43.974 -11.792 14.545  1.00 15.50 ?  74  PRO   B CD   1 
ATOM   4956 H HA   . PRO   B 1 74  ? 44.563 -13.002 11.744  1.00 16.08 ?  74  PRO   B HA   1 
ATOM   4957 H HB2  . PRO   B 1 74  ? 43.089 -14.550 13.192  1.00 17.18 ?  74  PRO   B HB2  1 
ATOM   4958 H HB3  . PRO   B 1 74  ? 44.617 -14.275 13.568  1.00 17.18 ?  74  PRO   B HB3  1 
ATOM   4959 H HG2  . PRO   B 1 74  ? 42.345 -13.049 14.653  1.00 19.05 ?  74  PRO   B HG2  1 
ATOM   4960 H HG3  . PRO   B 1 74  ? 43.614 -13.609 15.444  1.00 19.05 ?  74  PRO   B HG3  1 
ATOM   4961 H HD2  . PRO   B 1 74  ? 43.418 -11.109 14.957  1.00 18.59 ?  74  PRO   B HD2  1 
ATOM   4962 H HD3  . PRO   B 1 74  ? 44.858 -11.816 14.940  1.00 18.59 ?  74  PRO   B HD3  1 
ATOM   4963 N N    . LEU   B 1 75  ? 42.492 -13.563 10.497  1.00 11.82 ?  75  LEU   B N    1 
ATOM   4964 C CA   . LEU   B 1 75  ? 41.281 -13.781 9.726   1.00 12.16 ?  75  LEU   B CA   1 
ATOM   4965 C C    . LEU   B 1 75  ? 40.309 -14.648 10.525  1.00 12.40 ?  75  LEU   B C    1 
ATOM   4966 O O    . LEU   B 1 75  ? 40.647 -15.195 11.577  1.00 13.34 ?  75  LEU   B O    1 
ATOM   4967 C CB   . LEU   B 1 75  ? 41.609 -14.488 8.410   1.00 12.07 ?  75  LEU   B CB   1 
ATOM   4968 C CG   . LEU   B 1 75  ? 42.472 -13.740 7.388   1.00 13.84 ?  75  LEU   B CG   1 
ATOM   4969 C CD1  . LEU   B 1 75  ? 42.653 -14.569 6.121   1.00 15.08 ?  75  LEU   B CD1  1 
ATOM   4970 C CD2  . LEU   B 1 75  ? 41.902 -12.386 7.053   1.00 17.09 ?  75  LEU   B CD2  1 
ATOM   4971 H H    . LEU   B 1 75  ? 43.166 -14.015 10.208  1.00 14.18 ?  75  LEU   B H    1 
ATOM   4972 H HA   . LEU   B 1 75  ? 40.855 -12.936 9.531   1.00 14.58 ?  75  LEU   B HA   1 
ATOM   4973 H HB2  . LEU   B 1 75  ? 42.077 -15.314 8.619   1.00 14.47 ?  75  LEU   B HB2  1 
ATOM   4974 H HB3  . LEU   B 1 75  ? 40.775 -14.704 7.965   1.00 14.47 ?  75  LEU   B HB3  1 
ATOM   4975 H HG   . LEU   B 1 75  ? 43.352 -13.602 7.772   1.00 16.60 ?  75  LEU   B HG   1 
ATOM   4976 H HD11 . LEU   B 1 75  ? 43.207 -14.069 5.495   1.00 18.09 ?  75  LEU   B HD11 1 
ATOM   4977 H HD12 . LEU   B 1 75  ? 43.087 -15.405 6.347   1.00 18.09 ?  75  LEU   B HD12 1 
ATOM   4978 H HD13 . LEU   B 1 75  ? 41.785 -14.739 5.727   1.00 18.09 ?  75  LEU   B HD13 1 
ATOM   4979 H HD21 . LEU   B 1 75  ? 42.428 -11.986 6.344   1.00 20.50 ?  75  LEU   B HD21 1 
ATOM   4980 H HD22 . LEU   B 1 75  ? 40.983 -12.493 6.765   1.00 20.50 ?  75  LEU   B HD22 1 
ATOM   4981 H HD23 . LEU   B 1 75  ? 41.936 -11.824 7.846   1.00 20.50 ?  75  LEU   B HD23 1 
ATOM   4982 N N    . LYS   B 1 76  ? 39.082 -14.756 10.010  1.00 13.25 ?  76  LYS   B N    1 
ATOM   4983 C CA   . LYS   B 1 76  ? 38.093 -15.716 10.483  1.00 14.86 ?  76  LYS   B CA   1 
ATOM   4984 C C    . LYS   B 1 76  ? 38.180 -16.984 9.636   1.00 12.96 ?  76  LYS   B C    1 
ATOM   4985 O O    . LYS   B 1 76  ? 38.446 -16.919 8.438   1.00 12.54 ?  76  LYS   B O    1 
ATOM   4986 C CB   . LYS   B 1 76  ? 36.671 -15.146 10.308  1.00 17.74 ?  76  LYS   B CB   1 
ATOM   4987 C CG   . LYS   B 1 76  ? 36.384 -13.775 10.947  1.00 19.21 ?  76  LYS   B CG   1 
ATOM   4988 C CD   . LYS   B 1 76  ? 34.991 -13.226 10.565  1.00 20.75 ?  76  LYS   B CD   1 
ATOM   4989 C CE   . LYS   B 1 76  ? 34.736 -11.857 11.183  1.00 22.81 ?  76  LYS   B CE   1 
ATOM   4990 N NZ   . LYS   B 1 76  ? 33.453 -11.257 10.725  1.00 23.53 ?  76  LYS   B NZ   1 
ATOM   4991 H H    . LYS   B 1 76  ? 38.794 -14.271 9.362   1.00 15.90 ?  76  LYS   B H    1 
ATOM   4992 H HA   . LYS   B 1 76  ? 38.242 -15.938 11.415  1.00 17.82 ?  76  LYS   B HA   1 
ATOM   4993 H HB2  . LYS   B 1 76  ? 36.494 -15.063 9.357   1.00 21.28 ?  76  LYS   B HB2  1 
ATOM   4994 H HB3  . LYS   B 1 76  ? 36.042 -15.778 10.693  1.00 21.28 ?  76  LYS   B HB3  1 
ATOM   4995 H HG2  . LYS   B 1 76  ? 36.423 -13.862 11.911  1.00 23.05 ?  76  LYS   B HG2  1 
ATOM   4996 H HG3  . LYS   B 1 76  ? 37.054 -13.141 10.642  1.00 23.05 ?  76  LYS   B HG3  1 
ATOM   4997 H HD2  . LYS   B 1 76  ? 34.939 -13.138 9.599   1.00 24.89 ?  76  LYS   B HD2  1 
ATOM   4998 H HD3  . LYS   B 1 76  ? 34.311 -13.837 10.883  1.00 24.89 ?  76  LYS   B HD3  1 
ATOM   4999 H HE2  . LYS   B 1 76  ? 34.701 -11.949 12.148  1.00 27.37 ?  76  LYS   B HE2  1 
ATOM   5000 H HE3  . LYS   B 1 76  ? 35.458 -11.258 10.933  1.00 27.37 ?  76  LYS   B HE3  1 
ATOM   5001 H HZ1  . LYS   B 1 76  ? 33.336 -10.458 11.106  1.00 28.23 ?  76  LYS   B HZ1  1 
ATOM   5002 H HZ2  . LYS   B 1 76  ? 33.461 -11.152 9.841   1.00 28.23 ?  76  LYS   B HZ2  1 
ATOM   5003 H HZ3  . LYS   B 1 76  ? 32.771 -11.783 10.948  1.00 28.23 ?  76  LYS   B HZ3  1 
ATOM   5004 N N    . VAL   B 1 77  ? 37.921 -18.143 10.253  1.00 13.21 ?  77  VAL   B N    1 
ATOM   5005 C CA   . VAL   B 1 77  ? 37.716 -19.349 9.455   1.00 13.43 ?  77  VAL   B CA   1 
ATOM   5006 C C    . VAL   B 1 77  ? 36.523 -19.109 8.540   1.00 12.46 ?  77  VAL   B C    1 
ATOM   5007 O O    . VAL   B 1 77  ? 35.457 -18.661 8.987   1.00 12.55 ?  77  VAL   B O    1 
ATOM   5008 C CB   . VAL   B 1 77  ? 37.525 -20.587 10.346  1.00 14.77 ?  77  VAL   B CB   1 
ATOM   5009 C CG1  . VAL   B 1 77  ? 37.234 -21.812 9.485   1.00 15.40 ?  77  VAL   B CG1  1 
ATOM   5010 C CG2  . VAL   B 1 77  ? 38.762 -20.821 11.208  1.00 16.54 ?  77  VAL   B CG2  1 
ATOM   5011 H H    . VAL   B 1 77  ? 37.865 -18.253 11.101  1.00 15.84 ?  77  VAL   B H    1 
ATOM   5012 H HA   . VAL   B 1 77  ? 38.494 -19.496 8.896   1.00 16.11 ?  77  VAL   B HA   1 
ATOM   5013 H HB   . VAL   B 1 77  ? 36.767 -20.439 10.934  1.00 17.71 ?  77  VAL   B HB   1 
ATOM   5014 H HG11 . VAL   B 1 77  ? 37.305 -22.605 10.037  1.00 18.47 ?  77  VAL   B HG11 1 
ATOM   5015 H HG12 . VAL   B 1 77  ? 36.334 -21.742 9.124   1.00 18.47 ?  77  VAL   B HG12 1 
ATOM   5016 H HG13 . VAL   B 1 77  ? 37.879 -21.851 8.763   1.00 18.47 ?  77  VAL   B HG13 1 
ATOM   5017 H HG21 . VAL   B 1 77  ? 38.629 -21.623 11.733  1.00 19.85 ?  77  VAL   B HG21 1 
ATOM   5018 H HG22 . VAL   B 1 77  ? 39.531 -20.922 10.629  1.00 19.85 ?  77  VAL   B HG22 1 
ATOM   5019 H HG23 . VAL   B 1 77  ? 38.884 -20.056 11.794  1.00 19.85 ?  77  VAL   B HG23 1 
ATOM   5020 N N    . GLY   B 1 78  ? 36.705 -19.387 7.251   1.00 12.12 ?  78  GLY   B N    1 
ATOM   5021 C CA   . GLY   B 1 78  ? 35.731 -19.066 6.236   1.00 11.67 ?  78  GLY   B CA   1 
ATOM   5022 C C    . GLY   B 1 78  ? 35.973 -17.746 5.540   1.00 11.12 ?  78  GLY   B C    1 
ATOM   5023 O O    . GLY   B 1 78  ? 35.292 -17.461 4.548   1.00 11.48 ?  78  GLY   B O    1 
ATOM   5024 H H    . GLY   B 1 78  ? 37.414 -19.765 6.936   1.00 14.54 ?  78  GLY   B H    1 
ATOM   5025 H HA2  . GLY   B 1 78  ? 35.732 -19.761 5.562   1.00 13.99 ?  78  GLY   B HA2  1 
ATOM   5026 H HA3  . GLY   B 1 78  ? 34.852 -19.031 6.639   1.00 13.99 ?  78  GLY   B HA3  1 
ATOM   5027 N N    . GLY   B 1 79  ? 36.925 -16.943 6.027   1.00 11.27 ?  79  GLY   B N    1 
ATOM   5028 C CA   . GLY   B 1 79  ? 37.225 -15.648 5.456   1.00 11.05 ?  79  GLY   B CA   1 
ATOM   5029 C C    . GLY   B 1 79  ? 38.467 -15.665 4.574   1.00 10.68 ?  79  GLY   B C    1 
ATOM   5030 O O    . GLY   B 1 79  ? 39.082 -16.701 4.327   1.00 11.11 ?  79  GLY   B O    1 
ATOM   5031 H H    . GLY   B 1 79  ? 37.421 -17.141 6.696   1.00 13.52 ?  79  GLY   B H    1 
ATOM   5032 H HA2  . GLY   B 1 79  ? 36.471 -15.342 4.922   1.00 13.26 ?  79  GLY   B HA2  1 
ATOM   5033 H HA3  . GLY   B 1 79  ? 37.368 -15.006 6.170   1.00 13.26 ?  79  GLY   B HA3  1 
ATOM   5034 N N    . SER   B 1 80  ? 38.832 -14.470 4.101   1.00 10.77 ?  80  SER   B N    1 
ATOM   5035 C CA   . SER   B 1 80  ? 39.942 -14.333 3.169   1.00 10.53 ?  80  SER   B CA   1 
ATOM   5036 C C    . SER   B 1 80  ? 40.521 -12.927 3.231   1.00 10.47 ?  80  SER   B C    1 
ATOM   5037 O O    . SER   B 1 80  ? 39.900 -11.994 3.747   1.00 11.77 ?  80  SER   B O    1 
ATOM   5038 C CB   . SER   B 1 80  ? 39.495 -14.619 1.733   1.00 11.03 ?  80  SER   B CB   1 
ATOM   5039 O OG   . SER   B 1 80  ? 38.656 -13.592 1.229   1.00 11.95 ?  80  SER   B OG   1 
ATOM   5040 H H    . SER   B 1 80  ? 38.454 -13.723 4.306   1.00 12.92 ?  80  SER   B H    1 
ATOM   5041 H HA   . SER   B 1 80  ? 40.632 -14.968 3.413   1.00 12.63 ?  80  SER   B HA   1 
ATOM   5042 H HB2  . SER   B 1 80  ? 40.276 -14.684 1.165   1.00 13.23 ?  80  SER   B HB2  1 
ATOM   5043 H HB3  . SER   B 1 80  ? 39.004 -15.457 1.716   1.00 13.23 ?  80  SER   B HB3  1 
ATOM   5044 H HG   . SER   B 1 80  ? 37.966 -13.522 1.716   1.00 14.34 ?  80  SER   B HG   1 
ATOM   5045 N N    . CYS   B 1 81  ? 41.709 -12.782 2.646   1.00 10.35 ?  81  CYS   B N    1 
ATOM   5046 C CA   . CYS   B 1 81  ? 42.256 -11.469 2.334   1.00 10.52 ?  81  CYS   B CA   1 
ATOM   5047 C C    . CYS   B 1 81  ? 43.031 -11.547 1.027   1.00 10.17 ?  81  CYS   B C    1 
ATOM   5048 O O    . CYS   B 1 81  ? 43.542 -12.606 0.649   1.00 10.72 ?  81  CYS   B O    1 
ATOM   5049 C CB   . CYS   B 1 81  ? 43.148 -10.917 3.453   1.00 11.34 ?  81  CYS   B CB   1 
ATOM   5050 S SG   . CYS   B 1 81  ? 44.661 -11.853 3.718   1.00 11.91 ?  81  CYS   B SG   1 
ATOM   5051 H H    . CYS   B 1 81  ? 42.218 -13.436 2.415   1.00 12.41 ?  81  CYS   B H    1 
ATOM   5052 H HA   . CYS   B 1 81  ? 41.522 -10.848 2.208   1.00 12.62 ?  81  CYS   B HA   1 
ATOM   5053 H HB2  . CYS   B 1 81  ? 43.399 -10.007 3.232   1.00 13.60 ?  81  CYS   B HB2  1 
ATOM   5054 H HB3  . CYS   B 1 81  ? 42.642 -10.921 4.284   1.00 13.60 ?  81  CYS   B HB3  1 
ATOM   5055 H HG   . CYS   B 1 81  ? 45.281 -11.343 4.621   1.00 14.29 ?  81  CYS   B HG   1 
ATOM   5056 N N    . VAL   B 1 82  ? 43.127 -10.405 0.352   1.00 10.48 ?  82  VAL   B N    1 
ATOM   5057 C CA   . VAL   B 1 82  ? 43.888 -10.280 -0.886  1.00 10.76 ?  82  VAL   B CA   1 
ATOM   5058 C C    . VAL   B 1 82  ? 45.226 -9.636  -0.564  1.00 11.07 ?  82  VAL   B C    1 
ATOM   5059 O O    . VAL   B 1 82  ? 45.275 -8.516  -0.032  1.00 11.76 ?  82  VAL   B O    1 
ATOM   5060 C CB   . VAL   B 1 82  ? 43.145 -9.439  -1.935  1.00 12.03 ?  82  VAL   B CB   1 
ATOM   5061 C CG1  . VAL   B 1 82  ? 44.006 -9.280  -3.185  1.00 13.55 ?  82  VAL   B CG1  1 
ATOM   5062 C CG2  . VAL   B 1 82  ? 41.800 -10.055 -2.274  1.00 12.62 ?  82  VAL   B CG2  1 
ATOM   5063 H H    . VAL   B 1 82  ? 42.748 -9.669  0.596   1.00 12.57 ?  82  VAL   B H    1 
ATOM   5064 H HA   . VAL   B 1 82  ? 44.049 -11.160 -1.258  1.00 12.91 ?  82  VAL   B HA   1 
ATOM   5065 H HB   . VAL   B 1 82  ? 42.979 -8.558  -1.573  1.00 14.42 ?  82  VAL   B HB   1 
ATOM   5066 H HG11 . VAL   B 1 82  ? 43.447 -8.984  -3.919  1.00 16.25 ?  82  VAL   B HG11 1 
ATOM   5067 H HG12 . VAL   B 1 82  ? 44.697 -8.619  -3.011  1.00 16.25 ?  82  VAL   B HG12 1 
ATOM   5068 H HG13 . VAL   B 1 82  ? 44.412 -10.134 -3.402  1.00 16.25 ?  82  VAL   B HG13 1 
ATOM   5069 H HG21 . VAL   B 1 82  ? 41.365 -9.519  -2.958  1.00 15.14 ?  82  VAL   B HG21 1 
ATOM   5070 H HG22 . VAL   B 1 82  ? 41.936 -10.959 -2.606  1.00 15.14 ?  82  VAL   B HG22 1 
ATOM   5071 H HG23 . VAL   B 1 82  ? 41.248 -10.080 -1.476  1.00 15.14 ?  82  VAL   B HG23 1 
ATOM   5072 N N    . LEU   B 1 83  ? 46.307 -10.322 -0.925  1.00 10.51 ?  83  LEU   B N    1 
ATOM   5073 C CA   . LEU   B 1 83  ? 47.663 -9.808  -0.799  1.00 10.50 ?  83  LEU   B CA   1 
ATOM   5074 C C    . LEU   B 1 83  ? 48.370 -9.942  -2.150  1.00 10.42 ?  83  LEU   B C    1 
ATOM   5075 O O    . LEU   B 1 83  ? 47.772 -10.356 -3.152  1.00 10.44 ?  83  LEU   B O    1 
ATOM   5076 C CB   . LEU   B 1 83  ? 48.407 -10.491 0.360   1.00 11.35 ?  83  LEU   B CB   1 
ATOM   5077 C CG   . LEU   B 1 83  ? 47.895 -10.132 1.763   1.00 12.47 ?  83  LEU   B CG   1 
ATOM   5078 C CD1  . LEU   B 1 83  ? 48.529 -11.002 2.829   1.00 13.12 ?  83  LEU   B CD1  1 
ATOM   5079 C CD2  . LEU   B 1 83  ? 48.107 -8.654  2.092   1.00 13.42 ?  83  LEU   B CD2  1 
ATOM   5080 H H    . LEU   B 1 83  ? 46.272 -11.121 -1.254  1.00 12.60 ?  83  LEU   B H    1 
ATOM   5081 H HA   . LEU   B 1 83  ? 47.612 -8.867  -0.597  1.00 12.60 ?  83  LEU   B HA   1 
ATOM   5082 H HB2  . LEU   B 1 83  ? 48.334 -11.450 0.262   1.00 13.61 ?  83  LEU   B HB2  1 
ATOM   5083 H HB3  . LEU   B 1 83  ? 49.342 -10.230 0.322   1.00 13.61 ?  83  LEU   B HB3  1 
ATOM   5084 H HG   . LEU   B 1 83  ? 46.940 -10.297 1.785   1.00 14.96 ?  83  LEU   B HG   1 
ATOM   5085 H HD11 . LEU   B 1 83  ? 48.169 -10.753 3.696   1.00 15.74 ?  83  LEU   B HD11 1 
ATOM   5086 H HD12 . LEU   B 1 83  ? 48.315 -11.934 2.643   1.00 15.74 ?  83  LEU   B HD12 1 
ATOM   5087 H HD13 . LEU   B 1 83  ? 49.487 -10.876 2.817   1.00 15.74 ?  83  LEU   B HD13 1 
ATOM   5088 H HD21 . LEU   B 1 83  ? 47.891 -8.506  3.025   1.00 16.09 ?  83  LEU   B HD21 1 
ATOM   5089 H HD22 . LEU   B 1 83  ? 49.033 -8.424  1.924   1.00 16.09 ?  83  LEU   B HD22 1 
ATOM   5090 H HD23 . LEU   B 1 83  ? 47.525 -8.120  1.528   1.00 16.09 ?  83  LEU   B HD23 1 
ATOM   5091 N N    . SER   B 1 84  ? 49.648 -9.576  -2.195  1.00 11.27 ?  84  SER   B N    1 
ATOM   5092 C CA   . SER   B 1 84  ? 50.385 -9.680  -3.446  1.00 11.68 ?  84  SER   B CA   1 
ATOM   5093 C C    . SER   B 1 84  ? 50.535 -11.133 -3.881  1.00 10.90 ?  84  SER   B C    1 
ATOM   5094 O O    . SER   B 1 84  ? 50.641 -12.044 -3.061  1.00 10.49 ?  84  SER   B O    1 
ATOM   5095 C CB   . SER   B 1 84  ? 51.783 -9.083  -3.296  1.00 13.66 ?  84  SER   B CB   1 
ATOM   5096 O OG   . SER   B 1 84  ? 52.533 -9.277  -4.482  1.00 15.01 ?  84  SER   B OG   1 
ATOM   5097 H H    . SER   B 1 84  ? 50.099 -9.259  -1.530  1.00 13.51 ?  84  SER   B H    1 
ATOM   5098 H HA   . SER   B 1 84  ? 49.916 -9.199  -4.141  1.00 14.01 ?  84  SER   B HA   1 
ATOM   5099 H HB2  . SER   B 1 84  ? 51.704 -8.130  -3.115  1.00 16.38 ?  84  SER   B HB2  1 
ATOM   5100 H HB3  . SER   B 1 84  ? 52.245 -9.520  -2.566  1.00 16.38 ?  84  SER   B HB3  1 
ATOM   5101 H HG   . SER   B 1 84  ? 53.293 -8.929  -4.405  1.00 18.00 ?  84  SER   B HG   1 
ATOM   5102 N N    . GLY   B 1 85  ? 50.590 -11.340 -5.190  1.00 11.75 ?  85  GLY   B N    1 
ATOM   5103 C CA   . GLY   B 1 85  ? 50.943 -12.625 -5.747  1.00 12.35 ?  85  GLY   B CA   1 
ATOM   5104 C C    . GLY   B 1 85  ? 52.416 -12.822 -6.043  1.00 11.76 ?  85  GLY   B C    1 
ATOM   5105 O O    . GLY   B 1 85  ? 52.795 -13.902 -6.501  1.00 11.83 ?  85  GLY   B O    1 
ATOM   5106 H H    . GLY   B 1 85  ? 50.430 -10.740 -5.780  1.00 14.09 ?  85  GLY   B H    1 
ATOM   5107 H HA2  . GLY   B 1 85  ? 50.667 -13.322 -5.127  1.00 14.82 ?  85  GLY   B HA2  1 
ATOM   5108 H HA3  . GLY   B 1 85  ? 50.457 -12.754 -6.572  1.00 14.82 ?  85  GLY   B HA3  1 
ATOM   5109 N N    . HIS   B 1 86  ? 53.268 -11.829 -5.805  1.00 11.74 ?  86  HIS   B N    1 
ATOM   5110 C CA   . HIS   B 1 86  ? 54.729 -12.001 -5.885  1.00 11.71 ?  86  HIS   B CA   1 
ATOM   5111 C C    . HIS   B 1 86  ? 55.103 -12.504 -7.277  1.00 12.00 ?  86  HIS   B C    1 
ATOM   5112 O O    . HIS   B 1 86  ? 54.714 -11.882 -8.279  1.00 12.70 ?  86  HIS   B O    1 
ATOM   5113 C CB   . HIS   B 1 86  ? 55.216 -12.851 -4.713  1.00 12.32 ?  86  HIS   B CB   1 
ATOM   5114 C CG   . HIS   B 1 86  ? 54.904 -12.249 -3.384  1.00 12.43 ?  86  HIS   B CG   1 
ATOM   5115 N ND1  . HIS   B 1 86  ? 55.742 -11.355 -2.751  1.00 13.66 ?  86  HIS   B ND1  1 
ATOM   5116 C CD2  . HIS   B 1 86  ? 53.823 -12.392 -2.581  1.00 12.58 ?  86  HIS   B CD2  1 
ATOM   5117 C CE1  . HIS   B 1 86  ? 55.183 -10.971 -1.617  1.00 13.59 ?  86  HIS   B CE1  1 
ATOM   5118 N NE2  . HIS   B 1 86  ? 54.018 -11.583 -1.492  1.00 12.91 ?  86  HIS   B NE2  1 
ATOM   5119 H H    . HIS   B 1 86  ? 53.029 -11.033 -5.596  1.00 14.08 ?  86  HIS   B H    1 
ATOM   5120 H HA   . HIS   B 1 86  ? 55.139 -11.132 -5.785  1.00 14.05 ?  86  HIS   B HA   1 
ATOM   5121 H HB2  . HIS   B 1 86  ? 54.798 -13.724 -4.756  1.00 14.77 ?  86  HIS   B HB2  1 
ATOM   5122 H HB3  . HIS   B 1 86  ? 56.182 -12.946 -4.773  1.00 14.77 ?  86  HIS   B HB3  1 
ATOM   5123 H HD2  . HIS   B 1 86  ? 53.071 -12.922 -2.750  1.00 15.09 ?  86  HIS   B HD2  1 
ATOM   5124 H HE1  . HIS   B 1 86  ? 55.556 -10.387 -1.001  1.00 16.30 ?  86  HIS   B HE1  1 
ATOM   5125 H HE2  . HIS   B 1 86  ? 53.473 -11.500 -0.828  1.00 15.48 ?  86  HIS   B HE2  1 
ATOM   5126 N N    . ASN   B 1 87  ? 55.871 -13.584 -7.392  1.00 12.35 ?  87  ASN   B N    1 
ATOM   5127 C CA   . ASN   B 1 87  ? 56.271 -14.151 -8.670  1.00 13.15 ?  87  ASN   B CA   1 
ATOM   5128 C C    . ASN   B 1 87  ? 55.292 -15.200 -9.174  1.00 12.80 ?  87  ASN   B C    1 
ATOM   5129 O O    . ASN   B 1 87  ? 55.608 -15.919 -10.126 1.00 14.38 ?  87  ASN   B O    1 
ATOM   5130 C CB   . ASN   B 1 87  ? 57.667 -14.774 -8.550  1.00 15.02 ?  87  ASN   B CB   1 
ATOM   5131 C CG   . ASN   B 1 87  ? 57.720 -15.900 -7.520  1.00 16.00 ?  87  ASN   B CG   1 
ATOM   5132 O OD1  . ASN   B 1 87  ? 57.086 -15.826 -6.463  1.00 15.12 ?  87  ASN   B OD1  1 
ATOM   5133 N ND2  . ASN   B 1 87  ? 58.451 -16.966 -7.844  1.00 18.16 ?  87  ASN   B ND2  1 
ATOM   5134 H H    . ASN   B 1 87  ? 56.185 -14.023 -6.719  1.00 14.81 ?  87  ASN   B H    1 
ATOM   5135 H HA   . ASN   B 1 87  ? 56.316 -13.442 -9.329  1.00 15.77 ?  87  ASN   B HA   1 
ATOM   5136 H HB2  . ASN   B 1 87  ? 57.924 -15.142 -9.414  1.00 18.02 ?  87  ASN   B HB2  1 
ATOM   5137 H HB3  . ASN   B 1 87  ? 58.297 -14.089 -8.282  1.00 18.02 ?  87  ASN   B HB3  1 
ATOM   5138 H HD21 . ASN   B 1 87  ? 58.515 -17.625 -7.298  1.00 21.78 ?  87  ASN   B HD21 1 
ATOM   5139 H HD22 . ASN   B 1 87  ? 58.872 -16.987 -8.596  1.00 21.78 ?  87  ASN   B HD22 1 
ATOM   5140 N N    . LEU   B 1 88  ? 54.111 -15.300 -8.561  1.00 11.67 ?  88  LEU   B N    1 
ATOM   5141 C CA   . LEU   B 1 88  ? 53.134 -16.335 -8.884  1.00 11.93 ?  88  LEU   B CA   1 
ATOM   5142 C C    . LEU   B 1 88  ? 51.904 -15.826 -9.614  1.00 11.29 ?  88  LEU   B C    1 
ATOM   5143 O O    . LEU   B 1 88  ? 51.306 -16.578 -10.395 1.00 13.40 ?  88  LEU   B O    1 
ATOM   5144 C CB   . LEU   B 1 88  ? 52.662 -17.017 -7.595  1.00 13.08 ?  88  LEU   B CB   1 
ATOM   5145 C CG   . LEU   B 1 88  ? 53.787 -17.653 -6.785  1.00 15.14 ?  88  LEU   B CG   1 
ATOM   5146 C CD1  . LEU   B 1 88  ? 53.274 -18.112 -5.431  1.00 16.57 ?  88  LEU   B CD1  1 
ATOM   5147 C CD2  . LEU   B 1 88  ? 54.396 -18.805 -7.559  1.00 17.91 ?  88  LEU   B CD2  1 
ATOM   5148 H H    . LEU   B 1 88  ? 53.851 -14.767 -7.931  1.00 14.00 ?  88  LEU   B H    1 
ATOM   5149 H HA   . LEU   B 1 88  ? 53.557 -17.001 -9.440  1.00 14.31 ?  88  LEU   B HA   1 
ATOM   5150 H HB2  . LEU   B 1 88  ? 52.227 -16.359 -7.029  1.00 15.69 ?  88  LEU   B HB2  1 
ATOM   5151 H HB3  . LEU   B 1 88  ? 52.034 -17.718 -7.825  1.00 15.69 ?  88  LEU   B HB3  1 
ATOM   5152 H HG   . LEU   B 1 88  ? 54.480 -16.992 -6.630  1.00 18.16 ?  88  LEU   B HG   1 
ATOM   5153 H HD11 . LEU   B 1 88  ? 53.984 -18.580 -4.964  1.00 19.88 ?  88  LEU   B HD11 1 
ATOM   5154 H HD12 . LEU   B 1 88  ? 52.991 -17.340 -4.918  1.00 19.88 ?  88  LEU   B HD12 1 
ATOM   5155 H HD13 . LEU   B 1 88  ? 52.521 -18.710 -5.569  1.00 19.88 ?  88  LEU   B HD13 1 
ATOM   5156 H HD21 . LEU   B 1 88  ? 55.000 -19.290 -6.976  1.00 21.49 ?  88  LEU   B HD21 1 
ATOM   5157 H HD22 . LEU   B 1 88  ? 53.685 -19.389 -7.862  1.00 21.49 ?  88  LEU   B HD22 1 
ATOM   5158 H HD23 . LEU   B 1 88  ? 54.881 -18.451 -8.320  1.00 21.49 ?  88  LEU   B HD23 1 
ATOM   5159 N N    . ALA   B 1 89  ? 51.495 -14.590 -9.350  1.00 10.77 ?  89  ALA   B N    1 
ATOM   5160 C CA   . ALA   B 1 89  ? 50.194 -14.106 -9.791  1.00 10.53 ?  89  ALA   B CA   1 
ATOM   5161 C C    . ALA   B 1 89  ? 50.162 -12.612 -9.523  1.00 11.02 ?  89  ALA   B C    1 
ATOM   5162 O O    . ALA   B 1 89  ? 50.999 -12.087 -8.788  1.00 11.82 ?  89  ALA   B O    1 
ATOM   5163 C CB   . ALA   B 1 89  ? 49.062 -14.779 -9.019  1.00 10.81 ?  89  ALA   B CB   1 
ATOM   5164 H H    . ALA   B 1 89  ? 51.949 -14.005 -8.906  1.00 12.91 ?  89  ALA   B H    1 
ATOM   5165 H HA   . ALA   B 1 89  ? 50.076 -14.262 -10.740 1.00 12.62 ?  89  ALA   B HA   1 
ATOM   5166 H HB1  . ALA   B 1 89  ? 48.212 -14.444 -9.349  1.00 12.97 ?  89  ALA   B HB1  1 
ATOM   5167 H HB2  . ALA   B 1 89  ? 49.116 -15.737 -9.161  1.00 12.97 ?  89  ALA   B HB2  1 
ATOM   5168 H HB3  . ALA   B 1 89  ? 49.157 -14.575 -8.078  1.00 12.97 ?  89  ALA   B HB3  1 
ATOM   5169 N N    . LYS   B 1 90  ? 49.159 -11.930 -10.075 1.00 11.78 ?  90  LYS   B N    1 
ATOM   5170 C CA   . LYS   B 1 90  ? 48.967 -10.542 -9.673  1.00 12.13 ?  90  LYS   B CA   1 
ATOM   5171 C C    . LYS   B 1 90  ? 48.656 -10.467 -8.182  1.00 11.78 ?  90  LYS   B C    1 
ATOM   5172 O O    . LYS   B 1 90  ? 49.288 -9.701  -7.437  1.00 13.17 ?  90  LYS   B O    1 
ATOM   5173 C CB   . LYS   B 1 90  ? 47.883 -9.879  -10.522 1.00 13.65 ?  90  LYS   B CB   1 
ATOM   5174 C CG   . LYS   B 1 90  ? 47.620 -8.434  -10.158 1.00 14.56 ?  90  LYS   B CG   1 
ATOM   5175 C CD   . LYS   B 1 90  ? 48.849 -7.563  -10.250 1.00 17.42 ?  90  LYS   B CD   1 
ATOM   5176 C CE   . LYS   B 1 90  ? 48.432 -6.123  -10.065 1.00 19.56 ?  90  LYS   B CE   1 
ATOM   5177 N NZ   . LYS   B 1 90  ? 49.588 -5.206  -9.945  1.00 19.75 ?  90  LYS   B NZ   1 
ATOM   5178 H H    . LYS   B 1 90  ? 48.598 -12.236 -10.653 1.00 14.13 ?  90  LYS   B H    1 
ATOM   5179 H HA   . LYS   B 1 90  ? 49.792 -10.065 -9.823  1.00 14.54 ?  90  LYS   B HA   1 
ATOM   5180 H HB2  . LYS   B 1 90  ? 48.157 -9.905  -11.454 1.00 16.38 ?  90  LYS   B HB2  1 
ATOM   5181 H HB3  . LYS   B 1 90  ? 47.052 -10.369 -10.414 1.00 16.38 ?  90  LYS   B HB3  1 
ATOM   5182 H HG2  . LYS   B 1 90  ? 46.956 -8.073  -10.766 1.00 17.46 ?  90  LYS   B HG2  1 
ATOM   5183 H HG3  . LYS   B 1 90  ? 47.289 -8.390  -9.247  1.00 17.46 ?  90  LYS   B HG3  1 
ATOM   5184 H HD2  . LYS   B 1 90  ? 49.476 -7.801  -9.546  1.00 20.90 ?  90  LYS   B HD2  1 
ATOM   5185 H HD3  . LYS   B 1 90  ? 49.262 -7.665  -11.123 1.00 20.90 ?  90  LYS   B HD3  1 
ATOM   5186 H HE2  . LYS   B 1 90  ? 47.911 -5.839  -10.834 1.00 23.47 ?  90  LYS   B HE2  1 
ATOM   5187 H HE3  . LYS   B 1 90  ? 47.906 -6.040  -9.258  1.00 23.47 ?  90  LYS   B HE3  1 
ATOM   5188 H HZ1  . LYS   B 1 90  ? 49.310 -4.366  -9.841  1.00 23.70 ?  90  LYS   B HZ1  1 
ATOM   5189 H HZ2  . LYS   B 1 90  ? 50.089 -5.431  -9.244  1.00 23.70 ?  90  LYS   B HZ2  1 
ATOM   5190 H HZ3  . LYS   B 1 90  ? 50.094 -5.249  -10.681 1.00 23.70 ?  90  LYS   B HZ3  1 
ATOM   5191 N N    . HIS   B 1 91  ? 47.703 -11.287 -7.731  1.00 10.50 ?  91  HIS   B N    1 
ATOM   5192 C CA   . HIS   B 1 91  ? 47.240 -11.305 -6.356  1.00 10.57 ?  91  HIS   B CA   1 
ATOM   5193 C C    . HIS   B 1 91  ? 47.238 -12.730 -5.832  1.00 10.19 ?  91  HIS   B C    1 
ATOM   5194 O O    . HIS   B 1 91  ? 47.005 -13.683 -6.582  1.00 10.37 ?  91  HIS   B O    1 
ATOM   5195 C CB   . HIS   B 1 91  ? 45.786 -10.830 -6.248  1.00 12.47 ?  91  HIS   B CB   1 
ATOM   5196 C CG   . HIS   B 1 91  ? 45.567 -9.423  -6.688  1.00 15.94 ?  91  HIS   B CG   1 
ATOM   5197 N ND1  . HIS   B 1 91  ? 46.149 -8.344  -6.057  1.00 18.29 ?  91  HIS   B ND1  1 
ATOM   5198 C CD2  . HIS   B 1 91  ? 44.799 -8.912  -7.677  1.00 18.43 ?  91  HIS   B CD2  1 
ATOM   5199 C CE1  . HIS   B 1 91  ? 45.766 -7.229  -6.653  1.00 19.33 ?  91  HIS   B CE1  1 
ATOM   5200 N NE2  . HIS   B 1 91  ? 44.943 -7.546  -7.637  1.00 19.33 ?  91  HIS   B NE2  1 
ATOM   5201 H H    . HIS   B 1 91  ? 47.294 -11.859 -8.229  1.00 12.59 ?  91  HIS   B H    1 
ATOM   5202 H HA   . HIS   B 1 91  ? 47.806 -10.744 -5.796  1.00 12.68 ?  91  HIS   B HA   1 
ATOM   5203 H HB2  . HIS   B 1 91  ? 45.231 -11.403 -6.802  1.00 14.96 ?  91  HIS   B HB2  1 
ATOM   5204 H HB3  . HIS   B 1 91  ? 45.503 -10.900 -5.322  1.00 14.96 ?  91  HIS   B HB3  1 
ATOM   5205 H HD1  . HIS   B 1 91  ? 46.684 -8.393  -5.385  1.00 21.94 ?  91  HIS   B HD1  1 
ATOM   5206 H HD2  . HIS   B 1 91  ? 44.279 -9.388  -8.283  1.00 22.11 ?  91  HIS   B HD2  1 
ATOM   5207 H HE1  . HIS   B 1 91  ? 46.029 -6.368  -6.413  1.00 23.19 ?  91  HIS   B HE1  1 
ATOM   5208 N N    . CYS   B 1 92  ? 47.436 -12.862 -4.527  1.00 9.91  ?  92  CYS   B N    1 
ATOM   5209 C CA   . CYS   B 1 92  ? 47.140 -14.101 -3.821  1.00 9.71  ?  92  CYS   B CA   1 
ATOM   5210 C C    . CYS   B 1 92  ? 45.921 -13.870 -2.936  1.00 9.39  ?  92  CYS   B C    1 
ATOM   5211 O O    . CYS   B 1 92  ? 45.920 -12.970 -2.086  1.00 10.30 ?  92  CYS   B O    1 
ATOM   5212 C CB   . CYS   B 1 92  ? 48.318 -14.559 -2.968  1.00 10.09 ?  92  CYS   B CB   1 
ATOM   5213 S SG   . CYS   B 1 92  ? 47.965 -16.097 -2.070  1.00 10.16 ?  92  CYS   B SG   1 
ATOM   5214 H H    . CYS   B 1 92  ? 47.754 -12.239 -4.020  1.00 11.89 ?  92  CYS   B H    1 
ATOM   5215 H HA   . CYS   B 1 92  ? 46.943 -14.798 -4.468  1.00 11.65 ?  92  CYS   B HA   1 
ATOM   5216 H HB2  . CYS   B 1 92  ? 49.089 -14.710 -3.534  1.00 12.11 ?  92  CYS   B HB2  1 
ATOM   5217 H HB3  . CYS   B 1 92  ? 48.519 -13.870 -2.311  1.00 12.11 ?  92  CYS   B HB3  1 
ATOM   5218 H HG   . CYS   B 1 92  ? 48.931 -16.411 -1.436  1.00 12.19 ?  92  CYS   B HG   1 
ATOM   5219 N N    . LEU   B 1 93  ? 44.884 -14.674 -3.149  1.00 9.25  ?  93  LEU   B N    1 
ATOM   5220 C CA   . LEU   B 1 93  ? 43.711 -14.692 -2.285  1.00 9.46  ?  93  LEU   B CA   1 
ATOM   5221 C C    . LEU   B 1 93  ? 43.937 -15.760 -1.224  1.00 9.04  ?  93  LEU   B C    1 
ATOM   5222 O O    . LEU   B 1 93  ? 43.884 -16.962 -1.519  1.00 9.47  ?  93  LEU   B O    1 
ATOM   5223 C CB   . LEU   B 1 93  ? 42.450 -14.991 -3.092  1.00 9.93  ?  93  LEU   B CB   1 
ATOM   5224 C CG   . LEU   B 1 93  ? 41.148 -15.001 -2.290  1.00 10.19 ?  93  LEU   B CG   1 
ATOM   5225 C CD1  . LEU   B 1 93  ? 40.783 -13.613 -1.807  1.00 10.60 ?  93  LEU   B CD1  1 
ATOM   5226 C CD2  . LEU   B 1 93  ? 40.024 -15.591 -3.122  1.00 10.39 ?  93  LEU   B CD2  1 
ATOM   5227 H H    . LEU   B 1 93  ? 44.839 -15.243 -3.808  1.00 11.10 ?  93  LEU   B H    1 
ATOM   5228 H HA   . LEU   B 1 93  ? 43.616 -13.829 -1.856  1.00 11.35 ?  93  LEU   B HA   1 
ATOM   5229 H HB2  . LEU   B 1 93  ? 42.363 -14.313 -3.782  1.00 11.91 ?  93  LEU   B HB2  1 
ATOM   5230 H HB3  . LEU   B 1 93  ? 42.549 -15.861 -3.503  1.00 11.91 ?  93  LEU   B HB3  1 
ATOM   5231 H HG   . LEU   B 1 93  ? 41.265 -15.563 -1.512  1.00 12.21 ?  93  LEU   B HG   1 
ATOM   5232 H HD11 . LEU   B 1 93  ? 39.931 -13.651 -1.350  1.00 12.71 ?  93  LEU   B HD11 1 
ATOM   5233 H HD12 . LEU   B 1 93  ? 41.473 -13.297 -1.201  1.00 12.71 ?  93  LEU   B HD12 1 
ATOM   5234 H HD13 . LEU   B 1 93  ? 40.722 -13.017 -2.574  1.00 12.71 ?  93  LEU   B HD13 1 
ATOM   5235 H HD21 . LEU   B 1 93  ? 39.208 -15.582 -2.599  1.00 12.46 ?  93  LEU   B HD21 1 
ATOM   5236 H HD22 . LEU   B 1 93  ? 39.910 -15.058 -3.925  1.00 12.46 ?  93  LEU   B HD22 1 
ATOM   5237 H HD23 . LEU   B 1 93  ? 40.253 -16.504 -3.362  1.00 12.46 ?  93  LEU   B HD23 1 
ATOM   5238 N N    . HIS   B 1 94  ? 44.208 -15.323 0.002   1.00 8.93  ?  94  HIS   B N    1 
ATOM   5239 C CA   . HIS   B 1 94  ? 44.429 -16.228 1.124   1.00 9.21  ?  94  HIS   B CA   1 
ATOM   5240 C C    . HIS   B 1 94  ? 43.066 -16.585 1.699   1.00 9.39  ?  94  HIS   B C    1 
ATOM   5241 O O    . HIS   B 1 94  ? 42.393 -15.713 2.251   1.00 10.55 ?  94  HIS   B O    1 
ATOM   5242 C CB   . HIS   B 1 94  ? 45.297 -15.546 2.182   1.00 9.47  ?  94  HIS   B CB   1 
ATOM   5243 C CG   . HIS   B 1 94  ? 46.682 -15.246 1.714   1.00 9.46  ?  94  HIS   B CG   1 
ATOM   5244 N ND1  . HIS   B 1 94  ? 47.707 -16.163 1.797   1.00 9.62  ?  94  HIS   B ND1  1 
ATOM   5245 C CD2  . HIS   B 1 94  ? 47.191 -14.139 1.122   1.00 9.97  ?  94  HIS   B CD2  1 
ATOM   5246 C CE1  . HIS   B 1 94  ? 48.798 -15.613 1.291   1.00 9.68  ?  94  HIS   B CE1  1 
ATOM   5247 N NE2  . HIS   B 1 94  ? 48.513 -14.389 0.872   1.00 10.23 ?  94  HIS   B NE2  1 
ATOM   5248 H H    . HIS   B 1 94  ? 44.278 -14.488 0.213   1.00 10.71 ?  94  HIS   B H    1 
ATOM   5249 H HA   . HIS   B 1 94  ? 44.867 -17.037 0.817   1.00 11.04 ?  94  HIS   B HA   1 
ATOM   5250 H HB2  . HIS   B 1 94  ? 44.880 -14.714 2.437   1.00 11.36 ?  94  HIS   B HB2  1 
ATOM   5251 H HB3  . HIS   B 1 94  ? 45.364 -16.137 2.950   1.00 11.36 ?  94  HIS   B HB3  1 
ATOM   5252 H HD2  . HIS   B 1 94  ? 46.734 -13.357 0.928   1.00 11.95 ?  94  HIS   B HD2  1 
ATOM   5253 H HE1  . HIS   B 1 94  ? 49.634 -16.028 1.237   1.00 11.60 ?  94  HIS   B HE1  1 
ATOM   5254 H HE2  . HIS   B 1 94  ? 49.072 -13.846 0.512   1.00 12.27 ?  94  HIS   B HE2  1 
ATOM   5255 N N    . VAL   B 1 95  ? 42.638 -17.842 1.547   1.00 9.24  ?  95  VAL   B N    1 
ATOM   5256 C CA   . VAL   B 1 95  ? 41.313 -18.284 1.980   1.00 9.54  ?  95  VAL   B CA   1 
ATOM   5257 C C    . VAL   B 1 95  ? 41.484 -19.320 3.075   1.00 9.87  ?  95  VAL   B C    1 
ATOM   5258 O O    . VAL   B 1 95  ? 42.256 -20.272 2.913   1.00 10.21 ?  95  VAL   B O    1 
ATOM   5259 C CB   . VAL   B 1 95  ? 40.497 -18.888 0.820   1.00 9.94  ?  95  VAL   B CB   1 
ATOM   5260 C CG1  . VAL   B 1 95  ? 39.119 -19.335 1.305   1.00 11.06 ?  95  VAL   B CG1  1 
ATOM   5261 C CG2  . VAL   B 1 95  ? 40.376 -17.903 -0.329  1.00 10.03 ?  95  VAL   B CG2  1 
ATOM   5262 H H    . VAL   B 1 95  ? 43.099 -18.468 1.179   1.00 11.08 ?  95  VAL   B H    1 
ATOM   5263 H HA   . VAL   B 1 95  ? 40.818 -17.532 2.343   1.00 11.45 ?  95  VAL   B HA   1 
ATOM   5264 H HB   . VAL   B 1 95  ? 40.954 -19.666 0.485   1.00 11.92 ?  95  VAL   B HB   1 
ATOM   5265 H HG11 . VAL   B 1 95  ? 38.558 -19.532 0.530   1.00 13.26 ?  95  VAL   B HG11 1 
ATOM   5266 H HG12 . VAL   B 1 95  ? 39.213 -20.134 1.844   1.00 13.26 ?  95  VAL   B HG12 1 
ATOM   5267 H HG13 . VAL   B 1 95  ? 38.712 -18.626 1.825   1.00 13.26 ?  95  VAL   B HG13 1 
ATOM   5268 H HG21 . VAL   B 1 95  ? 39.801 -18.285 -1.013  1.00 12.02 ?  95  VAL   B HG21 1 
ATOM   5269 H HG22 . VAL   B 1 95  ? 39.989 -17.076 0.000   1.00 12.02 ?  95  VAL   B HG22 1 
ATOM   5270 H HG23 . VAL   B 1 95  ? 41.257 -17.736 -0.692  1.00 12.02 ?  95  VAL   B HG23 1 
ATOM   5271 N N    . VAL   B 1 96  ? 40.742 -19.153 4.166   1.00 10.05 ?  96  VAL   B N    1 
ATOM   5272 C CA   . VAL   B 1 96  ? 40.819 -20.065 5.305   1.00 10.59 ?  96  VAL   B CA   1 
ATOM   5273 C C    . VAL   B 1 96  ? 39.630 -21.021 5.255   1.00 10.98 ?  96  VAL   B C    1 
ATOM   5274 O O    . VAL   B 1 96  ? 38.508 -20.664 5.625   1.00 11.90 ?  96  VAL   B O    1 
ATOM   5275 C CB   . VAL   B 1 96  ? 40.874 -19.318 6.640   1.00 11.09 ?  96  VAL   B CB   1 
ATOM   5276 C CG1  . VAL   B 1 96  ? 41.049 -20.316 7.784   1.00 12.05 ?  96  VAL   B CG1  1 
ATOM   5277 C CG2  . VAL   B 1 96  ? 41.993 -18.277 6.646   1.00 12.01 ?  96  VAL   B CG2  1 
ATOM   5278 H H    . VAL   B 1 96  ? 40.179 -18.514 4.274   1.00 12.06 ?  96  VAL   B H    1 
ATOM   5279 H HA   . VAL   B 1 96  ? 41.628 -20.595 5.233   1.00 12.71 ?  96  VAL   B HA   1 
ATOM   5280 H HB   . VAL   B 1 96  ? 40.033 -18.852 6.779   1.00 13.30 ?  96  VAL   B HB   1 
ATOM   5281 H HG11 . VAL   B 1 96  ? 41.241 -19.829 8.603   1.00 14.45 ?  96  VAL   B HG11 1 
ATOM   5282 H HG12 . VAL   B 1 96  ? 40.232 -20.827 7.890   1.00 14.45 ?  96  VAL   B HG12 1 
ATOM   5283 H HG13 . VAL   B 1 96  ? 41.788 -20.909 7.576   1.00 14.45 ?  96  VAL   B HG13 1 
ATOM   5284 H HG21 . VAL   B 1 96  ? 42.041 -17.867 7.527   1.00 14.41 ?  96  VAL   B HG21 1 
ATOM   5285 H HG22 . VAL   B 1 96  ? 42.833 -18.711 6.439   1.00 14.41 ?  96  VAL   B HG22 1 
ATOM   5286 H HG23 . VAL   B 1 96  ? 41.798 -17.596 5.981   1.00 14.41 ?  96  VAL   B HG23 1 
ATOM   5287 N N    . GLY   B 1 97  ? 39.869 -22.256 4.825   1.00 10.80 ?  97  GLY   B N    1 
ATOM   5288 C CA   . GLY   B 1 97  ? 38.899 -23.313 4.984   1.00 11.56 ?  97  GLY   B CA   1 
ATOM   5289 C C    . GLY   B 1 97  ? 39.008 -23.925 6.365   1.00 12.07 ?  97  GLY   B C    1 
ATOM   5290 O O    . GLY   B 1 97  ? 40.042 -23.799 7.034   1.00 12.44 ?  97  GLY   B O    1 
ATOM   5291 H H    . GLY   B 1 97  ? 40.602 -22.501 4.439   1.00 12.95 ?  97  GLY   B H    1 
ATOM   5292 H HA2  . GLY   B 1 97  ? 38.008 -22.951 4.860   1.00 13.87 ?  97  GLY   B HA2  1 
ATOM   5293 H HA3  . GLY   B 1 97  ? 39.053 -24.001 4.316   1.00 13.87 ?  97  GLY   B HA3  1 
ATOM   5294 N N    . PRO   B 1 98  ? 37.955 -24.605 6.821   1.00 12.49 ?  98  PRO   B N    1 
ATOM   5295 C CA   . PRO   B 1 98  ? 38.040 -25.304 8.107   1.00 13.55 ?  98  PRO   B CA   1 
ATOM   5296 C C    . PRO   B 1 98  ? 39.073 -26.421 8.068   1.00 12.86 ?  98  PRO   B C    1 
ATOM   5297 O O    . PRO   B 1 98  ? 39.186 -27.159 7.088   1.00 13.20 ?  98  PRO   B O    1 
ATOM   5298 C CB   . PRO   B 1 98  ? 36.621 -25.850 8.298   1.00 13.89 ?  98  PRO   B CB   1 
ATOM   5299 C CG   . PRO   B 1 98  ? 36.080 -25.984 6.911   1.00 13.22 ?  98  PRO   B CG   1 
ATOM   5300 C CD   . PRO   B 1 98  ? 36.649 -24.806 6.169   1.00 12.68 ?  98  PRO   B CD   1 
ATOM   5301 H HA   . PRO   B 1 98  ? 38.254 -24.679 8.816   1.00 16.25 ?  98  PRO   B HA   1 
ATOM   5302 H HB2  . PRO   B 1 98  ? 36.664 -26.713 8.737   1.00 16.66 ?  98  PRO   B HB2  1 
ATOM   5303 H HB3  . PRO   B 1 98  ? 36.097 -25.221 8.813   1.00 16.66 ?  98  PRO   B HB3  1 
ATOM   5304 H HG2  . PRO   B 1 98  ? 36.386 -26.820 6.517   1.00 15.86 ?  98  PRO   B HG2  1 
ATOM   5305 H HG3  . PRO   B 1 98  ? 35.113 -25.946 6.930   1.00 15.86 ?  98  PRO   B HG3  1 
ATOM   5306 H HD2  . PRO   B 1 98  ? 36.765 -25.017 5.224   1.00 15.21 ?  98  PRO   B HD2  1 
ATOM   5307 H HD3  . PRO   B 1 98  ? 36.092 -24.021 6.287   1.00 15.21 ?  98  PRO   B HD3  1 
ATOM   5308 N N    . ASN   B 1 99  ? 39.823 -26.547 9.157   1.00 13.39 ?  99  ASN   B N    1 
ATOM   5309 C CA   . ASN   B 1 99  ? 40.806 -27.616 9.318   1.00 14.24 ?  99  ASN   B CA   1 
ATOM   5310 C C    . ASN   B 1 99  ? 40.169 -28.698 10.188  1.00 16.29 ?  99  ASN   B C    1 
ATOM   5311 O O    . ASN   B 1 99  ? 40.076 -28.553 11.409  1.00 17.03 ?  99  ASN   B O    1 
ATOM   5312 C CB   . ASN   B 1 99  ? 42.080 -27.061 9.944   1.00 15.11 ?  99  ASN   B CB   1 
ATOM   5313 C CG   . ASN   B 1 99  ? 43.203 -28.071 9.962   1.00 16.20 ?  99  ASN   B CG   1 
ATOM   5314 O OD1  . ASN   B 1 99  ? 42.965 -29.264 10.121  1.00 16.65 ?  99  ASN   B OD1  1 
ATOM   5315 N ND2  . ASN   B 1 99  ? 44.433 -27.603 9.800   1.00 16.61 ?  99  ASN   B ND2  1 
ATOM   5316 H H    . ASN   B 1 99  ? 39.788 -26.007 9.828   1.00 16.07 ?  99  ASN   B H    1 
ATOM   5317 H HA   . ASN   B 1 99  ? 41.022 -27.998 8.452   1.00 17.09 ?  99  ASN   B HA   1 
ATOM   5318 H HB2  . ASN   B 1 99  ? 42.375 -26.293 9.438   1.00 18.12 ?  99  ASN   B HB2  1 
ATOM   5319 H HB3  . ASN   B 1 99  ? 41.892 -26.806 10.862  1.00 18.12 ?  99  ASN   B HB3  1 
ATOM   5320 H HD21 . ASN   B 1 99  ? 45.105 -28.141 9.800   1.00 19.93 ?  99  ASN   B HD21 1 
ATOM   5321 H HD22 . ASN   B 1 99  ? 44.557 -26.760 9.694   1.00 19.93 ?  99  ASN   B HD22 1 
ATOM   5322 N N    A VAL   B 1 100 ? 39.699 -29.773 9.546   0.40 18.00 ?  100 VAL   B N    1 
ATOM   5323 N N    B VAL   B 1 100 ? 39.711 -29.776 9.544   0.60 17.82 ?  100 VAL   B N    1 
ATOM   5324 C CA   A VAL   B 1 100 ? 39.074 -30.870 10.283  0.40 20.43 ?  100 VAL   B CA   1 
ATOM   5325 C CA   B VAL   B 1 100 ? 39.080 -30.881 10.262  0.60 20.40 ?  100 VAL   B CA   1 
ATOM   5326 C C    A VAL   B 1 100 ? 40.071 -31.534 11.224  0.40 21.09 ?  100 VAL   B C    1 
ATOM   5327 C C    B VAL   B 1 100 ? 40.065 -31.558 11.204  0.60 21.01 ?  100 VAL   B C    1 
ATOM   5328 O O    A VAL   B 1 100 ? 39.692 -32.028 12.293  0.40 21.58 ?  100 VAL   B O    1 
ATOM   5329 O O    B VAL   B 1 100 ? 39.672 -32.094 12.247  0.60 21.45 ?  100 VAL   B O    1 
ATOM   5330 C CB   A VAL   B 1 100 ? 38.435 -31.882 9.309   0.40 22.28 ?  100 VAL   B CB   1 
ATOM   5331 C CB   B VAL   B 1 100 ? 38.473 -31.880 9.258   0.60 22.56 ?  100 VAL   B CB   1 
ATOM   5332 C CG1  A VAL   B 1 100 ? 37.957 -33.120 10.057  0.40 22.89 ?  100 VAL   B CG1  1 
ATOM   5333 C CG1  B VAL   B 1 100 ? 37.997 -33.138 9.971   0.60 23.36 ?  100 VAL   B CG1  1 
ATOM   5334 C CG2  A VAL   B 1 100 ? 37.280 -31.242 8.558   0.40 22.78 ?  100 VAL   B CG2  1 
ATOM   5335 C CG2  B VAL   B 1 100 ? 37.332 -31.233 8.500   0.60 23.15 ?  100 VAL   B CG2  1 
ATOM   5336 H H    A VAL   B 1 100 ? 39.719 -29.879 8.692   0.40 21.60 ?  100 VAL   B H    1 
ATOM   5337 H H    B VAL   B 1 100 ? 39.743 -29.879 8.690   0.60 21.37 ?  100 VAL   B H    1 
ATOM   5338 H HA   A VAL   B 1 100 ? 38.357 -30.504 10.824  0.40 24.51 ?  100 VAL   B HA   1 
ATOM   5339 H HA   B VAL   B 1 100 ? 38.351 -30.526 10.796  0.60 24.47 ?  100 VAL   B HA   1 
ATOM   5340 H HB   A VAL   B 1 100 ? 39.099 -32.162 8.662   0.40 26.73 ?  100 VAL   B HB   1 
ATOM   5341 H HB   B VAL   B 1 100 ? 39.155 -32.138 8.619   0.60 27.07 ?  100 VAL   B HB   1 
ATOM   5342 H HG11 A VAL   B 1 100 ? 37.368 -33.629 9.477   0.40 27.46 ?  100 VAL   B HG11 1 
ATOM   5343 H HG11 B VAL   B 1 100 ? 37.420 -33.638 9.373   0.60 28.03 ?  100 VAL   B HG11 1 
ATOM   5344 H HG12 A VAL   B 1 100 ? 38.723 -33.661 10.303  0.40 27.46 ?  100 VAL   B HG12 1 
ATOM   5345 H HG12 B VAL   B 1 100 ? 38.765 -33.679 10.215  0.60 28.03 ?  100 VAL   B HG12 1 
ATOM   5346 H HG13 A VAL   B 1 100 ? 37.475 -32.844 10.852  0.40 27.46 ?  100 VAL   B HG13 1 
ATOM   5347 H HG13 B VAL   B 1 100 ? 37.504 -32.884 10.767  0.60 28.03 ?  100 VAL   B HG13 1 
ATOM   5348 H HG21 A VAL   B 1 100 ? 36.896 -31.898 7.954   0.40 27.33 ?  100 VAL   B HG21 1 
ATOM   5349 H HG21 B VAL   B 1 100 ? 36.955 -31.883 7.887   0.60 27.77 ?  100 VAL   B HG21 1 
ATOM   5350 H HG22 A VAL   B 1 100 ? 36.611 -30.949 9.197   0.40 27.33 ?  100 VAL   B HG22 1 
ATOM   5351 H HG22 B VAL   B 1 100 ? 36.656 -30.945 9.134   0.60 27.77 ?  100 VAL   B HG22 1 
ATOM   5352 H HG23 A VAL   B 1 100 ? 37.613 -30.484 8.055   0.40 27.33 ?  100 VAL   B HG23 1 
ATOM   5353 H HG23 B VAL   B 1 100 ? 37.672 -30.471 8.008   0.60 27.77 ?  100 VAL   B HG23 1 
ATOM   5354 N N    . ASN   B 1 101 ? 41.351 -31.574 10.843  1.00 21.40 ?  101 ASN   B N    1 
ATOM   5355 C CA   . ASN   B 1 101 ? 42.372 -32.115 11.737  1.00 23.91 ?  101 ASN   B CA   1 
ATOM   5356 C C    . ASN   B 1 101 ? 42.520 -31.289 13.011  1.00 26.03 ?  101 ASN   B C    1 
ATOM   5357 O O    . ASN   B 1 101 ? 43.052 -31.798 14.006  1.00 26.88 ?  101 ASN   B O    1 
ATOM   5358 C CB   . ASN   B 1 101 ? 43.711 -32.248 11.005  1.00 24.04 ?  101 ASN   B CB   1 
ATOM   5359 C CG   . ASN   B 1 101 ? 43.710 -33.381 9.992   1.00 23.99 ?  101 ASN   B CG   1 
ATOM   5360 O OD1  . ASN   B 1 101 ? 43.046 -34.392 10.186  1.00 25.24 ?  101 ASN   B OD1  1 
ATOM   5361 N ND2  . ASN   B 1 101 ? 44.449 -33.211 8.904   1.00 23.79 ?  101 ASN   B ND2  1 
ATOM   5362 H H    A ASN   B 1 101 ? 41.642 -31.310 10.076  0.40 25.67 ?  101 ASN   B H    1 
ATOM   5363 H H    B ASN   B 1 101 ? 41.648 -31.293 10.085  0.60 25.67 ?  101 ASN   B H    1 
ATOM   5364 H HA   . ASN   B 1 101 ? 42.103 -33.001 12.004  1.00 28.68 ?  101 ASN   B HA   1 
ATOM   5365 H HB2  . ASN   B 1 101 ? 43.905 -31.428 10.527  1.00 28.84 ?  101 ASN   B HB2  1 
ATOM   5366 H HB3  . ASN   B 1 101 ? 44.410 -32.427 11.654  1.00 28.84 ?  101 ASN   B HB3  1 
ATOM   5367 H HD21 . ASN   B 1 101 ? 44.480 -33.829 8.304   1.00 28.55 ?  101 ASN   B HD21 1 
ATOM   5368 H HD22 . ASN   B 1 101 ? 44.895 -32.486 8.797   1.00 28.55 ?  101 ASN   B HD22 1 
ATOM   5369 N N    A LYS   B 1 102 ? 42.080 -30.030 12.996  0.40 27.35 ?  102 LYS   B N    1 
ATOM   5370 N N    B LYS   B 1 102 ? 42.049 -30.040 13.007  0.60 27.13 ?  102 LYS   B N    1 
ATOM   5371 C CA   A LYS   B 1 102 ? 42.074 -29.180 14.180  0.40 28.92 ?  102 LYS   B CA   1 
ATOM   5372 C CA   B LYS   B 1 102 ? 41.998 -29.205 14.201  0.60 28.63 ?  102 LYS   B CA   1 
ATOM   5373 C C    A LYS   B 1 102 ? 40.713 -29.152 14.864  0.40 28.50 ?  102 LYS   B C    1 
ATOM   5374 C C    B LYS   B 1 102 ? 40.620 -29.200 14.853  0.60 27.93 ?  102 LYS   B C    1 
ATOM   5375 O O    A LYS   B 1 102 ? 40.516 -28.370 15.799  0.40 28.81 ?  102 LYS   B O    1 
ATOM   5376 O O    B LYS   B 1 102 ? 40.404 -28.454 15.813  0.60 28.51 ?  102 LYS   B O    1 
ATOM   5377 C CB   A LYS   B 1 102 ? 42.485 -27.751 13.816  0.40 30.81 ?  102 LYS   B CB   1 
ATOM   5378 C CB   B LYS   B 1 102 ? 42.387 -27.763 13.865  0.60 30.81 ?  102 LYS   B CB   1 
ATOM   5379 C CG   A LYS   B 1 102 ? 43.951 -27.568 13.461  0.40 32.68 ?  102 LYS   B CG   1 
ATOM   5380 C CG   B LYS   B 1 102 ? 43.834 -27.553 13.462  0.60 33.03 ?  102 LYS   B CG   1 
ATOM   5381 C CD   A LYS   B 1 102 ? 44.236 -26.110 13.126  0.40 34.11 ?  102 LYS   B CD   1 
ATOM   5382 C CD   B LYS   B 1 102 ? 44.050 -26.110 13.030  0.60 34.73 ?  102 LYS   B CD   1 
ATOM   5383 C CE   A LYS   B 1 102 ? 45.704 -25.872 12.814  0.40 35.18 ?  102 LYS   B CE   1 
ATOM   5384 C CE   B LYS   B 1 102 ? 45.511 -25.808 12.760  0.60 35.99 ?  102 LYS   B CE   1 
ATOM   5385 N NZ   A LYS   B 1 102 ? 45.966 -24.447 12.460  0.40 35.80 ?  102 LYS   B NZ   1 
ATOM   5386 N NZ   B LYS   B 1 102 ? 45.706 -24.396 12.326  0.60 36.72 ?  102 LYS   B NZ   1 
ATOM   5387 H H    A LYS   B 1 102 ? 41.768 -29.639 12.295  0.40 32.81 ?  102 LYS   B H    1 
ATOM   5388 H H    B LYS   B 1 102 ? 41.747 -29.645 12.303  0.60 32.54 ?  102 LYS   B H    1 
ATOM   5389 H HA   A LYS   B 1 102 ? 42.725 -29.521 14.812  0.40 34.69 ?  102 LYS   B HA   1 
ATOM   5390 H HA   B LYS   B 1 102 ? 42.636 -29.544 14.848  0.60 34.35 ?  102 LYS   B HA   1 
ATOM   5391 H HB2  A LYS   B 1 102 ? 41.963 -27.463 13.053  0.40 36.97 ?  102 LYS   B HB2  1 
ATOM   5392 H HB2  B LYS   B 1 102 ? 41.833 -27.456 13.130  0.60 36.97 ?  102 LYS   B HB2  1 
ATOM   5393 H HB3  A LYS   B 1 102 ? 42.298 -27.174 14.574  0.40 36.97 ?  102 LYS   B HB3  1 
ATOM   5394 H HB3  B LYS   B 1 102 ? 42.221 -27.209 14.646  0.60 36.97 ?  102 LYS   B HB3  1 
ATOM   5395 H HG2  A LYS   B 1 102 ? 44.504 -27.822 14.217  0.40 39.20 ?  102 LYS   B HG2  1 
ATOM   5396 H HG2  B LYS   B 1 102 ? 44.415 -27.737 14.218  0.60 39.62 ?  102 LYS   B HG2  1 
ATOM   5397 H HG3  A LYS   B 1 102 ? 44.168 -28.109 12.686  0.40 39.20 ?  102 LYS   B HG3  1 
ATOM   5398 H HG3  B LYS   B 1 102 ? 44.053 -28.133 12.716  0.60 39.62 ?  102 LYS   B HG3  1 
ATOM   5399 H HD2  A LYS   B 1 102 ? 43.716 -25.854 12.348  0.40 40.92 ?  102 LYS   B HD2  1 
ATOM   5400 H HD2  B LYS   B 1 102 ? 43.551 -25.943 12.214  0.60 41.67 ?  102 LYS   B HD2  1 
ATOM   5401 H HD3  A LYS   B 1 102 ? 43.995 -25.555 13.885  0.40 40.92 ?  102 LYS   B HD3  1 
ATOM   5402 H HD3  B LYS   B 1 102 ? 43.743 -25.517 13.735  0.60 41.67 ?  102 LYS   B HD3  1 
ATOM   5403 H HE2  A LYS   B 1 102 ? 46.237 -26.094 13.594  0.40 42.21 ?  102 LYS   B HE2  1 
ATOM   5404 H HE2  B LYS   B 1 102 ? 46.022 -25.950 13.573  0.60 43.19 ?  102 LYS   B HE2  1 
ATOM   5405 H HE3  A LYS   B 1 102 ? 45.964 -26.425 12.061  0.40 42.21 ?  102 LYS   B HE3  1 
ATOM   5406 H HE3  B LYS   B 1 102 ? 45.833 -26.392 12.056  0.60 43.19 ?  102 LYS   B HE3  1 
ATOM   5407 H HZ1  A LYS   B 1 102 ? 46.830 -24.332 12.282  0.40 42.95 ?  102 LYS   B HZ1  1 
ATOM   5408 H HZ1  B LYS   B 1 102 ? 46.569 -24.242 12.174  0.60 44.05 ?  102 LYS   B HZ1  1 
ATOM   5409 H HZ2  A LYS   B 1 102 ? 45.490 -24.219 11.743  0.40 42.95 ?  102 LYS   B HZ2  1 
ATOM   5410 H HZ2  B LYS   B 1 102 ? 45.248 -24.243 11.578  0.60 44.05 ?  102 LYS   B HZ2  1 
ATOM   5411 H HZ3  A LYS   B 1 102 ? 45.738 -23.918 13.139  0.40 42.95 ?  102 LYS   B HZ3  1 
ATOM   5412 H HZ3  B LYS   B 1 102 ? 45.420 -23.841 12.960  0.60 44.05 ?  102 LYS   B HZ3  1 
ATOM   5413 N N    A GLY   B 1 103 ? 39.770 -29.976 14.413  0.40 27.87 ?  103 GLY   B N    1 
ATOM   5414 N N    B GLY   B 1 103 ? 39.680 -29.994 14.348  0.60 26.87 ?  103 GLY   B N    1 
ATOM   5415 C CA   A GLY   B 1 103 ? 38.441 -30.005 14.989  0.40 27.51 ?  103 GLY   B CA   1 
ATOM   5416 C CA   B GLY   B 1 103 ? 38.348 -30.039 14.916  0.60 26.27 ?  103 GLY   B CA   1 
ATOM   5417 C C    A GLY   B 1 103 ? 37.507 -28.920 14.504  0.40 26.84 ?  103 GLY   B C    1 
ATOM   5418 C C    B GLY   B 1 103 ? 37.417 -28.935 14.468  0.60 25.09 ?  103 GLY   B C    1 
ATOM   5419 O O    A GLY   B 1 103 ? 36.394 -28.803 15.032  0.40 27.10 ?  103 GLY   B O    1 
ATOM   5420 O O    B GLY   B 1 103 ? 36.355 -28.758 15.075  0.60 25.64 ?  103 GLY   B O    1 
ATOM   5421 H H    A GLY   B 1 103 ? 39.882 -30.533 13.770  0.40 33.44 ?  103 GLY   B H    1 
ATOM   5422 H H    B GLY   B 1 103 ? 39.792 -30.518 13.676  0.60 32.24 ?  103 GLY   B H    1 
ATOM   5423 H HA2  A GLY   B 1 103 ? 38.036 -30.864 14.791  0.40 33.00 ?  103 GLY   B HA2  1 
ATOM   5424 H HA2  B GLY   B 1 103 ? 37.939 -30.887 14.685  0.60 31.52 ?  103 GLY   B HA2  1 
ATOM   5425 H HA3  A GLY   B 1 103 ? 38.514 -29.924 15.952  0.40 33.00 ?  103 GLY   B HA3  1 
ATOM   5426 H HA3  B GLY   B 1 103 ? 38.419 -29.996 15.884  0.60 31.52 ?  103 GLY   B HA3  1 
ATOM   5427 N N    A GLU   B 1 104 ? 37.915 -28.123 13.520  0.40 25.79 ?  104 GLU   B N    1 
ATOM   5428 N N    B GLU   B 1 104 ? 37.772 -28.189 13.426  0.60 23.02 ?  104 GLU   B N    1 
ATOM   5429 C CA   A GLU   B 1 104 ? 37.075 -27.036 13.043  0.40 24.76 ?  104 GLU   B CA   1 
ATOM   5430 C CA   B GLU   B 1 104 ? 36.937 -27.088 12.969  0.60 21.15 ?  104 GLU   B CA   1 
ATOM   5431 C C    A GLU   B 1 104 ? 35.895 -27.579 12.237  0.40 24.83 ?  104 GLU   B C    1 
ATOM   5432 C C    B GLU   B 1 104 ? 35.774 -27.609 12.129  0.60 21.22 ?  104 GLU   B C    1 
ATOM   5433 O O    A GLU   B 1 104 ? 35.938 -28.676 11.674  0.40 25.09 ?  104 GLU   B O    1 
ATOM   5434 O O    B GLU   B 1 104 ? 35.845 -28.682 11.523  0.60 22.51 ?  104 GLU   B O    1 
ATOM   5435 C CB   A GLU   B 1 104 ? 37.909 -26.044 12.229  0.40 23.90 ?  104 GLU   B CB   1 
ATOM   5436 C CB   B GLU   B 1 104 ? 37.782 -26.074 12.197  0.60 19.99 ?  104 GLU   B CB   1 
ATOM   5437 C CG   A GLU   B 1 104 ? 39.002 -25.381 13.063  0.40 23.17 ?  104 GLU   B CG   1 
ATOM   5438 C CG   B GLU   B 1 104 ? 38.851 -25.439 13.082  0.60 18.94 ?  104 GLU   B CG   1 
ATOM   5439 C CD   A GLU   B 1 104 ? 39.931 -24.499 12.250  0.40 22.56 ?  104 GLU   B CD   1 
ATOM   5440 C CD   B GLU   B 1 104 ? 39.856 -24.580 12.340  0.60 17.64 ?  104 GLU   B CD   1 
ATOM   5441 O OE1  A GLU   B 1 104 ? 39.906 -24.574 11.003  0.40 21.73 ?  104 GLU   B OE1  1 
ATOM   5442 O OE1  B GLU   B 1 104 ? 39.877 -24.569 11.089  0.60 16.23 ?  104 GLU   B OE1  1 
ATOM   5443 O OE2  A GLU   B 1 104 ? 40.693 -23.725 12.867  0.40 23.14 -1 104 GLU   B OE2  1 
ATOM   5444 O OE2  B GLU   B 1 104 ? 40.646 -23.916 13.040  0.60 18.34 -1 104 GLU   B OE2  1 
ATOM   5445 H H    A GLU   B 1 104 ? 38.674 -28.187 13.121  0.40 30.94 ?  104 GLU   B H    1 
ATOM   5446 H H    B GLU   B 1 104 ? 38.494 -28.299 12.974  0.60 27.62 ?  104 GLU   B H    1 
ATOM   5447 H HA   A GLU   B 1 104 ? 36.718 -26.561 13.807  0.40 29.70 ?  104 GLU   B HA   1 
ATOM   5448 H HA   B GLU   B 1 104 ? 36.566 -26.638 13.743  0.60 25.38 ?  104 GLU   B HA   1 
ATOM   5449 H HB2  A GLU   B 1 104 ? 38.336 -26.511 11.494  0.40 28.67 ?  104 GLU   B HB2  1 
ATOM   5450 H HB2  B GLU   B 1 104 ? 38.224 -26.521 11.460  0.60 23.98 ?  104 GLU   B HB2  1 
ATOM   5451 H HB3  A GLU   B 1 104 ? 37.329 -25.345 11.887  0.40 28.67 ?  104 GLU   B HB3  1 
ATOM   5452 H HB3  B GLU   B 1 104 ? 37.204 -25.369 11.864  0.60 23.98 ?  104 GLU   B HB3  1 
ATOM   5453 H HG2  A GLU   B 1 104 ? 38.587 -24.828 13.745  0.40 27.80 ?  104 GLU   B HG2  1 
ATOM   5454 H HG2  B GLU   B 1 104 ? 38.416 -24.881 13.749  0.60 22.72 ?  104 GLU   B HG2  1 
ATOM   5455 H HG3  A GLU   B 1 104 ? 39.540 -26.070 13.486  0.40 27.80 ?  104 GLU   B HG3  1 
ATOM   5456 H HG3  B GLU   B 1 104 ? 39.356 -26.139 13.522  0.60 22.72 ?  104 GLU   B HG3  1 
ATOM   5457 N N    A ASP   B 1 105 ? 34.824 -26.787 12.196  0.40 25.01 ?  105 ASP   B N    1 
ATOM   5458 N N    B ASP   B 1 105 ? 34.692 -26.834 12.107  0.60 21.04 ?  105 ASP   B N    1 
ATOM   5459 C CA   A ASP   B 1 105 ? 33.545 -27.238 11.661  0.40 25.44 ?  105 ASP   B CA   1 
ATOM   5460 C CA   B ASP   B 1 105 ? 33.421 -27.301 11.565  0.60 21.61 ?  105 ASP   B CA   1 
ATOM   5461 C C    A ASP   B 1 105 ? 33.594 -27.286 10.137  0.40 24.33 ?  105 ASP   B C    1 
ATOM   5462 C C    B ASP   B 1 105 ? 33.467 -27.321 10.041  0.60 20.12 ?  105 ASP   B C    1 
ATOM   5463 O O    A ASP   B 1 105 ? 33.797 -26.258 9.482   0.40 24.12 ?  105 ASP   B O    1 
ATOM   5464 O O    B ASP   B 1 105 ? 33.587 -26.270 9.401   0.60 19.34 ?  105 ASP   B O    1 
ATOM   5465 C CB   A ASP   B 1 105 ? 32.436 -26.298 12.129  0.40 26.98 ?  105 ASP   B CB   1 
ATOM   5466 C CB   B ASP   B 1 105 ? 32.284 -26.407 12.057  0.60 23.83 ?  105 ASP   B CB   1 
ATOM   5467 C CG   A ASP   B 1 105 ? 31.063 -26.736 11.662  0.40 28.17 ?  105 ASP   B CG   1 
ATOM   5468 C CG   B ASP   B 1 105 ? 30.914 -26.994 11.765  0.60 25.35 ?  105 ASP   B CG   1 
ATOM   5469 O OD1  A ASP   B 1 105 ? 30.930 -27.882 11.184  0.40 28.58 ?  105 ASP   B OD1  1 
ATOM   5470 O OD1  B ASP   B 1 105 ? 30.826 -27.944 10.958  0.60 25.87 ?  105 ASP   B OD1  1 
ATOM   5471 O OD2  A ASP   B 1 105 ? 30.119 -25.925 11.761  0.40 28.74 -1 105 ASP   B OD2  1 
ATOM   5472 O OD2  B ASP   B 1 105 ? 29.923 -26.513 12.355  0.60 25.99 -1 105 ASP   B OD2  1 
ATOM   5473 H H    A ASP   B 1 105 ? 34.816 -25.974 12.476  0.40 30.01 ?  105 ASP   B H    1 
ATOM   5474 H H    B ASP   B 1 105 ? 34.673 -26.025 12.394  0.60 25.24 ?  105 ASP   B H    1 
ATOM   5475 H HA   A ASP   B 1 105 ? 33.352 -28.130 11.991  0.40 30.52 ?  105 ASP   B HA   1 
ATOM   5476 H HA   B ASP   B 1 105 ? 33.252 -28.203 11.873  0.60 25.92 ?  105 ASP   B HA   1 
ATOM   5477 H HB2  A ASP   B 1 105 ? 32.445 -26.259 13.102  0.40 32.36 ?  105 ASP   B HB2  1 
ATOM   5478 H HB2  B ASP   B 1 105 ? 32.366 -26.292 13.018  0.60 28.59 ?  105 ASP   B HB2  1 
ATOM   5479 H HB3  A ASP   B 1 105 ? 32.591 -25.416 11.763  0.40 32.36 ?  105 ASP   B HB3  1 
ATOM   5480 H HB3  B ASP   B 1 105 ? 32.346 -25.542 11.617  0.60 28.59 ?  105 ASP   B HB3  1 
ATOM   5481 N N    A ILE   B 1 106 ? 33.389 -28.481 9.576   0.40 23.81 ?  106 ILE   B N    1 
ATOM   5482 N N    B ILE   B 1 106 ? 33.351 -28.521 9.464   0.60 20.08 ?  106 ILE   B N    1 
ATOM   5483 C CA   A ILE   B 1 106 ? 33.396 -28.662 8.129   0.40 23.13 ?  106 ILE   B CA   1 
ATOM   5484 C CA   B ILE   B 1 106 ? 33.337 -28.683 8.015   0.60 19.58 ?  106 ILE   B CA   1 
ATOM   5485 C C    A ILE   B 1 106 ? 32.301 -27.850 7.446   0.40 22.34 ?  106 ILE   B C    1 
ATOM   5486 C C    B ILE   B 1 106 ? 32.238 -27.853 7.363   0.60 18.72 ?  106 ILE   B C    1 
ATOM   5487 O O    A ILE   B 1 106 ? 32.404 -27.555 6.251   0.40 21.96 ?  106 ILE   B O    1 
ATOM   5488 O O    B ILE   B 1 106 ? 32.336 -27.516 6.178   0.60 17.62 ?  106 ILE   B O    1 
ATOM   5489 C CB   A ILE   B 1 106 ? 33.292 -30.168 7.793   0.40 23.46 ?  106 ILE   B CB   1 
ATOM   5490 C CB   B ILE   B 1 106 ? 33.228 -30.186 7.663   0.60 20.82 ?  106 ILE   B CB   1 
ATOM   5491 C CG1  A ILE   B 1 106 ? 33.533 -30.417 6.302   0.40 23.55 ?  106 ILE   B CG1  1 
ATOM   5492 C CG1  B ILE   B 1 106 ? 33.533 -30.428 6.185   0.60 21.49 ?  106 ILE   B CG1  1 
ATOM   5493 C CG2  A ILE   B 1 106 ? 31.935 -30.720 8.210   0.40 23.86 ?  106 ILE   B CG2  1 
ATOM   5494 C CG2  B ILE   B 1 106 ? 31.847 -30.725 8.014   0.60 21.58 ?  106 ILE   B CG2  1 
ATOM   5495 C CD1  A ILE   B 1 106 ? 34.893 -29.968 5.821   0.40 23.54 ?  106 ILE   B CD1  1 
ATOM   5496 C CD1  B ILE   B 1 106 ? 34.914 -29.978 5.773   0.60 21.76 ?  106 ILE   B CD1  1 
ATOM   5497 H H    A ILE   B 1 106 ? 33.252 -29.203 10.018  0.40 28.57 ?  106 ILE   B H    1 
ATOM   5498 H H    B ILE   B 1 106 ? 33.286 -29.258 9.897   0.60 24.08 ?  106 ILE   B H    1 
ATOM   5499 H HA   A ILE   B 1 106 ? 34.245 -28.343 7.792   0.40 27.75 ?  106 ILE   B HA   1 
ATOM   5500 H HA   B ILE   B 1 106 ? 34.181 -28.361 7.669   0.60 23.48 ?  106 ILE   B HA   1 
ATOM   5501 H HB   A ILE   B 1 106 ? 33.975 -30.638 8.292   0.40 28.14 ?  106 ILE   B HB   1 
ATOM   5502 H HB   B ILE   B 1 106 ? 33.883 -30.670 8.191   0.60 24.98 ?  106 ILE   B HB   1 
ATOM   5503 H HG12 A ILE   B 1 106 ? 33.462 -31.371 6.130   0.40 28.25 ?  106 ILE   B HG12 1 
ATOM   5504 H HG12 B ILE   B 1 106 ? 33.468 -31.380 6.003   0.60 25.79 ?  106 ILE   B HG12 1 
ATOM   5505 H HG13 A ILE   B 1 106 ? 32.864 -29.943 5.787   0.40 28.25 ?  106 ILE   B HG13 1 
ATOM   5506 H HG13 B ILE   B 1 106 ? 32.890 -29.946 5.646   0.60 25.79 ?  106 ILE   B HG13 1 
ATOM   5507 H HG21 A ILE   B 1 106 ? 31.943 -31.685 8.107   0.40 28.63 ?  106 ILE   B HG21 1 
ATOM   5508 H HG21 B ILE   B 1 106 ? 31.861 -31.694 7.955   0.60 25.89 ?  106 ILE   B HG21 1 
ATOM   5509 H HG22 A ILE   B 1 106 ? 31.772 -30.490 9.138   0.40 28.63 ?  106 ILE   B HG22 1 
ATOM   5510 H HG22 B ILE   B 1 106 ? 31.624 -30.454 8.919   0.60 25.89 ?  106 ILE   B HG22 1 
ATOM   5511 H HG23 A ILE   B 1 106 ? 31.246 -30.335 7.647   0.40 28.63 ?  106 ILE   B HG23 1 
ATOM   5512 H HG23 B ILE   B 1 106 ? 31.197 -30.366 7.391   0.60 25.89 ?  106 ILE   B HG23 1 
ATOM   5513 H HD11 A ILE   B 1 106 ? 35.066 -30.361 4.953   0.40 28.24 ?  106 ILE   B HD11 1 
ATOM   5514 H HD11 B ILE   B 1 106 ? 35.148 -30.403 4.935   0.60 26.10 ?  106 ILE   B HD11 1 
ATOM   5515 H HD12 A ILE   B 1 106 ? 34.900 -29.000 5.753   0.40 28.24 ?  106 ILE   B HD12 1 
ATOM   5516 H HD12 B ILE   B 1 106 ? 34.914 -29.013 5.667   0.60 26.10 ?  106 ILE   B HD12 1 
ATOM   5517 H HD13 A ILE   B 1 106 ? 35.565 -30.261 6.457   0.40 28.24 ?  106 ILE   B HD13 1 
ATOM   5518 H HD13 B ILE   B 1 106 ? 35.549 -30.235 6.462   0.60 26.10 ?  106 ILE   B HD13 1 
ATOM   5519 N N    A GLN   B 1 107 ? 31.250 -27.473 8.179   0.40 22.36 ?  107 GLN   B N    1 
ATOM   5520 N N    B GLN   B 1 107 ? 31.196 -27.493 8.115   0.60 19.75 ?  107 GLN   B N    1 
ATOM   5521 C CA   A GLN   B 1 107 ? 30.169 -26.692 7.586   0.40 22.42 ?  107 GLN   B CA   1 
ATOM   5522 C CA   B GLN   B 1 107 ? 30.127 -26.669 7.563   0.60 20.81 ?  107 GLN   B CA   1 
ATOM   5523 C C    A GLN   B 1 107 ? 30.653 -25.349 7.056   0.40 20.29 ?  107 GLN   B C    1 
ATOM   5524 C C    B GLN   B 1 107 ? 30.625 -25.311 7.078   0.60 19.57 ?  107 GLN   B C    1 
ATOM   5525 O O    A GLN   B 1 107 ? 30.023 -24.787 6.155   0.40 20.67 ?  107 GLN   B O    1 
ATOM   5526 O O    B GLN   B 1 107 ? 29.976 -24.700 6.223   0.60 20.38 ?  107 GLN   B O    1 
ATOM   5527 C CB   A GLN   B 1 107 ? 29.054 -26.484 8.616   0.40 24.93 ?  107 GLN   B CB   1 
ATOM   5528 C CB   B GLN   B 1 107 ? 29.019 -26.491 8.605   0.60 24.05 ?  107 GLN   B CB   1 
ATOM   5529 C CG   A GLN   B 1 107 ? 27.737 -25.960 8.047   0.40 27.44 ?  107 GLN   B CG   1 
ATOM   5530 C CG   B GLN   B 1 107 ? 27.691 -25.987 8.047   0.60 27.58 ?  107 GLN   B CG   1 
ATOM   5531 C CD   A GLN   B 1 107 ? 27.699 -24.446 7.935   0.40 29.35 ?  107 GLN   B CD   1 
ATOM   5532 C CD   B GLN   B 1 107 ? 27.598 -24.471 8.019   0.60 30.19 ?  107 GLN   B CD   1 
ATOM   5533 O OE1  A GLN   B 1 107 ? 28.538 -23.746 8.506   0.40 30.10 ?  107 GLN   B OE1  1 
ATOM   5534 O OE1  B GLN   B 1 107 ? 28.437 -23.773 8.592   0.60 31.17 ?  107 GLN   B OE1  1 
ATOM   5535 N NE2  A GLN   B 1 107 ? 26.720 -23.932 7.195   0.40 30.06 ?  107 GLN   B NE2  1 
ATOM   5536 N NE2  B GLN   B 1 107 ? 26.569 -23.954 7.352   0.60 31.26 ?  107 GLN   B NE2  1 
ATOM   5537 H H    A GLN   B 1 107 ? 31.144 -27.651 9.011   0.40 26.82 ?  107 GLN   B H    1 
ATOM   5538 H H    B GLN   B 1 107 ? 31.090 -27.708 8.936   0.60 23.69 ?  107 GLN   B H    1 
ATOM   5539 H HA   A GLN   B 1 107 ? 29.795 -27.190 6.844   0.40 26.90 ?  107 GLN   B HA   1 
ATOM   5540 H HA   B GLN   B 1 107 ? 29.742 -27.130 6.802   0.60 24.96 ?  107 GLN   B HA   1 
ATOM   5541 H HB2  A GLN   B 1 107 ? 28.868 -27.333 9.040   0.40 29.91 ?  107 GLN   B HB2  1 
ATOM   5542 H HB2  B GLN   B 1 107 ? 28.851 -27.347 9.022   0.60 28.86 ?  107 GLN   B HB2  1 
ATOM   5543 H HB3  A GLN   B 1 107 ? 29.361 -25.847 9.280   0.40 29.91 ?  107 GLN   B HB3  1 
ATOM   5544 H HB3  B GLN   B 1 107 ? 29.320 -25.856 9.273   0.60 28.86 ?  107 GLN   B HB3  1 
ATOM   5545 H HG2  A GLN   B 1 107 ? 27.605 -26.326 7.160   0.40 32.92 ?  107 GLN   B HG2  1 
ATOM   5546 H HG2  B GLN   B 1 107 ? 27.584 -26.308 7.139   0.60 33.08 ?  107 GLN   B HG2  1 
ATOM   5547 H HG3  A GLN   B 1 107 ? 27.009 -26.237 8.630   0.40 32.92 ?  107 GLN   B HG3  1 
ATOM   5548 H HG3  B GLN   B 1 107 ? 26.967 -26.323 8.603   0.60 33.08 ?  107 GLN   B HG3  1 
ATOM   5549 H HE21 A GLN   B 1 107 ? 26.152 -24.451 6.809   0.40 36.06 ?  107 GLN   B HE21 1 
ATOM   5550 H HE21 B GLN   B 1 107 ? 26.003 -24.473 6.962   0.60 37.51 ?  107 GLN   B HE21 1 
ATOM   5551 H HE22 A GLN   B 1 107 ? 26.650 -23.079 7.103   0.40 36.06 ?  107 GLN   B HE22 1 
ATOM   5552 H HE22 B GLN   B 1 107 ? 26.468 -23.101 7.310   0.60 37.51 ?  107 GLN   B HE22 1 
ATOM   5553 N N    . LEU   B 1 108 ? 31.762 -24.829 7.583   1.00 17.98 ?  108 LEU   B N    1 
ATOM   5554 C CA   . LEU   B 1 108 ? 32.302 -23.535 7.166   1.00 15.88 ?  108 LEU   B CA   1 
ATOM   5555 C C    . LEU   B 1 108 ? 32.950 -23.560 5.790   1.00 14.36 ?  108 LEU   B C    1 
ATOM   5556 O O    . LEU   B 1 108 ? 33.381 -22.502 5.304   1.00 14.13 ?  108 LEU   B O    1 
ATOM   5557 C CB   . LEU   B 1 108 ? 33.309 -23.032 8.197   1.00 16.06 ?  108 LEU   B CB   1 
ATOM   5558 C CG   . LEU   B 1 108 ? 32.681 -22.623 9.528   1.00 18.03 ?  108 LEU   B CG   1 
ATOM   5559 C CD1  . LEU   B 1 108 ? 33.726 -22.509 10.623  1.00 18.63 ?  108 LEU   B CD1  1 
ATOM   5560 C CD2  . LEU   B 1 108 ? 31.946 -21.305 9.365   1.00 19.64 ?  108 LEU   B CD2  1 
ATOM   5561 H H    A LEU   B 1 108 ? 32.220 -25.211 8.198   0.40 21.57 ?  108 LEU   B H    1 
ATOM   5562 H H    B LEU   B 1 108 ? 32.235 -25.233 8.172   0.60 21.57 ?  108 LEU   B H    1 
ATOM   5563 H HA   . LEU   B 1 108 ? 31.574 -22.899 7.127   1.00 19.05 ?  108 LEU   B HA   1 
ATOM   5564 H HB2  . LEU   B 1 108 ? 33.947 -23.737 8.381   1.00 19.26 ?  108 LEU   B HB2  1 
ATOM   5565 H HB3  . LEU   B 1 108 ? 33.765 -22.258 7.836   1.00 19.26 ?  108 LEU   B HB3  1 
ATOM   5566 H HG   . LEU   B 1 108 ? 32.032 -23.293 9.797   1.00 21.63 ?  108 LEU   B HG   1 
ATOM   5567 H HD11 . LEU   B 1 108 ? 33.289 -22.268 11.456  1.00 22.35 ?  108 LEU   B HD11 1 
ATOM   5568 H HD12 . LEU   B 1 108 ? 34.174 -23.363 10.720  1.00 22.35 ?  108 LEU   B HD12 1 
ATOM   5569 H HD13 . LEU   B 1 108 ? 34.368 -21.824 10.377  1.00 22.35 ?  108 LEU   B HD13 1 
ATOM   5570 H HD21 . LEU   B 1 108 ? 31.642 -21.001 10.235  1.00 23.56 ?  108 LEU   B HD21 1 
ATOM   5571 H HD22 . LEU   B 1 108 ? 32.550 -20.652 8.979   1.00 23.56 ?  108 LEU   B HD22 1 
ATOM   5572 H HD23 . LEU   B 1 108 ? 31.183 -21.436 8.778   1.00 23.56 ?  108 LEU   B HD23 1 
ATOM   5573 N N    . LEU   B 1 109 ? 33.020 -24.730 5.157   1.00 13.50 ?  109 LEU   B N    1 
ATOM   5574 C CA   . LEU   B 1 109 ? 33.655 -24.838 3.852   1.00 12.85 ?  109 LEU   B CA   1 
ATOM   5575 C C    . LEU   B 1 109 ? 32.893 -24.052 2.791   1.00 12.05 ?  109 LEU   B C    1 
ATOM   5576 O O    . LEU   B 1 109 ? 33.508 -23.455 1.900   1.00 11.80 ?  109 LEU   B O    1 
ATOM   5577 C CB   . LEU   B 1 109 ? 33.769 -26.312 3.468   1.00 12.68 ?  109 LEU   B CB   1 
ATOM   5578 C CG   . LEU   B 1 109 ? 34.561 -26.655 2.208   1.00 12.52 ?  109 LEU   B CG   1 
ATOM   5579 C CD1  . LEU   B 1 109 ? 35.939 -26.000 2.214   1.00 12.58 ?  109 LEU   B CD1  1 
ATOM   5580 C CD2  . LEU   B 1 109 ? 34.691 -28.168 2.068   1.00 13.61 ?  109 LEU   B CD2  1 
ATOM   5581 H H    . LEU   B 1 109 ? 32.718 -25.471 5.459   1.00 16.20 ?  109 LEU   B H    1 
ATOM   5582 H HA   . LEU   B 1 109 ? 34.550 -24.474 3.900   1.00 15.42 ?  109 LEU   B HA   1 
ATOM   5583 H HB2  . LEU   B 1 109 ? 34.192 -26.783 4.201   1.00 15.21 ?  109 LEU   B HB2  1 
ATOM   5584 H HB3  . LEU   B 1 109 ? 32.872 -26.664 3.341   1.00 15.21 ?  109 LEU   B HB3  1 
ATOM   5585 H HG   . LEU   B 1 109 ? 34.076 -26.334 1.429   1.00 15.01 ?  109 LEU   B HG   1 
ATOM   5586 H HD11 . LEU   B 1 109 ? 36.465 -26.361 1.481   1.00 15.08 ?  109 LEU   B HD11 1 
ATOM   5587 H HD12 . LEU   B 1 109 ? 35.833 -25.044 2.104   1.00 15.08 ?  109 LEU   B HD12 1 
ATOM   5588 H HD13 . LEU   B 1 109 ? 36.375 -26.194 3.058   1.00 15.08 ?  109 LEU   B HD13 1 
ATOM   5589 H HD21 . LEU   B 1 109 ? 35.267 -28.368 1.311   1.00 16.32 ?  109 LEU   B HD21 1 
ATOM   5590 H HD22 . LEU   B 1 109 ? 35.078 -28.528 2.879   1.00 16.32 ?  109 LEU   B HD22 1 
ATOM   5591 H HD23 . LEU   B 1 109 ? 33.811 -28.552 1.920   1.00 16.32 ?  109 LEU   B HD23 1 
ATOM   5592 N N    . LYS   B 1 110 ? 31.561 -24.016 2.873   1.00 11.83 ?  110 LYS   B N    1 
ATOM   5593 C CA   . LYS   B 1 110 ? 30.805 -23.252 1.886   1.00 11.54 ?  110 LYS   B CA   1 
ATOM   5594 C C    . LYS   B 1 110 ? 31.142 -21.765 1.974   1.00 11.16 ?  110 LYS   B C    1 
ATOM   5595 O O    . LYS   B 1 110 ? 31.401 -21.117 0.954   1.00 11.12 ?  110 LYS   B O    1 
ATOM   5596 C CB   . LYS   B 1 110 ? 29.302 -23.497 2.039   1.00 12.46 ?  110 LYS   B CB   1 
ATOM   5597 C CG   . LYS   B 1 110 ? 28.494 -22.861 0.910   1.00 12.66 ?  110 LYS   B CG   1 
ATOM   5598 C CD   . LYS   B 1 110 ? 27.029 -23.292 0.916   1.00 13.12 ?  110 LYS   B CD   1 
ATOM   5599 C CE   . LYS   B 1 110 ? 26.283 -22.757 -0.311  1.00 13.81 ?  110 LYS   B CE   1 
ATOM   5600 N NZ   . LYS   B 1 110 ? 26.604 -23.485 -1.570  1.00 13.91 ?  110 LYS   B NZ   1 
ATOM   5601 H H    . LYS   B 1 110 ? 31.090 -24.419 3.462   1.00 14.18 ?  110 LYS   B H    1 
ATOM   5602 H HA   . LYS   B 1 110 ? 31.057 -23.555 0.997   1.00 13.84 ?  110 LYS   B HA   1 
ATOM   5603 H HB2  . LYS   B 1 110 ? 29.134 -24.455 2.027   1.00 14.95 ?  110 LYS   B HB2  1 
ATOM   5604 H HB3  . LYS   B 1 110 ? 29.001 -23.119 2.879   1.00 14.95 ?  110 LYS   B HB3  1 
ATOM   5605 H HG2  . LYS   B 1 110 ? 28.515 -21.895 1.007   1.00 15.18 ?  110 LYS   B HG2  1 
ATOM   5606 H HG3  . LYS   B 1 110 ? 28.875 -23.118 0.057   1.00 15.18 ?  110 LYS   B HG3  1 
ATOM   5607 H HD2  . LYS   B 1 110 ? 26.977 -24.265 0.901   1.00 15.73 ?  110 LYS   B HD2  1 
ATOM   5608 H HD3  . LYS   B 1 110 ? 26.590 -22.950 1.712   1.00 15.73 ?  110 LYS   B HD3  1 
ATOM   5609 H HE2  . LYS   B 1 110 ? 25.328 -22.833 -0.160  1.00 16.56 ?  110 LYS   B HE2  1 
ATOM   5610 H HE3  . LYS   B 1 110 ? 26.523 -21.825 -0.437  1.00 16.56 ?  110 LYS   B HE3  1 
ATOM   5611 H HZ1  . LYS   B 1 110 ? 26.153 -23.135 -2.249  1.00 16.68 ?  110 LYS   B HZ1  1 
ATOM   5612 H HZ2  . LYS   B 1 110 ? 27.478 -23.425 -1.740  1.00 16.68 ?  110 LYS   B HZ2  1 
ATOM   5613 H HZ3  . LYS   B 1 110 ? 26.388 -24.345 -1.487  1.00 16.68 ?  110 LYS   B HZ3  1 
ATOM   5614 N N    . SER   B 1 111 ? 31.165 -21.212 3.192   1.00 11.55 ?  111 SER   B N    1 
ATOM   5615 C CA   . SER   B 1 111 ? 31.561 -19.816 3.368   1.00 11.77 ?  111 SER   B CA   1 
ATOM   5616 C C    . SER   B 1 111 ? 32.943 -19.560 2.783   1.00 11.05 ?  111 SER   B C    1 
ATOM   5617 O O    . SER   B 1 111 ? 33.172 -18.526 2.142   1.00 11.36 ?  111 SER   B O    1 
ATOM   5618 C CB   . SER   B 1 111 ? 31.552 -19.445 4.849   1.00 13.19 ?  111 SER   B CB   1 
ATOM   5619 O OG   . SER   B 1 111 ? 30.244 -19.457 5.376   1.00 14.86 ?  111 SER   B OG   1 
ATOM   5620 H H    . SER   B 1 111 ? 30.968 -21.625 3.918   1.00 13.86 ?  111 SER   B H    1 
ATOM   5621 H HA   . SER   B 1 111 ? 30.931 -19.246 2.907   1.00 14.11 ?  111 SER   B HA   1 
ATOM   5622 H HB2  . SER   B 1 111 ? 32.090 -20.084 5.339   1.00 15.82 ?  111 SER   B HB2  1 
ATOM   5623 H HB3  . SER   B 1 111 ? 31.913 -18.555 4.954   1.00 15.82 ?  111 SER   B HB3  1 
ATOM   5624 H HG   . SER   B 1 111 ? 30.255 -19.258 6.196   1.00 17.82 ?  111 SER   B HG   1 
ATOM   5625 N N    . ALA   B 1 112 ? 33.878 -20.484 3.004   1.00 11.19 ?  112 ALA   B N    1 
ATOM   5626 C CA   . ALA   B 1 112 ? 35.224 -20.318 2.465   1.00 10.85 ?  112 ALA   B CA   1 
ATOM   5627 C C    . ALA   B 1 112 ? 35.197 -20.218 0.943   1.00 10.47 ?  112 ALA   B C    1 
ATOM   5628 O O    . ALA   B 1 112 ? 35.826 -19.329 0.355   1.00 10.60 ?  112 ALA   B O    1 
ATOM   5629 C CB   . ALA   B 1 112 ? 36.115 -21.468 2.941   1.00 11.56 ?  112 ALA   B CB   1 
ATOM   5630 H H    . ALA   B 1 112 ? 33.762 -21.208 3.456   1.00 13.41 ?  112 ALA   B H    1 
ATOM   5631 H HA   . ALA   B 1 112 ? 35.599 -19.493 2.807   1.00 13.01 ?  112 ALA   B HA   1 
ATOM   5632 H HB1  . ALA   B 1 112 ? 37.009 -21.342 2.580   1.00 13.87 ?  112 ALA   B HB1  1 
ATOM   5633 H HB2  . ALA   B 1 112 ? 36.150 -21.459 3.911   1.00 13.87 ?  112 ALA   B HB2  1 
ATOM   5634 H HB3  . ALA   B 1 112 ? 35.747 -22.306 2.629   1.00 13.87 ?  112 ALA   B HB3  1 
ATOM   5635 N N    . TYR   B 1 113 ? 34.466 -21.121 0.283   1.00 10.27 ?  113 TYR   B N    1 
ATOM   5636 C CA   . TYR   B 1 113 ? 34.387 -21.067 -1.172  1.00 10.06 ?  113 TYR   B CA   1 
ATOM   5637 C C    . TYR   B 1 113 ? 33.683 -19.814 -1.683  1.00 10.10 ?  113 TYR   B C    1 
ATOM   5638 O O    . TYR   B 1 113 ? 33.949 -19.384 -2.808  1.00 10.09 ?  113 TYR   B O    1 
ATOM   5639 C CB   . TYR   B 1 113 ? 33.715 -22.325 -1.721  1.00 10.43 ?  113 TYR   B CB   1 
ATOM   5640 C CG   . TYR   B 1 113 ? 34.672 -23.477 -1.978  1.00 10.74 ?  113 TYR   B CG   1 
ATOM   5641 C CD1  . TYR   B 1 113 ? 35.671 -23.371 -2.942  1.00 11.23 ?  113 TYR   B CD1  1 
ATOM   5642 C CD2  . TYR   B 1 113 ? 34.570 -24.669 -1.271  1.00 10.96 ?  113 TYR   B CD2  1 
ATOM   5643 C CE1  . TYR   B 1 113 ? 36.540 -24.406 -3.191  1.00 11.40 ?  113 TYR   B CE1  1 
ATOM   5644 C CE2  . TYR   B 1 113 ? 35.437 -25.724 -1.512  1.00 11.22 ?  113 TYR   B CE2  1 
ATOM   5645 C CZ   . TYR   B 1 113 ? 36.419 -25.591 -2.480  1.00 11.17 ?  113 TYR   B CZ   1 
ATOM   5646 O OH   . TYR   B 1 113 ? 37.307 -26.608 -2.759  1.00 11.84 ?  113 TYR   B OH   1 
ATOM   5647 H H    . TYR   B 1 113 ? 34.014 -21.761 0.653   1.00 12.31 ?  113 TYR   B H    1 
ATOM   5648 H HA   . TYR   B 1 113 ? 35.287 -21.051 -1.513  1.00 12.07 ?  113 TYR   B HA   1 
ATOM   5649 H HB2  . TYR   B 1 113 ? 33.051 -22.638 -1.084  1.00 12.51 ?  113 TYR   B HB2  1 
ATOM   5650 H HB3  . TYR   B 1 113 ? 33.284 -22.109 -2.561  1.00 12.51 ?  113 TYR   B HB3  1 
ATOM   5651 H HD1  . TYR   B 1 113 ? 35.754 -22.584 -3.431  1.00 13.46 ?  113 TYR   B HD1  1 
ATOM   5652 H HD2  . TYR   B 1 113 ? 33.905 -24.759 -0.628  1.00 13.14 ?  113 TYR   B HD2  1 
ATOM   5653 H HE1  . TYR   B 1 113 ? 37.198 -24.318 -3.844  1.00 13.67 ?  113 TYR   B HE1  1 
ATOM   5654 H HE2  . TYR   B 1 113 ? 35.353 -26.516 -1.033  1.00 13.46 ?  113 TYR   B HE2  1 
ATOM   5655 H HH   . TYR   B 1 113 ? 37.113 -27.287 -2.302  1.00 14.20 ?  113 TYR   B HH   1 
ATOM   5656 N N    . GLU   B 1 114 ? 32.762 -19.236 -0.906  1.00 10.18 ?  114 GLU   B N    1 
ATOM   5657 C CA   . GLU   B 1 114 ? 32.080 -18.029 -1.367  1.00 10.21 ?  114 GLU   B CA   1 
ATOM   5658 C C    . GLU   B 1 114 ? 33.063 -16.906 -1.665  1.00 10.01 ?  114 GLU   B C    1 
ATOM   5659 O O    . GLU   B 1 114 ? 32.782 -16.042 -2.500  1.00 10.23 ?  114 GLU   B O    1 
ATOM   5660 C CB   . GLU   B 1 114 ? 31.014 -17.596 -0.355  1.00 10.44 ?  114 GLU   B CB   1 
ATOM   5661 C CG   . GLU   B 1 114 ? 29.802 -18.518 -0.418  1.00 10.71 ?  114 GLU   B CG   1 
ATOM   5662 C CD   . GLU   B 1 114 ? 28.778 -18.336 0.693   1.00 10.75 ?  114 GLU   B CD   1 
ATOM   5663 O OE1  . GLU   B 1 114 ? 29.068 -17.720 1.739   1.00 10.83 ?  114 GLU   B OE1  1 
ATOM   5664 O OE2  . GLU   B 1 114 ? 27.647 -18.866 0.528   1.00 11.71 -1 114 GLU   B OE2  1 
ATOM   5665 H H    . GLU   B 1 114 ? 32.521 -19.518 -0.125  1.00 12.21 ?  114 GLU   B H    1 
ATOM   5666 H HA   . GLU   B 1 114 ? 31.627 -18.233 -2.191  1.00 12.24 ?  114 GLU   B HA   1 
ATOM   5667 H HB2  . GLU   B 1 114 ? 31.378 -17.637 0.544   1.00 12.52 ?  114 GLU   B HB2  1 
ATOM   5668 H HB3  . GLU   B 1 114 ? 30.719 -16.696 -0.559  1.00 12.52 ?  114 GLU   B HB3  1 
ATOM   5669 H HG2  . GLU   B 1 114 ? 29.352 -18.370 -1.263  1.00 12.85 ?  114 GLU   B HG2  1 
ATOM   5670 H HG3  . GLU   B 1 114 ? 30.117 -19.436 -0.374  1.00 12.85 ?  114 GLU   B HG3  1 
ATOM   5671 N N    . ASN   B 1 115 ? 34.225 -16.905 -1.010  1.00 10.00 ?  115 ASN   B N    1 
ATOM   5672 C CA   . ASN   B 1 115 ? 35.221 -15.877 -1.306  1.00 9.86  ?  115 ASN   B CA   1 
ATOM   5673 C C    . ASN   B 1 115 ? 35.634 -15.897 -2.770  1.00 9.46  ?  115 ASN   B C    1 
ATOM   5674 O O    . ASN   B 1 115 ? 36.020 -14.856 -3.328  1.00 10.14 ?  115 ASN   B O    1 
ATOM   5675 C CB   . ASN   B 1 115 ? 36.456 -16.058 -0.422  1.00 10.39 ?  115 ASN   B CB   1 
ATOM   5676 C CG   . ASN   B 1 115 ? 36.186 -15.791 1.036   1.00 10.91 ?  115 ASN   B CG   1 
ATOM   5677 O OD1  . ASN   B 1 115 ? 36.196 -14.644 1.480   1.00 12.59 ?  115 ASN   B OD1  1 
ATOM   5678 N ND2  . ASN   B 1 115 ? 36.015 -16.856 1.811   1.00 11.06 ?  115 ASN   B ND2  1 
ATOM   5679 H H    . ASN   B 1 115 ? 34.457 -17.466 -0.395  1.00 11.99 ?  115 ASN   B H    1 
ATOM   5680 H HA   . ASN   B 1 115 ? 34.845 -15.004 -1.112  1.00 11.82 ?  115 ASN   B HA   1 
ATOM   5681 H HB2  . ASN   B 1 115 ? 36.777 -16.968 -0.509  1.00 12.46 ?  115 ASN   B HB2  1 
ATOM   5682 H HB3  . ASN   B 1 115 ? 37.145 -15.436 -0.713  1.00 12.46 ?  115 ASN   B HB3  1 
ATOM   5683 H HD21 . ASN   B 1 115 ? 35.867 -16.755 2.653   1.00 13.27 ?  115 ASN   B HD21 1 
ATOM   5684 H HD22 . ASN   B 1 115 ? 36.029 -17.646 1.470   1.00 13.27 ?  115 ASN   B HD22 1 
ATOM   5685 N N    . PHE   B 1 116 ? 35.599 -17.073 -3.403  1.00 9.49  ?  116 PHE   B N    1 
ATOM   5686 C CA   . PHE   B 1 116 ? 36.033 -17.168 -4.792  1.00 9.86  ?  116 PHE   B CA   1 
ATOM   5687 C C    . PHE   B 1 116 ? 35.133 -16.348 -5.708  1.00 9.67  ?  116 PHE   B C    1 
ATOM   5688 O O    . PHE   B 1 116 ? 35.569 -15.921 -6.782  1.00 10.06 ?  116 PHE   B O    1 
ATOM   5689 C CB   . PHE   B 1 116 ? 36.002 -18.613 -5.310  1.00 9.91  ?  116 PHE   B CB   1 
ATOM   5690 C CG   . PHE   B 1 116 ? 37.075 -19.565 -4.765  1.00 9.72  ?  116 PHE   B CG   1 
ATOM   5691 C CD1  . PHE   B 1 116 ? 37.736 -19.380 -3.559  1.00 10.63 ?  116 PHE   B CD1  1 
ATOM   5692 C CD2  . PHE   B 1 116 ? 37.373 -20.702 -5.501  1.00 9.81  ?  116 PHE   B CD2  1 
ATOM   5693 C CE1  . PHE   B 1 116 ? 38.666 -20.317 -3.109  1.00 10.89 ?  116 PHE   B CE1  1 
ATOM   5694 C CE2  . PHE   B 1 116 ? 38.300 -21.640 -5.055  1.00 10.13 ?  116 PHE   B CE2  1 
ATOM   5695 C CZ   . PHE   B 1 116 ? 38.945 -21.448 -3.865  1.00 10.34 ?  116 PHE   B CZ   1 
ATOM   5696 H H    . PHE   B 1 116 ? 35.336 -17.820 -3.056  1.00 11.38 ?  116 PHE   B H    1 
ATOM   5697 H HA   . PHE   B 1 116 ? 36.942 -16.837 -4.872  1.00 11.82 ?  116 PHE   B HA   1 
ATOM   5698 H HB2  . PHE   B 1 116 ? 35.135 -18.994 -5.085  1.00 11.89 ?  116 PHE   B HB2  1 
ATOM   5699 H HB3  . PHE   B 1 116 ? 36.096 -18.591 -6.276  1.00 11.89 ?  116 PHE   B HB3  1 
ATOM   5700 H HD1  . PHE   B 1 116 ? 37.547 -18.629 -3.040  1.00 12.75 ?  116 PHE   B HD1  1 
ATOM   5701 H HD2  . PHE   B 1 116 ? 36.932 -20.855 -6.304  1.00 11.76 ?  116 PHE   B HD2  1 
ATOM   5702 H HE1  . PHE   B 1 116 ? 39.114 -20.183 -2.306  1.00 13.06 ?  116 PHE   B HE1  1 
ATOM   5703 H HE2  . PHE   B 1 116 ? 38.490 -22.392 -5.570  1.00 12.15 ?  116 PHE   B HE2  1 
ATOM   5704 H HZ   . PHE   B 1 116 ? 39.581 -22.061 -3.573  1.00 12.40 ?  116 PHE   B HZ   1 
ATOM   5705 N N    . ASN   B 1 117 ? 33.867 -16.144 -5.323  1.00 10.04 ?  117 ASN   B N    1 
ATOM   5706 C CA   . ASN   B 1 117 ? 32.925 -15.446 -6.196  1.00 10.19 ?  117 ASN   B CA   1 
ATOM   5707 C C    . ASN   B 1 117 ? 33.236 -13.965 -6.349  1.00 10.78 ?  117 ASN   B C    1 
ATOM   5708 O O    . ASN   B 1 117 ? 32.640 -13.309 -7.207  1.00 11.98 ?  117 ASN   B O    1 
ATOM   5709 C CB   . ASN   B 1 117 ? 31.503 -15.663 -5.701  1.00 10.23 ?  117 ASN   B CB   1 
ATOM   5710 C CG   . ASN   B 1 117 ? 31.046 -17.065 -5.956  1.00 10.33 ?  117 ASN   B CG   1 
ATOM   5711 O OD1  . ASN   B 1 117 ? 31.393 -17.652 -6.980  1.00 11.07 ?  117 ASN   B OD1  1 
ATOM   5712 N ND2  . ASN   B 1 117 ? 30.303 -17.633 -5.018  1.00 10.42 ?  117 ASN   B ND2  1 
ATOM   5713 H H    . ASN   B 1 117 ? 33.543 -16.398 -4.564  1.00 12.04 ?  117 ASN   B H    1 
ATOM   5714 H HA   . ASN   B 1 117 ? 32.990 -15.847 -7.073  1.00 12.22 ?  117 ASN   B HA   1 
ATOM   5715 H HB2  . ASN   B 1 117 ? 31.468 -15.499 -4.743  1.00 12.27 ?  117 ASN   B HB2  1 
ATOM   5716 H HB3  . ASN   B 1 117 ? 30.912 -15.051 -6.166  1.00 12.27 ?  117 ASN   B HB3  1 
ATOM   5717 H HD21 . ASN   B 1 117 ? 30.011 -18.433 -5.124  1.00 12.50 ?  117 ASN   B HD21 1 
ATOM   5718 H HD22 . ASN   B 1 117 ? 30.084 -17.186 -4.313  1.00 12.50 ?  117 ASN   B HD22 1 
ATOM   5719 N N    . GLN   B 1 118 ? 34.173 -13.440 -5.571  1.00 10.38 ?  118 GLN   B N    1 
ATOM   5720 C CA   . GLN   B 1 118 ? 34.599 -12.051 -5.707  1.00 11.05 ?  118 GLN   B CA   1 
ATOM   5721 C C    . GLN   B 1 118 ? 35.669 -11.860 -6.780  1.00 11.19 ?  118 GLN   B C    1 
ATOM   5722 O O    . GLN   B 1 118 ? 36.143 -10.732 -6.966  1.00 12.43 ?  118 GLN   B O    1 
ATOM   5723 C CB   . GLN   B 1 118 ? 35.079 -11.521 -4.351  1.00 11.44 ?  118 GLN   B CB   1 
ATOM   5724 C CG   . GLN   B 1 118 ? 34.000 -11.556 -3.280  1.00 11.54 ?  118 GLN   B CG   1 
ATOM   5725 C CD   . GLN   B 1 118 ? 32.821 -10.654 -3.611  1.00 11.60 ?  118 GLN   B CD   1 
ATOM   5726 O OE1  . GLN   B 1 118 ? 33.004 -9.509  -4.046  1.00 11.97 ?  118 GLN   B OE1  1 
ATOM   5727 N NE2  . GLN   B 1 118 ? 31.606 -11.154 -3.404  1.00 11.94 ?  118 GLN   B NE2  1 
ATOM   5728 H H    . GLN   B 1 118 ? 34.590 -13.867 -4.948  1.00 12.44 ?  118 GLN   B H    1 
ATOM   5729 H HA   . GLN   B 1 118 ? 33.829 -11.524 -5.971  1.00 13.25 ?  118 GLN   B HA   1 
ATOM   5730 H HB2  . GLN   B 1 118 ? 35.823 -12.059 -4.045  1.00 13.72 ?  118 GLN   B HB2  1 
ATOM   5731 H HB3  . GLN   B 1 118 ? 35.361 -10.596 -4.457  1.00 13.72 ?  118 GLN   B HB3  1 
ATOM   5732 H HG2  . GLN   B 1 118 ? 33.671 -12.464 -3.192  1.00 13.84 ?  118 GLN   B HG2  1 
ATOM   5733 H HG3  . GLN   B 1 118 ? 34.381 -11.258 -2.438  1.00 13.84 ?  118 GLN   B HG3  1 
ATOM   5734 H HE21 . GLN   B 1 118 ? 31.519 -11.955 -3.100  1.00 14.33 ?  118 GLN   B HE21 1 
ATOM   5735 H HE22 . GLN   B 1 118 ? 30.916 -10.680 -3.580  1.00 14.33 ?  118 GLN   B HE22 1 
ATOM   5736 N N    . HIS   B 1 119 ? 36.023 -12.919 -7.514  1.00 10.25 ?  119 HIS   B N    1 
ATOM   5737 C CA   . HIS   B 1 119 ? 37.064 -12.869 -8.532  1.00 10.75 ?  119 HIS   B CA   1 
ATOM   5738 C C    . HIS   B 1 119 ? 36.583 -13.605 -9.767  1.00 11.04 ?  119 HIS   B C    1 
ATOM   5739 O O    . HIS   B 1 119 ? 36.078 -14.721 -9.662  1.00 11.46 ?  119 HIS   B O    1 
ATOM   5740 C CB   . HIS   B 1 119 ? 38.348 -13.498 -7.984  1.00 11.44 ?  119 HIS   B CB   1 
ATOM   5741 C CG   . HIS   B 1 119 ? 38.826 -12.805 -6.755  1.00 12.89 ?  119 HIS   B CG   1 
ATOM   5742 N ND1  . HIS   B 1 119 ? 39.614 -11.676 -6.804  1.00 14.23 ?  119 HIS   B ND1  1 
ATOM   5743 C CD2  . HIS   B 1 119 ? 38.542 -13.014 -5.449  1.00 14.04 ?  119 HIS   B CD2  1 
ATOM   5744 C CE1  . HIS   B 1 119 ? 39.822 -11.241 -5.575  1.00 15.49 ?  119 HIS   B CE1  1 
ATOM   5745 N NE2  . HIS   B 1 119 ? 39.176 -12.028 -4.736  1.00 15.48 ?  119 HIS   B NE2  1 
ATOM   5746 H H    . HIS   B 1 119 ? 35.661 -13.699 -7.439  1.00 12.29 ?  119 HIS   B H    1 
ATOM   5747 H HA   . HIS   B 1 119 ? 37.241 -11.941 -8.770  1.00 12.90 ?  119 HIS   B HA   1 
ATOM   5748 H HB2  . HIS   B 1 119 ? 38.179 -14.424 -7.770  1.00 13.72 ?  119 HIS   B HB2  1 
ATOM   5749 H HB3  . HIS   B 1 119 ? 39.043 -13.429 -8.661  1.00 13.72 ?  119 HIS   B HB3  1 
ATOM   5750 H HD2  . HIS   B 1 119 ? 38.011 -13.700 -5.104  1.00 16.84 ?  119 HIS   B HD2  1 
ATOM   5751 H HE1  . HIS   B 1 119 ? 40.348 -10.515 -5.335  1.00 18.58 ?  119 HIS   B HE1  1 
ATOM   5752 H HE2  . HIS   B 1 119 ? 39.182 -11.964 -3.876  1.00 18.57 ?  119 HIS   B HE2  1 
ATOM   5753 N N    . GLU   B 1 120 ? 36.745 -12.992 -10.939 1.00 11.54 ?  120 GLU   B N    1 
ATOM   5754 C CA   . GLU   B 1 120 ? 36.153 -13.578 -12.137 1.00 12.89 ?  120 GLU   B CA   1 
ATOM   5755 C C    . GLU   B 1 120 ? 36.832 -14.877 -12.553 1.00 11.65 ?  120 GLU   B C    1 
ATOM   5756 O O    . GLU   B 1 120 ? 36.170 -15.750 -13.124 1.00 11.74 ?  120 GLU   B O    1 
ATOM   5757 C CB   . GLU   B 1 120 ? 36.152 -12.573 -13.286 1.00 16.67 ?  120 GLU   B CB   1 
ATOM   5758 C CG   . GLU   B 1 120 ? 35.214 -11.401 -13.057 1.00 22.10 ?  120 GLU   B CG   1 
ATOM   5759 C CD   . GLU   B 1 120 ? 35.033 -10.540 -14.291 1.00 27.04 ?  120 GLU   B CD   1 
ATOM   5760 O OE1  . GLU   B 1 120 ? 36.033 -10.286 -14.996 1.00 29.17 ?  120 GLU   B OE1  1 
ATOM   5761 O OE2  . GLU   B 1 120 ? 33.887 -10.122 -14.556 1.00 30.34 -1 120 GLU   B OE2  1 
ATOM   5762 H H    . GLU   B 1 120 ? 37.172 -12.255 -11.068 1.00 13.85 ?  120 GLU   B H    1 
ATOM   5763 H HA   . GLU   B 1 120 ? 35.230 -13.795 -11.943 1.00 15.46 ?  120 GLU   B HA   1 
ATOM   5764 H HB2  . GLU   B 1 120 ? 37.044 -12.221 -13.400 1.00 19.99 ?  120 GLU   B HB2  1 
ATOM   5765 H HB3  . GLU   B 1 120 ? 35.864 -13.024 -14.097 1.00 19.99 ?  120 GLU   B HB3  1 
ATOM   5766 H HG2  . GLU   B 1 120 ? 34.339 -11.737 -12.802 1.00 26.51 ?  120 GLU   B HG2  1 
ATOM   5767 H HG3  . GLU   B 1 120 ? 35.572 -10.843 -12.349 1.00 26.51 ?  120 GLU   B HG3  1 
ATOM   5768 N N    . VAL   B 1 121 ? 38.131 -15.020 -12.288 1.00 11.16 ?  121 VAL   B N    1 
ATOM   5769 C CA   . VAL   B 1 121 ? 38.874 -16.230 -12.632 1.00 11.26 ?  121 VAL   B CA   1 
ATOM   5770 C C    . VAL   B 1 121 ? 39.986 -16.427 -11.610 1.00 10.67 ?  121 VAL   B C    1 
ATOM   5771 O O    . VAL   B 1 121 ? 40.660 -15.466 -11.216 1.00 11.00 ?  121 VAL   B O    1 
ATOM   5772 C CB   . VAL   B 1 121 ? 39.394 -16.190 -14.088 1.00 12.69 ?  121 VAL   B CB   1 
ATOM   5773 C CG1  . VAL   B 1 121 ? 40.250 -14.955 -14.348 1.00 13.95 ?  121 VAL   B CG1  1 
ATOM   5774 C CG2  . VAL   B 1 121 ? 40.154 -17.467 -14.430 1.00 14.12 ?  121 VAL   B CG2  1 
ATOM   5775 H H    . VAL   B 1 121 ? 38.613 -14.419 -11.904 1.00 13.38 ?  121 VAL   B H    1 
ATOM   5776 H HA   . VAL   B 1 121 ? 38.269 -16.984 -12.563 1.00 13.50 ?  121 VAL   B HA   1 
ATOM   5777 H HB   . VAL   B 1 121 ? 38.629 -16.144 -14.686 1.00 15.22 ?  121 VAL   B HB   1 
ATOM   5778 H HG11 . VAL   B 1 121 ? 40.565 -14.973 -15.266 1.00 16.73 ?  121 VAL   B HG11 1 
ATOM   5779 H HG12 . VAL   B 1 121 ? 39.709 -14.159 -14.203 1.00 16.73 ?  121 VAL   B HG12 1 
ATOM   5780 H HG13 . VAL   B 1 121 ? 41.003 -14.956 -13.739 1.00 16.73 ?  121 VAL   B HG13 1 
ATOM   5781 H HG21 . VAL   B 1 121 ? 40.350 -17.471 -15.382 1.00 16.93 ?  121 VAL   B HG21 1 
ATOM   5782 H HG22 . VAL   B 1 121 ? 40.982 -17.487 -13.925 1.00 16.93 ?  121 VAL   B HG22 1 
ATOM   5783 H HG23 . VAL   B 1 121 ? 39.606 -18.232 -14.204 1.00 16.93 ?  121 VAL   B HG23 1 
ATOM   5784 N N    . LEU   B 1 122 ? 40.171 -17.684 -11.177 1.00 10.23 ?  122 LEU   B N    1 
ATOM   5785 C CA   . LEU   B 1 122 ? 41.148 -18.031 -10.149 1.00 10.24 ?  122 LEU   B CA   1 
ATOM   5786 C C    . LEU   B 1 122 ? 41.810 -19.359 -10.475 1.00 9.99  ?  122 LEU   B C    1 
ATOM   5787 O O    . LEU   B 1 122 ? 41.158 -20.280 -10.980 1.00 11.01 ?  122 LEU   B O    1 
ATOM   5788 C CB   . LEU   B 1 122 ? 40.486 -18.263 -8.775  1.00 11.91 ?  122 LEU   B CB   1 
ATOM   5789 C CG   . LEU   B 1 122 ? 39.460 -17.236 -8.276  1.00 11.83 ?  122 LEU   B CG   1 
ATOM   5790 C CD1  . LEU   B 1 122 ? 38.052 -17.581 -8.742  1.00 12.60 ?  122 LEU   B CD1  1 
ATOM   5791 C CD2  . LEU   B 1 122 ? 39.510 -17.123 -6.763  1.00 11.37 ?  122 LEU   B CD2  1 
ATOM   5792 H H    . LEU   B 1 122 ? 39.733 -18.365 -11.474 1.00 12.26 ?  122 LEU   B H    1 
ATOM   5793 H HA   . LEU   B 1 122 ? 41.823 -17.337 -10.071 1.00 12.28 ?  122 LEU   B HA   1 
ATOM   5794 H HB2  . LEU   B 1 122 ? 40.038 -19.119 -8.801  1.00 14.28 ?  122 LEU   B HB2  1 
ATOM   5795 H HB3  . LEU   B 1 122 ? 41.191 -18.293 -8.108  1.00 14.28 ?  122 LEU   B HB3  1 
ATOM   5796 H HG   . LEU   B 1 122 ? 39.680 -16.368 -8.640  1.00 14.18 ?  122 LEU   B HG   1 
ATOM   5797 H HD11 . LEU   B 1 122 ? 37.429 -16.924 -8.385  1.00 15.12 ?  122 LEU   B HD11 1 
ATOM   5798 H HD12 . LEU   B 1 122 ? 38.024 -17.562 -9.712  1.00 15.12 ?  122 LEU   B HD12 1 
ATOM   5799 H HD13 . LEU   B 1 122 ? 37.815 -18.464 -8.422  1.00 15.12 ?  122 LEU   B HD13 1 
ATOM   5800 H HD21 . LEU   B 1 122 ? 38.832 -16.493 -6.466  1.00 13.64 ?  122 LEU   B HD21 1 
ATOM   5801 H HD22 . LEU   B 1 122 ? 39.340 -17.996 -6.372  1.00 13.64 ?  122 LEU   B HD22 1 
ATOM   5802 H HD23 . LEU   B 1 122 ? 40.389 -16.809 -6.499  1.00 13.64 ?  122 LEU   B HD23 1 
ATOM   5803 N N    . LEU   B 1 123 ? 43.095 -19.460 -10.122 1.00 9.62  ?  123 LEU   B N    1 
ATOM   5804 C CA   . LEU   B 1 123 ? 43.810 -20.728 -9.991  1.00 9.86  ?  123 LEU   B CA   1 
ATOM   5805 C C    . LEU   B 1 123 ? 43.778 -21.119 -8.518  1.00 9.83  ?  123 LEU   B C    1 
ATOM   5806 O O    . LEU   B 1 123 ? 44.134 -20.296 -7.664  1.00 10.09 ?  123 LEU   B O    1 
ATOM   5807 C CB   . LEU   B 1 123 ? 45.260 -20.543 -10.445 1.00 10.30 ?  123 LEU   B CB   1 
ATOM   5808 C CG   . LEU   B 1 123 ? 46.209 -21.725 -10.206 1.00 10.47 ?  123 LEU   B CG   1 
ATOM   5809 C CD1  . LEU   B 1 123 ? 45.795 -22.975 -10.986 1.00 10.98 ?  123 LEU   B CD1  1 
ATOM   5810 C CD2  . LEU   B 1 123 ? 47.626 -21.328 -10.582 1.00 11.46 ?  123 LEU   B CD2  1 
ATOM   5811 H H    . LEU   B 1 123 ? 43.591 -18.780 -9.933  1.00 11.53 ?  123 LEU   B H    1 
ATOM   5812 H HA   . LEU   B 1 123 ? 43.379 -21.421 -10.520 1.00 11.82 ?  123 LEU   B HA   1 
ATOM   5813 H HB2  . LEU   B 1 123 ? 45.251 -20.369 -11.402 1.00 12.36 ?  123 LEU   B HB2  1 
ATOM   5814 H HB3  . LEU   B 1 123 ? 45.625 -19.778 -9.983  1.00 12.36 ?  123 LEU   B HB3  1 
ATOM   5815 H HG   . LEU   B 1 123 ? 46.210 -21.950 -9.264  1.00 12.55 ?  123 LEU   B HG   1 
ATOM   5816 H HD11 . LEU   B 1 123 ? 46.433 -23.680 -10.809 1.00 13.16 ?  123 LEU   B HD11 1 
ATOM   5817 H HD12 . LEU   B 1 123 ? 44.910 -23.244 -10.691 1.00 13.16 ?  123 LEU   B HD12 1 
ATOM   5818 H HD13 . LEU   B 1 123 ? 45.780 -22.762 -11.930 1.00 13.16 ?  123 LEU   B HD13 1 
ATOM   5819 H HD21 . LEU   B 1 123 ? 48.220 -22.080 -10.429 1.00 13.74 ?  123 LEU   B HD21 1 
ATOM   5820 H HD22 . LEU   B 1 123 ? 47.647 -21.078 -11.521 1.00 13.74 ?  123 LEU   B HD22 1 
ATOM   5821 H HD23 . LEU   B 1 123 ? 47.899 -20.574 -10.036 1.00 13.74 ?  123 LEU   B HD23 1 
ATOM   5822 N N    . ALA   B 1 124 ? 43.354 -22.350 -8.209  1.00 9.62  ?  124 ALA   B N    1 
ATOM   5823 C CA   . ALA   B 1 124 ? 43.084 -22.667 -6.813  1.00 9.51  ?  124 ALA   B CA   1 
ATOM   5824 C C    . ALA   B 1 124 ? 43.364 -24.128 -6.489  1.00 9.51  ?  124 ALA   B C    1 
ATOM   5825 O O    . ALA   B 1 124 ? 43.241 -25.006 -7.355  1.00 9.92  ?  124 ALA   B O    1 
ATOM   5826 C CB   . ALA   B 1 124 ? 41.627 -22.362 -6.454  1.00 10.18 ?  124 ALA   B CB   1 
ATOM   5827 H H    . ALA   B 1 124 ? 43.212 -22.994 -8.771  1.00 11.54 ?  124 ALA   B H    1 
ATOM   5828 H HA   . ALA   B 1 124 ? 43.655 -22.116 -6.264  1.00 11.41 ?  124 ALA   B HA   1 
ATOM   5829 H HB1  . ALA   B 1 124 ? 41.475 -22.579 -5.521  1.00 12.21 ?  124 ALA   B HB1  1 
ATOM   5830 H HB2  . ALA   B 1 124 ? 41.461 -21.413 -6.602  1.00 12.21 ?  124 ALA   B HB2  1 
ATOM   5831 H HB3  . ALA   B 1 124 ? 41.040 -22.888 -7.018  1.00 12.21 ?  124 ALA   B HB3  1 
ATOM   5832 N N    . PRO   B 1 125 ? 43.651 -24.423 -5.220  1.00 9.83  ?  125 PRO   B N    1 
ATOM   5833 C CA   . PRO   B 1 125 ? 43.587 -25.786 -4.695  1.00 10.43 ?  125 PRO   B CA   1 
ATOM   5834 C C    . PRO   B 1 125 ? 42.185 -26.060 -4.156  1.00 10.42 ?  125 PRO   B C    1 
ATOM   5835 O O    . PRO   B 1 125 ? 41.388 -25.144 -3.938  1.00 10.69 ?  125 PRO   B O    1 
ATOM   5836 C CB   . PRO   B 1 125 ? 44.569 -25.703 -3.517  1.00 11.32 ?  125 PRO   B CB   1 
ATOM   5837 C CG   . PRO   B 1 125 ? 44.313 -24.320 -2.953  1.00 11.36 ?  125 PRO   B CG   1 
ATOM   5838 C CD   . PRO   B 1 125 ? 43.981 -23.453 -4.157  1.00 10.42 ?  125 PRO   B CD   1 
ATOM   5839 H HA   . PRO   B 1 125 ? 43.866 -26.455 -5.339  1.00 12.51 ?  125 PRO   B HA   1 
ATOM   5840 H HB2  . PRO   B 1 125 ? 44.363 -26.388 -2.858  1.00 13.58 ?  125 PRO   B HB2  1 
ATOM   5841 H HB3  . PRO   B 1 125 ? 45.479 -25.784 -3.833  1.00 13.58 ?  125 PRO   B HB3  1 
ATOM   5842 H HG2  . PRO   B 1 125 ? 43.557 -24.341 -2.336  1.00 13.62 ?  125 PRO   B HG2  1 
ATOM   5843 H HG3  . PRO   B 1 125 ? 45.105 -23.988 -2.498  1.00 13.62 ?  125 PRO   B HG3  1 
ATOM   5844 H HD2  . PRO   B 1 125 ? 43.224 -22.877 -3.967  1.00 12.49 ?  125 PRO   B HD2  1 
ATOM   5845 H HD3  . PRO   B 1 125 ? 44.763 -22.928 -4.414  1.00 12.49 ?  125 PRO   B HD3  1 
ATOM   5846 N N    . LEU   B 1 126 ? 41.920 -27.340 -3.880  1.00 10.92 ?  126 LEU   B N    1 
ATOM   5847 C CA   . LEU   B 1 126 ? 40.699 -27.707 -3.169  1.00 11.49 ?  126 LEU   B CA   1 
ATOM   5848 C C    . LEU   B 1 126 ? 40.806 -27.304 -1.706  1.00 11.51 ?  126 LEU   B C    1 
ATOM   5849 O O    . LEU   B 1 126 ? 41.692 -27.763 -0.980  1.00 13.34 ?  126 LEU   B O    1 
ATOM   5850 C CB   . LEU   B 1 126 ? 40.443 -29.202 -3.278  1.00 12.63 ?  126 LEU   B CB   1 
ATOM   5851 C CG   . LEU   B 1 126 ? 39.927 -29.680 -4.632  1.00 13.72 ?  126 LEU   B CG   1 
ATOM   5852 C CD1  . LEU   B 1 126 ? 39.977 -31.194 -4.696  1.00 15.71 ?  126 LEU   B CD1  1 
ATOM   5853 C CD2  . LEU   B 1 126 ? 38.507 -29.202 -4.889  1.00 14.02 ?  126 LEU   B CD2  1 
ATOM   5854 H H    . LEU   B 1 126 ? 42.427 -28.008 -4.079  1.00 13.10 ?  126 LEU   B H    1 
ATOM   5855 H HA   . LEU   B 1 126 ? 39.950 -27.238 -3.560  1.00 13.78 ?  126 LEU   B HA   1 
ATOM   5856 H HB2  . LEU   B 1 126 ? 41.270 -29.672 -3.098  1.00 15.15 ?  126 LEU   B HB2  1 
ATOM   5857 H HB3  . LEU   B 1 126 ? 39.779 -29.450 -2.615  1.00 15.15 ?  126 LEU   B HB3  1 
ATOM   5858 H HG   . LEU   B 1 126 ? 40.503 -29.334 -5.334  1.00 16.45 ?  126 LEU   B HG   1 
ATOM   5859 H HD11 . LEU   B 1 126 ? 39.645 -31.486 -5.560  1.00 18.85 ?  126 LEU   B HD11 1 
ATOM   5860 H HD12 . LEU   B 1 126 ? 40.891 -31.490 -4.574  1.00 18.85 ?  126 LEU   B HD12 1 
ATOM   5861 H HD13 . LEU   B 1 126 ? 39.416 -31.557 -3.989  1.00 18.85 ?  126 LEU   B HD13 1 
ATOM   5862 H HD21 . LEU   B 1 126 ? 38.177 -29.612 -5.699  1.00 16.82 ?  126 LEU   B HD21 1 
ATOM   5863 H HD22 . LEU   B 1 126 ? 37.953 -29.447 -4.135  1.00 16.82 ?  126 LEU   B HD22 1 
ATOM   5864 H HD23 . LEU   B 1 126 ? 38.519 -28.233 -4.989  1.00 16.82 ?  126 LEU   B HD23 1 
ATOM   5865 N N    . LEU   B 1 127 ? 39.876 -26.469 -1.260  1.00 11.27 ?  127 LEU   B N    1 
ATOM   5866 C CA   . LEU   B 1 127 ? 39.921 -25.973 0.104   1.00 11.77 ?  127 LEU   B CA   1 
ATOM   5867 C C    . LEU   B 1 127 ? 39.657 -27.097 1.100   1.00 11.33 ?  127 LEU   B C    1 
ATOM   5868 O O    . LEU   B 1 127 ? 38.843 -28.004 0.869   1.00 11.67 ?  127 LEU   B O    1 
ATOM   5869 C CB   . LEU   B 1 127 ? 38.893 -24.860 0.302   1.00 12.19 ?  127 LEU   B CB   1 
ATOM   5870 C CG   . LEU   B 1 127 ? 39.075 -23.594 -0.541  1.00 12.56 ?  127 LEU   B CG   1 
ATOM   5871 C CD1  . LEU   B 1 127 ? 37.965 -22.625 -0.213  1.00 12.77 ?  127 LEU   B CD1  1 
ATOM   5872 C CD2  . LEU   B 1 127 ? 40.441 -22.954 -0.298  1.00 13.24 ?  127 LEU   B CD2  1 
ATOM   5873 H H    . LEU   B 1 127 ? 39.216 -26.162 -1.727  1.00 13.52 ?  127 LEU   B H    1 
ATOM   5874 H HA   . LEU   B 1 127 ? 40.802 -25.607 0.283   1.00 14.12 ?  127 LEU   B HA   1 
ATOM   5875 H HB2  . LEU   B 1 127 ? 38.012 -25.218 0.097   1.00 14.63 ?  127 LEU   B HB2  1 
ATOM   5876 H HB3  . LEU   B 1 127 ? 38.913 -24.587 1.234   1.00 14.63 ?  127 LEU   B HB3  1 
ATOM   5877 H HG   . LEU   B 1 127 ? 38.997 -23.821 -1.478  1.00 15.06 ?  127 LEU   B HG   1 
ATOM   5878 H HD11 . LEU   B 1 127 ? 38.082 -21.816 -0.743  1.00 15.31 ?  127 LEU   B HD11 1 
ATOM   5879 H HD12 . LEU   B 1 127 ? 37.108 -23.029 -0.420  1.00 15.31 ?  127 LEU   B HD12 1 
ATOM   5880 H HD13 . LEU   B 1 127 ? 38.004 -22.401 0.732   1.00 15.31 ?  127 LEU   B HD13 1 
ATOM   5881 H HD21 . LEU   B 1 127 ? 40.474 -22.099 -0.752  1.00 15.88 ?  127 LEU   B HD21 1 
ATOM   5882 H HD22 . LEU   B 1 127 ? 40.565 -22.828 0.656   1.00 15.88 ?  127 LEU   B HD22 1 
ATOM   5883 H HD23 . LEU   B 1 127 ? 41.126 -23.544 -0.646  1.00 15.88 ?  127 LEU   B HD23 1 
ATOM   5884 N N    . SER   B 1 128 ? 40.345 -27.013 2.228   1.00 11.37 ?  128 SER   B N    1 
ATOM   5885 C CA   . SER   B 1 128 ? 40.238 -27.932 3.351   1.00 11.86 ?  128 SER   B CA   1 
ATOM   5886 C C    . SER   B 1 128 ? 40.735 -29.338 3.032   1.00 12.83 ?  128 SER   B C    1 
ATOM   5887 O O    . SER   B 1 128 ? 40.642 -30.215 3.887   1.00 14.37 ?  128 SER   B O    1 
ATOM   5888 C CB   . SER   B 1 128 ? 38.837 -27.942 3.981   1.00 12.32 ?  128 SER   B CB   1 
ATOM   5889 O OG   . SER   B 1 128 ? 38.510 -26.669 4.528   1.00 12.73 ?  128 SER   B OG   1 
ATOM   5890 H H    . SER   B 1 128 ? 40.923 -26.392 2.372   1.00 13.64 ?  128 SER   B H    1 
ATOM   5891 H HA   . SER   B 1 128 ? 40.823 -27.595 4.037   1.00 14.23 ?  128 SER   B HA   1 
ATOM   5892 H HB2  . SER   B 1 128 ? 38.178 -28.176 3.308   1.00 14.77 ?  128 SER   B HB2  1 
ATOM   5893 H HB3  . SER   B 1 128 ? 38.817 -28.604 4.699   1.00 14.77 ?  128 SER   B HB3  1 
ATOM   5894 H HG   . SER   B 1 128 ? 39.073 -26.459 5.115   1.00 15.27 ?  128 SER   B HG   1 
ATOM   5895 N N    . ALA   B 1 129 ? 41.315 -29.556 1.851   1.00 13.78 ?  129 ALA   B N    1 
ATOM   5896 C CA   . ALA   B 1 129 ? 41.860 -30.850 1.485   1.00 14.58 ?  129 ALA   B CA   1 
ATOM   5897 C C    . ALA   B 1 129 ? 43.247 -31.030 2.087   1.00 13.66 ?  129 ALA   B C    1 
ATOM   5898 O O    . ALA   B 1 129 ? 43.807 -30.131 2.728   1.00 13.65 ?  129 ALA   B O    1 
ATOM   5899 C CB   . ALA   B 1 129 ? 41.920 -30.992 -0.034  1.00 16.42 ?  129 ALA   B CB   1 
ATOM   5900 H H    . ALA   B 1 129 ? 41.398 -28.957 1.239   1.00 16.53 ?  129 ALA   B H    1 
ATOM   5901 H HA   . ALA   B 1 129 ? 41.283 -31.546 1.832   1.00 17.49 ?  129 ALA   B HA   1 
ATOM   5902 H HB1  . ALA   B 1 129 ? 42.280 -31.865 -0.252  1.00 19.69 ?  129 ALA   B HB1  1 
ATOM   5903 H HB2  . ALA   B 1 129 ? 41.024 -30.903 -0.393  1.00 19.69 ?  129 ALA   B HB2  1 
ATOM   5904 H HB3  . ALA   B 1 129 ? 42.492 -30.297 -0.393  1.00 19.69 ?  129 ALA   B HB3  1 
ATOM   5905 N N    . GLY   B 1 130 ? 43.800 -32.220 1.876   1.00 13.91 ?  130 GLY   B N    1 
ATOM   5906 C CA   . GLY   B 1 130 ? 45.186 -32.452 2.229   1.00 14.98 ?  130 GLY   B CA   1 
ATOM   5907 C C    . GLY   B 1 130 ? 45.396 -32.353 3.720   1.00 14.76 ?  130 GLY   B C    1 
ATOM   5908 O O    . GLY   B 1 130 ? 44.696 -32.994 4.518   1.00 15.43 ?  130 GLY   B O    1 
ATOM   5909 H H    . GLY   B 1 130 ? 43.398 -32.896 1.530   1.00 16.68 ?  130 GLY   B H    1 
ATOM   5910 H HA2  . GLY   B 1 130 ? 45.452 -33.338 1.935   1.00 17.96 ?  130 GLY   B HA2  1 
ATOM   5911 H HA3  . GLY   B 1 130 ? 45.749 -31.797 1.789   1.00 17.96 ?  130 GLY   B HA3  1 
ATOM   5912 N N    . ILE   B 1 131 ? 46.372 -31.526 4.108   1.00 14.88 ?  131 ILE   B N    1 
ATOM   5913 C CA   . ILE   B 1 131 ? 46.722 -31.385 5.511   1.00 15.66 ?  131 ILE   B CA   1 
ATOM   5914 C C    . ILE   B 1 131 ? 45.596 -30.793 6.342   1.00 15.23 ?  131 ILE   B C    1 
ATOM   5915 O O    . ILE   B 1 131 ? 45.654 -30.868 7.570   1.00 16.52 ?  131 ILE   B O    1 
ATOM   5916 C CB   . ILE   B 1 131 ? 48.041 -30.597 5.711   1.00 17.61 ?  131 ILE   B CB   1 
ATOM   5917 C CG1  . ILE   B 1 131 ? 47.866 -29.117 5.335   1.00 18.53 ?  131 ILE   B CG1  1 
ATOM   5918 C CG2  . ILE   B 1 131 ? 49.173 -31.247 4.918   1.00 18.42 ?  131 ILE   B CG2  1 
ATOM   5919 C CD1  . ILE   B 1 131 ? 49.087 -28.258 5.638   1.00 19.57 ?  131 ILE   B CD1  1 
ATOM   5920 H H    . ILE   B 1 131 ? 46.847 -31.044 3.575   1.00 17.85 ?  131 ILE   B H    1 
ATOM   5921 H HA   . ILE   B 1 131 ? 46.878 -32.274 5.860   1.00 18.78 ?  131 ILE   B HA   1 
ATOM   5922 H HB   . ILE   B 1 131 ? 48.267 -30.639 6.653   1.00 21.12 ?  131 ILE   B HB   1 
ATOM   5923 H HG12 . ILE   B 1 131 ? 47.685 -29.056 4.385   1.00 22.23 ?  131 ILE   B HG12 1 
ATOM   5924 H HG13 . ILE   B 1 131 ? 47.119 -28.746 5.835   1.00 22.23 ?  131 ILE   B HG13 1 
ATOM   5925 H HG21 . ILE   B 1 131 ? 50.008 -30.832 5.173   1.00 22.10 ?  131 ILE   B HG21 1 
ATOM   5926 H HG22 . ILE   B 1 131 ? 49.189 -32.192 5.120   1.00 22.10 ?  131 ILE   B HG22 1 
ATOM   5927 H HG23 . ILE   B 1 131 ? 49.005 -31.110 3.972   1.00 22.10 ?  131 ILE   B HG23 1 
ATOM   5928 H HD11 . ILE   B 1 131 ? 48.867 -27.330 5.469   1.00 23.48 ?  131 ILE   B HD11 1 
ATOM   5929 H HD12 . ILE   B 1 131 ? 49.330 -28.378 6.570   1.00 23.48 ?  131 ILE   B HD12 1 
ATOM   5930 H HD13 . ILE   B 1 131 ? 49.817 -28.538 5.066   1.00 23.48 ?  131 ILE   B HD13 1 
ATOM   5931 N N    . PHE   B 1 132 ? 44.570 -30.213 5.706   1.00 13.40 ?  132 PHE   B N    1 
ATOM   5932 C CA   . PHE   B 1 132 ? 43.405 -29.713 6.430   1.00 13.77 ?  132 PHE   B CA   1 
ATOM   5933 C C    . PHE   B 1 132 ? 42.379 -30.804 6.751   1.00 14.71 ?  132 PHE   B C    1 
ATOM   5934 O O    . PHE   B 1 132 ? 41.466 -30.558 7.547   1.00 16.24 ?  132 PHE   B O    1 
ATOM   5935 C CB   . PHE   B 1 132 ? 42.736 -28.575 5.646   1.00 13.28 ?  132 PHE   B CB   1 
ATOM   5936 C CG   . PHE   B 1 132 ? 43.432 -27.234 5.766   1.00 13.14 ?  132 PHE   B CG   1 
ATOM   5937 C CD1  . PHE   B 1 132 ? 44.718 -27.042 5.280   1.00 14.06 ?  132 PHE   B CD1  1 
ATOM   5938 C CD2  . PHE   B 1 132 ? 42.766 -26.145 6.311   1.00 12.49 ?  132 PHE   B CD2  1 
ATOM   5939 C CE1  . PHE   B 1 132 ? 45.333 -25.799 5.376   1.00 14.92 ?  132 PHE   B CE1  1 
ATOM   5940 C CE2  . PHE   B 1 132 ? 43.375 -24.904 6.400   1.00 13.38 ?  132 PHE   B CE2  1 
ATOM   5941 C CZ   . PHE   B 1 132 ? 44.655 -24.735 5.933   1.00 14.71 ?  132 PHE   B CZ   1 
ATOM   5942 H H    . PHE   B 1 132 ? 44.527 -30.098 4.852   1.00 16.08 ?  132 PHE   B H    1 
ATOM   5943 H HA   . PHE   B 1 132 ? 43.707 -29.342 7.270   1.00 16.51 ?  132 PHE   B HA   1 
ATOM   5944 H HB2  . PHE   B 1 132 ? 42.727 -28.812 4.708   1.00 15.92 ?  132 PHE   B HB2  1 
ATOM   5945 H HB3  . PHE   B 1 132 ? 41.827 -28.466 5.968   1.00 15.92 ?  132 PHE   B HB3  1 
ATOM   5946 H HD1  . PHE   B 1 132 ? 45.178 -27.758 4.905   1.00 16.87 ?  132 PHE   B HD1  1 
ATOM   5947 H HD2  . PHE   B 1 132 ? 41.899 -26.257 6.630   1.00 14.99 ?  132 PHE   B HD2  1 
ATOM   5948 H HE1  . PHE   B 1 132 ? 46.200 -25.685 5.060   1.00 17.89 ?  132 PHE   B HE1  1 
ATOM   5949 H HE2  . PHE   B 1 132 ? 42.919 -24.187 6.785   1.00 16.04 ?  132 PHE   B HE2  1 
ATOM   5950 H HZ   . PHE   B 1 132 ? 45.068 -23.901 6.002   1.00 17.65 ?  132 PHE   B HZ   1 
ATOM   5951 N N    . GLY   B 1 133 ? 42.495 -31.999 6.158   1.00 14.51 ?  133 GLY   B N    1 
ATOM   5952 C CA   . GLY   B 1 133 ? 41.788 -33.169 6.648   1.00 15.49 ?  133 GLY   B CA   1 
ATOM   5953 C C    . GLY   B 1 133 ? 40.390 -33.433 6.115   1.00 15.90 ?  133 GLY   B C    1 
ATOM   5954 O O    . GLY   B 1 133 ? 39.804 -34.455 6.480   1.00 17.60 ?  133 GLY   B O    1 
ATOM   5955 H H    . GLY   B 1 133 ? 42.993 -32.152 5.471   1.00 17.41 ?  133 GLY   B H    1 
ATOM   5956 H HA2  . GLY   B 1 133 ? 42.323 -33.952 6.449   1.00 18.57 ?  133 GLY   B HA2  1 
ATOM   5957 H HA3  . GLY   B 1 133 ? 41.721 -33.099 7.613   1.00 18.57 ?  133 GLY   B HA3  1 
ATOM   5958 N N    . ALA   B 1 134 ? 39.827 -32.567 5.282   1.00 15.00 ?  134 ALA   B N    1 
ATOM   5959 C CA   . ALA   B 1 134 ? 38.501 -32.838 4.749   1.00 15.25 ?  134 ALA   B CA   1 
ATOM   5960 C C    . ALA   B 1 134 ? 38.579 -33.834 3.594   1.00 15.27 ?  134 ALA   B C    1 
ATOM   5961 O O    . ALA   B 1 134 ? 39.630 -34.032 2.977   1.00 16.12 ?  134 ALA   B O    1 
ATOM   5962 C CB   . ALA   B 1 134 ? 37.835 -31.549 4.270   1.00 15.72 ?  134 ALA   B CB   1 
ATOM   5963 H H    . ALA   B 1 134 ? 40.180 -31.827 5.019   1.00 17.99 ?  134 ALA   B H    1 
ATOM   5964 H HA   . ALA   B 1 134 ? 37.947 -33.221 5.451   1.00 18.29 ?  134 ALA   B HA   1 
ATOM   5965 H HB1  . ALA   B 1 134 ? 36.949 -31.759 3.935   1.00 18.85 ?  134 ALA   B HB1  1 
ATOM   5966 H HB2  . ALA   B 1 134 ? 37.770 -30.931 5.014   1.00 18.85 ?  134 ALA   B HB2  1 
ATOM   5967 H HB3  . ALA   B 1 134 ? 38.374 -31.162 3.563   1.00 18.85 ?  134 ALA   B HB3  1 
ATOM   5968 N N    . ASP   B 1 135 ? 37.444 -34.459 3.308   1.00 15.29 ?  135 ASP   B N    1 
ATOM   5969 C CA   . ASP   B 1 135 ? 37.339 -35.352 2.161   1.00 15.96 ?  135 ASP   B CA   1 
ATOM   5970 C C    . ASP   B 1 135 ? 37.447 -34.517 0.891   1.00 14.65 ?  135 ASP   B C    1 
ATOM   5971 O O    . ASP   B 1 135 ? 36.597 -33.642 0.664   1.00 14.24 ?  135 ASP   B O    1 
ATOM   5972 C CB   . ASP   B 1 135 ? 35.991 -36.070 2.214   1.00 17.95 ?  135 ASP   B CB   1 
ATOM   5973 C CG   . ASP   B 1 135 ? 35.793 -37.056 1.078   1.00 19.71 ?  135 ASP   B CG   1 
ATOM   5974 O OD1  . ASP   B 1 135 ? 36.660 -37.137 0.184   1.00 19.47 ?  135 ASP   B OD1  1 
ATOM   5975 O OD2  . ASP   B 1 135 ? 34.764 -37.774 1.095   1.00 22.51 -1 135 ASP   B OD2  1 
ATOM   5976 H H    . ASP   B 1 135 ? 36.719 -34.381 3.760   1.00 18.34 ?  135 ASP   B H    1 
ATOM   5977 H HA   . ASP   B 1 135 ? 38.052 -36.010 2.191   1.00 19.14 ?  135 ASP   B HA   1 
ATOM   5978 H HB2  . ASP   B 1 135 ? 35.931 -36.554 3.046   1.00 21.53 ?  135 ASP   B HB2  1 
ATOM   5979 H HB3  . ASP   B 1 135 ? 35.288 -35.409 2.153   1.00 21.53 ?  135 ASP   B HB3  1 
ATOM   5980 N N    . PRO   B 1 136 ? 38.457 -34.735 0.044   1.00 15.06 ?  136 PRO   B N    1 
ATOM   5981 C CA   . PRO   B 1 136 ? 38.564 -33.909 -1.169  1.00 14.28 ?  136 PRO   B CA   1 
ATOM   5982 C C    . PRO   B 1 136 ? 37.381 -34.064 -2.103  1.00 14.04 ?  136 PRO   B C    1 
ATOM   5983 O O    . PRO   B 1 136 ? 37.066 -33.121 -2.837  1.00 13.11 ?  136 PRO   B O    1 
ATOM   5984 C CB   . PRO   B 1 136 ? 39.878 -34.380 -1.808  1.00 15.43 ?  136 PRO   B CB   1 
ATOM   5985 C CG   . PRO   B 1 136 ? 40.085 -35.766 -1.266  1.00 16.68 ?  136 PRO   B CG   1 
ATOM   5986 C CD   . PRO   B 1 136 ? 39.540 -35.729 0.132   1.00 16.50 ?  136 PRO   B CD   1 
ATOM   5987 H HA   . PRO   B 1 136 ? 38.654 -32.971 -0.931  1.00 17.13 ?  136 PRO   B HA   1 
ATOM   5988 H HB2  . PRO   B 1 136 ? 39.788 -34.400 -2.775  1.00 18.51 ?  136 PRO   B HB2  1 
ATOM   5989 H HB3  . PRO   B 1 136 ? 40.604 -33.793 -1.544  1.00 18.51 ?  136 PRO   B HB3  1 
ATOM   5990 H HG2  . PRO   B 1 136 ? 39.598 -36.408 -1.804  1.00 20.01 ?  136 PRO   B HG2  1 
ATOM   5991 H HG3  . PRO   B 1 136 ? 41.033 -35.977 -1.254  1.00 20.01 ?  136 PRO   B HG3  1 
ATOM   5992 H HD2  . PRO   B 1 136 ? 39.179 -36.593 0.382   1.00 19.80 ?  136 PRO   B HD2  1 
ATOM   5993 H HD3  . PRO   B 1 136 ? 40.219 -35.431 0.761   1.00 19.80 ?  136 PRO   B HD3  1 
ATOM   5994 N N    . ILE   B 1 137 ? 36.718 -35.225 -2.105  1.00 14.31 ?  137 ILE   B N    1 
ATOM   5995 C CA   . ILE   B 1 137 ? 35.505 -35.387 -2.905  1.00 14.75 ?  137 ILE   B CA   1 
ATOM   5996 C C    . ILE   B 1 137 ? 34.427 -34.418 -2.432  1.00 14.07 ?  137 ILE   B C    1 
ATOM   5997 O O    . ILE   B 1 137 ? 33.713 -33.806 -3.238  1.00 13.81 ?  137 ILE   B O    1 
ATOM   5998 C CB   . ILE   B 1 137 ? 35.031 -36.854 -2.848  1.00 16.69 ?  137 ILE   B CB   1 
ATOM   5999 C CG1  . ILE   B 1 137 ? 36.051 -37.766 -3.539  1.00 19.02 ?  137 ILE   B CG1  1 
ATOM   6000 C CG2  . ILE   B 1 137 ? 33.647 -37.002 -3.478  1.00 17.28 ?  137 ILE   B CG2  1 
ATOM   6001 C CD1  . ILE   B 1 137 ? 35.669 -39.236 -3.526  1.00 21.20 ?  137 ILE   B CD1  1 
ATOM   6002 H H    . ILE   B 1 137 ? 36.951 -35.922 -1.662  1.00 17.17 ?  137 ILE   B H    1 
ATOM   6003 H HA   . ILE   B 1 137 ? 35.708 -35.179 -3.832  1.00 17.70 ?  137 ILE   B HA   1 
ATOM   6004 H HB   . ILE   B 1 137 ? 34.970 -37.118 -1.922  1.00 20.02 ?  137 ILE   B HB   1 
ATOM   6005 H HG12 . ILE   B 1 137 ? 36.144 -37.495 -4.466  1.00 22.82 ?  137 ILE   B HG12 1 
ATOM   6006 H HG13 . ILE   B 1 137 ? 36.905 -37.682 -3.086  1.00 22.82 ?  137 ILE   B HG13 1 
ATOM   6007 H HG21 . ILE   B 1 137 ? 33.356 -37.925 -3.405  1.00 20.73 ?  137 ILE   B HG21 1 
ATOM   6008 H HG22 . ILE   B 1 137 ? 33.014 -36.439 -3.011  1.00 20.73 ?  137 ILE   B HG22 1 
ATOM   6009 H HG23 . ILE   B 1 137 ? 33.694 -36.745 -4.413  1.00 20.73 ?  137 ILE   B HG23 1 
ATOM   6010 H HD11 . ILE   B 1 137 ? 36.327 -39.720 -4.043  1.00 25.43 ?  137 ILE   B HD11 1 
ATOM   6011 H HD12 . ILE   B 1 137 ? 35.659 -39.556 -2.610  1.00 25.43 ?  137 ILE   B HD12 1 
ATOM   6012 H HD13 . ILE   B 1 137 ? 34.797 -39.355 -3.932  1.00 25.43 ?  137 ILE   B HD13 1 
ATOM   6013 N N    . HIS   B 1 138 ? 34.290 -34.271 -1.118  1.00 14.15 ?  138 HIS   B N    1 
ATOM   6014 C CA   . HIS   B 1 138 ? 33.340 -33.304 -0.583  1.00 14.74 ?  138 HIS   B CA   1 
ATOM   6015 C C    . HIS   B 1 138 ? 33.763 -31.875 -0.895  1.00 13.82 ?  138 HIS   B C    1 
ATOM   6016 O O    . HIS   B 1 138 ? 32.918 -31.027 -1.204  1.00 13.99 ?  138 HIS   B O    1 
ATOM   6017 C CB   . HIS   B 1 138 ? 33.210 -33.485 0.921   1.00 16.10 ?  138 HIS   B CB   1 
ATOM   6018 C CG   . HIS   B 1 138 ? 32.278 -32.502 1.553   1.00 16.78 ?  138 HIS   B CG   1 
ATOM   6019 N ND1  . HIS   B 1 138 ? 30.936 -32.443 1.241   1.00 17.86 ?  138 HIS   B ND1  1 
ATOM   6020 C CD2  . HIS   B 1 138 ? 32.497 -31.523 2.460   1.00 17.38 ?  138 HIS   B CD2  1 
ATOM   6021 C CE1  . HIS   B 1 138 ? 30.367 -31.477 1.939   1.00 17.95 ?  138 HIS   B CE1  1 
ATOM   6022 N NE2  . HIS   B 1 138 ? 31.292 -30.904 2.688   1.00 17.77 ?  138 HIS   B NE2  1 
ATOM   6023 H H    . HIS   B 1 138 ? 34.729 -34.714 -0.528  1.00 16.97 ?  138 HIS   B H    1 
ATOM   6024 H HA   . HIS   B 1 138 ? 32.471 -33.461 -0.987  1.00 17.69 ?  138 HIS   B HA   1 
ATOM   6025 H HB2  . HIS   B 1 138 ? 32.870 -34.374 1.103   1.00 19.32 ?  138 HIS   B HB2  1 
ATOM   6026 H HB3  . HIS   B 1 138 ? 34.081 -33.370 1.327   1.00 19.32 ?  138 HIS   B HB3  1 
ATOM   6027 H HD1  . HIS   B 1 138 ? 30.530 -32.961 0.682   1.00 21.43 ?  138 HIS   B HD1  1 
ATOM   6028 H HD2  . HIS   B 1 138 ? 33.304 -31.310 2.861   1.00 20.84 ?  138 HIS   B HD2  1 
ATOM   6029 H HE1  . HIS   B 1 138 ? 29.463 -31.249 1.912   1.00 21.53 ?  138 HIS   B HE1  1 
ATOM   6030 N N    . SER   B 1 139 ? 35.059 -31.579 -0.812  1.00 13.55 ?  139 SER   B N    1 
ATOM   6031 C CA   . SER   B 1 139 ? 35.502 -30.230 -1.134  1.00 12.87 ?  139 SER   B CA   1 
ATOM   6032 C C    . SER   B 1 139 ? 35.167 -29.877 -2.574  1.00 12.29 ?  139 SER   B C    1 
ATOM   6033 O O    . SER   B 1 139 ? 34.715 -28.760 -2.853  1.00 11.85 ?  139 SER   B O    1 
ATOM   6034 C CB   . SER   B 1 139 ? 36.999 -30.096 -0.870  1.00 12.91 ?  139 SER   B CB   1 
ATOM   6035 O OG   . SER   B 1 139 ? 37.401 -28.763 -1.134  1.00 13.11 ?  139 SER   B OG   1 
ATOM   6036 H H    . SER   B 1 139 ? 35.680 -32.129 -0.593  1.00 16.26 ?  139 SER   B H    1 
ATOM   6037 H HA   . SER   B 1 139 ? 35.036 -29.609 -0.565  1.00 15.44 ?  139 SER   B HA   1 
ATOM   6038 H HB2  . SER   B 1 139 ? 37.180 -30.309 0.058   1.00 15.48 ?  139 SER   B HB2  1 
ATOM   6039 H HB3  . SER   B 1 139 ? 37.488 -30.698 -1.455  1.00 15.48 ?  139 SER   B HB3  1 
ATOM   6040 H HG   . SER   B 1 139 ? 37.013 -28.235 -0.603  1.00 15.73 ?  139 SER   B HG   1 
ATOM   6041 N N    . LEU   B 1 140 ? 35.364 -30.821 -3.503  1.00 11.68 ?  140 LEU   B N    1 
ATOM   6042 C CA   . LEU   B 1 140 ? 35.000 -30.575 -4.894  1.00 11.77 ?  140 LEU   B CA   1 
ATOM   6043 C C    . LEU   B 1 140 ? 33.500 -30.350 -5.032  1.00 12.05 ?  140 LEU   B C    1 
ATOM   6044 O O    . LEU   B 1 140 ? 33.067 -29.465 -5.773  1.00 12.00 ?  140 LEU   B O    1 
ATOM   6045 C CB   . LEU   B 1 140 ? 35.461 -31.737 -5.775  1.00 12.05 ?  140 LEU   B CB   1 
ATOM   6046 C CG   . LEU   B 1 140 ? 35.113 -31.634 -7.256  1.00 12.11 ?  140 LEU   B CG   1 
ATOM   6047 C CD1  . LEU   B 1 140 ? 35.665 -30.355 -7.872  1.00 12.67 ?  140 LEU   B CD1  1 
ATOM   6048 C CD2  . LEU   B 1 140 ? 35.620 -32.861 -7.995  1.00 13.02 ?  140 LEU   B CD2  1 
ATOM   6049 H H    . LEU   B 1 140 ? 35.699 -31.599 -3.357  1.00 14.00 ?  140 LEU   B H    1 
ATOM   6050 H HA   . LEU   B 1 140 ? 35.457 -29.772 -5.200  1.00 14.11 ?  140 LEU   B HA   1 
ATOM   6051 H HB2  . LEU   B 1 140 ? 36.427 -31.807 -5.712  1.00 14.46 ?  140 LEU   B HB2  1 
ATOM   6052 H HB3  . LEU   B 1 140 ? 35.055 -32.551 -5.444  1.00 14.46 ?  140 LEU   B HB3  1 
ATOM   6053 H HG   . LEU   B 1 140 ? 34.150 -31.606 -7.348  1.00 14.53 ?  140 LEU   B HG   1 
ATOM   6054 H HD11 . LEU   B 1 140 ? 35.516 -30.380 -8.831  1.00 15.20 ?  140 LEU   B HD11 1 
ATOM   6055 H HD12 . LEU   B 1 140 ? 35.205 -29.591 -7.488  1.00 15.20 ?  140 LEU   B HD12 1 
ATOM   6056 H HD13 . LEU   B 1 140 ? 36.614 -30.298 -7.687  1.00 15.20 ?  140 LEU   B HD13 1 
ATOM   6057 H HD21 . LEU   B 1 140 ? 35.389 -32.774 -8.934  1.00 15.62 ?  140 LEU   B HD21 1 
ATOM   6058 H HD22 . LEU   B 1 140 ? 36.581 -32.914 -7.892  1.00 15.62 ?  140 LEU   B HD22 1 
ATOM   6059 H HD23 . LEU   B 1 140 ? 35.197 -33.645 -7.619  1.00 15.62 ?  140 LEU   B HD23 1 
ATOM   6060 N N    . ARG   B 1 141 ? 32.696 -31.139 -4.318  1.00 11.98 ?  141 ARG   B N    1 
ATOM   6061 C CA   . ARG   B 1 141 ? 31.245 -30.963 -4.304  1.00 13.48 ?  141 ARG   B CA   1 
ATOM   6062 C C    . ARG   B 1 141 ? 30.863 -29.552 -3.876  1.00 13.01 ?  141 ARG   B C    1 
ATOM   6063 O O    . ARG   B 1 141 ? 30.060 -28.875 -4.536  1.00 12.85 ?  141 ARG   B O    1 
ATOM   6064 C CB   . ARG   B 1 141 ? 30.652 -31.992 -3.333  1.00 15.03 ?  141 ARG   B CB   1 
ATOM   6065 C CG   . ARG   B 1 141 ? 29.188 -31.863 -2.994  1.00 17.17 ?  141 ARG   B CG   1 
ATOM   6066 C CD   . ARG   B 1 141 ? 28.380 -32.495 -4.050  1.00 19.06 ?  141 ARG   B CD   1 
ATOM   6067 N NE   . ARG   B 1 141 ? 28.124 -31.589 -5.158  1.00 19.43 ?  141 ARG   B NE   1 
ATOM   6068 C CZ   . ARG   B 1 141 ? 28.105 -31.950 -6.433  1.00 19.00 ?  141 ARG   B CZ   1 
ATOM   6069 N NH1  . ARG   B 1 141 ? 28.528 -33.143 -6.821  1.00 19.03 ?  141 ARG   B NH1  1 
ATOM   6070 N NH2  . ARG   B 1 141 ? 27.643 -31.094 -7.341  1.00 19.71 ?  141 ARG   B NH2  1 
ATOM   6071 H H    . ARG   B 1 141 ? 32.974 -31.788 -3.833  1.00 14.37 ?  141 ARG   B H    1 
ATOM   6072 H HA   . ARG   B 1 141 ? 30.889 -31.125 -5.190  1.00 16.17 ?  141 ARG   B HA   1 
ATOM   6073 H HB2  . ARG   B 1 141 ? 30.792 -32.877 -3.712  1.00 18.03 ?  141 ARG   B HB2  1 
ATOM   6074 H HB3  . ARG   B 1 141 ? 31.141 -31.932 -2.500  1.00 18.03 ?  141 ARG   B HB3  1 
ATOM   6075 H HG2  . ARG   B 1 141 ? 29.016 -32.310 -2.154  1.00 20.60 ?  141 ARG   B HG2  1 
ATOM   6076 H HG3  . ARG   B 1 141 ? 28.939 -30.923 -2.929  1.00 20.60 ?  141 ARG   B HG3  1 
ATOM   6077 H HD2  . ARG   B 1 141 ? 28.848 -33.280 -4.385  1.00 22.86 ?  141 ARG   B HD2  1 
ATOM   6078 H HD3  . ARG   B 1 141 ? 27.533 -32.764 -3.672  1.00 22.86 ?  141 ARG   B HD3  1 
ATOM   6079 H HE   . ARG   B 1 141 ? 27.976 -30.763 -4.973  1.00 23.31 ?  141 ARG   B HE   1 
ATOM   6080 H HH11 . ARG   B 1 141 ? 28.813 -33.714 -6.245  1.00 22.83 ?  141 ARG   B HH11 1 
ATOM   6081 H HH12 . ARG   B 1 141 ? 28.508 -33.352 -7.652  1.00 22.83 ?  141 ARG   B HH12 1 
ATOM   6082 H HH21 . ARG   B 1 141 ? 27.366 -30.315 -7.100  1.00 23.64 ?  141 ARG   B HH21 1 
ATOM   6083 H HH22 . ARG   B 1 141 ? 27.637 -31.310 -8.174  1.00 23.64 ?  141 ARG   B HH22 1 
ATOM   6084 N N    . VAL   B 1 142 ? 31.409 -29.102 -2.749  1.00 12.51 ?  142 VAL   B N    1 
ATOM   6085 C CA   . VAL   B 1 142 ? 31.066 -27.772 -2.263  1.00 12.10 ?  142 VAL   B CA   1 
ATOM   6086 C C    . VAL   B 1 142 ? 31.544 -26.710 -3.245  1.00 11.90 ?  142 VAL   B C    1 
ATOM   6087 O O    . VAL   B 1 142 ? 30.845 -25.718 -3.496  1.00 12.41 ?  142 VAL   B O    1 
ATOM   6088 C CB   . VAL   B 1 142 ? 31.611 -27.549 -0.840  1.00 12.51 ?  142 VAL   B CB   1 
ATOM   6089 C CG1  . VAL   B 1 142 ? 31.298 -26.130 -0.362  1.00 12.60 ?  142 VAL   B CG1  1 
ATOM   6090 C CG2  . VAL   B 1 142 ? 31.029 -28.577 0.111   1.00 13.57 ?  142 VAL   B CG2  1 
ATOM   6091 H H    . VAL   B 1 142 ? 31.971 -29.535 -2.261  1.00 15.01 ?  142 VAL   B H    1 
ATOM   6092 H HA   . VAL   B 1 142 ? 30.104 -27.705 -2.215  1.00 14.51 ?  142 VAL   B HA   1 
ATOM   6093 H HB   . VAL   B 1 142 ? 32.576 -27.658 -0.847  1.00 15.00 ?  142 VAL   B HB   1 
ATOM   6094 H HG11 . VAL   B 1 142 ? 31.480 -26.073 0.588   1.00 15.11 ?  142 VAL   B HG11 1 
ATOM   6095 H HG12 . VAL   B 1 142 ? 31.856 -25.502 -0.845  1.00 15.11 ?  142 VAL   B HG12 1 
ATOM   6096 H HG13 . VAL   B 1 142 ? 30.362 -25.943 -0.531  1.00 15.11 ?  142 VAL   B HG13 1 
ATOM   6097 H HG21 . VAL   B 1 142 ? 31.345 -28.392 1.007   1.00 16.28 ?  142 VAL   B HG21 1 
ATOM   6098 H HG22 . VAL   B 1 142 ? 30.061 -28.519 0.080   1.00 16.28 ?  142 VAL   B HG22 1 
ATOM   6099 H HG23 . VAL   B 1 142 ? 31.316 -29.461 -0.166  1.00 16.28 ?  142 VAL   B HG23 1 
ATOM   6100 N N    . CYS   B 1 143 ? 32.727 -26.908 -3.832  1.00 11.94 ?  143 CYS   B N    1 
ATOM   6101 C CA   . CYS   B 1 143 ? 33.224 -25.968 -4.832  1.00 11.76 ?  143 CYS   B CA   1 
ATOM   6102 C C    . CYS   B 1 143 ? 32.228 -25.822 -5.975  1.00 11.56 ?  143 CYS   B C    1 
ATOM   6103 O O    . CYS   B 1 143 ? 31.827 -24.708 -6.334  1.00 11.79 ?  143 CYS   B O    1 
ATOM   6104 C CB   . CYS   B 1 143 ? 34.582 -26.456 -5.352  1.00 11.97 ?  143 CYS   B CB   1 
ATOM   6105 S SG   . CYS   B 1 143 ? 35.338 -25.360 -6.573  1.00 12.47 ?  143 CYS   B SG   1 
ATOM   6106 H H    . CYS   B 1 143 ? 33.256 -27.563 -3.668  1.00 14.32 ?  143 CYS   B H    1 
ATOM   6107 H HA   . CYS   B 1 143 ? 33.357 -25.098 -4.429  1.00 14.10 ?  143 CYS   B HA   1 
ATOM   6108 H HB2  . CYS   B 1 143 ? 35.202 -26.540 -4.609  1.00 14.35 ?  143 CYS   B HB2  1 
ATOM   6109 H HB3  . CYS   B 1 143 ? 34.467 -27.325 -5.770  1.00 14.35 ?  143 CYS   B HB3  1 
ATOM   6110 H HG   . CYS   B 1 143 ? 36.405 -25.803 -6.896  1.00 14.96 ?  143 CYS   B HG   1 
ATOM   6111 N N    . VAL   B 1 144 ? 31.821 -26.942 -6.565  1.00 12.12 ?  144 VAL   B N    1 
ATOM   6112 C CA   . VAL   B 1 144 ? 30.923 -26.892 -7.713  1.00 12.75 ?  144 VAL   B CA   1 
ATOM   6113 C C    . VAL   B 1 144 ? 29.582 -26.270 -7.341  1.00 13.15 ?  144 VAL   B C    1 
ATOM   6114 O O    . VAL   B 1 144 ? 28.968 -25.557 -8.145  1.00 14.55 ?  144 VAL   B O    1 
ATOM   6115 C CB   . VAL   B 1 144 ? 30.764 -28.307 -8.286  1.00 15.44 ?  144 VAL   B CB   1 
ATOM   6116 C CG1  . VAL   B 1 144 ? 29.495 -28.438 -9.114  1.00 17.41 ?  144 VAL   B CG1  1 
ATOM   6117 C CG2  . VAL   B 1 144 ? 32.007 -28.697 -9.086  1.00 15.56 ?  144 VAL   B CG2  1 
ATOM   6118 H H    . VAL   B 1 144 ? 32.047 -27.740 -6.326  1.00 14.53 ?  144 VAL   B H    1 
ATOM   6119 H HA   . VAL   B 1 144 ? 31.316 -26.346 -8.404  1.00 15.29 ?  144 VAL   B HA   1 
ATOM   6120 H HB   . VAL   B 1 144 ? 30.690 -28.940 -7.549  1.00 18.52 ?  144 VAL   B HB   1 
ATOM   6121 H HG11 . VAL   B 1 144 ? 29.563 -29.229 -9.674  1.00 20.89 ?  144 VAL   B HG11 1 
ATOM   6122 H HG12 . VAL   B 1 144 ? 28.735 -28.526 -8.518  1.00 20.89 ?  144 VAL   B HG12 1 
ATOM   6123 H HG13 . VAL   B 1 144 ? 29.398 -27.650 -9.669  1.00 20.89 ?  144 VAL   B HG13 1 
ATOM   6124 H HG21 . VAL   B 1 144 ? 31.893 -29.598 -9.434  1.00 18.66 ?  144 VAL   B HG21 1 
ATOM   6125 H HG22 . VAL   B 1 144 ? 32.115 -28.073 -9.821  1.00 18.66 ?  144 VAL   B HG22 1 
ATOM   6126 H HG23 . VAL   B 1 144 ? 32.780 -28.663 -8.504  1.00 18.66 ?  144 VAL   B HG23 1 
ATOM   6127 N N    . ASP   B 1 145 ? 29.112 -26.520 -6.126  1.00 12.90 ?  145 ASP   B N    1 
ATOM   6128 C CA   . ASP   B 1 145 ? 27.804 -26.050 -5.699  1.00 13.51 ?  145 ASP   B CA   1 
ATOM   6129 C C    . ASP   B 1 145 ? 27.832 -24.626 -5.152  1.00 13.09 ?  145 ASP   B C    1 
ATOM   6130 O O    . ASP   B 1 145 ? 26.769 -24.089 -4.816  1.00 14.95 ?  145 ASP   B O    1 
ATOM   6131 C CB   . ASP   B 1 145 ? 27.219 -26.975 -4.623  1.00 15.03 ?  145 ASP   B CB   1 
ATOM   6132 C CG   . ASP   B 1 145 ? 26.860 -28.352 -5.142  1.00 16.42 ?  145 ASP   B CG   1 
ATOM   6133 O OD1  . ASP   B 1 145 ? 26.764 -28.539 -6.370  1.00 16.92 ?  145 ASP   B OD1  1 
ATOM   6134 O OD2  . ASP   B 1 145 ? 26.673 -29.244 -4.292  1.00 18.66 -1 145 ASP   B OD2  1 
ATOM   6135 H H    . ASP   B 1 145 ? 29.538 -26.961 -5.526  1.00 15.47 ?  145 ASP   B H    1 
ATOM   6136 H HA   . ASP   B 1 145 ? 27.209 -26.045 -6.461  1.00 16.21 ?  145 ASP   B HA   1 
ATOM   6137 H HB2  . ASP   B 1 145 ? 27.864 -27.099 -3.924  1.00 18.03 ?  145 ASP   B HB2  1 
ATOM   6138 H HB3  . ASP   B 1 145 ? 26.408 -26.571 -4.273  1.00 18.03 ?  145 ASP   B HB3  1 
ATOM   6139 N N    . THR   B 1 146 ? 29.005 -24.008 -5.035  1.00 11.77 ?  146 THR   B N    1 
ATOM   6140 C CA   . THR   B 1 146 ? 29.132 -22.690 -4.420  1.00 11.38 ?  146 THR   B CA   1 
ATOM   6141 C C    . THR   B 1 146 ? 29.767 -21.656 -5.332  1.00 11.28 ?  146 THR   B C    1 
ATOM   6142 O O    . THR   B 1 146 ? 29.313 -20.496 -5.372  1.00 11.67 ?  146 THR   B O    1 
ATOM   6143 C CB   . THR   B 1 146 ? 29.960 -22.793 -3.127  1.00 11.57 ?  146 THR   B CB   1 
ATOM   6144 O OG1  . THR   B 1 146 ? 29.387 -23.779 -2.264  1.00 11.71 ?  146 THR   B OG1  1 
ATOM   6145 C CG2  . THR   B 1 146 ? 30.026 -21.457 -2.403  1.00 11.86 ?  146 THR   B CG2  1 
ATOM   6146 H H    . THR   B 1 146 ? 29.757 -24.341 -5.298  1.00 14.11 ?  146 THR   B H    1 
ATOM   6147 H HA   . THR   B 1 146 ? 28.254 -22.368 -4.186  1.00 13.65 ?  146 THR   B HA   1 
ATOM   6148 H HB   . THR   B 1 146 ? 30.865 -23.052 -3.349  1.00 13.87 ?  146 THR   B HB   1 
ATOM   6149 H HG1  . THR   B 1 146 ? 29.413 -24.534 -2.642  1.00 14.04 ?  146 THR   B HG1  1 
ATOM   6150 H HG21 . THR   B 1 146 ? 30.389 -21.581 -1.512  1.00 14.22 ?  146 THR   B HG21 1 
ATOM   6151 H HG22 . THR   B 1 146 ? 30.602 -20.842 -2.890  1.00 14.22 ?  146 THR   B HG22 1 
ATOM   6152 H HG23 . THR   B 1 146 ? 29.142 -21.070 -2.332  1.00 14.22 ?  146 THR   B HG23 1 
ATOM   6153 N N    . VAL   B 1 147 ? 30.832 -22.029 -6.035  1.00 11.33 ?  147 VAL   B N    1 
ATOM   6154 C CA   . VAL   B 1 147 ? 31.557 -21.088 -6.870  1.00 11.09 ?  147 VAL   B CA   1 
ATOM   6155 C C    . VAL   B 1 147 ? 30.830 -20.962 -8.197  1.00 11.36 ?  147 VAL   B C    1 
ATOM   6156 O O    . VAL   B 1 147 ? 30.464 -21.967 -8.822  1.00 12.15 ?  147 VAL   B O    1 
ATOM   6157 C CB   . VAL   B 1 147 ? 33.009 -21.550 -7.067  1.00 11.09 ?  147 VAL   B CB   1 
ATOM   6158 C CG1  . VAL   B 1 147 ? 33.781 -20.530 -7.877  1.00 11.35 ?  147 VAL   B CG1  1 
ATOM   6159 C CG2  . VAL   B 1 147 ? 33.679 -21.763 -5.717  1.00 11.28 ?  147 VAL   B CG2  1 
ATOM   6160 H H    . VAL   B 1 147 ? 31.161 -22.826 -6.046  1.00 13.59 ?  147 VAL   B H    1 
ATOM   6161 H HA   . VAL   B 1 147 ? 31.576 -20.217 -6.442  1.00 13.30 ?  147 VAL   B HA   1 
ATOM   6162 H HB   . VAL   B 1 147 ? 33.019 -22.396 -7.550  1.00 13.30 ?  147 VAL   B HB   1 
ATOM   6163 H HG11 . VAL   B 1 147 ? 34.721 -20.761 -7.862  1.00 13.61 ?  147 VAL   B HG11 1 
ATOM   6164 H HG12 . VAL   B 1 147 ? 33.452 -20.535 -8.789  1.00 13.61 ?  147 VAL   B HG12 1 
ATOM   6165 H HG13 . VAL   B 1 147 ? 33.648 -19.654 -7.481  1.00 13.61 ?  147 VAL   B HG13 1 
ATOM   6166 H HG21 . VAL   B 1 147 ? 34.620 -21.953 -5.856  1.00 13.53 ?  147 VAL   B HG21 1 
ATOM   6167 H HG22 . VAL   B 1 147 ? 33.578 -20.958 -5.187  1.00 13.53 ?  147 VAL   B HG22 1 
ATOM   6168 H HG23 . VAL   B 1 147 ? 33.255 -22.511 -5.266  1.00 13.53 ?  147 VAL   B HG23 1 
ATOM   6169 N N    . ARG   B 1 148 ? 30.621 -19.714 -8.622  1.00 11.16 ?  148 ARG   B N    1 
ATOM   6170 C CA   . ARG   B 1 148 ? 29.996 -19.394 -9.895  1.00 11.68 ?  148 ARG   B CA   1 
ATOM   6171 C C    . ARG   B 1 148 ? 30.956 -18.731 -10.870 1.00 11.58 ?  148 ARG   B C    1 
ATOM   6172 O O    . ARG   B 1 148 ? 30.678 -18.715 -12.069 1.00 12.87 ?  148 ARG   B O    1 
ATOM   6173 C CB   . ARG   B 1 148 ? 28.767 -18.498 -9.672  1.00 12.04 ?  148 ARG   B CB   1 
ATOM   6174 C CG   . ARG   B 1 148 ? 27.674 -19.196 -8.866  1.00 12.74 ?  148 ARG   B CG   1 
ATOM   6175 C CD   . ARG   B 1 148 ? 26.482 -18.296 -8.555  1.00 13.20 ?  148 ARG   B CD   1 
ATOM   6176 N NE   . ARG   B 1 148 ? 26.879 -17.103 -7.818  1.00 13.45 ?  148 ARG   B NE   1 
ATOM   6177 C CZ   . ARG   B 1 148 ? 27.175 -17.075 -6.526  1.00 12.41 ?  148 ARG   B CZ   1 
ATOM   6178 N NH1  . ARG   B 1 148 ? 27.096 -18.158 -5.769  1.00 12.39 ?  148 ARG   B NH1  1 
ATOM   6179 N NH2  . ARG   B 1 148 ? 27.577 -15.930 -5.981  1.00 12.27 ?  148 ARG   B NH2  1 
ATOM   6180 H H    . ARG   B 1 148 ? 30.846 -19.010 -8.169  1.00 13.39 ?  148 ARG   B H    1 
ATOM   6181 H HA   . ARG   B 1 148 ? 29.690 -20.215 -10.300 1.00 14.01 ?  148 ARG   B HA   1 
ATOM   6182 H HB2  . ARG   B 1 148 ? 29.036 -17.701 -9.185  1.00 14.45 ?  148 ARG   B HB2  1 
ATOM   6183 H HB3  . ARG   B 1 148 ? 28.396 -18.250 -10.533 1.00 14.45 ?  148 ARG   B HB3  1 
ATOM   6184 H HG2  . ARG   B 1 148 ? 27.348 -19.959 -9.374  1.00 15.29 ?  148 ARG   B HG2  1 
ATOM   6185 H HG3  . ARG   B 1 148 ? 28.047 -19.501 -8.023  1.00 15.29 ?  148 ARG   B HG3  1 
ATOM   6186 H HD2  . ARG   B 1 148 ? 26.074 -18.016 -9.387  1.00 15.84 ?  148 ARG   B HD2  1 
ATOM   6187 H HD3  . ARG   B 1 148 ? 25.843 -18.792 -8.018  1.00 15.84 ?  148 ARG   B HD3  1 
ATOM   6188 H HE   . ARG   B 1 148 ? 26.929 -16.369 -8.249  1.00 16.14 ?  148 ARG   B HE   1 
ATOM   6189 H HH11 . ARG   B 1 148 ? 26.835 -18.910 -6.103  1.00 14.85 ?  148 ARG   B HH11 1 
ATOM   6190 H HH12 . ARG   B 1 148 ? 27.292 -18.119 -4.927  1.00 14.85 ?  148 ARG   B HH12 1 
ATOM   6191 H HH21 . ARG   B 1 148 ? 27.639 -15.226 -6.463  1.00 14.72 ?  148 ARG   B HH21 1 
ATOM   6192 H HH22 . ARG   B 1 148 ? 27.776 -15.898 -5.143  1.00 14.72 ?  148 ARG   B HH22 1 
ATOM   6193 N N    . THR   B 1 149 ? 32.068 -18.185 -10.384 1.00 11.32 ?  149 THR   B N    1 
ATOM   6194 C CA   . THR   B 1 149 ? 33.111 -17.625 -11.228 1.00 11.60 ?  149 THR   B CA   1 
ATOM   6195 C C    . THR   B 1 149 ? 34.004 -18.762 -11.731 1.00 11.14 ?  149 THR   B C    1 
ATOM   6196 O O    . THR   B 1 149 ? 33.815 -19.930 -11.385 1.00 11.43 ?  149 THR   B O    1 
ATOM   6197 C CB   . THR   B 1 149 ? 33.880 -16.569 -10.442 1.00 11.77 ?  149 THR   B CB   1 
ATOM   6198 O OG1  . THR   B 1 149 ? 34.335 -17.167 -9.225  1.00 11.54 ?  149 THR   B OG1  1 
ATOM   6199 C CG2  . THR   B 1 149 ? 32.993 -15.365 -10.132 1.00 12.66 ?  149 THR   B CG2  1 
ATOM   6200 H H    . THR   B 1 149 ? 32.240 -18.123 -9.544  1.00 13.58 ?  149 THR   B H    1 
ATOM   6201 H HA   . THR   B 1 149 ? 32.705 -17.194 -11.995 1.00 13.91 ?  149 THR   B HA   1 
ATOM   6202 H HB   . THR   B 1 149 ? 34.644 -16.275 -10.960 1.00 14.12 ?  149 THR   B HB   1 
ATOM   6203 H HG1  . THR   B 1 149 ? 34.762 -16.599 -8.767  1.00 13.84 ?  149 THR   B HG1  1 
ATOM   6204 H HG21 . THR   B 1 149 ? 33.501 -14.698 -9.643  1.00 15.19 ?  149 THR   B HG21 1 
ATOM   6205 H HG22 . THR   B 1 149 ? 32.669 -14.972 -10.956 1.00 15.19 ?  149 THR   B HG22 1 
ATOM   6206 H HG23 . THR   B 1 149 ? 32.234 -15.640 -9.593  1.00 15.19 ?  149 THR   B HG23 1 
ATOM   6207 N N    . ASN   B 1 150 ? 34.971 -18.442 -12.582 1.00 11.21 ?  150 ASN   B N    1 
ATOM   6208 C CA   . ASN   B 1 150 ? 35.738 -19.473 -13.275 1.00 11.74 ?  150 ASN   B CA   1 
ATOM   6209 C C    . ASN   B 1 150 ? 36.903 -19.922 -12.401 1.00 11.67 ?  150 ASN   B C    1 
ATOM   6210 O O    . ASN   B 1 150 ? 37.828 -19.148 -12.132 1.00 12.32 ?  150 ASN   B O    1 
ATOM   6211 C CB   . ASN   B 1 150 ? 36.205 -18.944 -14.622 1.00 13.05 ?  150 ASN   B CB   1 
ATOM   6212 C CG   . ASN   B 1 150 ? 35.053 -18.709 -15.557 1.00 15.75 ?  150 ASN   B CG   1 
ATOM   6213 O OD1  . ASN   B 1 150 ? 34.163 -19.547 -15.661 1.00 17.20 ?  150 ASN   B OD1  1 
ATOM   6214 N ND2  . ASN   B 1 150 ? 35.032 -17.553 -16.210 1.00 17.39 ?  150 ASN   B ND2  1 
ATOM   6215 H H    . ASN   B 1 150 ? 35.206 -17.633 -12.776 1.00 13.45 ?  150 ASN   B H    1 
ATOM   6216 H HA   . ASN   B 1 150 ? 35.156 -20.239 -13.440 1.00 14.07 ?  150 ASN   B HA   1 
ATOM   6217 H HB2  . ASN   B 1 150 ? 36.661 -18.099 -14.494 1.00 15.65 ?  150 ASN   B HB2  1 
ATOM   6218 H HB3  . ASN   B 1 150 ? 36.796 -19.589 -15.035 1.00 15.65 ?  150 ASN   B HB3  1 
ATOM   6219 H HD21 . ASN   B 1 150 ? 34.391 -17.373 -16.757 1.00 20.86 ?  150 ASN   B HD21 1 
ATOM   6220 H HD22 . ASN   B 1 150 ? 35.671 -16.984 -16.101 1.00 20.86 ?  150 ASN   B HD22 1 
ATOM   6221 N N    . VAL   B 1 151 ? 36.858 -21.174 -11.955 1.00 11.28 ?  151 VAL   B N    1 
ATOM   6222 C CA   . VAL   B 1 151 ? 37.875 -21.701 -11.061 1.00 11.39 ?  151 VAL   B CA   1 
ATOM   6223 C C    . VAL   B 1 151 ? 38.585 -22.871 -11.734 1.00 11.25 ?  151 VAL   B C    1 
ATOM   6224 O O    . VAL   B 1 151 ? 37.948 -23.805 -12.247 1.00 12.10 ?  151 VAL   B O    1 
ATOM   6225 C CB   . VAL   B 1 151 ? 37.315 -22.029 -9.661  1.00 12.71 ?  151 VAL   B CB   1 
ATOM   6226 C CG1  . VAL   B 1 151 ? 36.159 -23.023 -9.732  1.00 13.86 ?  151 VAL   B CG1  1 
ATOM   6227 C CG2  . VAL   B 1 151 ? 38.425 -22.518 -8.735  1.00 13.17 ?  151 VAL   B CG2  1 
ATOM   6228 H H    . VAL   B 1 151 ? 36.236 -21.739 -12.158 1.00 13.53 ?  151 VAL   B H    1 
ATOM   6229 H HA   . VAL   B 1 151 ? 38.541 -21.008 -10.935 1.00 13.66 ?  151 VAL   B HA   1 
ATOM   6230 H HB   . VAL   B 1 151 ? 36.963 -21.209 -9.279  1.00 15.25 ?  151 VAL   B HB   1 
ATOM   6231 H HG11 . VAL   B 1 151 ? 35.847 -23.206 -8.832  1.00 16.62 ?  151 VAL   B HG11 1 
ATOM   6232 H HG12 . VAL   B 1 151 ? 35.442 -22.638 -10.259 1.00 16.62 ?  151 VAL   B HG12 1 
ATOM   6233 H HG13 . VAL   B 1 151 ? 36.472 -23.842 -10.146 1.00 16.62 ?  151 VAL   B HG13 1 
ATOM   6234 H HG21 . VAL   B 1 151 ? 38.068 -22.598 -7.836  1.00 15.80 ?  151 VAL   B HG21 1 
ATOM   6235 H HG22 . VAL   B 1 151 ? 38.740 -23.379 -9.045  1.00 15.80 ?  151 VAL   B HG22 1 
ATOM   6236 H HG23 . VAL   B 1 151 ? 39.150 -21.873 -8.746  1.00 15.80 ?  151 VAL   B HG23 1 
ATOM   6237 N N    . TYR   B 1 152 ? 39.915 -22.782 -11.743 1.00 10.40 ?  152 TYR   B N    1 
ATOM   6238 C CA   . TYR   B 1 152 ? 40.823 -23.757 -12.322 1.00 10.74 ?  152 TYR   B CA   1 
ATOM   6239 C C    . TYR   B 1 152 ? 41.542 -24.429 -11.160 1.00 10.25 ?  152 TYR   B C    1 
ATOM   6240 O O    . TYR   B 1 152 ? 42.386 -23.812 -10.506 1.00 10.65 ?  152 TYR   B O    1 
ATOM   6241 C CB   . TYR   B 1 152 ? 41.790 -23.038 -13.265 1.00 11.47 ?  152 TYR   B CB   1 
ATOM   6242 C CG   . TYR   B 1 152 ? 41.110 -22.583 -14.533 1.00 12.20 ?  152 TYR   B CG   1 
ATOM   6243 C CD1  . TYR   B 1 152 ? 40.434 -21.369 -14.599 1.00 12.49 ?  152 TYR   B CD1  1 
ATOM   6244 C CD2  . TYR   B 1 152 ? 41.122 -23.389 -15.661 1.00 13.18 ?  152 TYR   B CD2  1 
ATOM   6245 C CE1  . TYR   B 1 152 ? 39.795 -20.970 -15.760 1.00 13.79 ?  152 TYR   B CE1  1 
ATOM   6246 C CE2  . TYR   B 1 152 ? 40.490 -23.002 -16.824 1.00 13.94 ?  152 TYR   B CE2  1 
ATOM   6247 C CZ   . TYR   B 1 152 ? 39.824 -21.793 -16.871 1.00 14.15 ?  152 TYR   B CZ   1 
ATOM   6248 O OH   . TYR   B 1 152 ? 39.196 -21.422 -18.036 1.00 16.44 ?  152 TYR   B OH   1 
ATOM   6249 H H    . TYR   B 1 152 ? 40.341 -22.123 -11.384 1.00 12.47 ?  152 TYR   B H    1 
ATOM   6250 H HA   . TYR   B 1 152 ? 40.323 -24.428 -12.819 1.00 12.88 ?  152 TYR   B HA   1 
ATOM   6251 H HB2  . TYR   B 1 152 ? 42.146 -22.259 -12.810 1.00 13.75 ?  152 TYR   B HB2  1 
ATOM   6252 H HB3  . TYR   B 1 152 ? 42.510 -23.643 -13.502 1.00 13.75 ?  152 TYR   B HB3  1 
ATOM   6253 H HD1  . TYR   B 1 152 ? 40.410 -20.817 -13.848 1.00 14.98 ?  152 TYR   B HD1  1 
ATOM   6254 H HD2  . TYR   B 1 152 ? 41.564 -24.208 -15.631 1.00 15.80 ?  152 TYR   B HD2  1 
ATOM   6255 H HE1  . TYR   B 1 152 ? 39.352 -20.154 -15.791 1.00 16.54 ?  152 TYR   B HE1  1 
ATOM   6256 H HE2  . TYR   B 1 152 ? 40.511 -23.551 -17.572 1.00 16.72 ?  152 TYR   B HE2  1 
ATOM   6257 H HH   . TYR   B 1 152 ? 38.839 -20.668 -17.936 1.00 19.72 ?  152 TYR   B HH   1 
ATOM   6258 N N    . LEU   B 1 153 ? 41.181 -25.686 -10.892 1.00 10.48 ?  153 LEU   B N    1 
ATOM   6259 C CA   . LEU   B 1 153 ? 41.684 -26.432 -9.745  1.00 10.59 ?  153 LEU   B CA   1 
ATOM   6260 C C    . LEU   B 1 153 ? 42.918 -27.234 -10.137 1.00 10.80 ?  153 LEU   B C    1 
ATOM   6261 O O    . LEU   B 1 153 ? 42.900 -27.964 -11.131 1.00 11.69 ?  153 LEU   B O    1 
ATOM   6262 C CB   . LEU   B 1 153 ? 40.603 -27.385 -9.230  1.00 10.69 ?  153 LEU   B CB   1 
ATOM   6263 C CG   . LEU   B 1 153 ? 39.336 -26.731 -8.674  1.00 11.54 ?  153 LEU   B CG   1 
ATOM   6264 C CD1  . LEU   B 1 153 ? 38.244 -27.773 -8.526  1.00 12.05 ?  153 LEU   B CD1  1 
ATOM   6265 C CD2  . LEU   B 1 153 ? 39.618 -26.052 -7.342  1.00 12.35 ?  153 LEU   B CD2  1 
ATOM   6266 H H    . LEU   B 1 153 ? 40.622 -26.139 -11.370 1.00 12.57 ?  153 LEU   B H    1 
ATOM   6267 H HA   . LEU   B 1 153 ? 41.912 -25.816 -9.033  1.00 12.71 ?  153 LEU   B HA   1 
ATOM   6268 H HB2  . LEU   B 1 153 ? 40.332 -27.967 -9.958  1.00 12.82 ?  153 LEU   B HB2  1 
ATOM   6269 H HB3  . LEU   B 1 153 ? 40.982 -27.926 -8.516  1.00 12.82 ?  153 LEU   B HB3  1 
ATOM   6270 H HG   . LEU   B 1 153 ? 39.024 -26.059 -9.298  1.00 13.84 ?  153 LEU   B HG   1 
ATOM   6271 H HD11 . LEU   B 1 153 ? 37.436 -27.338 -8.203  1.00 14.45 ?  153 LEU   B HD11 1 
ATOM   6272 H HD12 . LEU   B 1 153 ? 38.076 -28.179 -9.389  1.00 14.45 ?  153 LEU   B HD12 1 
ATOM   6273 H HD13 . LEU   B 1 153 ? 38.532 -28.445 -7.891  1.00 14.45 ?  153 LEU   B HD13 1 
ATOM   6274 H HD21 . LEU   B 1 153 ? 38.794 -25.678 -6.994  1.00 14.81 ?  153 LEU   B HD21 1 
ATOM   6275 H HD22 . LEU   B 1 153 ? 39.973 -26.707 -6.720  1.00 14.81 ?  153 LEU   B HD22 1 
ATOM   6276 H HD23 . LEU   B 1 153 ? 40.268 -25.344 -7.482  1.00 14.81 ?  153 LEU   B HD23 1 
ATOM   6277 N N    . ALA   B 1 154 ? 43.972 -27.114 -9.336  1.00 10.90 ?  154 ALA   B N    1 
ATOM   6278 C CA   . ALA   B 1 154 ? 45.199 -27.879 -9.511  1.00 11.98 ?  154 ALA   B CA   1 
ATOM   6279 C C    . ALA   B 1 154 ? 45.258 -28.954 -8.434  1.00 12.14 ?  154 ALA   B C    1 
ATOM   6280 O O    . ALA   B 1 154 ? 45.177 -28.650 -7.237  1.00 13.42 ?  154 ALA   B O    1 
ATOM   6281 C CB   . ALA   B 1 154 ? 46.421 -26.970 -9.434  1.00 12.96 ?  154 ALA   B CB   1 
ATOM   6282 H H    . ALA   B 1 154 ? 44.002 -26.573 -8.664  1.00 13.07 ?  154 ALA   B H    1 
ATOM   6283 H HA   . ALA   B 1 154 ? 45.193 -28.310 -10.378 1.00 14.36 ?  154 ALA   B HA   1 
ATOM   6284 H HB1  . ALA   B 1 154 ? 47.224 -27.504 -9.552  1.00 15.55 ?  154 ALA   B HB1  1 
ATOM   6285 H HB2  . ALA   B 1 154 ? 46.365 -26.300 -10.134 1.00 15.55 ?  154 ALA   B HB2  1 
ATOM   6286 H HB3  . ALA   B 1 154 ? 46.442 -26.536 -8.565  1.00 15.55 ?  154 ALA   B HB3  1 
ATOM   6287 N N    . VAL   B 1 155 ? 45.376 -30.204 -8.862  1.00 11.60 ?  155 VAL   B N    1 
ATOM   6288 C CA   . VAL   B 1 155 ? 45.488 -31.347 -7.965  1.00 11.84 ?  155 VAL   B CA   1 
ATOM   6289 C C    . VAL   B 1 155 ? 46.831 -32.016 -8.238  1.00 11.67 ?  155 VAL   B C    1 
ATOM   6290 O O    . VAL   B 1 155 ? 47.068 -32.512 -9.346  1.00 13.05 ?  155 VAL   B O    1 
ATOM   6291 C CB   . VAL   B 1 155 ? 44.332 -32.337 -8.172  1.00 13.17 ?  155 VAL   B CB   1 
ATOM   6292 C CG1  . VAL   B 1 155 ? 44.503 -33.538 -7.262  1.00 12.99 ?  155 VAL   B CG1  1 
ATOM   6293 C CG2  . VAL   B 1 155 ? 43.001 -31.650 -7.918  1.00 14.23 ?  155 VAL   B CG2  1 
ATOM   6294 H H    . VAL   B 1 155 ? 45.401 -30.426 -9.696  1.00 13.92 ?  155 VAL   B H    1 
ATOM   6295 H HA   . VAL   B 1 155 ? 45.472 -31.043 -7.044  1.00 14.21 ?  155 VAL   B HA   1 
ATOM   6296 H HB   . VAL   B 1 155 ? 44.340 -32.647 -9.092  1.00 15.80 ?  155 VAL   B HB   1 
ATOM   6297 H HG11 . VAL   B 1 155 ? 43.677 -34.044 -7.242  1.00 15.59 ?  155 VAL   B HG11 1 
ATOM   6298 H HG12 . VAL   B 1 155 ? 45.221 -34.101 -7.607  1.00 15.59 ?  155 VAL   B HG12 1 
ATOM   6299 H HG13 . VAL   B 1 155 ? 44.727 -33.233 -6.369  1.00 15.59 ?  155 VAL   B HG13 1 
ATOM   6300 H HG21 . VAL   B 1 155 ? 42.291 -32.305 -8.002  1.00 17.07 ?  155 VAL   B HG21 1 
ATOM   6301 H HG22 . VAL   B 1 155 ? 43.007 -31.280 -7.022  1.00 17.07 ?  155 VAL   B HG22 1 
ATOM   6302 H HG23 . VAL   B 1 155 ? 42.881 -30.944 -8.570  1.00 17.07 ?  155 VAL   B HG23 1 
ATOM   6303 N N    . PHE   B 1 156 ? 47.695 -32.053 -7.222  1.00 12.17 ?  156 PHE   B N    1 
ATOM   6304 C CA   . PHE   B 1 156 ? 49.074 -32.507 -7.417  1.00 13.65 ?  156 PHE   B CA   1 
ATOM   6305 C C    . PHE   B 1 156 ? 49.171 -34.007 -7.698  1.00 14.47 ?  156 PHE   B C    1 
ATOM   6306 O O    . PHE   B 1 156 ? 49.899 -34.435 -8.604  1.00 15.92 ?  156 PHE   B O    1 
ATOM   6307 C CB   . PHE   B 1 156 ? 49.900 -32.137 -6.186  1.00 13.76 ?  156 PHE   B CB   1 
ATOM   6308 C CG   . PHE   B 1 156 ? 51.325 -32.598 -6.248  1.00 14.22 ?  156 PHE   B CG   1 
ATOM   6309 C CD1  . PHE   B 1 156 ? 52.208 -32.051 -7.161  1.00 16.11 ?  156 PHE   B CD1  1 
ATOM   6310 C CD2  . PHE   B 1 156 ? 51.786 -33.561 -5.378  1.00 14.68 ?  156 PHE   B CD2  1 
ATOM   6311 C CE1  . PHE   B 1 156 ? 53.528 -32.465 -7.211  1.00 17.07 ?  156 PHE   B CE1  1 
ATOM   6312 C CE2  . PHE   B 1 156 ? 53.103 -33.981 -5.424  1.00 16.24 ?  156 PHE   B CE2  1 
ATOM   6313 C CZ   . PHE   B 1 156 ? 53.970 -33.433 -6.343  1.00 17.01 ?  156 PHE   B CZ   1 
ATOM   6314 H H    . PHE   B 1 156 ? 47.508 -31.823 -6.412  1.00 14.59 ?  156 PHE   B H    1 
ATOM   6315 H HA   . PHE   B 1 156 ? 49.446 -32.036 -8.175  1.00 16.37 ?  156 PHE   B HA   1 
ATOM   6316 H HB2  . PHE   B 1 156 ? 49.907 -31.169 -6.094  1.00 16.50 ?  156 PHE   B HB2  1 
ATOM   6317 H HB3  . PHE   B 1 156 ? 49.495 -32.537 -5.401  1.00 16.50 ?  156 PHE   B HB3  1 
ATOM   6318 H HD1  . PHE   B 1 156 ? 51.913 -31.391 -7.750  1.00 19.33 ?  156 PHE   B HD1  1 
ATOM   6319 H HD2  . PHE   B 1 156 ? 51.201 -33.937 -4.760  1.00 17.61 ?  156 PHE   B HD2  1 
ATOM   6320 H HE1  . PHE   B 1 156 ? 54.113 -32.091 -7.834  1.00 20.48 ?  156 PHE   B HE1  1 
ATOM   6321 H HE2  . PHE   B 1 156 ? 53.398 -34.641 -4.838  1.00 19.48 ?  156 PHE   B HE2  1 
ATOM   6322 H HZ   . PHE   B 1 156 ? 54.853 -33.718 -6.376  1.00 20.40 ?  156 PHE   B HZ   1 
ATOM   6323 N N    . ASP   B 1 157 ? 48.504 -34.826 -6.895  1.00 14.70 ?  157 ASP   B N    1 
ATOM   6324 C CA   . ASP   B 1 157 ? 48.650 -36.274 -6.988  1.00 15.59 ?  157 ASP   B CA   1 
ATOM   6325 C C    . ASP   B 1 157 ? 47.740 -36.821 -8.082  1.00 15.75 ?  157 ASP   B C    1 
ATOM   6326 O O    . ASP   B 1 157 ? 46.513 -36.709 -7.980  1.00 15.15 ?  157 ASP   B O    1 
ATOM   6327 C CB   . ASP   B 1 157 ? 48.277 -36.886 -5.643  1.00 17.05 ?  157 ASP   B CB   1 
ATOM   6328 C CG   . ASP   B 1 157 ? 48.421 -38.398 -5.624  1.00 18.56 ?  157 ASP   B CG   1 
ATOM   6329 O OD1  . ASP   B 1 157 ? 48.760 -39.003 -6.670  1.00 19.25 ?  157 ASP   B OD1  1 
ATOM   6330 O OD2  . ASP   B 1 157 ? 48.210 -38.981 -4.544  1.00 20.58 -1 157 ASP   B OD2  1 
ATOM   6331 H H    . ASP   B 1 157 ? 47.967 -34.566 -6.283  1.00 17.63 ?  157 ASP   B H    1 
ATOM   6332 H HA   . ASP   B 1 157 ? 49.572 -36.506 -7.197  1.00 18.70 ?  157 ASP   B HA   1 
ATOM   6333 H HB2  . ASP   B 1 157 ? 48.851 -36.507 -4.961  1.00 20.45 ?  157 ASP   B HB2  1 
ATOM   6334 H HB3  . ASP   B 1 157 ? 47.349 -36.667 -5.450  1.00 20.45 ?  157 ASP   B HB3  1 
ATOM   6335 N N    . LYS   B 1 158 ? 48.336 -37.441 -9.112  1.00 16.59 ?  158 LYS   B N    1 
ATOM   6336 C CA   . LYS   B 1 158 ? 47.555 -38.038 -10.200 1.00 17.61 ?  158 LYS   B CA   1 
ATOM   6337 C C    . LYS   B 1 158 ? 46.498 -39.007 -9.678  1.00 17.16 ?  158 LYS   B C    1 
ATOM   6338 O O    . LYS   B 1 158 ? 45.395 -39.098 -10.234 1.00 17.13 ?  158 LYS   B O    1 
ATOM   6339 C CB   . LYS   B 1 158 ? 48.496 -38.748 -11.185 1.00 19.50 ?  158 LYS   B CB   1 
ATOM   6340 C CG   . LYS   B 1 158 ? 47.807 -39.651 -12.202 1.00 21.57 ?  158 LYS   B CG   1 
ATOM   6341 C CD   . LYS   B 1 158 ? 46.960 -38.876 -13.187 1.00 23.40 ?  158 LYS   B CD   1 
ATOM   6342 C CE   . LYS   B 1 158 ? 46.393 -39.802 -14.249 1.00 24.99 ?  158 LYS   B CE   1 
ATOM   6343 N NZ   . LYS   B 1 158 ? 45.310 -39.148 -15.037 1.00 24.74 ?  158 LYS   B NZ   1 
ATOM   6344 H H    . LYS   B 1 158 ? 49.192 -37.520 -9.209  1.00 19.90 ?  158 LYS   B H    1 
ATOM   6345 H HA   . LYS   B 1 158 ? 47.103 -37.332 -10.690 1.00 21.12 ?  158 LYS   B HA   1 
ATOM   6346 H HB2  . LYS   B 1 158 ? 48.990 -38.074 -11.688 1.00 23.39 ?  158 LYS   B HB2  1 
ATOM   6347 H HB3  . LYS   B 1 158 ? 49.120 -39.294 -10.684 1.00 23.39 ?  158 LYS   B HB3  1 
ATOM   6348 H HG2  . LYS   B 1 158 ? 48.487 -40.123 -12.708 1.00 25.87 ?  158 LYS   B HG2  1 
ATOM   6349 H HG3  . LYS   B 1 158 ? 47.240 -40.295 -11.748 1.00 25.87 ?  158 LYS   B HG3  1 
ATOM   6350 H HD2  . LYS   B 1 158 ? 46.222 -38.455 -12.720 1.00 28.07 ?  158 LYS   B HD2  1 
ATOM   6351 H HD3  . LYS   B 1 158 ? 47.508 -38.207 -13.627 1.00 28.07 ?  158 LYS   B HD3  1 
ATOM   6352 H HE2  . LYS   B 1 158 ? 47.098 -40.059 -14.861 1.00 29.98 ?  158 LYS   B HE2  1 
ATOM   6353 H HE3  . LYS   B 1 158 ? 46.018 -40.589 -13.821 1.00 29.98 ?  158 LYS   B HE3  1 
ATOM   6354 H HZ1  . LYS   B 1 158 ? 44.996 -39.711 -15.649 1.00 29.68 ?  158 LYS   B HZ1  1 
ATOM   6355 H HZ2  . LYS   B 1 158 ? 44.646 -38.904 -14.498 1.00 29.68 ?  158 LYS   B HZ2  1 
ATOM   6356 H HZ3  . LYS   B 1 158 ? 45.630 -38.424 -15.446 1.00 29.68 ?  158 LYS   B HZ3  1 
ATOM   6357 N N    . ASN   B 1 159 ? 46.824 -39.771 -8.633  1.00 17.42 ?  159 ASN   B N    1 
ATOM   6358 C CA   . ASN   B 1 159 ? 45.869 -40.750 -8.125  1.00 18.21 ?  159 ASN   B CA   1 
ATOM   6359 C C    . ASN   B 1 159 ? 44.672 -40.078 -7.452  1.00 17.31 ?  159 ASN   B C    1 
ATOM   6360 O O    . ASN   B 1 159 ? 43.543 -40.580 -7.554  1.00 17.14 ?  159 ASN   B O    1 
ATOM   6361 C CB   . ASN   B 1 159 ? 46.575 -41.723 -7.186  1.00 20.17 ?  159 ASN   B CB   1 
ATOM   6362 C CG   . ASN   B 1 159 ? 47.611 -42.565 -7.903  1.00 22.02 ?  159 ASN   B CG   1 
ATOM   6363 O OD1  . ASN   B 1 159 ? 47.366 -43.069 -9.007  1.00 22.92 ?  159 ASN   B OD1  1 
ATOM   6364 N ND2  . ASN   B 1 159 ? 48.775 -42.732 -7.278  1.00 23.04 ?  159 ASN   B ND2  1 
ATOM   6365 H H    . ASN   B 1 159 ? 47.570 -39.730 -8.212  1.00 20.90 ?  159 ASN   B H    1 
ATOM   6366 H HA   . ASN   B 1 159 ? 45.534 -41.261 -8.879  1.00 21.85 ?  159 ASN   B HA   1 
ATOM   6367 H HB2  . ASN   B 1 159 ? 47.025 -41.225 -6.488  1.00 24.20 ?  159 ASN   B HB2  1 
ATOM   6368 H HB3  . ASN   B 1 159 ? 45.920 -42.324 -6.803  1.00 24.20 ?  159 ASN   B HB3  1 
ATOM   6369 H HD21 . ASN   B 1 159 ? 49.400 -43.202 -7.644  1.00 27.64 ?  159 ASN   B HD21 1 
ATOM   6370 H HD22 . ASN   B 1 159 ? 48.905 -42.381 -6.504  1.00 27.64 ?  159 ASN   B HD22 1 
ATOM   6371 N N    . LEU   B 1 160 ? 44.881 -38.943 -6.777  1.00 16.22 ?  160 LEU   B N    1 
ATOM   6372 C CA   . LEU   B 1 160 ? 43.744 -38.216 -6.227  1.00 15.52 ?  160 LEU   B CA   1 
ATOM   6373 C C    . LEU   B 1 160 ? 42.956 -37.550 -7.339  1.00 14.65 ?  160 LEU   B C    1 
ATOM   6374 O O    . LEU   B 1 160 ? 41.721 -37.553 -7.320  1.00 14.27 ?  160 LEU   B O    1 
ATOM   6375 C CB   . LEU   B 1 160 ? 44.205 -37.185 -5.198  1.00 15.41 ?  160 LEU   B CB   1 
ATOM   6376 C CG   . LEU   B 1 160 ? 43.079 -36.288 -4.663  1.00 15.00 ?  160 LEU   B CG   1 
ATOM   6377 C CD1  . LEU   B 1 160 ? 41.944 -37.104 -4.061  1.00 15.99 ?  160 LEU   B CD1  1 
ATOM   6378 C CD2  . LEU   B 1 160 ? 43.618 -35.300 -3.645  1.00 14.96 ?  160 LEU   B CD2  1 
ATOM   6379 H H    . LEU   B 1 160 ? 45.655 -38.585 -6.636  1.00 19.46 ?  160 LEU   B H    1 
ATOM   6380 H HA   . LEU   B 1 160 ? 43.161 -38.847 -5.786  1.00 18.61 ?  160 LEU   B HA   1 
ATOM   6381 H HB2  . LEU   B 1 160 ? 44.599 -37.659 -4.445  1.00 18.48 ?  160 LEU   B HB2  1 
ATOM   6382 H HB3  . LEU   B 1 160 ? 44.876 -36.614 -5.607  1.00 18.48 ?  160 LEU   B HB3  1 
ATOM   6383 H HG   . LEU   B 1 160 ? 42.716 -35.777 -5.398  1.00 17.99 ?  160 LEU   B HG   1 
ATOM   6384 H HD11 . LEU   B 1 160 ? 41.312 -36.499 -3.644  1.00 19.19 ?  160 LEU   B HD11 1 
ATOM   6385 H HD12 . LEU   B 1 160 ? 41.504 -37.606 -4.765  1.00 19.19 ?  160 LEU   B HD12 1 
ATOM   6386 H HD13 . LEU   B 1 160 ? 42.307 -37.712 -3.397  1.00 19.19 ?  160 LEU   B HD13 1 
ATOM   6387 H HD21 . LEU   B 1 160 ? 42.894 -34.731 -3.345  1.00 17.94 ?  160 LEU   B HD21 1 
ATOM   6388 H HD22 . LEU   B 1 160 ? 43.990 -35.788 -2.893  1.00 17.94 ?  160 LEU   B HD22 1 
ATOM   6389 H HD23 . LEU   B 1 160 ? 44.311 -34.763 -4.063  1.00 17.94 ?  160 LEU   B HD23 1 
ATOM   6390 N N    . TYR   B 1 161 ? 43.655 -36.980 -8.321  1.00 14.83 ?  161 TYR   B N    1 
ATOM   6391 C CA   . TYR   B 1 161 ? 42.986 -36.415 -9.486  1.00 14.61 ?  161 TYR   B CA   1 
ATOM   6392 C C    . TYR   B 1 161 ? 42.050 -37.439 -10.114 1.00 15.07 ?  161 TYR   B C    1 
ATOM   6393 O O    . TYR   B 1 161 ? 40.878 -37.150 -10.369 1.00 14.64 ?  161 TYR   B O    1 
ATOM   6394 C CB   . TYR   B 1 161 ? 44.031 -35.927 -10.497 1.00 15.30 ?  161 TYR   B CB   1 
ATOM   6395 C CG   . TYR   B 1 161 ? 43.460 -35.465 -11.818 1.00 15.69 ?  161 TYR   B CG   1 
ATOM   6396 C CD1  . TYR   B 1 161 ? 43.062 -34.146 -11.997 1.00 15.61 ?  161 TYR   B CD1  1 
ATOM   6397 C CD2  . TYR   B 1 161 ? 43.303 -36.347 -12.883 1.00 16.41 ?  161 TYR   B CD2  1 
ATOM   6398 C CE1  . TYR   B 1 161 ? 42.535 -33.718 -13.192 1.00 16.75 ?  161 TYR   B CE1  1 
ATOM   6399 C CE2  . TYR   B 1 161 ? 42.770 -35.926 -14.083 1.00 17.26 ?  161 TYR   B CE2  1 
ATOM   6400 C CZ   . TYR   B 1 161 ? 42.392 -34.609 -14.232 1.00 17.34 ?  161 TYR   B CZ   1 
ATOM   6401 O OH   . TYR   B 1 161 ? 41.859 -34.173 -15.420 1.00 19.18 ?  161 TYR   B OH   1 
ATOM   6402 H H    . TYR   B 1 161 ? 44.511 -36.921 -8.346  1.00 17.79 ?  161 TYR   B H    1 
ATOM   6403 H HA   . TYR   B 1 161 ? 42.455 -35.652 -9.211  1.00 17.52 ?  161 TYR   B HA   1 
ATOM   6404 H HB2  . TYR   B 1 161 ? 44.508 -35.173 -10.111 1.00 18.35 ?  161 TYR   B HB2  1 
ATOM   6405 H HB3  . TYR   B 1 161 ? 44.648 -36.645 -10.685 1.00 18.35 ?  161 TYR   B HB3  1 
ATOM   6406 H HD1  . TYR   B 1 161 ? 43.157 -33.533 -11.302 1.00 18.72 ?  161 TYR   B HD1  1 
ATOM   6407 H HD2  . TYR   B 1 161 ? 43.554 -37.236 -12.788 1.00 19.68 ?  161 TYR   B HD2  1 
ATOM   6408 H HE1  . TYR   B 1 161 ? 42.278 -32.825 -13.297 1.00 20.10 ?  161 TYR   B HE1  1 
ATOM   6409 H HE2  . TYR   B 1 161 ? 42.671 -36.523 -14.791 1.00 20.70 ?  161 TYR   B HE2  1 
ATOM   6410 H HH   . TYR   B 1 161 ? 41.827 -34.810 -15.970 1.00 23.01 ?  161 TYR   B HH   1 
ATOM   6411 N N    . ASP   B 1 162 ? 42.549 -38.656 -10.345 1.00 15.45 ?  162 ASP   B N    1 
ATOM   6412 C CA   . ASP   B 1 162 ? 41.725 -39.692 -10.965 1.00 15.95 ?  162 ASP   B CA   1 
ATOM   6413 C C    . ASP   B 1 162 ? 40.516 -40.034 -10.102 1.00 15.24 ?  162 ASP   B C    1 
ATOM   6414 O O    . ASP   B 1 162 ? 39.415 -40.252 -10.621 1.00 15.76 ?  162 ASP   B O    1 
ATOM   6415 C CB   . ASP   B 1 162 ? 42.561 -40.949 -11.213 1.00 17.28 ?  162 ASP   B CB   1 
ATOM   6416 C CG   . ASP   B 1 162 ? 43.570 -40.783 -12.333 1.00 18.42 ?  162 ASP   B CG   1 
ATOM   6417 O OD1  . ASP   B 1 162 ? 43.444 -39.844 -13.141 1.00 18.56 ?  162 ASP   B OD1  1 
ATOM   6418 O OD2  . ASP   B 1 162 ? 44.486 -41.628 -12.419 1.00 19.90 -1 162 ASP   B OD2  1 
ATOM   6419 H H    . ASP   B 1 162 ? 43.349 -38.899 -10.156 1.00 18.53 ?  162 ASP   B H    1 
ATOM   6420 H HA   . ASP   B 1 162 ? 41.404 -39.369 -11.821 1.00 19.14 ?  162 ASP   B HA   1 
ATOM   6421 H HB2  . ASP   B 1 162 ? 43.052 -41.164 -10.406 1.00 20.73 ?  162 ASP   B HB2  1 
ATOM   6422 H HB3  . ASP   B 1 162 ? 41.973 -41.675 -11.454 1.00 20.73 ?  162 ASP   B HB3  1 
ATOM   6423 N N    A LYS   B 1 163 ? 40.697 -40.093 -8.781  0.40 15.03 ?  163 LYS   B N    1 
ATOM   6424 N N    B LYS   B 1 163 ? 40.702 -40.107 -8.783  0.60 14.62 ?  163 LYS   B N    1 
ATOM   6425 C CA   A LYS   B 1 163 ? 39.569 -40.388 -7.903  0.40 15.46 ?  163 LYS   B CA   1 
ATOM   6426 C CA   B LYS   B 1 163 ? 39.577 -40.384 -7.898  0.60 15.10 ?  163 LYS   B CA   1 
ATOM   6427 C C    A LYS   B 1 163 ? 38.528 -39.275 -7.946  0.40 14.29 ?  163 LYS   B C    1 
ATOM   6428 C C    B LYS   B 1 163 ? 38.531 -39.278 -7.971  0.60 14.13 ?  163 LYS   B C    1 
ATOM   6429 O O    A LYS   B 1 163 ? 37.320 -39.545 -7.929  0.40 14.71 ?  163 LYS   B O    1 
ATOM   6430 O O    B LYS   B 1 163 ? 37.324 -39.553 -8.006  0.60 14.77 ?  163 LYS   B O    1 
ATOM   6431 C CB   A LYS   B 1 163 ? 40.051 -40.602 -6.470  0.40 17.53 ?  163 LYS   B CB   1 
ATOM   6432 C CB   B LYS   B 1 163 ? 40.067 -40.548 -6.462  0.60 17.29 ?  163 LYS   B CB   1 
ATOM   6433 C CG   A LYS   B 1 163 ? 38.963 -41.145 -5.557  0.40 20.52 ?  163 LYS   B CG   1 
ATOM   6434 C CG   B LYS   B 1 163 ? 38.988 -41.038 -5.516  0.60 21.02 ?  163 LYS   B CG   1 
ATOM   6435 C CD   A LYS   B 1 163 ? 39.356 -41.106 -4.092  0.40 22.74 ?  163 LYS   B CD   1 
ATOM   6436 C CD   B LYS   B 1 163 ? 39.499 -41.218 -4.099  0.60 23.75 ?  163 LYS   B CD   1 
ATOM   6437 C CE   A LYS   B 1 163 ? 38.274 -41.740 -3.231  0.40 24.07 ?  163 LYS   B CE   1 
ATOM   6438 C CE   B LYS   B 1 163 ? 38.435 -41.862 -3.222  0.60 25.69 ?  163 LYS   B CE   1 
ATOM   6439 N NZ   A LYS   B 1 163 ? 38.434 -41.419 -1.787  0.40 24.74 ?  163 LYS   B NZ   1 
ATOM   6440 N NZ   B LYS   B 1 163 ? 38.731 -41.725 -1.768  0.60 27.63 ?  163 LYS   B NZ   1 
ATOM   6441 H H    A LYS   B 1 163 ? 41.447 -39.967 -8.380  0.40 18.03 ?  163 LYS   B H    1 
ATOM   6442 H H    B LYS   B 1 163 ? 41.460 -39.999 -8.389  0.60 17.54 ?  163 LYS   B H    1 
ATOM   6443 H HA   A LYS   B 1 163 ? 39.147 -41.208 -8.203  0.40 18.54 ?  163 LYS   B HA   1 
ATOM   6444 H HA   B LYS   B 1 163 ? 39.161 -41.215 -8.174  0.60 18.12 ?  163 LYS   B HA   1 
ATOM   6445 H HB2  A LYS   B 1 163 ? 40.784 -41.241 -6.474  0.40 21.03 ?  163 LYS   B HB2  1 
ATOM   6446 H HB2  B LYS   B 1 163 ? 40.792 -41.194 -6.450  0.60 20.74 ?  163 LYS   B HB2  1 
ATOM   6447 H HB3  A LYS   B 1 163 ? 40.352 -39.756 -6.107  0.40 21.03 ?  163 LYS   B HB3  1 
ATOM   6448 H HB3  B LYS   B 1 163 ? 40.383 -39.691 -6.138  0.60 20.74 ?  163 LYS   B HB3  1 
ATOM   6449 H HG2  A LYS   B 1 163 ? 38.160 -40.613 -5.665  0.40 24.62 ?  163 LYS   B HG2  1 
ATOM   6450 H HG2  B LYS   B 1 163 ? 38.264 -40.394 -5.496  0.60 25.22 ?  163 LYS   B HG2  1 
ATOM   6451 H HG3  A LYS   B 1 163 ? 38.783 -42.069 -5.795  0.40 24.62 ?  163 LYS   B HG3  1 
ATOM   6452 H HG3  B LYS   B 1 163 ? 38.658 -41.898 -5.829  0.60 25.22 ?  163 LYS   B HG3  1 
ATOM   6453 H HD2  A LYS   B 1 163 ? 40.179 -41.604 -3.965  0.40 27.28 ?  163 LYS   B HD2  1 
ATOM   6454 H HD2  B LYS   B 1 163 ? 40.280 -41.794 -4.109  0.60 28.49 ?  163 LYS   B HD2  1 
ATOM   6455 H HD3  A LYS   B 1 163 ? 39.472 -40.184 -3.814  0.40 27.28 ?  163 LYS   B HD3  1 
ATOM   6456 H HD3  B LYS   B 1 163 ? 39.722 -40.351 -3.726  0.60 28.49 ?  163 LYS   B HD3  1 
ATOM   6457 H HE2  A LYS   B 1 163 ? 37.404 -41.424 -3.521  0.40 28.87 ?  163 LYS   B HE2  1 
ATOM   6458 H HE2  B LYS   B 1 163 ? 37.579 -41.440 -3.398  0.60 30.82 ?  163 LYS   B HE2  1 
ATOM   6459 H HE3  A LYS   B 1 163 ? 38.320 -42.702 -3.330  0.40 28.87 ?  163 LYS   B HE3  1 
ATOM   6460 H HE3  B LYS   B 1 163 ? 38.385 -42.809 -3.430  0.60 30.82 ?  163 LYS   B HE3  1 
ATOM   6461 H HZ1  A LYS   B 1 163 ? 37.784 -41.804 -1.316  0.40 29.68 ?  163 LYS   B HZ1  1 
ATOM   6462 H HZ1  B LYS   B 1 163 ? 38.088 -42.111 -1.289  0.60 33.15 ?  163 LYS   B HZ1  1 
ATOM   6463 H HZ2  A LYS   B 1 163 ? 39.219 -41.720 -1.496  0.40 29.68 ?  163 LYS   B HZ2  1 
ATOM   6464 H HZ2  B LYS   B 1 163 ? 39.508 -42.113 -1.578  0.60 33.15 ?  163 LYS   B HZ2  1 
ATOM   6465 H HZ3  A LYS   B 1 163 ? 38.398 -40.538 -1.664  0.40 29.68 ?  163 LYS   B HZ3  1 
ATOM   6466 H HZ3  B LYS   B 1 163 ? 38.776 -40.863 -1.548  0.60 33.15 ?  163 LYS   B HZ3  1 
ATOM   6467 N N    . LEU   B 1 164 ? 38.979 -38.020 -7.997  1.00 13.03 ?  164 LEU   B N    1 
ATOM   6468 C CA   . LEU   B 1 164 ? 38.060 -36.887 -8.051  1.00 13.06 ?  164 LEU   B CA   1 
ATOM   6469 C C    . LEU   B 1 164 ? 37.287 -36.865 -9.364  1.00 13.19 ?  164 LEU   B C    1 
ATOM   6470 O O    . LEU   B 1 164 ? 36.064 -36.669 -9.373  1.00 14.31 ?  164 LEU   B O    1 
ATOM   6471 C CB   . LEU   B 1 164 ? 38.853 -35.589 -7.883  1.00 12.80 ?  164 LEU   B CB   1 
ATOM   6472 C CG   . LEU   B 1 164 ? 39.372 -35.302 -6.476  1.00 13.40 ?  164 LEU   B CG   1 
ATOM   6473 C CD1  . LEU   B 1 164 ? 40.470 -34.253 -6.513  1.00 13.17 ?  164 LEU   B CD1  1 
ATOM   6474 C CD2  . LEU   B 1 164 ? 38.238 -34.856 -5.566  1.00 15.01 ?  164 LEU   B CD2  1 
ATOM   6475 H H    A LEU   B 1 164 ? 39.813 -37.803 -8.007  0.40 15.63 ?  164 LEU   B H    1 
ATOM   6476 H H    B LEU   B 1 164 ? 39.812 -37.801 -7.985  0.60 15.63 ?  164 LEU   B H    1 
ATOM   6477 H HA   . LEU   B 1 164 ? 37.426 -36.957 -7.329  1.00 15.66 ?  164 LEU   B HA   1 
ATOM   6478 H HB2  . LEU   B 1 164 ? 39.622 -35.620 -8.474  1.00 15.35 ?  164 LEU   B HB2  1 
ATOM   6479 H HB3  . LEU   B 1 164 ? 38.281 -34.849 -8.136  1.00 15.35 ?  164 LEU   B HB3  1 
ATOM   6480 H HG   . LEU   B 1 164 ? 39.754 -36.112 -6.110  1.00 16.08 ?  164 LEU   B HG   1 
ATOM   6481 H HD11 . LEU   B 1 164 ? 40.778 -34.083 -5.606  1.00 15.80 ?  164 LEU   B HD11 1 
ATOM   6482 H HD12 . LEU   B 1 164 ? 41.209 -34.580 -7.053  1.00 15.80 ?  164 LEU   B HD12 1 
ATOM   6483 H HD13 . LEU   B 1 164 ? 40.119 -33.434 -6.898  1.00 15.80 ?  164 LEU   B HD13 1 
ATOM   6484 H HD21 . LEU   B 1 164 ? 38.599 -34.638 -4.692  1.00 18.00 ?  164 LEU   B HD21 1 
ATOM   6485 H HD22 . LEU   B 1 164 ? 37.809 -34.075 -5.950  1.00 18.00 ?  164 LEU   B HD22 1 
ATOM   6486 H HD23 . LEU   B 1 164 ? 37.596 -35.580 -5.486  1.00 18.00 ?  164 LEU   B HD23 1 
ATOM   6487 N N    . VAL   B 1 165 ? 37.987 -37.042 -10.486 1.00 14.34 ?  165 VAL   B N    1 
ATOM   6488 C CA   . VAL   B 1 165 ? 37.338 -36.985 -11.792 1.00 15.69 ?  165 VAL   B CA   1 
ATOM   6489 C C    . VAL   B 1 165 ? 36.418 -38.182 -11.978 1.00 16.94 ?  165 VAL   B C    1 
ATOM   6490 O O    . VAL   B 1 165 ? 35.259 -38.043 -12.387 1.00 17.86 ?  165 VAL   B O    1 
ATOM   6491 C CB   . VAL   B 1 165 ? 38.392 -36.897 -12.912 1.00 16.71 ?  165 VAL   B CB   1 
ATOM   6492 C CG1  . VAL   B 1 165 ? 37.740 -36.989 -14.279 1.00 18.18 ?  165 VAL   B CG1  1 
ATOM   6493 C CG2  . VAL   B 1 165 ? 39.190 -35.613 -12.782 1.00 16.67 ?  165 VAL   B CG2  1 
ATOM   6494 H H    . VAL   B 1 165 ? 38.835 -37.197 -10.517 1.00 17.20 ?  165 VAL   B H    1 
ATOM   6495 H HA   . VAL   B 1 165 ? 36.795 -36.186 -11.838 1.00 18.82 ?  165 VAL   B HA   1 
ATOM   6496 H HB   . VAL   B 1 165 ? 39.013 -37.638 -12.823 1.00 20.05 ?  165 VAL   B HB   1 
ATOM   6497 H HG11 . VAL   B 1 165 ? 38.378 -36.705 -14.951 1.00 21.81 ?  165 VAL   B HG11 1 
ATOM   6498 H HG12 . VAL   B 1 165 ? 37.484 -37.912 -14.442 1.00 21.81 ?  165 VAL   B HG12 1 
ATOM   6499 H HG13 . VAL   B 1 165 ? 36.961 -36.419 -14.296 1.00 21.81 ?  165 VAL   B HG13 1 
ATOM   6500 H HG21 . VAL   B 1 165 ? 39.830 -35.560 -13.510 1.00 20.00 ?  165 VAL   B HG21 1 
ATOM   6501 H HG22 . VAL   B 1 165 ? 38.583 -34.856 -12.824 1.00 20.00 ?  165 VAL   B HG22 1 
ATOM   6502 H HG23 . VAL   B 1 165 ? 39.659 -35.611 -11.932 1.00 20.00 ?  165 VAL   B HG23 1 
ATOM   6503 N N    . SER   B 1 166 ? 36.923 -39.380 -11.674 1.00 17.61 ?  166 SER   B N    1 
ATOM   6504 C CA   . SER   B 1 166 ? 36.162 -40.585 -11.961 1.00 18.58 ?  166 SER   B CA   1 
ATOM   6505 C C    . SER   B 1 166 ? 34.903 -40.670 -11.114 1.00 18.83 ?  166 SER   B C    1 
ATOM   6506 O O    . SER   B 1 166 ? 33.933 -41.296 -11.539 1.00 20.22 ?  166 SER   B O    1 
ATOM   6507 C CB   . SER   B 1 166 ? 37.022 -41.839 -11.784 1.00 19.45 ?  166 SER   B CB   1 
ATOM   6508 O OG   . SER   B 1 166 ? 37.387 -42.035 -10.431 1.00 19.09 ?  166 SER   B OG   1 
ATOM   6509 H H    . SER   B 1 166 ? 37.698 -39.516 -11.313 1.00 21.12 ?  166 SER   B H    1 
ATOM   6510 H HA   . SER   B 1 166 ? 35.886 -40.558 -12.888 1.00 22.28 ?  166 SER   B HA   1 
ATOM   6511 H HB2  . SER   B 1 166 ? 36.514 -42.612 -12.084 1.00 23.34 ?  166 SER   B HB2  1 
ATOM   6512 H HB3  . SER   B 1 166 ? 37.824 -41.750 -12.325 1.00 23.34 ?  166 SER   B HB3  1 
ATOM   6513 H HG   . SER   B 1 166 ? 37.846 -41.382 -10.164 1.00 22.90 ?  166 SER   B HG   1 
ATOM   6514 N N    . SER   B 1 167 ? 34.884 -40.058 -9.929  1.00 17.70 ?  167 SER   B N    1 
ATOM   6515 C CA   . SER   B 1 167 ? 33.723 -40.114 -9.045  1.00 17.08 ?  167 SER   B CA   1 
ATOM   6516 C C    . SER   B 1 167 ? 32.807 -38.895 -9.143  1.00 16.95 ?  167 SER   B C    1 
ATOM   6517 O O    . SER   B 1 167 ? 31.730 -38.894 -8.535  1.00 17.13 ?  167 SER   B O    1 
ATOM   6518 C CB   . SER   B 1 167 ? 34.162 -40.303 -7.587  1.00 17.10 ?  167 SER   B CB   1 
ATOM   6519 O OG   . SER   B 1 167 ? 34.829 -39.143 -7.103  1.00 16.81 ?  167 SER   B OG   1 
ATOM   6520 H H    . SER   B 1 167 ? 35.536 -39.597 -9.615  1.00 21.23 ?  167 SER   B H    1 
ATOM   6521 H HA   . SER   B 1 167 ? 33.194 -40.890 -9.289  1.00 20.49 ?  167 SER   B HA   1 
ATOM   6522 H HB2  . SER   B 1 167 ? 33.375 -40.473 -7.042  1.00 20.52 ?  167 SER   B HB2  1 
ATOM   6523 H HB3  . SER   B 1 167 ? 34.762 -41.070 -7.538  1.00 20.52 ?  167 SER   B HB3  1 
ATOM   6524 H HG   . SER   B 1 167 ? 35.514 -39.004 -7.568  1.00 20.16 ?  167 SER   B HG   1 
ATOM   6525 N N    . PHE   B 1 168 ? 33.180 -37.868 -9.904  1.00 16.77 ?  168 PHE   B N    1 
ATOM   6526 C CA   . PHE   B 1 168 ? 32.347 -36.667 -9.969  1.00 16.29 ?  168 PHE   B CA   1 
ATOM   6527 C C    . PHE   B 1 168 ? 31.028 -36.928 -10.693 1.00 14.36 ?  168 PHE   B C    1 
ATOM   6528 O O    . PHE   B 1 168 ? 29.988 -36.333 -10.351 1.00 14.98 ?  168 PHE   B O    1 
ATOM   6529 C CB   . PHE   B 1 168 ? 33.110 -35.542 -10.661 1.00 17.07 ?  168 PHE   B CB   1 
ATOM   6530 C CG   . PHE   B 1 168 ? 32.323 -34.284 -10.775 1.00 16.93 ?  168 PHE   B CG   1 
ATOM   6531 C CD1  . PHE   B 1 168 ? 32.004 -33.552 -9.639  1.00 18.11 ?  168 PHE   B CD1  1 
ATOM   6532 C CD2  . PHE   B 1 168 ? 31.876 -33.839 -12.002 1.00 16.46 ?  168 PHE   B CD2  1 
ATOM   6533 C CE1  . PHE   B 1 168 ? 31.256 -32.396 -9.725  1.00 18.75 ?  168 PHE   B CE1  1 
ATOM   6534 C CE2  . PHE   B 1 168 ? 31.139 -32.666 -12.100 1.00 17.41 ?  168 PHE   B CE2  1 
ATOM   6535 C CZ   . PHE   B 1 168 ? 30.823 -31.948 -10.956 1.00 18.12 ?  168 PHE   B CZ   1 
ATOM   6536 H H    . PHE   B 1 168 ? 33.898 -37.837 -10.376 1.00 20.11 ?  168 PHE   B H    1 
ATOM   6537 H HA   . PHE   B 1 168 ? 32.137 -36.377 -9.069  1.00 19.54 ?  168 PHE   B HA   1 
ATOM   6538 H HB2  . PHE   B 1 168 ? 33.911 -35.344 -10.152 1.00 20.48 ?  168 PHE   B HB2  1 
ATOM   6539 H HB3  . PHE   B 1 168 ? 33.346 -35.822 -11.557 1.00 20.48 ?  168 PHE   B HB3  1 
ATOM   6540 H HD1  . PHE   B 1 168 ? 32.288 -33.855 -8.806  1.00 21.73 ?  168 PHE   B HD1  1 
ATOM   6541 H HD2  . PHE   B 1 168 ? 32.088 -34.311 -12.770 1.00 19.75 ?  168 PHE   B HD2  1 
ATOM   6542 H HE1  . PHE   B 1 168 ? 31.049 -31.915 -8.954  1.00 22.49 ?  168 PHE   B HE1  1 
ATOM   6543 H HE2  . PHE   B 1 168 ? 30.845 -32.363 -12.930 1.00 20.88 ?  168 PHE   B HE2  1 
ATOM   6544 H HZ   . PHE   B 1 168 ? 30.324 -31.164 -11.019 1.00 21.74 ?  168 PHE   B HZ   1 
ATOM   6545 N N    . LEU   B 1 169 ? 31.057 -37.810 -11.690 1.00 14.40 ?  169 LEU   B N    1 
ATOM   6546 C CA   . LEU   B 1 169 ? 29.884 -38.109 -12.501 1.00 16.94 ?  169 LEU   B CA   1 
ATOM   6547 C C    . LEU   B 1 169 ? 29.910 -39.534 -13.038 1.00 19.37 ?  169 LEU   B C    1 
ATOM   6548 O O    . LEU   B 1 169 ? 29.012 -39.950 -13.772 1.00 21.81 ?  169 LEU   B O    1 
ATOM   6549 C CB   . LEU   B 1 169 ? 29.805 -37.145 -13.681 1.00 19.08 ?  169 LEU   B CB   1 
ATOM   6550 C CG   . LEU   B 1 169 ? 28.543 -36.287 -13.760 1.00 22.30 ?  169 LEU   B CG   1 
ATOM   6551 C CD1  . LEU   B 1 169 ? 28.508 -35.515 -15.068 1.00 23.76 ?  169 LEU   B CD1  1 
ATOM   6552 C CD2  . LEU   B 1 169 ? 27.298 -37.137 -13.605 1.00 22.56 ?  169 LEU   B CD2  1 
ATOM   6553 O OXT  . LEU   B 1 169 ? 30.844 -40.284 -12.771 1.00 19.95 -1 169 LEU   B OXT  1 
ATOM   6554 H H    . LEU   B 1 169 ? 31.758 -38.254 -11.926 1.00 17.28 ?  169 LEU   B H    1 
ATOM   6555 H HA   . LEU   B 1 169 ? 29.093 -37.993 -11.953 1.00 20.32 ?  169 LEU   B HA   1 
ATOM   6556 H HB2  . LEU   B 1 169 ? 30.564 -36.540 -13.636 1.00 22.89 ?  169 LEU   B HB2  1 
ATOM   6557 H HB3  . LEU   B 1 169 ? 29.854 -37.659 -14.504 1.00 22.89 ?  169 LEU   B HB3  1 
ATOM   6558 H HG   . LEU   B 1 169 ? 28.557 -35.640 -13.037 1.00 26.75 ?  169 LEU   B HG   1 
ATOM   6559 H HD11 . LEU   B 1 169 ? 27.711 -34.963 -15.085 1.00 28.50 ?  169 LEU   B HD11 1 
ATOM   6560 H HD12 . LEU   B 1 169 ? 29.299 -34.959 -15.127 1.00 28.50 ?  169 LEU   B HD12 1 
ATOM   6561 H HD13 . LEU   B 1 169 ? 28.489 -36.147 -15.804 1.00 28.50 ?  169 LEU   B HD13 1 
ATOM   6562 H HD21 . LEU   B 1 169 ? 26.546 -36.678 -14.006 1.00 27.06 ?  169 LEU   B HD21 1 
ATOM   6563 H HD22 . LEU   B 1 169 ? 27.442 -37.989 -14.048 1.00 27.06 ?  169 LEU   B HD22 1 
ATOM   6564 H HD23 . LEU   B 1 169 ? 27.133 -37.282 -12.660 1.00 27.06 ?  169 LEU   B HD23 1 
HETATM 6565 C C1   T TFA   C 2 .   ? 12.102 -1.320  1.466   0.10 6.58  ?  201 TFA   A C1   1 
HETATM 6566 C C2   T TFA   C 2 .   ? 12.758 -1.729  0.122   0.10 8.06  ?  201 TFA   A C2   1 
HETATM 6567 O O    T TFA   C 2 .   ? 12.796 -1.611  2.450   0.10 5.49  ?  201 TFA   A O    1 
HETATM 6568 F F1   T TFA   C 2 .   ? 12.813 -3.071  0.032   0.10 9.07  ?  201 TFA   A F1   1 
HETATM 6569 F F2   T TFA   C 2 .   ? 12.054 -1.308  -0.942  0.10 8.11  ?  201 TFA   A F2   1 
HETATM 6570 F F3   T TFA   C 2 .   ? 14.006 -1.266  -0.037  0.10 8.84  ?  201 TFA   A F3   1 
HETATM 6571 O OXT  T TFA   C 2 .   ? 11.002 -0.770  1.373   0.10 6.46  ?  201 TFA   A OXT  1 
HETATM 6572 S S    B DMS   D 3 .   ? 9.475  5.347   3.221   0.60 44.36 ?  202 DMS   A S    1 
HETATM 6573 O O    B DMS   D 3 .   ? 9.913  4.105   2.483   0.60 44.75 ?  202 DMS   A O    1 
HETATM 6574 C C1   B DMS   D 3 .   ? 8.260  4.818   4.461   0.60 44.63 ?  202 DMS   A C1   1 
HETATM 6575 C C2   B DMS   D 3 .   ? 8.402  6.271   2.080   0.60 44.69 ?  202 DMS   A C2   1 
HETATM 6576 H H11  B DMS   D 3 .   ? 7.443  4.524   3.905   0.60 53.55 ?  202 DMS   A H11  1 
HETATM 6577 H H12  B DMS   D 3 .   ? 8.091  5.652   5.045   0.60 53.55 ?  202 DMS   A H12  1 
HETATM 6578 H H13  B DMS   D 3 .   ? 8.690  4.030   4.996   0.60 53.55 ?  202 DMS   A H13  1 
HETATM 6579 H H21  B DMS   D 3 .   ? 8.988  6.998   1.617   0.60 53.62 ?  202 DMS   A H21  1 
HETATM 6580 H H22  B DMS   D 3 .   ? 7.669  6.670   2.691   0.60 53.62 ?  202 DMS   A H22  1 
HETATM 6581 H H23  B DMS   D 3 .   ? 8.036  5.570   1.417   0.60 53.62 ?  202 DMS   A H23  1 
HETATM 6582 N N2   B A1A9U E 4 .   ? 14.600 -0.091  4.290   0.60 11.55 ?  203 A1A9U A N2   1 
HETATM 6583 C C3   B A1A9U E 4 .   ? 17.534 1.838   -1.405  0.60 11.39 ?  203 A1A9U A C3   1 
HETATM 6584 C C6   B A1A9U E 4 .   ? 15.120 0.711   -0.486  0.60 11.59 ?  203 A1A9U A C6   1 
HETATM 6585 C C9   B A1A9U E 4 .   ? 12.568 -0.936  2.042   0.60 12.57 ?  203 A1A9U A C9   1 
HETATM 6586 C C12  B A1A9U E 4 .   ? 15.191 2.222   5.551   0.60 11.70 ?  203 A1A9U A C12  1 
HETATM 6587 C C14  B A1A9U E 4 .   ? 14.948 3.712   3.890   0.60 12.77 ?  203 A1A9U A C14  1 
HETATM 6588 C C1   B A1A9U E 4 .   ? 18.628 -0.452  -1.448  0.60 11.49 ?  203 A1A9U A C1   1 
HETATM 6589 C C10  B A1A9U E 4 .   ? 14.560 1.084   3.575   0.60 11.36 ?  203 A1A9U A C10  1 
HETATM 6590 C C11  B A1A9U E 4 .   ? 14.935 -0.004  5.612   0.60 11.77 ?  203 A1A9U A C11  1 
HETATM 6591 C C13  B A1A9U E 4 .   ? 14.866 2.313   4.188   0.60 11.61 ?  203 A1A9U A C13  1 
HETATM 6592 C C15  B A1A9U E 4 .   ? 15.331 4.387   5.024   0.60 12.86 ?  203 A1A9U A C15  1 
HETATM 6593 C C16  B A1A9U E 4 .   ? 16.247 -0.066  -0.732  0.60 11.72 ?  203 A1A9U A C16  1 
HETATM 6594 C C2   B A1A9U E 4 .   ? 17.454 0.451   -1.183  0.60 11.63 ?  203 A1A9U A C2   1 
HETATM 6595 C C4   B A1A9U E 4 .   ? 16.408 2.627   -1.164  0.60 11.07 ?  203 A1A9U A C4   1 
HETATM 6596 C C5   B A1A9U E 4 .   ? 15.222 2.085   -0.700  0.60 11.68 ?  203 A1A9U A C5   1 
HETATM 6597 C C7   B A1A9U E 4 .   ? 13.848 0.071   0.011   0.60 11.83 ?  203 A1A9U A C7   1 
HETATM 6598 C C8   B A1A9U E 4 .   ? 13.888 -0.245  1.525   0.60 11.90 ?  203 A1A9U A C8   1 
HETATM 6599 N N1   B A1A9U E 4 .   ? 14.204 0.976   2.268   0.60 12.05 ?  203 A1A9U A N1   1 
HETATM 6600 N N3   B A1A9U E 4 .   ? 15.231 1.085   6.317   0.60 11.73 ?  203 A1A9U A N3   1 
HETATM 6601 N N4   B A1A9U E 4 .   ? 15.476 3.473   6.094   0.60 11.86 ?  203 A1A9U A N4   1 
HETATM 6602 O O1   B A1A9U E 4 .   ? 11.486 -0.056  1.973   0.60 13.55 ?  203 A1A9U A O1   1 
HETATM 6603 H H5   B A1A9U E 4 .   ? 18.460 2.306   -1.769  0.60 13.66 ?  203 A1A9U A H5   1 
HETATM 6604 H H10  B A1A9U E 4 .   ? 12.723 -1.322  3.077   0.60 15.08 ?  203 A1A9U A H10  1 
HETATM 6605 H H11  B A1A9U E 4 .   ? 12.327 -1.852  1.451   0.60 15.08 ?  203 A1A9U A H11  1 
HETATM 6606 H H15  B A1A9U E 4 .   ? 14.779 4.211   2.944   0.60 15.31 ?  203 A1A9U A H15  1 
HETATM 6607 H H3   B A1A9U E 4 .   ? 19.541 0.062   -1.804  0.60 13.78 ?  203 A1A9U A H3   1 
HETATM 6608 H H2   B A1A9U E 4 .   ? 18.439 -1.206  -2.227  0.60 13.78 ?  203 A1A9U A H2   1 
HETATM 6609 H H4   B A1A9U E 4 .   ? 18.976 -1.011  -0.573  0.60 13.78 ?  203 A1A9U A H4   1 
HETATM 6610 H H14  B A1A9U E 4 .   ? 14.962 -0.916  6.234   0.60 14.12 ?  203 A1A9U A H14  1 
HETATM 6611 H H16  B A1A9U E 4 .   ? 15.509 5.434   5.269   0.60 15.42 ?  203 A1A9U A H16  1 
HETATM 6612 H H18  B A1A9U E 4 .   ? 16.188 -1.134  -0.581  0.60 14.05 ?  203 A1A9U A H18  1 
HETATM 6613 H H6   B A1A9U E 4 .   ? 16.493 3.709   -1.336  0.60 13.28 ?  203 A1A9U A H6   1 
HETATM 6614 H H7   B A1A9U E 4 .   ? 14.383 2.761   -0.536  0.60 14.01 ?  203 A1A9U A H7   1 
HETATM 6615 H H9   B A1A9U E 4 .   ? 13.667 -0.867  -0.582  0.60 14.19 ?  203 A1A9U A H9   1 
HETATM 6616 H H8   B A1A9U E 4 .   ? 12.968 0.691   -0.258  0.60 14.19 ?  203 A1A9U A H8   1 
HETATM 6617 H H1   B A1A9U E 4 .   ? 14.720 -0.995  1.653   0.60 14.27 ?  203 A1A9U A H1   1 
HETATM 6618 H H13  B A1A9U E 4 .   ? 14.147 1.840   1.758   0.60 14.45 ?  203 A1A9U A H13  1 
HETATM 6619 H H17  B A1A9U E 4 .   ? 15.728 3.645   7.039   0.60 14.22 ?  203 A1A9U A H17  1 
HETATM 6620 H H12  B A1A9U E 4 .   ? 10.689 -0.588  2.038   0.60 16.26 ?  203 A1A9U A H12  1 
HETATM 6621 O O    . HOH   F 5 .   ? 17.424 -2.162  0.840   1.00 55.47 ?  301 HOH   A O    1 
HETATM 6622 O O    . HOH   F 5 .   ? 14.712 -4.545  20.554  1.00 43.38 ?  302 HOH   A O    1 
HETATM 6623 O O    A HOH   F 5 .   ? 4.644  3.980   0.625   0.40 14.97 ?  303 HOH   A O    1 
HETATM 6624 O O    . HOH   F 5 .   ? 7.597  -6.382  -6.750  1.00 43.03 ?  304 HOH   A O    1 
HETATM 6625 O O    . HOH   F 5 .   ? 16.974 -17.944 15.062  1.00 27.59 ?  305 HOH   A O    1 
HETATM 6626 O O    B HOH   F 5 .   ? 4.926  3.496   0.491   0.60 16.22 ?  306 HOH   A O    1 
HETATM 6627 O O    . HOH   F 5 .   ? 34.336 -1.875  12.499  1.00 36.54 ?  307 HOH   A O    1 
HETATM 6628 O O    B HOH   F 5 .   ? 11.843 2.923   1.445   0.60 23.18 ?  308 HOH   A O    1 
HETATM 6629 O O    . HOH   F 5 .   ? 31.054 6.116   -12.278 1.00 27.59 ?  309 HOH   A O    1 
HETATM 6630 O O    . HOH   F 5 .   ? 28.907 0.559   -9.628  1.00 18.39 ?  310 HOH   A O    1 
HETATM 6631 O O    . HOH   F 5 .   ? 14.943 3.874   17.740  1.00 37.78 ?  311 HOH   A O    1 
HETATM 6632 O O    . HOH   F 5 .   ? 14.983 -12.074 18.707  1.00 35.04 ?  312 HOH   A O    1 
HETATM 6633 O O    . HOH   F 5 .   ? 19.850 -12.358 -9.055  1.00 22.51 ?  313 HOH   A O    1 
HETATM 6634 O O    A HOH   F 5 .   ? 14.578 -3.603  3.105   0.40 14.81 ?  314 HOH   A O    1 
HETATM 6635 O O    . HOH   F 5 .   ? 36.074 -5.062  -0.548  1.00 29.48 ?  315 HOH   A O    1 
HETATM 6636 O O    . HOH   F 5 .   ? 14.629 -13.891 16.755  1.00 22.08 ?  316 HOH   A O    1 
HETATM 6637 O O    . HOH   F 5 .   ? 42.414 10.547  5.263   1.00 19.58 ?  317 HOH   A O    1 
HETATM 6638 O O    . HOH   F 5 .   ? 11.906 0.438   14.827  1.00 31.44 ?  318 HOH   A O    1 
HETATM 6639 O O    A HOH   F 5 .   ? 14.022 -4.521  -11.727 0.40 18.69 ?  319 HOH   A O    1 
HETATM 6640 O O    A HOH   F 5 .   ? -0.534 -3.027  3.098   0.40 24.27 ?  320 HOH   A O    1 
HETATM 6641 O O    . HOH   F 5 .   ? 28.184 -0.043  -13.350 1.00 33.24 ?  321 HOH   A O    1 
HETATM 6642 O O    . HOH   F 5 .   ? 9.042  -10.074 19.348  1.00 40.90 ?  322 HOH   A O    1 
HETATM 6643 O O    . HOH   F 5 .   ? 30.176 -13.291 -8.580  1.00 18.87 ?  323 HOH   A O    1 
HETATM 6644 O O    A HOH   F 5 .   ? 14.219 0.621   6.811   0.40 18.07 ?  324 HOH   A O    1 
HETATM 6645 O O    . HOH   F 5 .   ? 26.407 -19.296 -1.805  1.00 13.01 ?  325 HOH   A O    1 
HETATM 6646 O O    . HOH   F 5 .   ? 28.071 -6.241  19.699  1.00 37.72 ?  326 HOH   A O    1 
HETATM 6647 O O    . HOH   F 5 .   ? 30.919 -18.100 7.805   1.00 19.12 ?  327 HOH   A O    1 
HETATM 6648 O O    . HOH   F 5 .   ? 27.246 13.780  2.934   1.00 26.92 ?  328 HOH   A O    1 
HETATM 6649 O O    A HOH   F 5 .   ? 6.882  -8.112  11.847  0.40 12.34 ?  329 HOH   A O    1 
HETATM 6650 O O    . HOH   F 5 .   ? 15.134 -8.092  -9.814  1.00 21.87 ?  330 HOH   A O    1 
HETATM 6651 O O    A HOH   F 5 .   ? 8.115  -21.341 3.977   0.40 26.19 ?  331 HOH   A O    1 
HETATM 6652 O O    . HOH   F 5 .   ? 37.175 -2.781  9.664   1.00 38.76 ?  332 HOH   A O    1 
HETATM 6653 O O    . HOH   F 5 .   ? 10.293 -21.996 -1.169  1.00 37.68 ?  333 HOH   A O    1 
HETATM 6654 O O    . HOH   F 5 .   ? 25.594 -0.707  -7.265  1.00 14.14 ?  334 HOH   A O    1 
HETATM 6655 O O    . HOH   F 5 .   ? 18.797 -21.907 7.001   1.00 32.95 ?  335 HOH   A O    1 
HETATM 6656 O O    A HOH   F 5 .   ? 13.259 -1.374  -6.515  0.40 12.74 ?  336 HOH   A O    1 
HETATM 6657 O O    B HOH   F 5 .   ? 8.962  3.274   -1.271  0.60 32.73 ?  337 HOH   A O    1 
HETATM 6658 O O    A HOH   F 5 .   ? 11.013 -0.325  1.942   0.30 19.31 ?  338 HOH   A O    1 
HETATM 6659 O O    . HOH   F 5 .   ? 38.239 10.093  7.232   1.00 26.76 ?  339 HOH   A O    1 
HETATM 6660 O O    . HOH   F 5 .   ? 18.553 9.452   9.056   1.00 21.65 ?  340 HOH   A O    1 
HETATM 6661 O O    . HOH   F 5 .   ? 13.576 -15.221 -7.458  1.00 22.71 ?  341 HOH   A O    1 
HETATM 6662 O O    . HOH   F 5 .   ? 39.710 -1.049  -5.195  1.00 18.33 ?  342 HOH   A O    1 
HETATM 6663 O O    . HOH   F 5 .   ? 38.525 4.959   6.960   1.00 14.68 ?  343 HOH   A O    1 
HETATM 6664 O O    . HOH   F 5 .   ? 24.013 -2.062  -2.058  1.00 9.51  ?  344 HOH   A O    1 
HETATM 6665 O O    B HOH   F 5 .   ? 10.889 2.133   12.177  0.60 22.11 ?  345 HOH   A O    1 
HETATM 6666 O O    . HOH   F 5 .   ? 20.545 -19.707 -5.087  1.00 27.46 ?  346 HOH   A O    1 
HETATM 6667 O O    . HOH   F 5 .   ? 33.910 -1.025  -8.992  1.00 26.81 ?  347 HOH   A O    1 
HETATM 6668 O O    . HOH   F 5 .   ? 37.326 11.940  4.982   1.00 31.37 ?  348 HOH   A O    1 
HETATM 6669 O O    . HOH   F 5 .   ? 44.295 7.080   6.501   1.00 24.64 ?  349 HOH   A O    1 
HETATM 6670 O O    . HOH   F 5 .   ? 14.239 -21.082 -4.271  1.00 29.62 ?  350 HOH   A O    1 
HETATM 6671 O O    . HOH   F 5 .   ? 37.559 2.757   10.206  1.00 27.41 ?  351 HOH   A O    1 
HETATM 6672 O O    . HOH   F 5 .   ? 31.746 -9.296  -6.690  1.00 20.38 ?  352 HOH   A O    1 
HETATM 6673 O O    B HOH   F 5 .   ? 14.958 -2.787  3.542   0.60 12.49 ?  353 HOH   A O    1 
HETATM 6674 O O    . HOH   F 5 .   ? 22.235 5.378   18.935  1.00 36.90 ?  354 HOH   A O    1 
HETATM 6675 O O    . HOH   F 5 .   ? 26.816 11.432  1.683   1.00 16.40 ?  355 HOH   A O    1 
HETATM 6676 O O    . HOH   F 5 .   ? -0.692 -8.185  2.194   1.00 47.09 ?  356 HOH   A O    1 
HETATM 6677 O O    B HOH   F 5 .   ? 11.856 6.625   10.426  0.60 28.48 ?  357 HOH   A O    1 
HETATM 6678 O O    . HOH   F 5 .   ? 35.710 -12.662 6.864   1.00 14.67 ?  358 HOH   A O    1 
HETATM 6679 O O    . HOH   F 5 .   ? 16.416 -21.983 0.931   1.00 28.14 ?  359 HOH   A O    1 
HETATM 6680 O O    . HOH   F 5 .   ? 24.286 3.611   -1.772  1.00 11.73 ?  360 HOH   A O    1 
HETATM 6681 O O    A HOH   F 5 .   ? 0.677  -4.545  0.241   0.40 23.34 ?  361 HOH   A O    1 
HETATM 6682 O O    . HOH   F 5 .   ? 31.684 8.185   14.910  1.00 22.16 ?  362 HOH   A O    1 
HETATM 6683 O O    . HOH   F 5 .   ? 22.174 -19.232 11.405  1.00 33.05 ?  363 HOH   A O    1 
HETATM 6684 O O    . HOH   F 5 .   ? 18.608 -19.372 13.559  1.00 37.69 ?  364 HOH   A O    1 
HETATM 6685 O O    . HOH   F 5 .   ? 43.918 8.416   -3.073  1.00 24.94 ?  365 HOH   A O    1 
HETATM 6686 O O    B HOH   F 5 .   ? 5.617  -0.206  -1.651  0.60 28.18 ?  366 HOH   A O    1 
HETATM 6687 O O    B HOH   F 5 .   ? 21.025 2.540   -0.009  0.60 12.28 ?  367 HOH   A O    1 
HETATM 6688 O O    . HOH   F 5 .   ? 42.494 4.235   5.290   1.00 26.34 ?  368 HOH   A O    1 
HETATM 6689 O O    . HOH   F 5 .   ? 7.940  -12.391 -0.983  1.00 18.52 ?  369 HOH   A O    1 
HETATM 6690 O O    . HOH   F 5 .   ? 30.994 -13.904 -2.479  1.00 11.95 ?  370 HOH   A O    1 
HETATM 6691 O O    . HOH   F 5 .   ? 20.016 4.527   -7.527  1.00 14.73 ?  371 HOH   A O    1 
HETATM 6692 O O    . HOH   F 5 .   ? 30.771 3.096   8.279   1.00 10.85 ?  372 HOH   A O    1 
HETATM 6693 O O    . HOH   F 5 .   ? 33.597 -7.147  4.294   1.00 14.99 ?  373 HOH   A O    1 
HETATM 6694 O O    . HOH   F 5 .   ? 21.807 -21.882 8.443   1.00 25.32 ?  374 HOH   A O    1 
HETATM 6695 O O    . HOH   F 5 .   ? 17.054 -17.739 -5.051  1.00 25.66 ?  375 HOH   A O    1 
HETATM 6696 O O    . HOH   F 5 .   ? 22.602 -11.943 21.782  1.00 43.11 ?  376 HOH   A O    1 
HETATM 6697 O O    . HOH   F 5 .   ? 21.239 10.221  15.087  1.00 32.97 ?  377 HOH   A O    1 
HETATM 6698 O O    A HOH   F 5 .   ? 3.533  -9.409  9.725   0.40 16.38 ?  378 HOH   A O    1 
HETATM 6699 O O    . HOH   F 5 .   ? 21.293 -2.228  -2.433  1.00 12.34 ?  379 HOH   A O    1 
HETATM 6700 O O    . HOH   F 5 .   ? 22.713 12.497  1.642   1.00 14.47 ?  380 HOH   A O    1 
HETATM 6701 O O    . HOH   F 5 .   ? 16.907 -19.175 4.912   1.00 14.34 ?  381 HOH   A O    1 
HETATM 6702 O O    B HOH   F 5 .   ? 1.072  -4.075  -0.606  0.60 22.33 ?  382 HOH   A O    1 
HETATM 6703 O O    . HOH   F 5 .   ? 27.436 -10.626 14.066  1.00 16.15 ?  383 HOH   A O    1 
HETATM 6704 O O    B HOH   F 5 .   ? 15.043 7.234   7.299   0.60 21.78 ?  384 HOH   A O    1 
HETATM 6705 O O    . HOH   F 5 .   ? 31.715 -7.260  -9.866  1.00 20.41 ?  385 HOH   A O    1 
HETATM 6706 O O    . HOH   F 5 .   ? 24.197 -7.753  14.461  1.00 16.04 ?  386 HOH   A O    1 
HETATM 6707 O O    . HOH   F 5 .   ? 5.464  3.095   4.596   1.00 31.06 ?  387 HOH   A O    1 
HETATM 6708 O O    . HOH   F 5 .   ? 15.476 11.795  7.934   1.00 40.83 ?  388 HOH   A O    1 
HETATM 6709 O O    . HOH   F 5 .   ? 6.660  -3.090  12.803  1.00 25.71 ?  389 HOH   A O    1 
HETATM 6710 O O    B HOH   F 5 .   ? 12.938 -1.558  -7.257  0.60 15.88 ?  390 HOH   A O    1 
HETATM 6711 O O    . HOH   F 5 .   ? 43.351 7.871   2.773   1.00 22.87 ?  391 HOH   A O    1 
HETATM 6712 O O    B HOH   F 5 .   ? 10.638 0.051   -0.719  0.60 30.98 ?  392 HOH   A O    1 
HETATM 6713 O O    . HOH   F 5 .   ? 27.281 -5.875  -13.986 1.00 34.23 ?  393 HOH   A O    1 
HETATM 6714 O O    . HOH   F 5 .   ? 6.316  -5.387  11.086  1.00 17.24 ?  394 HOH   A O    1 
HETATM 6715 O O    A HOH   F 5 .   ? 9.712  -21.288 5.720   0.40 12.76 ?  395 HOH   A O    1 
HETATM 6716 O O    . HOH   F 5 .   ? 13.842 -4.854  17.417  1.00 25.91 ?  396 HOH   A O    1 
HETATM 6717 O O    . HOH   F 5 .   ? 24.599 -17.535 12.698  1.00 23.24 ?  397 HOH   A O    1 
HETATM 6718 O O    T HOH   F 5 .   ? 15.353 -0.371  2.397   0.10 5.78  ?  398 HOH   A O    1 
HETATM 6719 O O    . HOH   F 5 .   ? 44.778 -0.716  3.021   1.00 37.07 ?  399 HOH   A O    1 
HETATM 6720 O O    A HOH   F 5 .   ? 21.299 3.204   -0.330  0.40 10.84 ?  400 HOH   A O    1 
HETATM 6721 O O    . HOH   F 5 .   ? 38.110 -1.370  -1.927  1.00 17.52 ?  401 HOH   A O    1 
HETATM 6722 O O    . HOH   F 5 .   ? 27.366 2.330   18.775  1.00 25.01 ?  402 HOH   A O    1 
HETATM 6723 O O    . HOH   F 5 .   ? 37.482 -1.997  5.750   1.00 24.05 ?  403 HOH   A O    1 
HETATM 6724 O O    A HOH   F 5 .   ? 24.537 2.092   -6.968  0.40 10.66 ?  404 HOH   A O    1 
HETATM 6725 O O    . HOH   F 5 .   ? 18.467 4.959   -15.152 1.00 38.80 ?  405 HOH   A O    1 
HETATM 6726 O O    . HOH   F 5 .   ? 9.005  -12.090 17.170  1.00 38.51 ?  406 HOH   A O    1 
HETATM 6727 O O    . HOH   F 5 .   ? 32.725 -9.222  5.946   1.00 18.92 ?  407 HOH   A O    1 
HETATM 6728 O O    . HOH   F 5 .   ? 28.480 -10.620 -13.928 1.00 47.18 ?  408 HOH   A O    1 
HETATM 6729 O O    A HOH   F 5 .   ? 15.744 -0.897  5.281   0.40 17.25 ?  409 HOH   A O    1 
HETATM 6730 O O    . HOH   F 5 .   ? 16.196 16.596  8.566   1.00 35.59 ?  410 HOH   A O    1 
HETATM 6731 O O    . HOH   F 5 .   ? 23.852 -15.637 -9.188  1.00 33.54 ?  411 HOH   A O    1 
HETATM 6732 O O    . HOH   F 5 .   ? 21.747 -13.711 -8.156  1.00 34.50 ?  412 HOH   A O    1 
HETATM 6733 O O    B HOH   F 5 .   ? 2.985  -3.170  8.516   0.60 22.51 ?  413 HOH   A O    1 
HETATM 6734 O O    . HOH   F 5 .   ? 30.011 -10.124 13.010  1.00 20.29 ?  414 HOH   A O    1 
HETATM 6735 O O    . HOH   F 5 .   ? 15.079 -21.444 14.231  1.00 17.22 ?  415 HOH   A O    1 
HETATM 6736 O O    . HOH   F 5 .   ? 18.643 -2.384  -16.453 1.00 43.89 ?  416 HOH   A O    1 
HETATM 6737 O O    . HOH   F 5 .   ? 14.397 -24.676 11.575  1.00 34.44 ?  417 HOH   A O    1 
HETATM 6738 O O    . HOH   F 5 .   ? 23.450 11.379  4.095   1.00 11.57 ?  418 HOH   A O    1 
HETATM 6739 O O    . HOH   F 5 .   ? 19.492 -11.051 24.162  1.00 62.05 ?  419 HOH   A O    1 
HETATM 6740 O O    . HOH   F 5 .   ? 20.486 -19.982 2.772   1.00 16.94 ?  420 HOH   A O    1 
HETATM 6741 O O    B HOH   F 5 .   ? 7.373  2.488   8.383   0.60 37.44 ?  421 HOH   A O    1 
HETATM 6742 O O    . HOH   F 5 .   ? 13.927 -22.944 7.410   1.00 17.42 ?  422 HOH   A O    1 
HETATM 6743 O O    B HOH   F 5 .   ? 3.940  0.285   10.019  0.60 36.99 ?  423 HOH   A O    1 
HETATM 6744 O O    . HOH   F 5 .   ? 30.726 1.826   16.699  1.00 18.54 ?  424 HOH   A O    1 
HETATM 6745 O O    A HOH   F 5 .   ? 24.046 4.009   -4.895  0.40 12.47 ?  425 HOH   A O    1 
HETATM 6746 O O    . HOH   F 5 .   ? 14.487 -0.481  -12.242 1.00 20.30 ?  426 HOH   A O    1 
HETATM 6747 O O    . HOH   F 5 .   ? 26.840 4.207   -0.672  1.00 10.91 ?  427 HOH   A O    1 
HETATM 6748 O O    . HOH   F 5 .   ? 23.820 -20.219 -1.363  1.00 15.12 ?  428 HOH   A O    1 
HETATM 6749 O O    . HOH   F 5 .   ? 40.843 -8.247  -6.707  1.00 35.28 ?  429 HOH   A O    1 
HETATM 6750 O O    . HOH   F 5 .   ? 30.253 -12.870 13.540  1.00 18.55 ?  430 HOH   A O    1 
HETATM 6751 O O    . HOH   F 5 .   ? 32.602 -4.273  -9.902  1.00 27.29 ?  431 HOH   A O    1 
HETATM 6752 O O    . HOH   F 5 .   ? 27.880 0.854   -7.132  1.00 12.57 ?  432 HOH   A O    1 
HETATM 6753 O O    B HOH   F 5 .   ? 20.741 4.403   -2.268  0.60 12.94 ?  433 HOH   A O    1 
HETATM 6754 O O    . HOH   F 5 .   ? 10.325 -13.624 -1.675  1.00 15.48 ?  434 HOH   A O    1 
HETATM 6755 O O    . HOH   F 5 .   ? 34.947 -5.216  -3.087  1.00 16.82 ?  435 HOH   A O    1 
HETATM 6756 O O    . HOH   F 5 .   ? 41.543 1.582   4.983   1.00 33.74 ?  436 HOH   A O    1 
HETATM 6757 O O    . HOH   F 5 .   ? 36.706 -4.915  5.358   1.00 22.17 ?  437 HOH   A O    1 
HETATM 6758 O O    . HOH   F 5 .   ? 16.158 -14.061 20.271  1.00 48.30 ?  438 HOH   A O    1 
HETATM 6759 O O    B HOH   F 5 .   ? 24.224 1.889   -6.680  0.60 18.62 ?  439 HOH   A O    1 
HETATM 6760 O O    . HOH   F 5 .   ? 22.720 8.074   18.422  1.00 39.75 ?  440 HOH   A O    1 
HETATM 6761 O O    . HOH   F 5 .   ? 15.894 2.192   24.777  1.00 47.54 ?  441 HOH   A O    1 
HETATM 6762 O O    . HOH   F 5 .   ? 32.497 -10.628 3.185   1.00 29.92 ?  442 HOH   A O    1 
HETATM 6763 O O    . HOH   F 5 .   ? 15.845 6.882   3.003   1.00 16.69 ?  443 HOH   A O    1 
HETATM 6764 O O    . HOH   F 5 .   ? 9.457  -16.212 -1.901  1.00 24.42 ?  444 HOH   A O    1 
HETATM 6765 O O    A HOH   F 5 .   ? 10.977 1.596   12.762  0.40 15.41 ?  445 HOH   A O    1 
HETATM 6766 O O    . HOH   F 5 .   ? 11.626 -10.572 16.982  1.00 24.87 ?  446 HOH   A O    1 
HETATM 6767 O O    A HOH   F 5 .   ? 18.907 -0.617  -1.613  0.40 13.94 ?  447 HOH   A O    1 
HETATM 6768 O O    . HOH   F 5 .   ? 20.529 -17.751 24.720  1.00 52.08 ?  448 HOH   A O    1 
HETATM 6769 O O    . HOH   F 5 .   ? 27.123 -3.216  19.346  1.00 33.65 ?  449 HOH   A O    1 
HETATM 6770 O O    . HOH   F 5 .   ? 23.554 -8.043  17.112  1.00 20.67 ?  450 HOH   A O    1 
HETATM 6771 O O    B HOH   F 5 .   ? 11.493 -1.898  -2.996  0.60 24.00 ?  451 HOH   A O    1 
HETATM 6772 O O    A HOH   F 5 .   ? 23.157 7.562   -3.212  0.40 19.86 ?  452 HOH   A O    1 
HETATM 6773 O O    . HOH   F 5 .   ? 23.247 -20.899 1.306   1.00 16.42 ?  453 HOH   A O    1 
HETATM 6774 O O    A HOH   F 5 .   ? 13.973 -0.287  3.472   0.30 30.26 ?  454 HOH   A O    1 
HETATM 6775 O O    . HOH   F 5 .   ? 18.341 -15.927 16.359  1.00 36.53 ?  455 HOH   A O    1 
HETATM 6776 O O    B HOH   F 5 .   ? 23.925 3.636   -4.465  0.60 18.81 ?  456 HOH   A O    1 
HETATM 6777 O O    B HOH   F 5 .   ? 23.231 6.446   -2.039  0.60 15.47 ?  457 HOH   A O    1 
HETATM 6778 O O    . HOH   F 5 .   ? 21.213 -9.069  21.347  1.00 47.72 ?  458 HOH   A O    1 
HETATM 6779 O O    A HOH   F 5 .   ? 11.677 -10.716 -10.066 0.40 28.09 ?  459 HOH   A O    1 
HETATM 6780 O O    . HOH   F 5 .   ? 34.357 -8.077  -0.539  1.00 28.67 ?  460 HOH   A O    1 
HETATM 6781 O O    A HOH   F 5 .   ? 18.813 2.084   -0.735  0.40 10.68 ?  461 HOH   A O    1 
HETATM 6782 O O    A HOH   F 5 .   ? 16.209 3.002   -1.426  0.40 13.45 ?  462 HOH   A O    1 
HETATM 6783 O O    . HOH   F 5 .   ? 31.253 -12.765 0.018   1.00 18.30 ?  463 HOH   A O    1 
HETATM 6784 O O    . HOH   F 5 .   ? 37.631 -8.756  -3.349  1.00 24.23 ?  464 HOH   A O    1 
HETATM 6785 O O    . HOH   F 5 .   ? 29.686 -16.024 10.593  1.00 30.39 ?  465 HOH   A O    1 
HETATM 6786 O O    A HOH   F 5 .   ? -1.491 -4.882  7.641   0.40 30.64 ?  466 HOH   A O    1 
HETATM 6787 O O    . HOH   F 5 .   ? 30.576 14.763  2.800   1.00 18.32 ?  467 HOH   A O    1 
HETATM 6788 O O    . HOH   F 5 .   ? 21.430 -14.655 17.981  1.00 51.72 ?  468 HOH   A O    1 
HETATM 6789 O O    . HOH   F 5 .   ? 29.696 -1.916  -12.735 1.00 40.11 ?  469 HOH   A O    1 
HETATM 6790 O O    . HOH   F 5 .   ? 25.368 8.235   -4.883  1.00 44.04 ?  470 HOH   A O    1 
HETATM 6791 O O    B HOH   F 5 .   ? 4.968  -2.892  -2.483  0.60 30.54 ?  471 HOH   A O    1 
HETATM 6792 O O    . HOH   F 5 .   ? 32.370 -15.902 10.898  1.00 34.64 ?  472 HOH   A O    1 
HETATM 6793 O O    . HOH   F 5 .   ? 24.774 5.618   20.816  1.00 48.98 ?  473 HOH   A O    1 
HETATM 6794 O O    . HOH   F 5 .   ? 19.794 -17.273 -5.036  1.00 23.50 ?  474 HOH   A O    1 
HETATM 6795 O O    . HOH   F 5 .   ? 27.880 7.156   -6.605  1.00 37.51 ?  475 HOH   A O    1 
HETATM 6796 O O    . HOH   F 5 .   ? 24.578 14.620  7.857   1.00 34.91 ?  476 HOH   A O    1 
HETATM 6797 O O    . HOH   F 5 .   ? 27.453 -11.292 16.661  1.00 34.63 ?  477 HOH   A O    1 
HETATM 6798 O O    . HOH   F 5 .   ? 15.635 -21.401 3.695   1.00 25.50 ?  478 HOH   A O    1 
HETATM 6799 O O    . HOH   F 5 .   ? 23.126 -22.426 -3.284  1.00 33.03 ?  479 HOH   A O    1 
HETATM 6800 O O    . HOH   F 5 .   ? 39.573 -7.011  -3.529  1.00 42.84 ?  480 HOH   A O    1 
HETATM 6801 O O    . HOH   F 5 .   ? 18.762 10.861  11.356  1.00 32.27 ?  481 HOH   A O    1 
HETATM 6802 O O    . HOH   F 5 .   ? 26.856 11.690  -1.465  1.00 32.84 ?  482 HOH   A O    1 
HETATM 6803 O O    . HOH   F 5 .   ? 11.060 -14.937 -6.163  1.00 32.21 ?  483 HOH   A O    1 
HETATM 6804 O O    . HOH   F 5 .   ? 12.318 1.636   17.401  1.00 38.30 ?  484 HOH   A O    1 
HETATM 6805 O O    A HOH   F 5 .   ? 21.921 5.320   -5.815  0.40 23.43 ?  485 HOH   A O    1 
HETATM 6806 O O    . HOH   F 5 .   ? 23.461 13.737  5.505   1.00 18.24 ?  486 HOH   A O    1 
HETATM 6807 O O    . HOH   F 5 .   ? 17.910 -16.233 -8.793  1.00 39.68 ?  487 HOH   A O    1 
HETATM 6808 O O    . HOH   F 5 .   ? 11.881 -13.295 16.478  1.00 48.70 ?  488 HOH   A O    1 
HETATM 6809 O O    . HOH   F 5 .   ? 25.738 10.780  -3.829  1.00 33.91 ?  489 HOH   A O    1 
HETATM 6810 O O    . HOH   F 5 .   ? 28.928 8.914   17.491  1.00 38.12 ?  490 HOH   A O    1 
HETATM 6811 O O    . HOH   F 5 .   ? 15.652 -17.148 -6.985  1.00 28.52 ?  491 HOH   A O    1 
HETATM 6812 O O    B HOH   F 5 .   ? 16.678 10.259  6.045   0.60 27.71 ?  492 HOH   A O    1 
HETATM 6813 O O    . HOH   F 5 .   ? 35.218 7.407   12.325  1.00 41.80 ?  493 HOH   A O    1 
HETATM 6814 O O    . HOH   F 5 .   ? 13.951 -10.367 -10.913 1.00 31.88 ?  494 HOH   A O    1 
HETATM 6815 O O    B HOH   F 5 .   ? 21.286 4.821   -4.972  0.60 12.81 ?  495 HOH   A O    1 
HETATM 6816 O O    . HOH   F 5 .   ? 17.392 -18.672 19.854  1.00 49.26 ?  496 HOH   A O    1 
HETATM 6817 O O    . HOH   F 5 .   ? 16.765 -20.497 16.139  1.00 28.32 ?  497 HOH   A O    1 
HETATM 6818 O O    . HOH   F 5 .   ? 40.855 -3.987  -0.368  1.00 38.05 ?  498 HOH   A O    1 
HETATM 6819 O O    . HOH   F 5 .   ? 8.084  -3.135  -5.918  1.00 50.47 ?  499 HOH   A O    1 
HETATM 6820 O O    . HOH   F 5 .   ? 28.555 -4.654  -12.317 1.00 32.12 ?  500 HOH   A O    1 
HETATM 6821 O O    . HOH   F 5 .   ? 16.007 -6.765  -11.995 1.00 41.22 ?  501 HOH   A O    1 
HETATM 6822 O O    . HOH   F 5 .   ? 30.842 0.746   19.241  1.00 37.44 ?  502 HOH   A O    1 
HETATM 6823 O O    B HOH   F 5 .   ? 20.831 9.859   -4.772  0.60 21.63 ?  503 HOH   A O    1 
HETATM 6824 O O    B HOH   F 5 .   ? 23.021 11.410  -4.391  0.60 25.50 ?  504 HOH   A O    1 
HETATM 6825 O O    . HOH   F 5 .   ? 31.421 -0.517  -10.549 1.00 27.29 ?  505 HOH   A O    1 
HETATM 6826 O O    B HOH   F 5 .   ? 10.448 -1.703  -5.910  0.60 26.09 ?  506 HOH   A O    1 
HETATM 6827 O O    B HOH   F 5 .   ? 8.188  2.019   -3.751  0.60 27.70 ?  507 HOH   A O    1 
HETATM 6828 O O    . HOH   F 5 .   ? 41.720 9.322   -4.089  1.00 29.02 ?  508 HOH   A O    1 
HETATM 6829 O O    . HOH   F 5 .   ? 28.563 -7.821  -15.248 1.00 47.53 ?  509 HOH   A O    1 
HETATM 6830 O O    . HOH   F 5 .   ? 44.518 10.470  -1.542  1.00 29.44 ?  510 HOH   A O    1 
HETATM 6831 O O    . HOH   F 5 .   ? 23.257 -12.846 19.343  1.00 42.98 ?  511 HOH   A O    1 
HETATM 6832 O O    . HOH   F 5 .   ? 39.112 2.416   7.563   1.00 31.64 ?  512 HOH   A O    1 
HETATM 6833 O O    . HOH   F 5 .   ? 18.309 -23.129 1.899   1.00 37.75 ?  513 HOH   A O    1 
HETATM 6834 O O    . HOH   F 5 .   ? 40.507 -0.232  -7.773  1.00 33.59 ?  514 HOH   A O    1 
HETATM 6835 O O    A HOH   F 5 .   ? 23.123 11.872  -4.090  0.40 13.52 ?  515 HOH   A O    1 
HETATM 6836 O O    . HOH   F 5 .   ? 13.818 -25.157 8.864   1.00 29.47 ?  516 HOH   A O    1 
HETATM 6837 O O    . HOH   F 5 .   ? 19.974 -22.290 4.168   1.00 25.83 ?  517 HOH   A O    1 
HETATM 6838 O O    . HOH   F 5 .   ? 30.699 5.791   -14.709 1.00 33.04 ?  518 HOH   A O    1 
HETATM 6839 O O    . HOH   F 5 .   ? 16.120 -23.339 5.785   1.00 28.28 ?  519 HOH   A O    1 
HETATM 6840 O O    . HOH   F 5 .   ? 23.075 -23.708 1.718   1.00 28.32 ?  520 HOH   A O    1 
HETATM 6841 O O    . HOH   F 5 .   ? 30.713 -5.784  -11.876 1.00 43.44 ?  521 HOH   A O    1 
HETATM 6842 O O    . HOH   F 5 .   ? 37.348 -6.632  7.516   1.00 21.98 ?  522 HOH   A O    1 
HETATM 6843 O O    B HOH   F 5 .   ? 14.590 7.884   4.833   0.60 23.19 ?  523 HOH   A O    1 
HETATM 6844 O O    . HOH   F 5 .   ? 38.023 13.825  6.825   1.00 43.63 ?  524 HOH   A O    1 
HETATM 6845 O O    . HOH   F 5 .   ? 39.483 0.022   6.549   1.00 26.60 ?  525 HOH   A O    1 
HETATM 6846 O O    . HOH   F 5 .   ? 29.013 14.364  0.890   1.00 43.15 ?  526 HOH   A O    1 
HETATM 6847 O O    . HOH   F 5 .   ? 20.386 -16.117 -7.389  1.00 26.87 ?  527 HOH   A O    1 
HETATM 6848 O O    . HOH   F 5 .   ? 36.387 -6.515  10.159  1.00 43.88 ?  528 HOH   A O    1 
HETATM 6849 O O    . HOH   F 5 .   ? 21.918 -24.009 4.398   1.00 26.31 ?  529 HOH   A O    1 
HETATM 6850 O O    B HOH   F 5 .   ? 21.576 7.403   -5.719  0.60 23.97 ?  530 HOH   A O    1 
HETATM 6851 O O    B HOH   F 5 .   ? 9.403  0.925   -5.801  0.60 29.99 ?  531 HOH   A O    1 
HETATM 6852 O O    A HOH   F 5 .   ? 14.803 8.700   4.909   0.40 33.21 ?  532 HOH   A O    1 
HETATM 6853 O O    T HOH   F 5 .   ? 11.870 -2.088  -3.647  0.10 6.59  ?  533 HOH   A O    1 
HETATM 6854 O O    . HOH   F 5 .   ? 17.302 -6.561  -14.237 1.00 39.16 ?  534 HOH   A O    1 
HETATM 6855 O O    . HOH   F 5 .   ? 24.015 9.144   -7.220  1.00 44.23 ?  535 HOH   A O    1 
HETATM 6856 O O    . HOH   F 5 .   ? 15.876 -12.290 27.515  1.00 43.65 ?  536 HOH   A O    1 
HETATM 6857 O O    . HOH   F 5 .   ? 16.275 -21.062 18.828  1.00 38.61 ?  537 HOH   A O    1 
HETATM 6858 O O    . HOH   F 5 .   ? 14.681 -22.777 19.826  1.00 36.36 ?  538 HOH   A O    1 
HETATM 6859 O O    . HOH   G 5 .   ? 52.811 -13.422 -20.304 1.00 32.55 ?  201 HOH   B O    1 
HETATM 6860 O O    . HOH   G 5 .   ? 29.715 -22.360 5.435   1.00 19.44 ?  202 HOH   B O    1 
HETATM 6861 O O    . HOH   G 5 .   ? 48.063 -6.857  15.569  1.00 31.75 ?  203 HOH   B O    1 
HETATM 6862 O O    . HOH   G 5 .   ? 47.267 -7.433  -3.953  1.00 38.91 ?  204 HOH   B O    1 
HETATM 6863 O O    . HOH   G 5 .   ? 49.366 -22.601 -19.682 1.00 43.57 ?  205 HOH   B O    1 
HETATM 6864 O O    . HOH   G 5 .   ? 41.849 -36.007 -17.227 1.00 27.56 ?  206 HOH   B O    1 
HETATM 6865 O O    . HOH   G 5 .   ? 37.812 -39.407 -0.240  1.00 34.40 ?  207 HOH   B O    1 
HETATM 6866 O O    . HOH   G 5 .   ? 59.073 -18.744 6.811   1.00 34.62 ?  208 HOH   B O    1 
HETATM 6867 O O    . HOH   G 5 .   ? 50.236 -3.247  7.287   1.00 33.90 ?  209 HOH   B O    1 
HETATM 6868 O O    . HOH   G 5 .   ? 57.637 -24.466 5.053   1.00 32.35 ?  210 HOH   B O    1 
HETATM 6869 O O    . HOH   G 5 .   ? 56.263 -19.660 7.387   1.00 32.90 ?  211 HOH   B O    1 
HETATM 6870 O O    . HOH   G 5 .   ? 27.813 -41.880 -15.087 1.00 31.18 ?  212 HOH   B O    1 
HETATM 6871 O O    . HOH   G 5 .   ? 27.640 -29.145 -1.849  1.00 36.72 ?  213 HOH   B O    1 
HETATM 6872 O O    . HOH   G 5 .   ? 41.233 -7.799  5.502   1.00 34.22 ?  214 HOH   B O    1 
HETATM 6873 O O    . HOH   G 5 .   ? 54.427 -9.310  -8.816  1.00 18.25 ?  215 HOH   B O    1 
HETATM 6874 O O    . HOH   G 5 .   ? 57.152 -26.873 -7.674  1.00 43.01 ?  216 HOH   B O    1 
HETATM 6875 O O    . HOH   G 5 .   ? 30.162 -41.004 -8.138  1.00 15.17 ?  217 HOH   B O    1 
HETATM 6876 O O    . HOH   G 5 .   ? 58.160 -12.894 8.445   1.00 30.83 ?  218 HOH   B O    1 
HETATM 6877 O O    . HOH   G 5 .   ? 50.664 -6.091  0.186   1.00 24.86 ?  219 HOH   B O    1 
HETATM 6878 O O    . HOH   G 5 .   ? 55.444 -16.500 -14.308 1.00 35.54 ?  220 HOH   B O    1 
HETATM 6879 O O    . HOH   G 5 .   ? 35.905 -43.181 -8.519  1.00 27.02 ?  221 HOH   B O    1 
HETATM 6880 O O    . HOH   G 5 .   ? 37.119 -19.726 -18.076 1.00 33.06 ?  222 HOH   B O    1 
HETATM 6881 O O    . HOH   G 5 .   ? 44.493 -7.179  2.162   1.00 33.63 ?  223 HOH   B O    1 
HETATM 6882 O O    . HOH   G 5 .   ? 44.920 -43.497 -10.521 1.00 27.44 ?  224 HOH   B O    1 
HETATM 6883 O O    . HOH   G 5 .   ? 41.469 -39.159 -14.849 1.00 20.51 ?  225 HOH   B O    1 
HETATM 6884 O O    . HOH   G 5 .   ? 45.019 -34.892 6.870   1.00 39.50 ?  226 HOH   B O    1 
HETATM 6885 O O    . HOH   G 5 .   ? 34.472 -36.339 -7.212  1.00 16.48 ?  227 HOH   B O    1 
HETATM 6886 O O    . HOH   G 5 .   ? 57.392 -16.241 -12.135 1.00 17.83 ?  228 HOH   B O    1 
HETATM 6887 O O    . HOH   G 5 .   ? 48.057 -24.495 -17.678 1.00 26.68 ?  229 HOH   B O    1 
HETATM 6888 O O    . HOH   G 5 .   ? 56.625 -30.778 -7.739  1.00 31.93 ?  230 HOH   B O    1 
HETATM 6889 O O    . HOH   G 5 .   ? 35.001 -7.990  -2.978  1.00 17.97 ?  231 HOH   B O    1 
HETATM 6890 O O    . HOH   G 5 .   ? 50.885 -39.940 -8.104  1.00 28.92 ?  232 HOH   B O    1 
HETATM 6891 O O    . HOH   G 5 .   ? 51.607 -6.455  4.461   1.00 19.55 ?  233 HOH   B O    1 
HETATM 6892 O O    . HOH   G 5 .   ? 39.256 -10.890 6.162   1.00 24.15 ?  234 HOH   B O    1 
HETATM 6893 O O    . HOH   G 5 .   ? 44.412 -27.696 -0.688  1.00 22.44 ?  235 HOH   B O    1 
HETATM 6894 O O    . HOH   G 5 .   ? 40.597 -15.975 14.200  1.00 24.77 ?  236 HOH   B O    1 
HETATM 6895 O O    . HOH   G 5 .   ? 41.279 -9.595  13.119  1.00 21.68 ?  237 HOH   B O    1 
HETATM 6896 O O    . HOH   G 5 .   ? 50.640 -12.929 -0.468  1.00 11.30 ?  238 HOH   B O    1 
HETATM 6897 O O    . HOH   G 5 .   ? 29.728 -34.213 -0.467  1.00 31.64 ?  239 HOH   B O    1 
HETATM 6898 O O    . HOH   G 5 .   ? 25.393 -25.936 -1.368  1.00 31.19 ?  240 HOH   B O    1 
HETATM 6899 O O    . HOH   G 5 .   ? 41.763 -23.454 9.322   1.00 15.63 ?  241 HOH   B O    1 
HETATM 6900 O O    . HOH   G 5 .   ? 30.753 -28.693 4.269   1.00 22.49 ?  242 HOH   B O    1 
HETATM 6901 O O    . HOH   G 5 .   ? 46.358 -1.547  13.306  1.00 28.55 ?  243 HOH   B O    1 
HETATM 6902 O O    . HOH   G 5 .   ? 28.346 -19.691 -13.141 1.00 23.53 ?  244 HOH   B O    1 
HETATM 6903 O O    . HOH   G 5 .   ? 29.760 -26.291 3.870   1.00 26.73 ?  245 HOH   B O    1 
HETATM 6904 O O    . HOH   G 5 .   ? 42.552 -22.839 3.855   1.00 10.70 ?  246 HOH   B O    1 
HETATM 6905 O O    . HOH   G 5 .   ? 43.039 -43.206 -8.210  1.00 27.39 ?  247 HOH   B O    1 
HETATM 6906 O O    . HOH   G 5 .   ? 51.506 -13.861 11.096  1.00 24.80 ?  248 HOH   B O    1 
HETATM 6907 O O    . HOH   G 5 .   ? 32.811 -43.804 -11.328 1.00 18.76 ?  249 HOH   B O    1 
HETATM 6908 O O    . HOH   G 5 .   ? 42.491 -25.328 2.622   1.00 13.83 ?  250 HOH   B O    1 
HETATM 6909 O O    . HOH   G 5 .   ? 48.522 -36.407 -15.514 1.00 39.64 ?  251 HOH   B O    1 
HETATM 6910 O O    . HOH   G 5 .   ? 39.416 -11.072 0.341   1.00 15.84 ?  252 HOH   B O    1 
HETATM 6911 O O    . HOH   G 5 .   ? 33.448 -16.978 8.061   1.00 17.77 ?  253 HOH   B O    1 
HETATM 6912 O O    . HOH   G 5 .   ? 34.836 -24.584 13.894  1.00 26.51 ?  254 HOH   B O    1 
HETATM 6913 O O    . HOH   G 5 .   ? 38.386 -11.035 -2.259  1.00 17.97 ?  255 HOH   B O    1 
HETATM 6914 O O    . HOH   G 5 .   ? 40.240 -12.728 -11.511 1.00 13.97 ?  256 HOH   B O    1 
HETATM 6915 O O    . HOH   G 5 .   ? 29.663 -25.220 -10.863 1.00 14.75 ?  257 HOH   B O    1 
HETATM 6916 O O    . HOH   G 5 .   ? 30.775 -15.703 2.637   1.00 12.27 ?  258 HOH   B O    1 
HETATM 6917 O O    . HOH   G 5 .   ? 57.511 -24.380 -3.842  1.00 20.85 ?  259 HOH   B O    1 
HETATM 6918 O O    . HOH   G 5 .   ? 38.844 -11.977 12.436  1.00 30.25 ?  260 HOH   B O    1 
HETATM 6919 O O    . HOH   G 5 .   ? 31.713 -17.860 -14.521 1.00 29.63 ?  261 HOH   B O    1 
HETATM 6920 O O    . HOH   G 5 .   ? 43.212 -32.354 -17.060 1.00 20.86 ?  262 HOH   B O    1 
HETATM 6921 O O    . HOH   G 5 .   ? 27.107 -31.816 -9.991  1.00 18.59 ?  263 HOH   B O    1 
HETATM 6922 O O    . HOH   G 5 .   ? 34.165 -18.457 11.462  1.00 22.66 ?  264 HOH   B O    1 
HETATM 6923 O O    . HOH   G 5 .   ? 43.289 -15.775 -12.168 1.00 12.88 ?  265 HOH   B O    1 
HETATM 6924 O O    . HOH   G 5 .   ? 58.094 -10.560 -4.076  1.00 20.95 ?  266 HOH   B O    1 
HETATM 6925 O O    . HOH   G 5 .   ? 57.392 -9.175  1.480   1.00 19.60 ?  267 HOH   B O    1 
HETATM 6926 O O    . HOH   G 5 .   ? 56.109 -23.454 -14.701 1.00 24.66 ?  268 HOH   B O    1 
HETATM 6927 O O    . HOH   G 5 .   ? 47.907 -22.747 5.872   1.00 15.78 ?  269 HOH   B O    1 
HETATM 6928 O O    . HOH   G 5 .   ? 28.227 -34.329 -9.423  1.00 18.10 ?  270 HOH   B O    1 
HETATM 6929 O O    . HOH   G 5 .   ? 49.278 -28.663 -6.853  1.00 14.56 ?  271 HOH   B O    1 
HETATM 6930 O O    . HOH   G 5 .   ? 49.871 -24.679 5.758   1.00 30.61 ?  272 HOH   B O    1 
HETATM 6931 O O    . HOH   G 5 .   ? 42.255 -9.861  9.406   1.00 20.22 ?  273 HOH   B O    1 
HETATM 6932 O O    . HOH   G 5 .   ? 27.889 -22.867 -8.045  1.00 16.19 ?  274 HOH   B O    1 
HETATM 6933 O O    . HOH   G 5 .   ? 34.875 -33.393 -19.182 1.00 25.22 ?  275 HOH   B O    1 
HETATM 6934 O O    . HOH   G 5 .   ? 30.610 -42.149 -10.639 1.00 26.82 ?  276 HOH   B O    1 
HETATM 6935 O O    . HOH   G 5 .   ? 43.504 -15.422 18.302  1.00 31.67 ?  277 HOH   B O    1 
HETATM 6936 O O    . HOH   G 5 .   ? 28.440 -30.850 -14.728 1.00 28.95 ?  278 HOH   B O    1 
HETATM 6937 O O    . HOH   G 5 .   ? 41.077 -5.545  11.553  1.00 41.95 ?  279 HOH   B O    1 
HETATM 6938 O O    . HOH   G 5 .   ? 42.297 -34.685 3.749   1.00 25.85 ?  280 HOH   B O    1 
HETATM 6939 O O    . HOH   G 5 .   ? 56.850 -8.607  8.512   1.00 18.39 ?  281 HOH   B O    1 
HETATM 6940 O O    . HOH   G 5 .   ? 46.545 -31.230 -4.736  1.00 18.08 ?  282 HOH   B O    1 
HETATM 6941 O O    . HOH   G 5 .   ? 49.704 -0.453  10.289  1.00 27.89 ?  283 HOH   B O    1 
HETATM 6942 O O    . HOH   G 5 .   ? 42.845 -20.317 -20.838 1.00 32.23 ?  284 HOH   B O    1 
HETATM 6943 O O    . HOH   G 5 .   ? 27.568 -26.769 -15.693 1.00 31.51 ?  285 HOH   B O    1 
HETATM 6944 O O    . HOH   G 5 .   ? 52.507 -10.395 13.032  1.00 22.85 ?  286 HOH   B O    1 
HETATM 6945 O O    . HOH   G 5 .   ? 34.382 -12.742 2.638   1.00 21.58 ?  287 HOH   B O    1 
HETATM 6946 O O    . HOH   G 5 .   ? 37.275 -35.635 7.162   1.00 31.20 ?  288 HOH   B O    1 
HETATM 6947 O O    . HOH   G 5 .   ? 48.350 -25.021 3.127   1.00 11.83 ?  289 HOH   B O    1 
HETATM 6948 O O    . HOH   G 5 .   ? 45.361 -33.398 -15.880 1.00 21.00 ?  290 HOH   B O    1 
HETATM 6949 O O    . HOH   G 5 .   ? 33.453 -15.285 -13.957 1.00 19.87 ?  291 HOH   B O    1 
HETATM 6950 O O    . HOH   G 5 .   ? 59.699 -15.245 8.199   1.00 31.47 ?  292 HOH   B O    1 
HETATM 6951 O O    . HOH   G 5 .   ? 51.194 -37.601 -9.478  1.00 24.39 ?  293 HOH   B O    1 
HETATM 6952 O O    . HOH   G 5 .   ? 41.110 -24.467 15.835  1.00 41.23 ?  294 HOH   B O    1 
HETATM 6953 O O    . HOH   G 5 .   ? 42.186 -10.000 -14.939 1.00 35.59 ?  295 HOH   B O    1 
HETATM 6954 O O    . HOH   G 5 .   ? 47.019 -33.931 -4.582  1.00 15.79 ?  296 HOH   B O    1 
HETATM 6955 O O    . HOH   G 5 .   ? 57.649 -22.084 3.071   1.00 28.62 ?  297 HOH   B O    1 
HETATM 6956 O O    . HOH   G 5 .   ? 48.636 -19.999 5.972   1.00 13.15 ?  298 HOH   B O    1 
HETATM 6957 O O    . HOH   G 5 .   ? 43.981 -29.308 -4.685  1.00 23.19 ?  299 HOH   B O    1 
HETATM 6958 O O    . HOH   G 5 .   ? 36.707 -12.739 -1.470  1.00 26.01 ?  300 HOH   B O    1 
HETATM 6959 O O    . HOH   G 5 .   ? 46.797 -29.456 9.843   1.00 30.24 ?  301 HOH   B O    1 
HETATM 6960 O O    . HOH   G 5 .   ? 57.005 -12.023 12.415  1.00 41.61 ?  302 HOH   B O    1 
HETATM 6961 O O    . HOH   G 5 .   ? 25.878 -21.450 -3.526  1.00 14.66 ?  303 HOH   B O    1 
HETATM 6962 O O    . HOH   G 5 .   ? 44.549 -27.399 2.006   1.00 14.01 ?  304 HOH   B O    1 
HETATM 6963 O O    . HOH   G 5 .   ? 52.569 -35.621 -8.511  1.00 26.28 ?  305 HOH   B O    1 
HETATM 6964 O O    . HOH   G 5 .   ? 42.589 -12.356 -18.554 1.00 29.55 ?  306 HOH   B O    1 
HETATM 6965 O O    . HOH   G 5 .   ? 53.427 -30.146 4.528   1.00 17.11 ?  307 HOH   B O    1 
HETATM 6966 O O    . HOH   G 5 .   ? 53.564 -12.611 -22.229 1.00 31.60 ?  308 HOH   B O    1 
HETATM 6967 O O    . HOH   G 5 .   ? 45.822 -40.369 -3.527  1.00 27.37 ?  309 HOH   B O    1 
HETATM 6968 O O    . HOH   G 5 .   ? 40.172 -10.803 -9.560  1.00 16.20 ?  310 HOH   B O    1 
HETATM 6969 O O    . HOH   G 5 .   ? 41.654 -8.067  1.374   1.00 24.40 ?  311 HOH   B O    1 
HETATM 6970 O O    . HOH   G 5 .   ? 34.917 -33.519 4.499   1.00 24.71 ?  312 HOH   B O    1 
HETATM 6971 O O    . HOH   G 5 .   ? 51.312 -32.889 -10.680 1.00 35.00 ?  313 HOH   B O    1 
HETATM 6972 O O    . HOH   G 5 .   ? 37.421 -18.186 13.160  1.00 28.08 ?  314 HOH   B O    1 
HETATM 6973 O O    . HOH   G 5 .   ? 43.123 -21.374 10.707  1.00 15.09 ?  315 HOH   B O    1 
HETATM 6974 O O    . HOH   G 5 .   ? 59.916 -17.100 -10.406 1.00 31.52 ?  316 HOH   B O    1 
HETATM 6975 O O    . HOH   G 5 .   ? 37.775 -10.227 -10.772 1.00 16.30 ?  317 HOH   B O    1 
HETATM 6976 O O    . HOH   G 5 .   ? 53.306 -16.127 -12.642 1.00 28.38 ?  318 HOH   B O    1 
HETATM 6977 O O    . HOH   G 5 .   ? 52.499 -29.205 -13.003 1.00 22.51 ?  319 HOH   B O    1 
HETATM 6978 O O    . HOH   G 5 .   ? 48.106 -32.615 -16.576 1.00 39.76 ?  320 HOH   B O    1 
HETATM 6979 O O    . HOH   G 5 .   ? 62.636 -13.545 4.731   1.00 26.89 ?  321 HOH   B O    1 
HETATM 6980 O O    . HOH   G 5 .   ? 32.753 -34.555 -5.947  1.00 15.41 ?  322 HOH   B O    1 
HETATM 6981 O O    . HOH   G 5 .   ? 38.269 -9.331  -13.273 1.00 23.98 ?  323 HOH   B O    1 
HETATM 6982 O O    . HOH   G 5 .   ? 27.956 -14.774 -9.341  1.00 32.03 ?  324 HOH   B O    1 
HETATM 6983 O O    . HOH   G 5 .   ? 26.271 -20.985 -6.252  1.00 15.21 ?  325 HOH   B O    1 
HETATM 6984 O O    . HOH   G 5 .   ? 44.501 -24.584 9.599   1.00 18.12 ?  326 HOH   B O    1 
HETATM 6985 O O    . HOH   G 5 .   ? 38.288 -12.747 7.943   1.00 17.71 ?  327 HOH   B O    1 
HETATM 6986 O O    . HOH   G 5 .   ? 51.667 -5.940  -7.905  1.00 50.49 ?  328 HOH   B O    1 
HETATM 6987 O O    . HOH   G 5 .   ? 62.814 -20.085 -0.767  1.00 34.54 ?  329 HOH   B O    1 
HETATM 6988 O O    . HOH   G 5 .   ? 36.634 -12.400 4.291   1.00 17.15 ?  330 HOH   B O    1 
HETATM 6989 O O    . HOH   G 5 .   ? 37.173 -30.532 -21.094 1.00 29.60 ?  331 HOH   B O    1 
HETATM 6990 O O    . HOH   G 5 .   ? 44.148 -1.724  7.603   1.00 41.90 ?  332 HOH   B O    1 
HETATM 6991 O O    . HOH   G 5 .   ? 48.506 -11.874 -13.787 1.00 25.53 ?  333 HOH   B O    1 
HETATM 6992 O O    . HOH   G 5 .   ? 47.078 -24.473 8.183   1.00 23.69 ?  334 HOH   B O    1 
HETATM 6993 O O    . HOH   G 5 .   ? 45.651 -36.256 -16.087 1.00 33.45 ?  335 HOH   B O    1 
HETATM 6994 O O    . HOH   G 5 .   ? 39.433 -23.525 -20.299 1.00 36.62 ?  336 HOH   B O    1 
HETATM 6995 O O    . HOH   G 5 .   ? 43.052 -34.672 0.124   1.00 17.97 ?  337 HOH   B O    1 
HETATM 6996 O O    . HOH   G 5 .   ? 42.848 -43.486 -14.315 1.00 37.63 ?  338 HOH   B O    1 
HETATM 6997 O O    . HOH   G 5 .   ? 36.954 -15.112 -16.506 1.00 38.45 ?  339 HOH   B O    1 
HETATM 6998 O O    . HOH   G 5 .   ? 33.417 -31.216 11.087  1.00 31.88 ?  340 HOH   B O    1 
HETATM 6999 O O    . HOH   G 5 .   ? 47.392 -27.400 2.040   1.00 13.53 ?  341 HOH   B O    1 
HETATM 7000 O O    . HOH   G 5 .   ? 46.682 -19.866 12.319  1.00 29.19 ?  342 HOH   B O    1 
HETATM 7001 O O    . HOH   G 5 .   ? 37.063 -45.221 -9.785  1.00 37.22 ?  343 HOH   B O    1 
HETATM 7002 O O    . HOH   G 5 .   ? 32.939 -14.663 1.053   1.00 17.10 ?  344 HOH   B O    1 
HETATM 7003 O O    . HOH   G 5 .   ? 38.418 -12.280 -16.190 1.00 36.64 ?  345 HOH   B O    1 
HETATM 7004 O O    . HOH   G 5 .   ? 38.510 -22.350 15.059  1.00 39.29 ?  346 HOH   B O    1 
HETATM 7005 O O    . HOH   G 5 .   ? 27.683 -26.542 -0.649  1.00 29.28 ?  347 HOH   B O    1 
HETATM 7006 O O    . HOH   G 5 .   ? 40.391 -43.450 -9.128  1.00 25.52 ?  348 HOH   B O    1 
HETATM 7007 O O    . HOH   G 5 .   ? 28.887 -42.991 -12.285 1.00 30.37 ?  349 HOH   B O    1 
HETATM 7008 O O    . HOH   G 5 .   ? 39.748 -44.311 -11.244 1.00 36.35 ?  350 HOH   B O    1 
HETATM 7009 O O    . HOH   G 5 .   ? 44.141 -37.321 -17.694 1.00 31.71 ?  351 HOH   B O    1 
HETATM 7010 O O    . HOH   G 5 .   ? 33.699 -9.245  -8.912  1.00 31.91 ?  352 HOH   B O    1 
HETATM 7011 O O    . HOH   G 5 .   ? 62.526 -20.137 -4.842  1.00 39.43 ?  353 HOH   B O    1 
HETATM 7012 O O    . HOH   G 5 .   ? 55.592 -8.267  10.937  1.00 25.50 ?  354 HOH   B O    1 
HETATM 7013 O O    . HOH   G 5 .   ? 36.030 -8.552  -9.714  1.00 33.27 ?  355 HOH   B O    1 
HETATM 7014 O O    . HOH   G 5 .   ? 23.099 -23.652 6.825   1.00 33.53 ?  356 HOH   B O    1 
HETATM 7015 O O    . HOH   G 5 .   ? 56.382 -7.196  3.149   1.00 25.62 ?  357 HOH   B O    1 
HETATM 7016 O O    . HOH   G 5 .   ? 34.595 -10.294 7.502   1.00 22.96 ?  358 HOH   B O    1 
HETATM 7017 O O    . HOH   G 5 .   ? 43.069 -12.717 -21.187 1.00 41.40 ?  359 HOH   B O    1 
HETATM 7018 O O    . HOH   G 5 .   ? 34.071 -7.750  11.449  1.00 37.88 ?  360 HOH   B O    1 
HETATM 7019 O O    . HOH   G 5 .   ? 61.455 -19.864 1.659   1.00 32.50 ?  361 HOH   B O    1 
HETATM 7020 O O    . HOH   G 5 .   ? 56.890 -21.491 -16.380 1.00 38.26 ?  362 HOH   B O    1 
HETATM 7021 O O    . HOH   G 5 .   ? 40.166 -8.844  9.954   1.00 38.44 ?  363 HOH   B O    1 
HETATM 7022 O O    . HOH   G 5 .   ? 27.059 -25.989 -11.410 1.00 31.58 ?  364 HOH   B O    1 
HETATM 7023 O O    . HOH   G 5 .   ? 36.058 -8.650  9.052   1.00 34.93 ?  365 HOH   B O    1 
HETATM 7024 O O    . HOH   G 5 .   ? 32.444 -23.614 14.137  1.00 38.23 ?  366 HOH   B O    1 
HETATM 7025 O O    . HOH   G 5 .   ? 54.139 -5.714  3.053   1.00 32.85 ?  367 HOH   B O    1 
HETATM 7026 O O    . HOH   G 5 .   ? 58.815 -10.406 9.337   1.00 37.21 ?  368 HOH   B O    1 
HETATM 7027 O O    . HOH   G 5 .   ? 48.277 -26.534 8.876   1.00 40.96 ?  369 HOH   B O    1 
HETATM 7028 O O    . HOH   G 5 .   ? 41.738 -10.075 -17.396 1.00 52.91 ?  370 HOH   B O    1 
HETATM 7029 O O    . HOH   G 5 .   ? 39.979 -11.380 -13.983 1.00 27.77 ?  371 HOH   B O    1 
HETATM 7030 O O    . HOH   G 5 .   ? 39.794 -6.964  7.921   1.00 40.96 ?  372 HOH   B O    1 
HETATM 7031 O O    . HOH   G 5 .   ? 51.995 -12.859 13.399  1.00 31.70 ?  373 HOH   B O    1 
HETATM 7032 O O    . HOH   G 5 .   ? 55.993 -7.768  -0.573  1.00 34.05 ?  374 HOH   B O    1 
HETATM 7033 O O    . HOH   G 5 .   ? 62.951 -12.347 6.940   1.00 37.35 ?  375 HOH   B O    1 
HETATM 7034 O O    . HOH   G 5 .   ? 37.978 -10.608 10.049  1.00 29.94 ?  376 HOH   B O    1 
HETATM 7035 O O    . HOH   G 5 .   ? 44.049 -5.558  -3.466  1.00 43.76 ?  377 HOH   B O    1 
HETATM 7036 O O    . HOH   G 5 .   ? 42.599 -17.190 -23.156 1.00 44.01 ?  378 HOH   B O    1 
HETATM 7037 O O    . HOH   G 5 .   ? 41.740 -6.675  -4.800  1.00 45.99 ?  379 HOH   B O    1 
HETATM 7038 O O    . HOH   G 5 .   ? 36.460 -22.701 13.312  1.00 24.99 ?  380 HOH   B O    1 
HETATM 7039 O O    . HOH   G 5 .   ? 39.619 -14.017 15.681  1.00 53.75 ?  381 HOH   B O    1 
HETATM 7040 O O    . HOH   G 5 .   ? 40.008 -7.584  3.255   1.00 29.97 ?  382 HOH   B O    1 
HETATM 7041 O O    . HOH   G 5 .   ? 52.792 -29.871 7.175   1.00 22.32 ?  383 HOH   B O    1 
HETATM 7042 O O    . HOH   G 5 .   ? 46.631 -5.397  2.951   1.00 38.67 ?  384 HOH   B O    1 
HETATM 7043 O O    . HOH   G 5 .   ? 60.426 -22.239 2.869   1.00 41.57 ?  385 HOH   B O    1 
HETATM 7044 O O    . HOH   G 5 .   ? 35.253 -33.654 7.208   1.00 38.11 ?  386 HOH   B O    1 
HETATM 7045 O O    . HOH   G 5 .   ? 25.780 -18.793 -11.907 1.00 37.93 ?  387 HOH   B O    1 
HETATM 7046 O O    . HOH   G 5 .   ? 23.827 -20.770 -7.669  1.00 27.31 ?  388 HOH   B O    1 
HETATM 7047 O O    . HOH   G 5 .   ? 35.246 -20.245 13.347  1.00 29.23 ?  389 HOH   B O    1 
HETATM 7048 O O    . HOH   G 5 .   ? 40.823 -9.849  15.868  1.00 42.39 ?  390 HOH   B O    1 
HETATM 7049 O O    . HOH   G 5 .   ? 40.690 -6.583  -0.884  1.00 22.43 ?  391 HOH   B O    1 
HETATM 7050 O O    . HOH   G 5 .   ? 44.051 -31.746 -3.820  1.00 31.31 ?  392 HOH   B O    1 
HETATM 7051 O O    . HOH   G 5 .   ? 26.613 -27.992 -13.556 1.00 31.13 ?  393 HOH   B O    1 
HETATM 7052 O O    . HOH   G 5 .   ? 27.755 -27.055 2.158   1.00 29.74 ?  394 HOH   B O    1 
HETATM 7053 O O    . HOH   G 5 .   ? 34.283 -33.374 9.641   1.00 32.14 ?  395 HOH   B O    1 
HETATM 7054 O O    . HOH   G 5 .   ? 45.662 -20.344 15.222  1.00 53.82 ?  396 HOH   B O    1 
HETATM 7055 O O    . HOH   G 5 .   ? 24.524 -20.618 -10.508 1.00 35.45 ?  397 HOH   B O    1 
HETATM 7056 O O    . HOH   G 5 .   ? 26.822 -30.674 -12.642 1.00 26.97 ?  398 HOH   B O    1 
HETATM 7057 O O    . HOH   G 5 .   ? 50.589 -30.738 8.743   1.00 25.69 ?  399 HOH   B O    1 
HETATM 7058 O O    . HOH   G 5 .   ? 57.588 -6.475  -2.373  1.00 33.14 ?  400 HOH   B O    1 
HETATM 7059 O O    . HOH   G 5 .   ? 40.941 -11.739 -22.380 1.00 39.08 ?  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   ? 0.5769 0.5868 0.6417 -0.0142 -0.0135 0.0520  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.5793 0.5891 0.6505 -0.0136 -0.0164 0.0586  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.5750 0.5856 0.6348 -0.0147 -0.0138 0.0525  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.5773 0.5876 0.6425 -0.0137 -0.0168 0.0589  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.5626 0.5766 0.6068 -0.0210 -0.0166 0.0582  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.5638 0.5778 0.6115 -0.0204 -0.0185 0.0620  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.5653 0.5792 0.6107 -0.0191 -0.0163 0.0589  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.5668 0.5807 0.6163 -0.0182 -0.0187 0.0635  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.5834 0.5918 0.6492 -0.0101 -0.0115 0.0488  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.5865 0.5943 0.6582 -0.0085 -0.0150 0.0571  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.5866 0.5944 0.6562 -0.0088 -0.0106 0.0475  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.5901 0.5974 0.6654 -0.0071 -0.0143 0.0564  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.5862 0.5937 0.6564 -0.0081 -0.0106 0.0476  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.5895 0.5958 0.6655 -0.0061 -0.0143 0.0569  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.5445 0.5626 0.5645 -0.0300 -0.0189 0.0639  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.5055 0.5315 0.4747 -0.0499 -0.0194 0.0696  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.4619 0.4995 0.4158 -0.0662 -0.0112 0.0436  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.4652 0.5011 0.4114 -0.0651 -0.0130 0.0482  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.5091 0.5311 0.4421 -0.0545 -0.0262 0.1008  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.5118 0.5288 0.4106 -0.0592 -0.0312 0.1299  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.5138 0.5263 0.3981 -0.0613 -0.0309 0.1412  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.5124 0.5284 0.3977 -0.0591 -0.0343 0.1414  4   ASN   A ND2 
46   N N   A SER   A 5   ? 0.4382 0.4811 0.3939 -0.0753 -0.0049 0.0286  5   SER   A N   
47   N N   B SER   A 5   ? 0.4383 0.4818 0.3885 -0.0756 -0.0067 0.0280  5   SER   A N   
48   C CA  A SER   A 5   ? 0.4142 0.4618 0.3735 -0.0830 0.0025  0.0147  5   SER   A CA  
49   C CA  B SER   A 5   ? 0.4143 0.4631 0.3666 -0.0834 -0.0005 0.0135  5   SER   A CA  
50   C C   A SER   A 5   ? 0.3875 0.4368 0.3318 -0.0900 0.0127  0.0077  5   SER   A C   
51   C C   B SER   A 5   ? 0.3881 0.4381 0.3254 -0.0898 0.0111  0.0063  5   SER   A C   
52   O O   A SER   A 5   ? 0.3885 0.4403 0.3338 -0.0867 0.0123  0.0006  5   SER   A O   
53   O O   B SER   A 5   ? 0.3900 0.4428 0.3251 -0.0851 0.0117  -0.0021 5   SER   A O   
54   C CB  A SER   A 5   ? 0.4177 0.4666 0.3868 -0.0829 0.0010  0.0094  5   SER   A CB  
55   C CB  B SER   A 5   ? 0.4180 0.4689 0.3781 -0.0838 -0.0040 0.0077  5   SER   A CB  
56   O OG  A SER   A 5   ? 0.4202 0.4692 0.3968 -0.0834 0.0015  0.0073  5   SER   A OG  
57   O OG  B SER   A 5   ? 0.4206 0.4720 0.3879 -0.0848 -0.0043 0.0051  5   SER   A OG  
68   N N   . PHE   A 6   ? 0.3586 0.4070 0.2879 -0.0988 0.0263  0.0094  6   PHE   A N   
69   C CA  . PHE   A 6   ? 0.3063 0.3502 0.2313 -0.1069 0.0504  0.0187  6   PHE   A CA  
70   C C   . PHE   A 6   ? 0.2898 0.3381 0.2315 -0.1053 0.0725  0.0115  6   PHE   A C   
71   O O   . PHE   A 6   ? 0.2939 0.3455 0.2578 -0.1103 0.0771  0.0195  6   PHE   A O   
72   C CB  . PHE   A 6   ? 0.2811 0.3140 0.1853 -0.1035 0.0425  0.0268  6   PHE   A CB  
73   C CG  . PHE   A 6   ? 0.2578 0.2868 0.1751 -0.0943 0.0312  0.0362  6   PHE   A CG  
74   C CD1 . PHE   A 6   ? 0.2449 0.2788 0.1768 -0.0833 0.0250  0.0360  6   PHE   A CD1 
75   C CD2 . PHE   A 6   ? 0.2615 0.2807 0.1995 -0.0787 0.0270  0.0376  6   PHE   A CD2 
76   C CE1 . PHE   A 6   ? 0.2399 0.2755 0.1863 -0.0810 0.0355  0.0387  6   PHE   A CE1 
77   C CE2 . PHE   A 6   ? 0.2563 0.2784 0.2127 -0.0701 0.0235  0.0339  6   PHE   A CE2 
78   C CZ  . PHE   A 6   ? 0.2450 0.2747 0.2034 -0.0787 0.0242  0.0314  6   PHE   A CZ  
89   N N   A SER   A 7   ? 0.2813 0.3324 0.2366 -0.0959 0.0729  0.0041  7   SER   A N   
90   N N   B SER   A 7   ? 0.2789 0.3259 0.2202 -0.1037 0.0847  0.0053  7   SER   A N   
91   C CA  A SER   A 7   ? 0.2749 0.3255 0.2559 -0.0826 0.0691  -0.0088 7   SER   A CA  
92   C CA  B SER   A 7   ? 0.2757 0.3194 0.2380 -0.0948 0.0862  -0.0132 7   SER   A CA  
93   C C   A SER   A 7   ? 0.2553 0.2987 0.2390 -0.0763 0.0719  -0.0072 7   SER   A C   
94   C C   B SER   A 7   ? 0.2544 0.2872 0.2209 -0.0939 0.0930  -0.0084 7   SER   A C   
95   O O   A SER   A 7   ? 0.2606 0.2961 0.2421 -0.0785 0.0703  -0.0072 7   SER   A O   
96   O O   B SER   A 7   ? 0.2613 0.2794 0.2282 -0.1006 0.0919  -0.0056 7   SER   A O   
97   C CB  A SER   A 7   ? 0.2866 0.3402 0.2913 -0.0750 0.0660  -0.0136 7   SER   A CB  
98   C CB  B SER   A 7   ? 0.2939 0.3397 0.2770 -0.0855 0.0844  -0.0214 7   SER   A CB  
99   O OG  A SER   A 7   ? 0.2979 0.3511 0.3129 -0.0680 0.0657  -0.0146 7   SER   A OG  
100  O OG  B SER   A 7   ? 0.3117 0.3586 0.3009 -0.0773 0.0859  -0.0245 7   SER   A OG  
111  N N   A GLY   A 8   ? 0.2314 0.2758 0.2286 -0.0665 0.0698  -0.0098 8   GLY   A N   
112  N N   B GLY   A 8   ? 0.2290 0.2651 0.2179 -0.0841 0.0873  -0.0154 8   GLY   A N   
113  C CA  A GLY   A 8   ? 0.2110 0.2532 0.2216 -0.0521 0.0634  -0.0067 8   GLY   A CA  
114  C CA  B GLY   A 8   ? 0.2098 0.2456 0.2190 -0.0644 0.0745  -0.0115 8   GLY   A CA  
115  C C   A GLY   A 8   ? 0.1860 0.2337 0.2123 -0.0355 0.0605  -0.0065 8   GLY   A C   
116  C C   B GLY   A 8   ? 0.1811 0.2298 0.2138 -0.0426 0.0654  -0.0117 8   GLY   A C   
117  O O   A GLY   A 8   ? 0.1864 0.2340 0.2246 -0.0235 0.0552  -0.0171 8   GLY   A O   
118  O O   B GLY   A 8   ? 0.1764 0.2320 0.2365 -0.0298 0.0567  -0.0288 8   GLY   A O   
125  N N   . TYR   A 9   ? 0.1686 0.2182 0.2022 -0.0298 0.0565  0.0044  9   TYR   A N   
126  C CA  . TYR   A 9   ? 0.1524 0.1946 0.1711 -0.0213 0.0365  0.0211  9   TYR   A CA  
127  C C   . TYR   A 9   ? 0.1475 0.1716 0.1726 -0.0101 0.0359  0.0429  9   TYR   A C   
128  O O   . TYR   A 9   ? 0.1744 0.1879 0.1973 -0.0117 0.0263  0.0486  9   TYR   A O   
129  C CB  . TYR   A 9   ? 0.1504 0.2017 0.1753 -0.0154 0.0313  0.0232  9   TYR   A CB  
130  C CG  . TYR   A 9   ? 0.1543 0.2046 0.1829 -0.0118 0.0366  0.0151  9   TYR   A CG  
131  C CD1 . TYR   A 9   ? 0.1579 0.2196 0.1913 -0.0276 0.0440  0.0041  9   TYR   A CD1 
132  C CD2 . TYR   A 9   ? 0.1570 0.1904 0.1751 -0.0027 0.0269  0.0180  9   TYR   A CD2 
133  C CE1 . TYR   A 9   ? 0.1606 0.2250 0.1959 -0.0358 0.0448  -0.0102 9   TYR   A CE1 
134  C CE2 . TYR   A 9   ? 0.1519 0.1974 0.1800 -0.0061 0.0302  0.0042  9   TYR   A CE2 
135  C CZ  . TYR   A 9   ? 0.1519 0.2171 0.1978 -0.0273 0.0488  -0.0083 9   TYR   A CZ  
136  O OH  . TYR   A 9   ? 0.1621 0.2333 0.2193 -0.0393 0.0528  -0.0137 9   TYR   A OH  
147  N N   A LEU   A 10  ? 0.1383 0.1592 0.1753 -0.0053 0.0336  0.0430  10  LEU   A N   
148  N N   B LEU   A 10  ? 0.1417 0.1556 0.1794 -0.0087 0.0276  0.0404  10  LEU   A N   
149  C CA  A LEU   A 10  ? 0.1279 0.1541 0.1786 -0.0061 0.0300  0.0521  10  LEU   A CA  
150  C CA  B LEU   A 10  ? 0.1329 0.1496 0.1872 -0.0126 0.0227  0.0546  10  LEU   A CA  
151  C C   A LEU   A 10  ? 0.1247 0.1482 0.1771 -0.0090 0.0200  0.0540  10  LEU   A C   
152  C C   B LEU   A 10  ? 0.1303 0.1451 0.1899 -0.0106 0.0213  0.0517  10  LEU   A C   
153  O O   A LEU   A 10  ? 0.1281 0.1391 0.1715 -0.0123 0.0221  0.0512  10  LEU   A O   
154  O O   B LEU   A 10  ? 0.1394 0.1330 0.1981 -0.0113 0.0338  0.0425  10  LEU   A O   
155  C CB  A LEU   A 10  ? 0.1257 0.1570 0.1980 -0.0002 0.0280  0.0541  10  LEU   A CB  
156  C CB  B LEU   A 10  ? 0.1353 0.1509 0.2191 -0.0120 0.0088  0.0615  10  LEU   A CB  
157  C CG  A LEU   A 10  ? 0.1330 0.1606 0.2208 0.0055  0.0186  0.0510  10  LEU   A CG  
158  C CG  B LEU   A 10  ? 0.1485 0.1565 0.2506 -0.0093 -0.0157 0.0597  10  LEU   A CG  
159  C CD1 A LEU   A 10  ? 0.1297 0.1580 0.2299 0.0021  0.0321  0.0567  10  LEU   A CD1 
160  C CD1 B LEU   A 10  ? 0.1534 0.1637 0.2783 -0.0100 -0.0073 0.0464  10  LEU   A CD1 
161  C CD2 A LEU   A 10  ? 0.1470 0.1684 0.2285 0.0128  0.0148  0.0466  10  LEU   A CD2 
162  C CD2 B LEU   A 10  ? 0.1626 0.1632 0.2583 -0.0001 -0.0155 0.0524  10  LEU   A CD2 
185  N N   . LYS   A 11  ? 0.1267 0.1475 0.1881 -0.0126 0.0154  0.0578  11  LYS   A N   
186  C CA  . LYS   A 11  ? 0.1308 0.1467 0.1940 -0.0252 0.0092  0.0512  11  LYS   A CA  
187  C C   . LYS   A 11  ? 0.1312 0.1567 0.1961 -0.0354 0.0058  0.0458  11  LYS   A C   
188  O O   . LYS   A 11  ? 0.1413 0.1901 0.2125 -0.0518 0.0117  0.0303  11  LYS   A O   
189  C CB  . LYS   A 11  ? 0.1511 0.1354 0.1909 -0.0240 0.0065  0.0394  11  LYS   A CB  
190  C CG  . LYS   A 11  ? 0.1598 0.1328 0.1875 -0.0277 0.0106  0.0338  11  LYS   A CG  
191  C CD  . LYS   A 11  ? 0.1727 0.1390 0.1880 -0.0148 0.0126  0.0388  11  LYS   A CD  
192  C CE  . LYS   A 11  ? 0.1836 0.1393 0.1909 -0.0157 0.0101  0.0418  11  LYS   A CE  
193  N NZ  . LYS   A 11  ? 0.1744 0.1426 0.1950 -0.0118 -0.0008 0.0355  11  LYS   A NZ  
208  N N   . LEU   A 12  ? 0.1193 0.1532 0.1837 -0.0281 0.0054  0.0384  12  LEU   A N   
209  C CA  . LEU   A 12  ? 0.1223 0.1701 0.1787 -0.0217 -0.0000 0.0474  12  LEU   A CA  
210  C C   . LEU   A 12  ? 0.1293 0.1607 0.1714 -0.0279 0.0120  0.0430  12  LEU   A C   
211  O O   . LEU   A 12  ? 0.1408 0.1680 0.1738 -0.0307 0.0044  0.0360  12  LEU   A O   
212  C CB  . LEU   A 12  ? 0.1282 0.1779 0.1880 -0.0153 -0.0022 0.0486  12  LEU   A CB  
213  C CG  . LEU   A 12  ? 0.1376 0.1833 0.2013 -0.0098 0.0118  0.0616  12  LEU   A CG  
214  C CD1 . LEU   A 12  ? 0.1474 0.1901 0.2148 -0.0065 0.0219  0.0643  12  LEU   A CD1 
215  C CD2 . LEU   A 12  ? 0.1395 0.1908 0.2230 -0.0054 0.0090  0.0583  12  LEU   A CD2 
227  N N   . THR   A 13  ? 0.1236 0.1494 0.1847 -0.0215 0.0093  0.0340  13  THR   A N   
228  C CA  . THR   A 13  ? 0.1268 0.1510 0.1946 -0.0236 0.0177  0.0293  13  THR   A CA  
229  C C   . THR   A 13  ? 0.1346 0.1425 0.1969 -0.0229 0.0107  0.0393  13  THR   A C   
230  O O   . THR   A 13  ? 0.1362 0.1489 0.1894 -0.0163 0.0012  0.0340  13  THR   A O   
231  C CB  . THR   A 13  ? 0.1395 0.1684 0.2087 -0.0254 0.0108  0.0319  13  THR   A CB  
232  O OG1 . THR   A 13  ? 0.1290 0.1660 0.2249 -0.0240 0.0074  0.0467  13  THR   A OG1 
233  C CG2 . THR   A 13  ? 0.1513 0.1847 0.2049 -0.0170 0.0156  0.0196  13  THR   A CG2 
241  N N   . ASP   A 14  ? 0.1398 0.1458 0.2025 -0.0283 0.0052  0.0450  14  ASP   A N   
242  C CA  . ASP   A 14  ? 0.1469 0.1489 0.2155 -0.0202 -0.0031 0.0588  14  ASP   A CA  
243  C C   . ASP   A 14  ? 0.1396 0.1553 0.1915 -0.0231 -0.0138 0.0586  14  ASP   A C   
244  O O   . ASP   A 14  ? 0.1674 0.1681 0.1967 -0.0370 -0.0146 0.0621  14  ASP   A O   
245  C CB  . ASP   A 14  ? 0.1695 0.1687 0.2759 -0.0226 0.0013  0.0648  14  ASP   A CB  
246  C CG  . ASP   A 14  ? 0.2027 0.2269 0.3497 -0.0118 0.0082  0.0564  14  ASP   A CG  
247  O OD1 . ASP   A 14  ? 0.2199 0.2401 0.3722 -0.0045 -0.0030 0.0543  14  ASP   A OD1 
248  O OD2 . ASP   A 14  ? 0.2249 0.2687 0.3889 -0.0027 -0.0028 0.0440  14  ASP   A OD2 
253  N N   . ASN   A 15  ? 0.1243 0.1384 0.1948 -0.0168 -0.0001 0.0537  15  ASN   A N   
254  C CA  . ASN   A 15  ? 0.1281 0.1357 0.2029 -0.0171 0.0001  0.0420  15  ASN   A CA  
255  C C   . ASN   A 15  ? 0.1278 0.1254 0.2269 -0.0162 0.0001  0.0432  15  ASN   A C   
256  O O   . ASN   A 15  ? 0.1306 0.1358 0.2758 -0.0184 -0.0178 0.0352  15  ASN   A O   
257  C CB  . ASN   A 15  ? 0.1198 0.1360 0.2040 -0.0070 0.0065  0.0364  15  ASN   A CB  
258  C CG  . ASN   A 15  ? 0.1258 0.1375 0.2075 -0.0064 0.0077  0.0261  15  ASN   A CG  
259  O OD1 . ASN   A 15  ? 0.1423 0.1477 0.2272 -0.0200 0.0098  0.0342  15  ASN   A OD1 
260  N ND2 . ASN   A 15  ? 0.1258 0.1543 0.2100 -0.0131 0.0071  0.0267  15  ASN   A ND2 
267  N N   . VAL   A 16  ? 0.1253 0.1285 0.2102 -0.0119 0.0051  0.0405  16  VAL   A N   
268  C CA  . VAL   A 16  ? 0.1226 0.1357 0.2039 -0.0134 0.0053  0.0415  16  VAL   A CA  
269  C C   . VAL   A 16  ? 0.1214 0.1343 0.1907 -0.0124 0.0070  0.0404  16  VAL   A C   
270  O O   . VAL   A 16  ? 0.1141 0.1339 0.1977 -0.0156 0.0142  0.0273  16  VAL   A O   
271  C CB  . VAL   A 16  ? 0.1336 0.1578 0.1976 0.0078  0.0289  0.0501  16  VAL   A CB  
272  C CG1 . VAL   A 16  ? 0.1485 0.1721 0.2054 0.0141  0.0353  0.0466  16  VAL   A CG1 
273  C CG2 . VAL   A 16  ? 0.1456 0.1708 0.2130 0.0065  0.0434  0.0501  16  VAL   A CG2 
283  N N   A TYR   A 17  ? 0.1237 0.1276 0.1822 -0.0132 0.0095  0.0353  17  TYR   A N   
284  N N   B TYR   A 17  ? 0.1132 0.1360 0.1907 -0.0113 0.0132  0.0435  17  TYR   A N   
285  C CA  A TYR   A 17  ? 0.1319 0.1239 0.1714 -0.0152 0.0086  0.0300  17  TYR   A CA  
286  C CA  B TYR   A 17  ? 0.1117 0.1424 0.1833 -0.0140 0.0113  0.0448  17  TYR   A CA  
287  C C   A TYR   A 17  ? 0.1340 0.1137 0.1621 -0.0174 0.0074  0.0240  17  TYR   A C   
288  C C   B TYR   A 17  ? 0.1154 0.1420 0.1849 -0.0136 0.0185  0.0464  17  TYR   A C   
289  O O   A TYR   A 17  ? 0.1360 0.1164 0.1876 -0.0123 0.0185  0.0285  17  TYR   A O   
290  O O   B TYR   A 17  ? 0.1104 0.1520 0.1992 -0.0109 0.0255  0.0572  17  TYR   A O   
291  C CB  A TYR   A 17  ? 0.1443 0.1204 0.1800 -0.0193 0.0038  0.0279  17  TYR   A CB  
292  C CB  B TYR   A 17  ? 0.1246 0.1433 0.1855 -0.0144 0.0011  0.0434  17  TYR   A CB  
293  C CG  A TYR   A 17  ? 0.1584 0.1230 0.1871 -0.0162 -0.0123 0.0278  17  TYR   A CG  
294  C CG  B TYR   A 17  ? 0.1453 0.1561 0.1923 -0.0139 -0.0070 0.0320  17  TYR   A CG  
295  C CD1 A TYR   A 17  ? 0.1645 0.1345 0.1971 -0.0139 -0.0166 0.0267  17  TYR   A CD1 
296  C CD1 B TYR   A 17  ? 0.1631 0.1664 0.2082 -0.0006 -0.0105 0.0304  17  TYR   A CD1 
297  C CD2 A TYR   A 17  ? 0.1625 0.1249 0.1751 -0.0226 -0.0169 0.0285  17  TYR   A CD2 
298  C CD2 B TYR   A 17  ? 0.1586 0.1650 0.1874 -0.0196 -0.0117 0.0268  17  TYR   A CD2 
299  C CE1 A TYR   A 17  ? 0.1622 0.1373 0.1971 -0.0176 -0.0193 0.0277  17  TYR   A CE1 
300  C CE1 B TYR   A 17  ? 0.1744 0.1682 0.2064 -0.0029 -0.0116 0.0329  17  TYR   A CE1 
301  C CE2 A TYR   A 17  ? 0.1655 0.1298 0.1816 -0.0256 -0.0185 0.0254  17  TYR   A CE2 
302  C CE2 B TYR   A 17  ? 0.1747 0.1665 0.2009 -0.0145 -0.0132 0.0211  17  TYR   A CE2 
303  C CZ  A TYR   A 17  ? 0.1656 0.1338 0.1888 -0.0218 -0.0207 0.0280  17  TYR   A CZ  
304  C CZ  B TYR   A 17  ? 0.1815 0.1638 0.2031 -0.0102 -0.0184 0.0278  17  TYR   A CZ  
305  O OH  A TYR   A 17  ? 0.1726 0.1398 0.1876 -0.0148 -0.0177 0.0303  17  TYR   A OH  
306  O OH  B TYR   A 17  ? 0.1926 0.1657 0.2093 -0.0048 -0.0197 0.0263  17  TYR   A OH  
325  N N   A ILE   A 18  ? 0.1340 0.1124 0.1331 -0.0186 0.0047  0.0218  18  ILE   A N   
326  N N   B ILE   A 18  ? 0.1185 0.1359 0.1649 -0.0131 0.0201  0.0335  18  ILE   A N   
327  C CA  A ILE   A 18  ? 0.1368 0.1104 0.1197 -0.0099 0.0065  0.0106  18  ILE   A CA  
328  C CA  B ILE   A 18  ? 0.1239 0.1270 0.1455 -0.0071 0.0200  0.0220  18  ILE   A CA  
329  C C   A ILE   A 18  ? 0.1414 0.1149 0.1299 -0.0100 0.0113  0.0105  18  ILE   A C   
330  C C   B ILE   A 18  ? 0.1194 0.1366 0.1414 -0.0174 0.0205  0.0233  18  ILE   A C   
331  O O   A ILE   A 18  ? 0.1398 0.1202 0.1288 -0.0124 0.0085  0.0148  18  ILE   A O   
332  O O   B ILE   A 18  ? 0.1186 0.1506 0.1454 -0.0233 0.0350  0.0265  18  ILE   A O   
333  C CB  A ILE   A 18  ? 0.1461 0.1171 0.1172 -0.0017 0.0151  0.0063  18  ILE   A CB  
334  C CB  B ILE   A 18  ? 0.1317 0.1253 0.1383 -0.0021 0.0336  0.0196  18  ILE   A CB  
335  C CG1 A ILE   A 18  ? 0.1506 0.1196 0.1006 0.0058  0.0165  0.0064  18  ILE   A CG1 
336  C CG1 B ILE   A 18  ? 0.1467 0.1388 0.1455 -0.0090 0.0281  0.0248  18  ILE   A CG1 
337  C CG2 A ILE   A 18  ? 0.1432 0.1141 0.1149 -0.0064 0.0101  -0.0042 18  ILE   A CG2 
338  C CG2 B ILE   A 18  ? 0.1334 0.1397 0.1513 -0.0077 0.0273  0.0283  18  ILE   A CG2 
339  C CD1 A ILE   A 18  ? 0.1629 0.1321 0.1134 0.0161  0.0259  0.0011  18  ILE   A CD1 
340  C CD1 B ILE   A 18  ? 0.1721 0.1542 0.1687 -0.0111 0.0107  0.0098  18  ILE   A CD1 
363  N N   A LYS   A 19  ? 0.1422 0.1139 0.1288 -0.0051 0.0202  0.0119  19  LYS   A N   
364  N N   B LYS   A 19  ? 0.1212 0.1353 0.1490 -0.0075 0.0389  0.0176  19  LYS   A N   
365  C CA  A LYS   A 19  ? 0.1529 0.1270 0.1503 -0.0099 0.0257  0.0116  19  LYS   A CA  
366  C CA  B LYS   A 19  ? 0.1364 0.1483 0.1676 -0.0013 0.0464  0.0123  19  LYS   A CA  
367  C C   A LYS   A 19  ? 0.1500 0.1226 0.1764 -0.0045 0.0319  0.0265  19  LYS   A C   
368  C C   B LYS   A 19  ? 0.1316 0.1451 0.1799 0.0040  0.0463  0.0257  19  LYS   A C   
369  O O   A LYS   A 19  ? 0.1426 0.1247 0.1777 -0.0013 0.0265  0.0345  19  LYS   A O   
370  O O   B LYS   A 19  ? 0.1262 0.1422 0.1752 0.0028  0.0410  0.0388  19  LYS   A O   
371  C CB  A LYS   A 19  ? 0.1731 0.1458 0.1636 -0.0171 0.0240  0.0120  19  LYS   A CB  
372  C CB  B LYS   A 19  ? 0.1496 0.1594 0.1690 -0.0051 0.0552  -0.0056 19  LYS   A CB  
373  C CG  A LYS   A 19  ? 0.1928 0.1579 0.1704 -0.0251 0.0328  0.0004  19  LYS   A CG  
374  C CG  B LYS   A 19  ? 0.1843 0.1784 0.1835 -0.0090 0.0550  -0.0057 19  LYS   A CG  
375  C CD  A LYS   A 19  ? 0.2056 0.1673 0.1821 -0.0312 0.0416  -0.0089 19  LYS   A CD  
376  C CD  B LYS   A 19  ? 0.2131 0.1949 0.2018 -0.0133 0.0628  -0.0087 19  LYS   A CD  
377  C CE  A LYS   A 19  ? 0.2164 0.1695 0.1848 -0.0344 0.0579  -0.0149 19  LYS   A CE  
378  C CE  B LYS   A 19  ? 0.2280 0.2107 0.2069 -0.0206 0.0649  -0.0109 19  LYS   A CE  
379  N NZ  A LYS   A 19  ? 0.2245 0.1700 0.1857 -0.0347 0.0678  -0.0211 19  LYS   A NZ  
380  N NZ  B LYS   A 19  ? 0.2367 0.2155 0.2175 -0.0292 0.0666  -0.0197 19  LYS   A NZ  
407  N N   A ASN   A 20  ? 0.1530 0.1258 0.1986 -0.0078 0.0407  0.0320  20  ASN   A N   
408  N N   B ASN   A 20  ? 0.1319 0.1466 0.2060 0.0009  0.0485  0.0211  20  ASN   A N   
409  C CA  A ASN   A 20  ? 0.1625 0.1301 0.2173 0.0010  0.0562  0.0384  20  ASN   A CA  
410  C CA  B ASN   A 20  ? 0.1358 0.1516 0.2242 0.0025  0.0481  0.0216  20  ASN   A CA  
411  C C   A ASN   A 20  ? 0.1696 0.1365 0.2206 -0.0029 0.0640  0.0371  20  ASN   A C   
412  C C   B ASN   A 20  ? 0.1490 0.1573 0.2264 0.0034  0.0641  0.0101  20  ASN   A C   
413  O O   A ASN   A 20  ? 0.1843 0.1325 0.2252 -0.0124 0.0736  0.0216  20  ASN   A O   
414  O O   B ASN   A 20  ? 0.1680 0.1621 0.2454 0.0001  0.0656  -0.0026 20  ASN   A O   
415  C CB  A ASN   A 20  ? 0.1714 0.1332 0.2204 0.0101  0.0663  0.0381  20  ASN   A CB  
416  C CB  B ASN   A 20  ? 0.1328 0.1599 0.2290 0.0060  0.0371  0.0222  20  ASN   A CB  
417  C CG  A ASN   A 20  ? 0.1843 0.1362 0.2475 0.0177  0.0670  0.0276  20  ASN   A CG  
418  C CG  B ASN   A 20  ? 0.1249 0.1604 0.2360 0.0151  0.0284  0.0147  20  ASN   A CG  
419  O OD1 A ASN   A 20  ? 0.2049 0.1553 0.2813 0.0156  0.0670  0.0153  20  ASN   A OD1 
420  O OD1 B ASN   A 20  ? 0.1209 0.1495 0.2326 0.0146  0.0330  0.0056  20  ASN   A OD1 
421  N ND2 A ASN   A 20  ? 0.1802 0.1178 0.2434 0.0253  0.0626  0.0276  20  ASN   A ND2 
422  N ND2 B ASN   A 20  ? 0.1331 0.1683 0.2636 0.0183  0.0212  0.0278  20  ASN   A ND2 
435  N N   A ALA   A 21  ? 0.1672 0.1413 0.2128 0.0012  0.0490  0.0434  21  ALA   A N   
436  N N   B ALA   A 21  ? 0.1566 0.1613 0.2246 0.0059  0.0517  0.0067  21  ALA   A N   
437  C CA  A ALA   A 21  ? 0.1650 0.1441 0.2110 -0.0001 0.0452  0.0399  21  ALA   A CA  
438  C CA  B ALA   A 21  ? 0.1657 0.1639 0.2248 0.0005  0.0489  0.0026  21  ALA   A CA  
439  C C   A ALA   A 21  ? 0.1509 0.1455 0.2158 -0.0027 0.0303  0.0338  21  ALA   A C   
440  C C   B ALA   A 21  ? 0.1538 0.1526 0.2098 0.0031  0.0610  0.0005  21  ALA   A C   
441  O O   A ALA   A 21  ? 0.1441 0.1553 0.2235 -0.0015 0.0205  0.0318  21  ALA   A O   
442  O O   B ALA   A 21  ? 0.1528 0.1542 0.2108 0.0055  0.0622  0.0020  21  ALA   A O   
443  C CB  A ALA   A 21  ? 0.1754 0.1492 0.2001 -0.0040 0.0540  0.0445  21  ALA   A CB  
444  C CB  B ALA   A 21  ? 0.1853 0.1730 0.2462 -0.0047 0.0376  0.0023  21  ALA   A CB  
455  N N   A ASP   A 22  ? 0.1522 0.1461 0.2299 -0.0059 0.0249  0.0303  22  ASP   A N   
456  N N   B ASP   A 22  ? 0.1569 0.1477 0.2151 -0.0045 0.0580  0.0112  22  ASP   A N   
457  C CA  A ASP   A 22  ? 0.1536 0.1476 0.2321 -0.0027 0.0204  0.0373  22  ASP   A CA  
458  C CA  B ASP   A 22  ? 0.1593 0.1478 0.2126 -0.0036 0.0550  0.0210  22  ASP   A CA  
459  C C   A ASP   A 22  ? 0.1494 0.1497 0.2118 0.0064  0.0248  0.0413  22  ASP   A C   
460  C C   B ASP   A 22  ? 0.1522 0.1439 0.1711 -0.0126 0.0510  0.0188  22  ASP   A C   
461  O O   A ASP   A 22  ? 0.1554 0.1489 0.2142 0.0092  0.0321  0.0452  22  ASP   A O   
462  O O   B ASP   A 22  ? 0.1522 0.1525 0.1699 -0.0170 0.0495  0.0076  22  ASP   A O   
463  C CB  A ASP   A 22  ? 0.1612 0.1471 0.2559 -0.0100 0.0120  0.0277  22  ASP   A CB  
464  C CB  B ASP   A 22  ? 0.1756 0.1518 0.2389 0.0092  0.0644  0.0083  22  ASP   A CB  
465  C CG  A ASP   A 22  ? 0.1710 0.1491 0.2801 -0.0106 -0.0023 0.0286  22  ASP   A CG  
466  C CG  B ASP   A 22  ? 0.1865 0.1552 0.2536 0.0116  0.0694  0.0137  22  ASP   A CG  
467  O OD1 A ASP   A 22  ? 0.1719 0.1454 0.2881 -0.0178 -0.0109 0.0271  22  ASP   A OD1 
468  O OD1 B ASP   A 22  ? 0.1879 0.1580 0.2228 0.0079  0.0639  0.0193  22  ASP   A OD1 
469  O OD2 A ASP   A 22  ? 0.1841 0.1588 0.3011 0.0016  -0.0006 0.0259  22  ASP   A OD2 
470  O OD2 B ASP   A 22  ? 0.1953 0.1668 0.2923 0.0064  0.0706  0.0185  22  ASP   A OD2 
479  N N   A ILE   A 23  ? 0.1479 0.1567 0.1928 0.0022  0.0241  0.0342  23  ILE   A N   
480  N N   B ILE   A 23  ? 0.1466 0.1399 0.1504 -0.0096 0.0421  0.0221  23  ILE   A N   
481  C CA  A ILE   A 23  ? 0.1545 0.1510 0.1692 0.0025  0.0329  0.0287  23  ILE   A CA  
482  C CA  B ILE   A 23  ? 0.1465 0.1463 0.1385 -0.0093 0.0305  0.0241  23  ILE   A CA  
483  C C   A ILE   A 23  ? 0.1585 0.1461 0.1621 0.0032  0.0451  0.0319  23  ILE   A C   
484  C C   B ILE   A 23  ? 0.1443 0.1567 0.1507 -0.0150 0.0370  0.0076  23  ILE   A C   
485  O O   A ILE   A 23  ? 0.1684 0.1520 0.1610 0.0034  0.0456  0.0197  23  ILE   A O   
486  O O   B ILE   A 23  ? 0.1505 0.1583 0.1520 -0.0132 0.0244  0.0045  23  ILE   A O   
487  C CB  A ILE   A 23  ? 0.1597 0.1488 0.1572 0.0015  0.0258  0.0183  23  ILE   A CB  
488  C CB  B ILE   A 23  ? 0.1412 0.1419 0.1212 -0.0017 0.0238  0.0266  23  ILE   A CB  
489  C CG1 A ILE   A 23  ? 0.1580 0.1428 0.1354 0.0019  0.0201  0.0078  23  ILE   A CG1 
490  C CG1 B ILE   A 23  ? 0.1517 0.1433 0.1269 0.0020  0.0157  0.0223  23  ILE   A CG1 
491  C CG2 A ILE   A 23  ? 0.1598 0.1524 0.1671 -0.0001 0.0264  0.0244  23  ILE   A CG2 
492  C CG2 B ILE   A 23  ? 0.1386 0.1397 0.1277 0.0036  0.0187  0.0248  23  ILE   A CG2 
493  C CD1 A ILE   A 23  ? 0.1535 0.1414 0.1318 0.0012  0.0141  0.0038  23  ILE   A CD1 
494  C CD1 B ILE   A 23  ? 0.1552 0.1383 0.1411 0.0041  0.0103  0.0140  23  ILE   A CD1 
517  N N   A VAL   A 24  ? 0.1614 0.1446 0.1617 0.0024  0.0437  0.0313  24  VAL   A N   
518  N N   B VAL   A 24  ? 0.1505 0.1637 0.1731 -0.0241 0.0353  -0.0058 24  VAL   A N   
519  C CA  A VAL   A 24  ? 0.1762 0.1557 0.1787 -0.0040 0.0395  0.0187  24  VAL   A CA  
520  C CA  B VAL   A 24  ? 0.1640 0.1725 0.1981 -0.0305 0.0289  -0.0143 24  VAL   A CA  
521  C C   A VAL   A 24  ? 0.1903 0.1690 0.1882 -0.0080 0.0379  0.0175  24  VAL   A C   
522  C C   B VAL   A 24  ? 0.1708 0.1863 0.2019 -0.0331 0.0349  -0.0348 24  VAL   A C   
523  O O   A VAL   A 24  ? 0.2033 0.1796 0.1880 -0.0082 0.0420  0.0224  24  VAL   A O   
524  O O   B VAL   A 24  ? 0.1826 0.1962 0.2007 -0.0229 0.0365  -0.0307 24  VAL   A O   
525  C CB  A VAL   A 24  ? 0.1769 0.1577 0.1943 -0.0035 0.0398  0.0125  24  VAL   A CB  
526  C CB  B VAL   A 24  ? 0.1705 0.1751 0.2375 -0.0294 0.0250  0.0044  24  VAL   A CB  
527  C CG1 A VAL   A 24  ? 0.1764 0.1628 0.2051 0.0020  0.0376  0.0024  24  VAL   A CG1 
528  C CG1 B VAL   A 24  ? 0.1852 0.1774 0.2606 -0.0298 0.0094  0.0044  24  VAL   A CG1 
529  C CG2 A VAL   A 24  ? 0.1814 0.1608 0.1978 -0.0016 0.0502  0.0186  24  VAL   A CG2 
530  C CG2 B VAL   A 24  ? 0.1826 0.1828 0.2465 -0.0223 0.0351  0.0219  24  VAL   A CG2 
549  N N   A GLU   A 25  ? 0.1959 0.1766 0.1934 -0.0072 0.0426  0.0062  25  GLU   A N   
550  N N   B GLU   A 25  ? 0.1790 0.1963 0.2066 -0.0328 0.0639  -0.0490 25  GLU   A N   
551  C CA  A GLU   A 25  ? 0.2078 0.1890 0.1964 -0.0005 0.0425  0.0010  25  GLU   A CA  
552  C CA  B GLU   A 25  ? 0.2054 0.2133 0.2148 -0.0404 0.0809  -0.0507 25  GLU   A CA  
553  C C   A GLU   A 25  ? 0.1955 0.1886 0.1743 -0.0025 0.0553  0.0027  25  GLU   A C   
554  C C   B GLU   A 25  ? 0.2042 0.2175 0.1877 -0.0458 0.0843  -0.0395 25  GLU   A C   
555  O O   A GLU   A 25  ? 0.1953 0.1890 0.1873 0.0034  0.0540  0.0010  25  GLU   A O   
556  O O   B GLU   A 25  ? 0.2124 0.2198 0.1932 -0.0427 0.0824  -0.0475 25  GLU   A O   
557  C CB  A GLU   A 25  ? 0.2295 0.2077 0.2326 -0.0018 0.0360  0.0044  25  GLU   A CB  
558  C CB  B GLU   A 25  ? 0.2303 0.2217 0.2429 -0.0391 0.0942  -0.0504 25  GLU   A CB  
559  C CG  A GLU   A 25  ? 0.2510 0.2245 0.2832 -0.0118 0.0259  0.0057  25  GLU   A CG  
560  C CG  B GLU   A 25  ? 0.2598 0.2361 0.2936 -0.0377 0.0836  -0.0438 25  GLU   A CG  
561  C CD  A GLU   A 25  ? 0.2670 0.2367 0.3217 -0.0210 0.0226  0.0084  25  GLU   A CD  
562  C CD  B GLU   A 25  ? 0.2818 0.2510 0.3371 -0.0374 0.0778  -0.0373 25  GLU   A CD  
563  O OE1 A GLU   A 25  ? 0.2692 0.2402 0.3295 -0.0233 0.0220  0.0013  25  GLU   A OE1 
564  O OE1 B GLU   A 25  ? 0.2878 0.2570 0.3506 -0.0356 0.0813  -0.0388 25  GLU   A OE1 
565  O OE2 A GLU   A 25  ? 0.2779 0.2454 0.3468 -0.0245 0.0197  0.0073  25  GLU   A OE2 
566  O OE2 B GLU   A 25  ? 0.2934 0.2544 0.3619 -0.0352 0.0771  -0.0318 25  GLU   A OE2 
579  N N   A GLU   A 26  ? 0.1899 0.1921 0.1690 -0.0132 0.0610  0.0050  26  GLU   A N   
580  N N   B GLU   A 26  ? 0.2002 0.2139 0.1827 -0.0538 0.0814  -0.0391 26  GLU   A N   
581  C CA  A GLU   A 26  ? 0.1891 0.2015 0.1648 -0.0228 0.0606  0.0030  26  GLU   A CA  
582  C CA  B GLU   A 26  ? 0.2052 0.2161 0.1824 -0.0581 0.0773  -0.0274 26  GLU   A CA  
583  C C   A GLU   A 26  ? 0.1836 0.2007 0.1533 -0.0194 0.0606  0.0035  26  GLU   A C   
584  C C   B GLU   A 26  ? 0.2030 0.2128 0.1611 -0.0569 0.0631  -0.0285 26  GLU   A C   
585  O O   A GLU   A 26  ? 0.1879 0.1999 0.1566 -0.0191 0.0644  0.0040  26  GLU   A O   
586  O O   B GLU   A 26  ? 0.2121 0.2175 0.1653 -0.0519 0.0559  -0.0241 26  GLU   A O   
587  C CB  A GLU   A 26  ? 0.1974 0.2120 0.1838 -0.0278 0.0568  0.0024  26  GLU   A CB  
588  C CB  B GLU   A 26  ? 0.2194 0.2224 0.2093 -0.0647 0.0747  -0.0210 26  GLU   A CB  
589  C CG  A GLU   A 26  ? 0.2124 0.2275 0.2320 -0.0241 0.0500  -0.0009 26  GLU   A CG  
590  C CG  B GLU   A 26  ? 0.2355 0.2314 0.2368 -0.0730 0.0847  -0.0265 26  GLU   A CG  
591  C CD  A GLU   A 26  ? 0.2222 0.2430 0.2740 -0.0235 0.0495  0.0048  26  GLU   A CD  
592  C CD  B GLU   A 26  ? 0.2508 0.2325 0.2427 -0.0875 0.1065  -0.0357 26  GLU   A CD  
593  O OE1 A GLU   A 26  ? 0.2285 0.2548 0.2778 -0.0207 0.0582  0.0093  26  GLU   A OE1 
594  O OE1 B GLU   A 26  ? 0.2574 0.2475 0.2395 -0.0834 0.1204  -0.0493 26  GLU   A OE1 
595  O OE2 A GLU   A 26  ? 0.2314 0.2511 0.3008 -0.0194 0.0391  0.0051  26  GLU   A OE2 
596  O OE2 B GLU   A 26  ? 0.2652 0.2380 0.2379 -0.0889 0.1219  -0.0311 26  GLU   A OE2 
609  N N   A ALA   A 27  ? 0.1792 0.2013 0.1538 -0.0176 0.0540  0.0048  27  ALA   A N   
610  N N   B ALA   A 27  ? 0.1924 0.2077 0.1540 -0.0576 0.0550  -0.0381 27  ALA   A N   
611  C CA  A ALA   A 27  ? 0.1898 0.2158 0.1500 -0.0200 0.0408  0.0133  27  ALA   A CA  
612  C CA  B ALA   A 27  ? 0.1975 0.2178 0.1529 -0.0525 0.0480  -0.0323 27  ALA   A CA  
613  C C   A ALA   A 27  ? 0.2167 0.2341 0.1616 -0.0282 0.0389  -0.0028 27  ALA   A C   
614  C C   B ALA   A 27  ? 0.2191 0.2301 0.1604 -0.0534 0.0492  -0.0449 27  ALA   A C   
615  O O   A ALA   A 27  ? 0.2243 0.2337 0.1533 -0.0334 0.0364  0.0058  27  ALA   A O   
616  O O   B ALA   A 27  ? 0.2287 0.2322 0.1592 -0.0535 0.0419  -0.0311 27  ALA   A O   
617  C CB  A ALA   A 27  ? 0.1801 0.2142 0.1457 -0.0190 0.0313  0.0201  27  ALA   A CB  
618  C CB  B ALA   A 27  ? 0.1870 0.2143 0.1563 -0.0525 0.0347  -0.0223 27  ALA   A CB  
629  N N   A LYS   A 28  ? 0.2426 0.2552 0.1748 -0.0308 0.0312  -0.0252 28  LYS   A N   
630  N N   B LYS   A 28  ? 0.2419 0.2451 0.1618 -0.0526 0.0441  -0.0705 28  LYS   A N   
631  C CA  A LYS   A 28  ? 0.2724 0.2807 0.2009 -0.0313 0.0254  -0.0422 28  LYS   A CA  
632  C CA  B LYS   A 28  ? 0.2706 0.2733 0.1847 -0.0455 0.0461  -0.0781 28  LYS   A CA  
633  C C   A LYS   A 28  ? 0.2929 0.3051 0.2091 -0.0391 0.0310  -0.0431 28  LYS   A C   
634  C C   B LYS   A 28  ? 0.2922 0.3030 0.1798 -0.0482 0.0541  -0.0698 28  LYS   A C   
635  O O   A LYS   A 28  ? 0.2965 0.3099 0.2263 -0.0381 0.0172  -0.0446 28  LYS   A O   
636  O O   B LYS   A 28  ? 0.2997 0.3125 0.2147 -0.0442 0.0295  -0.0599 28  LYS   A O   
637  C CB  A LYS   A 28  ? 0.2822 0.2842 0.2208 -0.0238 0.0183  -0.0494 28  LYS   A CB  
638  C CB  B LYS   A 28  ? 0.2812 0.2783 0.2176 -0.0347 0.0466  -0.0811 28  LYS   A CB  
639  C CG  A LYS   A 28  ? 0.2900 0.2865 0.2503 -0.0173 0.0151  -0.0504 28  LYS   A CG  
640  C CG  B LYS   A 28  ? 0.2925 0.2855 0.2661 -0.0264 0.0384  -0.0823 28  LYS   A CG  
641  C CD  A LYS   A 28  ? 0.2964 0.2924 0.2843 -0.0127 0.0107  -0.0469 28  LYS   A CD  
642  C CD  B LYS   A 28  ? 0.3024 0.2967 0.3150 -0.0217 0.0317  -0.0804 28  LYS   A CD  
643  C CE  A LYS   A 28  ? 0.3000 0.2971 0.3161 -0.0108 0.0103  -0.0386 28  LYS   A CE  
644  C CE  B LYS   A 28  ? 0.3080 0.3058 0.3561 -0.0203 0.0258  -0.0793 28  LYS   A CE  
645  N NZ  A LYS   A 28  ? 0.3026 0.3003 0.3342 -0.0077 0.0111  -0.0332 28  LYS   A NZ  
646  N NZ  B LYS   A 28  ? 0.3130 0.3131 0.3832 -0.0167 0.0252  -0.0737 28  LYS   A NZ  
673  N N   A LYS   A 29  ? 0.3091 0.3251 0.2121 -0.0500 0.0542  -0.0346 29  LYS   A N   
674  N N   B LYS   A 29  ? 0.3049 0.3259 0.1597 -0.0578 0.0918  -0.0551 29  LYS   A N   
675  C CA  A LYS   A 29  ? 0.3279 0.3451 0.2242 -0.0596 0.0690  -0.0241 29  LYS   A CA  
676  C CA  B LYS   A 29  ? 0.3259 0.3491 0.1800 -0.0668 0.1014  -0.0354 29  LYS   A CA  
677  C C   A LYS   A 29  ? 0.3317 0.3439 0.1911 -0.0711 0.0745  -0.0212 29  LYS   A C   
678  C C   B LYS   A 29  ? 0.3324 0.3475 0.1632 -0.0741 0.0893  -0.0285 29  LYS   A C   
679  O O   A LYS   A 29  ? 0.3389 0.3499 0.2008 -0.0685 0.0721  -0.0225 29  LYS   A O   
680  O O   B LYS   A 29  ? 0.3419 0.3565 0.1686 -0.0700 0.0892  -0.0285 29  LYS   A O   
681  C CB  A LYS   A 29  ? 0.3419 0.3648 0.2844 -0.0550 0.0735  -0.0158 29  LYS   A CB  
682  C CB  B LYS   A 29  ? 0.3412 0.3722 0.2479 -0.0619 0.1103  -0.0246 29  LYS   A CB  
683  C CG  A LYS   A 29  ? 0.3553 0.3800 0.3415 -0.0494 0.0742  -0.0127 29  LYS   A CG  
684  C CG  B LYS   A 29  ? 0.3580 0.3907 0.3203 -0.0545 0.1085  -0.0215 29  LYS   A CG  
685  C CD  A LYS   A 29  ? 0.3659 0.3910 0.3919 -0.0444 0.0729  -0.0129 29  LYS   A CD  
686  C CD  B LYS   A 29  ? 0.3717 0.4037 0.3836 -0.0481 0.1034  -0.0218 29  LYS   A CD  
687  C CE  A LYS   A 29  ? 0.3728 0.3977 0.4266 -0.0408 0.0735  -0.0117 29  LYS   A CE  
688  C CE  B LYS   A 29  ? 0.3798 0.4114 0.4267 -0.0444 0.1032  -0.0203 29  LYS   A CE  
689  N NZ  A LYS   A 29  ? 0.3755 0.4008 0.4442 -0.0382 0.0726  -0.0098 29  LYS   A NZ  
690  N NZ  B LYS   A 29  ? 0.3833 0.4149 0.4491 -0.0423 0.1011  -0.0173 29  LYS   A NZ  
717  N N   . VAL   A 30  ? 0.3277 0.3368 0.1589 -0.0832 0.0853  -0.0172 30  VAL   A N   
718  C CA  . VAL   A 30  ? 0.3270 0.3243 0.1538 -0.1008 0.0621  0.0018  30  VAL   A CA  
719  C C   . VAL   A 30  ? 0.3309 0.3120 0.1400 -0.1015 0.0448  0.0151  30  VAL   A C   
720  O O   . VAL   A 30  ? 0.3375 0.3188 0.1465 -0.1010 0.0383  0.0223  30  VAL   A O   
721  C CB  . VAL   A 30  ? 0.3293 0.3237 0.1987 -0.1074 0.0429  -0.0019 30  VAL   A CB  
722  C CG1 . VAL   A 30  ? 0.3343 0.3220 0.2197 -0.1100 0.0355  0.0022  30  VAL   A CG1 
723  C CG2 . VAL   A 30  ? 0.3298 0.3260 0.2220 -0.1090 0.0387  -0.0060 30  VAL   A CG2 
734  N N   . LYS   A 31  ? 0.3264 0.2946 0.1140 -0.1012 0.0337  0.0063  31  LYS   A N   
735  C CA  . LYS   A 31  ? 0.3387 0.2958 0.1279 -0.0897 0.0081  0.0092  31  LYS   A CA  
736  C C   . LYS   A 31  ? 0.3138 0.2715 0.1060 -0.0718 -0.0023 0.0404  31  LYS   A C   
737  O O   . LYS   A 31  ? 0.3231 0.2889 0.1174 -0.0618 -0.0195 0.0543  31  LYS   A O   
738  C CB  . LYS   A 31  ? 0.3797 0.3258 0.2253 -0.0806 -0.0132 -0.0070 31  LYS   A CB  
739  C CG  . LYS   A 31  ? 0.4213 0.3599 0.3538 -0.0691 -0.0331 -0.0106 31  LYS   A CG  
740  C CD  . LYS   A 31  ? 0.4539 0.3815 0.4606 -0.0612 -0.0498 -0.0186 31  LYS   A CD  
741  C CE  . LYS   A 31  ? 0.4821 0.3921 0.5282 -0.0534 -0.0633 -0.0243 31  LYS   A CE  
742  N NZ  . LYS   A 31  ? 0.4940 0.3977 0.5593 -0.0492 -0.0710 -0.0274 31  LYS   A NZ  
756  N N   . PRO   A 32  ? 0.2745 0.2392 0.0950 -0.0665 -0.0003 0.0298  32  PRO   A N   
757  C CA  . PRO   A 32  ? 0.2656 0.2216 0.1246 -0.0638 -0.0075 0.0380  32  PRO   A CA  
758  C C   . PRO   A 32  ? 0.2594 0.2176 0.1379 -0.0554 -0.0180 0.0428  32  PRO   A C   
759  O O   . PRO   A 32  ? 0.2500 0.2114 0.1461 -0.0495 -0.0341 0.0416  32  PRO   A O   
760  C CB  . PRO   A 32  ? 0.2518 0.2230 0.1367 -0.0651 -0.0069 0.0255  32  PRO   A CB  
761  C CG  . PRO   A 32  ? 0.2433 0.2239 0.0953 -0.0595 -0.0160 0.0201  32  PRO   A CG  
762  C CD  . PRO   A 32  ? 0.2520 0.2269 0.0919 -0.0653 -0.0120 0.0290  32  PRO   A CD  
770  N N   . THR   A 33  ? 0.2651 0.2165 0.1330 -0.0535 -0.0109 0.0474  33  THR   A N   
771  C CA  . THR   A 33  ? 0.2577 0.2157 0.1485 -0.0462 -0.0260 0.0486  33  THR   A CA  
772  C C   . THR   A 33  ? 0.2284 0.1947 0.1280 -0.0439 -0.0252 0.0394  33  THR   A C   
773  O O   . THR   A 33  ? 0.2308 0.2046 0.1250 -0.0415 -0.0369 0.0384  33  THR   A O   
774  C CB  . THR   A 33  ? 0.2783 0.2358 0.1626 -0.0349 -0.0351 0.0729  33  THR   A CB  
775  O OG1 . THR   A 33  ? 0.2974 0.2498 0.1939 -0.0263 -0.0290 0.0805  33  THR   A OG1 
776  C CG2 . THR   A 33  ? 0.2794 0.2463 0.1872 -0.0283 -0.0428 0.0706  33  THR   A CG2 
784  N N   . VAL   A 34  ? 0.2009 0.1858 0.1234 -0.0369 -0.0184 0.0311  34  VAL   A N   
785  C CA  . VAL   A 34  ? 0.1756 0.1639 0.1117 -0.0304 -0.0077 0.0333  34  VAL   A CA  
786  C C   . VAL   A 34  ? 0.1637 0.1616 0.1025 -0.0283 -0.0002 0.0271  34  VAL   A C   
787  O O   . VAL   A 34  ? 0.1683 0.1632 0.1233 -0.0369 -0.0002 0.0299  34  VAL   A O   
788  C CB  . VAL   A 34  ? 0.1850 0.1634 0.1267 -0.0263 -0.0066 0.0260  34  VAL   A CB  
789  C CG1 . VAL   A 34  ? 0.1922 0.1635 0.1366 -0.0268 0.0034  0.0186  34  VAL   A CG1 
790  C CG2 . VAL   A 34  ? 0.1935 0.1741 0.1560 -0.0188 -0.0196 0.0241  34  VAL   A CG2 
800  N N   . VAL   A 35  ? 0.1538 0.1512 0.1008 -0.0281 -0.0016 0.0195  35  VAL   A N   
801  C CA  . VAL   A 35  ? 0.1457 0.1490 0.1004 -0.0249 0.0036  0.0121  35  VAL   A CA  
802  C C   . VAL   A 35  ? 0.1325 0.1335 0.0992 -0.0171 0.0095  0.0102  35  VAL   A C   
803  O O   . VAL   A 35  ? 0.1292 0.1476 0.1083 -0.0229 0.0152  0.0069  35  VAL   A O   
804  C CB  . VAL   A 35  ? 0.1486 0.1535 0.1184 -0.0142 0.0206  0.0053  35  VAL   A CB  
805  C CG1 . VAL   A 35  ? 0.1569 0.1545 0.1340 -0.0116 0.0090  -0.0019 35  VAL   A CG1 
806  C CG2 . VAL   A 35  ? 0.1466 0.1560 0.1394 -0.0104 0.0231  0.0012  35  VAL   A CG2 
816  N N   . VAL   A 36  ? 0.1221 0.1299 0.0950 -0.0190 0.0097  0.0159  36  VAL   A N   
817  C CA  . VAL   A 36  ? 0.1169 0.1167 0.1032 -0.0157 0.0063  0.0089  36  VAL   A CA  
818  C C   . VAL   A 36  ? 0.1081 0.1174 0.1106 -0.0091 0.0087  0.0054  36  VAL   A C   
819  O O   . VAL   A 36  ? 0.1193 0.1211 0.1189 -0.0088 0.0169  0.0067  36  VAL   A O   
820  C CB  . VAL   A 36  ? 0.1139 0.1144 0.1106 -0.0110 0.0059  0.0082  36  VAL   A CB  
821  C CG1 . VAL   A 36  ? 0.1211 0.1152 0.1183 -0.0141 0.0062  0.0004  36  VAL   A CG1 
822  C CG2 . VAL   A 36  ? 0.1242 0.1112 0.1255 -0.0108 -0.0024 0.0119  36  VAL   A CG2 
832  N N   A ASN   A 37  ? 0.1129 0.1132 0.1009 -0.0091 0.0138  0.0138  37  ASN   A N   
833  N N   B ASN   A 37  ? 0.1047 0.1107 0.1057 -0.0039 0.0053  0.0054  37  ASN   A N   
834  C CA  A ASN   A 37  ? 0.1153 0.1090 0.0997 -0.0087 0.0176  0.0116  37  ASN   A CA  
835  C CA  B ASN   A 37  ? 0.1087 0.1075 0.0982 0.0046  0.0142  0.0099  37  ASN   A CA  
836  C C   A ASN   A 37  ? 0.1149 0.1093 0.1131 -0.0100 0.0198  0.0191  37  ASN   A C   
837  C C   B ASN   A 37  ? 0.1043 0.1070 0.0976 0.0067  0.0115  0.0195  37  ASN   A C   
838  O O   A ASN   A 37  ? 0.1229 0.1137 0.1156 -0.0051 0.0075  0.0165  37  ASN   A O   
839  O O   B ASN   A 37  ? 0.1082 0.1153 0.1023 0.0134  0.0045  -0.0001 37  ASN   A O   
840  C CB  A ASN   A 37  ? 0.1146 0.1086 0.1031 -0.0098 0.0099  0.0004  37  ASN   A CB  
841  C CB  B ASN   A 37  ? 0.1103 0.1088 0.1100 0.0054  0.0097  0.0062  37  ASN   A CB  
842  C CG  A ASN   A 37  ? 0.1122 0.1061 0.1019 -0.0055 0.0090  -0.0035 37  ASN   A CG  
843  C CG  B ASN   A 37  ? 0.1114 0.1073 0.1208 0.0079  0.0078  0.0157  37  ASN   A CG  
844  O OD1 A ASN   A 37  ? 0.1121 0.1060 0.1181 -0.0040 0.0080  -0.0072 37  ASN   A OD1 
845  O OD1 B ASN   A 37  ? 0.1087 0.1096 0.1470 0.0017  0.0089  0.0238  37  ASN   A OD1 
846  N ND2 A ASN   A 37  ? 0.1073 0.1065 0.1085 -0.0093 0.0074  0.0097  37  ASN   A ND2 
847  N ND2 B ASN   A 37  ? 0.1108 0.1102 0.1284 0.0039  0.0007  0.0242  37  ASN   A ND2 
860  N N   A ALA   A 38  ? 0.1109 0.1096 0.1165 -0.0092 0.0198  0.0105  38  ALA   A N   
861  N N   B ALA   A 38  ? 0.1127 0.1048 0.1075 0.0089  0.0064  0.0120  38  ALA   A N   
862  C CA  A ALA   A 38  ? 0.1086 0.1036 0.1114 -0.0091 0.0074  -0.0052 38  ALA   A CA  
863  C CA  B ALA   A 38  ? 0.1193 0.1065 0.1098 0.0029  0.0006  0.0173  38  ALA   A CA  
864  C C   A ALA   A 38  ? 0.1077 0.1078 0.0979 -0.0075 -0.0025 -0.0031 38  ALA   A C   
865  C C   B ALA   A 38  ? 0.1130 0.1140 0.1160 0.0047  -0.0091 0.0085  38  ALA   A C   
866  O O   A ALA   A 38  ? 0.1098 0.1067 0.1071 -0.0095 -0.0029 0.0012  38  ALA   A O   
867  O O   B ALA   A 38  ? 0.1128 0.1121 0.1358 0.0034  -0.0087 0.0089  38  ALA   A O   
868  C CB  A ALA   A 38  ? 0.1040 0.1118 0.1233 -0.0154 0.0096  -0.0157 38  ALA   A CB  
869  C CB  B ALA   A 38  ? 0.1246 0.1109 0.1358 -0.0057 -0.0082 0.0077  38  ALA   A CB  
880  N N   A ALA   A 39  ? 0.1055 0.1023 0.0943 -0.0009 0.0037  -0.0039 39  ALA   A N   
881  N N   B ALA   A 39  ? 0.1109 0.1223 0.1243 0.0040  0.0005  0.0155  39  ALA   A N   
882  C CA  A ALA   A 39  ? 0.1081 0.0989 0.0934 -0.0016 0.0090  -0.0091 39  ALA   A CA  
883  C CA  B ALA   A 39  ? 0.1171 0.1241 0.1284 -0.0013 0.0102  0.0139  39  ALA   A CA  
884  C C   A ALA   A 39  ? 0.1121 0.1048 0.1070 -0.0044 0.0077  -0.0006 39  ALA   A C   
885  C C   B ALA   A 39  ? 0.1116 0.1142 0.1291 -0.0026 0.0052  0.0077  39  ALA   A C   
886  O O   A ALA   A 39  ? 0.1221 0.1081 0.1025 -0.0083 0.0093  0.0055  39  ALA   A O   
887  O O   B ALA   A 39  ? 0.1234 0.1191 0.1373 -0.0056 0.0105  0.0062  39  ALA   A O   
888  C CB  A ALA   A 39  ? 0.1052 0.1044 0.0937 -0.0025 -0.0064 -0.0071 39  ALA   A CB  
889  C CB  B ALA   A 39  ? 0.1279 0.1445 0.1386 -0.0065 0.0014  0.0162  39  ALA   A CB  
900  N N   . ASN   A 40  ? 0.1193 0.1159 0.1168 -0.0093 0.0186  -0.0019 40  ASN   A N   
901  C CA  . ASN   A 40  ? 0.1244 0.1145 0.1144 -0.0060 0.0089  0.0000  40  ASN   A CA  
902  C C   . ASN   A 40  ? 0.1270 0.1062 0.1178 -0.0049 0.0229  0.0107  40  ASN   A C   
903  O O   . ASN   A 40  ? 0.1238 0.1138 0.1144 -0.0072 0.0225  0.0160  40  ASN   A O   
904  C CB  . ASN   A 40  ? 0.1337 0.1206 0.1323 -0.0007 -0.0014 0.0033  40  ASN   A CB  
905  C CG  . ASN   A 40  ? 0.1376 0.1214 0.1533 -0.0005 -0.0045 0.0055  40  ASN   A CG  
906  O OD1 . ASN   A 40  ? 0.1455 0.1247 0.1782 -0.0013 -0.0071 0.0024  40  ASN   A OD1 
907  N ND2 . ASN   A 40  ? 0.1421 0.1269 0.1746 0.0037  0.0048  -0.0080 40  ASN   A ND2 
915  N N   . VAL   A 41  ? 0.1324 0.1119 0.1211 -0.0057 0.0244  0.0082  41  VAL   A N   
916  C CA  . VAL   A 41  ? 0.1383 0.1154 0.1413 -0.0042 0.0305  0.0069  41  VAL   A CA  
917  C C   . VAL   A 41  ? 0.1318 0.1168 0.1410 -0.0028 0.0332  0.0104  41  VAL   A C   
918  O O   . VAL   A 41  ? 0.1353 0.1126 0.1505 -0.0012 0.0282  0.0017  41  VAL   A O   
919  C CB  . VAL   A 41  ? 0.1503 0.1309 0.1403 -0.0147 0.0424  0.0037  41  VAL   A CB  
920  C CG1 . VAL   A 41  ? 0.1592 0.1359 0.1467 -0.0115 0.0391  -0.0055 41  VAL   A CG1 
921  C CG2 . VAL   A 41  ? 0.1735 0.1427 0.1423 -0.0205 0.0426  0.0110  41  VAL   A CG2 
931  N N   A TYR   A 42  ? 0.1264 0.1134 0.1487 -0.0030 0.0290  0.0154  42  TYR   A N   
932  N N   B TYR   A 42  ? 0.1246 0.1104 0.1550 -0.0087 0.0319  0.0156  42  TYR   A N   
933  C CA  A TYR   A 42  ? 0.1263 0.1124 0.1481 -0.0012 0.0243  0.0183  42  TYR   A CA  
934  C CA  B TYR   A 42  ? 0.1234 0.1110 0.1546 -0.0097 0.0309  0.0158  42  TYR   A CA  
935  C C   A TYR   A 42  ? 0.1187 0.1123 0.1585 -0.0037 0.0179  0.0137  42  TYR   A C   
936  C C   B TYR   A 42  ? 0.1158 0.1115 0.1652 -0.0095 0.0231  0.0113  42  TYR   A C   
937  O O   A TYR   A 42  ? 0.1210 0.1139 0.1700 -0.0100 0.0129  0.0104  42  TYR   A O   
938  O O   B TYR   A 42  ? 0.1184 0.1116 0.1787 -0.0187 0.0221  0.0011  42  TYR   A O   
939  C CB  A TYR   A 42  ? 0.1396 0.1184 0.1517 0.0005  0.0174  0.0285  42  TYR   A CB  
940  C CB  B TYR   A 42  ? 0.1345 0.1225 0.1586 -0.0098 0.0275  0.0196  42  TYR   A CB  
941  C CG  A TYR   A 42  ? 0.1521 0.1257 0.1591 0.0069  0.0116  0.0322  42  TYR   A CG  
942  C CG  B TYR   A 42  ? 0.1440 0.1357 0.1658 -0.0049 0.0225  0.0196  42  TYR   A CG  
943  C CD1 A TYR   A 42  ? 0.1499 0.1306 0.1511 0.0037  0.0134  0.0412  42  TYR   A CD1 
944  C CD1 B TYR   A 42  ? 0.1499 0.1504 0.1543 -0.0056 0.0193  0.0134  42  TYR   A CD1 
945  C CD2 A TYR   A 42  ? 0.1637 0.1423 0.1709 0.0093  0.0114  0.0282  42  TYR   A CD2 
946  C CD2 B TYR   A 42  ? 0.1483 0.1513 0.1738 -0.0012 0.0160  0.0195  42  TYR   A CD2 
947  C CE1 A TYR   A 42  ? 0.1503 0.1408 0.1510 -0.0004 0.0159  0.0422  42  TYR   A CE1 
948  C CE1 B TYR   A 42  ? 0.1507 0.1590 0.1455 -0.0070 0.0270  0.0100  42  TYR   A CE1 
949  C CE2 A TYR   A 42  ? 0.1641 0.1544 0.1776 0.0080  0.0102  0.0241  42  TYR   A CE2 
950  C CE2 B TYR   A 42  ? 0.1487 0.1607 0.1763 -0.0047 0.0111  0.0166  42  TYR   A CE2 
951  C CZ  A TYR   A 42  ? 0.1574 0.1571 0.1690 0.0008  0.0166  0.0305  42  TYR   A CZ  
952  C CZ  B TYR   A 42  ? 0.1525 0.1603 0.1489 -0.0062 0.0258  0.0223  42  TYR   A CZ  
953  O OH  A TYR   A 42  ? 0.1530 0.1756 0.1864 0.0020  0.0093  0.0217  42  TYR   A OH  
954  O OH  B TYR   A 42  ? 0.1647 0.1757 0.1695 -0.0060 0.0214  0.0122  42  TYR   A OH  
973  N N   . LEU   A 43  ? 0.1190 0.1149 0.1472 -0.0077 0.0164  0.0048  43  LEU   A N   
974  C CA  . LEU   A 43  ? 0.1112 0.1109 0.1377 -0.0059 0.0138  0.0029  43  LEU   A CA  
975  C C   . LEU   A 43  ? 0.1135 0.1189 0.1320 -0.0053 0.0052  0.0051  43  LEU   A C   
976  O O   . LEU   A 43  ? 0.1352 0.1168 0.1404 0.0018  -0.0093 -0.0006 43  LEU   A O   
977  C CB  . LEU   A 43  ? 0.1209 0.1099 0.1406 -0.0099 0.0080  0.0095  43  LEU   A CB  
978  C CG  . LEU   A 43  ? 0.1260 0.1081 0.1462 -0.0029 0.0044  0.0073  43  LEU   A CG  
979  C CD1 . LEU   A 43  ? 0.1311 0.1180 0.1791 -0.0065 -0.0051 0.0143  43  LEU   A CD1 
980  C CD2 . LEU   A 43  ? 0.1390 0.1124 0.1488 -0.0079 0.0124  0.0054  43  LEU   A CD2 
993  N N   . LYS   A 44  ? 0.1259 0.1120 0.1264 -0.0065 0.0065  0.0063  44  LYS   A N   
994  C CA  . LYS   A 44  ? 0.1342 0.1141 0.1373 -0.0085 0.0099  0.0136  44  LYS   A CA  
995  C C   . LYS   A 44  ? 0.1189 0.1150 0.1288 0.0017  -0.0014 0.0087  44  LYS   A C   
996  O O   . LYS   A 44  ? 0.1258 0.1274 0.1341 -0.0030 0.0013  -0.0036 44  LYS   A O   
997  C CB  . LYS   A 44  ? 0.1655 0.1326 0.1607 -0.0033 0.0220  0.0329  44  LYS   A CB  
998  C CG  . LYS   A 44  ? 0.1943 0.1546 0.2268 -0.0123 0.0513  0.0479  44  LYS   A CG  
999  C CD  . LYS   A 44  ? 0.2374 0.2119 0.3339 -0.0273 0.0410  0.0315  44  LYS   A CD  
1000 C CE  . LYS   A 44  ? 0.2709 0.2599 0.3888 -0.0360 0.0316  0.0246  44  LYS   A CE  
1001 N NZ  . LYS   A 44  ? 0.2696 0.2710 0.4147 -0.0429 0.0328  0.0246  44  LYS   A NZ  
1015 N N   . HIS   A 45  ? 0.1101 0.1107 0.1327 -0.0027 -0.0041 0.0126  45  HIS   A N   
1016 C CA  . HIS   A 45  ? 0.1195 0.1124 0.1386 0.0008  -0.0089 0.0079  45  HIS   A CA  
1017 C C   . HIS   A 45  ? 0.1259 0.1250 0.1502 -0.0004 0.0036  0.0110  45  HIS   A C   
1018 O O   . HIS   A 45  ? 0.1437 0.1335 0.1787 0.0185  -0.0046 -0.0104 45  HIS   A O   
1019 C CB  . HIS   A 45  ? 0.1179 0.1096 0.1382 -0.0046 -0.0017 -0.0012 45  HIS   A CB  
1020 C CG  . HIS   A 45  ? 0.1114 0.1062 0.1227 -0.0082 0.0032  0.0039  45  HIS   A CG  
1021 N ND1 . HIS   A 45  ? 0.1092 0.1147 0.1332 -0.0077 -0.0034 0.0077  45  HIS   A ND1 
1022 C CD2 . HIS   A 45  ? 0.1104 0.1137 0.1365 -0.0143 -0.0067 0.0098  45  HIS   A CD2 
1023 C CE1 . HIS   A 45  ? 0.1104 0.1223 0.1171 -0.0102 -0.0037 0.0143  45  HIS   A CE1 
1024 N NE2 . HIS   A 45  ? 0.1078 0.1234 0.1227 -0.0092 -0.0001 0.0168  45  HIS   A NE2 
1032 N N   A GLY   A 46  ? 0.1395 0.1328 0.1620 0.0081  -0.0103 0.0181  46  GLY   A N   
1033 N N   B GLY   A 46  ? 0.1382 0.1385 0.1734 0.0134  -0.0126 0.0288  46  GLY   A N   
1034 C CA  A GLY   A 46  ? 0.1446 0.1355 0.1732 0.0122  -0.0100 0.0181  46  GLY   A CA  
1035 C CA  B GLY   A 46  ? 0.1410 0.1408 0.1955 0.0157  -0.0161 0.0379  46  GLY   A CA  
1036 C C   A GLY   A 46  ? 0.1472 0.1336 0.1639 0.0189  -0.0149 0.0173  46  GLY   A C   
1037 C C   B GLY   A 46  ? 0.1392 0.1312 0.1910 0.0162  -0.0252 0.0369  46  GLY   A C   
1038 O O   A GLY   A 46  ? 0.1553 0.1377 0.1752 0.0197  -0.0179 0.0184  46  GLY   A O   
1039 O O   B GLY   A 46  ? 0.1457 0.1265 0.2124 0.0169  -0.0333 0.0421  46  GLY   A O   
1046 N N   A GLY   A 47  ? 0.1488 0.1349 0.1509 0.0204  -0.0183 0.0095  47  GLY   A N   
1047 N N   B GLY   A 47  ? 0.1349 0.1357 0.1764 0.0124  -0.0272 0.0291  47  GLY   A N   
1048 C CA  A GLY   A 47  ? 0.1477 0.1363 0.1445 0.0203  -0.0240 -0.0067 47  GLY   A CA  
1049 C CA  B GLY   A 47  ? 0.1423 0.1433 0.1800 0.0125  -0.0376 0.0124  47  GLY   A CA  
1050 C C   A GLY   A 47  ? 0.1361 0.1294 0.1381 0.0226  -0.0263 -0.0071 47  GLY   A C   
1051 C C   B GLY   A 47  ? 0.1364 0.1366 0.1797 0.0104  -0.0337 -0.0003 47  GLY   A C   
1052 O O   A GLY   A 47  ? 0.1286 0.1219 0.1299 0.0263  -0.0245 0.0005  47  GLY   A O   
1053 O O   B GLY   A 47  ? 0.1311 0.1282 0.1823 0.0125  -0.0318 0.0065  47  GLY   A O   
1060 N N   A GLY   A 48  ? 0.1302 0.1318 0.1450 0.0245  -0.0319 -0.0062 48  GLY   A N   
1061 N N   B GLY   A 48  ? 0.1342 0.1459 0.1920 0.0127  -0.0351 0.0014  48  GLY   A N   
1062 C CA  A GLY   A 48  ? 0.1243 0.1249 0.1492 0.0173  -0.0304 -0.0097 48  GLY   A CA  
1063 C CA  B GLY   A 48  ? 0.1236 0.1406 0.1872 0.0031  -0.0353 -0.0017 48  GLY   A CA  
1064 C C   A GLY   A 48  ? 0.1152 0.1187 0.1385 0.0121  -0.0123 -0.0159 48  GLY   A C   
1065 C C   B GLY   A 48  ? 0.1123 0.1334 0.1679 -0.0020 -0.0134 0.0016  48  GLY   A C   
1066 O O   A GLY   A 48  ? 0.1249 0.1175 0.1398 0.0149  -0.0182 -0.0189 48  GLY   A O   
1067 O O   B GLY   A 48  ? 0.1307 0.1368 0.1772 0.0059  -0.0165 -0.0008 48  GLY   A O   
1074 N N   A VAL   A 49  ? 0.1143 0.1123 0.1341 0.0075  -0.0070 -0.0181 49  VAL   A N   
1075 N N   B VAL   A 49  ? 0.1084 0.1238 0.1570 -0.0089 -0.0136 0.0044  49  VAL   A N   
1076 C CA  A VAL   A 49  ? 0.1186 0.1091 0.1417 0.0042  0.0074  -0.0159 49  VAL   A CA  
1077 C CA  B VAL   A 49  ? 0.1103 0.1213 0.1463 -0.0098 0.0077  0.0032  49  VAL   A CA  
1078 C C   A VAL   A 49  ? 0.1141 0.1053 0.1146 0.0077  0.0061  -0.0106 49  VAL   A C   
1079 C C   B VAL   A 49  ? 0.1115 0.1138 0.1240 -0.0065 0.0070  0.0070  49  VAL   A C   
1080 O O   A VAL   A 49  ? 0.1169 0.1134 0.1034 0.0054  0.0113  -0.0116 49  VAL   A O   
1081 O O   B VAL   A 49  ? 0.1188 0.1239 0.1369 -0.0164 0.0108  0.0013  49  VAL   A O   
1082 C CB  A VAL   A 49  ? 0.1272 0.1089 0.1640 -0.0013 0.0167  -0.0214 49  VAL   A CB  
1083 C CB  B VAL   A 49  ? 0.1125 0.1196 0.1315 -0.0068 0.0126  -0.0048 49  VAL   A CB  
1084 C CG1 A VAL   A 49  ? 0.1398 0.1072 0.1789 -0.0002 0.0182  -0.0204 49  VAL   A CG1 
1085 C CG1 B VAL   A 49  ? 0.1149 0.1195 0.1174 -0.0007 0.0170  0.0062  49  VAL   A CG1 
1086 C CG2 A VAL   A 49  ? 0.1284 0.1080 0.1820 -0.0134 0.0202  -0.0248 49  VAL   A CG2 
1087 C CG2 B VAL   A 49  ? 0.1228 0.1223 0.1486 -0.0137 0.0127  -0.0090 49  VAL   A CG2 
1106 N N   A ALA   A 50  ? 0.1112 0.1065 0.1088 0.0026  -0.0025 -0.0050 50  ALA   A N   
1107 N N   B ALA   A 50  ? 0.1103 0.1129 0.1149 -0.0077 0.0005  0.0041  50  ALA   A N   
1108 C CA  A ALA   A 50  ? 0.1086 0.1072 0.1133 0.0012  -0.0054 0.0035  50  ALA   A CA  
1109 C CA  B ALA   A 50  ? 0.1066 0.1100 0.1165 -0.0094 -0.0011 0.0091  50  ALA   A CA  
1110 C C   A ALA   A 50  ? 0.1075 0.1098 0.1133 0.0007  -0.0039 -0.0012 50  ALA   A C   
1111 C C   B ALA   A 50  ? 0.1043 0.1111 0.1108 -0.0094 -0.0027 0.0008  50  ALA   A C   
1112 O O   A ALA   A 50  ? 0.1090 0.1119 0.1239 0.0046  -0.0010 -0.0014 50  ALA   A O   
1113 O O   B ALA   A 50  ? 0.1070 0.1120 0.1296 -0.0108 -0.0041 0.0031  50  ALA   A O   
1114 C CB  A ALA   A 50  ? 0.1073 0.1075 0.1108 -0.0012 -0.0068 0.0025  50  ALA   A CB  
1115 C CB  B ALA   A 50  ? 0.1092 0.1095 0.1105 -0.0098 0.0060  0.0044  50  ALA   A CB  
1126 N N   . GLY   A 51  ? 0.1101 0.1112 0.1235 0.0025  -0.0098 0.0010  51  GLY   A N   
1127 C CA  . GLY   A 51  ? 0.1307 0.1036 0.1422 0.0023  -0.0107 0.0056  51  GLY   A CA  
1128 C C   . GLY   A 51  ? 0.1149 0.1160 0.1392 0.0025  -0.0118 -0.0005 51  GLY   A C   
1129 O O   . GLY   A 51  ? 0.1197 0.1234 0.1392 0.0010  -0.0094 -0.0117 51  GLY   A O   
1134 N N   A ALA   A 52  ? 0.1126 0.1220 0.1318 0.0019  -0.0063 -0.0083 52  ALA   A N   
1135 N N   B ALA   A 52  ? 0.1104 0.1255 0.1369 0.0012  0.0015  -0.0225 52  ALA   A N   
1136 C CA  A ALA   A 52  ? 0.1140 0.1297 0.1424 -0.0013 -0.0055 -0.0072 52  ALA   A CA  
1137 C CA  B ALA   A 52  ? 0.1072 0.1349 0.1642 0.0007  0.0023  -0.0286 52  ALA   A CA  
1138 C C   A ALA   A 52  ? 0.1146 0.1263 0.1245 -0.0084 0.0047  -0.0106 52  ALA   A C   
1139 C C   B ALA   A 52  ? 0.1016 0.1312 0.1483 -0.0102 0.0088  -0.0211 52  ALA   A C   
1140 O O   A ALA   A 52  ? 0.1248 0.1351 0.1275 -0.0009 0.0075  -0.0146 52  ALA   A O   
1141 O O   B ALA   A 52  ? 0.1097 0.1385 0.1623 -0.0044 0.0092  -0.0246 52  ALA   A O   
1142 C CB  A ALA   A 52  ? 0.1196 0.1460 0.1500 -0.0038 -0.0085 -0.0035 52  ALA   A CB  
1143 C CB  B ALA   A 52  ? 0.1151 0.1599 0.1811 -0.0017 -0.0008 -0.0278 52  ALA   A CB  
1154 N N   A LEU   A 53  ? 0.1108 0.1239 0.1130 -0.0096 0.0025  -0.0110 53  LEU   A N   
1155 N N   B LEU   A 53  ? 0.1009 0.1309 0.1351 -0.0040 0.0052  -0.0196 53  LEU   A N   
1156 C CA  A LEU   A 53  ? 0.1185 0.1268 0.1160 -0.0094 0.0043  0.0001  53  LEU   A CA  
1157 C CA  B LEU   A 53  ? 0.1118 0.1310 0.1212 -0.0046 0.0091  -0.0050 53  LEU   A CA  
1158 C C   A LEU   A 53  ? 0.1197 0.1304 0.1090 -0.0030 0.0032  -0.0070 53  LEU   A C   
1159 C C   B LEU   A 53  ? 0.1184 0.1332 0.1036 0.0009  0.0086  -0.0129 53  LEU   A C   
1160 O O   A LEU   A 53  ? 0.1294 0.1378 0.1143 -0.0151 0.0019  -0.0053 53  LEU   A O   
1161 O O   B LEU   A 53  ? 0.1319 0.1419 0.1074 -0.0132 0.0056  -0.0085 53  LEU   A O   
1162 C CB  A LEU   A 53  ? 0.1235 0.1250 0.1302 -0.0085 -0.0020 0.0028  53  LEU   A CB  
1163 C CB  B LEU   A 53  ? 0.1124 0.1250 0.1203 -0.0046 0.0041  -0.0043 53  LEU   A CB  
1164 C CG  A LEU   A 53  ? 0.1232 0.1232 0.1377 -0.0051 0.0000  0.0054  53  LEU   A CG  
1165 C CG  B LEU   A 53  ? 0.1191 0.1268 0.1207 -0.0046 0.0048  0.0051  53  LEU   A CG  
1166 C CD1 A LEU   A 53  ? 0.1237 0.1238 0.1255 -0.0024 0.0135  0.0036  53  LEU   A CD1 
1167 C CD1 B LEU   A 53  ? 0.1289 0.1344 0.1177 -0.0041 0.0049  0.0099  53  LEU   A CD1 
1168 C CD2 A LEU   A 53  ? 0.1233 0.1271 0.1542 -0.0089 -0.0023 0.0177  53  LEU   A CD2 
1169 C CD2 B LEU   A 53  ? 0.1232 0.1256 0.1297 -0.0083 0.0135  0.0006  53  LEU   A CD2 
1192 N N   . ASN   A 54  ? 0.1109 0.1244 0.1035 0.0013  0.0026  -0.0020 54  ASN   A N   
1193 C CA  . ASN   A 54  ? 0.1084 0.1212 0.1216 -0.0036 -0.0064 -0.0035 54  ASN   A CA  
1194 C C   . ASN   A 54  ? 0.1163 0.1242 0.1322 -0.0074 0.0065  -0.0050 54  ASN   A C   
1195 O O   . ASN   A 54  ? 0.1218 0.1340 0.1290 -0.0087 -0.0006 -0.0190 54  ASN   A O   
1196 C CB  . ASN   A 54  ? 0.1046 0.1213 0.1349 -0.0106 -0.0079 -0.0040 54  ASN   A CB  
1197 C CG  . ASN   A 54  ? 0.1079 0.1226 0.1322 -0.0039 -0.0033 0.0023  54  ASN   A CG  
1198 O OD1 . ASN   A 54  ? 0.1118 0.1255 0.1252 -0.0053 -0.0090 -0.0005 54  ASN   A OD1 
1199 N ND2 . ASN   A 54  ? 0.1182 0.1275 0.1495 -0.0120 -0.0188 0.0035  54  ASN   A ND2 
1207 N N   . LYS   A 55  ? 0.1163 0.1260 0.1305 -0.0035 -0.0020 -0.0106 55  LYS   A N   
1208 C CA  . LYS   A 55  ? 0.1241 0.1328 0.1476 0.0055  -0.0004 -0.0177 55  LYS   A CA  
1209 C C   . LYS   A 55  ? 0.1224 0.1392 0.1449 -0.0005 0.0107  -0.0266 55  LYS   A C   
1210 O O   . LYS   A 55  ? 0.1334 0.1480 0.1463 -0.0005 0.0034  -0.0321 55  LYS   A O   
1211 C CB  . LYS   A 55  ? 0.1325 0.1482 0.1730 0.0189  -0.0076 -0.0269 55  LYS   A CB  
1212 C CG  . LYS   A 55  ? 0.1574 0.1814 0.1863 0.0340  -0.0150 -0.0297 55  LYS   A CG  
1213 C CD  . LYS   A 55  ? 0.1757 0.2094 0.2096 0.0525  -0.0122 -0.0319 55  LYS   A CD  
1214 C CE  . LYS   A 55  ? 0.2024 0.2312 0.2382 0.0559  -0.0173 -0.0239 55  LYS   A CE  
1215 N NZ  . LYS   A 55  ? 0.2106 0.2415 0.2582 0.0616  -0.0225 -0.0133 55  LYS   A NZ  
1229 N N   . ALA   A 56  ? 0.1291 0.1462 0.1430 -0.0060 0.0127  -0.0285 56  ALA   A N   
1230 C CA  . ALA   A 56  ? 0.1365 0.1620 0.1376 -0.0161 0.0166  -0.0268 56  ALA   A CA  
1231 C C   . ALA   A 56  ? 0.1424 0.1784 0.1158 -0.0163 0.0096  -0.0347 56  ALA   A C   
1232 O O   . ALA   A 56  ? 0.1481 0.2126 0.1314 -0.0037 0.0175  -0.0335 56  ALA   A O   
1233 C CB  . ALA   A 56  ? 0.1451 0.1793 0.1446 -0.0251 0.0125  -0.0150 56  ALA   A CB  
1239 N N   . THR   A 57  ? 0.1272 0.1555 0.1174 -0.0150 0.0094  -0.0240 57  THR   A N   
1240 C CA  . THR   A 57  ? 0.1301 0.1529 0.1308 -0.0104 -0.0022 -0.0183 57  THR   A CA  
1241 C C   . THR   A 57  ? 0.1344 0.1596 0.1378 -0.0060 -0.0008 -0.0295 57  THR   A C   
1242 O O   . THR   A 57  ? 0.1336 0.1628 0.1528 -0.0130 -0.0115 -0.0357 57  THR   A O   
1243 C CB  . THR   A 57  ? 0.1323 0.1513 0.1277 -0.0062 0.0015  -0.0222 57  THR   A CB  
1244 O OG1 . THR   A 57  ? 0.1206 0.1456 0.1245 -0.0090 0.0019  -0.0157 57  THR   A OG1 
1245 C CG2 . THR   A 57  ? 0.1328 0.1508 0.1273 -0.0116 0.0055  -0.0140 57  THR   A CG2 
1253 N N   . ASN   A 58  ? 0.1356 0.1549 0.1482 -0.0123 0.0034  -0.0378 58  ASN   A N   
1254 C CA  . ASN   A 58  ? 0.1574 0.1505 0.1683 -0.0164 0.0180  -0.0493 58  ASN   A CA  
1255 C C   . ASN   A 58  ? 0.1324 0.1390 0.1649 -0.0044 -0.0015 -0.0295 58  ASN   A C   
1256 O O   . ASN   A 58  ? 0.1318 0.1457 0.1853 -0.0169 -0.0086 -0.0395 58  ASN   A O   
1257 C CB  . ASN   A 58  ? 0.2085 0.1716 0.2186 -0.0292 0.0439  -0.0663 58  ASN   A CB  
1258 C CG  . ASN   A 58  ? 0.2591 0.1954 0.2960 -0.0306 0.0447  -0.0545 58  ASN   A CG  
1259 O OD1 . ASN   A 58  ? 0.2812 0.1927 0.3400 0.0024  0.0810  -0.0445 58  ASN   A OD1 
1260 N ND2 . ASN   A 58  ? 0.2780 0.2137 0.3200 -0.0374 0.0301  -0.0463 58  ASN   A ND2 
1267 N N   . ASN   A 59  ? 0.1193 0.1306 0.1497 -0.0065 -0.0071 -0.0198 59  ASN   A N   
1268 C CA  . ASN   A 59  ? 0.1237 0.1198 0.1555 -0.0024 -0.0086 -0.0146 59  ASN   A CA  
1269 C C   . ASN   A 59  ? 0.1228 0.1221 0.1389 -0.0046 -0.0153 -0.0123 59  ASN   A C   
1270 O O   . ASN   A 59  ? 0.1202 0.1268 0.1337 -0.0063 -0.0011 -0.0023 59  ASN   A O   
1271 C CB  . ASN   A 59  ? 0.1240 0.1191 0.1690 -0.0019 -0.0183 -0.0188 59  ASN   A CB  
1272 C CG  . ASN   A 59  ? 0.1252 0.1187 0.1676 -0.0045 -0.0244 -0.0022 59  ASN   A CG  
1273 O OD1 . ASN   A 59  ? 0.1387 0.1292 0.1535 -0.0147 -0.0166 0.0012  59  ASN   A OD1 
1274 N ND2 . ASN   A 59  ? 0.1334 0.1247 0.1707 -0.0139 -0.0190 -0.0030 59  ASN   A ND2 
1281 N N   . ALA   A 60  ? 0.1168 0.1294 0.1376 -0.0057 -0.0053 -0.0147 60  ALA   A N   
1282 C CA  . ALA   A 60  ? 0.1166 0.1278 0.1381 -0.0036 -0.0141 -0.0101 60  ALA   A CA  
1283 C C   . ALA   A 60  ? 0.1194 0.1206 0.1468 -0.0052 -0.0043 -0.0046 60  ALA   A C   
1284 O O   . ALA   A 60  ? 0.1127 0.1235 0.1656 -0.0030 -0.0064 -0.0110 60  ALA   A O   
1285 C CB  . ALA   A 60  ? 0.1299 0.1438 0.1501 -0.0038 -0.0203 -0.0198 60  ALA   A CB  
1291 N N   . MET   A 61  ? 0.1130 0.1225 0.1381 -0.0069 0.0007  -0.0085 61  MET   A N   
1292 C CA  . MET   A 61  ? 0.1162 0.1231 0.1281 -0.0063 0.0032  -0.0058 61  MET   A CA  
1293 C C   . MET   A 61  ? 0.1067 0.1140 0.1378 -0.0079 -0.0006 -0.0036 61  MET   A C   
1294 O O   . MET   A 61  ? 0.1144 0.1184 0.1400 -0.0034 0.0072  -0.0047 61  MET   A O   
1295 C CB  . MET   A 61  ? 0.1166 0.1197 0.1259 -0.0068 -0.0020 -0.0081 61  MET   A CB  
1296 C CG  . MET   A 61  ? 0.1121 0.1257 0.1405 -0.0083 0.0003  -0.0129 61  MET   A CG  
1297 S SD  . MET   A 61  ? 0.1182 0.1249 0.1773 -0.0131 0.0003  -0.0205 61  MET   A SD  
1298 C CE  . MET   A 61  ? 0.1386 0.1371 0.1882 -0.0195 0.0174  -0.0103 61  MET   A CE  
1308 N N   . GLN   A 62  ? 0.1096 0.1111 0.1393 -0.0114 -0.0011 -0.0070 62  GLN   A N   
1309 C CA  . GLN   A 62  ? 0.1123 0.1073 0.1446 -0.0081 0.0040  -0.0035 62  GLN   A CA  
1310 C C   . GLN   A 62  ? 0.1131 0.1005 0.1574 -0.0005 0.0049  0.0012  62  GLN   A C   
1311 O O   . GLN   A 62  ? 0.1179 0.1210 0.1382 -0.0040 0.0078  -0.0047 62  GLN   A O   
1312 C CB  . GLN   A 62  ? 0.1140 0.1071 0.1559 -0.0059 0.0030  -0.0052 62  GLN   A CB  
1313 C CG  . GLN   A 62  ? 0.1187 0.1067 0.1451 -0.0070 0.0014  0.0080  62  GLN   A CG  
1314 C CD  . GLN   A 62  ? 0.1250 0.1143 0.1434 -0.0035 0.0052  0.0059  62  GLN   A CD  
1315 O OE1 . GLN   A 62  ? 0.1277 0.1234 0.1488 -0.0042 -0.0002 -0.0030 62  GLN   A OE1 
1316 N NE2 . GLN   A 62  ? 0.1296 0.1165 0.1436 -0.0007 -0.0003 -0.0044 62  GLN   A NE2 
1325 N N   . VAL   A 63  ? 0.1137 0.1142 0.1655 -0.0065 0.0092  -0.0185 63  VAL   A N   
1326 C CA  . VAL   A 63  ? 0.1166 0.1260 0.1842 -0.0168 -0.0030 -0.0182 63  VAL   A CA  
1327 C C   . VAL   A 63  ? 0.1041 0.1222 0.1622 -0.0168 -0.0020 -0.0172 63  VAL   A C   
1328 O O   . VAL   A 63  ? 0.1080 0.1260 0.1746 -0.0127 0.0038  -0.0124 63  VAL   A O   
1329 C CB  . VAL   A 63  ? 0.1263 0.1420 0.2063 -0.0170 -0.0086 -0.0438 63  VAL   A CB  
1330 C CG1 . VAL   A 63  ? 0.1482 0.1654 0.2387 -0.0135 -0.0195 -0.0576 63  VAL   A CG1 
1331 C CG2 . VAL   A 63  ? 0.1390 0.1337 0.2145 -0.0156 0.0052  -0.0407 63  VAL   A CG2 
1341 N N   . GLU   A 64  ? 0.1079 0.1285 0.1544 -0.0025 -0.0017 -0.0134 64  GLU   A N   
1342 C CA  . GLU   A 64  ? 0.1114 0.1320 0.1557 -0.0061 -0.0070 0.0014  64  GLU   A CA  
1343 C C   . GLU   A 64  ? 0.1068 0.1202 0.1538 -0.0072 0.0010  0.0017  64  GLU   A C   
1344 O O   . GLU   A 64  ? 0.1109 0.1289 0.1517 0.0005  0.0018  -0.0049 64  GLU   A O   
1345 C CB  . GLU   A 64  ? 0.1177 0.1334 0.1601 -0.0062 -0.0011 -0.0040 64  GLU   A CB  
1346 C CG  . GLU   A 64  ? 0.1288 0.1399 0.1630 -0.0120 0.0079  0.0012  64  GLU   A CG  
1347 C CD  . GLU   A 64  ? 0.1393 0.1443 0.1662 -0.0190 0.0092  -0.0118 64  GLU   A CD  
1348 O OE1 . GLU   A 64  ? 0.1391 0.1594 0.1799 -0.0233 0.0183  -0.0069 64  GLU   A OE1 
1349 O OE2 . GLU   A 64  ? 0.1577 0.1443 0.1748 -0.0251 -0.0012 0.0023  64  GLU   A OE2 
1356 N N   . SER   A 65  ? 0.1042 0.1218 0.1433 0.0007  -0.0024 -0.0053 65  SER   A N   
1357 C CA  . SER   A 65  ? 0.1085 0.1124 0.1506 -0.0050 -0.0071 -0.0016 65  SER   A CA  
1358 C C   . SER   A 65  ? 0.1075 0.1195 0.1541 -0.0051 -0.0017 -0.0041 65  SER   A C   
1359 O O   . SER   A 65  ? 0.1198 0.1222 0.1575 -0.0022 0.0078  -0.0117 65  SER   A O   
1360 C CB  . SER   A 65  ? 0.1117 0.1130 0.1438 -0.0071 0.0111  -0.0023 65  SER   A CB  
1361 O OG  . SER   A 65  ? 0.1116 0.1278 0.1429 -0.0081 -0.0055 0.0063  65  SER   A OG  
1367 N N   . ASP   A 66  ? 0.1122 0.1155 0.1489 -0.0058 0.0107  0.0011  66  ASP   A N   
1368 C CA  . ASP   A 66  ? 0.1226 0.1247 0.1678 -0.0035 0.0024  0.0117  66  ASP   A CA  
1369 C C   . ASP   A 66  ? 0.1202 0.1223 0.1677 -0.0054 0.0050  0.0105  66  ASP   A C   
1370 O O   . ASP   A 66  ? 0.1257 0.1348 0.1742 -0.0029 0.0211  0.0118  66  ASP   A O   
1371 C CB  . ASP   A 66  ? 0.1355 0.1337 0.2024 0.0036  0.0090  0.0234  66  ASP   A CB  
1372 C CG  . ASP   A 66  ? 0.1580 0.1464 0.2360 -0.0009 0.0014  0.0383  66  ASP   A CG  
1373 O OD1 . ASP   A 66  ? 0.1538 0.1755 0.2020 -0.0063 -0.0020 0.0481  66  ASP   A OD1 
1374 O OD2 . ASP   A 66  ? 0.1763 0.1546 0.3128 0.0190  -0.0231 0.0217  66  ASP   A OD2 
1379 N N   . ASP   A 67  ? 0.1150 0.1224 0.1781 -0.0037 0.0054  0.0138  67  ASP   A N   
1380 C CA  . ASP   A 67  ? 0.1160 0.1390 0.1951 -0.0031 0.0023  0.0223  67  ASP   A CA  
1381 C C   . ASP   A 67  ? 0.1185 0.1385 0.1820 0.0009  0.0069  0.0264  67  ASP   A C   
1382 O O   . ASP   A 67  ? 0.1120 0.1505 0.1903 0.0030  0.0185  0.0269  67  ASP   A O   
1383 C CB  . ASP   A 67  ? 0.1223 0.1490 0.2200 -0.0093 -0.0122 0.0229  67  ASP   A CB  
1384 C CG  . ASP   A 67  ? 0.1273 0.1648 0.2528 -0.0083 -0.0285 0.0247  67  ASP   A CG  
1385 O OD1 . ASP   A 67  ? 0.1336 0.1830 0.3234 -0.0145 -0.0315 0.0401  67  ASP   A OD1 
1386 O OD2 . ASP   A 67  ? 0.1287 0.1677 0.2335 0.0019  -0.0143 0.0183  67  ASP   A OD2 
1391 N N   . TYR   A 68  ? 0.1203 0.1290 0.1775 -0.0014 0.0162  0.0228  68  TYR   A N   
1392 C CA  . TYR   A 68  ? 0.1261 0.1285 0.1747 0.0023  0.0213  0.0226  68  TYR   A CA  
1393 C C   . TYR   A 68  ? 0.1203 0.1246 0.1679 -0.0012 0.0245  0.0176  68  TYR   A C   
1394 O O   . TYR   A 68  ? 0.1256 0.1340 0.1752 0.0085  0.0258  0.0140  68  TYR   A O   
1395 C CB  . TYR   A 68  ? 0.1339 0.1203 0.1878 0.0122  0.0364  0.0193  68  TYR   A CB  
1396 C CG  . TYR   A 68  ? 0.1436 0.1402 0.2065 0.0088  0.0553  0.0249  68  TYR   A CG  
1397 C CD1 . TYR   A 68  ? 0.1502 0.1508 0.2333 -0.0145 0.0382  -0.0039 68  TYR   A CD1 
1398 C CD2 . TYR   A 68  ? 0.1658 0.1417 0.2227 0.0150  0.0568  0.0343  68  TYR   A CD2 
1399 C CE1 . TYR   A 68  ? 0.1539 0.1598 0.2591 -0.0155 0.0430  -0.0053 68  TYR   A CE1 
1400 C CE2 . TYR   A 68  ? 0.1594 0.1490 0.2418 0.0071  0.0620  0.0146  68  TYR   A CE2 
1401 C CZ  . TYR   A 68  ? 0.1585 0.1545 0.2567 -0.0184 0.0478  -0.0023 68  TYR   A CZ  
1402 O OH  . TYR   A 68  ? 0.1856 0.1531 0.2615 -0.0143 0.0216  -0.0157 68  TYR   A OH  
1412 N N   . ILE   A 69  ? 0.1149 0.1202 0.1704 0.0001  0.0173  0.0132  69  ILE   A N   
1413 C CA  . ILE   A 69  ? 0.1251 0.1217 0.1630 0.0037  0.0185  0.0055  69  ILE   A CA  
1414 C C   . ILE   A 69  ? 0.1219 0.1255 0.1637 0.0035  0.0221  0.0181  69  ILE   A C   
1415 O O   . ILE   A 69  ? 0.1330 0.1384 0.1593 -0.0014 0.0205  0.0215  69  ILE   A O   
1416 C CB  . ILE   A 69  ? 0.1299 0.1450 0.1718 0.0065  0.0139  0.0034  69  ILE   A CB  
1417 C CG1 . ILE   A 69  ? 0.1334 0.1575 0.1742 0.0094  0.0125  -0.0129 69  ILE   A CG1 
1418 C CG2 . ILE   A 69  ? 0.1549 0.1648 0.1876 0.0140  -0.0046 0.0037  69  ILE   A CG2 
1419 C CD1 . ILE   A 69  ? 0.1348 0.1676 0.1798 0.0040  0.0163  -0.0216 69  ILE   A CD1 
1431 N N   . ALA   A 70  ? 0.1299 0.1277 0.1666 -0.0097 0.0199  0.0191  70  ALA   A N   
1432 C CA  . ALA   A 70  ? 0.1350 0.1385 0.1904 -0.0154 0.0296  0.0189  70  ALA   A CA  
1433 C C   . ALA   A 70  ? 0.1328 0.1516 0.1901 -0.0077 0.0308  0.0191  70  ALA   A C   
1434 O O   . ALA   A 70  ? 0.1452 0.1837 0.2147 0.0011  0.0449  0.0341  70  ALA   A O   
1435 C CB  . ALA   A 70  ? 0.1397 0.1375 0.2226 -0.0219 0.0302  0.0121  70  ALA   A CB  
1441 N N   . THR   A 71  ? 0.1221 0.1515 0.1694 -0.0022 0.0196  0.0198  71  THR   A N   
1442 C CA  . THR   A 71  ? 0.1319 0.1661 0.2094 0.0037  0.0158  0.0164  71  THR   A CA  
1443 C C   . THR   A 71  ? 0.1245 0.1612 0.2172 0.0099  0.0282  0.0165  71  THR   A C   
1444 O O   . THR   A 71  ? 0.1318 0.1888 0.2536 0.0073  0.0400  -0.0044 71  THR   A O   
1445 C CB  . THR   A 71  ? 0.1553 0.1856 0.2278 0.0126  -0.0128 0.0226  71  THR   A CB  
1446 O OG1 . THR   A 71  ? 0.1831 0.2019 0.2293 0.0057  -0.0333 0.0179  71  THR   A OG1 
1447 C CG2 . THR   A 71  ? 0.1689 0.1983 0.2592 0.0223  -0.0170 0.0294  71  THR   A CG2 
1455 N N   . ASN   A 72  ? 0.1310 0.1458 0.1924 0.0088  0.0225  0.0193  72  ASN   A N   
1456 C CA  . ASN   A 72  ? 0.1343 0.1453 0.1994 0.0152  0.0294  0.0161  72  ASN   A CA  
1457 C C   . ASN   A 72  ? 0.1401 0.1413 0.1907 0.0081  0.0406  0.0077  72  ASN   A C   
1458 O O   . ASN   A 72  ? 0.1586 0.1460 0.2184 0.0141  0.0327  -0.0012 72  ASN   A O   
1459 C CB  . ASN   A 72  ? 0.1515 0.1512 0.2082 0.0120  0.0277  0.0223  72  ASN   A CB  
1460 C CG  . ASN   A 72  ? 0.1760 0.1683 0.2101 0.0231  0.0281  0.0259  72  ASN   A CG  
1461 O OD1 . ASN   A 72  ? 0.1906 0.1983 0.2219 0.0252  0.0395  0.0348  72  ASN   A OD1 
1462 N ND2 . ASN   A 72  ? 0.1884 0.1661 0.2081 0.0503  0.0060  0.0150  72  ASN   A ND2 
1469 N N   . GLY   A 73  ? 0.1425 0.1396 0.1842 0.0011  0.0391  0.0057  73  GLY   A N   
1470 C CA  . GLY   A 73  ? 0.1440 0.1417 0.1728 -0.0070 0.0351  0.0144  73  GLY   A CA  
1471 C C   . GLY   A 73  ? 0.1437 0.1340 0.1606 -0.0030 0.0450  0.0094  73  GLY   A C   
1472 O O   . GLY   A 73  ? 0.1444 0.1394 0.1695 0.0060  0.0357  0.0196  73  GLY   A O   
1476 N N   . PRO   A 74  ? 0.1488 0.1355 0.1666 -0.0137 0.0429  0.0111  74  PRO   A N   
1477 C CA  . PRO   A 74  ? 0.1430 0.1316 0.1828 -0.0085 0.0409  0.0153  74  PRO   A CA  
1478 C C   . PRO   A 74  ? 0.1380 0.1237 0.1710 -0.0038 0.0352  0.0039  74  PRO   A C   
1479 O O   . PRO   A 74  ? 0.1507 0.1230 0.1849 0.0027  0.0312  -0.0063 74  PRO   A O   
1480 C CB  . PRO   A 74  ? 0.1629 0.1543 0.2049 -0.0078 0.0407  0.0239  74  PRO   A CB  
1481 C CG  . PRO   A 74  ? 0.1886 0.1855 0.2421 -0.0229 0.0297  0.0022  74  PRO   A CG  
1482 C CD  . PRO   A 74  ? 0.1663 0.1659 0.1890 -0.0282 0.0357  -0.0047 74  PRO   A CD  
1490 N N   . LEU   A 75  ? 0.1415 0.1130 0.1560 0.0025  0.0232  0.0022  75  LEU   A N   
1491 C CA  . LEU   A 75  ? 0.1473 0.1125 0.1387 -0.0016 0.0197  0.0036  75  LEU   A CA  
1492 C C   . LEU   A 75  ? 0.1559 0.1228 0.1396 0.0031  0.0218  0.0075  75  LEU   A C   
1493 O O   . LEU   A 75  ? 0.1833 0.1349 0.1418 0.0078  0.0112  -0.0013 75  LEU   A O   
1494 C CB  . LEU   A 75  ? 0.1524 0.1206 0.1220 -0.0086 0.0083  0.0107  75  LEU   A CB  
1495 C CG  . LEU   A 75  ? 0.1716 0.1488 0.1437 -0.0361 0.0034  0.0172  75  LEU   A CG  
1496 C CD1 . LEU   A 75  ? 0.1838 0.1964 0.1526 -0.0375 0.0065  0.0017  75  LEU   A CD1 
1497 C CD2 . LEU   A 75  ? 0.1997 0.1859 0.1875 -0.0078 0.0040  0.0286  75  LEU   A CD2 
1509 N N   . LYS   A 76  ? 0.1577 0.1240 0.1538 -0.0060 0.0189  -0.0055 76  LYS   A N   
1510 C CA  . LYS   A 76  ? 0.1576 0.1443 0.1665 -0.0139 0.0195  -0.0195 76  LYS   A CA  
1511 C C   . LYS   A 76  ? 0.1498 0.1255 0.1415 -0.0042 0.0160  -0.0043 76  LYS   A C   
1512 O O   . LYS   A 76  ? 0.1575 0.1225 0.1210 -0.0042 0.0180  0.0045  76  LYS   A O   
1513 C CB  . LYS   A 76  ? 0.1579 0.1720 0.2088 -0.0029 0.0197  -0.0415 76  LYS   A CB  
1514 C CG  . LYS   A 76  ? 0.1687 0.1656 0.2597 0.0018  0.0227  -0.0392 76  LYS   A CG  
1515 C CD  . LYS   A 76  ? 0.1739 0.1563 0.3171 0.0067  0.0133  -0.0465 76  LYS   A CD  
1516 C CE  . LYS   A 76  ? 0.1922 0.1803 0.3671 -0.0014 0.0146  -0.0514 76  LYS   A CE  
1517 N NZ  . LYS   A 76  ? 0.1939 0.1795 0.4048 -0.0174 0.0044  -0.0598 76  LYS   A NZ  
1531 N N   . VAL   A 77  ? 0.1557 0.1313 0.1289 -0.0048 0.0238  0.0103  77  VAL   A N   
1532 C CA  . VAL   A 77  ? 0.1561 0.1353 0.1279 0.0051  0.0233  0.0109  77  VAL   A CA  
1533 C C   . VAL   A 77  ? 0.1492 0.1274 0.1192 0.0096  0.0159  0.0041  77  VAL   A C   
1534 O O   . VAL   A 77  ? 0.1565 0.1306 0.1143 0.0103  0.0284  -0.0047 77  VAL   A O   
1535 C CB  . VAL   A 77  ? 0.1762 0.1521 0.1336 0.0011  0.0152  0.0183  77  VAL   A CB  
1536 C CG1 . VAL   A 77  ? 0.1760 0.1691 0.1579 0.0082  0.0108  0.0059  77  VAL   A CG1 
1537 C CG2 . VAL   A 77  ? 0.1992 0.1584 0.1626 -0.0033 0.0044  0.0231  77  VAL   A CG2 
1547 N N   . GLY   A 78  ? 0.1485 0.1241 0.1200 0.0068  0.0241  -0.0005 78  GLY   A N   
1548 C CA  . GLY   A 78  ? 0.1411 0.1225 0.1293 0.0026  0.0246  0.0088  78  GLY   A CA  
1549 C C   . GLY   A 78  ? 0.1313 0.1134 0.1327 0.0031  0.0251  0.0080  78  GLY   A C   
1550 O O   . GLY   A 78  ? 0.1338 0.1187 0.1421 -0.0004 0.0188  0.0118  78  GLY   A O   
1554 N N   . GLY   A 79  ? 0.1359 0.1149 0.1247 0.0047  0.0178  0.0066  79  GLY   A N   
1555 C CA  . GLY   A 79  ? 0.1316 0.1172 0.1493 0.0026  0.0241  0.0095  79  GLY   A CA  
1556 C C   . GLY   A 79  ? 0.1187 0.1123 0.1393 0.0018  0.0154  0.0048  79  GLY   A C   
1557 O O   . GLY   A 79  ? 0.1270 0.1268 0.1318 0.0165  0.0121  0.0019  79  GLY   A O   
1561 N N   . SER   A 80  ? 0.1170 0.1295 0.1568 0.0057  0.0197  -0.0069 80  SER   A N   
1562 C CA  . SER   A 80  ? 0.1168 0.1231 0.1479 0.0014  0.0128  0.0002  80  SER   A CA  
1563 C C   . SER   A 80  ? 0.1115 0.1230 0.1361 0.0003  0.0055  0.0057  80  SER   A C   
1564 O O   . SER   A 80  ? 0.1155 0.1447 0.1704 0.0047  0.0079  -0.0072 80  SER   A O   
1565 C CB  . SER   A 80  ? 0.1312 0.1190 0.1651 -0.0046 0.0111  0.0040  80  SER   A CB  
1566 O OG  . SER   A 80  ? 0.1576 0.1269 0.2050 0.0018  0.0002  0.0120  80  SER   A OG  
1572 N N   . CYS   A 81  ? 0.1104 0.1199 0.1322 -0.0007 -0.0023 0.0075  81  CYS   A N   
1573 C CA  . CYS   A 81  ? 0.1084 0.1264 0.1376 -0.0060 -0.0040 0.0163  81  CYS   A CA  
1574 C C   . CYS   A 81  ? 0.1125 0.1213 0.1373 -0.0082 -0.0013 0.0212  81  CYS   A C   
1575 O O   . CYS   A 81  ? 0.1130 0.1474 0.1449 0.0020  0.0022  0.0261  81  CYS   A O   
1576 C CB  . CYS   A 81  ? 0.1153 0.1324 0.1565 -0.0133 -0.0024 0.0170  81  CYS   A CB  
1577 S SG  . CYS   A 81  ? 0.1327 0.1227 0.1477 -0.0153 0.0040  0.0094  81  CYS   A SG  
1583 N N   . VAL   A 82  ? 0.1191 0.1267 0.1327 0.0002  -0.0109 0.0201  82  VAL   A N   
1584 C CA  . VAL   A 82  ? 0.1300 0.1366 0.1249 0.0024  -0.0036 0.0243  82  VAL   A CA  
1585 C C   . VAL   A 82  ? 0.1264 0.1394 0.1389 0.0002  -0.0042 0.0212  82  VAL   A C   
1586 O O   . VAL   A 82  ? 0.1219 0.1516 0.1644 0.0015  -0.0028 -0.0008 82  VAL   A O   
1587 C CB  . VAL   A 82  ? 0.1597 0.1488 0.1421 0.0037  -0.0020 0.0229  82  VAL   A CB  
1588 C CG1 . VAL   A 82  ? 0.1818 0.1621 0.1641 0.0055  0.0041  0.0162  82  VAL   A CG1 
1589 C CG2 . VAL   A 82  ? 0.1659 0.1550 0.1662 -0.0030 -0.0059 0.0216  82  VAL   A CG2 
1599 N N   . LEU   A 83  ? 0.1223 0.1396 0.1284 -0.0069 -0.0105 0.0092  83  LEU   A N   
1600 C CA  . LEU   A 83  ? 0.1267 0.1390 0.1332 -0.0131 -0.0095 0.0028  83  LEU   A CA  
1601 C C   . LEU   A 83  ? 0.1348 0.1396 0.1218 -0.0124 -0.0133 0.0091  83  LEU   A C   
1602 O O   . LEU   A 83  ? 0.1414 0.1399 0.1263 -0.0208 -0.0056 0.0111  83  LEU   A O   
1603 C CB  . LEU   A 83  ? 0.1333 0.1420 0.1363 -0.0104 -0.0063 0.0107  83  LEU   A CB  
1604 C CG  . LEU   A 83  ? 0.1452 0.1504 0.1369 -0.0097 0.0045  0.0013  83  LEU   A CG  
1605 C CD1 . LEU   A 83  ? 0.1619 0.1592 0.1614 -0.0190 -0.0074 0.0188  83  LEU   A CD1 
1606 C CD2 . LEU   A 83  ? 0.1454 0.1646 0.1507 -0.0092 0.0094  0.0067  83  LEU   A CD2 
1618 N N   . SER   A 84  ? 0.1445 0.1459 0.1206 -0.0163 -0.0091 0.0115  84  SER   A N   
1619 C CA  . SER   A 84  ? 0.1500 0.1506 0.1115 -0.0139 -0.0110 0.0108  84  SER   A CA  
1620 C C   . SER   A 84  ? 0.1578 0.1413 0.1203 -0.0213 -0.0006 0.0032  84  SER   A C   
1621 O O   . SER   A 84  ? 0.1523 0.1576 0.1178 -0.0189 -0.0040 -0.0020 84  SER   A O   
1622 C CB  . SER   A 84  ? 0.1528 0.1669 0.1264 -0.0114 -0.0072 0.0014  84  SER   A CB  
1623 O OG  . SER   A 84  ? 0.1623 0.1907 0.1352 -0.0075 -0.0112 -0.0112 84  SER   A OG  
1629 N N   . GLY   A 85  ? 0.1692 0.1591 0.1160 -0.0209 0.0065  -0.0007 85  GLY   A N   
1630 C CA  . GLY   A 85  ? 0.1692 0.1683 0.1317 -0.0245 0.0151  -0.0101 85  GLY   A CA  
1631 C C   . GLY   A 85  ? 0.1647 0.1718 0.1180 -0.0185 0.0096  -0.0128 85  GLY   A C   
1632 O O   . GLY   A 85  ? 0.1702 0.1791 0.1315 -0.0212 0.0141  -0.0158 85  GLY   A O   
1636 N N   . HIS   A 86  ? 0.1601 0.1666 0.1129 -0.0217 0.0050  -0.0034 86  HIS   A N   
1637 C CA  . HIS   A 86  ? 0.1746 0.1731 0.1153 -0.0234 -0.0008 -0.0038 86  HIS   A CA  
1638 C C   . HIS   A 86  ? 0.2000 0.1795 0.1186 -0.0237 -0.0037 -0.0117 86  HIS   A C   
1639 O O   . HIS   A 86  ? 0.2105 0.2054 0.1227 -0.0215 0.0067  -0.0131 86  HIS   A O   
1640 C CB  . HIS   A 86  ? 0.1699 0.1648 0.1293 -0.0144 0.0067  0.0002  86  HIS   A CB  
1641 C CG  . HIS   A 86  ? 0.1656 0.1631 0.1324 -0.0088 0.0037  0.0030  86  HIS   A CG  
1642 N ND1 . HIS   A 86  ? 0.1736 0.1648 0.1709 -0.0168 -0.0003 -0.0045 86  HIS   A ND1 
1643 C CD2 . HIS   A 86  ? 0.1664 0.1570 0.1259 0.0009  0.0080  0.0033  86  HIS   A CD2 
1644 C CE1 . HIS   A 86  ? 0.1689 0.1632 0.1623 -0.0139 0.0205  0.0024  86  HIS   A CE1 
1645 N NE2 . HIS   A 86  ? 0.1678 0.1564 0.1304 -0.0024 0.0128  0.0148  86  HIS   A NE2 
1653 N N   . ASN   A 87  ? 0.2094 0.1872 0.1325 -0.0254 0.0194  -0.0186 87  ASN   A N   
1654 C CA  . ASN   A 87  ? 0.2229 0.1986 0.1500 -0.0187 0.0490  -0.0200 87  ASN   A CA  
1655 C C   . ASN   A 87  ? 0.2190 0.2142 0.1718 -0.0258 0.0640  -0.0107 87  ASN   A C   
1656 O O   . ASN   A 87  ? 0.2477 0.2375 0.2080 -0.0353 0.0853  -0.0195 87  ASN   A O   
1657 C CB  . ASN   A 87  ? 0.2367 0.2057 0.1594 -0.0119 0.0492  -0.0290 87  ASN   A CB  
1658 C CG  . ASN   A 87  ? 0.2462 0.2201 0.1626 -0.0063 0.0601  -0.0223 87  ASN   A CG  
1659 O OD1 . ASN   A 87  ? 0.2599 0.2246 0.1753 0.0092  0.0591  -0.0144 87  ASN   A OD1 
1660 N ND2 . ASN   A 87  ? 0.2495 0.2459 0.1741 -0.0070 0.0596  -0.0113 87  ASN   A ND2 
1667 N N   A LEU   A 88  ? 0.2060 0.2081 0.1643 -0.0298 0.0490  -0.0014 88  LEU   A N   
1668 N N   B LEU   A 88  ? 0.2012 0.2083 0.1610 -0.0289 0.0535  -0.0053 88  LEU   A N   
1669 C CA  A LEU   A 88  ? 0.1958 0.2047 0.1714 -0.0352 0.0335  0.0104  88  LEU   A CA  
1670 C CA  B LEU   A 88  ? 0.1880 0.2068 0.1694 -0.0342 0.0407  0.0054  88  LEU   A CA  
1671 C C   A LEU   A 88  ? 0.1923 0.2023 0.1653 -0.0331 0.0291  0.0157  88  LEU   A C   
1672 C C   B LEU   A 88  ? 0.1889 0.2042 0.1690 -0.0329 0.0328  0.0190  88  LEU   A C   
1673 O O   A LEU   A 88  ? 0.1964 0.2069 0.1882 -0.0323 0.0292  0.0255  88  LEU   A O   
1674 O O   B LEU   A 88  ? 0.1952 0.2105 0.2000 -0.0319 0.0339  0.0364  88  LEU   A O   
1675 C CB  A LEU   A 88  ? 0.1977 0.2073 0.1889 -0.0426 0.0073  0.0197  88  LEU   A CB  
1676 C CB  B LEU   A 88  ? 0.1878 0.2129 0.1858 -0.0403 0.0102  0.0052  88  LEU   A CB  
1677 C CG  A LEU   A 88  ? 0.2096 0.2152 0.2132 -0.0409 -0.0061 0.0223  88  LEU   A CG  
1678 C CG  B LEU   A 88  ? 0.2029 0.2248 0.2069 -0.0334 -0.0019 -0.0013 88  LEU   A CG  
1679 C CD1 A LEU   A 88  ? 0.2133 0.2183 0.2211 -0.0401 -0.0115 0.0179  88  LEU   A CD1 
1680 C CD1 B LEU   A 88  ? 0.2046 0.2283 0.1989 -0.0305 -0.0013 -0.0143 88  LEU   A CD1 
1681 C CD2 A LEU   A 88  ? 0.2196 0.2220 0.2262 -0.0353 -0.0055 0.0199  88  LEU   A CD2 
1682 C CD2 B LEU   A 88  ? 0.2168 0.2346 0.2305 -0.0243 0.0014  -0.0007 88  LEU   A CD2 
1705 N N   . ALA   A 89  ? 0.1879 0.1972 0.1421 -0.0294 0.0261  0.0051  89  ALA   A N   
1706 C CA  . ALA   A 89  ? 0.1931 0.1949 0.1195 -0.0254 0.0179  0.0055  89  ALA   A CA  
1707 C C   . ALA   A 89  ? 0.2019 0.1976 0.1258 -0.0224 0.0012  0.0021  89  ALA   A C   
1708 O O   . ALA   A 89  ? 0.1942 0.1950 0.1587 -0.0298 -0.0034 -0.0162 89  ALA   A O   
1709 C CB  . ALA   A 89  ? 0.1884 0.1913 0.1109 -0.0248 0.0115  0.0110  89  ALA   A CB  
1716 N N   . LYS   A 90  ? 0.2141 0.2090 0.1214 -0.0271 -0.0135 0.0070  90  LYS   A N   
1717 C CA  . LYS   A 90  ? 0.2173 0.2196 0.1361 -0.0198 -0.0230 0.0149  90  LYS   A CA  
1718 C C   . LYS   A 90  ? 0.1989 0.2002 0.1338 -0.0231 -0.0236 0.0030  90  LYS   A C   
1719 O O   . LYS   A 90  ? 0.1993 0.2167 0.1514 -0.0278 -0.0305 -0.0035 90  LYS   A O   
1720 C CB  . LYS   A 90  ? 0.2373 0.2487 0.1721 -0.0109 -0.0354 0.0322  90  LYS   A CB  
1721 C CG  . LYS   A 90  ? 0.2701 0.2819 0.2601 -0.0065 -0.0419 0.0321  90  LYS   A CG  
1722 C CD  . LYS   A 90  ? 0.2974 0.3077 0.3387 -0.0076 -0.0378 0.0411  90  LYS   A CD  
1723 C CE  . LYS   A 90  ? 0.3043 0.3153 0.4082 -0.0095 -0.0291 0.0435  90  LYS   A CE  
1724 N NZ  . LYS   A 90  ? 0.3183 0.3319 0.4484 -0.0115 -0.0236 0.0370  90  LYS   A NZ  
1738 N N   . HIS   A 91  ? 0.1841 0.1740 0.1161 -0.0247 -0.0261 0.0143  91  HIS   A N   
1739 C CA  . HIS   A 91  ? 0.1681 0.1627 0.1172 -0.0176 -0.0204 0.0169  91  HIS   A CA  
1740 C C   . HIS   A 91  ? 0.1498 0.1526 0.1061 -0.0180 -0.0079 0.0158  91  HIS   A C   
1741 O O   . HIS   A 91  ? 0.1520 0.1655 0.1082 -0.0228 -0.0016 0.0179  91  HIS   A O   
1742 C CB  . HIS   A 91  ? 0.1855 0.1906 0.1596 0.0040  -0.0288 0.0205  91  HIS   A CB  
1743 C CG  . HIS   A 91  ? 0.2301 0.2413 0.2254 0.0172  -0.0586 0.0130  91  HIS   A CG  
1744 N ND1 . HIS   A 91  ? 0.2424 0.2680 0.2701 0.0226  -0.0701 -0.0080 91  HIS   A ND1 
1745 C CD2 . HIS   A 91  ? 0.2512 0.2613 0.2441 0.0248  -0.0770 0.0211  91  HIS   A CD2 
1746 C CE1 . HIS   A 91  ? 0.2570 0.2772 0.2856 0.0239  -0.0735 -0.0031 91  HIS   A CE1 
1747 N NE2 . HIS   A 91  ? 0.2626 0.2775 0.2731 0.0285  -0.0805 0.0120  91  HIS   A NE2 
1755 N N   . CYS   A 92  ? 0.1418 0.1465 0.1103 -0.0182 -0.0093 0.0127  92  CYS   A N   
1756 C CA  . CYS   A 92  ? 0.1293 0.1382 0.1191 -0.0160 0.0024  0.0139  92  CYS   A CA  
1757 C C   . CYS   A 92  ? 0.1245 0.1359 0.1137 -0.0137 0.0010  0.0157  92  CYS   A C   
1758 O O   . CYS   A 92  ? 0.1241 0.1414 0.1204 -0.0154 0.0013  0.0019  92  CYS   A O   
1759 C CB  . CYS   A 92  ? 0.1324 0.1349 0.1322 -0.0084 -0.0114 0.0077  92  CYS   A CB  
1760 S SG  . CYS   A 92  ? 0.1300 0.1253 0.1313 -0.0123 0.0001  0.0067  92  CYS   A SG  
1766 N N   . LEU   A 93  ? 0.1269 0.1242 0.1149 -0.0101 0.0073  0.0144  93  LEU   A N   
1767 C CA  . LEU   A 93  ? 0.1184 0.1175 0.1160 -0.0061 0.0017  0.0110  93  LEU   A CA  
1768 C C   . LEU   A 93  ? 0.1104 0.1092 0.1124 -0.0045 0.0039  0.0051  93  LEU   A C   
1769 O O   . LEU   A 93  ? 0.1143 0.1224 0.1070 -0.0057 0.0051  0.0131  93  LEU   A O   
1770 C CB  . LEU   A 93  ? 0.1228 0.1183 0.1310 -0.0057 -0.0005 0.0189  93  LEU   A CB  
1771 C CG  . LEU   A 93  ? 0.1295 0.1197 0.1328 -0.0017 0.0016  0.0160  93  LEU   A CG  
1772 C CD1 . LEU   A 93  ? 0.1344 0.1233 0.1548 0.0007  0.0123  0.0125  93  LEU   A CD1 
1773 C CD2 . LEU   A 93  ? 0.1360 0.1173 0.1516 -0.0103 0.0038  0.0155  93  LEU   A CD2 
1785 N N   . HIS   A 94  ? 0.1075 0.1062 0.1144 -0.0040 0.0057  0.0133  94  HIS   A N   
1786 C CA  . HIS   A 94  ? 0.1067 0.1077 0.1166 -0.0010 0.0042  0.0142  94  HIS   A CA  
1787 C C   . HIS   A 94  ? 0.1017 0.1072 0.1210 -0.0002 0.0043  0.0107  94  HIS   A C   
1788 O O   . HIS   A 94  ? 0.1086 0.1286 0.1475 0.0022  0.0007  -0.0123 94  HIS   A O   
1789 C CB  . HIS   A 94  ? 0.1072 0.1034 0.1191 -0.0002 0.0034  0.0089  94  HIS   A CB  
1790 C CG  . HIS   A 94  ? 0.1142 0.1056 0.1123 -0.0024 -0.0008 0.0175  94  HIS   A CG  
1791 N ND1 . HIS   A 94  ? 0.1117 0.1091 0.1165 -0.0047 0.0003  0.0144  94  HIS   A ND1 
1792 C CD2 . HIS   A 94  ? 0.1151 0.1206 0.1145 -0.0092 -0.0052 0.0041  94  HIS   A CD2 
1793 C CE1 . HIS   A 94  ? 0.1139 0.1160 0.1246 -0.0060 -0.0049 0.0031  94  HIS   A CE1 
1794 N NE2 . HIS   A 94  ? 0.1220 0.1208 0.1229 -0.0096 -0.0022 0.0008  94  HIS   A NE2 
1802 N N   . VAL   A 95  ? 0.1053 0.1091 0.0924 -0.0020 0.0091  0.0029  95  VAL   A N   
1803 C CA  . VAL   A 95  ? 0.1104 0.1081 0.1066 -0.0054 0.0102  0.0002  95  VAL   A CA  
1804 C C   . VAL   A 95  ? 0.1087 0.1025 0.0909 -0.0066 0.0010  0.0075  95  VAL   A C   
1805 O O   . VAL   A 95  ? 0.1179 0.1193 0.1065 0.0070  0.0110  0.0064  95  VAL   A O   
1806 C CB  . VAL   A 95  ? 0.1142 0.1108 0.1178 -0.0088 0.0048  0.0008  95  VAL   A CB  
1807 C CG1 . VAL   A 95  ? 0.1300 0.1110 0.1428 -0.0125 0.0006  0.0012  95  VAL   A CG1 
1808 C CG2 . VAL   A 95  ? 0.1144 0.1219 0.1217 -0.0162 0.0104  0.0130  95  VAL   A CG2 
1818 N N   . VAL   A 96  ? 0.1148 0.1106 0.0947 -0.0043 0.0111  0.0035  96  VAL   A N   
1819 C CA  . VAL   A 96  ? 0.1213 0.1088 0.1045 -0.0015 0.0111  0.0106  96  VAL   A CA  
1820 C C   . VAL   A 96  ? 0.1247 0.1161 0.1053 -0.0021 0.0175  0.0108  96  VAL   A C   
1821 O O   . VAL   A 96  ? 0.1360 0.1248 0.1228 -0.0052 0.0180  -0.0039 96  VAL   A O   
1822 C CB  . VAL   A 96  ? 0.1215 0.1104 0.1201 -0.0022 0.0190  0.0102  96  VAL   A CB  
1823 C CG1 . VAL   A 96  ? 0.1329 0.1238 0.1102 -0.0042 0.0209  0.0109  96  VAL   A CG1 
1824 C CG2 . VAL   A 96  ? 0.1249 0.1210 0.1293 -0.0137 0.0231  0.0060  96  VAL   A CG2 
1834 N N   A GLY   A 97  ? 0.1249 0.1204 0.1105 -0.0054 0.0131  0.0069  97  GLY   A N   
1835 N N   B GLY   A 97  ? 0.1252 0.1196 0.1108 -0.0065 0.0081  0.0066  97  GLY   A N   
1836 C CA  A GLY   A 97  ? 0.1325 0.1257 0.1211 -0.0080 0.0119  0.0107  97  GLY   A CA  
1837 C CA  B GLY   A 97  ? 0.1368 0.1234 0.1273 -0.0112 0.0009  0.0156  97  GLY   A CA  
1838 C C   A GLY   A 97  ? 0.1329 0.1336 0.1127 -0.0079 0.0125  0.0062  97  GLY   A C   
1839 C C   B GLY   A 97  ? 0.1381 0.1315 0.1176 -0.0111 -0.0067 0.0125  97  GLY   A C   
1840 O O   A GLY   A 97  ? 0.1407 0.1365 0.1242 -0.0124 0.0117  0.0102  97  GLY   A O   
1841 O O   B GLY   A 97  ? 0.1442 0.1361 0.1375 -0.0165 -0.0113 0.0206  97  GLY   A O   
1848 N N   A PRO   A 98  ? 0.1341 0.1421 0.1128 -0.0031 0.0128  0.0093  98  PRO   A N   
1849 N N   B PRO   A 98  ? 0.1428 0.1392 0.1162 -0.0074 -0.0083 0.0193  98  PRO   A N   
1850 C CA  A PRO   A 98  ? 0.1436 0.1579 0.1197 -0.0070 0.0130  0.0087  98  PRO   A CA  
1851 C CA  B PRO   A 98  ? 0.1554 0.1584 0.1220 -0.0077 -0.0055 0.0175  98  PRO   A CA  
1852 C C   A PRO   A 98  ? 0.1485 0.1663 0.1123 -0.0152 0.0133  0.0152  98  PRO   A C   
1853 C C   B PRO   A 98  ? 0.1556 0.1652 0.1004 -0.0117 -0.0138 0.0293  98  PRO   A C   
1854 O O   A PRO   A 98  ? 0.1459 0.1588 0.1309 -0.0142 0.0122  0.0145  98  PRO   A O   
1855 O O   B PRO   A 98  ? 0.1515 0.1548 0.1228 -0.0075 -0.0101 0.0269  98  PRO   A O   
1856 C CB  A PRO   A 98  ? 0.1515 0.1620 0.1188 0.0006  0.0103  -0.0044 98  PRO   A CB  
1857 C CB  B PRO   A 98  ? 0.1684 0.1644 0.1203 -0.0011 -0.0066 -0.0010 98  PRO   A CB  
1858 C CG  A PRO   A 98  ? 0.1465 0.1579 0.1189 0.0057  0.0113  -0.0061 98  PRO   A CG  
1859 C CG  B PRO   A 98  ? 0.1625 0.1597 0.1198 0.0001  -0.0098 -0.0009 98  PRO   A CG  
1860 C CD  A PRO   A 98  ? 0.1367 0.1476 0.1148 0.0028  0.0139  0.0013  98  PRO   A CD  
1861 C CD  B PRO   A 98  ? 0.1497 0.1462 0.1152 -0.0043 -0.0050 0.0111  98  PRO   A CD  
1876 N N   A ASN   A 99  ? 0.1590 0.1835 0.1164 -0.0176 0.0233  0.0249  99  ASN   A N   
1877 N N   B ASN   A 99  ? 0.1662 0.1861 0.1139 -0.0090 -0.0152 0.0403  99  ASN   A N   
1878 C CA  A ASN   A 99  ? 0.1697 0.1929 0.1271 -0.0253 0.0183  0.0391  99  ASN   A CA  
1879 C CA  B ASN   A 99  ? 0.1802 0.1957 0.1200 -0.0148 -0.0231 0.0534  99  ASN   A CA  
1880 C C   A ASN   A 99  ? 0.1779 0.2181 0.1156 -0.0280 0.0271  0.0493  99  ASN   A C   
1881 C C   B ASN   A 99  ? 0.1988 0.2236 0.1190 -0.0219 -0.0171 0.0489  99  ASN   A C   
1882 O O   A ASN   A 99  ? 0.1825 0.2298 0.1170 -0.0225 0.0250  0.0469  99  ASN   A O   
1883 O O   B ASN   A 99  ? 0.2084 0.2490 0.1386 -0.0177 -0.0295 0.0543  99  ASN   A O   
1884 C CB  A ASN   A 99  ? 0.1710 0.1857 0.1581 -0.0254 0.0110  0.0317  99  ASN   A CB  
1885 C CB  B ASN   A 99  ? 0.1760 0.1925 0.1353 -0.0088 -0.0215 0.0524  99  ASN   A CB  
1886 C CG  A ASN   A 99  ? 0.1728 0.1773 0.1681 -0.0265 0.0074  0.0184  99  ASN   A CG  
1887 C CG  B ASN   A 99  ? 0.1743 0.1890 0.1298 -0.0031 -0.0256 0.0409  99  ASN   A CG  
1888 O OD1 A ASN   A 99  ? 0.1786 0.1852 0.1793 -0.0180 0.0040  0.0157  99  ASN   A OD1 
1889 O OD1 B ASN   A 99  ? 0.1846 0.2009 0.1380 0.0050  -0.0326 0.0329  99  ASN   A OD1 
1890 N ND2 A ASN   A 99  ? 0.1776 0.1756 0.1825 -0.0269 0.0006  0.0118  99  ASN   A ND2 
1891 N ND2 B ASN   A 99  ? 0.1737 0.1890 0.1489 -0.0028 -0.0252 0.0484  99  ASN   A ND2 
1904 N N   A VAL   A 100 ? 0.1913 0.2293 0.1243 -0.0286 0.0119  0.0487  100 VAL   A N   
1905 N N   B VAL   A 100 ? 0.2140 0.2233 0.1101 -0.0269 -0.0300 0.0221  100 VAL   A N   
1906 C CA  A VAL   A 100 ? 0.2098 0.2459 0.1545 -0.0304 0.0082  0.0509  100 VAL   A CA  
1907 C CA  B VAL   A 100 ? 0.2321 0.2245 0.1329 -0.0339 -0.0303 0.0126  100 VAL   A CA  
1908 C C   A VAL   A 100 ? 0.2174 0.2589 0.1591 -0.0329 0.0099  0.0657  100 VAL   A C   
1909 C C   B VAL   A 100 ? 0.2323 0.2240 0.1016 -0.0338 -0.0220 0.0251  100 VAL   A C   
1910 O O   A VAL   A 100 ? 0.2221 0.2673 0.1757 -0.0279 0.0167  0.0615  100 VAL   A O   
1911 O O   B VAL   A 100 ? 0.2456 0.2254 0.1234 -0.0295 -0.0074 0.0242  100 VAL   A O   
1912 C CB  A VAL   A 100 ? 0.2263 0.2503 0.1851 -0.0304 -0.0012 0.0401  100 VAL   A CB  
1913 C CB  B VAL   A 100 ? 0.2549 0.2286 0.1747 -0.0417 -0.0365 0.0065  100 VAL   A CB  
1914 C CG1 A VAL   A 100 ? 0.2268 0.2552 0.1939 -0.0291 -0.0013 0.0415  100 VAL   A CG1 
1915 C CG1 B VAL   A 100 ? 0.2578 0.2367 0.1940 -0.0386 -0.0345 0.0069  100 VAL   A CG1 
1916 C CG2 A VAL   A 100 ? 0.2386 0.2526 0.1983 -0.0317 -0.0039 0.0315  100 VAL   A CG2 
1917 C CG2 B VAL   A 100 ? 0.2708 0.2299 0.1846 -0.0469 -0.0347 0.0022  100 VAL   A CG2 
1936 N N   A ASN   A 101 ? 0.2277 0.2653 0.1728 -0.0368 0.0023  0.0783  101 ASN   A N   
1937 N N   B ASN   A 101 ? 0.2261 0.2277 0.1023 -0.0379 -0.0266 0.0366  101 ASN   A N   
1938 C CA  A ASN   A 101 ? 0.2470 0.2731 0.1919 -0.0383 0.0040  0.0850  101 ASN   A CA  
1939 C CA  B ASN   A 101 ? 0.2340 0.2423 0.1124 -0.0372 -0.0285 0.0429  101 ASN   A CA  
1940 C C   A ASN   A 101 ? 0.2673 0.2858 0.1974 -0.0413 0.0176  0.0927  101 ASN   A C   
1941 C C   B ASN   A 101 ? 0.2517 0.2698 0.1326 -0.0535 -0.0100 0.0491  101 ASN   A C   
1942 O O   A ASN   A 101 ? 0.2802 0.2867 0.2080 -0.0389 0.0184  0.0926  101 ASN   A O   
1943 O O   B ASN   A 101 ? 0.2693 0.2767 0.1800 -0.0505 -0.0030 0.0393  101 ASN   A O   
1944 C CB  A ASN   A 101 ? 0.2471 0.2674 0.2010 -0.0358 -0.0089 0.0762  101 ASN   A CB  
1945 C CB  B ASN   A 101 ? 0.2307 0.2381 0.1290 -0.0247 -0.0454 0.0237  101 ASN   A CB  
1946 C CG  A ASN   A 101 ? 0.2473 0.2603 0.2081 -0.0345 -0.0145 0.0630  101 ASN   A CG  
1947 C CG  B ASN   A 101 ? 0.2262 0.2366 0.1500 -0.0182 -0.0598 0.0088  101 ASN   A CG  
1948 O OD1 A ASN   A 101 ? 0.2478 0.2660 0.2204 -0.0296 -0.0105 0.0425  101 ASN   A OD1 
1949 O OD1 B ASN   A 101 ? 0.2267 0.2524 0.1717 -0.0088 -0.0667 -0.0125 101 ASN   A OD1 
1950 N ND2 A ASN   A 101 ? 0.2498 0.2511 0.2056 -0.0380 -0.0127 0.0718  101 ASN   A ND2 
1951 N ND2 B ASN   A 101 ? 0.2189 0.2260 0.1535 -0.0218 -0.0610 0.0169  101 ASN   A ND2 
1964 N N   A LYS   A 102 ? 0.2713 0.2987 0.2165 -0.0466 0.0264  0.0854  102 LYS   A N   
1965 N N   B LYS   A 102 ? 0.2491 0.2945 0.1491 -0.0730 -0.0063 0.0370  102 LYS   A N   
1966 C CA  A LYS   A 102 ? 0.2786 0.3109 0.2303 -0.0474 0.0275  0.0731  102 LYS   A CA  
1967 C CA  B LYS   A 102 ? 0.2560 0.3228 0.1575 -0.0801 0.0026  0.0386  102 LYS   A CA  
1968 C C   A LYS   A 102 ? 0.2852 0.3197 0.2227 -0.0408 0.0286  0.0648  102 LYS   A C   
1969 C C   B LYS   A 102 ? 0.2635 0.3436 0.1510 -0.0718 0.0296  0.0291  102 LYS   A C   
1970 O O   A LYS   A 102 ? 0.2884 0.3228 0.2278 -0.0361 0.0314  0.0694  102 LYS   A O   
1971 O O   B LYS   A 102 ? 0.2669 0.3483 0.1610 -0.0635 0.0380  0.0196  102 LYS   A O   
1972 C CB  A LYS   A 102 ? 0.2816 0.3133 0.2475 -0.0539 0.0246  0.0669  102 LYS   A CB  
1973 C CB  B LYS   A 102 ? 0.2607 0.3261 0.1754 -0.0921 -0.0101 0.0428  102 LYS   A CB  
1974 C CG  A LYS   A 102 ? 0.2840 0.3127 0.2617 -0.0589 0.0212  0.0572  102 LYS   A CG  
1975 C CG  B LYS   A 102 ? 0.2650 0.3275 0.1856 -0.1044 -0.0217 0.0431  102 LYS   A CG  
1976 C CD  A LYS   A 102 ? 0.2877 0.3128 0.2777 -0.0626 0.0176  0.0454  102 LYS   A CD  
1977 C CD  B LYS   A 102 ? 0.2721 0.3294 0.1970 -0.1139 -0.0335 0.0437  102 LYS   A CD  
1978 C CE  A LYS   A 102 ? 0.2923 0.3123 0.2881 -0.0648 0.0126  0.0397  102 LYS   A CE  
1979 C CE  B LYS   A 102 ? 0.2816 0.3299 0.2075 -0.1164 -0.0406 0.0492  102 LYS   A CE  
1980 N NZ  A LYS   A 102 ? 0.2958 0.3118 0.2970 -0.0676 0.0129  0.0368  102 LYS   A NZ  
1981 N NZ  B LYS   A 102 ? 0.2871 0.3278 0.2037 -0.1221 -0.0381 0.0548  102 LYS   A NZ  
2008 N N   A GLY   A 103 ? 0.2884 0.3248 0.2187 -0.0367 0.0224  0.0449  103 GLY   A N   
2009 N N   B GLY   A 103 ? 0.2701 0.3614 0.1543 -0.0641 0.0330  0.0068  103 GLY   A N   
2010 C CA  A GLY   A 103 ? 0.2910 0.3262 0.2085 -0.0357 0.0167  0.0381  103 GLY   A CA  
2011 C CA  B GLY   A 103 ? 0.2782 0.3757 0.1621 -0.0518 0.0390  -0.0108 103 GLY   A CA  
2012 C C   A GLY   A 103 ? 0.2907 0.3287 0.1989 -0.0379 0.0158  0.0305  103 GLY   A C   
2013 C C   B GLY   A 103 ? 0.2819 0.3870 0.1727 -0.0441 0.0523  -0.0224 103 GLY   A C   
2014 O O   A GLY   A 103 ? 0.2939 0.3318 0.2102 -0.0377 0.0150  0.0195  103 GLY   A O   
2015 O O   B GLY   A 103 ? 0.2892 0.3909 0.1817 -0.0408 0.0614  -0.0369 103 GLY   A O   
2022 N N   A GLU   A 104 ? 0.2862 0.3267 0.1754 -0.0420 0.0090  0.0310  104 GLU   A N   
2023 N N   B GLU   A 104 ? 0.2750 0.3911 0.1649 -0.0438 0.0506  -0.0161 104 GLU   A N   
2024 C CA  A GLU   A 104 ? 0.2771 0.3223 0.1578 -0.0513 0.0058  0.0218  104 GLU   A CA  
2025 C CA  B GLU   A 104 ? 0.2634 0.3909 0.1743 -0.0480 0.0510  -0.0164 104 GLU   A CA  
2026 C C   A GLU   A 104 ? 0.2813 0.3321 0.1520 -0.0489 0.0155  0.0031  104 GLU   A C   
2027 C C   B GLU   A 104 ? 0.2762 0.4082 0.1828 -0.0543 0.0512  -0.0316 104 GLU   A C   
2028 O O   A GLU   A 104 ? 0.2792 0.3312 0.1594 -0.0495 0.0113  -0.0022 104 GLU   A O   
2029 O O   B GLU   A 104 ? 0.2765 0.4129 0.1989 -0.0604 0.0415  -0.0450 104 GLU   A O   
2030 C CB  A GLU   A 104 ? 0.2631 0.3092 0.1473 -0.0603 -0.0016 0.0387  104 GLU   A CB  
2031 C CB  B GLU   A 104 ? 0.2369 0.3687 0.1581 -0.0470 0.0528  0.0022  104 GLU   A CB  
2032 C CG  A GLU   A 104 ? 0.2524 0.2979 0.1582 -0.0664 -0.0056 0.0535  104 GLU   A CG  
2033 C CG  B GLU   A 104 ? 0.2150 0.3455 0.1632 -0.0445 0.0480  0.0186  104 GLU   A CG  
2034 C CD  A GLU   A 104 ? 0.2418 0.2861 0.1616 -0.0703 -0.0078 0.0653  104 GLU   A CD  
2035 C CD  B GLU   A 104 ? 0.1953 0.3216 0.1690 -0.0369 0.0387  0.0323  104 GLU   A CD  
2036 O OE1 A GLU   A 104 ? 0.2364 0.2824 0.1478 -0.0714 -0.0143 0.0763  104 GLU   A OE1 
2037 O OE1 B GLU   A 104 ? 0.1779 0.3062 0.1396 -0.0329 0.0357  0.0258  104 GLU   A OE1 
2038 O OE2 A GLU   A 104 ? 0.2425 0.2795 0.1708 -0.0711 -0.0041 0.0664  104 GLU   A OE2 
2039 O OE2 B GLU   A 104 ? 0.2068 0.3166 0.1892 -0.0324 0.0233  0.0488  104 GLU   A OE2 
2052 N N   A ASP   A 105 ? 0.2883 0.3435 0.1621 -0.0454 0.0276  -0.0108 105 ASP   A N   
2053 N N   B ASP   A 105 ? 0.2857 0.4179 0.1876 -0.0508 0.0535  -0.0418 105 ASP   A N   
2054 C CA  A ASP   A 105 ? 0.2925 0.3523 0.1920 -0.0390 0.0347  -0.0274 105 ASP   A CA  
2055 C CA  B ASP   A 105 ? 0.2927 0.4256 0.2106 -0.0497 0.0427  -0.0561 105 ASP   A CA  
2056 C C   A ASP   A 105 ? 0.2775 0.3468 0.1655 -0.0438 0.0312  -0.0360 105 ASP   A C   
2057 C C   B ASP   A 105 ? 0.2687 0.4127 0.1806 -0.0580 0.0312  -0.0699 105 ASP   A C   
2058 O O   A ASP   A 105 ? 0.2674 0.3430 0.1235 -0.0460 0.0357  -0.0486 105 ASP   A O   
2059 O O   B ASP   A 105 ? 0.2540 0.4029 0.1409 -0.0581 0.0317  -0.0873 105 ASP   A O   
2060 C CB  A ASP   A 105 ? 0.3087 0.3633 0.2494 -0.0305 0.0410  -0.0362 105 ASP   A CB  
2061 C CB  B ASP   A 105 ? 0.3174 0.4409 0.2667 -0.0418 0.0364  -0.0646 105 ASP   A CB  
2062 C CG  A ASP   A 105 ? 0.3226 0.3731 0.2967 -0.0227 0.0431  -0.0454 105 ASP   A CG  
2063 C CG  B ASP   A 105 ? 0.3394 0.4530 0.3096 -0.0362 0.0285  -0.0755 105 ASP   A CG  
2064 O OD1 A ASP   A 105 ? 0.3321 0.3781 0.3142 -0.0210 0.0420  -0.0505 105 ASP   A OD1 
2065 O OD1 B ASP   A 105 ? 0.3467 0.4585 0.3126 -0.0366 0.0265  -0.0864 105 ASP   A OD1 
2066 O OD2 A ASP   A 105 ? 0.3250 0.3765 0.3172 -0.0216 0.0486  -0.0454 105 ASP   A OD2 
2067 O OD2 B ASP   A 105 ? 0.3520 0.4567 0.3340 -0.0344 0.0233  -0.0746 105 ASP   A OD2 
2076 N N   A ILE   A 106 ? 0.2724 0.3444 0.1907 -0.0460 0.0158  -0.0302 106 ILE   A N   
2077 N N   B ILE   A 106 ? 0.2565 0.4015 0.2087 -0.0644 0.0047  -0.0620 106 ILE   A N   
2078 C CA  A ILE   A 106 ? 0.2639 0.3375 0.2177 -0.0501 0.0046  -0.0339 106 ILE   A CA  
2079 C CA  B ILE   A 106 ? 0.2347 0.3818 0.2253 -0.0734 -0.0150 -0.0733 106 ILE   A CA  
2080 C C   A ILE   A 106 ? 0.2585 0.3237 0.2329 -0.0557 0.0114  -0.0453 106 ILE   A C   
2081 C C   B ILE   A 106 ? 0.2105 0.3470 0.2254 -0.0911 -0.0058 -0.1087 106 ILE   A C   
2082 O O   A ILE   A 106 ? 0.2525 0.3218 0.2266 -0.0582 0.0143  -0.0488 106 ILE   A O   
2083 O O   B ILE   A 106 ? 0.1888 0.3349 0.2204 -0.0962 0.0096  -0.1136 106 ILE   A O   
2084 C CB  A ILE   A 106 ? 0.2638 0.3443 0.2497 -0.0456 -0.0104 -0.0215 106 ILE   A CB  
2085 C CB  B ILE   A 106 ? 0.2407 0.3946 0.2623 -0.0628 -0.0326 -0.0421 106 ILE   A CB  
2086 C CG1 A ILE   A 106 ? 0.2581 0.3474 0.2668 -0.0407 -0.0135 -0.0074 106 ILE   A CG1 
2087 C CG1 B ILE   A 106 ? 0.2369 0.3989 0.2876 -0.0549 -0.0328 -0.0181 106 ILE   A CG1 
2088 C CG2 A ILE   A 106 ? 0.2671 0.3453 0.2597 -0.0455 -0.0167 -0.0222 106 ILE   A CG2 
2089 C CG2 B ILE   A 106 ? 0.2468 0.3977 0.2737 -0.0616 -0.0416 -0.0405 106 ILE   A CG2 
2090 C CD1 A ILE   A 106 ? 0.2570 0.3484 0.2738 -0.0342 -0.0112 -0.0017 106 ILE   A CD1 
2091 C CD1 B ILE   A 106 ? 0.2413 0.4009 0.3011 -0.0439 -0.0254 -0.0062 106 ILE   A CD1 
2114 N N   A GLN   A 107 ? 0.2620 0.3101 0.2601 -0.0545 0.0178  -0.0520 107 GLN   A N   
2115 N N   B GLN   A 107 ? 0.2211 0.3273 0.2520 -0.0879 -0.0001 -0.1244 107 GLN   A N   
2116 C CA  A GLN   A 107 ? 0.2650 0.2942 0.3038 -0.0476 0.0312  -0.0555 107 GLN   A CA  
2117 C CA  B GLN   A 107 ? 0.2365 0.3027 0.3077 -0.0668 0.0288  -0.1179 107 GLN   A CA  
2118 C C   A GLN   A 107 ? 0.2432 0.2583 0.2824 -0.0418 0.0432  -0.0407 107 GLN   A C   
2119 C C   B GLN   A 107 ? 0.2181 0.2553 0.2965 -0.0521 0.0534  -0.0928 107 GLN   A C   
2120 O O   A GLN   A 107 ? 0.2501 0.2587 0.3183 -0.0404 0.0458  -0.0354 107 GLN   A O   
2121 O O   B GLN   A 107 ? 0.2282 0.2491 0.3580 -0.0445 0.0655  -0.0795 107 GLN   A O   
2122 C CB  A GLN   A 107 ? 0.2863 0.3126 0.3670 -0.0477 0.0256  -0.0620 107 GLN   A CB  
2123 C CB  B GLN   A 107 ? 0.2702 0.3259 0.3877 -0.0623 0.0180  -0.1082 107 GLN   A CB  
2124 C CG  A GLN   A 107 ? 0.3054 0.3304 0.4329 -0.0468 0.0200  -0.0641 107 GLN   A CG  
2125 C CG  B GLN   A 107 ? 0.2976 0.3473 0.4713 -0.0585 0.0053  -0.0913 107 GLN   A CG  
2126 C CD  A GLN   A 107 ? 0.3203 0.3446 0.4885 -0.0457 0.0203  -0.0599 107 GLN   A CD  
2127 C CD  B GLN   A 107 ? 0.3187 0.3644 0.5407 -0.0548 -0.0009 -0.0706 107 GLN   A CD  
2128 O OE1 A GLN   A 107 ? 0.3259 0.3513 0.5095 -0.0433 0.0222  -0.0619 107 GLN   A OE1 
2129 O OE1 B GLN   A 107 ? 0.3323 0.3706 0.5700 -0.0511 -0.0019 -0.0633 107 GLN   A OE1 
2130 N NE2 A GLN   A 107 ? 0.3270 0.3490 0.5067 -0.0461 0.0187  -0.0581 107 GLN   A NE2 
2131 N NE2 B GLN   A 107 ? 0.3258 0.3710 0.5625 -0.0558 -0.0014 -0.0651 107 GLN   A NE2 
2148 N N   A LEU   A 108 ? 0.2121 0.2184 0.2346 -0.0396 0.0461  -0.0344 108 LEU   A N   
2149 N N   B LEU   A 108 ? 0.1890 0.2053 0.2259 -0.0453 0.0584  -0.0893 108 LEU   A N   
2150 C CA  A LEU   A 108 ? 0.1845 0.1821 0.2032 -0.0251 0.0423  -0.0127 108 LEU   A CA  
2151 C CA  B LEU   A 108 ? 0.1727 0.1706 0.2020 -0.0155 0.0501  -0.0300 108 LEU   A CA  
2152 C C   A LEU   A 108 ? 0.1599 0.1506 0.1901 -0.0118 0.0361  0.0075  108 LEU   A C   
2153 C C   B LEU   A 108 ? 0.1505 0.1375 0.1914 -0.0041 0.0388  0.0045  108 LEU   A C   
2154 O O   A LEU   A 108 ? 0.1573 0.1473 0.1919 -0.0077 0.0364  0.0097  108 LEU   A O   
2155 O O   B LEU   A 108 ? 0.1437 0.1302 0.1989 0.0061  0.0367  0.0101  108 LEU   A O   
2156 C CB  A LEU   A 108 ? 0.1819 0.1833 0.1939 -0.0338 0.0460  -0.0165 108 LEU   A CB  
2157 C CB  B LEU   A 108 ? 0.1796 0.1786 0.2015 -0.0153 0.0543  -0.0147 108 LEU   A CB  
2158 C CG  A LEU   A 108 ? 0.1825 0.1937 0.1969 -0.0400 0.0506  -0.0195 108 LEU   A CG  
2159 C CG  B LEU   A 108 ? 0.1949 0.2001 0.2159 -0.0153 0.0582  -0.0052 108 LEU   A CG  
2160 C CD1 A LEU   A 108 ? 0.1835 0.1951 0.1930 -0.0400 0.0496  -0.0196 108 LEU   A CD1 
2161 C CD1 B LEU   A 108 ? 0.2034 0.2042 0.2095 -0.0156 0.0615  0.0025  108 LEU   A CD1 
2162 C CD2 A LEU   A 108 ? 0.1794 0.1967 0.2082 -0.0490 0.0526  -0.0152 108 LEU   A CD2 
2163 C CD2 B LEU   A 108 ? 0.2018 0.2108 0.2421 -0.0159 0.0509  0.0033  108 LEU   A CD2 
2186 N N   . LEU   A 109 ? 0.1445 0.1369 0.1781 0.0008  0.0305  0.0157  109 LEU   A N   
2187 C CA  . LEU   A 109 ? 0.1369 0.1274 0.1624 0.0009  0.0121  0.0125  109 LEU   A CA  
2188 C C   . LEU   A 109 ? 0.1245 0.1223 0.1480 -0.0042 0.0160  0.0076  109 LEU   A C   
2189 O O   . LEU   A 109 ? 0.1322 0.1141 0.1612 -0.0006 0.0003  -0.0005 109 LEU   A O   
2190 C CB  . LEU   A 109 ? 0.1420 0.1378 0.1765 0.0095  0.0089  0.0250  109 LEU   A CB  
2191 C CG  . LEU   A 109 ? 0.1306 0.1414 0.1733 0.0055  0.0133  0.0302  109 LEU   A CG  
2192 C CD1 . LEU   A 109 ? 0.1431 0.1278 0.1857 0.0060  0.0200  0.0159  109 LEU   A CD1 
2193 C CD2 . LEU   A 109 ? 0.1361 0.1624 0.1824 0.0019  0.0142  0.0293  109 LEU   A CD2 
2206 N N   . LYS   A 110 ? 0.1257 0.1244 0.1443 -0.0057 0.0018  0.0062  110 LYS   A N   
2207 C CA  . LYS   A 110 ? 0.1243 0.1170 0.1548 -0.0054 0.0021  0.0057  110 LYS   A CA  
2208 C C   . LYS   A 110 ? 0.1265 0.1125 0.1457 -0.0062 0.0047  -0.0010 110 LYS   A C   
2209 O O   . LYS   A 110 ? 0.1234 0.1131 0.1445 -0.0076 0.0068  -0.0017 110 LYS   A O   
2210 C CB  . LYS   A 110 ? 0.1348 0.1227 0.1665 -0.0013 -0.0053 -0.0028 110 LYS   A CB  
2211 C CG  . LYS   A 110 ? 0.1353 0.1198 0.1799 -0.0020 -0.0001 -0.0043 110 LYS   A CG  
2212 C CD  . LYS   A 110 ? 0.1374 0.1250 0.1913 -0.0107 -0.0003 -0.0076 110 LYS   A CD  
2213 C CE  . LYS   A 110 ? 0.1465 0.1298 0.2123 -0.0044 0.0165  -0.0143 110 LYS   A CE  
2214 N NZ  . LYS   A 110 ? 0.1511 0.1366 0.2157 -0.0138 0.0206  -0.0127 110 LYS   A NZ  
2228 N N   . SER   A 111 ? 0.1268 0.1148 0.1466 -0.0042 0.0067  0.0039  111 SER   A N   
2229 C CA  . SER   A 111 ? 0.1224 0.1220 0.1539 -0.0042 0.0189  0.0050  111 SER   A CA  
2230 C C   . SER   A 111 ? 0.1181 0.1097 0.1511 -0.0057 0.0114  0.0079  111 SER   A C   
2231 O O   . SER   A 111 ? 0.1287 0.1129 0.1518 -0.0045 0.0105  0.0070  111 SER   A O   
2232 C CB  . SER   A 111 ? 0.1403 0.1428 0.1631 -0.0046 0.0185  -0.0057 111 SER   A CB  
2233 O OG  . SER   A 111 ? 0.1831 0.1657 0.1623 -0.0002 0.0279  -0.0193 111 SER   A OG  
2239 N N   . ALA   A 112 ? 0.1206 0.1066 0.1550 -0.0015 0.0186  0.0083  112 ALA   A N   
2240 C CA  . ALA   A 112 ? 0.1250 0.1058 0.1555 -0.0080 0.0185  -0.0023 112 ALA   A CA  
2241 C C   . ALA   A 112 ? 0.1148 0.1013 0.1664 -0.0035 0.0094  -0.0004 112 ALA   A C   
2242 O O   . ALA   A 112 ? 0.1173 0.1068 0.1591 -0.0086 0.0151  0.0043  112 ALA   A O   
2243 C CB  . ALA   A 112 ? 0.1310 0.1058 0.1605 -0.0032 0.0143  0.0001  112 ALA   A CB  
2249 N N   . TYR   A 113 ? 0.1091 0.1079 0.1542 0.0000  0.0109  0.0037  113 TYR   A N   
2250 C CA  . TYR   A 113 ? 0.1065 0.1049 0.1607 -0.0041 0.0220  0.0098  113 TYR   A CA  
2251 C C   . TYR   A 113 ? 0.1064 0.1077 0.1457 -0.0073 0.0112  0.0077  113 TYR   A C   
2252 O O   . TYR   A 113 ? 0.1098 0.1123 0.1566 -0.0050 0.0116  0.0041  113 TYR   A O   
2253 C CB  . TYR   A 113 ? 0.1117 0.1161 0.1581 -0.0047 0.0034  0.0198  113 TYR   A CB  
2254 C CG  . TYR   A 113 ? 0.1107 0.1173 0.1488 -0.0058 0.0129  0.0182  113 TYR   A CG  
2255 C CD1 . TYR   A 113 ? 0.1181 0.1287 0.1453 -0.0025 0.0103  0.0253  113 TYR   A CD1 
2256 C CD2 . TYR   A 113 ? 0.1186 0.1237 0.1431 -0.0067 0.0038  0.0210  113 TYR   A CD2 
2257 C CE1 . TYR   A 113 ? 0.1175 0.1344 0.1450 -0.0009 0.0114  0.0285  113 TYR   A CE1 
2258 C CE2 . TYR   A 113 ? 0.1184 0.1332 0.1491 -0.0091 0.0040  0.0235  113 TYR   A CE2 
2259 C CZ  . TYR   A 113 ? 0.1177 0.1292 0.1438 0.0026  0.0145  0.0330  113 TYR   A CZ  
2260 O OH  . TYR   A 113 ? 0.1191 0.1418 0.1588 0.0096  0.0134  0.0217  113 TYR   A OH  
2270 N N   . GLU   A 114 ? 0.1119 0.1085 0.1489 -0.0039 0.0109  0.0069  114 GLU   A N   
2271 C CA  . GLU   A 114 ? 0.1124 0.1026 0.1610 0.0004  0.0150  0.0072  114 GLU   A CA  
2272 C C   . GLU   A 114 ? 0.1076 0.1104 0.1671 0.0047  0.0177  0.0045  114 GLU   A C   
2273 O O   . GLU   A 114 ? 0.1160 0.1128 0.1523 0.0014  0.0091  0.0087  114 GLU   A O   
2274 C CB  . GLU   A 114 ? 0.1162 0.1059 0.1603 -0.0051 0.0070  0.0084  114 GLU   A CB  
2275 C CG  . GLU   A 114 ? 0.1204 0.1122 0.1647 0.0004  0.0106  0.0015  114 GLU   A CG  
2276 C CD  . GLU   A 114 ? 0.1284 0.1121 0.1538 -0.0057 0.0083  -0.0022 114 GLU   A CD  
2277 O OE1 . GLU   A 114 ? 0.1321 0.1105 0.1595 -0.0056 0.0130  -0.0057 114 GLU   A OE1 
2278 O OE2 . GLU   A 114 ? 0.1472 0.1188 0.1781 -0.0106 0.0141  -0.0111 114 GLU   A OE2 
2285 N N   . ASN   A 115 ? 0.1128 0.1092 0.1473 -0.0054 0.0123  0.0023  115 ASN   A N   
2286 C CA  . ASN   A 115 ? 0.1137 0.1128 0.1557 -0.0083 0.0155  0.0087  115 ASN   A CA  
2287 C C   . ASN   A 115 ? 0.1157 0.1093 0.1521 -0.0089 0.0060  0.0081  115 ASN   A C   
2288 O O   . ASN   A 115 ? 0.1171 0.1243 0.1434 -0.0062 0.0111  0.0133  115 ASN   A O   
2289 C CB  . ASN   A 115 ? 0.1243 0.1162 0.1486 -0.0172 0.0156  -0.0039 115 ASN   A CB  
2290 C CG  . ASN   A 115 ? 0.1210 0.1389 0.1547 -0.0158 0.0196  0.0064  115 ASN   A CG  
2291 O OD1 . ASN   A 115 ? 0.1300 0.2335 0.1743 -0.0146 0.0203  0.0188  115 ASN   A OD1 
2292 N ND2 . ASN   A 115 ? 0.1228 0.1215 0.1582 -0.0134 0.0321  0.0038  115 ASN   A ND2 
2299 N N   . PHE   A 116 ? 0.1148 0.1146 0.1508 -0.0046 0.0097  0.0150  116 PHE   A N   
2300 C CA  . PHE   A 116 ? 0.1106 0.1203 0.1384 -0.0020 0.0177  0.0108  116 PHE   A CA  
2301 C C   . PHE   A 116 ? 0.1082 0.1262 0.1485 -0.0050 0.0184  0.0180  116 PHE   A C   
2302 O O   . PHE   A 116 ? 0.1172 0.1310 0.1506 0.0001  0.0144  0.0243  116 PHE   A O   
2303 C CB  . PHE   A 116 ? 0.1158 0.1128 0.1531 -0.0064 0.0177  0.0129  116 PHE   A CB  
2304 C CG  . PHE   A 116 ? 0.1120 0.1129 0.1346 -0.0054 0.0150  0.0070  116 PHE   A CG  
2305 C CD1 . PHE   A 116 ? 0.1159 0.1148 0.1382 -0.0071 0.0198  0.0077  116 PHE   A CD1 
2306 C CD2 . PHE   A 116 ? 0.1160 0.1177 0.1629 -0.0032 0.0174  0.0153  116 PHE   A CD2 
2307 C CE1 . PHE   A 116 ? 0.1225 0.1105 0.1462 -0.0162 0.0103  0.0062  116 PHE   A CE1 
2308 C CE2 . PHE   A 116 ? 0.1173 0.1163 0.1636 -0.0014 0.0195  0.0093  116 PHE   A CE2 
2309 C CZ  . PHE   A 116 ? 0.1206 0.1082 0.1473 -0.0039 0.0065  0.0035  116 PHE   A CZ  
2319 N N   . ASN   A 117 ? 0.1113 0.1175 0.1627 0.0011  0.0158  0.0206  117 ASN   A N   
2320 C CA  . ASN   A 117 ? 0.1094 0.1142 0.1665 -0.0006 0.0148  0.0226  117 ASN   A CA  
2321 C C   . ASN   A 117 ? 0.1141 0.1262 0.1791 -0.0011 0.0168  0.0221  117 ASN   A C   
2322 O O   . ASN   A 117 ? 0.1273 0.1312 0.1911 -0.0045 -0.0051 0.0296  117 ASN   A O   
2323 C CB  . ASN   A 117 ? 0.1182 0.1168 0.1683 -0.0006 0.0159  0.0226  117 ASN   A CB  
2324 C CG  . ASN   A 117 ? 0.1139 0.1152 0.1653 -0.0037 0.0183  0.0180  117 ASN   A CG  
2325 O OD1 . ASN   A 117 ? 0.1166 0.1409 0.1716 -0.0121 0.0119  0.0128  117 ASN   A OD1 
2326 N ND2 . ASN   A 117 ? 0.1108 0.1187 0.1661 0.0002  0.0167  0.0198  117 ASN   A ND2 
2333 N N   . GLN   A 118 ? 0.1140 0.1253 0.1728 -0.0034 0.0002  0.0210  118 GLN   A N   
2334 C CA  . GLN   A 118 ? 0.1227 0.1341 0.1693 -0.0030 -0.0032 0.0215  118 GLN   A CA  
2335 C C   . GLN   A 118 ? 0.1260 0.1390 0.1720 -0.0065 -0.0034 0.0195  118 GLN   A C   
2336 O O   . GLN   A 118 ? 0.1283 0.1735 0.1980 0.0018  -0.0096 0.0060  118 GLN   A O   
2337 C CB  . GLN   A 118 ? 0.1177 0.1367 0.1839 -0.0025 0.0052  0.0199  118 GLN   A CB  
2338 C CG  . GLN   A 118 ? 0.1128 0.1414 0.1908 -0.0049 0.0131  0.0199  118 GLN   A CG  
2339 C CD  . GLN   A 118 ? 0.1161 0.1420 0.2004 -0.0031 0.0086  0.0173  118 GLN   A CD  
2340 O OE1 . GLN   A 118 ? 0.1217 0.1524 0.2160 0.0099  0.0001  0.0053  118 GLN   A OE1 
2341 N NE2 . GLN   A 118 ? 0.1254 0.1356 0.1829 -0.0002 0.0002  0.0226  118 GLN   A NE2 
2350 N N   . HIS   A 119 ? 0.1291 0.1408 0.1557 -0.0072 0.0018  0.0245  119 HIS   A N   
2351 C CA  . HIS   A 119 ? 0.1341 0.1491 0.1543 -0.0077 0.0004  0.0239  119 HIS   A CA  
2352 C C   . HIS   A 119 ? 0.1433 0.1628 0.1507 -0.0051 0.0038  0.0319  119 HIS   A C   
2353 O O   . HIS   A 119 ? 0.1427 0.1667 0.1474 -0.0197 -0.0024 0.0269  119 HIS   A O   
2354 C CB  . HIS   A 119 ? 0.1408 0.1458 0.1852 -0.0050 0.0169  0.0316  119 HIS   A CB  
2355 C CG  . HIS   A 119 ? 0.1443 0.1479 0.2307 0.0002  0.0196  0.0381  119 HIS   A CG  
2356 N ND1 . HIS   A 119 ? 0.1589 0.1663 0.2764 -0.0103 0.0180  0.0230  119 HIS   A ND1 
2357 C CD2 . HIS   A 119 ? 0.1554 0.1573 0.2385 0.0140  0.0423  0.0581  119 HIS   A CD2 
2358 C CE1 . HIS   A 119 ? 0.1642 0.1639 0.2912 -0.0114 0.0365  0.0438  119 HIS   A CE1 
2359 N NE2 . HIS   A 119 ? 0.1697 0.1636 0.2815 0.0042  0.0541  0.0638  119 HIS   A NE2 
2367 N N   . GLU   A 120 ? 0.1469 0.1789 0.1568 -0.0045 -0.0062 0.0517  120 GLU   A N   
2368 C CA  . GLU   A 120 ? 0.1739 0.2076 0.1885 0.0046  0.0020  0.0860  120 GLU   A CA  
2369 C C   . GLU   A 120 ? 0.1582 0.1871 0.1696 -0.0093 0.0061  0.0783  120 GLU   A C   
2370 O O   . GLU   A 120 ? 0.1533 0.1808 0.1721 -0.0172 0.0012  0.0639  120 GLU   A O   
2371 C CB  . GLU   A 120 ? 0.2265 0.2707 0.2398 0.0185  0.0046  0.1398  120 GLU   A CB  
2372 C CG  . GLU   A 120 ? 0.2936 0.3226 0.3398 0.0329  0.0032  0.1491  120 GLU   A CG  
2373 C CD  . GLU   A 120 ? 0.3810 0.3923 0.4481 0.0433  0.0137  0.1384  120 GLU   A CD  
2374 O OE1 . GLU   A 120 ? 0.3921 0.3986 0.4841 0.0465  0.0166  0.1316  120 GLU   A OE1 
2375 O OE2 . GLU   A 120 ? 0.4556 0.4556 0.4913 0.0463  0.0145  0.1348  120 GLU   A OE2 
2382 N N   . VAL   A 121 ? 0.1549 0.1862 0.1399 -0.0078 0.0088  0.0572  121 VAL   A N   
2383 C CA  . VAL   A 121 ? 0.1637 0.1936 0.1258 -0.0077 0.0191  0.0575  121 VAL   A CA  
2384 C C   . VAL   A 121 ? 0.1511 0.1784 0.1181 -0.0177 0.0141  0.0357  121 VAL   A C   
2385 O O   . VAL   A 121 ? 0.1573 0.1746 0.1370 -0.0259 0.0003  0.0319  121 VAL   A O   
2386 C CB  . VAL   A 121 ? 0.2005 0.2273 0.1703 0.0053  0.0319  0.0671  121 VAL   A CB  
2387 C CG1 . VAL   A 121 ? 0.2012 0.2471 0.1697 0.0125  0.0439  0.0657  121 VAL   A CG1 
2388 C CG2 . VAL   A 121 ? 0.2211 0.2442 0.2038 -0.0033 0.0273  0.0578  121 VAL   A CG2 
2398 N N   . LEU   A 122 ? 0.1401 0.1577 0.1278 -0.0179 0.0131  0.0309  122 LEU   A N   
2399 C CA  . LEU   A 122 ? 0.1480 0.1428 0.1255 -0.0126 0.0233  0.0269  122 LEU   A CA  
2400 C C   . LEU   A 122 ? 0.1440 0.1396 0.1242 -0.0193 0.0162  0.0279  122 LEU   A C   
2401 O O   . LEU   A 122 ? 0.1440 0.1474 0.1604 -0.0257 0.0111  0.0245  122 LEU   A O   
2402 C CB  . LEU   A 122 ? 0.1588 0.1461 0.1713 -0.0040 0.0126  0.0348  122 LEU   A CB  
2403 C CG  . LEU   A 122 ? 0.1635 0.1481 0.1534 -0.0074 0.0187  0.0300  122 LEU   A CG  
2404 C CD1 . LEU   A 122 ? 0.1752 0.1458 0.1740 -0.0145 0.0283  0.0342  122 LEU   A CD1 
2405 C CD2 . LEU   A 122 ? 0.1594 0.1434 0.1439 -0.0036 0.0284  0.0255  122 LEU   A CD2 
2417 N N   A LEU   A 123 ? 0.1410 0.1387 0.1303 -0.0182 0.0140  0.0266  123 LEU   A N   
2418 N N   B LEU   A 123 ? 0.1365 0.1416 0.1099 -0.0196 0.0096  0.0210  123 LEU   A N   
2419 C CA  A LEU   A 123 ? 0.1403 0.1347 0.1252 -0.0164 0.0142  0.0266  123 LEU   A CA  
2420 C CA  B LEU   A 123 ? 0.1360 0.1354 0.1010 -0.0164 0.0113  0.0153  123 LEU   A CA  
2421 C C   A LEU   A 123 ? 0.1296 0.1241 0.1239 -0.0198 0.0136  0.0262  123 LEU   A C   
2422 C C   B LEU   A 123 ? 0.1298 0.1311 0.0989 -0.0129 0.0108  0.0122  123 LEU   A C   
2423 O O   A LEU   A 123 ? 0.1224 0.1221 0.1176 -0.0229 0.0188  0.0101  123 LEU   A O   
2424 O O   B LEU   A 123 ? 0.1258 0.1370 0.1094 -0.0169 0.0158  0.0048  123 LEU   A O   
2425 C CB  A LEU   A 123 ? 0.1511 0.1471 0.1248 -0.0141 0.0248  0.0195  123 LEU   A CB  
2426 C CB  B LEU   A 123 ? 0.1427 0.1453 0.1091 -0.0231 0.0155  0.0122  123 LEU   A CB  
2427 C CG  A LEU   A 123 ? 0.1541 0.1594 0.1337 -0.0068 0.0203  0.0027  123 LEU   A CG  
2428 C CG  B LEU   A 123 ? 0.1473 0.1556 0.1226 -0.0207 0.0211  0.0089  123 LEU   A CG  
2429 C CD1 A LEU   A 123 ? 0.1530 0.1682 0.1433 -0.0028 0.0165  -0.0022 123 LEU   A CD1 
2430 C CD1 B LEU   A 123 ? 0.1499 0.1590 0.1414 -0.0218 0.0179  0.0055  123 LEU   A CD1 
2431 C CD2 A LEU   A 123 ? 0.1582 0.1632 0.1363 -0.0084 0.0047  -0.0021 123 LEU   A CD2 
2432 C CD2 B LEU   A 123 ? 0.1543 0.1625 0.1285 -0.0232 0.0156  0.0023  123 LEU   A CD2 
2455 N N   A ALA   A 124 ? 0.1265 0.1178 0.1241 -0.0201 0.0134  0.0338  124 ALA   A N   
2456 N N   B ALA   A 124 ? 0.1306 0.1200 0.1107 -0.0093 0.0090  0.0115  124 ALA   A N   
2457 C CA  A ALA   A 124 ? 0.1229 0.1186 0.1202 -0.0151 0.0128  0.0324  124 ALA   A CA  
2458 C CA  B ALA   A 124 ? 0.1275 0.1211 0.1152 -0.0054 0.0126  0.0101  124 ALA   A CA  
2459 C C   A ALA   A 124 ? 0.1117 0.1154 0.1262 -0.0145 0.0101  0.0187  124 ALA   A C   
2460 C C   B ALA   A 124 ? 0.1212 0.1192 0.1083 -0.0057 0.0239  0.0090  124 ALA   A C   
2461 O O   A ALA   A 124 ? 0.1069 0.1124 0.1445 -0.0146 0.0192  0.0144  124 ALA   A O   
2462 O O   B ALA   A 124 ? 0.1268 0.1260 0.1252 -0.0032 0.0243  0.0197  124 ALA   A O   
2463 C CB  A ALA   A 124 ? 0.1293 0.1219 0.1335 -0.0171 0.0159  0.0288  124 ALA   A CB  
2464 C CB  B ALA   A 124 ? 0.1240 0.1217 0.1270 -0.0037 0.0140  0.0162  124 ALA   A CB  
2475 N N   A PRO   A 125 ? 0.1101 0.1199 0.1282 -0.0080 0.0035  0.0145  125 PRO   A N   
2476 N N   B PRO   A 125 ? 0.1142 0.1195 0.1117 -0.0080 0.0197  0.0213  125 PRO   A N   
2477 C CA  A PRO   A 125 ? 0.1130 0.1152 0.1245 -0.0051 0.0024  0.0089  125 PRO   A CA  
2478 C CA  B PRO   A 125 ? 0.1194 0.1183 0.1213 -0.0084 0.0170  0.0218  125 PRO   A CA  
2479 C C   A PRO   A 125 ? 0.1041 0.1101 0.1194 -0.0034 0.0132  0.0199  125 PRO   A C   
2480 C C   B PRO   A 125 ? 0.1230 0.1274 0.1073 -0.0012 0.0062  0.0178  125 PRO   A C   
2481 O O   A PRO   A 125 ? 0.1065 0.1096 0.1176 -0.0033 0.0173  0.0160  125 PRO   A O   
2482 O O   B PRO   A 125 ? 0.1247 0.1327 0.1126 -0.0026 0.0090  0.0163  125 PRO   A O   
2483 C CB  A PRO   A 125 ? 0.1160 0.1181 0.1352 -0.0130 0.0024  0.0092  125 PRO   A CB  
2484 C CB  B PRO   A 125 ? 0.1169 0.1171 0.1316 -0.0110 0.0246  0.0223  125 PRO   A CB  
2485 C CG  A PRO   A 125 ? 0.1248 0.1214 0.1420 -0.0087 -0.0020 0.0149  125 PRO   A CG  
2486 C CG  B PRO   A 125 ? 0.1064 0.1076 0.1333 -0.0074 0.0215  0.0233  125 PRO   A CG  
2487 C CD  A PRO   A 125 ? 0.1158 0.1284 0.1373 -0.0059 -0.0010 0.0192  125 PRO   A CD  
2488 C CD  B PRO   A 125 ? 0.1100 0.1174 0.1328 -0.0086 0.0284  0.0328  125 PRO   A CD  
2503 N N   A LEU   A 126 ? 0.0961 0.1159 0.1272 -0.0068 0.0159  0.0133  126 LEU   A N   
2504 N N   B LEU   A 126 ? 0.1275 0.1357 0.1229 0.0040  0.0013  0.0157  126 LEU   A N   
2505 C CA  A LEU   A 126 ? 0.1060 0.1227 0.1203 -0.0054 0.0130  0.0082  126 LEU   A CA  
2506 C CA  B LEU   A 126 ? 0.1315 0.1416 0.1319 -0.0123 0.0001  0.0127  126 LEU   A CA  
2507 C C   A LEU   A 126 ? 0.1200 0.1198 0.1229 -0.0003 0.0028  0.0068  126 LEU   A C   
2508 C C   B LEU   A 126 ? 0.1354 0.1280 0.1263 -0.0043 0.0046  0.0089  126 LEU   A C   
2509 O O   A LEU   A 126 ? 0.1292 0.1271 0.1357 0.0086  0.0169  0.0137  126 LEU   A O   
2510 O O   B LEU   A 126 ? 0.1471 0.1286 0.1503 -0.0042 0.0064  0.0141  126 LEU   A O   
2511 C CB  A LEU   A 126 ? 0.1062 0.1268 0.1188 -0.0076 0.0077  0.0124  126 LEU   A CB  
2512 C CB  B LEU   A 126 ? 0.1460 0.1674 0.1864 -0.0243 -0.0069 0.0211  126 LEU   A CB  
2513 C CG  A LEU   A 126 ? 0.1012 0.1465 0.1361 -0.0177 0.0168  0.0150  126 LEU   A CG  
2514 C CG  B LEU   A 126 ? 0.1565 0.1884 0.2342 -0.0223 -0.0139 0.0233  126 LEU   A CG  
2515 C CD1 A LEU   A 126 ? 0.1025 0.1539 0.1634 -0.0190 0.0042  0.0181  126 LEU   A CD1 
2516 C CD1 B LEU   A 126 ? 0.1543 0.1960 0.2469 -0.0243 -0.0167 0.0234  126 LEU   A CD1 
2517 C CD2 A LEU   A 126 ? 0.1065 0.1461 0.1239 -0.0201 0.0114  0.0187  126 LEU   A CD2 
2518 C CD2 B LEU   A 126 ? 0.1633 0.1915 0.2526 -0.0214 -0.0214 0.0218  126 LEU   A CD2 
2541 N N   A LEU   A 127 ? 0.1256 0.1256 0.1215 0.0014  0.0053  0.0070  127 LEU   A N   
2542 N N   B LEU   A 127 ? 0.1376 0.1254 0.1163 0.0075  0.0071  0.0151  127 LEU   A N   
2543 C CA  A LEU   A 127 ? 0.1213 0.1204 0.1127 -0.0075 0.0105  -0.0011 127 LEU   A CA  
2544 C CA  B LEU   A 127 ? 0.1334 0.1249 0.1256 0.0058  0.0025  0.0197  127 LEU   A CA  
2545 C C   A LEU   A 127 ? 0.1214 0.1153 0.1158 -0.0112 0.0097  -0.0096 127 LEU   A C   
2546 C C   B LEU   A 127 ? 0.1333 0.1214 0.1247 0.0040  -0.0058 0.0153  127 LEU   A C   
2547 O O   A LEU   A 127 ? 0.1224 0.1131 0.0972 -0.0208 0.0119  -0.0037 127 LEU   A O   
2548 O O   B LEU   A 127 ? 0.1482 0.1271 0.1333 -0.0021 -0.0082 0.0165  127 LEU   A O   
2549 C CB  A LEU   A 127 ? 0.1256 0.1204 0.1203 0.0000  0.0081  -0.0030 127 LEU   A CB  
2550 C CB  B LEU   A 127 ? 0.1402 0.1364 0.1414 0.0119  0.0018  0.0214  127 LEU   A CB  
2551 C CG  A LEU   A 127 ? 0.1338 0.1146 0.1238 -0.0042 -0.0017 0.0022  127 LEU   A CG  
2552 C CG  B LEU   A 127 ? 0.1420 0.1500 0.1398 0.0098  -0.0056 0.0242  127 LEU   A CG  
2553 C CD1 A LEU   A 127 ? 0.1284 0.1023 0.1272 -0.0101 0.0009  -0.0063 127 LEU   A CD1 
2554 C CD1 B LEU   A 127 ? 0.1436 0.1591 0.1527 0.0164  0.0011  0.0312  127 LEU   A CD1 
2555 C CD2 A LEU   A 127 ? 0.1450 0.1111 0.1230 -0.0043 -0.0125 0.0162  127 LEU   A CD2 
2556 C CD2 B LEU   A 127 ? 0.1553 0.1669 0.1333 0.0051  -0.0226 0.0156  127 LEU   A CD2 
2579 N N   A SER   A 128 ? 0.1266 0.1192 0.1308 -0.0182 0.0032  0.0008  128 SER   A N   
2580 N N   B SER   A 128 ? 0.1247 0.1246 0.1126 -0.0004 -0.0059 0.0149  128 SER   A N   
2581 C CA  A SER   A 128 ? 0.1377 0.1216 0.1319 -0.0204 0.0005  0.0067  128 SER   A CA  
2582 C CA  B SER   A 128 ? 0.1371 0.1256 0.1096 0.0039  -0.0104 0.0111  128 SER   A CA  
2583 C C   A SER   A 128 ? 0.1426 0.1177 0.1263 -0.0190 -0.0105 0.0096  128 SER   A C   
2584 C C   B SER   A 128 ? 0.1385 0.1231 0.1115 0.0113  -0.0103 0.0107  128 SER   A C   
2585 O O   A SER   A 128 ? 0.1493 0.1210 0.1227 -0.0194 -0.0173 0.0093  128 SER   A O   
2586 O O   B SER   A 128 ? 0.1574 0.1344 0.1396 0.0146  -0.0114 0.0027  128 SER   A O   
2587 C CB  A SER   A 128 ? 0.1385 0.1303 0.1356 -0.0240 0.0051  0.0172  128 SER   A CB  
2588 C CB  B SER   A 128 ? 0.1332 0.1304 0.1042 0.0041  -0.0066 0.0109  128 SER   A CB  
2589 O OG  A SER   A 128 ? 0.1404 0.1411 0.1409 -0.0221 0.0100  0.0195  128 SER   A OG  
2590 O OG  B SER   A 128 ? 0.1352 0.1356 0.1217 0.0038  -0.0010 0.0014  128 SER   A OG  
2601 N N   A ALA   A 129 ? 0.1428 0.1248 0.1535 -0.0136 -0.0096 0.0175  129 ALA   A N   
2602 N N   B ALA   A 129 ? 0.1325 0.1322 0.1230 0.0086  0.0019  0.0171  129 ALA   A N   
2603 C CA  A ALA   A 129 ? 0.1434 0.1322 0.1715 -0.0135 -0.0119 0.0202  129 ALA   A CA  
2604 C CA  B ALA   A 129 ? 0.1279 0.1414 0.1421 0.0036  -0.0007 0.0221  129 ALA   A CA  
2605 C C   A ALA   A 129 ? 0.1453 0.1332 0.1697 -0.0193 -0.0095 0.0138  129 ALA   A C   
2606 C C   B ALA   A 129 ? 0.1302 0.1369 0.1305 0.0023  0.0040  0.0064  129 ALA   A C   
2607 O O   A ALA   A 129 ? 0.1485 0.1388 0.1760 -0.0246 0.0056  0.0212  129 ALA   A O   
2608 O O   B ALA   A 129 ? 0.1327 0.1442 0.1407 -0.0006 -0.0021 0.0087  129 ALA   A O   
2609 C CB  A ALA   A 129 ? 0.1412 0.1412 0.1919 -0.0096 -0.0061 0.0206  129 ALA   A CB  
2610 C CB  B ALA   A 129 ? 0.1189 0.1556 0.1570 -0.0036 0.0037  0.0316  129 ALA   A CB  
2621 N N   A GLY   A 130 ? 0.1512 0.1302 0.1749 -0.0192 -0.0181 0.0117  130 GLY   A N   
2622 N N   B GLY   A 130 ? 0.1296 0.1318 0.1410 -0.0033 -0.0065 0.0055  130 GLY   A N   
2623 C CA  A GLY   A 130 ? 0.1597 0.1336 0.1828 -0.0134 -0.0174 0.0091  130 GLY   A CA  
2624 C CA  B GLY   A 130 ? 0.1380 0.1332 0.1364 -0.0014 -0.0040 -0.0003 130 GLY   A CA  
2625 C C   A GLY   A 130 ? 0.1639 0.1335 0.1751 -0.0070 -0.0208 0.0139  130 GLY   A C   
2626 C C   B GLY   A 130 ? 0.1411 0.1324 0.1360 -0.0013 -0.0034 -0.0045 130 GLY   A C   
2627 O O   A GLY   A 130 ? 0.1697 0.1330 0.1670 0.0032  -0.0186 0.0111  130 GLY   A O   
2628 O O   B GLY   A 130 ? 0.1501 0.1373 0.1361 -0.0059 -0.0071 -0.0048 130 GLY   A O   
2635 N N   A ILE   A 131 ? 0.1645 0.1336 0.1719 -0.0157 -0.0252 0.0139  131 ILE   A N   
2636 N N   B ILE   A 131 ? 0.1454 0.1266 0.1429 -0.0018 -0.0027 0.0006  131 ILE   A N   
2637 C CA  A ILE   A 131 ? 0.1670 0.1380 0.1487 -0.0146 -0.0357 0.0126  131 ILE   A CA  
2638 C CA  B ILE   A 131 ? 0.1462 0.1252 0.1510 -0.0059 -0.0061 0.0141  131 ILE   A CA  
2639 C C   A ILE   A 131 ? 0.1598 0.1375 0.1429 -0.0101 -0.0276 0.0210  131 ILE   A C   
2640 C C   B ILE   A 131 ? 0.1567 0.1292 0.1417 -0.0074 0.0005  0.0241  131 ILE   A C   
2641 O O   A ILE   A 131 ? 0.1613 0.1444 0.1508 -0.0082 -0.0245 0.0191  131 ILE   A O   
2642 O O   B ILE   A 131 ? 0.1684 0.1314 0.1449 -0.0102 0.0004  0.0309  131 ILE   A O   
2643 C CB  A ILE   A 131 ? 0.1785 0.1511 0.1585 -0.0157 -0.0472 0.0034  131 ILE   A CB  
2644 C CB  B ILE   A 131 ? 0.1415 0.1293 0.1638 -0.0050 -0.0077 0.0035  131 ILE   A CB  
2645 C CG1 A ILE   A 131 ? 0.1799 0.1691 0.1653 -0.0139 -0.0564 -0.0027 131 ILE   A CG1 
2646 C CG1 B ILE   A 131 ? 0.1401 0.1438 0.1567 0.0006  -0.0086 0.0086  131 ILE   A CG1 
2647 C CG2 A ILE   A 131 ? 0.1857 0.1469 0.1736 -0.0158 -0.0452 0.0008  131 ILE   A CG2 
2648 C CG2 B ILE   A 131 ? 0.1454 0.1135 0.1696 0.0010  -0.0052 -0.0006 131 ILE   A CG2 
2649 C CD1 A ILE   A 131 ? 0.1837 0.1761 0.1902 -0.0095 -0.0551 -0.0027 131 ILE   A CD1 
2650 C CD1 B ILE   A 131 ? 0.1395 0.1568 0.1600 0.0012  -0.0232 -0.0004 131 ILE   A CD1 
2673 N N   A PHE   A 132 ? 0.1512 0.1325 0.1337 -0.0072 -0.0190 0.0240  132 PHE   A N   
2674 N N   B PHE   A 132 ? 0.1534 0.1335 0.1361 0.0000  0.0064  0.0140  132 PHE   A N   
2675 C CA  A PHE   A 132 ? 0.1482 0.1313 0.1314 -0.0133 -0.0126 0.0164  132 PHE   A CA  
2676 C CA  B PHE   A 132 ? 0.1551 0.1419 0.1291 -0.0050 0.0020  0.0127  132 PHE   A CA  
2677 C C   A PHE   A 132 ? 0.1585 0.1465 0.1327 -0.0046 -0.0134 0.0148  132 PHE   A C   
2678 C C   B PHE   A 132 ? 0.1649 0.1581 0.1332 -0.0011 -0.0028 0.0176  132 PHE   A C   
2679 O O   A PHE   A 132 ? 0.1714 0.1644 0.1380 -0.0006 -0.0088 0.0078  132 PHE   A O   
2680 O O   B PHE   A 132 ? 0.1770 0.1751 0.1374 -0.0004 -0.0020 0.0095  132 PHE   A O   
2681 C CB  A PHE   A 132 ? 0.1354 0.1184 0.1183 -0.0156 -0.0051 0.0207  132 PHE   A CB  
2682 C CB  B PHE   A 132 ? 0.1550 0.1378 0.1181 0.0010  0.0028  0.0140  132 PHE   A CB  
2683 C CG  A PHE   A 132 ? 0.1328 0.1141 0.1080 -0.0056 -0.0058 0.0180  132 PHE   A CG  
2684 C CG  B PHE   A 132 ? 0.1555 0.1378 0.1109 0.0102  -0.0018 0.0128  132 PHE   A CG  
2685 C CD1 A PHE   A 132 ? 0.1352 0.1207 0.1368 0.0040  -0.0060 0.0134  132 PHE   A CD1 
2686 C CD1 B PHE   A 132 ? 0.1568 0.1491 0.1333 0.0120  -0.0072 0.0061  132 PHE   A CD1 
2687 C CD2 A PHE   A 132 ? 0.1318 0.1256 0.1118 -0.0036 -0.0050 0.0157  132 PHE   A CD2 
2688 C CD2 B PHE   A 132 ? 0.1561 0.1490 0.1244 0.0059  0.0072  0.0086  132 PHE   A CD2 
2689 C CE1 A PHE   A 132 ? 0.1377 0.1258 0.1451 0.0046  -0.0116 0.0033  132 PHE   A CE1 
2690 C CE1 B PHE   A 132 ? 0.1600 0.1526 0.1338 -0.0011 0.0082  0.0067  132 PHE   A CE1 
2691 C CE2 A PHE   A 132 ? 0.1319 0.1323 0.1373 0.0049  -0.0169 0.0025  132 PHE   A CE2 
2692 C CE2 B PHE   A 132 ? 0.1596 0.1525 0.1231 0.0078  0.0140  0.0092  132 PHE   A CE2 
2693 C CZ  A PHE   A 132 ? 0.1340 0.1318 0.1458 0.0041  -0.0220 0.0016  132 PHE   A CZ  
2694 C CZ  B PHE   A 132 ? 0.1533 0.1517 0.1223 -0.0047 0.0181  0.0148  132 PHE   A CZ  
2713 N N   A GLY   A 133 ? 0.1582 0.1491 0.1323 -0.0108 -0.0219 0.0108  133 GLY   A N   
2714 N N   B GLY   A 133 ? 0.1680 0.1672 0.1422 -0.0105 -0.0185 0.0172  133 GLY   A N   
2715 C CA  A GLY   A 133 ? 0.1612 0.1560 0.1323 -0.0080 -0.0210 0.0053  133 GLY   A CA  
2716 C CA  B GLY   A 133 ? 0.1753 0.1798 0.1429 -0.0110 -0.0258 0.0091  133 GLY   A CA  
2717 C C   A GLY   A 133 ? 0.1575 0.1616 0.1230 -0.0049 -0.0168 -0.0023 133 GLY   A C   
2718 C C   B GLY   A 133 ? 0.1751 0.1880 0.1302 -0.0133 -0.0256 -0.0023 133 GLY   A C   
2719 O O   A GLY   A 133 ? 0.1611 0.1744 0.1261 0.0015  -0.0112 -0.0210 133 GLY   A O   
2720 O O   B GLY   A 133 ? 0.1811 0.1959 0.1266 -0.0094 -0.0152 -0.0195 133 GLY   A O   
2727 N N   A ALA   A 134 ? 0.1579 0.1472 0.1257 -0.0110 -0.0095 -0.0002 134 ALA   A N   
2728 N N   B ALA   A 134 ? 0.1744 0.1828 0.1236 -0.0215 -0.0200 -0.0093 134 ALA   A N   
2729 C CA  A ALA   A 134 ? 0.1530 0.1404 0.1410 -0.0041 -0.0056 -0.0084 134 ALA   A CA  
2730 C CA  B ALA   A 134 ? 0.1722 0.1852 0.1427 -0.0144 -0.0119 -0.0126 134 ALA   A CA  
2731 C C   A ALA   A 134 ? 0.1534 0.1391 0.1400 0.0011  -0.0036 -0.0051 134 ALA   A C   
2732 C C   B ALA   A 134 ? 0.1686 0.1832 0.1316 -0.0179 -0.0083 0.0022  134 ALA   A C   
2733 O O   A ALA   A 134 ? 0.1647 0.1438 0.1493 0.0026  0.0121  -0.0107 134 ALA   A O   
2734 O O   B ALA   A 134 ? 0.1829 0.1894 0.1322 -0.0229 -0.0097 -0.0108 134 ALA   A O   
2735 C CB  A ALA   A 134 ? 0.1518 0.1344 0.1514 -0.0030 -0.0026 -0.0121 134 ALA   A CB  
2736 C CB  B ALA   A 134 ? 0.1773 0.1838 0.1751 -0.0093 -0.0077 -0.0286 134 ALA   A CB  
2747 N N   A ASP   A 135 ? 0.1531 0.1425 0.1369 -0.0060 -0.0092 -0.0005 135 ASP   A N   
2748 N N   B ASP   A 135 ? 0.1658 0.1795 0.1543 -0.0137 -0.0062 0.0106  135 ASP   A N   
2749 C CA  A ASP   A 135 ? 0.1493 0.1480 0.1550 -0.0109 -0.0162 0.0088  135 ASP   A CA  
2750 C CA  B ASP   A 135 ? 0.1654 0.1845 0.1571 -0.0114 -0.0178 0.0175  135 ASP   A CA  
2751 C C   A ASP   A 135 ? 0.1411 0.1429 0.1624 -0.0044 -0.0094 0.0137  135 ASP   A C   
2752 C C   B ASP   A 135 ? 0.1634 0.1703 0.1515 -0.0062 -0.0071 0.0235  135 ASP   A C   
2753 O O   A ASP   A 135 ? 0.1369 0.1406 0.1582 -0.0071 -0.0084 0.0191  135 ASP   A O   
2754 O O   B ASP   A 135 ? 0.1610 0.1657 0.1600 -0.0051 -0.0173 0.0285  135 ASP   A O   
2755 C CB  A ASP   A 135 ? 0.1644 0.1721 0.1903 -0.0191 -0.0198 0.0045  135 ASP   A CB  
2756 C CB  B ASP   A 135 ? 0.1848 0.2117 0.2136 -0.0216 -0.0259 -0.0008 135 ASP   A CB  
2757 C CG  A ASP   A 135 ? 0.1767 0.2003 0.2238 -0.0215 -0.0250 0.0005  135 ASP   A CG  
2758 C CG  B ASP   A 135 ? 0.1968 0.2327 0.2587 -0.0314 -0.0375 -0.0171 135 ASP   A CG  
2759 O OD1 A ASP   A 135 ? 0.1732 0.2028 0.2246 -0.0150 -0.0227 0.0027  135 ASP   A OD1 
2760 O OD1 B ASP   A 135 ? 0.1982 0.2457 0.2713 -0.0390 -0.0470 -0.0142 135 ASP   A OD1 
2761 O OD2 A ASP   A 135 ? 0.1908 0.2192 0.2617 -0.0237 -0.0285 -0.0062 135 ASP   A OD2 
2762 O OD2 B ASP   A 135 ? 0.2137 0.2434 0.3075 -0.0342 -0.0228 -0.0207 135 ASP   A OD2 
2771 N N   A PRO   A 136 ? 0.1347 0.1379 0.1603 0.0021  -0.0096 0.0076  136 PRO   A N   
2772 N N   B PRO   A 136 ? 0.1621 0.1632 0.1627 -0.0017 -0.0080 0.0181  136 PRO   A N   
2773 C CA  A PRO   A 136 ? 0.1304 0.1385 0.1610 -0.0009 -0.0050 -0.0026 136 PRO   A CA  
2774 C CA  B PRO   A 136 ? 0.1523 0.1543 0.1675 -0.0071 -0.0078 0.0084  136 PRO   A CA  
2775 C C   A PRO   A 136 ? 0.1213 0.1393 0.1472 0.0013  0.0007  -0.0044 136 PRO   A C   
2776 C C   B PRO   A 136 ? 0.1387 0.1498 0.1629 -0.0010 -0.0051 0.0104  136 PRO   A C   
2777 O O   A PRO   A 136 ? 0.1176 0.1347 0.1420 0.0038  0.0119  0.0076  136 PRO   A O   
2778 O O   B PRO   A 136 ? 0.1355 0.1527 0.1593 -0.0122 -0.0030 0.0166  136 PRO   A O   
2779 C CB  A PRO   A 136 ? 0.1400 0.1388 0.1761 0.0018  -0.0101 -0.0089 136 PRO   A CB  
2780 C CB  B PRO   A 136 ? 0.1668 0.1540 0.1729 -0.0089 -0.0091 0.0086  136 PRO   A CB  
2781 C CG  A PRO   A 136 ? 0.1469 0.1389 0.1824 0.0107  -0.0123 -0.0116 136 PRO   A CG  
2782 C CG  B PRO   A 136 ? 0.1754 0.1609 0.1772 -0.0016 -0.0162 0.0052  136 PRO   A CG  
2783 C CD  A PRO   A 136 ? 0.1389 0.1349 0.1740 0.0091  -0.0115 0.0099  136 PRO   A CD  
2784 C CD  B PRO   A 136 ? 0.1761 0.1612 0.1730 0.0034  -0.0098 0.0098  136 PRO   A CD  
2799 N N   A ILE   A 137 ? 0.1215 0.1413 0.1590 0.0004  -0.0030 -0.0051 137 ILE   A N   
2800 N N   B ILE   A 137 ? 0.1298 0.1486 0.1632 0.0027  -0.0116 0.0059  137 ILE   A N   
2801 C CA  A ILE   A 137 ? 0.1281 0.1436 0.1680 -0.0018 -0.0073 -0.0151 137 ILE   A CA  
2802 C CA  B ILE   A 137 ? 0.1357 0.1543 0.1807 -0.0068 -0.0110 0.0082  137 ILE   A CA  
2803 C C   A ILE   A 137 ? 0.1283 0.1408 0.1567 -0.0071 -0.0004 -0.0139 137 ILE   A C   
2804 C C   B ILE   A 137 ? 0.1414 0.1495 0.1726 -0.0071 -0.0097 0.0133  137 ILE   A C   
2805 O O   A ILE   A 137 ? 0.1276 0.1419 0.1692 -0.0070 0.0062  -0.0060 137 ILE   A O   
2806 O O   B ILE   A 137 ? 0.1503 0.1492 0.1795 -0.0082 -0.0037 0.0160  137 ILE   A O   
2807 C CB  A ILE   A 137 ? 0.1327 0.1433 0.1819 -0.0027 -0.0239 -0.0260 137 ILE   A CB  
2808 C CB  B ILE   A 137 ? 0.1380 0.1654 0.2109 -0.0090 -0.0220 0.0001  137 ILE   A CB  
2809 C CG1 A ILE   A 137 ? 0.1380 0.1513 0.1992 0.0034  -0.0386 -0.0255 137 ILE   A CG1 
2810 C CG1 B ILE   A 137 ? 0.1423 0.1773 0.2352 -0.0065 -0.0190 0.0015  137 ILE   A CG1 
2811 C CG2 A ILE   A 137 ? 0.1370 0.1359 0.1852 -0.0021 -0.0191 -0.0339 137 ILE   A CG2 
2812 C CG2 B ILE   A 137 ? 0.1443 0.1680 0.2160 -0.0172 -0.0184 -0.0219 137 ILE   A CG2 
2813 C CD1 A ILE   A 137 ? 0.1469 0.1612 0.2200 0.0097  -0.0361 -0.0261 137 ILE   A CD1 
2814 C CD1 B ILE   A 137 ? 0.1532 0.1875 0.2525 -0.0001 -0.0165 -0.0063 137 ILE   A CD1 
2837 N N   A HIS   A 138 ? 0.1330 0.1455 0.1507 -0.0107 0.0076  -0.0175 138 HIS   A N   
2838 N N   B HIS   A 138 ? 0.1402 0.1515 0.1594 -0.0070 -0.0055 0.0124  138 HIS   A N   
2839 C CA  A HIS   A 138 ? 0.1374 0.1367 0.1467 -0.0117 0.0074  -0.0144 138 HIS   A CA  
2840 C CA  B HIS   A 138 ? 0.1452 0.1610 0.1665 -0.0032 0.0009  0.0052  138 HIS   A CA  
2841 C C   A HIS   A 138 ? 0.1320 0.1233 0.1557 -0.0108 0.0038  -0.0090 138 HIS   A C   
2842 C C   B HIS   A 138 ? 0.1331 0.1522 0.1588 -0.0057 0.0009  0.0106  138 HIS   A C   
2843 O O   A HIS   A 138 ? 0.1351 0.1210 0.1473 -0.0119 0.0110  -0.0113 138 HIS   A O   
2844 O O   B HIS   A 138 ? 0.1367 0.1558 0.1673 -0.0033 0.0056  0.0170  138 HIS   A O   
2845 C CB  A HIS   A 138 ? 0.1443 0.1449 0.1375 -0.0043 0.0055  -0.0205 138 HIS   A CB  
2846 C CB  B HIS   A 138 ? 0.1634 0.1742 0.1753 -0.0052 -0.0024 0.0047  138 HIS   A CB  
2847 C CG  A HIS   A 138 ? 0.1514 0.1539 0.1407 -0.0019 -0.0018 -0.0222 138 HIS   A CG  
2848 C CG  B HIS   A 138 ? 0.1765 0.1892 0.1862 -0.0063 -0.0029 -0.0008 138 HIS   A CG  
2849 N ND1 A HIS   A 138 ? 0.1593 0.1624 0.1681 0.0021  -0.0051 -0.0278 138 HIS   A ND1 
2850 N ND1 B HIS   A 138 ? 0.1892 0.2016 0.2081 -0.0081 -0.0001 -0.0117 138 HIS   A ND1 
2851 C CD2 A HIS   A 138 ? 0.1521 0.1590 0.1461 0.0014  0.0007  -0.0214 138 HIS   A CD2 
2852 C CD2 B HIS   A 138 ? 0.1801 0.1980 0.1914 -0.0076 -0.0013 0.0049  138 HIS   A CD2 
2853 C CE1 A HIS   A 138 ? 0.1638 0.1682 0.1687 0.0091  -0.0079 -0.0293 138 HIS   A CE1 
2854 C CE1 B HIS   A 138 ? 0.1915 0.2082 0.2194 -0.0018 0.0006  -0.0093 138 HIS   A CE1 
2855 N NE2 A HIS   A 138 ? 0.1609 0.1664 0.1503 0.0092  -0.0020 -0.0272 138 HIS   A NE2 
2856 N NE2 B HIS   A 138 ? 0.1842 0.2076 0.2028 -0.0013 0.0012  -0.0029 138 HIS   A NE2 
2871 N N   A SER   A 139 ? 0.1267 0.1148 0.1593 -0.0131 -0.0020 0.0007  139 SER   A N   
2872 N N   B SER   A 139 ? 0.1230 0.1431 0.1612 -0.0052 -0.0102 0.0175  139 SER   A N   
2873 C CA  A SER   A 139 ? 0.1228 0.1225 0.1639 -0.0046 -0.0025 0.0051  139 SER   A CA  
2874 C CA  B SER   A 139 ? 0.1176 0.1376 0.1600 -0.0103 0.0058  0.0254  139 SER   A CA  
2875 C C   A SER   A 139 ? 0.1196 0.1217 0.1640 -0.0104 -0.0004 0.0139  139 SER   A C   
2876 C C   B SER   A 139 ? 0.1154 0.1310 0.1571 -0.0117 0.0155  0.0271  139 SER   A C   
2877 O O   A SER   A 139 ? 0.1187 0.1059 0.1678 -0.0105 -0.0141 0.0194  139 SER   A O   
2878 O O   B SER   A 139 ? 0.1067 0.1271 0.1508 -0.0133 0.0158  0.0185  139 SER   A O   
2879 C CB  A SER   A 139 ? 0.1183 0.1176 0.1479 0.0000  -0.0019 0.0038  139 SER   A CB  
2880 C CB  B SER   A 139 ? 0.1097 0.1356 0.1445 -0.0092 0.0115  0.0149  139 SER   A CB  
2881 O OG  A SER   A 139 ? 0.1233 0.1141 0.1456 -0.0052 -0.0024 0.0039  139 SER   A OG  
2882 O OG  B SER   A 139 ? 0.1091 0.1231 0.1408 -0.0047 0.0143  0.0137  139 SER   A OG  
2893 N N   . LEU   A 140 ? 0.1169 0.1360 0.1605 -0.0091 0.0025  0.0309  140 LEU   A N   
2894 C CA  . LEU   A 140 ? 0.1138 0.1354 0.1689 -0.0108 0.0010  0.0266  140 LEU   A CA  
2895 C C   . LEU   A 140 ? 0.1071 0.1449 0.1723 -0.0106 0.0051  0.0244  140 LEU   A C   
2896 O O   . LEU   A 140 ? 0.1127 0.1456 0.1724 -0.0033 0.0014  0.0277  140 LEU   A O   
2897 C CB  . LEU   A 140 ? 0.1132 0.1489 0.1727 -0.0117 0.0071  0.0273  140 LEU   A CB  
2898 C CG  . LEU   A 140 ? 0.1160 0.1611 0.1750 -0.0139 0.0105  0.0340  140 LEU   A CG  
2899 C CD1 . LEU   A 140 ? 0.1208 0.1702 0.1879 -0.0082 0.0112  0.0313  140 LEU   A CD1 
2900 C CD2 . LEU   A 140 ? 0.1203 0.1759 0.2015 -0.0090 0.0206  0.0418  140 LEU   A CD2 
2913 N N   . ARG   A 141 ? 0.1217 0.1487 0.1715 -0.0147 0.0010  0.0238  141 ARG   A N   
2914 C CA  . ARG   A 141 ? 0.1299 0.1628 0.1879 -0.0195 -0.0041 0.0093  141 ARG   A CA  
2915 C C   . ARG   A 141 ? 0.1310 0.1495 0.1771 -0.0146 -0.0079 0.0129  141 ARG   A C   
2916 O O   . ARG   A 141 ? 0.1286 0.1431 0.1935 -0.0175 -0.0027 0.0076  141 ARG   A O   
2917 C CB  . ARG   A 141 ? 0.1478 0.1856 0.2027 -0.0277 -0.0009 -0.0054 141 ARG   A CB  
2918 C CG  . ARG   A 141 ? 0.1740 0.2137 0.2350 -0.0329 0.0124  -0.0153 141 ARG   A CG  
2919 C CD  . ARG   A 141 ? 0.2026 0.2327 0.2771 -0.0390 0.0088  -0.0255 141 ARG   A CD  
2920 N NE  . ARG   A 141 ? 0.1999 0.2444 0.3020 -0.0422 0.0042  -0.0167 141 ARG   A NE  
2921 C CZ  . ARG   A 141 ? 0.2011 0.2523 0.2964 -0.0515 0.0090  -0.0050 141 ARG   A CZ  
2922 N NH1 . ARG   A 141 ? 0.1937 0.2559 0.2721 -0.0689 0.0267  -0.0146 141 ARG   A NH1 
2923 N NH2 . ARG   A 141 ? 0.2024 0.2579 0.3243 -0.0342 -0.0027 0.0056  141 ARG   A NH2 
2937 N N   . VAL   A 142 ? 0.1238 0.1461 0.1746 -0.0152 0.0064  0.0104  142 VAL   A N   
2938 C CA  . VAL   A 142 ? 0.1269 0.1350 0.1726 -0.0086 0.0138  0.0134  142 VAL   A CA  
2939 C C   . VAL   A 142 ? 0.1121 0.1305 0.1697 -0.0107 0.0132  0.0130  142 VAL   A C   
2940 O O   . VAL   A 142 ? 0.1189 0.1332 0.1740 0.0000  0.0112  0.0086  142 VAL   A O   
2941 C CB  . VAL   A 142 ? 0.1336 0.1475 0.1733 -0.0054 0.0124  0.0123  142 VAL   A CB  
2942 C CG1 . VAL   A 142 ? 0.1301 0.1438 0.1725 -0.0145 0.0177  0.0100  142 VAL   A CG1 
2943 C CG2 . VAL   A 142 ? 0.1491 0.1652 0.1920 -0.0012 0.0144  0.0091  142 VAL   A CG2 
2953 N N   . CYS   A 143 ? 0.1188 0.1263 0.1666 -0.0143 0.0089  0.0133  143 CYS   A N   
2954 C CA  . CYS   A 143 ? 0.1149 0.1297 0.1677 -0.0119 0.0118  0.0188  143 CYS   A CA  
2955 C C   . CYS   A 143 ? 0.1127 0.1321 0.1806 -0.0098 0.0118  0.0233  143 CYS   A C   
2956 O O   . CYS   A 143 ? 0.1138 0.1356 0.1735 -0.0030 0.0071  0.0316  143 CYS   A O   
2957 C CB  . CYS   A 143 ? 0.1261 0.1346 0.1691 -0.0065 0.0162  0.0254  143 CYS   A CB  
2958 S SG  . CYS   A 143 ? 0.1435 0.1448 0.1685 0.0026  0.0186  0.0166  143 CYS   A SG  
2964 N N   . VAL   A 144 ? 0.1146 0.1357 0.1891 -0.0090 0.0096  0.0362  144 VAL   A N   
2965 C CA  . VAL   A 144 ? 0.1184 0.1457 0.2203 -0.0129 0.0182  0.0401  144 VAL   A CA  
2966 C C   . VAL   A 144 ? 0.1237 0.1390 0.2135 -0.0204 -0.0085 0.0299  144 VAL   A C   
2967 O O   . VAL   A 144 ? 0.1396 0.1430 0.2114 -0.0100 -0.0071 0.0296  144 VAL   A O   
2968 C CB  . VAL   A 144 ? 0.1529 0.1752 0.2876 -0.0080 0.0340  0.0470  144 VAL   A CB  
2969 C CG1 . VAL   A 144 ? 0.1790 0.1943 0.3363 -0.0174 0.0157  0.0585  144 VAL   A CG1 
2970 C CG2 . VAL   A 144 ? 0.1313 0.1798 0.2776 -0.0036 0.0411  0.0562  144 VAL   A CG2 
2980 N N   . ASP   A 145 ? 0.1301 0.1324 0.2229 -0.0162 -0.0087 0.0206  145 ASP   A N   
2981 C CA  . ASP   A 145 ? 0.1397 0.1371 0.2380 -0.0242 -0.0115 0.0155  145 ASP   A CA  
2982 C C   . ASP   A 145 ? 0.1409 0.1299 0.2415 -0.0088 -0.0032 0.0032  145 ASP   A C   
2983 O O   . ASP   A 145 ? 0.1530 0.1413 0.2865 -0.0091 -0.0108 -0.0297 145 ASP   A O   
2984 C CB  . ASP   A 145 ? 0.1612 0.1725 0.2631 -0.0348 -0.0301 0.0174  145 ASP   A CB  
2985 C CG  . ASP   A 145 ? 0.1837 0.2061 0.2967 -0.0482 -0.0457 0.0322  145 ASP   A CG  
2986 O OD1 . ASP   A 145 ? 0.1769 0.2247 0.3096 -0.0621 -0.0282 0.0325  145 ASP   A OD1 
2987 O OD2 . ASP   A 145 ? 0.1974 0.2290 0.3082 -0.0537 -0.0618 0.0388  145 ASP   A OD2 
2992 N N   . THR   A 146 ? 0.1234 0.1239 0.1920 -0.0113 0.0053  0.0061  146 THR   A N   
2993 C CA  . THR   A 146 ? 0.1226 0.1224 0.1773 -0.0073 0.0100  0.0077  146 THR   A CA  
2994 C C   . THR   A 146 ? 0.1188 0.1203 0.1753 -0.0031 0.0103  0.0124  146 THR   A C   
2995 O O   . THR   A 146 ? 0.1307 0.1369 0.1840 0.0080  -0.0014 0.0115  146 THR   A O   
2996 C CB  . THR   A 146 ? 0.1210 0.1264 0.1691 -0.0045 0.0088  0.0075  146 THR   A CB  
2997 O OG1 . THR   A 146 ? 0.1220 0.1416 0.1666 0.0020  0.0015  0.0011  146 THR   A OG1 
2998 C CG2 . THR   A 146 ? 0.1195 0.1277 0.1864 -0.0018 0.0124  0.0096  146 THR   A CG2 
3006 N N   . VAL   A 147 ? 0.1126 0.1302 0.1697 -0.0031 0.0111  0.0208  147 VAL   A N   
3007 C CA  . VAL   A 147 ? 0.1152 0.1272 0.1778 -0.0083 0.0237  0.0241  147 VAL   A CA  
3008 C C   . VAL   A 147 ? 0.1180 0.1219 0.1812 -0.0098 0.0178  0.0246  147 VAL   A C   
3009 O O   . VAL   A 147 ? 0.1207 0.1330 0.2022 -0.0111 0.0129  0.0275  147 VAL   A O   
3010 C CB  . VAL   A 147 ? 0.1299 0.1243 0.1708 -0.0103 0.0243  0.0229  147 VAL   A CB  
3011 C CG1 . VAL   A 147 ? 0.1615 0.1350 0.1711 -0.0061 0.0247  0.0230  147 VAL   A CG1 
3012 C CG2 . VAL   A 147 ? 0.1372 0.1224 0.1818 -0.0116 0.0148  0.0227  147 VAL   A CG2 
3022 N N   . ARG   A 148 ? 0.1195 0.1224 0.1855 -0.0106 0.0172  0.0332  148 ARG   A N   
3023 C CA  . ARG   A 148 ? 0.1234 0.1289 0.1867 -0.0109 0.0146  0.0421  148 ARG   A CA  
3024 C C   . ARG   A 148 ? 0.1313 0.1344 0.1848 -0.0140 0.0156  0.0499  148 ARG   A C   
3025 O O   . ARG   A 148 ? 0.1691 0.1481 0.1918 -0.0229 0.0181  0.0406  148 ARG   A O   
3026 C CB  . ARG   A 148 ? 0.1296 0.1295 0.2044 -0.0100 0.0194  0.0341  148 ARG   A CB  
3027 C CG  . ARG   A 148 ? 0.1498 0.1278 0.2268 -0.0135 0.0277  0.0254  148 ARG   A CG  
3028 C CD  . ARG   A 148 ? 0.1654 0.1277 0.2390 -0.0021 0.0406  0.0391  148 ARG   A CD  
3029 N NE  . ARG   A 148 ? 0.1570 0.1370 0.2457 0.0079  0.0487  0.0424  148 ARG   A NE  
3030 C CZ  . ARG   A 148 ? 0.1538 0.1270 0.2360 0.0042  0.0465  0.0324  148 ARG   A CZ  
3031 N NH1 . ARG   A 148 ? 0.1623 0.1317 0.2334 -0.0096 0.0428  0.0170  148 ARG   A NH1 
3032 N NH2 . ARG   A 148 ? 0.1517 0.1435 0.2389 0.0143  0.0486  0.0413  148 ARG   A NH2 
3046 N N   . THR   A 149 ? 0.1346 0.1411 0.1725 -0.0172 -0.0020 0.0412  149 THR   A N   
3047 C CA  . THR   A 149 ? 0.1380 0.1435 0.1697 -0.0121 -0.0014 0.0453  149 THR   A CA  
3048 C C   . THR   A 149 ? 0.1324 0.1404 0.1674 -0.0202 0.0099  0.0437  149 THR   A C   
3049 O O   . THR   A 149 ? 0.1296 0.1541 0.1813 -0.0189 0.0010  0.0376  149 THR   A O   
3050 C CB  . THR   A 149 ? 0.1378 0.1543 0.1786 -0.0112 0.0064  0.0344  149 THR   A CB  
3051 O OG1 . THR   A 149 ? 0.1409 0.1468 0.1843 -0.0241 0.0056  0.0230  149 THR   A OG1 
3052 C CG2 . THR   A 149 ? 0.1402 0.1654 0.1835 -0.0042 -0.0018 0.0285  149 THR   A CG2 
3060 N N   . ASN   A 150 ? 0.1409 0.1494 0.1708 -0.0091 -0.0007 0.0529  150 ASN   A N   
3061 C CA  . ASN   A 150 ? 0.1475 0.1546 0.1687 -0.0114 0.0055  0.0476  150 ASN   A CA  
3062 C C   . ASN   A 150 ? 0.1344 0.1500 0.1746 -0.0194 0.0067  0.0406  150 ASN   A C   
3063 O O   . ASN   A 150 ? 0.1414 0.1582 0.2038 -0.0170 -0.0056 0.0344  150 ASN   A O   
3064 C CB  . ASN   A 150 ? 0.1899 0.1797 0.1912 -0.0176 0.0203  0.0605  150 ASN   A CB  
3065 C CG  . ASN   A 150 ? 0.2437 0.2165 0.2607 -0.0221 0.0062  0.0645  150 ASN   A CG  
3066 O OD1 . ASN   A 150 ? 0.2658 0.2287 0.2740 -0.0336 0.0140  0.0824  150 ASN   A OD1 
3067 N ND2 . ASN   A 150 ? 0.2743 0.2385 0.2950 -0.0139 -0.0106 0.0590  150 ASN   A ND2 
3074 N N   . VAL   A 151 ? 0.1315 0.1381 0.1667 -0.0146 0.0075  0.0352  151 VAL   A N   
3075 C CA  . VAL   A 151 ? 0.1396 0.1364 0.1542 -0.0136 0.0178  0.0330  151 VAL   A CA  
3076 C C   . VAL   A 151 ? 0.1269 0.1307 0.1697 -0.0200 0.0168  0.0409  151 VAL   A C   
3077 O O   . VAL   A 151 ? 0.1366 0.1396 0.2094 -0.0193 0.0106  0.0298  151 VAL   A O   
3078 C CB  . VAL   A 151 ? 0.1717 0.1567 0.1731 0.0031  0.0118  0.0308  151 VAL   A CB  
3079 C CG1 . VAL   A 151 ? 0.1652 0.1814 0.2155 -0.0035 -0.0037 0.0261  151 VAL   A CG1 
3080 C CG2 . VAL   A 151 ? 0.1827 0.1563 0.1698 0.0014  0.0256  0.0255  151 VAL   A CG2 
3090 N N   . TYR   A 152 ? 0.1278 0.1364 0.1671 -0.0223 0.0149  0.0336  152 TYR   A N   
3091 C CA  . TYR   A 152 ? 0.1289 0.1398 0.1627 -0.0158 0.0201  0.0315  152 TYR   A CA  
3092 C C   . TYR   A 152 ? 0.1237 0.1335 0.1501 -0.0130 0.0285  0.0289  152 TYR   A C   
3093 O O   . TYR   A 152 ? 0.1330 0.1350 0.1542 -0.0189 0.0234  0.0304  152 TYR   A O   
3094 C CB  . TYR   A 152 ? 0.1494 0.1493 0.1637 -0.0141 0.0291  0.0352  152 TYR   A CB  
3095 C CG  . TYR   A 152 ? 0.1634 0.1682 0.1563 -0.0167 0.0310  0.0394  152 TYR   A CG  
3096 C CD1 . TYR   A 152 ? 0.1727 0.1914 0.1695 -0.0091 0.0292  0.0542  152 TYR   A CD1 
3097 C CD2 . TYR   A 152 ? 0.1686 0.1798 0.1482 -0.0303 0.0262  0.0344  152 TYR   A CD2 
3098 C CE1 . TYR   A 152 ? 0.1994 0.2070 0.1828 -0.0053 0.0150  0.0660  152 TYR   A CE1 
3099 C CE2 . TYR   A 152 ? 0.1906 0.2022 0.1728 -0.0295 0.0236  0.0490  152 TYR   A CE2 
3100 C CZ  . TYR   A 152 ? 0.2092 0.2079 0.1699 -0.0190 0.0155  0.0731  152 TYR   A CZ  
3101 O OH  . TYR   A 152 ? 0.2362 0.2297 0.2080 -0.0146 0.0170  0.0861  152 TYR   A OH  
3111 N N   A LEU   A 153 ? 0.1183 0.1239 0.1533 -0.0177 0.0266  0.0300  153 LEU   A N   
3112 N N   B LEU   A 153 ? 0.1214 0.1301 0.1556 -0.0175 0.0264  0.0316  153 LEU   A N   
3113 C CA  A LEU   A 153 ? 0.1167 0.1172 0.1612 -0.0132 0.0238  0.0266  153 LEU   A CA  
3114 C CA  B LEU   A 153 ? 0.1228 0.1264 0.1664 -0.0044 0.0228  0.0286  153 LEU   A CA  
3115 C C   A LEU   A 153 ? 0.1190 0.1151 0.1486 -0.0157 0.0271  0.0260  153 LEU   A C   
3116 C C   B LEU   A 153 ? 0.1265 0.1335 0.1657 -0.0012 0.0306  0.0295  153 LEU   A C   
3117 O O   A LEU   A 153 ? 0.1237 0.1191 0.1682 -0.0153 0.0338  0.0211  153 LEU   A O   
3118 O O   B LEU   A 153 ? 0.1326 0.1429 0.1916 -0.0045 0.0460  0.0329  153 LEU   A O   
3119 C CB  A LEU   A 153 ? 0.1161 0.1190 0.1680 -0.0125 0.0227  0.0219  153 LEU   A CB  
3120 C CB  B LEU   A 153 ? 0.1204 0.1302 0.1774 0.0049  0.0198  0.0348  153 LEU   A CB  
3121 C CG  A LEU   A 153 ? 0.1193 0.1264 0.1561 -0.0168 0.0262  0.0153  153 LEU   A CG  
3122 C CG  B LEU   A 153 ? 0.1252 0.1458 0.1713 0.0065  0.0150  0.0353  153 LEU   A CG  
3123 C CD1 A LEU   A 153 ? 0.1262 0.1214 0.1626 -0.0197 0.0175  0.0145  153 LEU   A CD1 
3124 C CD1 B LEU   A 153 ? 0.1376 0.1493 0.1873 0.0038  0.0105  0.0318  153 LEU   A CD1 
3125 C CD2 A LEU   A 153 ? 0.1236 0.1306 0.1478 -0.0148 0.0271  0.0078  153 LEU   A CD2 
3126 C CD2 B LEU   A 153 ? 0.1302 0.1563 0.1767 0.0072  0.0071  0.0272  153 LEU   A CD2 
3149 N N   A ALA   A 154 ? 0.1196 0.1125 0.1319 -0.0154 0.0245  0.0239  154 ALA   A N   
3150 N N   B ALA   A 154 ? 0.1274 0.1328 0.1320 0.0032  0.0263  0.0237  154 ALA   A N   
3151 C CA  A ALA   A 154 ? 0.1236 0.1127 0.1290 -0.0133 0.0231  0.0216  154 ALA   A CA  
3152 C CA  B ALA   A 154 ? 0.1308 0.1327 0.1384 0.0001  0.0231  0.0189  154 ALA   A CA  
3153 C C   A ALA   A 154 ? 0.1228 0.1053 0.1235 -0.0053 0.0203  0.0167  154 ALA   A C   
3154 C C   B ALA   A 154 ? 0.1256 0.1325 0.1259 -0.0033 0.0146  0.0196  154 ALA   A C   
3155 O O   A ALA   A 154 ? 0.1261 0.1194 0.1382 -0.0043 0.0099  0.0111  154 ALA   A O   
3156 O O   B ALA   A 154 ? 0.1270 0.1446 0.1147 -0.0081 0.0166  0.0243  154 ALA   A O   
3157 C CB  A ALA   A 154 ? 0.1348 0.1196 0.1420 -0.0140 0.0159  0.0158  154 ALA   A CB  
3158 C CB  B ALA   A 154 ? 0.1415 0.1317 0.1390 0.0036  0.0081  0.0034  154 ALA   A CB  
3169 N N   A VAL   A 155 ? 0.1202 0.0997 0.0886 -0.0021 0.0299  0.0210  155 VAL   A N   
3170 N N   B VAL   A 155 ? 0.1262 0.1305 0.1528 -0.0030 0.0161  0.0243  155 VAL   A N   
3171 C CA  A VAL   A 155 ? 0.1273 0.1067 0.1284 0.0031  0.0251  0.0227  155 VAL   A CA  
3172 C CA  B VAL   A 155 ? 0.1357 0.1395 0.1660 -0.0044 0.0155  0.0198  155 VAL   A CA  
3173 C CA  T VAL   A 155 ? 0.1388 0.1333 0.1300 0.0003  0.0067  0.0166  155 VAL   A CA  
3174 C C   A VAL   A 155 ? 0.1363 0.1135 0.1554 0.0116  0.0341  0.0346  155 VAL   A C   
3175 C C   B VAL   A 155 ? 0.1394 0.1428 0.1992 -0.0014 0.0157  0.0239  155 VAL   A C   
3176 C C   T VAL   A 155 ? 0.1402 0.1309 0.1311 0.0021  0.0120  0.0198  155 VAL   A C   
3177 O O   A VAL   A 155 ? 0.1301 0.1191 0.1693 0.0198  0.0543  0.0318  155 VAL   A O   
3178 O O   B VAL   A 155 ? 0.1396 0.1524 0.2110 0.0094  0.0230  0.0213  155 VAL   A O   
3179 O O   T VAL   A 155 ? 0.1379 0.1328 0.1268 0.0034  0.0159  0.0163  155 VAL   A O   
3180 C CB  A VAL   A 155 ? 0.1301 0.1085 0.1455 0.0006  0.0073  0.0210  155 VAL   A CB  
3181 C CB  B VAL   A 155 ? 0.1466 0.1465 0.1697 -0.0013 0.0009  0.0152  155 VAL   A CB  
3182 C CB  T VAL   A 155 ? 0.1393 0.1357 0.1340 -0.0012 0.0008  0.0146  155 VAL   A CB  
3183 C CG1 A VAL   A 155 ? 0.1371 0.1125 0.1529 0.0077  0.0037  0.0211  155 VAL   A CG1 
3184 C CG1 B VAL   A 155 ? 0.1531 0.1507 0.1699 -0.0084 -0.0110 0.0085  155 VAL   A CG1 
3185 C CG1 T VAL   A 155 ? 0.1416 0.1378 0.1335 0.0006  -0.0002 0.0145  155 VAL   A CG1 
3186 C CG2 A VAL   A 155 ? 0.1285 0.1108 0.1586 -0.0083 -0.0014 0.0208  155 VAL   A CG2 
3187 C CG2 B VAL   A 155 ? 0.1536 0.1488 0.1829 0.0018  0.0004  0.0109  155 VAL   A CG2 
3188 C CG2 T VAL   A 155 ? 0.1386 0.1374 0.1386 -0.0043 -0.0024 0.0137  155 VAL   A CG2 
3214 N N   A PHE   A 156 ? 0.1543 0.1166 0.1900 0.0131  0.0214  0.0513  156 PHE   A N   
3215 N N   B PHE   A 156 ? 0.1386 0.1392 0.2055 -0.0016 0.0124  0.0276  156 PHE   A N   
3216 N N   T PHE   A 156 ? 0.1453 0.1269 0.1425 0.0037  0.0116  0.0279  156 PHE   A N   
3217 C CA  A PHE   A 156 ? 0.1766 0.1261 0.2166 0.0221  0.0130  0.0616  156 PHE   A CA  
3218 C CA  B PHE   A 156 ? 0.1550 0.1504 0.2338 0.0027  0.0088  0.0179  156 PHE   A CA  
3219 C CA  T PHE   A 156 ? 0.1521 0.1241 0.1480 0.0066  0.0154  0.0347  156 PHE   A CA  
3220 C C   A PHE   A 156 ? 0.1788 0.1341 0.2140 0.0277  0.0289  0.0640  156 PHE   A C   
3221 C C   B PHE   A 156 ? 0.1500 0.1506 0.2326 0.0048  0.0137  0.0224  156 PHE   A C   
3222 C C   T PHE   A 156 ? 0.1581 0.1377 0.1606 0.0073  0.0217  0.0331  156 PHE   A C   
3223 O O   A PHE   A 156 ? 0.1867 0.1345 0.2166 0.0301  0.0410  0.0548  156 PHE   A O   
3224 O O   B PHE   A 156 ? 0.1587 0.1585 0.2557 0.0116  0.0168  0.0151  156 PHE   A O   
3225 O O   T PHE   A 156 ? 0.1604 0.1383 0.1617 0.0077  0.0266  0.0322  156 PHE   A O   
3226 C CB  A PHE   A 156 ? 0.1917 0.1337 0.2410 0.0175  0.0011  0.0708  156 PHE   A CB  
3227 C CB  B PHE   A 156 ? 0.1694 0.1740 0.2567 -0.0045 0.0128  0.0078  156 PHE   A CB  
3228 C CB  T PHE   A 156 ? 0.1499 0.1092 0.1415 0.0068  0.0152  0.0454  156 PHE   A CB  
3229 C CG  A PHE   A 156 ? 0.2080 0.1485 0.2574 0.0242  -0.0097 0.0683  156 PHE   A CG  
3230 C CG  B PHE   A 156 ? 0.1960 0.2043 0.2956 -0.0052 0.0127  -0.0019 156 PHE   A CG  
3231 C CG  T PHE   A 156 ? 0.1498 0.0992 0.1392 0.0107  0.0090  0.0531  156 PHE   A CG  
3232 C CD1 A PHE   A 156 ? 0.2111 0.1626 0.2507 0.0237  -0.0060 0.0630  156 PHE   A CD1 
3233 C CD1 B PHE   A 156 ? 0.2126 0.2148 0.3129 0.0017  0.0090  -0.0108 156 PHE   A CD1 
3234 C CD1 T PHE   A 156 ? 0.1509 0.0991 0.1396 0.0135  0.0028  0.0508  156 PHE   A CD1 
3235 C CD2 A PHE   A 156 ? 0.2214 0.1562 0.2526 0.0336  -0.0153 0.0794  156 PHE   A CD2 
3236 C CD2 B PHE   A 156 ? 0.2071 0.2182 0.3192 -0.0127 0.0255  -0.0034 156 PHE   A CD2 
3237 C CD2 T PHE   A 156 ? 0.1541 0.0996 0.1465 0.0159  0.0001  0.0564  156 PHE   A CD2 
3238 C CE1 A PHE   A 156 ? 0.2201 0.1709 0.2566 0.0261  0.0020  0.0535  156 PHE   A CE1 
3239 C CE1 B PHE   A 156 ? 0.2213 0.2251 0.3272 -0.0003 0.0119  -0.0135 156 PHE   A CE1 
3240 C CE1 T PHE   A 156 ? 0.1519 0.0993 0.1487 0.0158  0.0009  0.0434  156 PHE   A CE1 
3241 C CE2 A PHE   A 156 ? 0.2296 0.1681 0.2466 0.0381  -0.0172 0.0666  156 PHE   A CE2 
3242 C CE2 B PHE   A 156 ? 0.2190 0.2224 0.3346 -0.0166 0.0171  -0.0029 156 PHE   A CE2 
3243 C CE2 T PHE   A 156 ? 0.1554 0.1013 0.1528 0.0164  -0.0041 0.0496  156 PHE   A CE2 
3244 C CZ  A PHE   A 156 ? 0.2278 0.1742 0.2544 0.0342  -0.0034 0.0518  156 PHE   A CZ  
3245 C CZ  B PHE   A 156 ? 0.2222 0.2274 0.3306 -0.0059 0.0090  -0.0142 156 PHE   A CZ  
3246 C CZ  T PHE   A 156 ? 0.1523 0.0979 0.1538 0.0140  -0.0020 0.0451  156 PHE   A CZ  
3274 N N   A ASP   A 157 ? 0.1729 0.1429 0.2137 0.0367  0.0327  0.0622  157 ASP   A N   
3275 N N   B ASP   A 157 ? 0.1317 0.1356 0.2240 -0.0002 0.0241  0.0233  157 ASP   A N   
3276 N N   T ASP   A 157 ? 0.1606 0.1500 0.1681 0.0102  0.0230  0.0308  157 ASP   A N   
3277 C CA  A ASP   A 157 ? 0.1756 0.1584 0.2185 0.0408  0.0301  0.0638  157 ASP   A CA  
3278 C CA  B ASP   A 157 ? 0.1336 0.1377 0.2321 -0.0024 0.0204  0.0423  157 ASP   A CA  
3279 C CA  T ASP   A 157 ? 0.1651 0.1622 0.1777 0.0141  0.0201  0.0281  157 ASP   A CA  
3280 C C   A ASP   A 157 ? 0.1737 0.1678 0.2363 0.0398  0.0424  0.0632  157 ASP   A C   
3281 C C   B ASP   A 157 ? 0.1363 0.1414 0.2397 0.0032  0.0215  0.0475  157 ASP   A C   
3282 C C   T ASP   A 157 ? 0.1720 0.1724 0.1909 0.0147  0.0227  0.0253  157 ASP   A C   
3283 O O   A ASP   A 157 ? 0.1673 0.1647 0.2350 0.0406  0.0462  0.0632  157 ASP   A O   
3284 O O   B ASP   A 157 ? 0.1419 0.1413 0.2575 -0.0013 0.0286  0.0393  157 ASP   A O   
3285 O O   T ASP   A 157 ? 0.1703 0.1713 0.1906 0.0171  0.0242  0.0228  157 ASP   A O   
3286 C CB  A ASP   A 157 ? 0.1838 0.1699 0.2271 0.0440  0.0210  0.0530  157 ASP   A CB  
3287 C CB  B ASP   A 157 ? 0.1349 0.1370 0.2394 -0.0012 0.0072  0.0458  157 ASP   A CB  
3288 C CB  T ASP   A 157 ? 0.1632 0.1642 0.1796 0.0178  0.0156  0.0252  157 ASP   A CB  
3289 C CG  A ASP   A 157 ? 0.1975 0.1829 0.2335 0.0436  0.0133  0.0515  157 ASP   A CG  
3290 C CG  B ASP   A 157 ? 0.1352 0.1359 0.2523 -0.0007 -0.0064 0.0436  157 ASP   A CG  
3291 C CG  T ASP   A 157 ? 0.1627 0.1652 0.1793 0.0219  0.0111  0.0249  157 ASP   A CG  
3292 O OD1 A ASP   A 157 ? 0.2052 0.1932 0.2548 0.0389  0.0124  0.0455  157 ASP   A OD1 
3293 O OD1 B ASP   A 157 ? 0.1454 0.1384 0.2709 -0.0020 -0.0119 0.0223  157 ASP   A OD1 
3294 O OD1 T ASP   A 157 ? 0.1617 0.1662 0.1831 0.0229  0.0089  0.0207  157 ASP   A OD1 
3295 O OD2 A ASP   A 157 ? 0.1988 0.1839 0.2295 0.0455  0.0077  0.0548  157 ASP   A OD2 
3296 O OD2 B ASP   A 157 ? 0.1416 0.1506 0.2694 0.0051  -0.0162 0.0596  157 ASP   A OD2 
3297 O OD2 T ASP   A 157 ? 0.1625 0.1651 0.1765 0.0237  0.0095  0.0290  157 ASP   A OD2 
3310 N N   A LYS   A 158 ? 0.1850 0.1833 0.2627 0.0347  0.0513  0.0570  158 LYS   A N   
3311 N N   B LYS   A 158 ? 0.1392 0.1466 0.2401 0.0093  0.0286  0.0601  158 LYS   A N   
3312 N N   T LYS   A 158 ? 0.1820 0.1836 0.2067 0.0119  0.0239  0.0236  158 LYS   A N   
3313 C CA  A LYS   A 158 ? 0.1929 0.2044 0.2838 0.0284  0.0547  0.0538  158 LYS   A CA  
3314 C CA  B LYS   A 158 ? 0.1361 0.1616 0.2548 0.0115  0.0372  0.0644  158 LYS   A CA  
3315 C CA  T LYS   A 158 ? 0.1908 0.1968 0.2240 0.0085  0.0226  0.0214  158 LYS   A CA  
3316 C C   A LYS   A 158 ? 0.1889 0.2099 0.2861 0.0209  0.0503  0.0595  158 LYS   A C   
3317 C C   B LYS   A 158 ? 0.1266 0.1426 0.2611 0.0102  0.0304  0.0612  158 LYS   A C   
3318 C C   T LYS   A 158 ? 0.1941 0.2031 0.2279 0.0074  0.0199  0.0233  158 LYS   A C   
3319 O O   A LYS   A 158 ? 0.1902 0.2125 0.2939 0.0180  0.0489  0.0628  158 LYS   A O   
3320 O O   B LYS   A 158 ? 0.1379 0.1470 0.2810 0.0029  0.0362  0.0489  158 LYS   A O   
3321 O O   T LYS   A 158 ? 0.1951 0.2043 0.2311 0.0068  0.0195  0.0237  158 LYS   A O   
3322 C CB  A LYS   A 158 ? 0.2052 0.2185 0.2974 0.0289  0.0644  0.0517  158 LYS   A CB  
3323 C CB  B LYS   A 158 ? 0.1473 0.1947 0.2853 0.0112  0.0558  0.0574  158 LYS   A CB  
3324 C CB  T LYS   A 158 ? 0.1961 0.2026 0.2373 0.0059  0.0256  0.0194  158 LYS   A CB  
3325 C CG  A LYS   A 158 ? 0.2198 0.2333 0.3138 0.0296  0.0736  0.0497  158 LYS   A CG  
3326 C CG  B LYS   A 158 ? 0.1613 0.2236 0.3029 0.0054  0.0645  0.0584  158 LYS   A CG  
3327 C CG  T LYS   A 158 ? 0.2013 0.2078 0.2495 0.0032  0.0292  0.0191  158 LYS   A CG  
3328 C CD  A LYS   A 158 ? 0.2322 0.2475 0.3235 0.0324  0.0830  0.0489  158 LYS   A CD  
3329 C CD  B LYS   A 158 ? 0.1808 0.2467 0.3217 0.0031  0.0601  0.0515  158 LYS   A CD  
3330 C CD  T LYS   A 158 ? 0.2052 0.2114 0.2591 0.0016  0.0315  0.0204  158 LYS   A CD  
3331 C CE  A LYS   A 158 ? 0.2418 0.2571 0.3301 0.0328  0.0892  0.0560  158 LYS   A CE  
3332 C CE  B LYS   A 158 ? 0.1932 0.2538 0.3269 0.0052  0.0527  0.0479  158 LYS   A CE  
3333 C CE  T LYS   A 158 ? 0.2076 0.2134 0.2661 -0.0005 0.0330  0.0234  158 LYS   A CE  
3334 N NZ  A LYS   A 158 ? 0.2468 0.2603 0.3293 0.0326  0.0943  0.0623  158 LYS   A NZ  
3335 N NZ  B LYS   A 158 ? 0.2042 0.2578 0.3303 0.0084  0.0488  0.0412  158 LYS   A NZ  
3336 N NZ  T LYS   A 158 ? 0.2083 0.2133 0.2671 -0.0023 0.0356  0.0270  158 LYS   A NZ  
3376 N N   A ASN   A 159 ? 0.1853 0.2119 0.2862 0.0111  0.0419  0.0612  159 ASN   A N   
3377 N N   B ASN   A 159 ? 0.1274 0.1382 0.2708 0.0006  0.0082  0.0523  159 ASN   A N   
3378 N N   T ASN   A 159 ? 0.1968 0.2073 0.2313 0.0047  0.0157  0.0238  159 ASN   A N   
3379 C CA  A ASN   A 159 ? 0.1832 0.2102 0.2777 0.0020  0.0327  0.0670  159 ASN   A CA  
3380 C CA  B ASN   A 159 ? 0.1390 0.1407 0.2820 -0.0065 0.0015  0.0511  159 ASN   A CA  
3381 C CA  T ASN   A 159 ? 0.1996 0.2099 0.2308 0.0018  0.0115  0.0242  159 ASN   A CA  
3382 C C   A ASN   A 159 ? 0.1775 0.2098 0.2736 -0.0027 0.0307  0.0639  159 ASN   A C   
3383 C C   B ASN   A 159 ? 0.1410 0.1536 0.2856 -0.0032 -0.0032 0.0338  159 ASN   A C   
3384 C C   T ASN   A 159 ? 0.2000 0.2108 0.2300 -0.0010 0.0105  0.0227  159 ASN   A C   
3385 O O   A ASN   A 159 ? 0.1795 0.2150 0.2813 0.0009  0.0221  0.0594  159 ASN   A O   
3386 O O   B ASN   A 159 ? 0.1294 0.1527 0.2991 -0.0036 -0.0179 0.0029  159 ASN   A O   
3387 O O   T ASN   A 159 ? 0.2007 0.2127 0.2318 -0.0011 0.0089  0.0229  159 ASN   A O   
3388 C CB  A ASN   A 159 ? 0.1835 0.2104 0.2743 -0.0049 0.0267  0.0764  159 ASN   A CB  
3389 C CB  B ASN   A 159 ? 0.1586 0.1559 0.3065 0.0029  -0.0188 0.0571  159 ASN   A CB  
3390 C CB  T ASN   A 159 ? 0.2009 0.2116 0.2332 0.0002  0.0082  0.0259  159 ASN   A CB  
3391 C CG  A ASN   A 159 ? 0.1867 0.2130 0.2762 -0.0097 0.0246  0.0795  159 ASN   A CG  
3392 C CG  B ASN   A 159 ? 0.1716 0.1774 0.3341 0.0115  -0.0249 0.0478  159 ASN   A CG  
3393 C CG  T ASN   A 159 ? 0.2027 0.2134 0.2362 -0.0014 0.0066  0.0261  159 ASN   A CG  
3394 O OD1 A ASN   A 159 ? 0.1893 0.2150 0.2876 -0.0127 0.0297  0.0824  159 ASN   A OD1 
3395 O OD1 B ASN   A 159 ? 0.1744 0.1969 0.3556 0.0198  -0.0045 0.0447  159 ASN   A OD1 
3396 O OD1 T ASN   A 159 ? 0.2035 0.2147 0.2415 -0.0023 0.0085  0.0275  159 ASN   A OD1 
3397 N ND2 A ASN   A 159 ? 0.1867 0.2137 0.2694 -0.0078 0.0227  0.0813  159 ASN   A ND2 
3398 N ND2 B ASN   A 159 ? 0.1799 0.1876 0.3428 0.0234  -0.0467 0.0452  159 ASN   A ND2 
3399 N ND2 T ASN   A 159 ? 0.2033 0.2141 0.2342 -0.0006 0.0043  0.0257  159 ASN   A ND2 
3418 N N   A LEU   A 160 ? 0.1706 0.2041 0.2653 -0.0053 0.0344  0.0656  160 LEU   A N   
3419 N N   B LEU   A 160 ? 0.1486 0.1575 0.2727 0.0060  0.0105  0.0505  160 LEU   A N   
3420 N N   T LEU   A 160 ? 0.1998 0.2097 0.2291 -0.0025 0.0116  0.0219  160 LEU   A N   
3421 C CA  A LEU   A 160 ? 0.1693 0.2029 0.2571 -0.0023 0.0362  0.0615  160 LEU   A CA  
3422 C CA  B LEU   A 160 ? 0.1598 0.1695 0.2801 0.0066  0.0198  0.0466  160 LEU   A CA  
3423 C CA  T LEU   A 160 ? 0.2007 0.2090 0.2259 -0.0040 0.0141  0.0202  160 LEU   A CA  
3424 C C   A LEU   A 160 ? 0.1618 0.2019 0.2512 0.0035  0.0368  0.0603  160 LEU   A C   
3425 C C   B LEU   A 160 ? 0.1508 0.1594 0.2784 0.0097  0.0243  0.0557  160 LEU   A C   
3426 O O   A LEU   A 160 ? 0.1584 0.2046 0.2528 0.0049  0.0338  0.0614  160 LEU   A O   
3427 O O   B LEU   A 160 ? 0.1524 0.1660 0.2810 0.0062  0.0171  0.0600  160 LEU   A O   
3428 C CB  A LEU   A 160 ? 0.1674 0.2061 0.2524 -0.0033 0.0400  0.0561  160 LEU   A CB  
3429 C CB  B LEU   A 160 ? 0.1727 0.1890 0.2810 0.0073  0.0232  0.0286  160 LEU   A CB  
3430 C CB  T LEU   A 160 ? 0.1999 0.2089 0.2236 -0.0046 0.0164  0.0183  160 LEU   A CB  
3431 C CG  A LEU   A 160 ? 0.1665 0.2109 0.2560 -0.0027 0.0366  0.0404  160 LEU   A CG  
3432 C CG  B LEU   A 160 ? 0.1897 0.2124 0.2878 0.0084  0.0136  0.0054  160 LEU   A CG  
3433 C CG  T LEU   A 160 ? 0.1986 0.2084 0.2220 -0.0055 0.0176  0.0146  160 LEU   A CG  
3434 C CD1 A LEU   A 160 ? 0.1671 0.2126 0.2581 -0.0034 0.0354  0.0360  160 LEU   A CD1 
3435 C CD1 B LEU   A 160 ? 0.1911 0.2177 0.2896 0.0060  0.0121  -0.0005 160 LEU   A CD1 
3436 C CD1 T LEU   A 160 ? 0.1980 0.2086 0.2229 -0.0055 0.0172  0.0128  160 LEU   A CD1 
3437 C CD2 A LEU   A 160 ? 0.1647 0.2137 0.2547 -0.0025 0.0362  0.0382  160 LEU   A CD2 
3438 C CD2 B LEU   A 160 ? 0.1995 0.2227 0.2883 0.0100  0.0108  0.0069  160 LEU   A CD2 
3439 C CD2 T LEU   A 160 ? 0.1980 0.2080 0.2211 -0.0061 0.0189  0.0149  160 LEU   A CD2 
3472 N N   A TYR   A 161 ? 0.1615 0.1995 0.2506 0.0037  0.0387  0.0595  161 TYR   A N   
3473 N N   B TYR   A 161 ? 0.1480 0.1524 0.2820 0.0110  0.0304  0.0573  161 TYR   A N   
3474 C CA  A TYR   A 161 ? 0.1578 0.1997 0.2435 0.0066  0.0386  0.0554  161 TYR   A CA  
3475 C CA  B TYR   A 161 ? 0.1417 0.1520 0.2674 0.0118  0.0298  0.0446  161 TYR   A CA  
3476 C C   A TYR   A 161 ? 0.1584 0.2083 0.2517 0.0097  0.0313  0.0627  161 TYR   A C   
3477 C C   B TYR   A 161 ? 0.1484 0.1609 0.2740 0.0057  0.0200  0.0506  161 TYR   A C   
3478 O O   A TYR   A 161 ? 0.1551 0.2085 0.2529 0.0094  0.0270  0.0598  161 TYR   A O   
3479 O O   B TYR   A 161 ? 0.1417 0.1595 0.2597 0.0036  0.0093  0.0520  161 TYR   A O   
3480 C CB  A TYR   A 161 ? 0.1609 0.1987 0.2421 0.0038  0.0460  0.0429  161 TYR   A CB  
3481 C CB  B TYR   A 161 ? 0.1443 0.1614 0.2645 0.0142  0.0386  0.0286  161 TYR   A CB  
3482 C CG  A TYR   A 161 ? 0.1590 0.1932 0.2377 0.0073  0.0368  0.0417  161 TYR   A CG  
3483 C CG  B TYR   A 161 ? 0.1316 0.1575 0.2560 0.0176  0.0344  0.0252  161 TYR   A CG  
3484 C CD1 A TYR   A 161 ? 0.1609 0.1921 0.2476 0.0077  0.0326  0.0382  161 TYR   A CD1 
3485 C CD1 B TYR   A 161 ? 0.1330 0.1545 0.2636 0.0165  0.0339  0.0267  161 TYR   A CD1 
3486 C CD2 A TYR   A 161 ? 0.1575 0.1899 0.2292 0.0121  0.0306  0.0461  161 TYR   A CD2 
3487 C CD2 B TYR   A 161 ? 0.1281 0.1660 0.2472 0.0178  0.0342  0.0156  161 TYR   A CD2 
3488 C CE1 A TYR   A 161 ? 0.1608 0.1863 0.2488 0.0095  0.0243  0.0484  161 TYR   A CE1 
3489 C CE1 B TYR   A 161 ? 0.1294 0.1580 0.2680 0.0137  0.0284  0.0338  161 TYR   A CE1 
3490 C CE2 A TYR   A 161 ? 0.1586 0.1829 0.2323 0.0105  0.0185  0.0562  161 TYR   A CE2 
3491 C CE2 B TYR   A 161 ? 0.1249 0.1682 0.2470 0.0054  0.0326  0.0183  161 TYR   A CE2 
3492 C CZ  A TYR   A 161 ? 0.1635 0.1808 0.2427 0.0096  0.0115  0.0574  161 TYR   A CZ  
3493 C CZ  B TYR   A 161 ? 0.1363 0.1683 0.2570 -0.0026 0.0274  0.0262  161 TYR   A CZ  
3494 O OH  A TYR   A 161 ? 0.1708 0.1755 0.2556 0.0133  -0.0007 0.0722  161 TYR   A OH  
3495 O OH  B TYR   A 161 ? 0.1545 0.1822 0.2667 -0.0153 0.0289  0.0250  161 TYR   A OH  
3514 N N   A ASP   A 162 ? 0.1568 0.2201 0.2538 0.0089  0.0361  0.0739  162 ASP   A N   
3515 N N   B ASP   A 162 ? 0.1506 0.1749 0.2888 -0.0013 0.0246  0.0668  162 ASP   A N   
3516 C CA  A ASP   A 162 ? 0.1545 0.2334 0.2574 0.0100  0.0363  0.0796  162 ASP   A CA  
3517 C CA  B ASP   A 162 ? 0.1530 0.1915 0.2891 0.0060  0.0172  0.0810  162 ASP   A CA  
3518 C C   A ASP   A 162 ? 0.1491 0.2358 0.2503 0.0008  0.0327  0.0911  162 ASP   A C   
3519 C C   B ASP   A 162 ? 0.1569 0.1864 0.2844 0.0018  -0.0027 0.0746  162 ASP   A C   
3520 O O   A ASP   A 162 ? 0.1521 0.2353 0.2561 -0.0001 0.0363  0.0980  162 ASP   A O   
3521 O O   B ASP   A 162 ? 0.1587 0.1825 0.2828 0.0012  -0.0060 0.0659  162 ASP   A O   
3522 C CB  A ASP   A 162 ? 0.1636 0.2438 0.2627 0.0167  0.0385  0.0754  162 ASP   A CB  
3523 C CB  B ASP   A 162 ? 0.1587 0.2111 0.3059 0.0182  0.0229  0.0925  162 ASP   A CB  
3524 C CG  A ASP   A 162 ? 0.1726 0.2562 0.2740 0.0190  0.0443  0.0701  162 ASP   A CG  
3525 C CG  B ASP   A 162 ? 0.1633 0.2220 0.3142 0.0255  0.0338  0.1049  162 ASP   A CG  
3526 O OD1 A ASP   A 162 ? 0.1799 0.2594 0.2756 0.0158  0.0471  0.0746  162 ASP   A OD1 
3527 O OD1 B ASP   A 162 ? 0.1679 0.2304 0.3217 0.0285  0.0370  0.1063  162 ASP   A OD1 
3528 O OD2 A ASP   A 162 ? 0.1771 0.2619 0.2920 0.0248  0.0491  0.0614  162 ASP   A OD2 
3529 O OD2 B ASP   A 162 ? 0.1688 0.2320 0.3212 0.0360  0.0455  0.1078  162 ASP   A OD2 
3538 N N   A LYS   A 163 ? 0.1477 0.2410 0.2508 0.0001  0.0210  0.0884  163 LYS   A N   
3539 N N   B LYS   A 163 ? 0.1670 0.1981 0.2844 -0.0000 -0.0071 0.0714  163 LYS   A N   
3540 C CA  A LYS   A 163 ? 0.1511 0.2483 0.2635 -0.0051 0.0081  0.0720  163 LYS   A CA  
3541 C CA  B LYS   A 163 ? 0.1755 0.2044 0.2832 0.0002  -0.0088 0.0678  163 LYS   A CA  
3542 C C   A LYS   A 163 ? 0.1448 0.2386 0.2637 -0.0133 0.0085  0.0647  163 LYS   A C   
3543 C C   B LYS   A 163 ? 0.1686 0.1893 0.2605 -0.0014 -0.0087 0.0544  163 LYS   A C   
3544 O O   A LYS   A 163 ? 0.1448 0.2411 0.2778 -0.0161 0.0038  0.0655  163 LYS   A O   
3545 O O   B LYS   A 163 ? 0.1616 0.1844 0.2497 -0.0039 -0.0158 0.0390  163 LYS   A O   
3546 C CB  A LYS   A 163 ? 0.1702 0.2639 0.2864 0.0047  0.0026  0.0603  163 LYS   A CB  
3547 C CB  B LYS   A 163 ? 0.2060 0.2305 0.3001 0.0044  0.0017  0.0774  163 LYS   A CB  
3548 C CG  A LYS   A 163 ? 0.1885 0.2771 0.3205 0.0046  0.0012  0.0502  163 LYS   A CG  
3549 C CG  B LYS   A 163 ? 0.2373 0.2578 0.3393 0.0020  0.0139  0.0785  163 LYS   A CG  
3550 C CD  A LYS   A 163 ? 0.2011 0.2883 0.3517 0.0011  -0.0003 0.0410  163 LYS   A CD  
3551 C CD  B LYS   A 163 ? 0.2609 0.2817 0.3759 0.0002  0.0258  0.0771  163 LYS   A CD  
3552 C CE  A LYS   A 163 ? 0.2100 0.2961 0.3791 -0.0042 -0.0011 0.0338  163 LYS   A CE  
3553 C CE  B LYS   A 163 ? 0.2727 0.2985 0.4097 -0.0030 0.0325  0.0761  163 LYS   A CE  
3554 N NZ  A LYS   A 163 ? 0.2136 0.3014 0.3888 -0.0089 -0.0017 0.0338  163 LYS   A NZ  
3555 N NZ  B LYS   A 163 ? 0.2783 0.3072 0.4329 -0.0039 0.0329  0.0687  163 LYS   A NZ  
3582 N N   A LEU   A 164 ? 0.1317 0.2213 0.2435 -0.0142 0.0119  0.0572  164 LEU   A N   
3583 N N   B LEU   A 164 ? 0.1613 0.1793 0.2393 0.0077  -0.0026 0.0524  164 LEU   A N   
3584 C CA  A LEU   A 164 ? 0.1282 0.2070 0.2304 -0.0219 0.0203  0.0456  164 LEU   A CA  
3585 C CA  B LEU   A 164 ? 0.1659 0.1760 0.2319 0.0058  0.0062  0.0440  164 LEU   A CA  
3586 C C   A LEU   A 164 ? 0.1312 0.2088 0.2291 -0.0153 0.0201  0.0386  164 LEU   A C   
3587 C C   B LEU   A 164 ? 0.1630 0.1659 0.2285 0.0033  0.0042  0.0384  164 LEU   A C   
3588 O O   A LEU   A 164 ? 0.1311 0.2118 0.2141 -0.0161 0.0276  0.0347  164 LEU   A O   
3589 O O   B LEU   A 164 ? 0.1639 0.1686 0.2246 -0.0048 0.0094  0.0287  164 LEU   A O   
3590 C CB  A LEU   A 164 ? 0.1241 0.1956 0.2168 -0.0314 0.0247  0.0333  164 LEU   A CB  
3591 C CB  B LEU   A 164 ? 0.1677 0.1807 0.2279 0.0094  0.0122  0.0349  164 LEU   A CB  
3592 C CG  A LEU   A 164 ? 0.1323 0.1906 0.2186 -0.0330 0.0258  0.0257  164 LEU   A CG  
3593 C CG  B LEU   A 164 ? 0.1771 0.1869 0.2280 0.0108  0.0198  0.0361  164 LEU   A CG  
3594 C CD1 A LEU   A 164 ? 0.1285 0.1885 0.2264 -0.0349 0.0311  0.0243  164 LEU   A CD1 
3595 C CD1 B LEU   A 164 ? 0.1764 0.1905 0.2393 0.0139  0.0333  0.0360  164 LEU   A CD1 
3596 C CD2 A LEU   A 164 ? 0.1405 0.1915 0.2117 -0.0328 0.0257  0.0213  164 LEU   A CD2 
3597 C CD2 B LEU   A 164 ? 0.1842 0.1912 0.2282 0.0029  0.0133  0.0347  164 LEU   A CD2 
3620 N N   A VAL   A 165 ? 0.1241 0.2113 0.2401 -0.0158 0.0222  0.0373  165 VAL   A N   
3621 N N   B VAL   A 165 ? 0.1499 0.1620 0.2222 -0.0030 0.0100  0.0469  165 VAL   A N   
3622 C CA  A VAL   A 165 ? 0.1314 0.2180 0.2354 -0.0116 0.0277  0.0389  165 VAL   A CA  
3623 C CA  B VAL   A 165 ? 0.1550 0.1634 0.2153 0.0028  0.0062  0.0428  165 VAL   A CA  
3624 C C   A VAL   A 165 ? 0.1329 0.2235 0.2342 -0.0108 0.0246  0.0399  165 VAL   A C   
3625 C C   B VAL   A 165 ? 0.1488 0.1622 0.2099 0.0008  0.0110  0.0444  165 VAL   A C   
3626 O O   A VAL   A 165 ? 0.1287 0.2283 0.2340 -0.0161 0.0363  0.0394  165 VAL   A O   
3627 O O   B VAL   A 165 ? 0.1463 0.1575 0.2069 -0.0018 0.0144  0.0360  165 VAL   A O   
3628 C CB  A VAL   A 165 ? 0.1385 0.2189 0.2343 -0.0112 0.0363  0.0420  165 VAL   A CB  
3629 C CB  B VAL   A 165 ? 0.1701 0.1739 0.2169 0.0027  0.0094  0.0324  165 VAL   A CB  
3630 C CG1 A VAL   A 165 ? 0.1413 0.2211 0.2254 -0.0119 0.0390  0.0436  165 VAL   A CG1 
3631 C CG1 B VAL   A 165 ? 0.1758 0.1767 0.2055 0.0017  0.0115  0.0217  165 VAL   A CG1 
3632 C CG2 A VAL   A 165 ? 0.1443 0.2189 0.2370 -0.0103 0.0368  0.0436  165 VAL   A CG2 
3633 C CG2 B VAL   A 165 ? 0.1779 0.1743 0.2228 0.0027  0.0036  0.0371  165 VAL   A CG2 
3652 N N   A SER   A 166 ? 0.1316 0.2256 0.2340 -0.0063 0.0220  0.0432  166 SER   A N   
3653 N N   B SER   A 166 ? 0.1370 0.1769 0.2164 0.0036  0.0148  0.0464  166 SER   A N   
3654 C CA  A SER   A 166 ? 0.1358 0.2321 0.2300 -0.0077 0.0192  0.0444  166 SER   A CA  
3655 C CA  B SER   A 166 ? 0.1448 0.1990 0.2225 0.0004  0.0101  0.0446  166 SER   A CA  
3656 C C   A SER   A 166 ? 0.1444 0.2406 0.2279 -0.0074 0.0039  0.0468  166 SER   A C   
3657 C C   B SER   A 166 ? 0.1393 0.2024 0.2092 0.0014  -0.0079 0.0445  166 SER   A C   
3658 O O   A SER   A 166 ? 0.1501 0.2475 0.2378 -0.0036 -0.0016 0.0476  166 SER   A O   
3659 O O   B SER   A 166 ? 0.1512 0.2072 0.2077 -0.0052 -0.0272 0.0371  166 SER   A O   
3660 C CB  A SER   A 166 ? 0.1388 0.2332 0.2400 -0.0081 0.0165  0.0349  166 SER   A CB  
3661 C CB  B SER   A 166 ? 0.1593 0.2184 0.2584 0.0003  -0.0030 0.0357  166 SER   A CB  
3662 O OG  A SER   A 166 ? 0.1449 0.2360 0.2421 -0.0120 0.0192  0.0290  166 SER   A OG  
3663 O OG  B SER   A 166 ? 0.1750 0.2373 0.2912 -0.0046 -0.0089 0.0362  166 SER   A OG  
3674 N N   A SER   A 167 ? 0.1550 0.2455 0.2344 -0.0084 0.0001  0.0397  167 SER   A N   
3675 N N   B SER   A 167 ? 0.1396 0.2137 0.2069 0.0113  -0.0017 0.0519  167 SER   A N   
3676 C CA  A SER   A 167 ? 0.1736 0.2498 0.2369 -0.0092 -0.0048 0.0318  167 SER   A CA  
3677 C CA  B SER   A 167 ? 0.1614 0.2229 0.2136 0.0102  0.0020  0.0481  167 SER   A CA  
3678 C C   A SER   A 167 ? 0.1788 0.2485 0.2274 -0.0062 0.0019  0.0283  167 SER   A C   
3679 C C   B SER   A 167 ? 0.1645 0.2222 0.2096 0.0177  0.0219  0.0467  167 SER   A C   
3680 O O   A SER   A 167 ? 0.1874 0.2530 0.2339 -0.0015 -0.0033 0.0303  167 SER   A O   
3681 O O   B SER   A 167 ? 0.1799 0.2335 0.2271 0.0213  0.0128  0.0487  167 SER   A O   
3682 C CB  A SER   A 167 ? 0.1840 0.2548 0.2455 -0.0085 -0.0001 0.0375  167 SER   A CB  
3683 C CB  B SER   A 167 ? 0.1756 0.2317 0.2150 0.0056  0.0104  0.0623  167 SER   A CB  
3684 O OG  A SER   A 167 ? 0.1904 0.2586 0.2500 -0.0092 0.0029  0.0373  167 SER   A OG  
3685 O OG  B SER   A 167 ? 0.1823 0.2405 0.2157 0.0002  0.0300  0.0610  167 SER   A OG  
3696 N N   A PHE   A 168 ? 0.1756 0.2434 0.2194 -0.0048 0.0036  0.0267  168 PHE   A N   
3697 N N   B PHE   A 168 ? 0.1539 0.2110 0.1975 0.0277  0.0339  0.0491  168 PHE   A N   
3698 C CA  A PHE   A 168 ? 0.1760 0.2394 0.2164 -0.0094 0.0082  0.0257  168 PHE   A CA  
3699 C CA  B PHE   A 168 ? 0.1455 0.2057 0.2079 0.0279  0.0383  0.0462  168 PHE   A CA  
3700 C C   A PHE   A 168 ? 0.1964 0.2540 0.2420 -0.0113 0.0211  0.0198  168 PHE   A C   
3701 C C   B PHE   A 168 ? 0.1530 0.2096 0.2017 0.0254  0.0600  0.0327  168 PHE   A C   
3702 O O   A PHE   A 168 ? 0.2043 0.2572 0.2651 -0.0187 0.0260  0.0202  168 PHE   A O   
3703 O O   B PHE   A 168 ? 0.1573 0.2127 0.2364 0.0063  0.0652  0.0197  168 PHE   A O   
3704 C CB  A PHE   A 168 ? 0.1665 0.2260 0.1955 -0.0123 -0.0025 0.0202  168 PHE   A CB  
3705 C CB  B PHE   A 168 ? 0.1493 0.2012 0.2207 0.0277  0.0263  0.0460  168 PHE   A CB  
3706 C CG  A PHE   A 168 ? 0.1502 0.2112 0.1752 -0.0171 -0.0096 0.0179  168 PHE   A CG  
3707 C CG  B PHE   A 168 ? 0.1483 0.1899 0.2313 0.0178  0.0236  0.0462  168 PHE   A CG  
3708 C CD1 A PHE   A 168 ? 0.1438 0.2053 0.1790 -0.0224 -0.0103 0.0198  168 PHE   A CD1 
3709 C CD1 B PHE   A 168 ? 0.1537 0.1879 0.2471 0.0107  0.0215  0.0519  168 PHE   A CD1 
3710 C CD2 A PHE   A 168 ? 0.1477 0.2064 0.1696 -0.0152 -0.0041 0.0151  168 PHE   A CD2 
3711 C CD2 B PHE   A 168 ? 0.1417 0.1867 0.2343 0.0055  0.0422  0.0510  168 PHE   A CD2 
3712 C CE1 A PHE   A 168 ? 0.1322 0.2005 0.1708 -0.0271 -0.0141 0.0125  168 PHE   A CE1 
3713 C CE1 B PHE   A 168 ? 0.1516 0.1904 0.2557 0.0067  0.0273  0.0566  168 PHE   A CE1 
3714 C CE2 A PHE   A 168 ? 0.1504 0.2015 0.1753 -0.0131 -0.0046 0.0142  168 PHE   A CE2 
3715 C CE2 B PHE   A 168 ? 0.1515 0.1844 0.2504 0.0081  0.0380  0.0592  168 PHE   A CE2 
3716 C CZ  A PHE   A 168 ? 0.1417 0.2004 0.1768 -0.0193 -0.0127 0.0092  168 PHE   A CZ  
3717 C CZ  B PHE   A 168 ? 0.1487 0.1849 0.2509 0.0060  0.0333  0.0576  168 PHE   A CZ  
3736 N N   A LEU   A 169 ? 0.2196 0.2659 0.2667 -0.0124 0.0221  0.0064  169 LEU   A N   
3737 N N   B LEU   A 169 ? 0.1901 0.2128 0.2101 0.0252  0.0582  0.0229  169 LEU   A N   
3738 C CA  A LEU   A 169 ? 0.2465 0.2798 0.2938 -0.0058 0.0162  -0.0040 169 LEU   A CA  
3739 C CA  B LEU   A 169 ? 0.2223 0.2260 0.2223 0.0364  0.0413  0.0183  169 LEU   A CA  
3740 C C   A LEU   A 169 ? 0.2498 0.2834 0.3043 -0.0045 0.0221  -0.0004 169 LEU   A C   
3741 C C   B LEU   A 169 ? 0.2148 0.2244 0.2036 0.0261  0.0461  0.0356  169 LEU   A C   
3742 O O   A LEU   A 169 ? 0.2546 0.2900 0.3135 -0.0009 0.0178  -0.0013 169 LEU   A O   
3743 O O   B LEU   A 169 ? 0.2139 0.2323 0.2101 0.0305  0.0459  0.0329  169 LEU   A O   
3744 C CB  A LEU   A 169 ? 0.2653 0.2896 0.3111 -0.0026 0.0120  -0.0159 169 LEU   A CB  
3745 C CB  B LEU   A 169 ? 0.2529 0.2483 0.2583 0.0396  0.0308  -0.0079 169 LEU   A CB  
3746 C CG  A LEU   A 169 ? 0.2811 0.2964 0.3253 -0.0010 0.0096  -0.0282 169 LEU   A CG  
3747 C CG  B LEU   A 169 ? 0.2689 0.2648 0.2879 0.0424  0.0239  -0.0318 169 LEU   A CG  
3748 C CD1 A LEU   A 169 ? 0.2890 0.2969 0.3346 -0.0019 0.0053  -0.0317 169 LEU   A CD1 
3749 C CD1 B LEU   A 169 ? 0.2705 0.2684 0.3069 0.0415  0.0139  -0.0359 169 LEU   A CD1 
3750 C CD2 A LEU   A 169 ? 0.2842 0.3001 0.3307 -0.0021 0.0118  -0.0307 169 LEU   A CD2 
3751 C CD2 B LEU   A 169 ? 0.2774 0.2734 0.2991 0.0401  0.0239  -0.0381 169 LEU   A CD2 
3752 O OXT A LEU   A 169 ? 0.2491 0.2821 0.3034 -0.0053 0.0327  -0.0016 169 LEU   A OXT 
3753 O OXT B LEU   A 169 ? 0.2151 0.2244 0.2019 0.0100  0.0436  0.0436  169 LEU   A OXT 
3776 N N   A SER   B 1   ? 0.3415 0.3393 0.3811 -0.0709 -0.0666 0.0480  1   SER   B N   
3777 N N   B SER   B 1   ? 0.3142 0.3439 0.3455 -0.1020 -0.0878 0.0496  1   SER   B N   
3778 C CA  A SER   B 1   ? 0.3358 0.3365 0.3723 -0.0731 -0.0671 0.0487  1   SER   B CA  
3779 C CA  B SER   B 1   ? 0.3020 0.3435 0.3329 -0.1060 -0.0954 0.0494  1   SER   B CA  
3780 C C   A SER   B 1   ? 0.3204 0.3276 0.3596 -0.0742 -0.0657 0.0601  1   SER   B C   
3781 C C   B SER   B 1   ? 0.2758 0.3387 0.3023 -0.1053 -0.1049 0.0632  1   SER   B C   
3782 O O   A SER   B 1   ? 0.3271 0.3296 0.3569 -0.0699 -0.0625 0.0597  1   SER   B O   
3783 O O   B SER   B 1   ? 0.2757 0.3377 0.2777 -0.1020 -0.1127 0.0676  1   SER   B O   
3784 C CB  A SER   B 1   ? 0.3431 0.3402 0.3873 -0.0718 -0.0642 0.0393  1   SER   B CB  
3785 C CB  B SER   B 1   ? 0.3139 0.3456 0.3657 -0.1066 -0.0849 0.0351  1   SER   B CB  
3786 O OG  A SER   B 1   ? 0.3501 0.3469 0.4019 -0.0702 -0.0573 0.0315  1   SER   B OG  
3787 O OG  B SER   B 1   ? 0.3249 0.3537 0.3954 -0.1067 -0.0728 0.0226  1   SER   B OG  
3802 N N   A MET   B 2   ? 0.2995 0.3148 0.3507 -0.0783 -0.0622 0.0806  2   MET   B N   
3803 N N   B MET   B 2   ? 0.2617 0.3350 0.3070 -0.0994 -0.0927 0.0870  2   MET   B N   
3804 C CA  A MET   B 2   ? 0.2805 0.3015 0.3448 -0.0738 -0.0599 0.0948  2   MET   B CA  
3805 C CA  B MET   B 2   ? 0.2591 0.3312 0.3171 -0.0767 -0.0803 0.1016  2   MET   B CA  
3806 C C   A MET   B 2   ? 0.2410 0.2704 0.2957 -0.0763 -0.0684 0.1167  2   MET   B C   
3807 C C   B MET   B 2   ? 0.2370 0.3052 0.2857 -0.0558 -0.0756 0.1128  2   MET   B C   
3808 O O   A MET   B 2   ? 0.2263 0.2699 0.2814 -0.0826 -0.0741 0.1259  2   MET   B O   
3809 O O   B MET   B 2   ? 0.2398 0.3150 0.2925 -0.0480 -0.0734 0.1096  2   MET   B O   
3810 C CB  A MET   B 2   ? 0.3030 0.3216 0.4055 -0.0591 -0.0472 0.0773  2   MET   B CB  
3811 C CB  B MET   B 2   ? 0.2892 0.3556 0.3827 -0.0614 -0.0708 0.0961  2   MET   B CB  
3812 C CG  A MET   B 2   ? 0.3213 0.3370 0.4682 -0.0453 -0.0346 0.0666  2   MET   B CG  
3813 C CG  B MET   B 2   ? 0.3135 0.3751 0.4427 -0.0463 -0.0599 0.1009  2   MET   B CG  
3814 S SD  A MET   B 2   ? 0.3377 0.3494 0.5185 -0.0346 -0.0249 0.0570  2   MET   B SD  
3815 S SD  B MET   B 2   ? 0.3367 0.3925 0.4875 -0.0325 -0.0515 0.1047  2   MET   B SD  
3816 C CE  A MET   B 2   ? 0.3364 0.3508 0.5245 -0.0351 -0.0189 0.0544  2   MET   B CE  
3817 C CE  B MET   B 2   ? 0.3364 0.3928 0.4983 -0.0316 -0.0460 0.0978  2   MET   B CE  
3836 N N   A VAL   B 3   ? 0.2172 0.2380 0.2745 -0.0776 -0.0690 0.1175  3   VAL   B N   
3837 N N   B VAL   B 3   ? 0.2171 0.2681 0.2568 -0.0480 -0.0694 0.1115  3   VAL   B N   
3838 C CA  A VAL   B 3   ? 0.2039 0.2110 0.2594 -0.0713 -0.0613 0.1031  3   VAL   B CA  
3839 C CA  B VAL   B 3   ? 0.2127 0.2371 0.2529 -0.0382 -0.0502 0.0833  3   VAL   B CA  
3840 C C   A VAL   B 3   ? 0.1856 0.1989 0.2294 -0.0605 -0.0553 0.0941  3   VAL   B C   
3841 C C   B VAL   B 3   ? 0.1989 0.2218 0.2268 -0.0357 -0.0416 0.0769  3   VAL   B C   
3842 O O   A VAL   B 3   ? 0.1736 0.1851 0.2319 -0.0598 -0.0576 0.1078  3   VAL   B O   
3843 O O   B VAL   B 3   ? 0.2016 0.2290 0.2272 -0.0249 -0.0399 0.0690  3   VAL   B O   
3844 C CB  A VAL   B 3   ? 0.2156 0.2073 0.2828 -0.0746 -0.0534 0.0831  3   VAL   B CB  
3845 C CB  B VAL   B 3   ? 0.2270 0.2250 0.2727 -0.0365 -0.0367 0.0646  3   VAL   B CB  
3846 C CG1 A VAL   B 3   ? 0.2194 0.2064 0.2927 -0.0723 -0.0559 0.0762  3   VAL   B CG1 
3847 C CG1 B VAL   B 3   ? 0.2317 0.2230 0.2864 -0.0360 -0.0357 0.0598  3   VAL   B CG1 
3848 C CG2 A VAL   B 3   ? 0.2205 0.2072 0.2907 -0.0767 -0.0441 0.0827  3   VAL   B CG2 
3849 C CG2 B VAL   B 3   ? 0.2332 0.2228 0.2748 -0.0353 -0.0308 0.0636  3   VAL   B CG2 
3868 N N   . ASN   B 4   ? 0.1868 0.2000 0.2037 -0.0487 -0.0448 0.0777  4   ASN   B N   
3869 C CA  . ASN   B 4   ? 0.1853 0.1988 0.1748 -0.0490 -0.0372 0.0412  4   ASN   B CA  
3870 C C   . ASN   B 4   ? 0.1971 0.2147 0.1821 -0.0555 -0.0200 0.0243  4   ASN   B C   
3871 O O   . ASN   B 4   ? 0.1990 0.2254 0.2023 -0.0549 -0.0232 0.0111  4   ASN   B O   
3872 C CB  . ASN   B 4   ? 0.1772 0.1938 0.1675 -0.0404 -0.0474 0.0327  4   ASN   B CB  
3873 C CG  . ASN   B 4   ? 0.1721 0.1860 0.1621 -0.0432 -0.0459 0.0254  4   ASN   B CG  
3874 O OD1 . ASN   B 4   ? 0.1781 0.1707 0.1686 -0.0404 -0.0476 0.0223  4   ASN   B OD1 
3875 N ND2 . ASN   B 4   ? 0.1910 0.1957 0.1684 -0.0293 -0.0357 0.0201  4   ASN   B ND2 
3883 N N   . SER   B 5   ? 0.2168 0.2315 0.1887 -0.0581 -0.0003 0.0318  5   SER   B N   
3884 C CA  . SER   B 5   ? 0.2440 0.2635 0.2234 -0.0456 0.0202  0.0298  5   SER   B CA  
3885 C C   . SER   B 5   ? 0.2553 0.2633 0.2499 -0.0554 0.0401  0.0331  5   SER   B C   
3886 O O   . SER   B 5   ? 0.2654 0.2614 0.3142 -0.0507 0.0551  0.0279  5   SER   B O   
3887 C CB  . SER   B 5   ? 0.2598 0.2873 0.2493 -0.0371 0.0150  0.0373  5   SER   B CB  
3888 O OG  . SER   B 5   ? 0.2834 0.3217 0.2973 -0.0235 0.0206  0.0444  5   SER   B OG  
3894 N N   . PHE   B 6   ? 0.2659 0.2747 0.2187 -0.0578 0.0515  0.0370  6   PHE   B N   
3895 C CA  . PHE   B 6   ? 0.2687 0.2715 0.1932 -0.0737 0.0509  0.0258  6   PHE   B CA  
3896 C C   . PHE   B 6   ? 0.3158 0.2985 0.2264 -0.0710 0.0620  -0.0101 6   PHE   B C   
3897 O O   . PHE   B 6   ? 0.3307 0.3289 0.2468 -0.0558 0.0404  -0.0278 6   PHE   B O   
3898 C CB  . PHE   B 6   ? 0.2377 0.2515 0.1798 -0.0711 0.0260  0.0245  6   PHE   B CB  
3899 C CG  . PHE   B 6   ? 0.2065 0.2226 0.1741 -0.0699 0.0125  0.0154  6   PHE   B CG  
3900 C CD1 . PHE   B 6   ? 0.2039 0.1948 0.1726 -0.0642 -0.0035 0.0065  6   PHE   B CD1 
3901 C CD2 . PHE   B 6   ? 0.1889 0.2256 0.1734 -0.0518 0.0133  0.0316  6   PHE   B CD2 
3902 C CE1 . PHE   B 6   ? 0.2006 0.1793 0.1713 -0.0512 -0.0096 0.0023  6   PHE   B CE1 
3903 C CE2 . PHE   B 6   ? 0.1934 0.2113 0.2009 -0.0440 0.0163  0.0298  6   PHE   B CE2 
3904 C CZ  . PHE   B 6   ? 0.1933 0.1857 0.1853 -0.0466 0.0035  0.0098  6   PHE   B CZ  
3914 N N   A SER   B 7   ? 0.3305 0.2898 0.2375 -0.0793 0.0688  -0.0226 7   SER   B N   
3915 N N   B SER   B 7   ? 0.3356 0.2871 0.2232 -0.0841 0.0774  -0.0253 7   SER   B N   
3916 C CA  A SER   B 7   ? 0.3438 0.2885 0.2675 -0.0809 0.0739  -0.0303 7   SER   B CA  
3917 C CA  B SER   B 7   ? 0.3541 0.2888 0.2533 -0.0849 0.0882  -0.0331 7   SER   B CA  
3918 C C   A SER   B 7   ? 0.3416 0.2766 0.2662 -0.0827 0.0838  -0.0398 7   SER   B C   
3919 C C   B SER   B 7   ? 0.3505 0.2774 0.2520 -0.0857 0.1013  -0.0447 7   SER   B C   
3920 O O   A SER   B 7   ? 0.3456 0.2791 0.2818 -0.0822 0.0854  -0.0377 7   SER   B O   
3921 O O   B SER   B 7   ? 0.3556 0.2810 0.2767 -0.0846 0.1038  -0.0410 7   SER   B O   
3922 C CB  A SER   B 7   ? 0.3557 0.2989 0.3032 -0.0781 0.0758  -0.0308 7   SER   B CB  
3923 C CB  B SER   B 7   ? 0.3708 0.3022 0.2945 -0.0808 0.0924  -0.0340 7   SER   B CB  
3924 O OG  A SER   B 7   ? 0.3633 0.3084 0.3282 -0.0768 0.0752  -0.0336 7   SER   B OG  
3925 O OG  B SER   B 7   ? 0.3815 0.3153 0.3266 -0.0782 0.0895  -0.0382 7   SER   B OG  
3936 N N   A GLY   B 8   ? 0.3379 0.2638 0.2610 -0.0793 0.0887  -0.0502 8   GLY   B N   
3937 N N   B GLY   B 8   ? 0.3453 0.2659 0.2519 -0.0795 0.1027  -0.0572 8   GLY   B N   
3938 C CA  A GLY   B 8   ? 0.3311 0.2490 0.2589 -0.0793 0.0943  -0.0547 8   GLY   B CA  
3939 C CA  B GLY   B 8   ? 0.3357 0.2519 0.2565 -0.0787 0.1046  -0.0600 8   GLY   B CA  
3940 C C   A GLY   B 8   ? 0.3234 0.2325 0.2479 -0.0799 0.1009  -0.0517 8   GLY   B C   
3941 C C   B GLY   B 8   ? 0.3247 0.2358 0.2466 -0.0795 0.1074  -0.0516 8   GLY   B C   
3942 O O   A GLY   B 8   ? 0.3270 0.2315 0.2667 -0.0793 0.1032  -0.0505 8   GLY   B O   
3943 O O   B GLY   B 8   ? 0.3300 0.2418 0.2727 -0.0730 0.1082  -0.0446 8   GLY   B O   
3950 N N   . TYR   B 9   ? 0.3165 0.2208 0.2308 -0.0762 0.0942  -0.0548 9   TYR   B N   
3951 C CA  . TYR   B 9   ? 0.2980 0.1949 0.2023 -0.0621 0.0742  -0.0442 9   TYR   B CA  
3952 C C   . TYR   B 9   ? 0.2877 0.2005 0.1902 -0.0549 0.0417  -0.0360 9   TYR   B C   
3953 O O   . TYR   B 9   ? 0.3008 0.2211 0.2224 -0.0542 0.0270  -0.0212 9   TYR   B O   
3954 C CB  . TYR   B 9   ? 0.2971 0.1763 0.2100 -0.0501 0.0767  -0.0325 9   TYR   B CB  
3955 C CG  . TYR   B 9   ? 0.2864 0.1534 0.2287 -0.0551 0.0717  -0.0361 9   TYR   B CG  
3956 C CD1 . TYR   B 9   ? 0.2873 0.1607 0.2496 -0.0681 0.0728  -0.0391 9   TYR   B CD1 
3957 C CD2 . TYR   B 9   ? 0.2701 0.1449 0.2222 -0.0475 0.0671  -0.0344 9   TYR   B CD2 
3958 C CE1 . TYR   B 9   ? 0.2816 0.1680 0.2563 -0.0730 0.0721  -0.0511 9   TYR   B CE1 
3959 C CE2 . TYR   B 9   ? 0.2670 0.1479 0.2351 -0.0480 0.0647  -0.0425 9   TYR   B CE2 
3960 C CZ  . TYR   B 9   ? 0.2709 0.1694 0.2533 -0.0633 0.0677  -0.0567 9   TYR   B CZ  
3961 O OH  . TYR   B 9   ? 0.2652 0.1850 0.2643 -0.0742 0.0648  -0.0748 9   TYR   B OH  
3972 N N   . LEU   B 10  ? 0.2648 0.1782 0.1725 -0.0482 0.0248  -0.0436 10  LEU   B N   
3973 C CA  . LEU   B 10  ? 0.2604 0.1779 0.1721 -0.0529 -0.0093 -0.0375 10  LEU   B CA  
3974 C C   . LEU   B 10  ? 0.2386 0.1763 0.1704 -0.0538 -0.0270 -0.0353 10  LEU   B C   
3975 O O   . LEU   B 10  ? 0.2248 0.1720 0.1753 -0.0361 -0.0261 -0.0261 10  LEU   B O   
3976 C CB  . LEU   B 10  ? 0.2746 0.1779 0.1929 -0.0610 -0.0290 -0.0186 10  LEU   B CB  
3977 C CG  . LEU   B 10  ? 0.2916 0.1862 0.2299 -0.0591 -0.0442 -0.0054 10  LEU   B CG  
3978 C CD1 . LEU   B 10  ? 0.3018 0.2008 0.2611 -0.0521 -0.0400 -0.0061 10  LEU   B CD1 
3979 C CD2 . LEU   B 10  ? 0.3024 0.1906 0.2549 -0.0594 -0.0394 0.0108  10  LEU   B CD2 
3991 N N   . LYS   B 11  ? 0.2476 0.2016 0.1727 -0.0471 -0.0241 -0.0345 11  LYS   B N   
3992 C CA  . LYS   B 11  ? 0.2595 0.2281 0.1965 -0.0370 -0.0447 -0.0327 11  LYS   B CA  
3993 C C   . LYS   B 11  ? 0.2509 0.2122 0.2024 -0.0573 -0.0463 -0.0425 11  LYS   B C   
3994 O O   . LYS   B 11  ? 0.2705 0.2295 0.2376 -0.0700 -0.0360 -0.0698 11  LYS   B O   
3995 C CB  . LYS   B 11  ? 0.2884 0.2720 0.2677 -0.0140 -0.0457 -0.0170 11  LYS   B CB  
3996 C CG  . LYS   B 11  ? 0.3181 0.3018 0.3450 -0.0000 -0.0502 -0.0159 11  LYS   B CG  
3997 C CD  . LYS   B 11  ? 0.3401 0.3279 0.4124 0.0095  -0.0523 -0.0228 11  LYS   B CD  
3998 C CE  . LYS   B 11  ? 0.3548 0.3485 0.4626 0.0146  -0.0468 -0.0277 11  LYS   B CE  
3999 N NZ  . LYS   B 11  ? 0.3618 0.3615 0.4925 0.0178  -0.0410 -0.0275 11  LYS   B NZ  
4013 N N   . LEU   B 12  ? 0.2243 0.1848 0.2077 -0.0516 -0.0459 -0.0336 12  LEU   B N   
4014 C CA  . LEU   B 12  ? 0.2130 0.1703 0.2318 -0.0490 -0.0384 -0.0225 12  LEU   B CA  
4015 C C   . LEU   B 12  ? 0.2027 0.1667 0.2445 -0.0525 -0.0438 -0.0231 12  LEU   B C   
4016 O O   . LEU   B 12  ? 0.2024 0.1682 0.2616 -0.0632 -0.0474 -0.0167 12  LEU   B O   
4017 C CB  . LEU   B 12  ? 0.2125 0.1531 0.2295 -0.0445 -0.0314 -0.0217 12  LEU   B CB  
4018 C CG  . LEU   B 12  ? 0.2111 0.1502 0.2391 -0.0436 -0.0219 -0.0272 12  LEU   B CG  
4019 C CD1 . LEU   B 12  ? 0.2205 0.1491 0.2389 -0.0296 -0.0134 -0.0133 12  LEU   B CD1 
4020 C CD2 . LEU   B 12  ? 0.2160 0.1562 0.2566 -0.0412 -0.0246 -0.0337 12  LEU   B CD2 
4032 N N   . THR   B 13  ? 0.1932 0.1669 0.2354 -0.0521 -0.0448 -0.0354 13  THR   B N   
4033 C CA  . THR   B 13  ? 0.1943 0.1805 0.2239 -0.0506 -0.0525 -0.0265 13  THR   B CA  
4034 C C   . THR   B 13  ? 0.2282 0.1922 0.2367 -0.0595 -0.0688 -0.0181 13  THR   B C   
4035 O O   . THR   B 13  ? 0.2465 0.1895 0.2686 -0.0605 -0.0295 -0.0097 13  THR   B O   
4036 C CB  . THR   B 13  ? 0.1784 0.1796 0.2300 -0.0452 -0.0462 -0.0242 13  THR   B CB  
4037 O OG1 . THR   B 13  ? 0.1709 0.1702 0.2382 -0.0375 -0.0352 -0.0188 13  THR   B OG1 
4038 C CG2 . THR   B 13  ? 0.1865 0.1922 0.2308 -0.0375 -0.0373 -0.0093 13  THR   B CG2 
4046 N N   A ASP   B 14  ? 0.2351 0.2003 0.2442 -0.0615 -0.0866 -0.0069 14  ASP   B N   
4047 N N   B ASP   B 14  ? 0.2397 0.2063 0.2372 -0.0589 -0.0944 -0.0043 14  ASP   B N   
4048 C CA  A ASP   B 14  ? 0.2392 0.2094 0.2725 -0.0599 -0.0862 0.0097  14  ASP   B CA  
4049 C CA  B ASP   B 14  ? 0.2494 0.2218 0.2688 -0.0526 -0.0893 0.0178  14  ASP   B CA  
4050 C C   A ASP   B 14  ? 0.2256 0.1945 0.2459 -0.0597 -0.0723 0.0115  14  ASP   B C   
4051 C C   B ASP   B 14  ? 0.2334 0.2028 0.2454 -0.0564 -0.0731 0.0146  14  ASP   B C   
4052 O O   A ASP   B 14  ? 0.2389 0.2021 0.2474 -0.0609 -0.0699 0.0174  14  ASP   B O   
4053 O O   B ASP   B 14  ? 0.2530 0.2139 0.2505 -0.0558 -0.0737 0.0214  14  ASP   B O   
4054 C CB  A ASP   B 14  ? 0.2541 0.2329 0.3349 -0.0591 -0.0933 0.0125  14  ASP   B CB  
4055 C CB  B ASP   B 14  ? 0.2721 0.2552 0.3355 -0.0443 -0.0890 0.0253  14  ASP   B CB  
4056 C CG  A ASP   B 14  ? 0.2698 0.2492 0.3933 -0.0599 -0.0923 0.0082  14  ASP   B CG  
4057 C CG  B ASP   B 14  ? 0.2950 0.2813 0.4016 -0.0380 -0.0803 0.0208  14  ASP   B CG  
4058 O OD1 A ASP   B 14  ? 0.2755 0.2540 0.4066 -0.0695 -0.0927 0.0027  14  ASP   B OD1 
4059 O OD1 B ASP   B 14  ? 0.2999 0.2919 0.4214 -0.0387 -0.0726 0.0171  14  ASP   B OD1 
4060 O OD2 A ASP   B 14  ? 0.2750 0.2537 0.4243 -0.0581 -0.0893 0.0098  14  ASP   B OD2 
4061 O OD2 B ASP   B 14  ? 0.3070 0.2915 0.4369 -0.0400 -0.0783 0.0194  14  ASP   B OD2 
4070 N N   . ASN   B 15  ? 0.2010 0.1750 0.2185 -0.0500 -0.0730 0.0073  15  ASN   B N   
4071 C CA  . ASN   B 15  ? 0.1652 0.1503 0.2022 -0.0306 -0.0451 0.0045  15  ASN   B CA  
4072 C C   . ASN   B 15  ? 0.1542 0.1369 0.1925 -0.0216 -0.0336 -0.0075 15  ASN   B C   
4073 O O   . ASN   B 15  ? 0.1573 0.1322 0.2082 -0.0222 -0.0374 -0.0137 15  ASN   B O   
4074 C CB  . ASN   B 15  ? 0.1596 0.1512 0.2188 -0.0152 -0.0379 -0.0017 15  ASN   B CB  
4075 C CG  . ASN   B 15  ? 0.1520 0.1451 0.2288 -0.0217 -0.0225 0.0013  15  ASN   B CG  
4076 O OD1 . ASN   B 15  ? 0.1572 0.1697 0.2555 -0.0403 -0.0313 0.0146  15  ASN   B OD1 
4077 N ND2 . ASN   B 15  ? 0.1529 0.1279 0.2122 -0.0110 -0.0049 -0.0146 15  ASN   B ND2 
4085 N N   . VAL   B 16  ? 0.1629 0.1270 0.1980 -0.0242 -0.0429 -0.0063 16  VAL   B N   
4086 C CA  . VAL   B 16  ? 0.1569 0.1305 0.1822 -0.0258 -0.0333 -0.0160 16  VAL   B CA  
4087 C C   . VAL   B 16  ? 0.1536 0.1393 0.1795 -0.0315 -0.0358 -0.0167 16  VAL   B C   
4088 O O   . VAL   B 16  ? 0.1635 0.1595 0.1996 -0.0322 -0.0232 -0.0307 16  VAL   B O   
4089 C CB  . VAL   B 16  ? 0.1669 0.1361 0.1970 -0.0172 -0.0222 -0.0200 16  VAL   B CB  
4090 C CG1 . VAL   B 16  ? 0.1730 0.1344 0.1909 -0.0031 -0.0282 -0.0104 16  VAL   B CG1 
4091 C CG2 . VAL   B 16  ? 0.1666 0.1429 0.2096 -0.0103 -0.0234 -0.0158 16  VAL   B CG2 
4101 N N   . TYR   B 17  ? 0.1581 0.1424 0.1731 -0.0280 -0.0274 -0.0198 17  TYR   B N   
4102 C CA  . TYR   B 17  ? 0.1684 0.1513 0.1692 -0.0337 -0.0236 -0.0006 17  TYR   B CA  
4103 C C   . TYR   B 17  ? 0.1604 0.1339 0.1765 -0.0333 -0.0155 -0.0049 17  TYR   B C   
4104 O O   . TYR   B 17  ? 0.1563 0.1399 0.1863 -0.0236 -0.0236 -0.0278 17  TYR   B O   
4105 C CB  . TYR   B 17  ? 0.1980 0.1879 0.1878 -0.0191 -0.0284 0.0294  17  TYR   B CB  
4106 C CG  . TYR   B 17  ? 0.2291 0.2298 0.2311 -0.0138 -0.0321 0.0243  17  TYR   B CG  
4107 C CD1 . TYR   B 17  ? 0.2454 0.2427 0.2432 -0.0065 -0.0358 0.0339  17  TYR   B CD1 
4108 C CD2 . TYR   B 17  ? 0.2514 0.2608 0.2515 -0.0054 -0.0343 0.0140  17  TYR   B CD2 
4109 C CE1 . TYR   B 17  ? 0.2638 0.2615 0.2530 0.0014  -0.0437 0.0254  17  TYR   B CE1 
4110 C CE2 . TYR   B 17  ? 0.2681 0.2734 0.2675 0.0084  -0.0422 0.0190  17  TYR   B CE2 
4111 C CZ  . TYR   B 17  ? 0.2780 0.2719 0.2694 0.0099  -0.0526 0.0249  17  TYR   B CZ  
4112 O OH  . TYR   B 17  ? 0.2937 0.2880 0.2948 0.0167  -0.0674 0.0211  17  TYR   B OH  
4122 N N   . ILE   B 18  ? 0.1706 0.1325 0.1760 -0.0281 -0.0109 -0.0133 18  ILE   B N   
4123 C CA  . ILE   B 18  ? 0.1781 0.1248 0.1706 -0.0270 -0.0137 -0.0160 18  ILE   B CA  
4124 C C   . ILE   B 18  ? 0.1888 0.1301 0.1592 -0.0370 -0.0093 -0.0276 18  ILE   B C   
4125 O O   . ILE   B 18  ? 0.2101 0.1473 0.1797 -0.0361 0.0013  -0.0360 18  ILE   B O   
4126 C CB  . ILE   B 18  ? 0.1800 0.1303 0.1806 -0.0324 -0.0163 -0.0190 18  ILE   B CB  
4127 C CG1 . ILE   B 18  ? 0.1810 0.1364 0.1857 -0.0340 -0.0082 -0.0094 18  ILE   B CG1 
4128 C CG2 . ILE   B 18  ? 0.1804 0.1405 0.1880 -0.0356 -0.0150 -0.0157 18  ILE   B CG2 
4129 C CD1 . ILE   B 18  ? 0.1847 0.1650 0.2131 -0.0366 -0.0173 0.0098  18  ILE   B CD1 
4141 N N   . LYS   B 19  ? 0.1890 0.1375 0.1673 -0.0253 0.0137  -0.0366 19  LYS   B N   
4142 C CA  . LYS   B 19  ? 0.1954 0.1400 0.1821 -0.0260 0.0235  -0.0385 19  LYS   B CA  
4143 C C   . LYS   B 19  ? 0.1766 0.1402 0.2017 -0.0215 0.0269  -0.0353 19  LYS   B C   
4144 O O   . LYS   B 19  ? 0.1670 0.1427 0.1965 -0.0101 0.0178  -0.0317 19  LYS   B O   
4145 C CB  . LYS   B 19  ? 0.2132 0.1580 0.2051 -0.0275 0.0323  -0.0219 19  LYS   B CB  
4146 C CG  . LYS   B 19  ? 0.2356 0.1827 0.2109 -0.0296 0.0328  -0.0186 19  LYS   B CG  
4147 C CD  . LYS   B 19  ? 0.2572 0.2079 0.2222 -0.0384 0.0383  -0.0186 19  LYS   B CD  
4148 C CE  . LYS   B 19  ? 0.2789 0.2353 0.2449 -0.0386 0.0415  -0.0161 19  LYS   B CE  
4149 N NZ  . LYS   B 19  ? 0.2930 0.2509 0.2620 -0.0433 0.0438  -0.0100 19  LYS   B NZ  
4163 N N   . ASN   B 20  ? 0.1738 0.1553 0.2327 -0.0157 0.0327  -0.0468 20  ASN   B N   
4164 C CA  . ASN   B 20  ? 0.1724 0.1656 0.2517 -0.0092 0.0318  -0.0604 20  ASN   B CA  
4165 C C   . ASN   B 20  ? 0.1712 0.1823 0.2424 -0.0145 0.0442  -0.0690 20  ASN   B C   
4166 O O   . ASN   B 20  ? 0.1862 0.2201 0.2703 -0.0293 0.0481  -0.0676 20  ASN   B O   
4167 C CB  . ASN   B 20  ? 0.1949 0.1681 0.2748 0.0114  0.0173  -0.0608 20  ASN   B CB  
4168 C CG  . ASN   B 20  ? 0.2202 0.1739 0.2973 0.0391  0.0159  -0.0707 20  ASN   B CG  
4169 O OD1 . ASN   B 20  ? 0.2519 0.2022 0.3317 0.0537  0.0203  -0.0692 20  ASN   B OD1 
4170 N ND2 . ASN   B 20  ? 0.2114 0.1778 0.2919 0.0373  0.0042  -0.0663 20  ASN   B ND2 
4177 N N   . ALA   B 21  ? 0.1748 0.1644 0.2350 -0.0225 0.0425  -0.0549 21  ALA   B N   
4178 C CA  . ALA   B 21  ? 0.1849 0.1730 0.2597 -0.0272 0.0326  -0.0438 21  ALA   B CA  
4179 C C   . ALA   B 21  ? 0.1844 0.1503 0.2489 -0.0213 0.0341  -0.0303 21  ALA   B C   
4180 O O   . ALA   B 21  ? 0.1864 0.1455 0.2629 -0.0305 0.0279  -0.0274 21  ALA   B O   
4181 C CB  . ALA   B 21  ? 0.2035 0.2004 0.2827 -0.0385 0.0273  -0.0200 21  ALA   B CB  
4187 N N   . ASP   B 22  ? 0.1766 0.1483 0.2443 -0.0180 0.0305  -0.0241 22  ASP   B N   
4188 C CA  . ASP   B 22  ? 0.1732 0.1392 0.2309 -0.0075 0.0231  -0.0193 22  ASP   B CA  
4189 C C   . ASP   B 22  ? 0.1661 0.1360 0.2018 -0.0116 0.0153  -0.0107 22  ASP   B C   
4190 O O   . ASP   B 22  ? 0.1661 0.1412 0.2045 -0.0072 0.0105  -0.0045 22  ASP   B O   
4191 C CB  . ASP   B 22  ? 0.1816 0.1497 0.2711 -0.0071 0.0225  -0.0081 22  ASP   B CB  
4192 C CG  . ASP   B 22  ? 0.1834 0.1619 0.3114 -0.0036 0.0021  -0.0007 22  ASP   B CG  
4193 O OD1 . ASP   B 22  ? 0.1982 0.1529 0.3064 -0.0010 -0.0184 -0.0016 22  ASP   B OD1 
4194 O OD2 . ASP   B 22  ? 0.1894 0.1875 0.3619 0.0073  -0.0192 -0.0101 22  ASP   B OD2 
4199 N N   . ILE   B 23  ? 0.1628 0.1290 0.1793 -0.0101 0.0050  0.0109  23  ILE   B N   
4200 C CA  . ILE   B 23  ? 0.1536 0.1322 0.1651 -0.0111 0.0027  0.0004  23  ILE   B CA  
4201 C C   . ILE   B 23  ? 0.1479 0.1307 0.1604 -0.0043 -0.0122 -0.0011 23  ILE   B C   
4202 O O   . ILE   B 23  ? 0.1425 0.1323 0.1561 -0.0085 -0.0029 0.0077  23  ILE   B O   
4203 C CB  . ILE   B 23  ? 0.1506 0.1410 0.1851 -0.0165 -0.0005 0.0094  23  ILE   B CB  
4204 C CG1 . ILE   B 23  ? 0.1548 0.1473 0.1986 -0.0134 0.0017  0.0232  23  ILE   B CG1 
4205 C CG2 . ILE   B 23  ? 0.1593 0.1634 0.1985 -0.0148 0.0017  0.0048  23  ILE   B CG2 
4206 C CD1 . ILE   B 23  ? 0.1646 0.1609 0.2069 -0.0127 0.0130  0.0198  23  ILE   B CD1 
4218 N N   . VAL   B 24  ? 0.1515 0.1270 0.1671 -0.0065 -0.0088 0.0047  24  VAL   B N   
4219 C CA  . VAL   B 24  ? 0.1452 0.1390 0.1976 -0.0100 -0.0131 -0.0019 24  VAL   B CA  
4220 C C   . VAL   B 24  ? 0.1451 0.1414 0.2059 -0.0156 -0.0042 0.0005  24  VAL   B C   
4221 O O   . VAL   B 24  ? 0.1474 0.1413 0.2142 -0.0168 -0.0005 0.0168  24  VAL   B O   
4222 C CB  . VAL   B 24  ? 0.1542 0.1546 0.2074 0.0000  -0.0237 -0.0109 24  VAL   B CB  
4223 C CG1 . VAL   B 24  ? 0.1544 0.1643 0.2401 -0.0090 -0.0279 -0.0094 24  VAL   B CG1 
4224 C CG2 . VAL   B 24  ? 0.1674 0.1842 0.2173 0.0114  -0.0237 -0.0191 24  VAL   B CG2 
4234 N N   . GLU   B 25  ? 0.1704 0.1507 0.2185 -0.0132 0.0059  0.0063  25  GLU   B N   
4235 C CA  . GLU   B 25  ? 0.1758 0.1787 0.2346 -0.0021 0.0165  -0.0038 25  GLU   B CA  
4236 C C   . GLU   B 25  ? 0.1692 0.1730 0.2085 -0.0095 0.0166  -0.0023 25  GLU   B C   
4237 O O   . GLU   B 25  ? 0.1741 0.1869 0.2126 -0.0085 0.0216  0.0077  25  GLU   B O   
4238 C CB  . GLU   B 25  ? 0.2028 0.2212 0.2783 0.0148  0.0252  0.0012  25  GLU   B CB  
4239 C CG  . GLU   B 25  ? 0.2445 0.2652 0.3609 0.0197  0.0190  -0.0034 25  GLU   B CG  
4240 C CD  . GLU   B 25  ? 0.2875 0.3100 0.4315 0.0106  0.0127  -0.0036 25  GLU   B CD  
4241 O OE1 . GLU   B 25  ? 0.2954 0.3272 0.4651 0.0105  0.0167  0.0009  25  GLU   B OE1 
4242 O OE2 . GLU   B 25  ? 0.2889 0.3299 0.4659 0.0082  0.0036  -0.0094 25  GLU   B OE2 
4249 N N   . GLU   B 26  ? 0.1665 0.1581 0.1821 -0.0250 0.0108  0.0066  26  GLU   B N   
4250 C CA  . GLU   B 26  ? 0.1667 0.1705 0.1820 -0.0337 0.0002  0.0126  26  GLU   B CA  
4251 C C   . GLU   B 26  ? 0.1578 0.1666 0.1776 -0.0223 0.0052  0.0235  26  GLU   B C   
4252 O O   . GLU   B 26  ? 0.1750 0.1912 0.1749 -0.0229 -0.0032 0.0328  26  GLU   B O   
4253 C CB  . GLU   B 26  ? 0.1930 0.1917 0.1984 -0.0424 -0.0049 0.0250  26  GLU   B CB  
4254 C CG  . GLU   B 26  ? 0.2359 0.2280 0.2470 -0.0494 0.0084  0.0053  26  GLU   B CG  
4255 C CD  . GLU   B 26  ? 0.2642 0.2548 0.2624 -0.0676 0.0228  -0.0267 26  GLU   B CD  
4256 O OE1 . GLU   B 26  ? 0.2850 0.2421 0.2550 -0.0775 0.0654  -0.0263 26  GLU   B OE1 
4257 O OE2 . GLU   B 26  ? 0.2627 0.2917 0.2899 -0.0649 0.0255  -0.0158 26  GLU   B OE2 
4264 N N   . ALA   B 27  ? 0.1439 0.1520 0.1821 -0.0229 0.0083  0.0198  27  ALA   B N   
4265 C CA  . ALA   B 27  ? 0.1403 0.1519 0.1955 -0.0143 0.0063  0.0267  27  ALA   B CA  
4266 C C   . ALA   B 27  ? 0.1492 0.1602 0.2132 -0.0104 0.0164  0.0355  27  ALA   B C   
4267 O O   . ALA   B 27  ? 0.1579 0.1679 0.2217 0.0053  0.0205  0.0470  27  ALA   B O   
4268 C CB  . ALA   B 27  ? 0.1559 0.1347 0.1975 -0.0160 0.0062  0.0168  27  ALA   B CB  
4274 N N   . LYS   B 28  ? 0.1452 0.1748 0.2423 -0.0129 0.0245  0.0557  28  LYS   B N   
4275 C CA  . LYS   B 28  ? 0.1622 0.2136 0.2734 -0.0060 0.0518  0.0681  28  LYS   B CA  
4276 C C   . LYS   B 28  ? 0.1814 0.2247 0.2639 -0.0016 0.0596  0.0644  28  LYS   B C   
4277 O O   . LYS   B 28  ? 0.2077 0.2298 0.2727 -0.0056 0.0652  0.0661  28  LYS   B O   
4278 C CB  . LYS   B 28  ? 0.1830 0.2483 0.3195 -0.0031 0.0713  0.0855  28  LYS   B CB  
4279 C CG  . LYS   B 28  ? 0.2150 0.2931 0.3642 0.0012  0.0805  0.0996  28  LYS   B CG  
4280 C CD  . LYS   B 28  ? 0.2470 0.3335 0.4191 0.0129  0.0926  0.0954  28  LYS   B CD  
4281 C CE  . LYS   B 28  ? 0.2820 0.3626 0.4578 0.0243  0.0938  0.0947  28  LYS   B CE  
4282 N NZ  . LYS   B 28  ? 0.3392 0.4062 0.4831 0.0333  0.0955  0.1026  28  LYS   B NZ  
4296 N N   . LYS   B 29  ? 0.1934 0.2449 0.2579 0.0214  0.0667  0.0535  29  LYS   B N   
4297 C CA  . LYS   B 29  ? 0.2373 0.2803 0.2926 0.0219  0.0576  0.0586  29  LYS   B CA  
4298 C C   . LYS   B 29  ? 0.2306 0.2862 0.2565 0.0267  0.0427  0.0755  29  LYS   B C   
4299 O O   . LYS   B 29  ? 0.2426 0.3047 0.2668 0.0277  0.0411  0.0784  29  LYS   B O   
4300 C CB  . LYS   B 29  ? 0.2921 0.3137 0.3746 0.0194  0.0491  0.0479  29  LYS   B CB  
4301 C CG  . LYS   B 29  ? 0.3271 0.3402 0.4473 0.0177  0.0523  0.0440  29  LYS   B CG  
4302 C CD  . LYS   B 29  ? 0.3522 0.3567 0.5100 0.0157  0.0595  0.0366  29  LYS   B CD  
4303 C CE  . LYS   B 29  ? 0.3656 0.3638 0.5596 0.0143  0.0670  0.0320  29  LYS   B CE  
4304 N NZ  . LYS   B 29  ? 0.3760 0.3688 0.5807 0.0148  0.0689  0.0304  29  LYS   B NZ  
4318 N N   . VAL   B 30  ? 0.2048 0.2720 0.2415 0.0233  0.0420  0.0783  30  VAL   B N   
4319 C CA  . VAL   B 30  ? 0.1938 0.2639 0.2734 0.0077  0.0157  0.0831  30  VAL   B CA  
4320 C C   . VAL   B 30  ? 0.1739 0.2602 0.2742 0.0025  0.0306  0.1078  30  VAL   B C   
4321 O O   . VAL   B 30  ? 0.1904 0.2787 0.2707 0.0115  0.0274  0.1231  30  VAL   B O   
4322 C CB  . VAL   B 30  ? 0.1983 0.2555 0.2912 -0.0027 -0.0161 0.0685  30  VAL   B CB  
4323 C CG1 . VAL   B 30  ? 0.2020 0.2635 0.2876 -0.0047 -0.0223 0.0605  30  VAL   B CG1 
4324 C CG2 . VAL   B 30  ? 0.2056 0.2538 0.3120 -0.0116 -0.0212 0.0473  30  VAL   B CG2 
4334 N N   . LYS   B 31  ? 0.1655 0.2269 0.3097 -0.0170 0.0240  0.1147  31  LYS   B N   
4335 C CA  . LYS   B 31  ? 0.1582 0.2193 0.3410 -0.0361 0.0164  0.1121  31  LYS   B CA  
4336 C C   . LYS   B 31  ? 0.1518 0.1814 0.3000 -0.0329 -0.0063 0.0923  31  LYS   B C   
4337 O O   . LYS   B 31  ? 0.1575 0.1978 0.3146 -0.0227 -0.0034 0.1098  31  LYS   B O   
4338 C CB  . LYS   B 31  ? 0.1824 0.2700 0.3977 -0.0361 0.0421  0.1243  31  LYS   B CB  
4339 C CG  . LYS   B 31  ? 0.2230 0.3137 0.4381 -0.0327 0.0535  0.1205  31  LYS   B CG  
4340 C CD  . LYS   B 31  ? 0.2502 0.3431 0.4708 -0.0237 0.0498  0.1092  31  LYS   B CD  
4341 C CE  . LYS   B 31  ? 0.2629 0.3662 0.4987 -0.0172 0.0430  0.0975  31  LYS   B CE  
4342 N NZ  . LYS   B 31  ? 0.3044 0.3913 0.5144 -0.0077 0.0297  0.0843  31  LYS   B NZ  
4356 N N   . PRO   B 32  ? 0.1570 0.1462 0.2293 -0.0292 -0.0323 0.0517  32  PRO   B N   
4357 C CA  . PRO   B 32  ? 0.1642 0.1427 0.1813 -0.0302 -0.0318 0.0345  32  PRO   B CA  
4358 C C   . PRO   B 32  ? 0.1782 0.1312 0.1836 -0.0316 -0.0507 0.0323  32  PRO   B C   
4359 O O   . PRO   B 32  ? 0.1906 0.1307 0.2163 -0.0309 -0.0749 0.0281  32  PRO   B O   
4360 C CB  . PRO   B 32  ? 0.1794 0.1378 0.1661 -0.0329 -0.0317 0.0165  32  PRO   B CB  
4361 C CG  . PRO   B 32  ? 0.1982 0.1333 0.1791 -0.0259 -0.0545 0.0160  32  PRO   B CG  
4362 C CD  . PRO   B 32  ? 0.1849 0.1371 0.2041 -0.0206 -0.0654 0.0282  32  PRO   B CD  
4370 N N   . THR   B 33  ? 0.1785 0.1256 0.1602 -0.0314 -0.0409 0.0245  33  THR   B N   
4371 C CA  . THR   B 33  ? 0.1805 0.1344 0.1593 -0.0304 -0.0392 0.0245  33  THR   B CA  
4372 C C   . THR   B 33  ? 0.1812 0.1242 0.1512 -0.0310 -0.0411 0.0134  33  THR   B C   
4373 O O   . THR   B 33  ? 0.2074 0.1260 0.1653 -0.0362 -0.0558 0.0148  33  THR   B O   
4374 C CB  . THR   B 33  ? 0.1870 0.1434 0.1712 -0.0184 -0.0408 0.0327  33  THR   B CB  
4375 O OG1 . THR   B 33  ? 0.1782 0.1484 0.1755 -0.0161 -0.0471 0.0280  33  THR   B OG1 
4376 C CG2 . THR   B 33  ? 0.2056 0.1446 0.1779 -0.0039 -0.0384 0.0231  33  THR   B CG2 
4384 N N   . VAL   B 34  ? 0.1695 0.1191 0.1449 -0.0285 -0.0349 0.0069  34  VAL   B N   
4385 C CA  . VAL   B 34  ? 0.1535 0.1210 0.1374 -0.0179 -0.0293 0.0067  34  VAL   B CA  
4386 C C   . VAL   B 34  ? 0.1410 0.1130 0.1368 -0.0274 -0.0157 0.0041  34  VAL   B C   
4387 O O   . VAL   B 34  ? 0.1606 0.1172 0.1290 -0.0258 -0.0272 0.0032  34  VAL   B O   
4388 C CB  . VAL   B 34  ? 0.1622 0.1274 0.1607 -0.0108 -0.0269 0.0011  34  VAL   B CB  
4389 C CG1 . VAL   B 34  ? 0.1601 0.1394 0.1671 -0.0079 -0.0145 0.0004  34  VAL   B CG1 
4390 C CG2 . VAL   B 34  ? 0.1724 0.1323 0.1847 -0.0067 -0.0264 0.0010  34  VAL   B CG2 
4400 N N   . VAL   B 35  ? 0.1298 0.1124 0.1311 -0.0194 -0.0080 0.0033  35  VAL   B N   
4401 C CA  . VAL   B 35  ? 0.1248 0.1094 0.1243 -0.0166 -0.0052 0.0038  35  VAL   B CA  
4402 C C   . VAL   B 35  ? 0.1192 0.1081 0.1256 -0.0124 -0.0083 0.0040  35  VAL   B C   
4403 O O   . VAL   B 35  ? 0.1283 0.1154 0.1272 -0.0201 -0.0026 -0.0072 35  VAL   B O   
4404 C CB  . VAL   B 35  ? 0.1307 0.1259 0.1260 -0.0172 0.0018  0.0051  35  VAL   B CB  
4405 C CG1 . VAL   B 35  ? 0.1266 0.1402 0.1404 -0.0219 0.0007  0.0045  35  VAL   B CG1 
4406 C CG2 . VAL   B 35  ? 0.1325 0.1258 0.1474 -0.0084 0.0005  -0.0043 35  VAL   B CG2 
4416 N N   . VAL   B 36  ? 0.1227 0.1093 0.1131 -0.0175 -0.0079 0.0044  36  VAL   B N   
4417 C CA  . VAL   B 36  ? 0.1213 0.1008 0.1130 -0.0126 -0.0066 0.0016  36  VAL   B CA  
4418 C C   . VAL   B 36  ? 0.1161 0.1019 0.1193 -0.0130 -0.0017 0.0074  36  VAL   B C   
4419 O O   . VAL   B 36  ? 0.1231 0.1172 0.1275 -0.0067 -0.0011 -0.0024 36  VAL   B O   
4420 C CB  . VAL   B 36  ? 0.1164 0.1076 0.1270 -0.0132 -0.0032 0.0039  36  VAL   B CB  
4421 C CG1 . VAL   B 36  ? 0.1184 0.1183 0.1347 -0.0186 -0.0041 0.0004  36  VAL   B CG1 
4422 C CG2 . VAL   B 36  ? 0.1226 0.1142 0.1400 -0.0139 -0.0035 0.0043  36  VAL   B CG2 
4432 N N   . ASN   B 37  ? 0.1158 0.1150 0.1215 -0.0048 -0.0015 0.0011  37  ASN   B N   
4433 C CA  . ASN   B 37  ? 0.1141 0.1125 0.1279 0.0049  -0.0048 0.0106  37  ASN   B CA  
4434 C C   . ASN   B 37  ? 0.1164 0.1118 0.1253 0.0046  -0.0077 -0.0027 37  ASN   B C   
4435 O O   . ASN   B 37  ? 0.1269 0.1239 0.1168 0.0038  -0.0013 0.0014  37  ASN   B O   
4436 C CB  . ASN   B 37  ? 0.1202 0.1143 0.1266 -0.0028 -0.0112 0.0020  37  ASN   B CB  
4437 C CG  . ASN   B 37  ? 0.1240 0.1161 0.1367 -0.0011 -0.0073 -0.0020 37  ASN   B CG  
4438 O OD1 . ASN   B 37  ? 0.1319 0.1246 0.1365 0.0081  -0.0153 -0.0005 37  ASN   B OD1 
4439 N ND2 . ASN   B 37  ? 0.1276 0.1126 0.1372 0.0019  -0.0151 0.0053  37  ASN   B ND2 
4446 N N   . ALA   B 38  ? 0.1217 0.1143 0.1242 0.0054  0.0040  0.0055  38  ALA   B N   
4447 C CA  . ALA   B 38  ? 0.1307 0.1186 0.1297 -0.0004 0.0012  0.0033  38  ALA   B CA  
4448 C C   . ALA   B 38  ? 0.1289 0.1132 0.1362 0.0024  0.0056  0.0071  38  ALA   B C   
4449 O O   . ALA   B 38  ? 0.1434 0.1260 0.1382 0.0079  -0.0026 0.0088  38  ALA   B O   
4450 C CB  . ALA   B 38  ? 0.1541 0.1205 0.1398 -0.0076 0.0072  0.0031  38  ALA   B CB  
4456 N N   . ALA   B 39  ? 0.1271 0.1191 0.1231 0.0057  -0.0037 0.0057  39  ALA   B N   
4457 C CA  . ALA   B 39  ? 0.1347 0.1190 0.1265 -0.0022 -0.0061 0.0032  39  ALA   B CA  
4458 C C   . ALA   B 39  ? 0.1394 0.1292 0.1174 0.0056  0.0015  -0.0009 39  ALA   B C   
4459 O O   . ALA   B 39  ? 0.1420 0.1337 0.1363 -0.0005 0.0016  0.0047  39  ALA   B O   
4460 C CB  . ALA   B 39  ? 0.1414 0.1281 0.1483 -0.0065 -0.0033 -0.0033 39  ALA   B CB  
4466 N N   . ASN   B 40  ? 0.1462 0.1521 0.1117 -0.0057 0.0028  -0.0137 40  ASN   B N   
4467 C CA  . ASN   B 40  ? 0.1517 0.1596 0.1370 -0.0010 -0.0018 -0.0108 40  ASN   B CA  
4468 C C   . ASN   B 40  ? 0.1515 0.1598 0.1283 -0.0018 -0.0052 -0.0090 40  ASN   B C   
4469 O O   . ASN   B 40  ? 0.1511 0.1553 0.1211 0.0052  -0.0075 -0.0028 40  ASN   B O   
4470 C CB  . ASN   B 40  ? 0.1608 0.1562 0.1510 0.0025  -0.0085 0.0038  40  ASN   B CB  
4471 C CG  . ASN   B 40  ? 0.1630 0.1592 0.1841 0.0008  -0.0204 0.0095  40  ASN   B CG  
4472 O OD1 . ASN   B 40  ? 0.1609 0.1593 0.2619 -0.0038 -0.0369 0.0176  40  ASN   B OD1 
4473 N ND2 . ASN   B 40  ? 0.1681 0.1652 0.1932 0.0011  -0.0110 0.0166  40  ASN   B ND2 
4480 N N   . VAL   B 41  ? 0.1589 0.1598 0.1263 0.0026  -0.0020 -0.0028 41  VAL   B N   
4481 C CA  . VAL   B 41  ? 0.1668 0.1733 0.1262 0.0067  -0.0029 -0.0159 41  VAL   B CA  
4482 C C   . VAL   B 41  ? 0.1693 0.1716 0.1234 0.0139  -0.0142 -0.0151 41  VAL   B C   
4483 O O   . VAL   B 41  ? 0.1711 0.1657 0.1450 0.0157  -0.0184 -0.0201 41  VAL   B O   
4484 C CB  . VAL   B 41  ? 0.1830 0.1937 0.1479 -0.0022 0.0113  -0.0266 41  VAL   B CB  
4485 C CG1 . VAL   B 41  ? 0.1818 0.1971 0.1566 -0.0054 0.0232  -0.0198 41  VAL   B CG1 
4486 C CG2 . VAL   B 41  ? 0.2000 0.2101 0.1606 -0.0117 0.0131  -0.0285 41  VAL   B CG2 
4496 N N   . TYR   B 42  ? 0.1707 0.1713 0.1291 0.0130  -0.0213 -0.0045 42  TYR   B N   
4497 C CA  . TYR   B 42  ? 0.1745 0.1795 0.1481 0.0115  -0.0294 -0.0125 42  TYR   B CA  
4498 C C   . TYR   B 42  ? 0.1603 0.1622 0.1482 0.0153  -0.0255 -0.0106 42  TYR   B C   
4499 O O   . TYR   B 42  ? 0.1674 0.1641 0.1757 0.0111  -0.0301 -0.0234 42  TYR   B O   
4500 C CB  . TYR   B 42  ? 0.1982 0.2083 0.1652 0.0071  -0.0363 -0.0046 42  TYR   B CB  
4501 C CG  . TYR   B 42  ? 0.2111 0.2332 0.1640 -0.0017 -0.0310 0.0070  42  TYR   B CG  
4502 C CD1 . TYR   B 42  ? 0.2105 0.2366 0.1437 -0.0058 -0.0241 0.0052  42  TYR   B CD1 
4503 C CD2 . TYR   B 42  ? 0.2337 0.2492 0.1973 0.0024  -0.0080 0.0107  42  TYR   B CD2 
4504 C CE1 . TYR   B 42  ? 0.2262 0.2509 0.1608 -0.0035 -0.0191 0.0063  42  TYR   B CE1 
4505 C CE2 . TYR   B 42  ? 0.2418 0.2576 0.1887 0.0052  0.0110  0.0210  42  TYR   B CE2 
4506 C CZ  . TYR   B 42  ? 0.2499 0.2675 0.1854 0.0138  0.0107  0.0152  42  TYR   B CZ  
4507 O OH  . TYR   B 42  ? 0.2812 0.2968 0.2271 0.0289  0.0255  0.0280  42  TYR   B OH  
4517 N N   . LEU   B 43  ? 0.1481 0.1442 0.1389 0.0075  -0.0164 -0.0092 43  LEU   B N   
4518 C CA  . LEU   B 43  ? 0.1505 0.1400 0.1421 0.0045  -0.0160 -0.0025 43  LEU   B CA  
4519 C C   . LEU   B 43  ? 0.1563 0.1418 0.1292 0.0007  -0.0223 -0.0018 43  LEU   B C   
4520 O O   . LEU   B 43  ? 0.1511 0.1455 0.1607 0.0038  -0.0253 0.0019  43  LEU   B O   
4521 C CB  . LEU   B 43  ? 0.1499 0.1365 0.1563 0.0018  -0.0228 -0.0121 43  LEU   B CB  
4522 C CG  . LEU   B 43  ? 0.1563 0.1338 0.1566 0.0000  -0.0286 -0.0076 43  LEU   B CG  
4523 C CD1 . LEU   B 43  ? 0.1634 0.1339 0.1837 0.0020  -0.0390 -0.0042 43  LEU   B CD1 
4524 C CD2 . LEU   B 43  ? 0.1543 0.1367 0.1598 -0.0032 -0.0238 -0.0086 43  LEU   B CD2 
4536 N N   . LYS   B 44  ? 0.1541 0.1420 0.1301 0.0046  -0.0134 -0.0032 44  LYS   B N   
4537 C CA  . LYS   B 44  ? 0.1664 0.1523 0.1323 0.0069  -0.0207 0.0082  44  LYS   B CA  
4538 C C   . LYS   B 44  ? 0.1545 0.1479 0.1358 0.0067  -0.0176 0.0073  44  LYS   B C   
4539 O O   . LYS   B 44  ? 0.1696 0.1489 0.1589 -0.0003 -0.0101 0.0017  44  LYS   B O   
4540 C CB  . LYS   B 44  ? 0.1972 0.1710 0.1608 0.0150  -0.0349 0.0027  44  LYS   B CB  
4541 C CG  . LYS   B 44  ? 0.2379 0.1977 0.1997 0.0151  -0.0552 0.0073  44  LYS   B CG  
4542 C CD  . LYS   B 44  ? 0.2735 0.2226 0.2461 -0.0009 -0.0624 0.0047  44  LYS   B CD  
4543 C CE  . LYS   B 44  ? 0.3026 0.2502 0.2847 -0.0071 -0.0626 0.0065  44  LYS   B CE  
4544 N NZ  . LYS   B 44  ? 0.3104 0.2597 0.3059 -0.0024 -0.0690 0.0162  44  LYS   B NZ  
4558 N N   . HIS   B 45  ? 0.1496 0.1468 0.1389 -0.0003 -0.0221 0.0110  45  HIS   B N   
4559 C CA  . HIS   B 45  ? 0.1532 0.1400 0.1421 0.0092  -0.0160 -0.0046 45  HIS   B CA  
4560 C C   . HIS   B 45  ? 0.1779 0.1581 0.1746 0.0189  -0.0236 -0.0090 45  HIS   B C   
4561 O O   . HIS   B 45  ? 0.1846 0.1907 0.2175 0.0437  0.0020  -0.0001 45  HIS   B O   
4562 C CB  . HIS   B 45  ? 0.1474 0.1431 0.1416 0.0024  -0.0095 -0.0042 45  HIS   B CB  
4563 C CG  . HIS   B 45  ? 0.1473 0.1411 0.1428 -0.0038 -0.0092 0.0008  45  HIS   B CG  
4564 N ND1 . HIS   B 45  ? 0.1434 0.1372 0.1471 -0.0016 -0.0113 -0.0086 45  HIS   B ND1 
4565 C CD2 . HIS   B 45  ? 0.1595 0.1475 0.1590 -0.0142 -0.0166 -0.0000 45  HIS   B CD2 
4566 C CE1 . HIS   B 45  ? 0.1548 0.1303 0.1445 -0.0041 -0.0255 -0.0077 45  HIS   B CE1 
4567 N NE2 . HIS   B 45  ? 0.1604 0.1382 0.1462 -0.0029 -0.0244 -0.0041 45  HIS   B NE2 
4575 N N   A GLY   B 46  ? 0.1894 0.1589 0.2060 0.0162  -0.0361 -0.0029 46  GLY   B N   
4576 N N   B GLY   B 46  ? 0.1940 0.1592 0.2013 0.0154  -0.0423 0.0054  46  GLY   B N   
4577 C CA  A GLY   B 46  ? 0.1934 0.1660 0.2407 0.0167  -0.0434 -0.0049 46  GLY   B CA  
4578 C CA  B GLY   B 46  ? 0.2011 0.1702 0.2341 0.0145  -0.0535 0.0064  46  GLY   B CA  
4579 C C   A GLY   B 46  ? 0.1883 0.1784 0.2765 0.0240  -0.0348 -0.0082 46  GLY   B C   
4580 C C   B GLY   B 46  ? 0.1961 0.1891 0.2698 0.0223  -0.0403 0.0068  46  GLY   B C   
4581 O O   A GLY   B 46  ? 0.1926 0.1840 0.3336 0.0293  -0.0232 -0.0283 46  GLY   B O   
4582 O O   B GLY   B 46  ? 0.2080 0.2103 0.3194 0.0220  -0.0236 0.0048  46  GLY   B O   
4589 N N   . GLY   B 47  ? 0.1881 0.1906 0.2584 0.0131  -0.0170 -0.0074 47  GLY   B N   
4590 C CA  . GLY   B 47  ? 0.1789 0.1698 0.2150 0.0031  -0.0142 -0.0016 47  GLY   B CA  
4591 C C   . GLY   B 47  ? 0.1575 0.1414 0.1751 0.0046  0.0010  0.0088  47  GLY   B C   
4592 O O   . GLY   B 47  ? 0.1727 0.1287 0.1818 0.0014  -0.0047 0.0102  47  GLY   B O   
4597 N N   . GLY   B 48  ? 0.1413 0.1323 0.1818 0.0040  -0.0069 0.0148  48  GLY   B N   
4598 C CA  . GLY   B 48  ? 0.1432 0.1290 0.1763 0.0004  -0.0015 0.0079  48  GLY   B CA  
4599 C C   . GLY   B 48  ? 0.1407 0.1283 0.1560 -0.0003 0.0027  0.0097  48  GLY   B C   
4600 O O   . GLY   B 48  ? 0.1369 0.1350 0.1794 0.0047  -0.0040 0.0067  48  GLY   B O   
4604 N N   . VAL   B 49  ? 0.1400 0.1314 0.1503 0.0105  -0.0011 0.0085  49  VAL   B N   
4605 C CA  . VAL   B 49  ? 0.1440 0.1428 0.1441 0.0124  -0.0146 -0.0037 49  VAL   B CA  
4606 C C   . VAL   B 49  ? 0.1293 0.1353 0.1270 0.0120  -0.0091 0.0034  49  VAL   B C   
4607 O O   . VAL   B 49  ? 0.1348 0.1359 0.1436 0.0029  0.0008  0.0039  49  VAL   B O   
4608 C CB  . VAL   B 49  ? 0.1430 0.1558 0.1746 0.0034  -0.0287 0.0023  49  VAL   B CB  
4609 C CG1 . VAL   B 49  ? 0.1468 0.1608 0.1758 0.0072  -0.0311 0.0048  49  VAL   B CG1 
4610 C CG2 . VAL   B 49  ? 0.1591 0.1688 0.1930 -0.0072 -0.0377 0.0023  49  VAL   B CG2 
4620 N N   . ALA   B 50  ? 0.1247 0.1313 0.1369 0.0048  -0.0045 0.0084  50  ALA   B N   
4621 C CA  . ALA   B 50  ? 0.1300 0.1254 0.1441 0.0048  -0.0077 0.0108  50  ALA   B CA  
4622 C C   . ALA   B 50  ? 0.1348 0.1287 0.1441 0.0074  -0.0050 0.0056  50  ALA   B C   
4623 O O   . ALA   B 50  ? 0.1382 0.1251 0.1361 0.0055  -0.0035 0.0036  50  ALA   B O   
4624 C CB  . ALA   B 50  ? 0.1345 0.1226 0.1475 -0.0005 0.0028  0.0081  50  ALA   B CB  
4630 N N   . GLY   B 51  ? 0.1275 0.1355 0.1541 0.0114  -0.0090 0.0107  51  GLY   B N   
4631 C CA  . GLY   B 51  ? 0.1325 0.1416 0.1668 0.0168  -0.0121 0.0080  51  GLY   B CA  
4632 C C   . GLY   B 51  ? 0.1301 0.1393 0.1705 0.0144  -0.0119 0.0118  51  GLY   B C   
4633 O O   . GLY   B 51  ? 0.1374 0.1512 0.1802 0.0092  -0.0082 0.0030  51  GLY   B O   
4637 N N   . ALA   B 52  ? 0.1337 0.1314 0.1650 0.0142  -0.0069 0.0155  52  ALA   B N   
4638 C CA  . ALA   B 52  ? 0.1410 0.1420 0.1542 0.0150  0.0038  0.0049  52  ALA   B CA  
4639 C C   . ALA   B 52  ? 0.1345 0.1431 0.1381 0.0069  0.0036  0.0101  52  ALA   B C   
4640 O O   . ALA   B 52  ? 0.1337 0.1468 0.1575 0.0102  0.0048  0.0052  52  ALA   B O   
4641 C CB  . ALA   B 52  ? 0.1584 0.1486 0.1505 0.0028  0.0104  0.0010  52  ALA   B CB  
4647 N N   . LEU   B 53  ? 0.1285 0.1323 0.1356 0.0184  0.0019  0.0073  53  LEU   B N   
4648 C CA  . LEU   B 53  ? 0.1263 0.1394 0.1422 0.0139  -0.0012 0.0119  53  LEU   B CA  
4649 C C   . LEU   B 53  ? 0.1305 0.1377 0.1380 0.0081  -0.0044 0.0121  53  LEU   B C   
4650 O O   . LEU   B 53  ? 0.1370 0.1405 0.1474 -0.0013 -0.0022 0.0135  53  LEU   B O   
4651 C CB  . LEU   B 53  ? 0.1282 0.1472 0.1468 0.0120  -0.0039 0.0141  53  LEU   B CB  
4652 C CG  . LEU   B 53  ? 0.1263 0.1660 0.1563 0.0023  0.0019  0.0208  53  LEU   B CG  
4653 C CD1 . LEU   B 53  ? 0.1318 0.1869 0.1794 0.0114  -0.0085 0.0062  53  LEU   B CD1 
4654 C CD2 . LEU   B 53  ? 0.1418 0.1897 0.1816 -0.0105 -0.0015 -0.0125 53  LEU   B CD2 
4666 N N   . ASN   B 54  ? 0.1288 0.1325 0.1344 0.0052  -0.0083 0.0112  54  ASN   B N   
4667 C CA  . ASN   B 54  ? 0.1334 0.1381 0.1524 0.0029  -0.0042 0.0077  54  ASN   B CA  
4668 C C   . ASN   B 54  ? 0.1289 0.1440 0.1771 0.0026  0.0025  0.0105  54  ASN   B C   
4669 O O   . ASN   B 54  ? 0.1284 0.1489 0.1701 -0.0015 0.0017  0.0079  54  ASN   B O   
4670 C CB  . ASN   B 54  ? 0.1378 0.1541 0.1702 0.0030  -0.0030 0.0024  54  ASN   B CB  
4671 C CG  . ASN   B 54  ? 0.1379 0.1652 0.1669 0.0033  -0.0027 0.0035  54  ASN   B CG  
4672 O OD1 . ASN   B 54  ? 0.1373 0.1568 0.1670 -0.0003 -0.0121 -0.0051 54  ASN   B OD1 
4673 N ND2 . ASN   B 54  ? 0.1495 0.1846 0.1840 -0.0055 -0.0305 0.0149  54  ASN   B ND2 
4680 N N   . LYS   B 55  ? 0.1281 0.1471 0.1854 0.0095  -0.0021 0.0110  55  LYS   B N   
4681 C CA  . LYS   B 55  ? 0.1348 0.1626 0.2070 0.0206  0.0040  0.0157  55  LYS   B CA  
4682 C C   . LYS   B 55  ? 0.1302 0.1613 0.1977 0.0140  0.0066  0.0069  55  LYS   B C   
4683 O O   . LYS   B 55  ? 0.1249 0.1712 0.2040 0.0091  0.0071  -0.0016 55  LYS   B O   
4684 C CB  . LYS   B 55  ? 0.1479 0.1799 0.2305 0.0312  0.0034  0.0285  55  LYS   B CB  
4685 C CG  . LYS   B 55  ? 0.1932 0.2031 0.2994 0.0303  0.0195  0.0323  55  LYS   B CG  
4686 C CD  . LYS   B 55  ? 0.2313 0.2209 0.3609 0.0418  0.0302  0.0327  55  LYS   B CD  
4687 C CE  . LYS   B 55  ? 0.2597 0.2426 0.4165 0.0508  0.0353  0.0312  55  LYS   B CE  
4688 N NZ  . LYS   B 55  ? 0.2702 0.2586 0.4468 0.0537  0.0210  0.0400  55  LYS   B NZ  
4702 N N   . ALA   B 56  ? 0.1324 0.1603 0.1833 0.0101  0.0027  0.0030  56  ALA   B N   
4703 C CA  . ALA   B 56  ? 0.1424 0.1751 0.1833 0.0049  0.0097  0.0043  56  ALA   B CA  
4704 C C   . ALA   B 56  ? 0.1477 0.1729 0.1702 0.0014  0.0134  0.0124  56  ALA   B C   
4705 O O   . ALA   B 56  ? 0.1609 0.1820 0.1792 0.0077  0.0280  0.0095  56  ALA   B O   
4706 C CB  . ALA   B 56  ? 0.1532 0.1986 0.1767 -0.0108 0.0059  0.0031  56  ALA   B CB  
4712 N N   . THR   B 57  ? 0.1384 0.1628 0.1777 0.0020  0.0213  0.0148  57  THR   B N   
4713 C CA  . THR   B 57  ? 0.1416 0.1638 0.1802 -0.0009 0.0138  0.0183  57  THR   B CA  
4714 C C   . THR   B 57  ? 0.1443 0.1751 0.1957 -0.0014 0.0163  0.0202  57  THR   B C   
4715 O O   . THR   B 57  ? 0.1495 0.1811 0.1982 -0.0197 0.0168  0.0180  57  THR   B O   
4716 C CB  . THR   B 57  ? 0.1458 0.1515 0.1626 -0.0005 0.0141  0.0180  57  THR   B CB  
4717 O OG1 . THR   B 57  ? 0.1479 0.1450 0.1704 -0.0040 0.0063  0.0073  57  THR   B OG1 
4718 C CG2 . THR   B 57  ? 0.1483 0.1523 0.1609 -0.0007 0.0172  0.0079  57  THR   B CG2 
4726 N N   . ASN   B 58  ? 0.1315 0.1918 0.2175 -0.0115 0.0064  0.0027  58  ASN   B N   
4727 C CA  . ASN   B 58  ? 0.1446 0.2246 0.2571 -0.0241 0.0179  0.0077  58  ASN   B CA  
4728 C C   . ASN   B 58  ? 0.1388 0.2104 0.2192 -0.0173 -0.0082 0.0063  58  ASN   B C   
4729 O O   . ASN   B 58  ? 0.1475 0.2179 0.2293 -0.0201 -0.0138 -0.0111 58  ASN   B O   
4730 C CB  . ASN   B 58  ? 0.1908 0.2665 0.3569 -0.0405 0.0410  0.0092  58  ASN   B CB  
4731 C CG  . ASN   B 58  ? 0.2969 0.3291 0.4796 -0.0428 0.0461  0.0332  58  ASN   B CG  
4732 O OD1 . ASN   B 58  ? 0.3166 0.3366 0.5228 -0.0466 0.0469  0.0449  58  ASN   B OD1 
4733 N ND2 . ASN   B 58  ? 0.3908 0.3908 0.5198 -0.0455 0.0488  0.0415  58  ASN   B ND2 
4740 N N   . ASN   B 59  ? 0.1349 0.1939 0.2052 -0.0092 -0.0077 0.0132  59  ASN   B N   
4741 C CA  . ASN   B 59  ? 0.1383 0.1921 0.1920 -0.0088 -0.0186 0.0182  59  ASN   B CA  
4742 C C   . ASN   B 59  ? 0.1345 0.1813 0.1827 -0.0187 -0.0117 0.0069  59  ASN   B C   
4743 O O   . ASN   B 59  ? 0.1385 0.1852 0.1858 -0.0174 -0.0155 0.0030  59  ASN   B O   
4744 C CB  . ASN   B 59  ? 0.1465 0.2105 0.2058 -0.0043 -0.0272 0.0126  59  ASN   B CB  
4745 C CG  . ASN   B 59  ? 0.1600 0.2294 0.2174 -0.0038 -0.0344 0.0114  59  ASN   B CG  
4746 O OD1 . ASN   B 59  ? 0.1645 0.2344 0.2174 -0.0018 -0.0283 0.0223  59  ASN   B OD1 
4747 N ND2 . ASN   B 59  ? 0.1679 0.2418 0.2271 -0.0079 -0.0352 0.0043  59  ASN   B ND2 
4754 N N   . ALA   B 60  ? 0.1327 0.1700 0.1854 -0.0195 -0.0054 0.0047  60  ALA   B N   
4755 C CA  . ALA   B 60  ? 0.1413 0.1600 0.1962 -0.0226 -0.0010 0.0122  60  ALA   B CA  
4756 C C   . ALA   B 60  ? 0.1441 0.1508 0.1706 -0.0161 -0.0046 0.0058  60  ALA   B C   
4757 O O   . ALA   B 60  ? 0.1480 0.1528 0.1745 -0.0194 0.0015  -0.0037 60  ALA   B O   
4758 C CB  . ALA   B 60  ? 0.1589 0.1601 0.2218 -0.0111 -0.0009 0.0195  60  ALA   B CB  
4764 N N   . MET   B 61  ? 0.1370 0.1407 0.1705 -0.0114 -0.0030 0.0062  61  MET   B N   
4765 C CA  . MET   B 61  ? 0.1325 0.1393 0.1647 -0.0091 -0.0139 0.0081  61  MET   B CA  
4766 C C   . MET   B 61  ? 0.1378 0.1332 0.1656 -0.0102 -0.0181 0.0053  61  MET   B C   
4767 O O   . MET   B 61  ? 0.1409 0.1347 0.1574 -0.0025 -0.0145 -0.0096 61  MET   B O   
4768 C CB  . MET   B 61  ? 0.1267 0.1426 0.1693 -0.0074 -0.0121 -0.0019 61  MET   B CB  
4769 C CG  . MET   B 61  ? 0.1277 0.1419 0.1585 0.0013  -0.0048 0.0054  61  MET   B CG  
4770 S SD  . MET   B 61  ? 0.1296 0.1406 0.1729 -0.0032 -0.0055 -0.0085 61  MET   B SD  
4771 C CE  . MET   B 61  ? 0.1401 0.1593 0.1856 0.0029  -0.0080 -0.0200 61  MET   B CE  
4781 N N   . GLN   B 62  ? 0.1368 0.1411 0.1592 -0.0052 -0.0167 0.0047  62  GLN   B N   
4782 C CA  . GLN   B 62  ? 0.1413 0.1509 0.1596 -0.0086 -0.0203 0.0008  62  GLN   B CA  
4783 C C   . GLN   B 62  ? 0.1371 0.1531 0.1595 -0.0077 -0.0267 -0.0017 62  GLN   B C   
4784 O O   . GLN   B 62  ? 0.1466 0.1566 0.1685 -0.0053 -0.0309 -0.0114 62  GLN   B O   
4785 C CB  . GLN   B 62  ? 0.1409 0.1542 0.1684 -0.0034 -0.0167 0.0134  62  GLN   B CB  
4786 C CG  . GLN   B 62  ? 0.1442 0.1545 0.1727 -0.0001 -0.0261 0.0022  62  GLN   B CG  
4787 C CD  . GLN   B 62  ? 0.1464 0.1531 0.1537 0.0023  -0.0281 0.0064  62  GLN   B CD  
4788 O OE1 . GLN   B 62  ? 0.1485 0.1513 0.1695 -0.0061 -0.0247 -0.0069 62  GLN   B OE1 
4789 N NE2 . GLN   B 62  ? 0.1462 0.1597 0.1488 0.0008  -0.0218 -0.0073 62  GLN   B NE2 
4798 N N   . VAL   B 63  ? 0.1422 0.1575 0.1814 -0.0098 -0.0234 -0.0098 63  VAL   B N   
4799 C CA  . VAL   B 63  ? 0.1513 0.1580 0.1962 -0.0162 -0.0284 -0.0083 63  VAL   B CA  
4800 C C   . VAL   B 63  ? 0.1543 0.1489 0.1814 -0.0226 -0.0304 -0.0112 63  VAL   B C   
4801 O O   . VAL   B 63  ? 0.1644 0.1510 0.1910 -0.0209 -0.0379 -0.0108 63  VAL   B O   
4802 C CB  . VAL   B 63  ? 0.1503 0.1799 0.2294 -0.0304 -0.0273 -0.0120 63  VAL   B CB  
4803 C CG1 . VAL   B 63  ? 0.1598 0.1889 0.2417 -0.0381 -0.0169 -0.0191 63  VAL   B CG1 
4804 C CG2 . VAL   B 63  ? 0.1486 0.1922 0.2433 -0.0225 -0.0245 -0.0089 63  VAL   B CG2 
4814 N N   . GLU   B 64  ? 0.1528 0.1442 0.1771 -0.0163 -0.0273 -0.0083 64  GLU   B N   
4815 C CA  . GLU   B 64  ? 0.1548 0.1315 0.1754 -0.0147 -0.0314 -0.0084 64  GLU   B CA  
4816 C C   . GLU   B 64  ? 0.1507 0.1340 0.1565 -0.0103 -0.0307 -0.0156 64  GLU   B C   
4817 O O   . GLU   B 64  ? 0.1603 0.1407 0.1521 -0.0108 -0.0261 -0.0170 64  GLU   B O   
4818 C CB  . GLU   B 64  ? 0.1588 0.1377 0.1852 -0.0174 -0.0294 -0.0079 64  GLU   B CB  
4819 C CG  . GLU   B 64  ? 0.1667 0.1494 0.1768 -0.0250 -0.0331 -0.0147 64  GLU   B CG  
4820 C CD  . GLU   B 64  ? 0.1698 0.1564 0.1829 -0.0319 -0.0305 -0.0112 64  GLU   B CD  
4821 O OE1 . GLU   B 64  ? 0.1689 0.1708 0.1778 -0.0322 -0.0283 -0.0221 64  GLU   B OE1 
4822 O OE2 . GLU   B 64  ? 0.1835 0.1640 0.1831 -0.0374 -0.0508 -0.0115 64  GLU   B OE2 
4829 N N   . SER   B 65  ? 0.1456 0.1314 0.1625 -0.0114 -0.0181 -0.0165 65  SER   B N   
4830 C CA  . SER   B 65  ? 0.1493 0.1342 0.1656 -0.0065 -0.0194 -0.0139 65  SER   B CA  
4831 C C   . SER   B 65  ? 0.1523 0.1373 0.1572 -0.0040 -0.0329 -0.0236 65  SER   B C   
4832 O O   . SER   B 65  ? 0.1519 0.1458 0.1664 -0.0042 -0.0220 -0.0273 65  SER   B O   
4833 C CB  . SER   B 65  ? 0.1492 0.1347 0.1642 -0.0115 -0.0192 -0.0133 65  SER   B CB  
4834 O OG  . SER   B 65  ? 0.1521 0.1343 0.1678 -0.0108 -0.0129 -0.0159 65  SER   B OG  
4840 N N   . ASP   B 66  ? 0.1594 0.1431 0.1570 -0.0065 -0.0264 -0.0168 66  ASP   B N   
4841 C CA  . ASP   B 66  ? 0.1630 0.1536 0.1526 -0.0016 -0.0249 -0.0131 66  ASP   B CA  
4842 C C   . ASP   B 66  ? 0.1686 0.1540 0.1603 -0.0052 -0.0217 -0.0185 66  ASP   B C   
4843 O O   . ASP   B 66  ? 0.1715 0.1626 0.1588 -0.0038 -0.0280 -0.0206 66  ASP   B O   
4844 C CB  . ASP   B 66  ? 0.1808 0.1647 0.1675 0.0065  -0.0388 -0.0177 66  ASP   B CB  
4845 C CG  . ASP   B 66  ? 0.2140 0.1772 0.1863 0.0155  -0.0547 -0.0059 66  ASP   B CG  
4846 O OD1 . ASP   B 66  ? 0.2437 0.1740 0.2045 0.0059  -0.0475 -0.0010 66  ASP   B OD1 
4847 O OD2 . ASP   B 66  ? 0.2317 0.2017 0.2599 0.0346  -0.0536 -0.0025 66  ASP   B OD2 
4852 N N   . ASP   B 67  ? 0.1652 0.1454 0.1556 -0.0121 -0.0251 -0.0196 67  ASP   B N   
4853 C CA  . ASP   B 67  ? 0.1808 0.1449 0.1659 -0.0173 -0.0287 -0.0134 67  ASP   B CA  
4854 C C   . ASP   B 67  ? 0.1762 0.1470 0.1771 -0.0064 -0.0302 -0.0142 67  ASP   B C   
4855 O O   . ASP   B 67  ? 0.1804 0.1536 0.1872 -0.0047 -0.0216 -0.0232 67  ASP   B O   
4856 C CB  . ASP   B 67  ? 0.2029 0.1569 0.1882 -0.0218 -0.0442 -0.0068 67  ASP   B CB  
4857 C CG  . ASP   B 67  ? 0.2402 0.1644 0.1943 -0.0131 -0.0637 -0.0120 67  ASP   B CG  
4858 O OD1 . ASP   B 67  ? 0.2589 0.1652 0.2140 -0.0155 -0.0690 -0.0069 67  ASP   B OD1 
4859 O OD2 . ASP   B 67  ? 0.2531 0.1735 0.2030 -0.0022 -0.0750 -0.0116 67  ASP   B OD2 
4864 N N   . TYR   B 68  ? 0.1665 0.1503 0.1657 0.0020  -0.0395 -0.0239 68  TYR   B N   
4865 C CA  . TYR   B 68  ? 0.1682 0.1665 0.1887 0.0066  -0.0417 -0.0371 68  TYR   B CA  
4866 C C   . TYR   B 68  ? 0.1583 0.1593 0.1822 0.0029  -0.0354 -0.0476 68  TYR   B C   
4867 O O   . TYR   B 68  ? 0.1625 0.1697 0.1911 0.0046  -0.0324 -0.0636 68  TYR   B O   
4868 C CB  . TYR   B 68  ? 0.1736 0.1818 0.1924 0.0128  -0.0471 -0.0505 68  TYR   B CB  
4869 C CG  . TYR   B 68  ? 0.1855 0.2007 0.1908 0.0158  -0.0388 -0.0703 68  TYR   B CG  
4870 C CD1 . TYR   B 68  ? 0.1883 0.2006 0.2240 -0.0013 -0.0345 -0.0740 68  TYR   B CD1 
4871 C CD2 . TYR   B 68  ? 0.1897 0.2174 0.2048 0.0243  -0.0471 -0.0561 68  TYR   B CD2 
4872 C CE1 . TYR   B 68  ? 0.1947 0.2154 0.2397 -0.0011 -0.0353 -0.0726 68  TYR   B CE1 
4873 C CE2 . TYR   B 68  ? 0.1901 0.2220 0.2188 0.0200  -0.0368 -0.0697 68  TYR   B CE2 
4874 C CZ  . TYR   B 68  ? 0.1855 0.2219 0.2338 0.0042  -0.0395 -0.0757 68  TYR   B CZ  
4875 O OH  . TYR   B 68  ? 0.1831 0.2437 0.2615 0.0005  -0.0370 -0.0541 68  TYR   B OH  
4885 N N   . ILE   B 69  ? 0.1626 0.1516 0.1746 0.0040  -0.0301 -0.0419 69  ILE   B N   
4886 C CA  . ILE   B 69  ? 0.1702 0.1585 0.1864 -0.0020 -0.0142 -0.0438 69  ILE   B CA  
4887 C C   . ILE   B 69  ? 0.1689 0.1562 0.1756 0.0032  -0.0322 -0.0360 69  ILE   B C   
4888 O O   . ILE   B 69  ? 0.1760 0.1694 0.1735 0.0022  -0.0224 -0.0363 69  ILE   B O   
4889 C CB  . ILE   B 69  ? 0.1780 0.1671 0.2115 -0.0080 0.0037  -0.0387 69  ILE   B CB  
4890 C CG1 . ILE   B 69  ? 0.1801 0.1659 0.2263 -0.0104 0.0038  -0.0330 69  ILE   B CG1 
4891 C CG2 . ILE   B 69  ? 0.1907 0.1769 0.2347 -0.0091 -0.0002 -0.0330 69  ILE   B CG2 
4892 C CD1 . ILE   B 69  ? 0.1799 0.1693 0.2366 -0.0166 0.0055  -0.0438 69  ILE   B CD1 
4904 N N   . ALA   B 70  ? 0.1648 0.1553 0.1678 0.0057  -0.0355 -0.0298 70  ALA   B N   
4905 C CA  . ALA   B 70  ? 0.1670 0.1575 0.1643 0.0049  -0.0401 -0.0228 70  ALA   B CA  
4906 C C   . ALA   B 70  ? 0.1693 0.1541 0.1818 0.0028  -0.0442 -0.0342 70  ALA   B C   
4907 O O   . ALA   B 70  ? 0.1750 0.1596 0.1776 0.0034  -0.0364 -0.0402 70  ALA   B O   
4908 C CB  . ALA   B 70  ? 0.1715 0.1733 0.1688 -0.0027 -0.0402 -0.0208 70  ALA   B CB  
4914 N N   . THR   B 71  ? 0.1773 0.1612 0.1791 0.0060  -0.0525 -0.0347 71  THR   B N   
4915 C CA  . THR   B 71  ? 0.1913 0.1650 0.2009 0.0082  -0.0665 -0.0376 71  THR   B CA  
4916 C C   . THR   B 71  ? 0.1880 0.1692 0.2246 0.0235  -0.0655 -0.0546 71  THR   B C   
4917 O O   . THR   B 71  ? 0.1936 0.1712 0.2604 0.0309  -0.0569 -0.0681 71  THR   B O   
4918 C CB  . THR   B 71  ? 0.2108 0.1836 0.2279 0.0009  -0.0726 -0.0131 71  THR   B CB  
4919 O OG1 . THR   B 71  ? 0.2256 0.2084 0.2594 -0.0159 -0.0682 0.0012  71  THR   B OG1 
4920 C CG2 . THR   B 71  ? 0.2303 0.1779 0.2580 0.0047  -0.0646 0.0004  71  THR   B CG2 
4928 N N   . ASN   B 72  ? 0.1753 0.1725 0.2234 0.0145  -0.0601 -0.0728 72  ASN   B N   
4929 C CA  . ASN   B 72  ? 0.1752 0.1882 0.2219 0.0141  -0.0543 -0.0771 72  ASN   B CA  
4930 C C   . ASN   B 72  ? 0.1758 0.2021 0.2323 0.0029  -0.0245 -0.0785 72  ASN   B C   
4931 O O   . ASN   B 72  ? 0.1798 0.2142 0.2527 0.0108  -0.0105 -0.0778 72  ASN   B O   
4932 C CB  . ASN   B 72  ? 0.1811 0.2010 0.2432 0.0117  -0.0634 -0.0649 72  ASN   B CB  
4933 C CG  . ASN   B 72  ? 0.1949 0.2161 0.2528 0.0241  -0.0587 -0.0404 72  ASN   B CG  
4934 O OD1 . ASN   B 72  ? 0.2183 0.2343 0.2430 0.0129  -0.0453 -0.0457 72  ASN   B OD1 
4935 N ND2 . ASN   B 72  ? 0.2009 0.2218 0.2832 0.0406  -0.0470 -0.0115 72  ASN   B ND2 
4942 N N   . GLY   B 73  ? 0.1773 0.2016 0.2117 -0.0037 -0.0205 -0.0759 73  GLY   B N   
4943 C CA  . GLY   B 73  ? 0.1703 0.2048 0.1916 -0.0043 -0.0127 -0.0686 73  GLY   B CA  
4944 C C   . GLY   B 73  ? 0.1652 0.2016 0.1470 0.0017  -0.0130 -0.0592 73  GLY   B C   
4945 O O   . GLY   B 73  ? 0.1618 0.1885 0.1594 0.0031  -0.0118 -0.0425 73  GLY   B O   
4949 N N   . PRO   B 74  ? 0.1742 0.2131 0.1461 -0.0013 -0.0199 -0.0510 74  PRO   B N   
4950 C CA  . PRO   B 74  ? 0.1678 0.2117 0.1300 0.0045  -0.0173 -0.0317 74  PRO   B CA  
4951 C C   . PRO   B 74  ? 0.1592 0.1938 0.1285 0.0084  -0.0123 -0.0261 74  PRO   B C   
4952 O O   . PRO   B 74  ? 0.1584 0.1961 0.1696 0.0069  -0.0099 -0.0369 74  PRO   B O   
4953 C CB  . PRO   B 74  ? 0.1836 0.2248 0.1357 0.0018  -0.0211 -0.0300 74  PRO   B CB  
4954 C CG  . PRO   B 74  ? 0.1934 0.2358 0.1742 0.0009  -0.0186 -0.0317 74  PRO   B CG  
4955 C CD  . PRO   B 74  ? 0.1914 0.2270 0.1705 0.0033  -0.0131 -0.0427 74  PRO   B CD  
4963 N N   . LEU   B 75  ? 0.1494 0.1789 0.1209 0.0105  -0.0163 -0.0183 75  LEU   B N   
4964 C CA  . LEU   B 75  ? 0.1528 0.1803 0.1289 0.0065  -0.0162 -0.0146 75  LEU   B CA  
4965 C C   . LEU   B 75  ? 0.1521 0.1885 0.1306 0.0108  -0.0098 -0.0163 75  LEU   B C   
4966 O O   . LEU   B 75  ? 0.1671 0.2030 0.1367 -0.0020 -0.0034 -0.0086 75  LEU   B O   
4967 C CB  . LEU   B 75  ? 0.1564 0.1773 0.1248 -0.0012 -0.0201 0.0024  75  LEU   B CB  
4968 C CG  . LEU   B 75  ? 0.1839 0.1927 0.1493 -0.0258 -0.0119 0.0003  75  LEU   B CG  
4969 C CD1 . LEU   B 75  ? 0.2155 0.2049 0.1525 -0.0364 0.0057  -0.0062 75  LEU   B CD1 
4970 C CD2 . LEU   B 75  ? 0.2159 0.2165 0.2170 -0.0177 -0.0022 0.0084  75  LEU   B CD2 
4982 N N   . LYS   B 76  ? 0.1521 0.2080 0.1435 0.0059  0.0003  -0.0094 76  LYS   B N   
4983 C CA  . LYS   B 76  ? 0.1672 0.2175 0.1799 -0.0074 0.0170  -0.0111 76  LYS   B CA  
4984 C C   . LYS   B 76  ? 0.1507 0.1966 0.1451 0.0006  0.0100  0.0102  76  LYS   B C   
4985 O O   . LYS   B 76  ? 0.1501 0.1812 0.1452 0.0012  -0.0016 0.0157  76  LYS   B O   
4986 C CB  . LYS   B 76  ? 0.1877 0.2309 0.2554 -0.0109 0.0392  -0.0360 76  LYS   B CB  
4987 C CG  . LYS   B 76  ? 0.1911 0.2469 0.2920 0.0030  0.0429  -0.0482 76  LYS   B CG  
4988 C CD  . LYS   B 76  ? 0.1944 0.2585 0.3354 0.0158  0.0277  -0.0607 76  LYS   B CD  
4989 C CE  . LYS   B 76  ? 0.2161 0.2746 0.3761 0.0190  0.0068  -0.0665 76  LYS   B CE  
4990 N NZ  . LYS   B 76  ? 0.2148 0.2796 0.3997 0.0147  -0.0156 -0.0820 76  LYS   B NZ  
5004 N N   . VAL   B 77  ? 0.1610 0.2028 0.1380 0.0059  0.0105  0.0094  77  VAL   B N   
5005 C CA  . VAL   B 77  ? 0.1632 0.1908 0.1562 0.0172  0.0138  0.0314  77  VAL   B CA  
5006 C C   . VAL   B 77  ? 0.1513 0.1741 0.1479 0.0197  0.0170  0.0243  77  VAL   B C   
5007 O O   . VAL   B 77  ? 0.1569 0.1695 0.1504 0.0260  0.0244  0.0205  77  VAL   B O   
5008 C CB  . VAL   B 77  ? 0.1741 0.2005 0.1865 0.0164  0.0226  0.0469  77  VAL   B CB  
5009 C CG1 . VAL   B 77  ? 0.1817 0.1915 0.2119 0.0129  0.0284  0.0477  77  VAL   B CG1 
5010 C CG2 . VAL   B 77  ? 0.1869 0.2178 0.2239 0.0122  0.0088  0.0543  77  VAL   B CG2 
5020 N N   . GLY   B 78  ? 0.1499 0.1647 0.1459 0.0160  0.0164  0.0151  78  GLY   B N   
5021 C CA  . GLY   B 78  ? 0.1442 0.1603 0.1388 0.0135  0.0194  0.0142  78  GLY   B CA  
5022 C C   . GLY   B 78  ? 0.1387 0.1512 0.1325 0.0127  0.0188  0.0098  78  GLY   B C   
5023 O O   . GLY   B 78  ? 0.1431 0.1540 0.1393 0.0195  0.0119  0.0166  78  GLY   B O   
5027 N N   . GLY   B 79  ? 0.1350 0.1536 0.1396 0.0088  0.0133  0.0065  79  GLY   B N   
5028 C CA  . GLY   B 79  ? 0.1404 0.1400 0.1395 0.0121  0.0141  0.0054  79  GLY   B CA  
5029 C C   . GLY   B 79  ? 0.1306 0.1354 0.1397 0.0118  0.0106  -0.0002 79  GLY   B C   
5030 O O   . GLY   B 79  ? 0.1363 0.1356 0.1501 0.0127  0.0170  0.0112  79  GLY   B O   
5034 N N   . SER   B 80  ? 0.1290 0.1310 0.1493 0.0077  0.0150  0.0010  80  SER   B N   
5035 C CA  . SER   B 80  ? 0.1234 0.1276 0.1493 0.0029  0.0046  -0.0001 80  SER   B CA  
5036 C C   . SER   B 80  ? 0.1293 0.1271 0.1416 0.0092  -0.0056 -0.0002 80  SER   B C   
5037 O O   . SER   B 80  ? 0.1392 0.1313 0.1766 0.0116  -0.0010 -0.0097 80  SER   B O   
5038 C CB  . SER   B 80  ? 0.1297 0.1347 0.1545 -0.0023 -0.0034 -0.0031 80  SER   B CB  
5039 O OG  . SER   B 80  ? 0.1373 0.1483 0.1686 0.0013  -0.0074 0.0004  80  SER   B OG  
5045 N N   . CYS   B 81  ? 0.1281 0.1181 0.1469 0.0023  -0.0076 -0.0031 81  CYS   B N   
5046 C CA  . CYS   B 81  ? 0.1352 0.1106 0.1540 0.0055  -0.0099 -0.0052 81  CYS   B CA  
5047 C C   . CYS   B 81  ? 0.1338 0.1098 0.1428 0.0028  -0.0139 -0.0085 81  CYS   B C   
5048 O O   . CYS   B 81  ? 0.1547 0.1136 0.1392 0.0105  0.0005  -0.0030 81  CYS   B O   
5049 C CB  . CYS   B 81  ? 0.1487 0.1296 0.1526 0.0009  -0.0172 -0.0057 81  CYS   B CB  
5050 S SG  . CYS   B 81  ? 0.1496 0.1469 0.1562 -0.0020 -0.0265 -0.0150 81  CYS   B SG  
5056 N N   . VAL   B 82  ? 0.1375 0.1101 0.1507 0.0012  -0.0129 -0.0107 82  VAL   B N   
5057 C CA  . VAL   B 82  ? 0.1415 0.1167 0.1507 -0.0057 -0.0125 -0.0012 82  VAL   B CA  
5058 C C   . VAL   B 82  ? 0.1456 0.1114 0.1636 -0.0038 -0.0092 -0.0040 82  VAL   B C   
5059 O O   . VAL   B 82  ? 0.1522 0.1139 0.1806 -0.0064 -0.0084 -0.0135 82  VAL   B O   
5060 C CB  . VAL   B 82  ? 0.1509 0.1379 0.1680 -0.0012 -0.0143 0.0062  82  VAL   B CB  
5061 C CG1 . VAL   B 82  ? 0.1652 0.1663 0.1833 0.0008  -0.0065 0.0095  82  VAL   B CG1 
5062 C CG2 . VAL   B 82  ? 0.1590 0.1484 0.1721 -0.0107 -0.0243 0.0099  82  VAL   B CG2 
5072 N N   . LEU   B 83  ? 0.1338 0.1082 0.1572 -0.0125 -0.0173 -0.0130 83  LEU   B N   
5073 C CA  . LEU   B 83  ? 0.1399 0.1130 0.1462 -0.0130 -0.0114 -0.0126 83  LEU   B CA  
5074 C C   . LEU   B 83  ? 0.1370 0.1106 0.1483 -0.0193 -0.0120 -0.0060 83  LEU   B C   
5075 O O   . LEU   B 83  ? 0.1416 0.1255 0.1296 -0.0230 -0.0131 0.0017  83  LEU   B O   
5076 C CB  . LEU   B 83  ? 0.1444 0.1273 0.1594 -0.0115 -0.0210 -0.0078 83  LEU   B CB  
5077 C CG  . LEU   B 83  ? 0.1644 0.1478 0.1617 -0.0181 -0.0117 -0.0092 83  LEU   B CG  
5078 C CD1 . LEU   B 83  ? 0.1762 0.1492 0.1732 -0.0122 -0.0310 0.0001  83  LEU   B CD1 
5079 C CD2 . LEU   B 83  ? 0.1801 0.1566 0.1731 -0.0078 -0.0131 -0.0253 83  LEU   B CD2 
5091 N N   . SER   B 84  ? 0.1457 0.1242 0.1583 -0.0219 -0.0098 -0.0001 84  SER   B N   
5092 C CA  . SER   B 84  ? 0.1437 0.1411 0.1592 -0.0263 -0.0160 0.0107  84  SER   B CA  
5093 C C   . SER   B 84  ? 0.1375 0.1551 0.1215 -0.0201 -0.0165 0.0129  84  SER   B C   
5094 O O   . SER   B 84  ? 0.1416 0.1421 0.1149 -0.0164 -0.0112 0.0064  84  SER   B O   
5095 C CB  . SER   B 84  ? 0.1657 0.1491 0.2042 -0.0274 0.0085  0.0103  84  SER   B CB  
5096 O OG  . SER   B 84  ? 0.1676 0.1592 0.2434 -0.0382 0.0093  0.0190  84  SER   B OG  
5102 N N   . GLY   B 85  ? 0.1412 0.1754 0.1296 -0.0210 -0.0187 0.0174  85  GLY   B N   
5103 C CA  . GLY   B 85  ? 0.1382 0.1818 0.1494 -0.0313 -0.0045 -0.0044 85  GLY   B CA  
5104 C C   . GLY   B 85  ? 0.1363 0.1615 0.1490 -0.0396 -0.0036 0.0112  85  GLY   B C   
5105 O O   . GLY   B 85  ? 0.1463 0.1642 0.1391 -0.0474 0.0122  0.0049  85  GLY   B O   
5109 N N   . HIS   B 86  ? 0.1350 0.1503 0.1606 -0.0307 -0.0191 0.0274  86  HIS   B N   
5110 C CA  . HIS   B 86  ? 0.1360 0.1498 0.1593 -0.0344 -0.0128 0.0270  86  HIS   B CA  
5111 C C   . HIS   B 86  ? 0.1361 0.1629 0.1569 -0.0442 -0.0026 0.0363  86  HIS   B C   
5112 O O   . HIS   B 86  ? 0.1527 0.1776 0.1521 -0.0342 -0.0031 0.0340  86  HIS   B O   
5113 C CB  . HIS   B 86  ? 0.1452 0.1544 0.1685 -0.0219 -0.0183 0.0124  86  HIS   B CB  
5114 C CG  . HIS   B 86  ? 0.1517 0.1583 0.1625 -0.0130 -0.0248 0.0155  86  HIS   B CG  
5115 N ND1 . HIS   B 86  ? 0.1650 0.1790 0.1752 -0.0243 -0.0322 0.0023  86  HIS   B ND1 
5116 C CD2 . HIS   B 86  ? 0.1503 0.1599 0.1679 -0.0121 -0.0272 0.0147  86  HIS   B CD2 
5117 C CE1 . HIS   B 86  ? 0.1716 0.1792 0.1657 -0.0183 -0.0190 -0.0211 86  HIS   B CE1 
5118 N NE2 . HIS   B 86  ? 0.1649 0.1754 0.1501 -0.0032 -0.0161 -0.0015 86  HIS   B NE2 
5126 N N   . ASN   B 87  ? 0.1392 0.1683 0.1616 -0.0352 -0.0057 0.0312  87  ASN   B N   
5127 C CA  . ASN   B 87  ? 0.1459 0.1875 0.1663 -0.0337 0.0201  0.0261  87  ASN   B CA  
5128 C C   . ASN   B 87  ? 0.1573 0.1767 0.1522 -0.0279 0.0304  0.0224  87  ASN   B C   
5129 O O   . ASN   B 87  ? 0.1837 0.1874 0.1752 -0.0235 0.0408  0.0204  87  ASN   B O   
5130 C CB  . ASN   B 87  ? 0.1507 0.2261 0.1940 -0.0268 0.0163  0.0218  87  ASN   B CB  
5131 C CG  . ASN   B 87  ? 0.1577 0.2462 0.2039 0.0034  0.0259  0.0418  87  ASN   B CG  
5132 O OD1 . ASN   B 87  ? 0.1493 0.2293 0.1961 0.0052  0.0415  0.0583  87  ASN   B OD1 
5133 N ND2 . ASN   B 87  ? 0.1879 0.2613 0.2407 0.0065  0.0300  0.0369  87  ASN   B ND2 
5140 N N   . LEU   B 88  ? 0.1465 0.1596 0.1374 -0.0345 0.0180  0.0150  88  LEU   B N   
5141 C CA  . LEU   B 88  ? 0.1572 0.1567 0.1396 -0.0325 0.0089  0.0046  88  LEU   B CA  
5142 C C   . LEU   B 88  ? 0.1543 0.1458 0.1290 -0.0333 0.0038  0.0006  88  LEU   B C   
5143 O O   . LEU   B 88  ? 0.1824 0.1540 0.1729 -0.0207 -0.0205 -0.0133 88  LEU   B O   
5144 C CB  . LEU   B 88  ? 0.1699 0.1626 0.1646 -0.0340 -0.0013 0.0207  88  LEU   B CB  
5145 C CG  . LEU   B 88  ? 0.2015 0.1905 0.1834 -0.0294 -0.0235 0.0355  88  LEU   B CG  
5146 C CD1 . LEU   B 88  ? 0.2125 0.2249 0.1922 -0.0378 -0.0254 0.0455  88  LEU   B CD1 
5147 C CD2 . LEU   B 88  ? 0.2321 0.2172 0.2312 0.0083  -0.0499 0.0266  88  LEU   B CD2 
5159 N N   . ALA   B 89  ? 0.1429 0.1419 0.1242 -0.0330 0.0147  0.0007  89  ALA   B N   
5160 C CA  . ALA   B 89  ? 0.1445 0.1400 0.1154 -0.0346 0.0096  0.0082  89  ALA   B CA  
5161 C C   . ALA   B 89  ? 0.1566 0.1422 0.1201 -0.0411 0.0167  0.0072  89  ALA   B C   
5162 O O   . ALA   B 89  ? 0.1421 0.1506 0.1562 -0.0398 0.0110  -0.0223 89  ALA   B O   
5163 C CB  . ALA   B 89  ? 0.1421 0.1447 0.1241 -0.0341 0.0063  0.0170  89  ALA   B CB  
5169 N N   . LYS   B 90  ? 0.1845 0.1297 0.1335 -0.0423 -0.0055 0.0115  90  LYS   B N   
5170 C CA  . LYS   B 90  ? 0.2012 0.1267 0.1328 -0.0382 -0.0059 0.0152  90  LYS   B CA  
5171 C C   . LYS   B 90  ? 0.1837 0.1208 0.1431 -0.0416 -0.0085 0.0027  90  LYS   B C   
5172 O O   . LYS   B 90  ? 0.1991 0.1414 0.1599 -0.0596 -0.0012 0.0029  90  LYS   B O   
5173 C CB  . LYS   B 90  ? 0.2234 0.1338 0.1615 -0.0284 -0.0018 0.0288  90  LYS   B CB  
5174 C CG  . LYS   B 90  ? 0.2282 0.1476 0.1773 -0.0142 0.0302  0.0266  90  LYS   B CG  
5175 C CD  . LYS   B 90  ? 0.2544 0.1816 0.2259 -0.0150 0.0423  0.0011  90  LYS   B CD  
5176 C CE  . LYS   B 90  ? 0.2713 0.2023 0.2696 -0.0248 0.0392  -0.0085 90  LYS   B CE  
5177 N NZ  . LYS   B 90  ? 0.2729 0.1994 0.2783 -0.0380 0.0475  -0.0193 90  LYS   B NZ  
5191 N N   . HIS   B 91  ? 0.1605 0.1083 0.1302 -0.0273 -0.0153 0.0032  91  HIS   B N   
5192 C CA  . HIS   B 91  ? 0.1484 0.1161 0.1373 -0.0243 -0.0172 -0.0024 91  HIS   B CA  
5193 C C   . HIS   B 91  ? 0.1401 0.1191 0.1280 -0.0284 -0.0084 0.0053  91  HIS   B C   
5194 O O   . HIS   B 91  ? 0.1519 0.1187 0.1236 -0.0240 -0.0188 0.0005  91  HIS   B O   
5195 C CB  . HIS   B 91  ? 0.1667 0.1198 0.1873 -0.0107 -0.0074 0.0153  91  HIS   B CB  
5196 C CG  . HIS   B 91  ? 0.2107 0.1388 0.2561 0.0059  0.0193  0.0226  91  HIS   B CG  
5197 N ND1 . HIS   B 91  ? 0.2428 0.1457 0.3066 0.0030  0.0261  0.0045  91  HIS   B ND1 
5198 C CD2 . HIS   B 91  ? 0.2276 0.1726 0.3001 0.0205  0.0058  0.0520  91  HIS   B CD2 
5199 C CE1 . HIS   B 91  ? 0.2465 0.1617 0.3261 0.0199  0.0250  0.0115  91  HIS   B CE1 
5200 N NE2 . HIS   B 91  ? 0.2348 0.1760 0.3235 0.0318  0.0199  0.0565  91  HIS   B NE2 
5208 N N   . CYS   B 92  ? 0.1318 0.1168 0.1280 -0.0242 -0.0137 0.0028  92  CYS   B N   
5209 C CA  . CYS   B 92  ? 0.1300 0.1146 0.1244 -0.0193 -0.0062 -0.0012 92  CYS   B CA  
5210 C C   . CYS   B 92  ? 0.1288 0.1069 0.1211 -0.0172 -0.0107 0.0019  92  CYS   B C   
5211 O O   . CYS   B 92  ? 0.1367 0.1153 0.1393 -0.0199 -0.0066 -0.0048 92  CYS   B O   
5212 C CB  . CYS   B 92  ? 0.1250 0.1273 0.1312 -0.0157 -0.0061 0.0018  92  CYS   B CB  
5213 S SG  . CYS   B 92  ? 0.1301 0.1238 0.1323 -0.0111 -0.0097 0.0041  92  CYS   B SG  
5219 N N   . LEU   B 93  ? 0.1219 0.1105 0.1192 -0.0099 -0.0032 -0.0048 93  LEU   B N   
5220 C CA  . LEU   B 93  ? 0.1168 0.1124 0.1304 -0.0017 -0.0053 0.0012  93  LEU   B CA  
5221 C C   . LEU   B 93  ? 0.1156 0.1093 0.1187 -0.0006 0.0021  0.0039  93  LEU   B C   
5222 O O   . LEU   B 93  ? 0.1295 0.1078 0.1226 -0.0060 -0.0035 -0.0042 93  LEU   B O   
5223 C CB  . LEU   B 93  ? 0.1218 0.1173 0.1382 -0.0043 -0.0061 0.0018  93  LEU   B CB  
5224 C CG  . LEU   B 93  ? 0.1164 0.1226 0.1480 -0.0038 -0.0024 0.0043  93  LEU   B CG  
5225 C CD1 . LEU   B 93  ? 0.1251 0.1362 0.1414 0.0063  -0.0011 -0.0076 93  LEU   B CD1 
5226 C CD2 . LEU   B 93  ? 0.1162 0.1264 0.1521 -0.0041 -0.0011 -0.0025 93  LEU   B CD2 
5238 N N   . HIS   B 94  ? 0.1204 0.1082 0.1108 -0.0067 -0.0081 0.0033  94  HIS   B N   
5239 C CA  . HIS   B 94  ? 0.1178 0.1088 0.1233 -0.0002 -0.0055 0.0013  94  HIS   B CA  
5240 C C   . HIS   B 94  ? 0.1165 0.1108 0.1295 -0.0004 0.0017  0.0004  94  HIS   B C   
5241 O O   . HIS   B 94  ? 0.1215 0.1205 0.1588 -0.0035 0.0142  -0.0092 94  HIS   B O   
5242 C CB  . HIS   B 94  ? 0.1197 0.1186 0.1216 -0.0058 -0.0051 -0.0017 94  HIS   B CB  
5243 C CG  . HIS   B 94  ? 0.1279 0.1118 0.1198 -0.0086 -0.0224 -0.0014 94  HIS   B CG  
5244 N ND1 . HIS   B 94  ? 0.1296 0.1158 0.1201 -0.0055 -0.0176 0.0012  94  HIS   B ND1 
5245 C CD2 . HIS   B 94  ? 0.1295 0.1112 0.1380 -0.0043 -0.0221 0.0010  94  HIS   B CD2 
5246 C CE1 . HIS   B 94  ? 0.1324 0.1190 0.1163 -0.0117 -0.0165 0.0008  94  HIS   B CE1 
5247 N NE2 . HIS   B 94  ? 0.1264 0.1222 0.1400 -0.0164 -0.0134 -0.0011 94  HIS   B NE2 
5255 N N   . VAL   B 95  ? 0.1145 0.1099 0.1266 -0.0016 0.0012  0.0034  95  VAL   B N   
5256 C CA  . VAL   B 95  ? 0.1153 0.1200 0.1274 -0.0023 0.0011  0.0048  95  VAL   B CA  
5257 C C   . VAL   B 95  ? 0.1205 0.1178 0.1367 -0.0021 0.0061  0.0029  95  VAL   B C   
5258 O O   . VAL   B 95  ? 0.1228 0.1200 0.1452 0.0040  0.0028  0.0075  95  VAL   B O   
5259 C CB  . VAL   B 95  ? 0.1198 0.1166 0.1413 0.0002  -0.0061 0.0036  95  VAL   B CB  
5260 C CG1 . VAL   B 95  ? 0.1265 0.1382 0.1555 -0.0086 -0.0020 0.0128  95  VAL   B CG1 
5261 C CG2 . VAL   B 95  ? 0.1289 0.1142 0.1378 0.0003  -0.0100 0.0012  95  VAL   B CG2 
5271 N N   . VAL   B 96  ? 0.1278 0.1224 0.1318 0.0088  0.0018  0.0089  96  VAL   B N   
5272 C CA  . VAL   B 96  ? 0.1337 0.1331 0.1358 0.0121  -0.0000 0.0082  96  VAL   B CA  
5273 C C   . VAL   B 96  ? 0.1383 0.1357 0.1433 0.0112  0.0025  0.0124  96  VAL   B C   
5274 O O   . VAL   B 96  ? 0.1423 0.1430 0.1670 0.0037  0.0163  0.0042  96  VAL   B O   
5275 C CB  . VAL   B 96  ? 0.1409 0.1469 0.1337 0.0101  0.0042  0.0057  96  VAL   B CB  
5276 C CG1 . VAL   B 96  ? 0.1460 0.1593 0.1526 0.0132  0.0085  -0.0010 96  VAL   B CG1 
5277 C CG2 . VAL   B 96  ? 0.1510 0.1558 0.1497 0.0037  0.0031  0.0032  96  VAL   B CG2 
5287 N N   . GLY   B 97  ? 0.1407 0.1366 0.1331 0.0068  0.0030  0.0128  97  GLY   B N   
5288 C CA  . GLY   B 97  ? 0.1523 0.1391 0.1479 0.0027  0.0102  0.0194  97  GLY   B CA  
5289 C C   . GLY   B 97  ? 0.1669 0.1471 0.1445 0.0102  0.0051  0.0176  97  GLY   B C   
5290 O O   . GLY   B 97  ? 0.1775 0.1566 0.1386 0.0034  0.0018  0.0077  97  GLY   B O   
5294 N N   . PRO   B 98  ? 0.1756 0.1505 0.1487 0.0083  0.0179  0.0271  98  PRO   B N   
5295 C CA  . PRO   B 98  ? 0.1873 0.1633 0.1642 0.0125  0.0198  0.0199  98  PRO   B CA  
5296 C C   . PRO   B 98  ? 0.1933 0.1653 0.1302 0.0191  0.0219  0.0374  98  PRO   B C   
5297 O O   . PRO   B 98  ? 0.1867 0.1599 0.1551 0.0202  0.0249  0.0293  98  PRO   B O   
5298 C CB  . PRO   B 98  ? 0.1726 0.1681 0.1871 0.0058  0.0313  0.0117  98  PRO   B CB  
5299 C CG  . PRO   B 98  ? 0.1686 0.1609 0.1728 0.0015  0.0226  0.0258  98  PRO   B CG  
5300 C CD  . PRO   B 98  ? 0.1615 0.1540 0.1665 0.0024  0.0178  0.0323  98  PRO   B CD  
5308 N N   . ASN   B 99  ? 0.2000 0.1786 0.1304 0.0288  0.0199  0.0167  99  ASN   B N   
5309 C CA  . ASN   B 99  ? 0.2187 0.1811 0.1414 0.0338  0.0127  0.0265  99  ASN   B CA  
5310 C C   . ASN   B 99  ? 0.2468 0.2055 0.1667 0.0219  0.0261  0.0470  99  ASN   B C   
5311 O O   . ASN   B 99  ? 0.2612 0.2106 0.1752 0.0219  0.0166  0.0435  99  ASN   B O   
5312 C CB  . ASN   B 99  ? 0.2271 0.1809 0.1659 0.0353  0.0057  0.0286  99  ASN   B CB  
5313 C CG  . ASN   B 99  ? 0.2312 0.1924 0.1921 0.0337  -0.0073 0.0231  99  ASN   B CG  
5314 O OD1 . ASN   B 99  ? 0.2375 0.1933 0.2019 0.0365  -0.0087 0.0275  99  ASN   B OD1 
5315 N ND2 . ASN   B 99  ? 0.2311 0.1983 0.2019 0.0360  -0.0200 0.0151  99  ASN   B ND2 
5322 N N   A VAL   B 100 ? 0.2657 0.2174 0.2010 0.0166  0.0299  0.0612  100 VAL   B N   
5323 N N   B VAL   B 100 ? 0.2607 0.2159 0.2004 0.0118  0.0361  0.0630  100 VAL   B N   
5324 C CA  A VAL   B 100 ? 0.2920 0.2362 0.2480 0.0112  0.0338  0.0707  100 VAL   B CA  
5325 C CA  B VAL   B 100 ? 0.2868 0.2355 0.2527 0.0025  0.0433  0.0723  100 VAL   B CA  
5326 C C   A VAL   B 100 ? 0.3117 0.2431 0.2467 0.0171  0.0387  0.0877  100 VAL   B C   
5327 C C   B VAL   B 100 ? 0.3092 0.2419 0.2471 0.0111  0.0462  0.0887  100 VAL   B C   
5328 O O   A VAL   B 100 ? 0.3160 0.2490 0.2550 0.0174  0.0408  0.0807  100 VAL   B O   
5329 O O   B VAL   B 100 ? 0.3144 0.2480 0.2525 0.0100  0.0505  0.0792  100 VAL   B O   
5330 C CB  A VAL   B 100 ? 0.3007 0.2496 0.2965 0.0013  0.0313  0.0685  100 VAL   B CB  
5331 C CB  B VAL   B 100 ? 0.2947 0.2511 0.3116 -0.0125 0.0434  0.0729  100 VAL   B CB  
5332 C CG1 A VAL   B 100 ? 0.3043 0.2539 0.3114 0.0000  0.0311  0.0662  100 VAL   B CG1 
5333 C CG1 B VAL   B 100 ? 0.2992 0.2569 0.3317 -0.0139 0.0427  0.0698  100 VAL   B CG1 
5334 C CG2 A VAL   B 100 ? 0.3038 0.2545 0.3073 -0.0021 0.0320  0.0704  100 VAL   B CG2 
5335 C CG2 B VAL   B 100 ? 0.2974 0.2568 0.3253 -0.0174 0.0456  0.0763  100 VAL   B CG2 
5354 N N   . ASN   B 101 ? 0.3268 0.2463 0.2401 0.0268  0.0366  0.1045  101 ASN   B N   
5355 C CA  . ASN   B 101 ? 0.3675 0.2688 0.2721 0.0367  0.0190  0.1110  101 ASN   B CA  
5356 C C   . ASN   B 101 ? 0.4027 0.3118 0.2744 0.0344  -0.0009 0.1074  101 ASN   B C   
5357 O O   . ASN   B 101 ? 0.4084 0.3237 0.2892 0.0415  -0.0100 0.0937  101 ASN   B O   
5358 C CB  . ASN   B 101 ? 0.3741 0.2577 0.2815 0.0367  0.0293  0.1011  101 ASN   B CB  
5359 C CG  . ASN   B 101 ? 0.3779 0.2485 0.2850 0.0367  0.0347  0.1011  101 ASN   B CG  
5360 O OD1 . ASN   B 101 ? 0.3862 0.2526 0.3202 0.0299  0.0461  0.0897  101 ASN   B OD1 
5361 N ND2 . ASN   B 101 ? 0.3733 0.2491 0.2817 0.0375  0.0342  0.0905  101 ASN   B ND2 
5369 N N   A LYS   B 102 ? 0.4156 0.3319 0.2917 0.0294  -0.0003 0.0890  102 LYS   B N   
5370 N N   B LYS   B 102 ? 0.4181 0.3307 0.2819 0.0262  0.0018  0.0993  102 LYS   B N   
5371 C CA  A LYS   B 102 ? 0.4272 0.3539 0.3177 0.0237  0.0044  0.0680  102 LYS   B CA  
5372 C CA  B LYS   B 102 ? 0.4326 0.3533 0.3020 0.0173  0.0095  0.0860  102 LYS   B CA  
5373 C C   A LYS   B 102 ? 0.4225 0.3555 0.3047 0.0255  0.0115  0.0672  102 LYS   B C   
5374 C C   B LYS   B 102 ? 0.4283 0.3515 0.2813 0.0187  0.0194  0.0950  102 LYS   B C   
5375 O O   A LYS   B 102 ? 0.4274 0.3592 0.3082 0.0249  0.0089  0.0645  102 LYS   B O   
5376 O O   B LYS   B 102 ? 0.4351 0.3564 0.2916 0.0182  0.0148  0.0882  102 LYS   B O   
5377 C CB  A LYS   B 102 ? 0.4410 0.3720 0.3577 0.0168  0.0063  0.0469  102 LYS   B CB  
5378 C CB  B LYS   B 102 ? 0.4486 0.3753 0.3468 0.0079  0.0137  0.0592  102 LYS   B CB  
5379 C CG  A LYS   B 102 ? 0.4516 0.3865 0.4034 0.0112  0.0081  0.0248  102 LYS   B CG  
5380 C CG  B LYS   B 102 ? 0.4611 0.3931 0.4006 0.0007  0.0176  0.0296  102 LYS   B CG  
5381 C CD  A LYS   B 102 ? 0.4589 0.3973 0.4397 0.0062  0.0100  0.0074  102 LYS   B CD  
5382 C CD  B LYS   B 102 ? 0.4698 0.4065 0.4435 -0.0057 0.0209  0.0069  102 LYS   B CD  
5383 C CE  A LYS   B 102 ? 0.4629 0.4039 0.4700 0.0022  0.0126  -0.0034 102 LYS   B CE  
5384 C CE  B LYS   B 102 ? 0.4747 0.4147 0.4783 -0.0112 0.0243  -0.0072 102 LYS   B CE  
5385 N NZ  A LYS   B 102 ? 0.4652 0.4077 0.4873 0.0003  0.0144  -0.0080 102 LYS   B NZ  
5386 N NZ  B LYS   B 102 ? 0.4775 0.4195 0.4980 -0.0136 0.0267  -0.0133 102 LYS   B NZ  
5413 N N   A GLY   B 103 ? 0.4112 0.3525 0.2953 0.0273  0.0213  0.0653  103 GLY   B N   
5414 N N   B GLY   B 103 ? 0.4150 0.3438 0.2623 0.0192  0.0357  0.1042  103 GLY   B N   
5415 C CA  A GLY   B 103 ? 0.3989 0.3489 0.2973 0.0273  0.0321  0.0585  103 GLY   B CA  
5416 C CA  B GLY   B 103 ? 0.3997 0.3360 0.2627 0.0161  0.0559  0.1002  103 GLY   B CA  
5417 C C   A GLY   B 103 ? 0.3843 0.3430 0.2924 0.0260  0.0413  0.0482  103 GLY   B C   
5418 C C   B GLY   B 103 ? 0.3799 0.3251 0.2483 0.0101  0.0769  0.0901  103 GLY   B C   
5419 O O   A GLY   B 103 ? 0.3854 0.3468 0.2976 0.0239  0.0419  0.0484  103 GLY   B O   
5420 O O   B GLY   B 103 ? 0.3824 0.3327 0.2592 0.0087  0.0788  0.0854  103 GLY   B O   
5427 N N   A GLU   B 104 ? 0.3675 0.3317 0.2808 0.0261  0.0479  0.0333  104 GLU   B N   
5428 N N   B GLU   B 104 ? 0.3553 0.3032 0.2164 0.0052  0.0927  0.0776  104 GLU   B N   
5429 C CA  A GLU   B 104 ? 0.3503 0.3214 0.2689 0.0277  0.0482  0.0158  104 GLU   B CA  
5430 C CA  B GLU   B 104 ? 0.3310 0.2842 0.1885 0.0052  0.0927  0.0538  104 GLU   B CA  
5431 C C   A GLU   B 104 ? 0.3473 0.3177 0.2786 0.0200  0.0599  0.0095  104 GLU   B C   
5432 C C   B GLU   B 104 ? 0.3299 0.2788 0.1974 -0.0033 0.1058  0.0447  104 GLU   B C   
5433 O O   A GLU   B 104 ? 0.3468 0.3166 0.2899 0.0202  0.0568  0.0043  104 GLU   B O   
5434 O O   B GLU   B 104 ? 0.3333 0.2797 0.2422 -0.0004 0.0917  0.0354  104 GLU   B O   
5435 C CB  A GLU   B 104 ? 0.3387 0.3143 0.2552 0.0348  0.0325  0.0029  104 GLU   B CB  
5436 C CB  B GLU   B 104 ? 0.3151 0.2685 0.1758 0.0109  0.0610  0.0349  104 GLU   B CB  
5437 C CG  A GLU   B 104 ? 0.3290 0.3080 0.2434 0.0407  0.0155  -0.0113 104 GLU   B CG  
5438 C CG  B GLU   B 104 ? 0.3038 0.2556 0.1604 0.0174  0.0247  0.0089  104 GLU   B CG  
5439 C CD  A GLU   B 104 ? 0.3193 0.3005 0.2373 0.0470  0.0001  -0.0185 104 GLU   B CD  
5440 C CD  B GLU   B 104 ? 0.2918 0.2377 0.1407 0.0207  -0.0060 0.0041  104 GLU   B CD  
5441 O OE1 A GLU   B 104 ? 0.3085 0.2932 0.2241 0.0525  0.0054  -0.0193 104 GLU   B OE1 
5442 O OE1 B GLU   B 104 ? 0.2701 0.2162 0.1303 0.0260  0.0013  0.0092  104 GLU   B OE1 
5443 O OE2 A GLU   B 104 ? 0.3222 0.3046 0.2526 0.0467  -0.0157 -0.0226 104 GLU   B OE2 
5444 O OE2 B GLU   B 104 ? 0.3009 0.2494 0.1465 0.0140  -0.0328 -0.0008 104 GLU   B OE2 
5457 N N   A ASP   B 105 ? 0.3444 0.3173 0.2887 0.0110  0.0715  0.0108  105 ASP   B N   
5458 N N   B ASP   B 105 ? 0.3239 0.2767 0.1989 -0.0169 0.1242  0.0445  105 ASP   B N   
5459 C CA  A ASP   B 105 ? 0.3438 0.3171 0.3059 0.0017  0.0836  0.0075  105 ASP   B CA  
5460 C CA  B ASP   B 105 ? 0.3220 0.2754 0.2236 -0.0299 0.1396  0.0314  105 ASP   B CA  
5461 C C   A ASP   B 105 ? 0.3345 0.3021 0.2878 -0.0022 0.0839  0.0041  105 ASP   B C   
5462 C C   B ASP   B 105 ? 0.3080 0.2460 0.2106 -0.0429 0.1284  0.0228  105 ASP   B C   
5463 O O   A ASP   B 105 ? 0.3321 0.2996 0.2847 -0.0001 0.0865  0.0035  105 ASP   B O   
5464 O O   B ASP   B 105 ? 0.2953 0.2369 0.2026 -0.0428 0.1233  0.0181  105 ASP   B O   
5465 C CB  A ASP   B 105 ? 0.3514 0.3289 0.3447 0.0001  0.0928  0.0045  105 ASP   B CB  
5466 C CB  B ASP   B 105 ? 0.3323 0.2992 0.2741 -0.0234 0.1555  0.0217  105 ASP   B CB  
5467 C CG  A ASP   B 105 ? 0.3551 0.3356 0.3796 -0.0032 0.0994  0.0031  105 ASP   B CG  
5468 C CG  B ASP   B 105 ? 0.3351 0.3126 0.3156 -0.0252 0.1685  0.0185  105 ASP   B CG  
5469 O OD1 A ASP   B 105 ? 0.3547 0.3399 0.3912 -0.0061 0.0991  0.0019  105 ASP   B OD1 
5470 O OD1 B ASP   B 105 ? 0.3336 0.3188 0.3307 -0.0293 0.1702  0.0175  105 ASP   B OD1 
5471 O OD2 A ASP   B 105 ? 0.3570 0.3363 0.3987 -0.0028 0.0999  0.0033  105 ASP   B OD2 
5472 O OD2 B ASP   B 105 ? 0.3337 0.3171 0.3369 -0.0271 0.1753  0.0199  105 ASP   B OD2 
5481 N N   A ILE   B 106 ? 0.3286 0.2900 0.2862 -0.0033 0.0769  0.0037  106 ILE   B N   
5482 N N   B ILE   B 106 ? 0.3082 0.2289 0.2258 -0.0462 0.1101  0.0183  106 ILE   B N   
5483 C CA  A ILE   B 106 ? 0.3181 0.2776 0.2831 -0.0041 0.0771  0.0030  106 ILE   B CA  
5484 C CA  B ILE   B 106 ? 0.2969 0.2122 0.2347 -0.0542 0.1116  0.0149  106 ILE   B CA  
5485 C C   A ILE   B 106 ? 0.2980 0.2730 0.2777 -0.0013 0.0752  -0.0051 106 ILE   B C   
5486 C C   B ILE   B 106 ? 0.2666 0.2135 0.2313 -0.0556 0.1107  -0.0067 106 ILE   B C   
5487 O O   A ILE   B 106 ? 0.2947 0.2662 0.2734 0.0019  0.0734  -0.0052 106 ILE   B O   
5488 O O   B ILE   B 106 ? 0.2569 0.1967 0.2158 -0.0601 0.1027  -0.0137 106 ILE   B O   
5489 C CB  A ILE   B 106 ? 0.3278 0.2741 0.2895 -0.0074 0.0754  0.0069  106 ILE   B CB  
5490 C CB  B ILE   B 106 ? 0.3189 0.2094 0.2629 -0.0530 0.1035  0.0213  106 ILE   B CB  
5491 C CG1 A ILE   B 106 ? 0.3318 0.2725 0.2905 -0.0064 0.0754  0.0055  106 ILE   B CG1 
5492 C CG1 B ILE   B 106 ? 0.3295 0.2128 0.2744 -0.0415 0.0982  0.0120  106 ILE   B CG1 
5493 C CG2 A ILE   B 106 ? 0.3309 0.2751 0.3006 -0.0098 0.0747  0.0086  106 ILE   B CG2 
5494 C CG2 B ILE   B 106 ? 0.3241 0.2114 0.2845 -0.0585 0.1029  0.0278  106 ILE   B CG2 
5495 C CD1 A ILE   B 106 ? 0.3343 0.2724 0.2876 -0.0042 0.0762  0.0067  106 ILE   B CD1 
5496 C CD1 B ILE   B 106 ? 0.3356 0.2168 0.2744 -0.0317 0.0983  0.0122  106 ILE   B CD1 
5519 N N   A GLN   B 107 ? 0.2835 0.2780 0.2879 -0.0041 0.0702  -0.0074 107 GLN   B N   
5520 N N   B GLN   B 107 ? 0.2556 0.2386 0.2563 -0.0490 0.1058  -0.0088 107 GLN   B N   
5521 C CA  A GLN   B 107 ? 0.2688 0.2800 0.3030 -0.0051 0.0660  -0.0068 107 GLN   B CA  
5522 C CA  B GLN   B 107 ? 0.2447 0.2609 0.2851 -0.0373 0.1057  -0.0060 107 GLN   B CA  
5523 C C   A GLN   B 107 ? 0.2404 0.2569 0.2736 0.0012  0.0600  -0.0101 107 GLN   B C   
5524 C C   B GLN   B 107 ? 0.2272 0.2481 0.2683 -0.0164 0.0798  -0.0111 107 GLN   B C   
5525 O O   A GLN   B 107 ? 0.2402 0.2563 0.2888 0.0074  0.0485  -0.0117 107 GLN   B O   
5526 O O   B GLN   B 107 ? 0.2276 0.2495 0.2972 -0.0076 0.0613  -0.0204 107 GLN   B O   
5527 C CB  A GLN   B 107 ? 0.2883 0.3035 0.3554 -0.0085 0.0586  -0.0041 107 GLN   B CB  
5528 C CB  B GLN   B 107 ? 0.2697 0.2952 0.3490 -0.0351 0.1014  -0.0027 107 GLN   B CB  
5529 C CG  A GLN   B 107 ? 0.3078 0.3231 0.4118 -0.0078 0.0426  -0.0026 107 GLN   B CG  
5530 C CG  B GLN   B 107 ? 0.3004 0.3247 0.4227 -0.0258 0.0737  -0.0041 107 GLN   B CG  
5531 C CD  A GLN   B 107 ? 0.3221 0.3362 0.4568 -0.0079 0.0297  -0.0018 107 GLN   B CD  
5532 C CD  B GLN   B 107 ? 0.3236 0.3440 0.4794 -0.0198 0.0513  -0.0053 107 GLN   B CD  
5533 O OE1 A GLN   B 107 ? 0.3267 0.3424 0.4747 -0.0041 0.0263  -0.0040 107 GLN   B OE1 
5534 O OE1 B GLN   B 107 ? 0.3313 0.3520 0.5009 -0.0132 0.0454  -0.0076 107 GLN   B OE1 
5535 N NE2 A GLN   B 107 ? 0.3294 0.3394 0.4733 -0.0087 0.0251  0.0023  107 GLN   B NE2 
5536 N NE2 B GLN   B 107 ? 0.3365 0.3502 0.5011 -0.0185 0.0433  -0.0021 107 GLN   B NE2 
5553 N N   . LEU   B 108 ? 0.2120 0.2345 0.2367 0.0063  0.0636  -0.0103 108 LEU   B N   
5554 C CA  . LEU   B 108 ? 0.1988 0.2095 0.1951 0.0223  0.0432  0.0043  108 LEU   B CA  
5555 C C   . LEU   B 108 ? 0.1761 0.1748 0.1948 0.0219  0.0254  0.0201  108 LEU   B C   
5556 O O   . LEU   B 108 ? 0.1818 0.1656 0.1893 0.0199  0.0184  0.0210  108 LEU   B O   
5557 C CB  . LEU   B 108 ? 0.2138 0.2263 0.1701 0.0214  0.0523  0.0121  108 LEU   B CB  
5558 C CG  . LEU   B 108 ? 0.2385 0.2574 0.1892 0.0185  0.0404  -0.0095 108 LEU   B CG  
5559 C CD1 . LEU   B 108 ? 0.2465 0.2728 0.1885 0.0085  0.0329  -0.0040 108 LEU   B CD1 
5560 C CD2 . LEU   B 108 ? 0.2585 0.2730 0.2149 0.0244  0.0277  -0.0278 108 LEU   B CD2 
5573 N N   . LEU   B 109 ? 0.1657 0.1589 0.1885 0.0176  0.0316  0.0175  109 LEU   B N   
5574 C CA  . LEU   B 109 ? 0.1496 0.1367 0.2021 0.0101  0.0279  0.0204  109 LEU   B CA  
5575 C C   . LEU   B 109 ? 0.1378 0.1214 0.1986 0.0064  0.0301  0.0197  109 LEU   B C   
5576 O O   . LEU   B 109 ? 0.1344 0.1188 0.1951 0.0074  0.0274  0.0229  109 LEU   B O   
5577 C CB  . LEU   B 109 ? 0.1531 0.1309 0.1979 0.0045  0.0223  0.0249  109 LEU   B CB  
5578 C CG  . LEU   B 109 ? 0.1542 0.1286 0.1928 0.0059  0.0186  0.0171  109 LEU   B CG  
5579 C CD1 . LEU   B 109 ? 0.1489 0.1441 0.1849 0.0087  0.0232  0.0243  109 LEU   B CD1 
5580 C CD2 . LEU   B 109 ? 0.1710 0.1390 0.2071 0.0077  0.0089  0.0167  109 LEU   B CD2 
5592 N N   . LYS   B 110 ? 0.1346 0.1227 0.1920 0.0027  0.0247  0.0208  110 LYS   B N   
5593 C CA  . LYS   B 110 ? 0.1308 0.1176 0.1902 0.0002  0.0207  0.0145  110 LYS   B CA  
5594 C C   . LYS   B 110 ? 0.1273 0.1229 0.1737 0.0019  0.0184  0.0098  110 LYS   B C   
5595 O O   . LYS   B 110 ? 0.1281 0.1304 0.1638 -0.0007 0.0141  0.0046  110 LYS   B O   
5596 C CB  . LYS   B 110 ? 0.1334 0.1223 0.2178 -0.0029 0.0295  0.0034  110 LYS   B CB  
5597 C CG  . LYS   B 110 ? 0.1318 0.1242 0.2248 -0.0013 0.0165  0.0107  110 LYS   B CG  
5598 C CD  . LYS   B 110 ? 0.1399 0.1239 0.2347 -0.0031 0.0198  0.0097  110 LYS   B CD  
5599 C CE  . LYS   B 110 ? 0.1363 0.1378 0.2505 -0.0002 0.0154  0.0046  110 LYS   B CE  
5600 N NZ  . LYS   B 110 ? 0.1340 0.1527 0.2416 -0.0033 0.0053  -0.0033 110 LYS   B NZ  
5614 N N   . SER   B 111 ? 0.1342 0.1239 0.1810 -0.0049 0.0250  0.0121  111 SER   B N   
5615 C CA  . SER   B 111 ? 0.1379 0.1300 0.1793 0.0032  0.0177  0.0162  111 SER   B CA  
5616 C C   . SER   B 111 ? 0.1287 0.1240 0.1673 0.0019  0.0110  0.0093  111 SER   B C   
5617 O O   . SER   B 111 ? 0.1280 0.1264 0.1772 0.0005  0.0078  0.0090  111 SER   B O   
5618 C CB  . SER   B 111 ? 0.1529 0.1521 0.1960 0.0029  0.0344  0.0156  111 SER   B CB  
5619 O OG  . SER   B 111 ? 0.1686 0.1918 0.2041 0.0081  0.0366  0.0170  111 SER   B OG  
5625 N N   . ALA   B 112 ? 0.1246 0.1254 0.1750 0.0073  0.0141  0.0152  112 ALA   B N   
5626 C CA  . ALA   B 112 ? 0.1229 0.1327 0.1567 0.0051  0.0065  0.0005  112 ALA   B CA  
5627 C C   . ALA   B 112 ? 0.1178 0.1255 0.1546 0.0030  0.0063  0.0015  112 ALA   B C   
5628 O O   . ALA   B 112 ? 0.1189 0.1234 0.1605 -0.0048 0.0061  -0.0043 112 ALA   B O   
5629 C CB  . ALA   B 112 ? 0.1259 0.1398 0.1737 0.0113  0.0074  0.0164  112 ALA   B CB  
5635 N N   . TYR   B 113 ? 0.1156 0.1115 0.1629 -0.0012 0.0064  0.0040  113 TYR   B N   
5636 C CA  . TYR   B 113 ? 0.1091 0.1110 0.1623 -0.0010 0.0070  -0.0011 113 TYR   B CA  
5637 C C   . TYR   B 113 ? 0.1129 0.1076 0.1634 -0.0070 -0.0017 0.0038  113 TYR   B C   
5638 O O   . TYR   B 113 ? 0.1167 0.1096 0.1569 -0.0034 0.0035  -0.0056 113 TYR   B O   
5639 C CB  . TYR   B 113 ? 0.1180 0.1100 0.1681 -0.0071 0.0116  0.0062  113 TYR   B CB  
5640 C CG  . TYR   B 113 ? 0.1196 0.1102 0.1782 -0.0036 0.0159  0.0042  113 TYR   B CG  
5641 C CD1 . TYR   B 113 ? 0.1270 0.1154 0.1842 -0.0018 0.0098  0.0164  113 TYR   B CD1 
5642 C CD2 . TYR   B 113 ? 0.1295 0.1079 0.1790 -0.0016 0.0143  0.0087  113 TYR   B CD2 
5643 C CE1 . TYR   B 113 ? 0.1304 0.1182 0.1846 -0.0010 0.0221  0.0075  113 TYR   B CE1 
5644 C CE2 . TYR   B 113 ? 0.1304 0.1059 0.1901 0.0018  0.0114  0.0184  113 TYR   B CE2 
5645 C CZ  . TYR   B 113 ? 0.1231 0.1125 0.1886 0.0046  0.0104  0.0089  113 TYR   B CZ  
5646 O OH  . TYR   B 113 ? 0.1300 0.1126 0.2073 0.0094  0.0128  0.0054  113 TYR   B OH  
5656 N N   . GLU   B 114 ? 0.1127 0.1039 0.1702 -0.0012 0.0087  0.0054  114 GLU   B N   
5657 C CA  . GLU   B 114 ? 0.1101 0.1054 0.1722 0.0039  0.0083  -0.0036 114 GLU   B CA  
5658 C C   . GLU   B 114 ? 0.1109 0.1101 0.1595 -0.0037 0.0078  -0.0046 114 GLU   B C   
5659 O O   . GLU   B 114 ? 0.1122 0.1080 0.1687 0.0014  0.0023  -0.0004 114 GLU   B O   
5660 C CB  . GLU   B 114 ? 0.1095 0.1151 0.1720 -0.0026 0.0076  0.0035  114 GLU   B CB  
5661 C CG  . GLU   B 114 ? 0.1172 0.1153 0.1745 0.0026  0.0129  0.0029  114 GLU   B CG  
5662 C CD  . GLU   B 114 ? 0.1148 0.1174 0.1761 -0.0030 0.0062  0.0047  114 GLU   B CD  
5663 O OE1 . GLU   B 114 ? 0.1115 0.1290 0.1711 -0.0066 0.0158  0.0080  114 GLU   B OE1 
5664 O OE2 . GLU   B 114 ? 0.1199 0.1349 0.1901 -0.0164 0.0136  0.0048  114 GLU   B OE2 
5671 N N   . ASN   B 115 ? 0.1159 0.1057 0.1585 -0.0026 0.0029  -0.0020 115 ASN   B N   
5672 C CA  . ASN   B 115 ? 0.1153 0.1108 0.1485 -0.0067 -0.0011 0.0051  115 ASN   B CA  
5673 C C   . ASN   B 115 ? 0.1131 0.1052 0.1413 -0.0058 0.0012  -0.0052 115 ASN   B C   
5674 O O   . ASN   B 115 ? 0.1244 0.1070 0.1540 -0.0069 0.0022  -0.0008 115 ASN   B O   
5675 C CB  . ASN   B 115 ? 0.1216 0.1191 0.1540 -0.0093 0.0017  0.0040  115 ASN   B CB  
5676 C CG  . ASN   B 115 ? 0.1337 0.1258 0.1549 0.0003  -0.0044 -0.0020 115 ASN   B CG  
5677 O OD1 . ASN   B 115 ? 0.1703 0.1388 0.1693 -0.0005 0.0095  -0.0110 115 ASN   B OD1 
5678 N ND2 . ASN   B 115 ? 0.1330 0.1336 0.1537 -0.0035 -0.0031 -0.0046 115 ASN   B ND2 
5685 N N   . PHE   B 116 ? 0.1137 0.1107 0.1361 -0.0056 -0.0005 0.0040  116 PHE   B N   
5686 C CA  . PHE   B 116 ? 0.1198 0.1088 0.1461 -0.0081 -0.0013 0.0001  116 PHE   B CA  
5687 C C   . PHE   B 116 ? 0.1198 0.1006 0.1470 -0.0083 0.0007  0.0036  116 PHE   B C   
5688 O O   . PHE   B 116 ? 0.1237 0.1092 0.1495 -0.0034 0.0004  0.0049  116 PHE   B O   
5689 C CB  . PHE   B 116 ? 0.1164 0.1118 0.1484 -0.0092 -0.0121 -0.0008 116 PHE   B CB  
5690 C CG  . PHE   B 116 ? 0.1120 0.1036 0.1537 -0.0056 -0.0019 -0.0029 116 PHE   B CG  
5691 C CD1 . PHE   B 116 ? 0.1219 0.1110 0.1711 -0.0066 -0.0053 0.0020  116 PHE   B CD1 
5692 C CD2 . PHE   B 116 ? 0.1183 0.1114 0.1429 -0.0043 0.0004  -0.0043 116 PHE   B CD2 
5693 C CE1 . PHE   B 116 ? 0.1215 0.1187 0.1737 -0.0060 -0.0129 -0.0008 116 PHE   B CE1 
5694 C CE2 . PHE   B 116 ? 0.1175 0.1103 0.1570 -0.0012 0.0053  -0.0021 116 PHE   B CE2 
5695 C CZ  . PHE   B 116 ? 0.1115 0.1162 0.1652 -0.0062 -0.0044 -0.0025 116 PHE   B CZ  
5705 N N   . ASN   B 117 ? 0.1158 0.1076 0.1583 -0.0030 -0.0040 0.0007  117 ASN   B N   
5706 C CA  . ASN   B 117 ? 0.1184 0.1121 0.1568 0.0034  -0.0031 0.0010  117 ASN   B CA  
5707 C C   . ASN   B 117 ? 0.1203 0.1071 0.1824 -0.0006 -0.0043 -0.0041 117 ASN   B C   
5708 O O   . ASN   B 117 ? 0.1357 0.1114 0.2081 -0.0032 -0.0221 0.0107  117 ASN   B O   
5709 C CB  . ASN   B 117 ? 0.1215 0.1127 0.1547 0.0014  -0.0012 -0.0043 117 ASN   B CB  
5710 C CG  . ASN   B 117 ? 0.1156 0.1107 0.1664 0.0046  0.0022  -0.0059 117 ASN   B CG  
5711 O OD1 . ASN   B 117 ? 0.1412 0.1119 0.1675 -0.0110 0.0037  -0.0018 117 ASN   B OD1 
5712 N ND2 . ASN   B 117 ? 0.1199 0.1141 0.1619 -0.0003 0.0069  -0.0049 117 ASN   B ND2 
5719 N N   . GLN   B 118 ? 0.1231 0.1002 0.1709 -0.0063 -0.0073 -0.0005 118 GLN   B N   
5720 C CA  . GLN   B 118 ? 0.1338 0.1086 0.1774 0.0015  -0.0049 -0.0042 118 GLN   B CA  
5721 C C   . GLN   B 118 ? 0.1362 0.1074 0.1816 -0.0000 -0.0060 -0.0041 118 GLN   B C   
5722 O O   . GLN   B 118 ? 0.1542 0.1044 0.2138 -0.0061 0.0045  0.0016  118 GLN   B O   
5723 C CB  . GLN   B 118 ? 0.1363 0.1090 0.1893 0.0016  -0.0087 -0.0045 118 GLN   B CB  
5724 C CG  . GLN   B 118 ? 0.1462 0.1135 0.1788 0.0067  -0.0078 -0.0124 118 GLN   B CG  
5725 C CD  . GLN   B 118 ? 0.1466 0.1128 0.1814 0.0008  -0.0031 -0.0144 118 GLN   B CD  
5726 O OE1 . GLN   B 118 ? 0.1538 0.1104 0.1905 0.0073  0.0068  -0.0004 118 GLN   B OE1 
5727 N NE2 . GLN   B 118 ? 0.1521 0.1109 0.1908 -0.0018 -0.0036 -0.0010 118 GLN   B NE2 
5736 N N   . HIS   B 119 ? 0.1348 0.1090 0.1457 -0.0057 -0.0072 0.0042  119 HIS   B N   
5737 C CA  . HIS   B 119 ? 0.1379 0.1231 0.1477 -0.0025 -0.0086 0.0031  119 HIS   B CA  
5738 C C   . HIS   B 119 ? 0.1390 0.1227 0.1579 -0.0023 -0.0135 0.0059  119 HIS   B C   
5739 O O   . HIS   B 119 ? 0.1466 0.1246 0.1641 -0.0257 -0.0107 0.0071  119 HIS   B O   
5740 C CB  . HIS   B 119 ? 0.1430 0.1367 0.1550 -0.0003 -0.0111 -0.0002 119 HIS   B CB  
5741 C CG  . HIS   B 119 ? 0.1486 0.1621 0.1790 0.0107  -0.0275 -0.0249 119 HIS   B CG  
5742 N ND1 . HIS   B 119 ? 0.1613 0.1784 0.2010 0.0064  -0.0458 -0.0396 119 HIS   B ND1 
5743 C CD2 . HIS   B 119 ? 0.1661 0.1742 0.1931 0.0359  -0.0337 -0.0271 119 HIS   B CD2 
5744 C CE1 . HIS   B 119 ? 0.1835 0.1928 0.2122 0.0180  -0.0494 -0.0525 119 HIS   B CE1 
5745 N NE2 . HIS   B 119 ? 0.1854 0.1979 0.2050 0.0303  -0.0412 -0.0414 119 HIS   B NE2 
5753 N N   . GLU   B 120 ? 0.1535 0.1236 0.1615 -0.0065 -0.0211 0.0097  120 GLU   B N   
5754 C CA  . GLU   B 120 ? 0.1786 0.1396 0.1716 -0.0005 -0.0380 0.0203  120 GLU   B CA  
5755 C C   . GLU   B 120 ? 0.1630 0.1300 0.1496 -0.0081 -0.0264 0.0177  120 GLU   B C   
5756 O O   . GLU   B 120 ? 0.1615 0.1379 0.1468 -0.0109 -0.0273 0.0113  120 GLU   B O   
5757 C CB  . GLU   B 120 ? 0.2390 0.1648 0.2294 0.0177  -0.0686 0.0425  120 GLU   B CB  
5758 C CG  . GLU   B 120 ? 0.2919 0.2199 0.3280 0.0313  -0.0843 0.0567  120 GLU   B CG  
5759 C CD  . GLU   B 120 ? 0.3268 0.2769 0.4237 0.0258  -0.0851 0.0667  120 GLU   B CD  
5760 O OE1 . GLU   B 120 ? 0.3443 0.3078 0.4562 0.0167  -0.0762 0.0729  120 GLU   B OE1 
5761 O OE2 . GLU   B 120 ? 0.3412 0.3362 0.4754 0.0229  -0.0820 0.0618  120 GLU   B OE2 
5768 N N   . VAL   B 121 ? 0.1573 0.1228 0.1438 -0.0152 -0.0163 0.0137  121 VAL   B N   
5769 C CA  . VAL   B 121 ? 0.1522 0.1372 0.1382 -0.0153 -0.0136 0.0097  121 VAL   B CA  
5770 C C   . VAL   B 121 ? 0.1435 0.1270 0.1348 -0.0188 -0.0124 0.0154  121 VAL   B C   
5771 O O   . VAL   B 121 ? 0.1483 0.1247 0.1450 -0.0258 -0.0160 -0.0007 121 VAL   B O   
5772 C CB  . VAL   B 121 ? 0.1704 0.1675 0.1444 -0.0022 -0.0175 0.0164  121 VAL   B CB  
5773 C CG1 . VAL   B 121 ? 0.1778 0.1788 0.1734 -0.0142 -0.0128 0.0144  121 VAL   B CG1 
5774 C CG2 . VAL   B 121 ? 0.1951 0.1845 0.1568 0.0116  -0.0177 0.0038  121 VAL   B CG2 
5784 N N   . LEU   B 122 ? 0.1374 0.1224 0.1287 -0.0158 -0.0150 0.0039  122 LEU   B N   
5785 C CA  . LEU   B 122 ? 0.1318 0.1299 0.1272 -0.0149 -0.0139 0.0052  122 LEU   B CA  
5786 C C   . LEU   B 122 ? 0.1327 0.1150 0.1319 -0.0207 -0.0169 0.0153  122 LEU   B C   
5787 O O   . LEU   B 122 ? 0.1406 0.1163 0.1616 -0.0274 -0.0197 -0.0017 122 LEU   B O   
5788 C CB  . LEU   B 122 ? 0.1516 0.1373 0.1635 -0.0032 -0.0189 0.0160  122 LEU   B CB  
5789 C CG  . LEU   B 122 ? 0.1445 0.1408 0.1640 -0.0115 -0.0016 0.0095  122 LEU   B CG  
5790 C CD1 . LEU   B 122 ? 0.1454 0.1609 0.1725 -0.0141 -0.0172 -0.0003 122 LEU   B CD1 
5791 C CD2 . LEU   B 122 ? 0.1444 0.1506 0.1370 -0.0047 0.0016  -0.0054 122 LEU   B CD2 
5803 N N   . LEU   B 123 ? 0.1324 0.1113 0.1217 -0.0216 -0.0102 0.0066  123 LEU   B N   
5804 C CA  . LEU   B 123 ? 0.1347 0.1086 0.1313 -0.0214 -0.0170 0.0010  123 LEU   B CA  
5805 C C   . LEU   B 123 ? 0.1306 0.1059 0.1369 -0.0202 -0.0137 -0.0036 123 LEU   B C   
5806 O O   . LEU   B 123 ? 0.1428 0.1138 0.1266 -0.0257 -0.0142 0.0004  123 LEU   B O   
5807 C CB  . LEU   B 123 ? 0.1368 0.1129 0.1418 -0.0218 -0.0104 -0.0069 123 LEU   B CB  
5808 C CG  . LEU   B 123 ? 0.1318 0.1196 0.1463 -0.0135 -0.0024 0.0045  123 LEU   B CG  
5809 C CD1 . LEU   B 123 ? 0.1409 0.1250 0.1511 -0.0100 0.0032  -0.0087 123 LEU   B CD1 
5810 C CD2 . LEU   B 123 ? 0.1409 0.1280 0.1664 -0.0118 0.0001  0.0185  123 LEU   B CD2 
5822 N N   . ALA   B 124 ? 0.1266 0.1120 0.1270 -0.0171 -0.0054 -0.0063 124 ALA   B N   
5823 C CA  . ALA   B 124 ? 0.1196 0.1109 0.1310 -0.0186 -0.0078 -0.0112 124 ALA   B CA  
5824 C C   . ALA   B 124 ? 0.1127 0.1147 0.1340 -0.0201 -0.0056 -0.0060 124 ALA   B C   
5825 O O   . ALA   B 124 ? 0.1299 0.1119 0.1350 -0.0093 -0.0090 -0.0036 124 ALA   B O   
5826 C CB  . ALA   B 124 ? 0.1302 0.1159 0.1408 -0.0062 0.0000  -0.0030 124 ALA   B CB  
5832 N N   . PRO   B 125 ? 0.1268 0.1134 0.1334 -0.0157 -0.0089 0.0013  125 PRO   B N   
5833 C CA  . PRO   B 125 ? 0.1372 0.1105 0.1485 -0.0142 -0.0121 0.0140  125 PRO   B CA  
5834 C C   . PRO   B 125 ? 0.1249 0.1127 0.1585 -0.0157 -0.0116 0.0115  125 PRO   B C   
5835 O O   . PRO   B 125 ? 0.1271 0.1078 0.1712 -0.0053 -0.0026 0.0075  125 PRO   B O   
5836 C CB  . PRO   B 125 ? 0.1382 0.1347 0.1574 -0.0210 -0.0158 0.0241  125 PRO   B CB  
5837 C CG  . PRO   B 125 ? 0.1405 0.1374 0.1536 -0.0287 -0.0172 0.0110  125 PRO   B CG  
5838 C CD  . PRO   B 125 ? 0.1349 0.1256 0.1352 -0.0224 -0.0069 0.0062  125 PRO   B CD  
5846 N N   . LEU   B 126 ? 0.1279 0.1066 0.1805 -0.0147 0.0051  0.0116  126 LEU   B N   
5847 C CA  . LEU   B 126 ? 0.1328 0.1160 0.1879 -0.0121 0.0139  0.0101  126 LEU   B CA  
5848 C C   . LEU   B 126 ? 0.1308 0.1272 0.1795 -0.0025 0.0139  0.0145  126 LEU   B C   
5849 O O   . LEU   B 126 ? 0.1524 0.1503 0.2041 0.0155  -0.0091 -0.0110 126 LEU   B O   
5850 C CB  . LEU   B 126 ? 0.1505 0.1197 0.2097 -0.0176 0.0249  0.0038  126 LEU   B CB  
5851 C CG  . LEU   B 126 ? 0.1681 0.1287 0.2244 -0.0263 0.0237  -0.0171 126 LEU   B CG  
5852 C CD1 . LEU   B 126 ? 0.1826 0.1393 0.2752 -0.0240 0.0250  -0.0214 126 LEU   B CD1 
5853 C CD2 . LEU   B 126 ? 0.1706 0.1393 0.2230 -0.0296 0.0192  -0.0173 126 LEU   B CD2 
5865 N N   . LEU   B 127 ? 0.1298 0.1157 0.1828 -0.0011 0.0133  0.0059  127 LEU   B N   
5866 C CA  . LEU   B 127 ? 0.1333 0.1204 0.1936 -0.0046 0.0168  0.0133  127 LEU   B CA  
5867 C C   . LEU   B 127 ? 0.1286 0.1170 0.1851 -0.0030 0.0132  0.0121  127 LEU   B C   
5868 O O   . LEU   B 127 ? 0.1337 0.1274 0.1823 -0.0148 -0.0005 0.0148  127 LEU   B O   
5869 C CB  . LEU   B 127 ? 0.1444 0.1208 0.1981 -0.0058 0.0174  0.0171  127 LEU   B CB  
5870 C CG  . LEU   B 127 ? 0.1529 0.1238 0.2004 0.0011  0.0233  0.0234  127 LEU   B CG  
5871 C CD1 . LEU   B 127 ? 0.1594 0.1232 0.2026 0.0054  0.0161  0.0136  127 LEU   B CD1 
5872 C CD2 . LEU   B 127 ? 0.1588 0.1267 0.2176 -0.0075 0.0179  0.0312  127 LEU   B CD2 
5884 N N   . SER   B 128 ? 0.1359 0.1199 0.1762 0.0019  -0.0028 0.0100  128 SER   B N   
5885 C CA  . SER   B 128 ? 0.1505 0.1242 0.1761 0.0095  -0.0045 0.0160  128 SER   B CA  
5886 C C   . SER   B 128 ? 0.1533 0.1291 0.2052 0.0111  -0.0142 0.0189  128 SER   B C   
5887 O O   . SER   B 128 ? 0.1674 0.1327 0.2460 0.0013  -0.0088 0.0331  128 SER   B O   
5888 C CB  . SER   B 128 ? 0.1624 0.1290 0.1765 0.0090  -0.0027 0.0261  128 SER   B CB  
5889 O OG  . SER   B 128 ? 0.1602 0.1415 0.1821 0.0150  0.0042  0.0220  128 SER   B OG  
5895 N N   . ALA   B 129 ? 0.1618 0.1345 0.2272 0.0280  -0.0123 0.0040  129 ALA   B N   
5896 C CA  . ALA   B 129 ? 0.1815 0.1439 0.2285 0.0283  -0.0068 -0.0011 129 ALA   B CA  
5897 C C   . ALA   B 129 ? 0.1682 0.1369 0.2139 0.0178  0.0094  0.0010  129 ALA   B C   
5898 O O   . ALA   B 129 ? 0.1573 0.1398 0.2215 0.0165  0.0014  0.0031  129 ALA   B O   
5899 C CB  . ALA   B 129 ? 0.2046 0.1681 0.2511 0.0293  -0.0021 -0.0083 129 ALA   B CB  
5905 N N   . GLY   B 130 ? 0.1675 0.1392 0.2217 0.0217  0.0104  0.0049  130 GLY   B N   
5906 C CA  . GLY   B 130 ? 0.1727 0.1499 0.2464 0.0221  0.0237  -0.0024 130 GLY   B CA  
5907 C C   . GLY   B 130 ? 0.1728 0.1500 0.2379 0.0183  0.0236  0.0038  130 GLY   B C   
5908 O O   . GLY   B 130 ? 0.1854 0.1575 0.2433 0.0185  0.0151  0.0088  130 GLY   B O   
5912 N N   . ILE   B 131 ? 0.1685 0.1585 0.2385 0.0298  0.0061  0.0078  131 ILE   B N   
5913 C CA  . ILE   B 131 ? 0.1854 0.1714 0.2381 0.0274  -0.0182 0.0213  131 ILE   B CA  
5914 C C   . ILE   B 131 ? 0.1972 0.1669 0.2147 0.0202  -0.0134 0.0227  131 ILE   B C   
5915 O O   . ILE   B 131 ? 0.2232 0.1839 0.2206 0.0228  -0.0320 0.0222  131 ILE   B O   
5916 C CB  . ILE   B 131 ? 0.1881 0.2016 0.2794 0.0185  -0.0234 0.0270  131 ILE   B CB  
5917 C CG1 . ILE   B 131 ? 0.1918 0.2150 0.2974 0.0023  -0.0101 0.0237  131 ILE   B CG1 
5918 C CG2 . ILE   B 131 ? 0.1850 0.2186 0.2963 0.0217  -0.0152 0.0221  131 ILE   B CG2 
5919 C CD1 . ILE   B 131 ? 0.2005 0.2286 0.3146 -0.0146 -0.0071 0.0246  131 ILE   B CD1 
5931 N N   . PHE   B 132 ? 0.1748 0.1456 0.1889 0.0136  0.0025  0.0267  132 PHE   B N   
5932 C CA  . PHE   B 132 ? 0.1837 0.1498 0.1896 0.0037  0.0229  0.0139  132 PHE   B CA  
5933 C C   . PHE   B 132 ? 0.2003 0.1660 0.1927 0.0069  0.0223  0.0181  132 PHE   B C   
5934 O O   . PHE   B 132 ? 0.2164 0.1890 0.2118 0.0007  0.0357  0.0212  132 PHE   B O   
5935 C CB  . PHE   B 132 ? 0.1733 0.1470 0.1842 0.0079  0.0274  0.0177  132 PHE   B CB  
5936 C CG  . PHE   B 132 ? 0.1701 0.1523 0.1769 0.0110  0.0218  0.0218  132 PHE   B CG  
5937 C CD1 . PHE   B 132 ? 0.1737 0.1557 0.2049 0.0051  0.0197  0.0240  132 PHE   B CD1 
5938 C CD2 . PHE   B 132 ? 0.1689 0.1567 0.1492 0.0175  0.0228  0.0284  132 PHE   B CD2 
5939 C CE1 . PHE   B 132 ? 0.1767 0.1637 0.2262 0.0075  0.0176  0.0291  132 PHE   B CE1 
5940 C CE2 . PHE   B 132 ? 0.1775 0.1599 0.1709 0.0176  0.0153  0.0216  132 PHE   B CE2 
5941 C CZ  . PHE   B 132 ? 0.1779 0.1664 0.2148 0.0087  0.0071  0.0312  132 PHE   B CZ  
5951 N N   . GLY   B 133 ? 0.1987 0.1560 0.1967 0.0036  0.0125  0.0337  133 GLY   B N   
5952 C CA  . GLY   B 133 ? 0.2052 0.1649 0.2183 -0.0117 0.0094  0.0306  133 GLY   B CA  
5953 C C   . GLY   B 133 ? 0.2123 0.1678 0.2238 -0.0207 0.0167  0.0338  133 GLY   B C   
5954 O O   . GLY   B 133 ? 0.2342 0.1752 0.2594 -0.0355 0.0195  0.0506  133 GLY   B O   
5958 N N   . ALA   B 134 ? 0.1948 0.1660 0.2090 -0.0217 0.0209  0.0289  134 ALA   B N   
5959 C CA  . ALA   B 134 ? 0.1909 0.1682 0.2202 -0.0168 0.0210  0.0122  134 ALA   B CA  
5960 C C   . ALA   B 134 ? 0.2000 0.1608 0.2193 -0.0098 0.0210  0.0179  134 ALA   B C   
5961 O O   . ALA   B 134 ? 0.2055 0.1819 0.2251 -0.0010 0.0234  0.0132  134 ALA   B O   
5962 C CB  . ALA   B 134 ? 0.1903 0.1731 0.2337 -0.0115 0.0137  0.0113  134 ALA   B CB  
5968 N N   . ASP   B 135 ? 0.2109 0.1489 0.2212 -0.0134 0.0070  0.0281  135 ASP   B N   
5969 C CA  . ASP   B 135 ? 0.2218 0.1436 0.2409 -0.0064 -0.0033 0.0315  135 ASP   B CA  
5970 C C   . ASP   B 135 ? 0.2009 0.1374 0.2181 -0.0004 0.0009  0.0220  135 ASP   B C   
5971 O O   . ASP   B 135 ? 0.1907 0.1345 0.2159 0.0004  0.0014  0.0220  135 ASP   B O   
5972 C CB  . ASP   B 135 ? 0.2505 0.1540 0.2774 -0.0249 -0.0080 0.0337  135 ASP   B CB  
5973 C CG  . ASP   B 135 ? 0.2804 0.1554 0.3130 -0.0451 -0.0088 0.0281  135 ASP   B CG  
5974 O OD1 . ASP   B 135 ? 0.2929 0.1409 0.3059 -0.0339 -0.0253 0.0271  135 ASP   B OD1 
5975 O OD2 . ASP   B 135 ? 0.2988 0.1865 0.3700 -0.0579 -0.0004 0.0145  135 ASP   B OD2 
5980 N N   . PRO   B 136 ? 0.1982 0.1412 0.2327 0.0156  -0.0091 0.0176  136 PRO   B N   
5981 C CA  . PRO   B 136 ? 0.1808 0.1329 0.2290 0.0156  -0.0142 0.0119  136 PRO   B CA  
5982 C C   . PRO   B 136 ? 0.1687 0.1238 0.2407 0.0118  -0.0061 0.0060  136 PRO   B C   
5983 O O   . PRO   B 136 ? 0.1542 0.1214 0.2224 0.0080  0.0063  0.0007  136 PRO   B O   
5984 C CB  . PRO   B 136 ? 0.1894 0.1595 0.2372 0.0252  -0.0256 -0.0040 136 PRO   B CB  
5985 C CG  . PRO   B 136 ? 0.2078 0.1664 0.2595 0.0314  -0.0179 0.0020  136 PRO   B CG  
5986 C CD  . PRO   B 136 ? 0.2073 0.1606 0.2591 0.0336  -0.0029 0.0074  136 PRO   B CD  
5994 N N   . ILE   B 137 ? 0.1776 0.1178 0.2484 0.0129  -0.0079 0.0040  137 ILE   B N   
5995 C CA  . ILE   B 137 ? 0.1814 0.1204 0.2589 0.0011  -0.0079 0.0027  137 ILE   B CA  
5996 C C   . ILE   B 137 ? 0.1660 0.1191 0.2495 -0.0077 0.0090  0.0143  137 ILE   B C   
5997 O O   . ILE   B 137 ? 0.1586 0.1223 0.2437 -0.0100 0.0095  0.0052  137 ILE   B O   
5998 C CB  . ILE   B 137 ? 0.2082 0.1269 0.2989 -0.0054 -0.0104 -0.0039 137 ILE   B CB  
5999 C CG1 . ILE   B 137 ? 0.2357 0.1409 0.3462 0.0055  0.0022  -0.0174 137 ILE   B CG1 
6000 C CG2 . ILE   B 137 ? 0.2153 0.1308 0.3103 -0.0302 -0.0112 -0.0016 137 ILE   B CG2 
6001 C CD1 . ILE   B 137 ? 0.2571 0.1656 0.3828 0.0246  0.0043  -0.0129 137 ILE   B CD1 
6013 N N   . HIS   B 138 ? 0.1734 0.1208 0.2433 -0.0036 0.0202  0.0122  138 HIS   B N   
6014 C CA  . HIS   B 138 ? 0.1916 0.1299 0.2387 -0.0015 0.0259  0.0222  138 HIS   B CA  
6015 C C   . HIS   B 138 ? 0.1731 0.1268 0.2253 -0.0022 0.0317  0.0253  138 HIS   B C   
6016 O O   . HIS   B 138 ? 0.1631 0.1326 0.2360 0.0041  0.0291  0.0322  138 HIS   B O   
6017 C CB  . HIS   B 138 ? 0.2175 0.1486 0.2457 -0.0080 0.0416  0.0160  138 HIS   B CB  
6018 C CG  . HIS   B 138 ? 0.2280 0.1644 0.2451 -0.0106 0.0602  0.0386  138 HIS   B CG  
6019 N ND1 . HIS   B 138 ? 0.2290 0.1779 0.2719 -0.0047 0.0698  0.0288  138 HIS   B ND1 
6020 C CD2 . HIS   B 138 ? 0.2409 0.1752 0.2441 -0.0091 0.0583  0.0304  138 HIS   B CD2 
6021 C CE1 . HIS   B 138 ? 0.2348 0.1785 0.2687 -0.0081 0.0665  0.0297  138 HIS   B CE1 
6022 N NE2 . HIS   B 138 ? 0.2441 0.1743 0.2567 -0.0024 0.0635  0.0214  138 HIS   B NE2 
6030 N N   . SER   B 139 ? 0.1674 0.1191 0.2285 0.0038  0.0247  0.0170  139 SER   B N   
6031 C CA  . SER   B 139 ? 0.1636 0.1145 0.2109 -0.0031 0.0197  0.0004  139 SER   B CA  
6032 C C   . SER   B 139 ? 0.1436 0.1089 0.2145 -0.0004 0.0147  -0.0015 139 SER   B C   
6033 O O   . SER   B 139 ? 0.1383 0.1053 0.2067 0.0024  0.0076  0.0047  139 SER   B O   
6034 C CB  . SER   B 139 ? 0.1674 0.1157 0.2074 -0.0018 0.0040  0.0014  139 SER   B CB  
6035 O OG  . SER   B 139 ? 0.1703 0.1130 0.2149 0.0014  -0.0099 0.0116  139 SER   B OG  
6041 N N   . LEU   B 140 ? 0.1355 0.1047 0.2034 -0.0035 0.0126  -0.0008 140 LEU   B N   
6042 C CA  . LEU   B 140 ? 0.1347 0.1085 0.2038 -0.0032 0.0092  0.0028  140 LEU   B CA  
6043 C C   . LEU   B 140 ? 0.1321 0.1081 0.2177 -0.0036 0.0052  -0.0070 140 LEU   B C   
6044 O O   . LEU   B 140 ? 0.1290 0.1111 0.2159 -0.0025 0.0014  0.0043  140 LEU   B O   
6045 C CB  . LEU   B 140 ? 0.1300 0.1074 0.2206 -0.0125 0.0104  -0.0081 140 LEU   B CB  
6046 C CG  . LEU   B 140 ? 0.1355 0.1118 0.2130 -0.0140 0.0003  0.0014  140 LEU   B CG  
6047 C CD1 . LEU   B 140 ? 0.1452 0.1228 0.2134 -0.0071 0.0046  0.0006  140 LEU   B CD1 
6048 C CD2 . LEU   B 140 ? 0.1578 0.1235 0.2135 -0.0133 -0.0007 -0.0103 140 LEU   B CD2 
6060 N N   . ARG   B 141 ? 0.1261 0.1054 0.2237 -0.0120 0.0041  -0.0060 141 ARG   B N   
6061 C CA  . ARG   B 141 ? 0.1308 0.1101 0.2715 -0.0154 0.0195  -0.0024 141 ARG   B CA  
6062 C C   . ARG   B 141 ? 0.1250 0.1102 0.2593 -0.0156 0.0120  -0.0027 141 ARG   B C   
6063 O O   . ARG   B 141 ? 0.1278 0.1114 0.2490 -0.0122 0.0034  -0.0079 141 ARG   B O   
6064 C CB  . ARG   B 141 ? 0.1462 0.1239 0.3011 -0.0165 0.0319  -0.0074 141 ARG   B CB  
6065 C CG  . ARG   B 141 ? 0.1771 0.1532 0.3223 -0.0147 0.0332  -0.0004 141 ARG   B CG  
6066 C CD  . ARG   B 141 ? 0.2191 0.1727 0.3323 -0.0131 0.0188  -0.0099 141 ARG   B CD  
6067 N NE  . ARG   B 141 ? 0.2366 0.1740 0.3278 -0.0400 0.0212  -0.0128 141 ARG   B NE  
6068 C CZ  . ARG   B 141 ? 0.2450 0.1598 0.3172 -0.0405 0.0301  -0.0259 141 ARG   B CZ  
6069 N NH1 . ARG   B 141 ? 0.2641 0.1467 0.3121 -0.0345 0.0231  -0.0315 141 ARG   B NH1 
6070 N NH2 . ARG   B 141 ? 0.2511 0.1762 0.3215 -0.0267 0.0188  -0.0243 141 ARG   B NH2 
6084 N N   . VAL   B 142 ? 0.1261 0.1064 0.2429 -0.0080 0.0130  -0.0039 142 VAL   B N   
6085 C CA  . VAL   B 142 ? 0.1233 0.1114 0.2249 -0.0052 0.0156  -0.0068 142 VAL   B CA  
6086 C C   . VAL   B 142 ? 0.1223 0.1107 0.2193 -0.0054 0.0080  -0.0051 142 VAL   B C   
6087 O O   . VAL   B 142 ? 0.1284 0.1091 0.2339 0.0004  0.0104  0.0011  142 VAL   B O   
6088 C CB  . VAL   B 142 ? 0.1327 0.1208 0.2218 -0.0021 0.0157  0.0060  142 VAL   B CB  
6089 C CG1 . VAL   B 142 ? 0.1393 0.1183 0.2212 0.0045  0.0179  -0.0014 142 VAL   B CG1 
6090 C CG2 . VAL   B 142 ? 0.1476 0.1290 0.2391 -0.0015 0.0180  0.0071  142 VAL   B CG2 
6100 N N   . CYS   B 143 ? 0.1247 0.1124 0.2164 -0.0051 0.0124  0.0050  143 CYS   B N   
6101 C CA  . CYS   B 143 ? 0.1215 0.1070 0.2183 -0.0091 -0.0005 0.0037  143 CYS   B CA  
6102 C C   . CYS   B 143 ? 0.1178 0.1071 0.2144 -0.0074 0.0014  -0.0039 143 CYS   B C   
6103 O O   . CYS   B 143 ? 0.1285 0.1120 0.2074 -0.0050 0.0013  -0.0022 143 CYS   B O   
6104 C CB  . CYS   B 143 ? 0.1266 0.1145 0.2136 -0.0059 0.0060  -0.0010 143 CYS   B CB  
6105 S SG  . CYS   B 143 ? 0.1278 0.1313 0.2149 -0.0041 0.0080  0.0030  143 CYS   B SG  
6111 N N   . VAL   B 144 ? 0.1232 0.1123 0.2248 -0.0079 -0.0031 -0.0094 144 VAL   B N   
6112 C CA  . VAL   B 144 ? 0.1288 0.1181 0.2376 -0.0103 -0.0098 -0.0174 144 VAL   B CA  
6113 C C   . VAL   B 144 ? 0.1289 0.1260 0.2445 -0.0080 -0.0097 0.0009  144 VAL   B C   
6114 O O   . VAL   B 144 ? 0.1375 0.1426 0.2727 0.0005  -0.0050 0.0159  144 VAL   B O   
6115 C CB  . VAL   B 144 ? 0.1537 0.1398 0.2932 -0.0132 -0.0154 -0.0309 144 VAL   B CB  
6116 C CG1 . VAL   B 144 ? 0.1801 0.1740 0.3075 -0.0044 -0.0182 -0.0335 144 VAL   B CG1 
6117 C CG2 . VAL   B 144 ? 0.1693 0.1399 0.2821 -0.0028 -0.0240 -0.0387 144 VAL   B CG2 
6127 N N   . ASP   B 145 ? 0.1270 0.1157 0.2473 -0.0051 -0.0041 -0.0160 145 ASP   B N   
6128 C CA  . ASP   B 145 ? 0.1251 0.1221 0.2663 -0.0075 0.0041  -0.0114 145 ASP   B CA  
6129 C C   . ASP   B 145 ? 0.1208 0.1220 0.2544 -0.0034 0.0074  -0.0102 145 ASP   B C   
6130 O O   . ASP   B 145 ? 0.1247 0.1390 0.3044 -0.0119 0.0111  -0.0271 145 ASP   B O   
6131 C CB  . ASP   B 145 ? 0.1397 0.1321 0.2995 -0.0146 0.0236  -0.0080 145 ASP   B CB  
6132 C CG  . ASP   B 145 ? 0.1548 0.1344 0.3345 -0.0260 0.0283  -0.0100 145 ASP   B CG  
6133 O OD1 . ASP   B 145 ? 0.1596 0.1352 0.3479 -0.0218 -0.0019 -0.0183 145 ASP   B OD1 
6134 O OD2 . ASP   B 145 ? 0.1884 0.1455 0.3750 -0.0297 0.0552  -0.0029 145 ASP   B OD2 
6139 N N   . THR   B 146 ? 0.1179 0.1144 0.2149 -0.0068 0.0003  -0.0000 146 THR   B N   
6140 C CA  . THR   B 146 ? 0.1242 0.1136 0.1946 -0.0081 0.0101  -0.0021 146 THR   B CA  
6141 C C   . THR   B 146 ? 0.1253 0.1107 0.1927 -0.0015 0.0055  -0.0002 146 THR   B C   
6142 O O   . THR   B 146 ? 0.1307 0.1102 0.2027 -0.0017 0.0080  -0.0018 146 THR   B O   
6143 C CB  . THR   B 146 ? 0.1300 0.1132 0.1963 -0.0023 0.0163  -0.0040 146 THR   B CB  
6144 O OG1 . THR   B 146 ? 0.1327 0.1132 0.1990 -0.0063 0.0179  0.0072  146 THR   B OG1 
6145 C CG2 . THR   B 146 ? 0.1369 0.1203 0.1934 -0.0014 0.0142  -0.0043 146 THR   B CG2 
6153 N N   . VAL   B 147 ? 0.1287 0.1154 0.1865 -0.0052 0.0120  0.0009  147 VAL   B N   
6154 C CA  . VAL   B 147 ? 0.1297 0.1082 0.1833 -0.0081 -0.0049 -0.0026 147 VAL   B CA  
6155 C C   . VAL   B 147 ? 0.1237 0.1115 0.1963 -0.0140 -0.0017 -0.0048 147 VAL   B C   
6156 O O   . VAL   B 147 ? 0.1359 0.1227 0.2030 -0.0188 -0.0230 -0.0164 147 VAL   B O   
6157 C CB  . VAL   B 147 ? 0.1290 0.1232 0.1690 -0.0117 -0.0040 -0.0002 147 VAL   B CB  
6158 C CG1 . VAL   B 147 ? 0.1287 0.1415 0.1611 -0.0179 -0.0043 -0.0000 147 VAL   B CG1 
6159 C CG2 . VAL   B 147 ? 0.1286 0.1266 0.1735 -0.0113 0.0051  0.0029  147 VAL   B CG2 
6169 N N   . ARG   B 148 ? 0.1251 0.1130 0.1860 -0.0104 -0.0104 -0.0154 148 ARG   B N   
6170 C CA  . ARG   B 148 ? 0.1312 0.1283 0.1843 -0.0065 -0.0203 -0.0139 148 ARG   B CA  
6171 C C   . ARG   B 148 ? 0.1333 0.1324 0.1742 -0.0078 -0.0211 -0.0105 148 ARG   B C   
6172 O O   . ARG   B 148 ? 0.1487 0.1657 0.1746 -0.0202 -0.0263 -0.0079 148 ARG   B O   
6173 C CB  . ARG   B 148 ? 0.1317 0.1323 0.1937 -0.0008 -0.0292 -0.0168 148 ARG   B CB  
6174 C CG  . ARG   B 148 ? 0.1316 0.1510 0.2017 -0.0054 -0.0221 -0.0349 148 ARG   B CG  
6175 C CD  . ARG   B 148 ? 0.1385 0.1610 0.2022 0.0097  -0.0223 -0.0336 148 ARG   B CD  
6176 N NE  . ARG   B 148 ? 0.1486 0.1589 0.2037 0.0227  -0.0283 -0.0339 148 ARG   B NE  
6177 C CZ  . ARG   B 148 ? 0.1383 0.1539 0.1794 0.0142  -0.0172 -0.0216 148 ARG   B CZ  
6178 N NH1 . ARG   B 148 ? 0.1326 0.1574 0.1805 0.0014  -0.0015 -0.0134 148 ARG   B NH1 
6179 N NH2 . ARG   B 148 ? 0.1616 0.1394 0.1653 0.0209  -0.0143 -0.0151 148 ARG   B NH2 
6193 N N   . THR   B 149 ? 0.1363 0.1266 0.1673 -0.0098 -0.0145 -0.0027 149 THR   B N   
6194 C CA  . THR   B 149 ? 0.1466 0.1274 0.1667 -0.0128 -0.0138 0.0017  149 THR   B CA  
6195 C C   . THR   B 149 ? 0.1421 0.1223 0.1590 -0.0150 -0.0201 -0.0034 149 THR   B C   
6196 O O   . THR   B 149 ? 0.1464 0.1192 0.1688 -0.0180 -0.0080 -0.0016 149 THR   B O   
6197 C CB  . THR   B 149 ? 0.1472 0.1266 0.1735 -0.0138 -0.0177 0.0011  149 THR   B CB  
6198 O OG1 . THR   B 149 ? 0.1417 0.1313 0.1654 -0.0187 -0.0229 -0.0029 149 THR   B OG1 
6199 C CG2 . THR   B 149 ? 0.1559 0.1311 0.1942 -0.0065 -0.0113 0.0005  149 THR   B CG2 
6207 N N   . ASN   B 150 ? 0.1466 0.1261 0.1534 -0.0132 -0.0220 -0.0025 150 ASN   B N   
6208 C CA  . ASN   B 150 ? 0.1534 0.1356 0.1570 -0.0143 -0.0196 -0.0086 150 ASN   B CA  
6209 C C   . ASN   B 150 ? 0.1464 0.1308 0.1662 -0.0108 -0.0261 -0.0112 150 ASN   B C   
6210 O O   . ASN   B 150 ? 0.1513 0.1297 0.1871 -0.0265 -0.0338 -0.0056 150 ASN   B O   
6211 C CB  . ASN   B 150 ? 0.1698 0.1643 0.1616 -0.0126 -0.0234 -0.0006 150 ASN   B CB  
6212 C CG  . ASN   B 150 ? 0.1927 0.2080 0.1975 -0.0141 -0.0308 0.0198  150 ASN   B CG  
6213 O OD1 . ASN   B 150 ? 0.2083 0.2294 0.2159 -0.0227 -0.0513 0.0181  150 ASN   B OD1 
6214 N ND2 . ASN   B 150 ? 0.2032 0.2272 0.2302 -0.0033 -0.0298 0.0540  150 ASN   B ND2 
6221 N N   . VAL   B 151 ? 0.1374 0.1313 0.1600 -0.0147 -0.0207 -0.0056 151 VAL   B N   
6222 C CA  . VAL   B 151 ? 0.1354 0.1313 0.1661 -0.0189 -0.0153 -0.0027 151 VAL   B CA  
6223 C C   . VAL   B 151 ? 0.1375 0.1240 0.1658 -0.0248 -0.0203 -0.0015 151 VAL   B C   
6224 O O   . VAL   B 151 ? 0.1468 0.1329 0.1800 -0.0287 -0.0154 -0.0078 151 VAL   B O   
6225 C CB  . VAL   B 151 ? 0.1574 0.1500 0.1757 -0.0023 -0.0067 -0.0057 151 VAL   B CB  
6226 C CG1 . VAL   B 151 ? 0.1699 0.1510 0.2056 -0.0072 0.0010  -0.0200 151 VAL   B CG1 
6227 C CG2 . VAL   B 151 ? 0.1703 0.1627 0.1675 0.0074  -0.0095 0.0053  151 VAL   B CG2 
6237 N N   . TYR   B 152 ? 0.1339 0.1137 0.1474 -0.0224 -0.0150 -0.0076 152 TYR   B N   
6238 C CA  . TYR   B 152 ? 0.1414 0.1263 0.1404 -0.0225 -0.0096 -0.0110 152 TYR   B CA  
6239 C C   . TYR   B 152 ? 0.1387 0.1142 0.1366 -0.0217 -0.0072 -0.0091 152 TYR   B C   
6240 O O   . TYR   B 152 ? 0.1439 0.1259 0.1348 -0.0227 -0.0078 -0.0023 152 TYR   B O   
6241 C CB  . TYR   B 152 ? 0.1504 0.1369 0.1483 -0.0167 -0.0057 0.0055  152 TYR   B CB  
6242 C CG  . TYR   B 152 ? 0.1659 0.1456 0.1520 -0.0246 -0.0106 0.0025  152 TYR   B CG  
6243 C CD1 . TYR   B 152 ? 0.1767 0.1551 0.1428 -0.0247 -0.0188 0.0067  152 TYR   B CD1 
6244 C CD2 . TYR   B 152 ? 0.1816 0.1563 0.1627 -0.0267 -0.0055 -0.0024 152 TYR   B CD2 
6245 C CE1 . TYR   B 152 ? 0.1904 0.1723 0.1612 -0.0257 -0.0213 0.0174  152 TYR   B CE1 
6246 C CE2 . TYR   B 152 ? 0.1923 0.1769 0.1604 -0.0260 -0.0159 -0.0048 152 TYR   B CE2 
6247 C CZ  . TYR   B 152 ? 0.1975 0.1883 0.1519 -0.0270 -0.0375 0.0169  152 TYR   B CZ  
6248 O OH  . TYR   B 152 ? 0.2201 0.2188 0.1858 -0.0156 -0.0376 0.0221  152 TYR   B OH  
6258 N N   . LEU   B 153 ? 0.1325 0.1148 0.1510 -0.0200 -0.0160 -0.0047 153 LEU   B N   
6259 C CA  . LEU   B 153 ? 0.1382 0.1143 0.1501 -0.0149 -0.0115 -0.0115 153 LEU   B CA  
6260 C C   . LEU   B 153 ? 0.1378 0.1138 0.1586 -0.0199 -0.0058 -0.0134 153 LEU   B C   
6261 O O   . LEU   B 153 ? 0.1445 0.1306 0.1690 -0.0109 -0.0024 -0.0282 153 LEU   B O   
6262 C CB  . LEU   B 153 ? 0.1371 0.1106 0.1586 -0.0194 -0.0019 -0.0075 153 LEU   B CB  
6263 C CG  . LEU   B 153 ? 0.1384 0.1204 0.1796 -0.0218 -0.0023 -0.0041 153 LEU   B CG  
6264 C CD1 . LEU   B 153 ? 0.1425 0.1342 0.1812 -0.0255 -0.0006 0.0077  153 LEU   B CD1 
6265 C CD2 . LEU   B 153 ? 0.1390 0.1347 0.1955 -0.0248 0.0099  -0.0007 153 LEU   B CD2 
6277 N N   . ALA   B 154 ? 0.1326 0.1109 0.1708 -0.0130 -0.0104 -0.0090 154 ALA   B N   
6278 C CA  . ALA   B 154 ? 0.1425 0.1209 0.1916 0.0029  -0.0149 -0.0203 154 ALA   B CA  
6279 C C   . ALA   B 154 ? 0.1535 0.1210 0.1868 0.0031  -0.0150 -0.0237 154 ALA   B C   
6280 O O   . ALA   B 154 ? 0.1830 0.1279 0.1989 0.0023  0.0022  -0.0082 154 ALA   B O   
6281 C CB  . ALA   B 154 ? 0.1378 0.1364 0.2184 -0.0008 -0.0154 -0.0233 154 ALA   B CB  
6287 N N   . VAL   B 155 ? 0.1263 0.1160 0.1985 -0.0038 0.0015  -0.0114 155 VAL   B N   
6288 C CA  . VAL   B 155 ? 0.1230 0.1201 0.2070 -0.0004 -0.0099 -0.0102 155 VAL   B CA  
6289 C C   . VAL   B 155 ? 0.1264 0.1203 0.1966 -0.0062 -0.0098 -0.0132 155 VAL   B C   
6290 O O   . VAL   B 155 ? 0.1405 0.1375 0.2179 0.0053  -0.0110 -0.0291 155 VAL   B O   
6291 C CB  . VAL   B 155 ? 0.1265 0.1349 0.2391 -0.0070 -0.0162 0.0058  155 VAL   B CB  
6292 C CG1 . VAL   B 155 ? 0.1316 0.1271 0.2350 -0.0086 -0.0093 0.0021  155 VAL   B CG1 
6293 C CG2 . VAL   B 155 ? 0.1223 0.1451 0.2734 -0.0096 -0.0144 0.0381  155 VAL   B CG2 
6303 N N   . PHE   B 156 ? 0.1198 0.1265 0.2159 0.0054  -0.0160 -0.0150 156 PHE   B N   
6304 C CA  . PHE   B 156 ? 0.1250 0.1365 0.2572 0.0079  -0.0120 -0.0107 156 PHE   B CA  
6305 C C   . PHE   B 156 ? 0.1245 0.1416 0.2838 0.0136  -0.0163 -0.0270 156 PHE   B C   
6306 O O   . PHE   B 156 ? 0.1418 0.1607 0.3024 0.0267  -0.0014 -0.0330 156 PHE   B O   
6307 C CB  . PHE   B 156 ? 0.1297 0.1331 0.2600 0.0047  -0.0259 -0.0024 156 PHE   B CB  
6308 C CG  . PHE   B 156 ? 0.1287 0.1451 0.2665 -0.0026 -0.0183 0.0048  156 PHE   B CG  
6309 C CD1 . PHE   B 156 ? 0.1357 0.1747 0.3018 0.0041  -0.0015 0.0446  156 PHE   B CD1 
6310 C CD2 . PHE   B 156 ? 0.1385 0.1587 0.2608 0.0095  -0.0220 0.0094  156 PHE   B CD2 
6311 C CE1 . PHE   B 156 ? 0.1405 0.1921 0.3162 0.0051  0.0023  0.0499  156 PHE   B CE1 
6312 C CE2 . PHE   B 156 ? 0.1422 0.1803 0.2947 0.0153  -0.0192 0.0117  156 PHE   B CE2 
6313 C CZ  . PHE   B 156 ? 0.1381 0.1910 0.3171 0.0197  -0.0181 0.0314  156 PHE   B CZ  
6323 N N   . ASP   B 157 ? 0.1272 0.1343 0.2969 0.0134  -0.0262 -0.0102 157 ASP   B N   
6324 C CA  . ASP   B 157 ? 0.1355 0.1345 0.3225 0.0092  -0.0267 -0.0182 157 ASP   B CA  
6325 C C   . ASP   B 157 ? 0.1358 0.1287 0.3338 0.0138  -0.0259 -0.0381 157 ASP   B C   
6326 O O   . ASP   B 157 ? 0.1296 0.1342 0.3119 0.0092  -0.0257 -0.0351 157 ASP   B O   
6327 C CB  . ASP   B 157 ? 0.1606 0.1512 0.3361 -0.0024 -0.0355 -0.0057 157 ASP   B CB  
6328 C CG  . ASP   B 157 ? 0.1959 0.1554 0.3540 -0.0064 -0.0255 -0.0139 157 ASP   B CG  
6329 O OD1 . ASP   B 157 ? 0.2085 0.1496 0.3732 0.0047  -0.0284 -0.0192 157 ASP   B OD1 
6330 O OD2 . ASP   B 157 ? 0.2262 0.1770 0.3787 -0.0099 -0.0061 -0.0006 157 ASP   B OD2 
6335 N N   . LYS   B 158 ? 0.1348 0.1535 0.3419 0.0085  -0.0116 -0.0595 158 LYS   B N   
6336 C CA  . LYS   B 158 ? 0.1528 0.1710 0.3452 0.0043  -0.0022 -0.0687 158 LYS   B CA  
6337 C C   . LYS   B 158 ? 0.1514 0.1573 0.3433 0.0061  -0.0084 -0.0703 158 LYS   B C   
6338 O O   . LYS   B 158 ? 0.1526 0.1606 0.3377 -0.0042 -0.0028 -0.0742 158 LYS   B O   
6339 C CB  . LYS   B 158 ? 0.1765 0.2094 0.3549 -0.0002 0.0047  -0.0762 158 LYS   B CB  
6340 C CG  . LYS   B 158 ? 0.2076 0.2446 0.3673 -0.0010 0.0143  -0.0853 158 LYS   B CG  
6341 C CD  . LYS   B 158 ? 0.2309 0.2790 0.3793 -0.0073 0.0214  -0.0847 158 LYS   B CD  
6342 C CE  . LYS   B 158 ? 0.2504 0.3017 0.3975 -0.0082 0.0224  -0.0804 158 LYS   B CE  
6343 N NZ  . LYS   B 158 ? 0.2448 0.3026 0.3926 -0.0165 0.0235  -0.0839 158 LYS   B NZ  
6357 N N   . ASN   B 159 ? 0.1558 0.1474 0.3588 0.0074  -0.0179 -0.0581 159 ASN   B N   
6358 C CA  . ASN   B 159 ? 0.1676 0.1459 0.3786 0.0176  -0.0364 -0.0411 159 ASN   B CA  
6359 C C   . ASN   B 159 ? 0.1538 0.1345 0.3693 0.0152  -0.0416 -0.0323 159 ASN   B C   
6360 O O   . ASN   B 159 ? 0.1507 0.1270 0.3736 0.0008  -0.0445 -0.0272 159 ASN   B O   
6361 C CB  . ASN   B 159 ? 0.1894 0.1601 0.4171 0.0252  -0.0347 -0.0260 159 ASN   B CB  
6362 C CG  . ASN   B 159 ? 0.2150 0.1794 0.4424 0.0245  -0.0388 -0.0384 159 ASN   B CG  
6363 O OD1 . ASN   B 159 ? 0.2297 0.1887 0.4525 0.0286  -0.0350 -0.0584 159 ASN   B OD1 
6364 N ND2 . ASN   B 159 ? 0.2194 0.1906 0.4654 0.0300  -0.0396 -0.0326 159 ASN   B ND2 
6371 N N   . LEU   B 160 ? 0.1434 0.1321 0.3409 0.0097  -0.0436 -0.0299 160 LEU   B N   
6372 C CA  . LEU   B 160 ? 0.1402 0.1343 0.3150 0.0061  -0.0341 -0.0163 160 LEU   B CA  
6373 C C   . LEU   B 160 ? 0.1348 0.1256 0.2964 -0.0013 -0.0235 -0.0297 160 LEU   B C   
6374 O O   . LEU   B 160 ? 0.1279 0.1302 0.2841 -0.0054 -0.0282 -0.0168 160 LEU   B O   
6375 C CB  . LEU   B 160 ? 0.1369 0.1500 0.2984 0.0084  -0.0426 -0.0053 160 LEU   B CB  
6376 C CG  . LEU   B 160 ? 0.1398 0.1638 0.2662 0.0101  -0.0407 0.0012  160 LEU   B CG  
6377 C CD1 . LEU   B 160 ? 0.1548 0.1831 0.2698 -0.0010 -0.0262 0.0084  160 LEU   B CD1 
6378 C CD2 . LEU   B 160 ? 0.1420 0.1695 0.2567 0.0124  -0.0321 -0.0088 160 LEU   B CD2 
6390 N N   . TYR   B 161 ? 0.1322 0.1363 0.2951 -0.0070 -0.0091 -0.0392 161 TYR   B N   
6391 C CA  . TYR   B 161 ? 0.1348 0.1308 0.2894 -0.0133 0.0053  -0.0432 161 TYR   B CA  
6392 C C   . TYR   B 161 ? 0.1473 0.1313 0.2938 -0.0089 0.0110  -0.0406 161 TYR   B C   
6393 O O   . TYR   B 161 ? 0.1483 0.1334 0.2747 -0.0154 0.0046  -0.0392 161 TYR   B O   
6394 C CB  . TYR   B 161 ? 0.1504 0.1441 0.2868 -0.0244 0.0200  -0.0503 161 TYR   B CB  
6395 C CG  . TYR   B 161 ? 0.1766 0.1478 0.2719 -0.0217 0.0308  -0.0562 161 TYR   B CG  
6396 C CD1 . TYR   B 161 ? 0.1805 0.1402 0.2724 -0.0331 0.0361  -0.0515 161 TYR   B CD1 
6397 C CD2 . TYR   B 161 ? 0.1969 0.1549 0.2717 -0.0188 0.0369  -0.0494 161 TYR   B CD2 
6398 C CE1 . TYR   B 161 ? 0.1990 0.1548 0.2828 -0.0304 0.0380  -0.0458 161 TYR   B CE1 
6399 C CE2 . TYR   B 161 ? 0.2135 0.1679 0.2744 -0.0230 0.0438  -0.0398 161 TYR   B CE2 
6400 C CZ  . TYR   B 161 ? 0.2126 0.1675 0.2788 -0.0344 0.0412  -0.0313 161 TYR   B CZ  
6401 O OH  . TYR   B 161 ? 0.2408 0.1851 0.3030 -0.0323 0.0355  -0.0274 161 TYR   B OH  
6411 N N   . ASP   B 162 ? 0.1511 0.1313 0.3047 -0.0062 0.0046  -0.0485 162 ASP   B N   
6412 C CA  . ASP   B 162 ? 0.1615 0.1383 0.3063 -0.0048 -0.0075 -0.0490 162 ASP   B CA  
6413 C C   . ASP   B 162 ? 0.1562 0.1270 0.2958 -0.0077 -0.0111 -0.0413 162 ASP   B C   
6414 O O   . ASP   B 162 ? 0.1614 0.1351 0.3022 -0.0090 -0.0243 -0.0344 162 ASP   B O   
6415 C CB  . ASP   B 162 ? 0.1738 0.1584 0.3245 -0.0010 -0.0159 -0.0672 162 ASP   B CB  
6416 C CG  . ASP   B 162 ? 0.1804 0.1849 0.3347 0.0102  -0.0060 -0.0777 162 ASP   B CG  
6417 O OD1 . ASP   B 162 ? 0.1781 0.2021 0.3251 0.0093  -0.0004 -0.0784 162 ASP   B OD1 
6418 O OD2 . ASP   B 162 ? 0.1961 0.2033 0.3566 0.0232  0.0169  -0.0775 162 ASP   B OD2 
6423 N N   A LYS   B 163 ? 0.1537 0.1290 0.2884 -0.0096 -0.0169 -0.0284 163 LYS   B N   
6424 N N   B LYS   B 163 ? 0.1518 0.1185 0.2853 -0.0115 -0.0196 -0.0312 163 LYS   B N   
6425 C CA  A LYS   B 163 ? 0.1605 0.1408 0.2861 -0.0107 -0.0212 -0.0117 163 LYS   B CA  
6426 C CA  B LYS   B 163 ? 0.1625 0.1296 0.2818 -0.0129 -0.0264 -0.0131 163 LYS   B CA  
6427 C C   A LYS   B 163 ? 0.1395 0.1318 0.2719 -0.0149 -0.0231 -0.0039 163 LYS   B C   
6428 C C   B LYS   B 163 ? 0.1404 0.1272 0.2693 -0.0167 -0.0235 -0.0067 163 LYS   B C   
6429 O O   A LYS   B 163 ? 0.1395 0.1371 0.2822 -0.0189 -0.0283 -0.0013 163 LYS   B O   
6430 O O   B LYS   B 163 ? 0.1433 0.1362 0.2819 -0.0226 -0.0263 -0.0114 163 LYS   B O   
6431 C CB  A LYS   B 163 ? 0.1881 0.1673 0.3107 -0.0076 -0.0253 0.0013  163 LYS   B CB  
6432 C CB  B LYS   B 163 ? 0.1968 0.1538 0.3065 -0.0097 -0.0360 0.0069  163 LYS   B CB  
6433 C CG  A LYS   B 163 ? 0.2239 0.2106 0.3454 -0.0060 -0.0201 0.0059  163 LYS   B CG  
6434 C CG  B LYS   B 163 ? 0.2437 0.2075 0.3476 -0.0088 -0.0292 0.0138  163 LYS   B CG  
6435 C CD  A LYS   B 163 ? 0.2495 0.2354 0.3791 -0.0071 -0.0138 0.0008  163 LYS   B CD  
6436 C CD  B LYS   B 163 ? 0.2736 0.2386 0.3901 -0.0115 -0.0207 0.0109  163 LYS   B CD  
6437 C CE  A LYS   B 163 ? 0.2636 0.2458 0.4050 -0.0084 -0.0096 -0.0004 163 LYS   B CE  
6438 C CE  B LYS   B 163 ? 0.2950 0.2563 0.4249 -0.0158 -0.0144 0.0104  163 LYS   B CE  
6439 N NZ  A LYS   B 163 ? 0.2695 0.2521 0.4184 -0.0089 -0.0092 -0.0024 163 LYS   B NZ  
6440 N NZ  B LYS   B 163 ? 0.3201 0.2855 0.4442 -0.0186 -0.0139 0.0093  163 LYS   B NZ  
6467 N N   . LEU   B 164 ? 0.1228 0.1190 0.2532 -0.0163 -0.0233 -0.0040 164 LEU   B N   
6468 C CA  . LEU   B 164 ? 0.1318 0.1199 0.2445 -0.0075 -0.0247 -0.0062 164 LEU   B CA  
6469 C C   . LEU   B 164 ? 0.1381 0.1192 0.2439 -0.0098 -0.0343 -0.0073 164 LEU   B C   
6470 O O   . LEU   B 164 ? 0.1354 0.1417 0.2667 -0.0128 -0.0327 -0.0032 164 LEU   B O   
6471 C CB  . LEU   B 164 ? 0.1286 0.1212 0.2365 -0.0135 -0.0219 -0.0125 164 LEU   B CB  
6472 C CG  . LEU   B 164 ? 0.1370 0.1363 0.2360 -0.0124 -0.0132 -0.0038 164 LEU   B CG  
6473 C CD1 . LEU   B 164 ? 0.1367 0.1313 0.2325 -0.0169 -0.0242 -0.0087 164 LEU   B CD1 
6474 C CD2 . LEU   B 164 ? 0.1503 0.1690 0.2509 -0.0135 0.0069  -0.0279 164 LEU   B CD2 
6487 N N   . VAL   B 165 ? 0.1626 0.1277 0.2545 -0.0147 -0.0400 -0.0187 165 VAL   B N   
6488 C CA  . VAL   B 165 ? 0.1940 0.1397 0.2623 -0.0174 -0.0550 -0.0151 165 VAL   B CA  
6489 C C   . VAL   B 165 ? 0.2150 0.1492 0.2793 -0.0284 -0.0742 -0.0196 165 VAL   B C   
6490 O O   . VAL   B 165 ? 0.2304 0.1653 0.2831 -0.0350 -0.0765 -0.0042 165 VAL   B O   
6491 C CB  . VAL   B 165 ? 0.2154 0.1560 0.2637 0.0006  -0.0246 -0.0146 165 VAL   B CB  
6492 C CG1 . VAL   B 165 ? 0.2311 0.1623 0.2973 -0.0037 -0.0116 -0.0201 165 VAL   B CG1 
6493 C CG2 . VAL   B 165 ? 0.2132 0.1589 0.2613 0.0040  -0.0152 -0.0092 165 VAL   B CG2 
6503 N N   . SER   B 166 ? 0.2205 0.1424 0.3061 -0.0261 -0.0736 -0.0346 166 SER   B N   
6504 C CA  . SER   B 166 ? 0.2207 0.1440 0.3411 -0.0308 -0.0606 -0.0348 166 SER   B CA  
6505 C C   . SER   B 166 ? 0.2089 0.1473 0.3591 -0.0284 -0.0583 -0.0161 166 SER   B C   
6506 O O   . SER   B 166 ? 0.2143 0.1704 0.3838 -0.0458 -0.0695 -0.0306 166 SER   B O   
6507 C CB  . SER   B 166 ? 0.2248 0.1530 0.3614 -0.0251 -0.0470 -0.0418 166 SER   B CB  
6508 O OG  . SER   B 166 ? 0.2083 0.1478 0.3692 -0.0180 -0.0522 -0.0252 166 SER   B OG  
6514 N N   . SER   B 167 ? 0.1869 0.1453 0.3403 -0.0289 -0.0567 0.0193  167 SER   B N   
6515 C CA  . SER   B 167 ? 0.1752 0.1499 0.3239 -0.0264 -0.0424 0.0256  167 SER   B CA  
6516 C C   . SER   B 167 ? 0.1727 0.1577 0.3137 -0.0381 -0.0442 0.0352  167 SER   B C   
6517 O O   . SER   B 167 ? 0.1726 0.1685 0.3099 -0.0424 -0.0457 0.0293  167 SER   B O   
6518 C CB  . SER   B 167 ? 0.1668 0.1605 0.3225 -0.0268 -0.0277 0.0248  167 SER   B CB  
6519 O OG  . SER   B 167 ? 0.1587 0.1685 0.3115 -0.0155 -0.0110 0.0314  167 SER   B OG  
6525 N N   . PHE   B 168 ? 0.1721 0.1556 0.3094 -0.0364 -0.0355 0.0452  168 PHE   B N   
6526 C CA  . PHE   B 168 ? 0.1775 0.1536 0.2877 -0.0417 -0.0305 0.0268  168 PHE   B CA  
6527 C C   . PHE   B 168 ? 0.1532 0.1479 0.2445 -0.0217 -0.0136 0.0144  168 PHE   B C   
6528 O O   . PHE   B 168 ? 0.1754 0.1446 0.2491 0.0010  -0.0083 -0.0058 168 PHE   B O   
6529 C CB  . PHE   B 168 ? 0.1978 0.1564 0.2946 -0.0506 -0.0452 0.0361  168 PHE   B CB  
6530 C CG  . PHE   B 168 ? 0.2213 0.1449 0.2771 -0.0508 -0.0514 0.0181  168 PHE   B CG  
6531 C CD1 . PHE   B 168 ? 0.2548 0.1501 0.2833 -0.0413 -0.0540 0.0149  168 PHE   B CD1 
6532 C CD2 . PHE   B 168 ? 0.2108 0.1430 0.2717 -0.0421 -0.0512 0.0227  168 PHE   B CD2 
6533 C CE1 . PHE   B 168 ? 0.2677 0.1602 0.2844 -0.0290 -0.0424 0.0095  168 PHE   B CE1 
6534 C CE2 . PHE   B 168 ? 0.2324 0.1485 0.2805 -0.0306 -0.0589 0.0166  168 PHE   B CE2 
6535 C CZ  . PHE   B 168 ? 0.2516 0.1463 0.2906 -0.0160 -0.0556 0.0148  168 PHE   B CZ  
6545 N N   . LEU   B 169 ? 0.1557 0.1605 0.2311 -0.0014 0.0046  0.0017  169 LEU   B N   
6546 C CA  . LEU   B 169 ? 0.1794 0.1919 0.2722 -0.0058 -0.0015 -0.0295 169 LEU   B CA  
6547 C C   . LEU   B 169 ? 0.2033 0.2135 0.3191 0.0058  -0.0059 -0.0547 169 LEU   B C   
6548 O O   . LEU   B 169 ? 0.2256 0.2335 0.3697 0.0047  -0.0076 -0.0722 169 LEU   B O   
6549 C CB  . LEU   B 169 ? 0.2017 0.2353 0.2881 -0.0130 -0.0083 -0.0032 169 LEU   B CB  
6550 C CG  . LEU   B 169 ? 0.2413 0.2757 0.3301 -0.0036 -0.0074 0.0047  169 LEU   B CG  
6551 C CD1 . LEU   B 169 ? 0.2587 0.3001 0.3437 -0.0024 -0.0050 0.0201  169 LEU   B CD1 
6552 C CD2 . LEU   B 169 ? 0.2389 0.2838 0.3345 0.0093  0.0091  -0.0079 169 LEU   B CD2 
6553 O OXT . LEU   B 169 ? 0.2175 0.2277 0.3129 0.0302  -0.0032 -0.0522 169 LEU   B OXT 
6565 C C1  T TFA   C .   ? 0.0908 0.0903 0.0690 0.0043  0.0120  0.0125  201 TFA   A C1  
6566 C C2  T TFA   C .   ? 0.1104 0.1073 0.0888 -0.0057 0.0129  -0.0010 201 TFA   A C2  
6567 O O   T TFA   C .   ? 0.0699 0.0774 0.0612 0.0117  0.0087  0.0309  201 TFA   A O   
6568 F F1  T TFA   C .   ? 0.1189 0.1139 0.1120 -0.0044 0.0133  -0.0098 201 TFA   A F1  
6569 F F2  T TFA   C .   ? 0.1128 0.1108 0.0847 -0.0110 0.0105  0.0052  201 TFA   A F2  
6570 F F3  T TFA   C .   ? 0.1168 0.1116 0.1075 -0.0144 0.0172  -0.0103 201 TFA   A F3  
6571 O OXT T TFA   C .   ? 0.0897 0.0842 0.0716 0.0126  0.0188  0.0064  201 TFA   A OXT 
6572 S S   B DMS   D .   ? 0.6884 0.5006 0.4966 0.1458  0.1478  0.0616  202 DMS   A S   
6573 O O   B DMS   D .   ? 0.6887 0.5025 0.5090 0.1435  0.1484  0.0601  202 DMS   A O   
6574 C C1  B DMS   D .   ? 0.6878 0.5012 0.5068 0.1465  0.1467  0.0600  202 DMS   A C1  
6575 C C2  B DMS   D .   ? 0.6902 0.5018 0.5060 0.1456  0.1473  0.0623  202 DMS   A C2  
6582 N N2  B A1A9U E .   ? 0.1427 0.1322 0.1638 -0.0056 0.0006  0.0018  203 A1A9U A N2  
6583 C C3  B A1A9U E .   ? 0.1514 0.1466 0.1347 -0.0061 -0.0018 0.0248  203 A1A9U A C3  
6584 C C6  B A1A9U E .   ? 0.1426 0.1494 0.1482 -0.0046 -0.0005 0.0113  203 A1A9U A C6  
6585 C C9  B A1A9U E .   ? 0.1311 0.1650 0.1816 -0.0104 0.0209  0.0187  203 A1A9U A C9  
6586 C C12 B A1A9U E .   ? 0.1462 0.1370 0.1613 -0.0034 -0.0072 0.0167  203 A1A9U A C12 
6587 C C14 B A1A9U E .   ? 0.1726 0.1436 0.1689 -0.0192 -0.0385 0.0141  203 A1A9U A C14 
6588 C C1  B A1A9U E .   ? 0.1266 0.1652 0.1447 -0.0088 -0.0122 0.0360  203 A1A9U A C1  
6589 C C10 B A1A9U E .   ? 0.1467 0.1325 0.1525 -0.0105 -0.0067 0.0145  203 A1A9U A C10 
6590 C C11 B A1A9U E .   ? 0.1432 0.1399 0.1642 -0.0035 0.0131  0.0116  203 A1A9U A C11 
6591 C C13 B A1A9U E .   ? 0.1550 0.1348 0.1513 -0.0123 -0.0134 0.0145  203 A1A9U A C13 
6592 C C15 B A1A9U E .   ? 0.1712 0.1404 0.1769 -0.0182 -0.0389 0.0184  203 A1A9U A C15 
6593 C C16 B A1A9U E .   ? 0.1435 0.1515 0.1503 -0.0101 -0.0077 0.0102  203 A1A9U A C16 
6594 C C2  B A1A9U E .   ? 0.1430 0.1572 0.1418 -0.0045 -0.0095 0.0244  203 A1A9U A C2  
6595 C C4  B A1A9U E .   ? 0.1532 0.1222 0.1453 -0.0120 0.0097  0.0157  203 A1A9U A C4  
6596 C C5  B A1A9U E .   ? 0.1514 0.1431 0.1494 -0.0034 0.0085  0.0118  203 A1A9U A C5  
6597 C C7  B A1A9U E .   ? 0.1361 0.1509 0.1625 -0.0034 -0.0048 0.0070  203 A1A9U A C7  
6598 C C8  B A1A9U E .   ? 0.1401 0.1457 0.1662 -0.0115 -0.0016 0.0148  203 A1A9U A C8  
6599 N N1  B A1A9U E .   ? 0.1611 0.1338 0.1629 -0.0042 -0.0077 0.0212  203 A1A9U A N1  
6600 N N3  B A1A9U E .   ? 0.1436 0.1418 0.1604 -0.0032 0.0128  0.0155  203 A1A9U A N3  
6601 N N4  B A1A9U E .   ? 0.1483 0.1369 0.1652 -0.0131 -0.0323 0.0285  203 A1A9U A N4  
6602 O O1  B A1A9U E .   ? 0.1299 0.1789 0.2061 0.0025  0.0316  0.0407  203 A1A9U A O1  
6621 O O   . HOH   F .   ? 0.8040 0.7102 0.5935 -0.0679 0.0746  -0.1033 301 HOH   A O   
6622 O O   . HOH   F .   ? 0.4045 0.7495 0.4941 -0.1103 0.0139  0.1242  302 HOH   A O   
6623 O O   A HOH   F .   ? 0.1521 0.1098 0.3068 0.0330  -0.0330 0.0405  303 HOH   A O   
6624 O O   . HOH   F .   ? 0.2978 0.8146 0.5227 -0.1009 -0.0770 0.1761  304 HOH   A O   
6625 O O   . HOH   F .   ? 0.3007 0.2519 0.4956 -0.0306 -0.1606 0.1137  305 HOH   A O   
6626 O O   B HOH   F .   ? 0.1705 0.1226 0.3232 0.0349  -0.0022 0.0614  306 HOH   A O   
6627 O O   . HOH   F .   ? 0.5987 0.4423 0.3475 0.1784  -0.1040 0.0737  307 HOH   A O   
6628 O O   B HOH   F .   ? 0.2596 0.2341 0.3869 0.0471  0.0496  0.0951  308 HOH   A O   
6629 O O   . HOH   F .   ? 0.4892 0.2747 0.2844 -0.1151 0.0703  0.0223  309 HOH   A O   
6630 O O   . HOH   F .   ? 0.2547 0.2950 0.1489 -0.0458 0.0306  0.0362  310 HOH   A O   
6631 O O   . HOH   F .   ? 0.4707 0.5280 0.4367 0.1715  0.1129  -0.1308 311 HOH   A O   
6632 O O   . HOH   F .   ? 0.5144 0.3972 0.4199 -0.0974 0.1432  0.0677  312 HOH   A O   
6633 O O   . HOH   F .   ? 0.1860 0.3086 0.3607 -0.0319 0.0535  -0.0933 313 HOH   A O   
6634 O O   A HOH   F .   ? 0.1139 0.2632 0.1855 0.0427  0.0439  0.0720  314 HOH   A O   
6635 O O   . HOH   F .   ? 0.3921 0.3640 0.3640 -0.0722 0.1772  0.0256  315 HOH   A O   
6636 O O   . HOH   F .   ? 0.2906 0.2935 0.2550 -0.0858 0.0152  0.0631  316 HOH   A O   
6637 O O   . HOH   F .   ? 0.2142 0.1653 0.3644 -0.0426 0.0118  -0.0199 317 HOH   A O   
6638 O O   . HOH   F .   ? 0.4486 0.3507 0.3955 -0.0157 0.1325  0.0000  318 HOH   A O   
6639 O O   A HOH   F .   ? 0.2770 0.2452 0.1881 -0.0630 -0.0202 0.0271  319 HOH   A O   
6640 O O   A HOH   F .   ? 0.1947 0.2937 0.4339 0.0039  -0.0422 -0.0516 320 HOH   A O   
6641 O O   . HOH   F .   ? 0.4811 0.4972 0.2846 -0.1404 0.1346  0.0779  321 HOH   A O   
6642 O O   . HOH   F .   ? 0.5489 0.5434 0.4616 -0.0937 0.1232  0.2280  322 HOH   A O   
6643 O O   . HOH   F .   ? 0.1674 0.2594 0.2902 0.0242  0.0009  -0.0133 323 HOH   A O   
6644 O O   A HOH   F .   ? 0.2159 0.2634 0.2073 0.0859  -0.0196 -0.0379 324 HOH   A O   
6645 O O   . HOH   F .   ? 0.1378 0.1406 0.2160 -0.0199 0.0109  0.0002  325 HOH   A O   
6646 O O   . HOH   F .   ? 0.5810 0.5541 0.2981 0.0035  -0.0808 0.1018  326 HOH   A O   
6647 O O   . HOH   F .   ? 0.2477 0.2265 0.2522 0.0454  0.0136  0.0258  327 HOH   A O   
6648 O O   . HOH   F .   ? 0.3796 0.2000 0.4433 0.0135  -0.1375 0.0223  328 HOH   A O   
6649 O O   A HOH   F .   ? 0.1609 0.1549 0.1532 0.0150  0.0585  0.0496  329 HOH   A O   
6650 O O   . HOH   F .   ? 0.2599 0.2716 0.2995 -0.0013 -0.0337 -0.0602 330 HOH   A O   
6651 O O   A HOH   F .   ? 0.4367 0.1813 0.3771 0.0287  -0.1141 0.0860  331 HOH   A O   
6652 O O   . HOH   F .   ? 0.3566 0.6924 0.4238 -0.0468 -0.1534 0.0974  332 HOH   A O   
6653 O O   . HOH   F .   ? 0.4357 0.5100 0.4861 -0.0820 0.0946  -0.0035 333 HOH   A O   
6654 O O   . HOH   F .   ? 0.1720 0.1861 0.1791 -0.0203 -0.0022 0.0570  334 HOH   A O   
6655 O O   . HOH   F .   ? 0.5375 0.1802 0.5344 0.0479  0.0767  0.0034  335 HOH   A O   
6656 O O   A HOH   F .   ? 0.1787 0.1361 0.1694 -0.0003 -0.0379 -0.0203 336 HOH   A O   
6657 O O   B HOH   F .   ? 0.2890 0.4241 0.5306 0.0018  -0.0647 0.2648  337 HOH   A O   
6658 O O   A HOH   F .   ? 0.1637 0.2561 0.3139 0.0657  0.0730  0.0787  338 HOH   A O   
6659 O O   . HOH   F .   ? 0.3340 0.3349 0.3478 0.0922  -0.1502 -0.1440 339 HOH   A O   
6660 O O   . HOH   F .   ? 0.1991 0.2850 0.3386 0.0407  0.0616  -0.0797 340 HOH   A O   
6661 O O   . HOH   F .   ? 0.2790 0.2679 0.3161 -0.0788 0.0025  -0.0389 341 HOH   A O   
6662 O O   . HOH   F .   ? 0.1776 0.2030 0.3158 0.0140  0.0733  -0.0194 342 HOH   A O   
6663 O O   . HOH   F .   ? 0.1350 0.2196 0.2030 0.0074  -0.0133 0.0602  343 HOH   A O   
6664 O O   . HOH   F .   ? 0.1237 0.1187 0.1187 -0.0049 0.0160  0.0056  344 HOH   A O   
6665 O O   B HOH   F .   ? 0.2839 0.3646 0.1915 -0.0511 0.0932  -0.0034 345 HOH   A O   
6666 O O   . HOH   F .   ? 0.2890 0.3697 0.3847 -0.0844 -0.0724 -0.0555 346 HOH   A O   
6667 O O   . HOH   F .   ? 0.3116 0.4002 0.3067 0.0198  0.0666  0.0360  347 HOH   A O   
6668 O O   . HOH   F .   ? 0.4419 0.2828 0.4672 -0.1608 0.1719  -0.0454 348 HOH   A O   
6669 O O   . HOH   F .   ? 0.2227 0.3771 0.3363 0.0799  -0.0673 -0.0104 349 HOH   A O   
6670 O O   . HOH   F .   ? 0.2816 0.3260 0.5177 -0.0662 -0.1061 -0.1006 350 HOH   A O   
6671 O O   . HOH   F .   ? 0.2168 0.4578 0.3669 -0.0122 -0.0326 0.1595  351 HOH   A O   
6672 O O   . HOH   F .   ? 0.3781 0.1862 0.2100 0.0980  0.0480  0.0144  352 HOH   A O   
6673 O O   B HOH   F .   ? 0.1448 0.1458 0.1840 -0.0060 0.0144  0.0036  353 HOH   A O   
6674 O O   . HOH   F .   ? 0.5258 0.4227 0.4536 0.0743  0.2154  -0.0456 354 HOH   A O   
6675 O O   . HOH   F .   ? 0.2034 0.1614 0.2584 0.0235  -0.0502 -0.0052 355 HOH   A O   
6676 O O   . HOH   F .   ? 0.5776 0.5348 0.6767 0.0635  -0.0202 -0.0160 356 HOH   A O   
6677 O O   B HOH   F .   ? 0.3792 0.2607 0.4423 0.0420  0.1136  -0.0570 357 HOH   A O   
6678 O O   . HOH   F .   ? 0.1448 0.1746 0.2382 0.0103  -0.0097 0.0085  358 HOH   A O   
6679 O O   . HOH   F .   ? 0.3622 0.2887 0.4184 -0.1171 -0.0487 0.0615  359 HOH   A O   
6680 O O   . HOH   F .   ? 0.1504 0.1634 0.1320 0.0038  0.0051  0.0061  360 HOH   A O   
6681 O O   A HOH   F .   ? 0.2068 0.3939 0.2860 0.0176  0.0046  0.0771  361 HOH   A O   
6682 O O   . HOH   F .   ? 0.2971 0.3230 0.2219 -0.0803 -0.0108 -0.0604 362 HOH   A O   
6683 O O   . HOH   F .   ? 0.6172 0.3720 0.2667 -0.0325 -0.0170 0.1160  363 HOH   A O   
6684 O O   . HOH   F .   ? 0.5575 0.4264 0.4480 -0.2037 -0.1117 0.2078  364 HOH   A O   
6685 O O   . HOH   F .   ? 0.2365 0.4018 0.3094 0.0556  0.0856  0.1765  365 HOH   A O   
6686 O O   B HOH   F .   ? 0.4018 0.2429 0.4258 -0.1227 0.0927  -0.0603 366 HOH   A O   
6687 O O   B HOH   F .   ? 0.1236 0.1680 0.1750 -0.0038 -0.0172 -0.0531 367 HOH   A O   
6688 O O   . HOH   F .   ? 0.3467 0.3543 0.2996 0.1673  0.0824  0.0685  368 HOH   A O   
6689 O O   . HOH   F .   ? 0.1441 0.2912 0.2684 0.0097  0.0275  0.0479  369 HOH   A O   
6690 O O   . HOH   F .   ? 0.1396 0.1201 0.1945 -0.0054 0.0141  -0.0087 370 HOH   A O   
6691 O O   . HOH   F .   ? 0.1853 0.1947 0.1796 -0.0006 -0.0089 0.0361  371 HOH   A O   
6692 O O   . HOH   F .   ? 0.1380 0.1402 0.1342 -0.0056 -0.0092 -0.0047 372 HOH   A O   
6693 O O   . HOH   F .   ? 0.1827 0.1749 0.2120 -0.0325 0.0127  0.0246  373 HOH   A O   
6694 O O   . HOH   F .   ? 0.3848 0.2200 0.3571 -0.1065 0.0723  0.0349  374 HOH   A O   
6695 O O   . HOH   F .   ? 0.2688 0.4222 0.2840 -0.0376 0.0774  -0.0054 375 HOH   A O   
6696 O O   . HOH   F .   ? 0.5727 0.4674 0.5978 -0.0372 -0.0444 0.1425  376 HOH   A O   
6697 O O   . HOH   F .   ? 0.3161 0.5816 0.3550 0.0937  0.0942  -0.1062 377 HOH   A O   
6698 O O   A HOH   F .   ? 0.2093 0.1831 0.2299 0.0379  0.0988  0.0963  378 HOH   A O   
6699 O O   . HOH   F .   ? 0.1464 0.1425 0.1800 0.0029  -0.0212 -0.0179 379 HOH   A O   
6700 O O   . HOH   F .   ? 0.1687 0.1588 0.2221 0.0212  -0.0172 0.0291  380 HOH   A O   
6701 O O   . HOH   F .   ? 0.1553 0.1701 0.2193 -0.0174 0.0032  0.0415  381 HOH   A O   
6702 O O   B HOH   F .   ? 0.2284 0.2459 0.3740 -0.0271 -0.0806 0.0895  382 HOH   A O   
6703 O O   . HOH   F .   ? 0.1961 0.2086 0.2090 -0.0298 -0.0339 0.0392  383 HOH   A O   
6704 O O   B HOH   F .   ? 0.3142 0.2716 0.2416 -0.0388 -0.0021 0.0453  384 HOH   A O   
6705 O O   . HOH   F .   ? 0.3048 0.2655 0.2051 0.0336  0.0830  0.0124  385 HOH   A O   
6706 O O   . HOH   F .   ? 0.2631 0.1854 0.1610 -0.0584 0.0200  0.0247  386 HOH   A O   
6707 O O   . HOH   F .   ? 0.3863 0.4943 0.2997 0.2537  0.0142  -0.0244 387 HOH   A O   
6708 O O   . HOH   F .   ? 0.4188 0.5920 0.5405 0.1020  -0.0358 0.1534  388 HOH   A O   
6709 O O   . HOH   F .   ? 0.2822 0.3529 0.3418 -0.0619 0.1197  0.0049  389 HOH   A O   
6710 O O   B HOH   F .   ? 0.2072 0.1671 0.2291 -0.0330 -0.0595 0.0168  390 HOH   A O   
6711 O O   . HOH   F .   ? 0.2005 0.3910 0.2775 -0.0336 0.0018  -0.0040 391 HOH   A O   
6712 O O   B HOH   F .   ? 0.2408 0.5319 0.4045 -0.0546 -0.0517 -0.0660 392 HOH   A O   
6713 O O   . HOH   F .   ? 0.3848 0.5636 0.3523 -0.0219 -0.0103 0.0842  393 HOH   A O   
6714 O O   . HOH   F .   ? 0.1605 0.1960 0.2985 -0.0079 0.0745  0.0630  394 HOH   A O   
6715 O O   A HOH   F .   ? 0.1973 0.1333 0.1543 -0.0041 -0.0017 0.0239  395 HOH   A O   
6716 O O   . HOH   F .   ? 0.2913 0.3658 0.3272 -0.1264 0.1012  -0.0078 396 HOH   A O   
6717 O O   . HOH   F .   ? 0.3410 0.2389 0.3029 -0.0082 -0.0316 0.0976  397 HOH   A O   
6718 O O   T HOH   F .   ? 0.0661 0.0500 0.1034 -0.0140 0.0116  0.0284  398 HOH   A O   
6719 O O   . HOH   F .   ? 0.5600 0.3658 0.4827 0.1592  -0.1032 0.1236  399 HOH   A O   
6720 O O   A HOH   F .   ? 0.1476 0.1145 0.1497 0.0407  -0.0551 -0.0584 400 HOH   A O   
6721 O O   . HOH   F .   ? 0.2190 0.2160 0.2306 -0.0646 -0.0085 0.0562  401 HOH   A O   
6722 O O   . HOH   F .   ? 0.4314 0.3388 0.1801 -0.0554 0.0773  0.0326  402 HOH   A O   
6723 O O   . HOH   F .   ? 0.2492 0.3450 0.3198 -0.0214 0.0905  -0.0474 403 HOH   A O   
6724 O O   A HOH   F .   ? 0.1256 0.1285 0.1510 -0.0199 -0.0143 0.0105  404 HOH   A O   
6725 O O   . HOH   F .   ? 0.4813 0.6751 0.3177 0.1244  -0.0893 0.1169  405 HOH   A O   
6726 O O   . HOH   F .   ? 0.5635 0.4871 0.4125 -0.1025 0.0114  0.1832  406 HOH   A O   
6727 O O   . HOH   F .   ? 0.1737 0.1859 0.3594 0.0364  0.0975  0.1057  407 HOH   A O   
6728 O O   . HOH   F .   ? 0.6938 0.6547 0.4442 0.2005  -0.0402 -0.0191 408 HOH   A O   
6729 O O   A HOH   F .   ? 0.2082 0.1370 0.3102 -0.0263 0.0352  0.0009  409 HOH   A O   
6730 O O   . HOH   F .   ? 0.4868 0.4816 0.3838 0.1682  -0.1134 -0.1423 410 HOH   A O   
6731 O O   . HOH   F .   ? 0.5409 0.2706 0.4629 0.0862  0.0070  -0.0409 411 HOH   A O   
6732 O O   . HOH   F .   ? 0.3124 0.5350 0.4634 0.0055  0.1672  0.0000  412 HOH   A O   
6733 O O   B HOH   F .   ? 0.1473 0.2791 0.4287 -0.0093 0.0441  0.1419  413 HOH   A O   
6734 O O   . HOH   F .   ? 0.1707 0.2563 0.3440 -0.0052 0.0025  -0.0071 414 HOH   A O   
6735 O O   . HOH   F .   ? 0.1783 0.2253 0.2505 -0.0145 -0.0131 0.0803  415 HOH   A O   
6736 O O   . HOH   F .   ? 0.6869 0.5942 0.3864 -0.1339 0.0373  0.2347  416 HOH   A O   
6737 O O   . HOH   F .   ? 0.4751 0.3588 0.4747 0.0469  0.1522  -0.0954 417 HOH   A O   
6738 O O   . HOH   F .   ? 0.1278 0.1348 0.1770 -0.0044 -0.0163 0.0043  418 HOH   A O   
6739 O O   . HOH   F .   ? 0.8115 0.8530 0.6929 0.0055  -0.0249 -0.0577 419 HOH   A O   
6740 O O   . HOH   F .   ? 0.2055 0.1583 0.2798 -0.0021 -0.0395 0.0152  420 HOH   A O   
6741 O O   B HOH   F .   ? 0.6039 0.4169 0.4016 0.0079  0.0141  0.0337  421 HOH   A O   
6742 O O   . HOH   F .   ? 0.2428 0.1659 0.2530 0.0027  0.0157  0.0165  422 HOH   A O   
6743 O O   B HOH   F .   ? 0.4137 0.4874 0.5042 0.0185  -0.0963 -0.0957 423 HOH   A O   
6744 O O   . HOH   F .   ? 0.2710 0.2395 0.1941 -0.0618 -0.0539 0.0069  424 HOH   A O   
6745 O O   A HOH   F .   ? 0.1220 0.1302 0.2214 0.0184  -0.0447 -0.0512 425 HOH   A O   
6746 O O   . HOH   F .   ? 0.2757 0.2903 0.2054 0.0029  -0.0491 0.0178  426 HOH   A O   
6747 O O   . HOH   F .   ? 0.1480 0.1257 0.1406 -0.0183 0.0061  -0.0036 427 HOH   A O   
6748 O O   . HOH   F .   ? 0.1406 0.1629 0.2709 -0.0039 -0.0002 0.0143  428 HOH   A O   
6749 O O   . HOH   F .   ? 0.3086 0.3470 0.6849 0.0010  0.1283  -0.0407 429 HOH   A O   
6750 O O   . HOH   F .   ? 0.1921 0.2837 0.2289 -0.0009 -0.0520 0.0441  430 HOH   A O   
6751 O O   . HOH   F .   ? 0.2830 0.5766 0.1773 -0.0580 0.0591  0.0164  431 HOH   A O   
6752 O O   . HOH   F .   ? 0.1750 0.1569 0.1456 -0.0081 0.0241  0.0196  432 HOH   A O   
6753 O O   B HOH   F .   ? 0.1627 0.1508 0.1782 0.0063  -0.0055 0.0139  433 HOH   A O   
6754 O O   . HOH   F .   ? 0.1518 0.1749 0.2614 -0.0097 0.0096  0.0221  434 HOH   A O   
6755 O O   . HOH   F .   ? 0.3192 0.1169 0.2030 0.0024  -0.0502 0.0078  435 HOH   A O   
6756 O O   . HOH   F .   ? 0.4806 0.5060 0.2953 -0.0719 0.0035  0.0842  436 HOH   A O   
6757 O O   . HOH   F .   ? 0.2191 0.4154 0.2079 0.1569  -0.0002 0.0200  437 HOH   A O   
6758 O O   . HOH   F .   ? 0.6550 0.6002 0.5802 -0.1171 -0.0119 -0.1044 438 HOH   A O   
6759 O O   B HOH   F .   ? 0.1800 0.2397 0.2878 -0.0274 -0.0006 0.0971  439 HOH   A O   
6760 O O   . HOH   F .   ? 0.5051 0.6154 0.3900 0.0662  0.2493  -0.0470 440 HOH   A O   
6761 O O   . HOH   F .   ? 0.5415 0.7072 0.5574 0.0686  0.0800  0.1159  441 HOH   A O   
6762 O O   . HOH   F .   ? 0.4053 0.2131 0.5186 -0.0691 -0.2310 0.1014  442 HOH   A O   
6763 O O   . HOH   F .   ? 0.1879 0.1700 0.2762 0.0133  -0.0449 0.0237  443 HOH   A O   
6764 O O   . HOH   F .   ? 0.2965 0.2107 0.4205 -0.0461 0.1357  -0.0252 444 HOH   A O   
6765 O O   A HOH   F .   ? 0.2140 0.2258 0.1457 -0.0217 0.0675  -0.0014 445 HOH   A O   
6766 O O   . HOH   F .   ? 0.3107 0.4361 0.1981 -0.0332 -0.0390 0.0394  446 HOH   A O   
6767 O O   A HOH   F .   ? 0.1192 0.1745 0.2360 0.0244  -0.0264 0.0221  447 HOH   A O   
6768 O O   . HOH   F .   ? 0.6724 0.6889 0.6176 0.1346  -0.1087 0.0003  448 HOH   A O   
6769 O O   . HOH   F .   ? 0.4163 0.4697 0.3925 0.0063  -0.0917 0.0140  449 HOH   A O   
6770 O O   . HOH   F .   ? 0.3644 0.2545 0.1666 -0.0830 0.0485  0.0553  450 HOH   A O   
6771 O O   B HOH   F .   ? 0.1711 0.2038 0.5369 0.0113  -0.0218 0.0928  451 HOH   A O   
6772 O O   A HOH   F .   ? 0.2568 0.1728 0.3247 0.0398  0.0913  0.0295  452 HOH   A O   
6773 O O   . HOH   F .   ? 0.2336 0.1481 0.2420 0.0032  0.0092  0.0097  453 HOH   A O   
6774 O O   A HOH   F .   ? 0.5392 0.3321 0.2784 0.0162  -0.0153 0.0637  454 HOH   A O   
6775 O O   . HOH   F .   ? 0.4390 0.4676 0.4815 -0.0921 -0.1123 -0.1480 455 HOH   A O   
6776 O O   B HOH   F .   ? 0.2368 0.2292 0.2486 -0.0873 0.0361  0.0297  456 HOH   A O   
6777 O O   B HOH   F .   ? 0.1922 0.1835 0.2121 0.0403  -0.0126 -0.0336 457 HOH   A O   
6778 O O   . HOH   F .   ? 0.5740 0.5696 0.6695 -0.1254 -0.1268 -0.1227 458 HOH   A O   
6779 O O   A HOH   F .   ? 0.3172 0.4038 0.3465 -0.0270 -0.0693 -0.0249 459 HOH   A O   
6780 O O   . HOH   F .   ? 0.4191 0.4058 0.2643 0.2445  -0.0532 -0.0469 460 HOH   A O   
6781 O O   A HOH   F .   ? 0.1396 0.1427 0.1237 -0.0083 -0.0037 -0.0179 461 HOH   A O   
6782 O O   A HOH   F .   ? 0.1864 0.1607 0.1638 0.0123  0.0022  0.0019  462 HOH   A O   
6783 O O   . HOH   F .   ? 0.1960 0.2643 0.2349 0.0014  -0.0153 -0.0587 463 HOH   A O   
6784 O O   . HOH   F .   ? 0.1909 0.2307 0.4992 -0.0334 -0.1008 0.0836  464 HOH   A O   
6785 O O   . HOH   F .   ? 0.4892 0.2731 0.3922 0.0625  0.0295  0.0819  465 HOH   A O   
6786 O O   A HOH   F .   ? 0.4322 0.3532 0.3789 0.0654  0.0323  0.1225  466 HOH   A O   
6787 O O   . HOH   F .   ? 0.2356 0.1874 0.2731 0.0158  0.0242  0.0265  467 HOH   A O   
6788 O O   . HOH   F .   ? 0.6282 0.5577 0.7794 0.0549  -0.1207 0.2258  468 HOH   A O   
6789 O O   . HOH   F .   ? 0.5780 0.5262 0.4199 -0.0859 0.0645  0.0787  469 HOH   A O   
6790 O O   . HOH   F .   ? 0.5476 0.6209 0.5047 0.2281  -0.1377 0.1617  470 HOH   A O   
6791 O O   B HOH   F .   ? 0.4647 0.3885 0.3071 -0.1514 0.0291  0.0399  471 HOH   A O   
6792 O O   . HOH   F .   ? 0.4547 0.3354 0.5262 0.0632  0.0826  0.0736  472 HOH   A O   
6793 O O   . HOH   F .   ? 0.6815 0.7275 0.4520 0.0874  -0.0135 -0.0251 473 HOH   A O   
6794 O O   . HOH   F .   ? 0.2632 0.2412 0.3884 -0.0347 0.0342  -0.0839 474 HOH   A O   
6795 O O   . HOH   F .   ? 0.4085 0.4341 0.5827 0.0924  -0.0284 0.0607  475 HOH   A O   
6796 O O   . HOH   F .   ? 0.4123 0.4433 0.4708 0.0807  -0.0653 0.1152  476 HOH   A O   
6797 O O   . HOH   F .   ? 0.4183 0.5911 0.3065 -0.1150 -0.1157 0.1890  477 HOH   A O   
6798 O O   . HOH   F .   ? 0.2838 0.3028 0.3821 -0.1395 0.0896  -0.0655 478 HOH   A O   
6799 O O   . HOH   F .   ? 0.3004 0.4254 0.5292 -0.1110 0.0725  -0.2040 479 HOH   A O   
6800 O O   . HOH   F .   ? 0.6299 0.3453 0.6526 0.1119  0.0196  0.1807  480 HOH   A O   
6801 O O   . HOH   F .   ? 0.2655 0.4527 0.5078 0.0621  -0.0036 -0.2076 481 HOH   A O   
6802 O O   . HOH   F .   ? 0.2809 0.4362 0.5308 -0.0493 0.0051  -0.0208 482 HOH   A O   
6803 O O   . HOH   F .   ? 0.3496 0.5157 0.3587 0.0306  -0.0259 -0.0582 483 HOH   A O   
6804 O O   . HOH   F .   ? 0.4834 0.4685 0.5035 0.0071  0.1008  0.0486  484 HOH   A O   
6805 O O   A HOH   F .   ? 0.2298 0.2605 0.3999 0.0187  -0.0878 -0.0185 485 HOH   A O   
6806 O O   . HOH   F .   ? 0.2744 0.1665 0.2522 0.0267  -0.0954 -0.0256 486 HOH   A O   
6807 O O   . HOH   F .   ? 0.4415 0.5287 0.5376 0.0742  0.0290  -0.0472 487 HOH   A O   
6808 O O   . HOH   F .   ? 0.5804 0.6631 0.6069 -0.0580 0.1063  0.2104  488 HOH   A O   
6809 O O   . HOH   F .   ? 0.4234 0.4472 0.4177 0.1226  0.1093  0.0800  489 HOH   A O   
6810 O O   . HOH   F .   ? 0.4353 0.4643 0.5487 -0.2079 -0.0826 -0.0238 490 HOH   A O   
6811 O O   . HOH   F .   ? 0.3709 0.4440 0.2685 0.0240  0.0241  -0.0115 491 HOH   A O   
6812 O O   B HOH   F .   ? 0.4515 0.2996 0.3017 0.0894  0.0735  -0.0064 492 HOH   A O   
6813 O O   . HOH   F .   ? 0.4827 0.5534 0.5519 -0.1720 -0.1344 0.0183  493 HOH   A O   
6814 O O   . HOH   F .   ? 0.4839 0.4050 0.3224 -0.0172 -0.0875 -0.0507 494 HOH   A O   
6815 O O   B HOH   F .   ? 0.1559 0.1580 0.1726 0.0039  -0.0194 0.0007  495 HOH   A O   
6816 O O   . HOH   F .   ? 0.6285 0.5668 0.6762 -0.0664 0.0366  -0.0508 496 HOH   A O   
6817 O O   . HOH   F .   ? 0.4595 0.2725 0.3440 -0.1036 -0.1148 0.0539  497 HOH   A O   
6818 O O   . HOH   F .   ? 0.6057 0.4111 0.4287 0.0224  0.0013  -0.1191 498 HOH   A O   
6819 O O   . HOH   F .   ? 0.6622 0.6864 0.5692 0.1768  -0.1410 0.0604  499 HOH   A O   
6820 O O   . HOH   F .   ? 0.5418 0.3792 0.2994 -0.0101 0.1320  0.0092  500 HOH   A O   
6821 O O   . HOH   F .   ? 0.6102 0.5152 0.4409 -0.1130 -0.0874 -0.0797 501 HOH   A O   
6822 O O   . HOH   F .   ? 0.7394 0.3818 0.3012 -0.0096 -0.1015 0.0468  502 HOH   A O   
6823 O O   B HOH   F .   ? 0.2021 0.2135 0.4064 0.0023  -0.0857 -0.0336 503 HOH   A O   
6824 O O   B HOH   F .   ? 0.3261 0.3176 0.3252 -0.0475 0.0647  0.0693  504 HOH   A O   
6825 O O   . HOH   F .   ? 0.4225 0.3564 0.2580 -0.0794 0.1458  -0.0406 505 HOH   A O   
6826 O O   B HOH   F .   ? 0.3323 0.2367 0.4225 0.1108  0.0433  0.1283  506 HOH   A O   
6827 O O   B HOH   F .   ? 0.4360 0.1900 0.4264 -0.0670 0.1455  -0.0253 507 HOH   A O   
6828 O O   . HOH   F .   ? 0.2734 0.4828 0.3465 0.1097  0.0970  0.2150  508 HOH   A O   
6829 O O   . HOH   F .   ? 0.5521 0.6237 0.6300 0.0719  0.1574  -0.1211 509 HOH   A O   
6830 O O   . HOH   F .   ? 0.2696 0.3463 0.5027 -0.0096 0.1191  0.0826  510 HOH   A O   
6831 O O   . HOH   F .   ? 0.6054 0.6362 0.3913 -0.0419 0.0705  0.1239  511 HOH   A O   
6832 O O   . HOH   F .   ? 0.2389 0.2499 0.7132 -0.0107 -0.1199 0.0392  512 HOH   A O   
6833 O O   . HOH   F .   ? 0.4452 0.4191 0.5700 0.0026  -0.0834 0.0160  513 HOH   A O   
6834 O O   . HOH   F .   ? 0.4888 0.3421 0.4455 -0.0670 0.2020  0.0266  514 HOH   A O   
6835 O O   A HOH   F .   ? 0.1686 0.1610 0.1842 0.0145  -0.0127 -0.0307 515 HOH   A O   
6836 O O   . HOH   F .   ? 0.4212 0.2689 0.4296 -0.0736 -0.0016 0.0914  516 HOH   A O   
6837 O O   . HOH   F .   ? 0.2780 0.2044 0.4990 -0.0020 0.0209  0.0936  517 HOH   A O   
6838 O O   . HOH   F .   ? 0.6025 0.2488 0.4040 -0.0826 0.0040  0.0652  518 HOH   A O   
6839 O O   . HOH   F .   ? 0.2720 0.3320 0.4707 -0.0090 0.1117  -0.0493 519 HOH   A O   
6840 O O   . HOH   F .   ? 0.4600 0.2411 0.3748 -0.1340 0.0095  0.0232  520 HOH   A O   
6841 O O   . HOH   F .   ? 0.3696 0.7730 0.5081 -0.0651 -0.0420 0.1846  521 HOH   A O   
6842 O O   . HOH   F .   ? 0.2163 0.2705 0.3482 0.0218  -0.0302 0.0603  522 HOH   A O   
6843 O O   B HOH   F .   ? 0.2491 0.3213 0.3106 0.0920  0.0793  0.1358  523 HOH   A O   
6844 O O   . HOH   F .   ? 0.6245 0.4363 0.5968 0.1029  0.1330  -0.0100 524 HOH   A O   
6845 O O   . HOH   F .   ? 0.2339 0.3921 0.3848 0.0101  -0.0218 -0.0061 525 HOH   A O   
6846 O O   . HOH   F .   ? 0.4821 0.6532 0.5040 0.0261  -0.0944 -0.0133 526 HOH   A O   
6847 O O   . HOH   F .   ? 0.3022 0.4258 0.2929 -0.0114 -0.0230 -0.0764 527 HOH   A O   
6848 O O   . HOH   F .   ? 0.5115 0.6347 0.5211 0.3071  -0.0282 0.0697  528 HOH   A O   
6849 O O   . HOH   F .   ? 0.2781 0.2322 0.4892 0.0172  0.0493  0.0595  529 HOH   A O   
6850 O O   B HOH   F .   ? 0.2786 0.2622 0.3701 -0.0019 0.1327  0.0721  530 HOH   A O   
6851 O O   B HOH   F .   ? 0.3074 0.2501 0.5821 0.0413  0.0330  -0.0121 531 HOH   A O   
6852 O O   A HOH   F .   ? 0.4243 0.5071 0.3305 0.1598  0.0366  -0.0446 532 HOH   A O   
6853 O O   T HOH   F .   ? 0.0421 0.0884 0.1198 0.0022  0.0029  0.0601  533 HOH   A O   
6854 O O   . HOH   F .   ? 0.4832 0.5447 0.4602 -0.0387 -0.0223 -0.1399 534 HOH   A O   
6855 O O   . HOH   F .   ? 0.3864 0.7317 0.5624 0.1066  0.0547  -0.0999 535 HOH   A O   
6856 O O   . HOH   F .   ? 0.4634 0.6698 0.5253 -0.0828 -0.0570 0.0287  536 HOH   A O   
6857 O O   . HOH   F .   ? 0.4797 0.5280 0.4594 0.0673  0.0054  0.0773  537 HOH   A O   
6858 O O   . HOH   F .   ? 0.3738 0.4340 0.5738 0.0170  -0.1149 0.2439  538 HOH   A O   
6859 O O   . HOH   G .   ? 0.3415 0.4314 0.4639 -0.0814 0.0468  -0.1472 201 HOH   B O   
6860 O O   . HOH   G .   ? 0.2226 0.2199 0.2959 0.0139  0.0901  0.0246  202 HOH   B O   
6861 O O   . HOH   G .   ? 0.4858 0.4204 0.3000 0.0282  -0.1111 -0.1421 203 HOH   B O   
6862 O O   . HOH   G .   ? 0.4271 0.4250 0.6264 -0.0177 -0.1229 0.2786  204 HOH   B O   
6863 O O   . HOH   G .   ? 0.6056 0.4914 0.5586 0.1182  0.1071  -0.0155 205 HOH   B O   
6864 O O   . HOH   G .   ? 0.3902 0.2928 0.3644 -0.0609 0.0074  -0.0983 206 HOH   B O   
6865 O O   . HOH   G .   ? 0.6415 0.2483 0.4171 0.0749  0.0442  -0.0174 207 HOH   B O   
6866 O O   . HOH   G .   ? 0.3117 0.6452 0.3584 0.0182  0.0041  0.2429  208 HOH   B O   
6867 O O   . HOH   G .   ? 0.4124 0.4909 0.3846 0.2172  -0.0689 0.0110  209 HOH   B O   
6868 O O   . HOH   G .   ? 0.3273 0.5043 0.3976 0.2254  0.0384  -0.0044 210 HOH   B O   
6869 O O   . HOH   G .   ? 0.2912 0.2906 0.6681 0.0760  -0.1118 0.0701  211 HOH   B O   
6870 O O   . HOH   G .   ? 0.2553 0.4726 0.4567 -0.0436 0.1244  -0.2153 212 HOH   B O   
6871 O O   . HOH   G .   ? 0.3157 0.4858 0.5936 -0.0717 0.0201  -0.0695 213 HOH   B O   
6872 O O   . HOH   G .   ? 0.4061 0.5683 0.3259 0.2355  -0.1188 -0.0619 214 HOH   B O   
6873 O O   . HOH   G .   ? 0.1806 0.2341 0.2789 0.0003  0.0275  -0.0064 215 HOH   B O   
6874 O O   . HOH   G .   ? 0.4945 0.5252 0.6146 0.0116  -0.1471 -0.1163 216 HOH   B O   
6875 O O   . HOH   G .   ? 0.1510 0.1794 0.2460 -0.0170 0.0011  -0.0063 217 HOH   B O   
6876 O O   . HOH   G .   ? 0.4093 0.3886 0.3736 -0.0186 -0.1223 0.0945  218 HOH   B O   
6877 O O   . HOH   G .   ? 0.4558 0.1902 0.2984 -0.0057 -0.0718 0.0024  219 HOH   B O   
6878 O O   . HOH   G .   ? 0.6307 0.3190 0.4006 -0.1938 0.0568  0.0303  220 HOH   B O   
6879 O O   . HOH   G .   ? 0.2539 0.2512 0.5216 -0.0043 0.0288  0.0178  221 HOH   B O   
6880 O O   . HOH   G .   ? 0.3342 0.5773 0.3448 0.1415  -0.0028 -0.0171 222 HOH   B O   
6881 O O   . HOH   G .   ? 0.4612 0.4306 0.3859 0.0694  0.0481  -0.1839 223 HOH   B O   
6882 O O   . HOH   G .   ? 0.3991 0.2526 0.3910 0.1017  -0.0268 -0.0497 224 HOH   B O   
6883 O O   . HOH   G .   ? 0.2177 0.2062 0.3552 -0.0429 -0.0188 -0.0573 225 HOH   B O   
6884 O O   . HOH   G .   ? 0.5911 0.5842 0.3257 0.1633  0.0443  0.0732  226 HOH   B O   
6885 O O   . HOH   G .   ? 0.1621 0.1917 0.2721 -0.0090 0.0038  0.0028  227 HOH   B O   
6886 O O   . HOH   G .   ? 0.2457 0.1732 0.2587 -0.0265 0.1137  -0.0104 228 HOH   B O   
6887 O O   . HOH   G .   ? 0.4101 0.2910 0.3128 -0.0735 0.0369  -0.0441 229 HOH   B O   
6888 O O   . HOH   G .   ? 0.2741 0.4300 0.5092 0.0690  -0.1207 0.0659  230 HOH   B O   
6889 O O   . HOH   G .   ? 0.2134 0.1234 0.3460 0.0156  -0.0824 -0.0313 231 HOH   B O   
6890 O O   . HOH   G .   ? 0.2113 0.2858 0.6017 0.0677  -0.0593 -0.0908 232 HOH   B O   
6891 O O   . HOH   G .   ? 0.3647 0.1643 0.2137 0.0134  -0.0712 -0.0048 233 HOH   B O   
6892 O O   . HOH   G .   ? 0.2744 0.3552 0.2881 -0.0908 0.0597  -0.0826 234 HOH   B O   
6893 O O   . HOH   G .   ? 0.2005 0.4066 0.2457 -0.0371 -0.0269 0.0678  235 HOH   B O   
6894 O O   . HOH   G .   ? 0.3878 0.3393 0.2141 0.0438  0.0637  0.0628  236 HOH   B O   
6895 O O   . HOH   G .   ? 0.2673 0.2441 0.3122 0.0339  0.0374  -0.0951 237 HOH   B O   
6896 O O   . HOH   G .   ? 0.1330 0.1332 0.1631 -0.0142 -0.0136 -0.0002 238 HOH   B O   
6897 O O   . HOH   G .   ? 0.3473 0.4076 0.4473 -0.1494 -0.0258 0.0489  239 HOH   B O   
6898 O O   . HOH   G .   ? 0.4765 0.3106 0.3982 -0.2200 -0.0217 0.0188  240 HOH   B O   
6899 O O   . HOH   G .   ? 0.2219 0.1994 0.1725 0.0082  -0.0109 0.0036  241 HOH   B O   
6900 O O   . HOH   G .   ? 0.2905 0.1922 0.3718 0.0015  0.0994  -0.0053 242 HOH   B O   
6901 O O   . HOH   G .   ? 0.3731 0.2903 0.4212 0.0629  -0.1203 -0.1710 243 HOH   B O   
6902 O O   . HOH   G .   ? 0.2136 0.3834 0.2972 -0.0464 -0.0669 -0.0405 244 HOH   B O   
6903 O O   . HOH   G .   ? 0.2897 0.2024 0.5237 0.0321  0.1886  0.0975  245 HOH   B O   
6904 O O   . HOH   G .   ? 0.1379 0.1208 0.1477 -0.0003 -0.0050 0.0037  246 HOH   B O   
6905 O O   . HOH   G .   ? 0.3069 0.1670 0.5670 -0.0258 -0.1284 -0.0248 247 HOH   B O   
6906 O O   . HOH   G .   ? 0.2827 0.3534 0.3060 -0.0841 -0.0342 -0.0374 248 HOH   B O   
6907 O O   . HOH   G .   ? 0.2080 0.2238 0.2810 -0.0554 0.0232  -0.0333 249 HOH   B O   
6908 O O   . HOH   G .   ? 0.1499 0.1370 0.2386 -0.0025 0.0010  -0.0187 250 HOH   B O   
6909 O O   . HOH   G .   ? 0.5842 0.4565 0.4655 0.1539  0.0173  -0.0830 251 HOH   B O   
6910 O O   . HOH   G .   ? 0.2218 0.1865 0.1936 -0.0261 -0.0519 0.0045  252 HOH   B O   
6911 O O   . HOH   G .   ? 0.1651 0.2708 0.2393 0.0499  0.0411  0.0871  253 HOH   B O   
6912 O O   . HOH   G .   ? 0.4392 0.3296 0.2386 0.0829  0.0577  -0.0176 254 HOH   B O   
6913 O O   . HOH   G .   ? 0.2327 0.2010 0.2489 0.0769  -0.0742 -0.0663 255 HOH   B O   
6914 O O   . HOH   G .   ? 0.1928 0.1386 0.1995 -0.0269 -0.0276 0.0216  256 HOH   B O   
6915 O O   . HOH   G .   ? 0.1473 0.1643 0.2487 -0.0220 -0.0127 0.0065  257 HOH   B O   
6916 O O   . HOH   G .   ? 0.1294 0.1478 0.1891 -0.0064 0.0040  0.0024  258 HOH   B O   
6917 O O   . HOH   G .   ? 0.2874 0.2072 0.2978 0.0940  0.0862  0.0157  259 HOH   B O   
6918 O O   . HOH   G .   ? 0.2487 0.3905 0.5100 0.0043  0.0400  -0.0919 260 HOH   B O   
6919 O O   . HOH   G .   ? 0.3064 0.4478 0.3714 -0.0427 -0.1064 0.0880  261 HOH   B O   
6920 O O   . HOH   G .   ? 0.2832 0.2180 0.2914 -0.0282 0.0029  -0.0503 262 HOH   B O   
6921 O O   . HOH   G .   ? 0.1935 0.1804 0.3326 0.0041  -0.0482 -0.0267 263 HOH   B O   
6922 O O   . HOH   G .   ? 0.3156 0.3384 0.2070 0.0363  0.0651  0.0030  264 HOH   B O   
6923 O O   . HOH   G .   ? 0.1708 0.1718 0.1467 -0.0408 -0.0270 0.0046  265 HOH   B O   
6924 O O   . HOH   G .   ? 0.2312 0.3398 0.2249 -0.0701 0.0246  0.0864  266 HOH   B O   
6925 O O   . HOH   G .   ? 0.2683 0.1974 0.2790 -0.0736 0.0120  -0.0177 267 HOH   B O   
6926 O O   . HOH   G .   ? 0.2288 0.3512 0.3571 0.0194  0.1060  0.0143  268 HOH   B O   
6927 O O   . HOH   G .   ? 0.2155 0.2093 0.1747 -0.0000 -0.0091 0.0079  269 HOH   B O   
6928 O O   . HOH   G .   ? 0.1640 0.1288 0.3950 -0.0086 -0.0230 -0.0074 270 HOH   B O   
6929 O O   . HOH   G .   ? 0.1882 0.1415 0.2234 -0.0243 -0.0033 0.0166  271 HOH   B O   
6930 O O   . HOH   G .   ? 0.5427 0.3475 0.2728 0.2399  0.0717  0.0697  272 HOH   B O   
6931 O O   . HOH   G .   ? 0.2473 0.2871 0.2338 -0.0434 -0.0763 0.0040  273 HOH   B O   
6932 O O   . HOH   G .   ? 0.1560 0.1461 0.3132 -0.0201 0.0033  0.0071  274 HOH   B O   
6933 O O   . HOH   G .   ? 0.2455 0.2759 0.4369 -0.0042 -0.0160 -0.1274 275 HOH   B O   
6934 O O   . HOH   G .   ? 0.4612 0.3054 0.2524 0.0675  -0.0329 -0.0609 276 HOH   B O   
6935 O O   . HOH   G .   ? 0.4461 0.5366 0.2204 0.1293  -0.0594 -0.0253 277 HOH   B O   
6936 O O   . HOH   G .   ? 0.2056 0.4520 0.4423 -0.0549 -0.0260 -0.1136 278 HOH   B O   
6937 O O   . HOH   G .   ? 0.2861 0.6114 0.6964 0.1328  -0.0266 -0.0847 279 HOH   B O   
6938 O O   . HOH   G .   ? 0.2663 0.2079 0.5080 0.0105  0.0577  0.0348  280 HOH   B O   
6939 O O   . HOH   G .   ? 0.2351 0.2373 0.2264 -0.0395 -0.0679 -0.0323 281 HOH   B O   
6940 O O   . HOH   G .   ? 0.2169 0.2479 0.2222 0.0512  -0.0170 -0.0255 282 HOH   B O   
6941 O O   . HOH   G .   ? 0.3935 0.2594 0.4068 -0.0195 -0.1067 -0.0468 283 HOH   B O   
6942 O O   . HOH   G .   ? 0.4168 0.5738 0.2341 0.0291  -0.0598 0.0919  284 HOH   B O   
6943 O O   . HOH   G .   ? 0.2426 0.4931 0.4615 -0.0937 -0.1158 0.0995  285 HOH   B O   
6944 O O   . HOH   G .   ? 0.3610 0.2870 0.2201 0.0576  -0.0721 -0.0243 286 HOH   B O   
6945 O O   . HOH   G .   ? 0.2050 0.3011 0.3140 -0.0437 0.0495  -0.1158 287 HOH   B O   
6946 O O   . HOH   G .   ? 0.4407 0.2830 0.4618 -0.0955 0.0424  0.0667  288 HOH   B O   
6947 O O   . HOH   G .   ? 0.1494 0.1397 0.1605 0.0046  -0.0057 0.0014  289 HOH   B O   
6948 O O   . HOH   G .   ? 0.3002 0.2409 0.2570 -0.0042 0.0149  -0.1079 290 HOH   B O   
6949 O O   . HOH   G .   ? 0.2186 0.2447 0.2916 0.0228  -0.0745 0.0080  291 HOH   B O   
6950 O O   . HOH   G .   ? 0.2431 0.7228 0.2299 0.0545  -0.0302 -0.0366 292 HOH   B O   
6951 O O   . HOH   G .   ? 0.1583 0.3087 0.4596 0.0235  0.0023  -0.1241 293 HOH   B O   
6952 O O   . HOH   G .   ? 0.6178 0.4971 0.4516 -0.1073 0.0025  0.0829  294 HOH   B O   
6953 O O   . HOH   G .   ? 0.2917 0.6626 0.3980 0.1185  -0.0545 0.1767  295 HOH   B O   
6954 O O   . HOH   G .   ? 0.1479 0.1816 0.2704 0.0181  -0.0081 0.0218  296 HOH   B O   
6955 O O   . HOH   G .   ? 0.2573 0.4060 0.4243 -0.0705 -0.1396 0.1291  297 HOH   B O   
6956 O O   . HOH   G .   ? 0.1537 0.1997 0.1463 -0.0111 -0.0150 0.0028  298 HOH   B O   
6957 O O   . HOH   G .   ? 0.3723 0.1777 0.3312 0.0720  0.1460  0.0481  299 HOH   B O   
6958 O O   . HOH   G .   ? 0.3593 0.2121 0.4167 -0.0914 -0.2103 0.0744  300 HOH   B O   
6959 O O   . HOH   G .   ? 0.3145 0.3792 0.4552 0.1140  -0.0607 -0.0989 301 HOH   B O   
6960 O O   . HOH   G .   ? 0.4293 0.6189 0.5328 0.0455  -0.1527 0.0351  302 HOH   B O   
6961 O O   . HOH   G .   ? 0.1585 0.1349 0.2635 0.0078  -0.0063 -0.0056 303 HOH   B O   
6962 O O   . HOH   G .   ? 0.1593 0.1414 0.2317 0.0006  -0.0066 0.0172  304 HOH   B O   
6963 O O   . HOH   G .   ? 0.1939 0.2626 0.5422 0.0468  -0.0386 -0.0821 305 HOH   B O   
6964 O O   . HOH   G .   ? 0.4842 0.3775 0.2611 0.1670  -0.0970 0.0369  306 HOH   B O   
6965 O O   . HOH   G .   ? 0.2070 0.1514 0.2918 0.0310  -0.0921 0.0071  307 HOH   B O   
6966 O O   . HOH   G .   ? 0.2324 0.5181 0.4502 -0.0881 -0.0337 -0.0601 308 HOH   B O   
6967 O O   . HOH   G .   ? 0.2861 0.2651 0.4889 -0.0284 -0.0755 0.0869  309 HOH   B O   
6968 O O   . HOH   G .   ? 0.2102 0.1500 0.2554 -0.0149 -0.0333 -0.0080 310 HOH   B O   
6969 O O   . HOH   G .   ? 0.4185 0.2432 0.2653 0.1630  0.1065  0.0358  311 HOH   B O   
6970 O O   . HOH   G .   ? 0.2469 0.2949 0.3971 -0.0797 0.0907  -0.0462 312 HOH   B O   
6971 O O   . HOH   G .   ? 0.3260 0.3250 0.6786 0.0040  -0.0746 0.1567  313 HOH   B O   
6972 O O   . HOH   G .   ? 0.4119 0.4426 0.2125 0.0198  0.0383  0.0554  314 HOH   B O   
6973 O O   . HOH   G .   ? 0.2037 0.1940 0.1759 -0.0072 0.0300  0.0173  315 HOH   B O   
6974 O O   . HOH   G .   ? 0.4121 0.3266 0.4589 0.0702  0.1693  0.1453  316 HOH   B O   
6975 O O   . HOH   G .   ? 0.2312 0.1379 0.2502 -0.0125 -0.0085 0.0364  317 HOH   B O   
6976 O O   . HOH   G .   ? 0.5392 0.2846 0.2546 -0.1868 0.1117  -0.0202 318 HOH   B O   
6977 O O   . HOH   G .   ? 0.2514 0.2773 0.3266 -0.0329 0.0793  -0.0608 319 HOH   B O   
6978 O O   . HOH   G .   ? 0.5254 0.4279 0.5576 0.1733  0.1087  -0.0009 320 HOH   B O   
6979 O O   . HOH   G .   ? 0.2198 0.3131 0.4889 -0.0374 -0.0217 0.0346  321 HOH   B O   
6980 O O   . HOH   G .   ? 0.1475 0.1714 0.2666 -0.0232 -0.0116 0.0124  322 HOH   B O   
6981 O O   . HOH   G .   ? 0.4000 0.2340 0.2771 0.0306  0.0361  0.0707  323 HOH   B O   
6982 O O   . HOH   G .   ? 0.7432 0.1913 0.2824 -0.0063 -0.0642 0.0046  324 HOH   B O   
6983 O O   . HOH   G .   ? 0.1458 0.1589 0.2732 -0.0133 -0.0136 -0.0059 325 HOH   B O   
6984 O O   . HOH   G .   ? 0.2554 0.2127 0.2203 0.0119  -0.0146 0.0133  326 HOH   B O   
6985 O O   . HOH   G .   ? 0.1554 0.2709 0.2466 -0.0106 -0.0212 0.0601  327 HOH   B O   
6986 O O   . HOH   G .   ? 0.6732 0.6945 0.5506 0.3387  -0.0064 -0.0497 328 HOH   B O   
6987 O O   . HOH   G .   ? 0.3866 0.3494 0.5763 0.0892  -0.0204 0.0778  329 HOH   B O   
6988 O O   . HOH   G .   ? 0.1755 0.1837 0.2926 0.0345  0.0409  0.0218  330 HOH   B O   
6989 O O   . HOH   G .   ? 0.4399 0.4582 0.2264 0.0743  -0.0310 -0.0611 331 HOH   B O   
6990 O O   . HOH   G .   ? 0.5520 0.4310 0.6089 0.0980  -0.0509 0.1598  332 HOH   B O   
6991 O O   . HOH   G .   ? 0.2199 0.2160 0.5343 -0.0479 -0.0140 0.1256  333 HOH   B O   
6992 O O   . HOH   G .   ? 0.2459 0.1983 0.4558 -0.0035 0.0042  0.0215  334 HOH   B O   
6993 O O   . HOH   G .   ? 0.5602 0.3139 0.3971 0.0346  0.0591  -0.1583 335 HOH   B O   
6994 O O   . HOH   G .   ? 0.5123 0.5540 0.3253 -0.0515 -0.1025 0.0536  336 HOH   B O   
6995 O O   . HOH   G .   ? 0.1571 0.2457 0.2798 0.0160  -0.0136 -0.0497 337 HOH   B O   
6996 O O   . HOH   G .   ? 0.5094 0.4210 0.4993 -0.0223 -0.0150 -0.0988 338 HOH   B O   
6997 O O   . HOH   G .   ? 0.3935 0.7212 0.3462 -0.0301 -0.0255 0.1676  339 HOH   B O   
6998 O O   . HOH   G .   ? 0.5238 0.3538 0.3337 -0.0290 0.0704  0.1163  340 HOH   B O   
6999 O O   . HOH   G .   ? 0.1657 0.1361 0.2122 0.0039  -0.0227 0.0036  341 HOH   B O   
7000 O O   . HOH   G .   ? 0.4215 0.3557 0.3320 0.0636  -0.1177 -0.0643 342 HOH   B O   
7001 O O   . HOH   G .   ? 0.3853 0.6182 0.4106 -0.1350 -0.1297 -0.0800 343 HOH   B O   
7002 O O   . HOH   G .   ? 0.2020 0.1943 0.2536 -0.0055 0.0481  -0.0277 344 HOH   B O   
7003 O O   . HOH   G .   ? 0.6067 0.5324 0.2531 -0.0051 -0.0237 0.0978  345 HOH   B O   
7004 O O   . HOH   G .   ? 0.5163 0.5446 0.4319 -0.1226 0.1132  0.0643  346 HOH   B O   
7005 O O   . HOH   G .   ? 0.2285 0.3729 0.5112 0.0460  0.0428  0.0435  347 HOH   B O   
7006 O O   . HOH   G .   ? 0.2642 0.2283 0.4772 -0.0334 -0.0853 -0.0556 348 HOH   B O   
7007 O O   . HOH   G .   ? 0.1802 0.4476 0.5261 0.0280  0.0550  0.0547  349 HOH   B O   
7008 O O   . HOH   G .   ? 0.3759 0.4684 0.5370 0.0385  -0.0937 0.0350  350 HOH   B O   
7009 O O   . HOH   G .   ? 0.3250 0.3871 0.4929 -0.1147 0.0092  -0.0358 351 HOH   B O   
7010 O O   . HOH   G .   ? 0.2348 0.5664 0.4114 0.1497  -0.0571 -0.1465 352 HOH   B O   
7011 O O   . HOH   G .   ? 0.4565 0.4674 0.5744 -0.0050 0.0001  -0.0149 353 HOH   B O   
7012 O O   . HOH   G .   ? 0.3961 0.2224 0.3506 -0.0961 0.0570  -0.1133 354 HOH   B O   
7013 O O   . HOH   G .   ? 0.4771 0.3649 0.4221 0.1001  0.1218  -0.0584 355 HOH   B O   
7014 O O   . HOH   G .   ? 0.4350 0.3011 0.5379 -0.0965 0.1106  0.0732  356 HOH   B O   
7015 O O   . HOH   G .   ? 0.3694 0.2554 0.3487 -0.0830 -0.0094 -0.0574 357 HOH   B O   
7016 O O   . HOH   G .   ? 0.3069 0.1822 0.3830 0.0356  -0.1157 -0.0562 358 HOH   B O   
7017 O O   . HOH   G .   ? 0.5161 0.5402 0.5169 -0.1028 -0.0786 0.0742  359 HOH   B O   
7018 O O   . HOH   G .   ? 0.4602 0.4925 0.4866 0.1680  -0.1301 0.1442  360 HOH   B O   
7019 O O   . HOH   G .   ? 0.4158 0.3258 0.4931 0.0140  -0.1646 0.0028  361 HOH   B O   
7020 O O   . HOH   G .   ? 0.4112 0.4013 0.6412 0.0108  0.1188  0.0888  362 HOH   B O   
7021 O O   . HOH   G .   ? 0.4840 0.6665 0.3100 0.2001  -0.0050 0.0566  363 HOH   B O   
7022 O O   . HOH   G .   ? 0.2137 0.3705 0.6156 -0.0727 -0.0632 -0.0765 364 HOH   B O   
7023 O O   . HOH   G .   ? 0.4500 0.3483 0.5291 0.1067  -0.1513 -0.0089 365 HOH   B O   
7024 O O   . HOH   G .   ? 0.5319 0.4515 0.4692 0.0856  0.0843  0.0606  366 HOH   B O   
7025 O O   . HOH   G .   ? 0.4209 0.3275 0.4996 -0.1270 -0.0533 0.0347  367 HOH   B O   
7026 O O   . HOH   G .   ? 0.5042 0.5401 0.3696 0.0938  -0.1433 0.0997  368 HOH   B O   
7027 O O   . HOH   G .   ? 0.4727 0.6084 0.4752 -0.1081 -0.0943 -0.1125 369 HOH   B O   
7028 O O   . HOH   G .   ? 0.7415 0.7362 0.5329 0.2290  -0.1192 0.0938  370 HOH   B O   
7029 O O   . HOH   G .   ? 0.5248 0.2109 0.3196 0.0136  -0.0140 0.0488  371 HOH   B O   
7030 O O   . HOH   G .   ? 0.4440 0.5836 0.5287 0.2742  0.0958  0.1319  372 HOH   B O   
7031 O O   . HOH   G .   ? 0.4591 0.3589 0.3864 0.0737  -0.1460 -0.0513 373 HOH   B O   
7032 O O   . HOH   G .   ? 0.6118 0.3995 0.2823 -0.1629 -0.0987 -0.0049 374 HOH   B O   
7033 O O   . HOH   G .   ? 0.3985 0.5620 0.4585 -0.1465 -0.0240 0.0657  375 HOH   B O   
7034 O O   . HOH   G .   ? 0.2239 0.4806 0.4332 0.0365  -0.0515 -0.0818 376 HOH   B O   
7035 O O   . HOH   G .   ? 0.7389 0.3802 0.5437 -0.0592 -0.0479 -0.0200 377 HOH   B O   
7036 O O   . HOH   G .   ? 0.5564 0.7163 0.3996 -0.1433 0.0458  -0.1416 378 HOH   B O   
7037 O O   . HOH   G .   ? 0.4710 0.6158 0.6607 0.1402  0.0341  0.2342  379 HOH   B O   
7038 O O   . HOH   G .   ? 0.3527 0.3765 0.2204 0.0558  0.0595  0.0083  380 HOH   B O   
7039 O O   . HOH   G .   ? 0.6287 0.7689 0.6446 -0.0115 0.1639  0.0971  381 HOH   B O   
7040 O O   . HOH   G .   ? 0.3234 0.4002 0.4149 0.1274  0.0100  0.0237  382 HOH   B O   
7041 O O   . HOH   G .   ? 0.3155 0.2500 0.2827 -0.0109 0.0105  0.0280  383 HOH   B O   
7042 O O   . HOH   G .   ? 0.6103 0.4182 0.4407 0.0314  0.0364  -0.1363 384 HOH   B O   
7043 O O   . HOH   G .   ? 0.3054 0.7379 0.5363 0.1140  0.1325  0.0869  385 HOH   B O   
7044 O O   . HOH   G .   ? 0.5376 0.4459 0.4647 -0.0901 0.0156  -0.0220 386 HOH   B O   
7045 O O   . HOH   G .   ? 0.5239 0.4798 0.4374 0.0512  -0.0997 -0.0240 387 HOH   B O   
7046 O O   . HOH   G .   ? 0.2342 0.4419 0.3615 -0.0828 -0.0920 -0.0249 388 HOH   B O   
7047 O O   . HOH   G .   ? 0.4785 0.3539 0.2782 0.0009  0.0430  -0.0258 389 HOH   B O   
7048 O O   . HOH   G .   ? 0.6440 0.5518 0.4149 0.1634  0.0336  0.0773  390 HOH   B O   
7049 O O   . HOH   G .   ? 0.3164 0.2165 0.3193 0.0433  -0.0197 0.0027  391 HOH   B O   
7050 O O   . HOH   G .   ? 0.4374 0.3743 0.3779 -0.0426 0.0111  0.0413  392 HOH   B O   
7051 O O   . HOH   G .   ? 0.2452 0.3346 0.6032 -0.1120 -0.0553 0.0394  393 HOH   B O   
7052 O O   . HOH   G .   ? 0.3745 0.2185 0.5372 -0.0145 0.0786  0.0633  394 HOH   B O   
7053 O O   . HOH   G .   ? 0.3998 0.4401 0.3812 -0.0503 0.0978  0.0980  395 HOH   B O   
7054 O O   . HOH   G .   ? 0.6327 0.6706 0.7416 0.1291  -0.0116 0.2069  396 HOH   B O   
7055 O O   . HOH   G .   ? 0.4290 0.5501 0.3679 0.0906  -0.0264 -0.0893 397 HOH   B O   
7056 O O   . HOH   G .   ? 0.1966 0.2482 0.5798 -0.0531 -0.0940 0.0216  398 HOH   B O   
7057 O O   . HOH   G .   ? 0.3021 0.3067 0.3672 0.0302  0.0148  -0.0099 399 HOH   B O   
7058 O O   . HOH   G .   ? 0.5407 0.4076 0.3109 -0.2250 -0.0399 0.1177  400 HOH   B O   
7059 O O   . HOH   G .   ? 0.5346 0.5945 0.3556 0.1480  0.0477  0.0005  401 HOH   B O   
# 
