data_7HE0
# 
_entry.id   7HE0 
# 
_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   7HE0         pdb_00007he0 10.2210/pdb7he0/pdb 
WWPDB D_1001407354 ?            ?                   
# 
_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                        7HE0 
_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 '(R)-phenyl[(2R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' 294.351   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                35.453    1   ? ? ? ? 
5 water       nat water                                                                         18.015    427 ? ? ? ? 
# 
_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 '(R)-phenyl[(2R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' A1A9A 
4 'CHLORIDE ION'                                                                CL    
5 water                                                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A9A non-polymer         . '(R)-phenyl[(2R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' ? 'C17 H18 N4 O'   
294.351 
ALA   'L-peptide linking' y ALANINE                                                                       ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                      ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                    ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                               ? 'C4 H7 N O4'     
133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                                ? 'Cl -1'          
35.453  
CYS   'L-peptide linking' y CYSTEINE                                                                      ? 'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                     ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                               ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                       ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                     ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                         ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                    ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                       ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                        ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                    ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                 ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                       ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                        ? 'C3 H7 N O3'     
105.093 
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 A1A9A 1   202 201  A1A9A LA1 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 153  HOH   HOH A . 
F 5 HOH   2   302 292  HOH   HOH A . 
F 5 HOH   3   303 247  HOH   HOH A . 
F 5 HOH   4   304 229  HOH   HOH A . 
F 5 HOH   5   305 1290 HOH   HOH A . 
F 5 HOH   6   306 625  HOH   HOH A . 
F 5 HOH   7   307 196  HOH   HOH A . 
F 5 HOH   8   308 17   HOH   HOH A . 
F 5 HOH   9   309 2    HOH   HOH A . 
F 5 HOH   10  310 1283 HOH   HOH A . 
F 5 HOH   11  311 409  HOH   HOH A . 
F 5 HOH   12  312 209  HOH   HOH A . 
F 5 HOH   13  313 19   HOH   HOH A . 
F 5 HOH   14  314 337  HOH   HOH A . 
F 5 HOH   15  315 151  HOH   HOH A . 
F 5 HOH   16  316 76   HOH   HOH A . 
F 5 HOH   17  317 57   HOH   HOH A . 
F 5 HOH   18  318 109  HOH   HOH A . 
F 5 HOH   19  319 96   HOH   HOH A . 
F 5 HOH   20  320 155  HOH   HOH A . 
F 5 HOH   21  321 74   HOH   HOH A . 
F 5 HOH   22  322 1295 HOH   HOH A . 
F 5 HOH   23  323 136  HOH   HOH A . 
F 5 HOH   24  324 281  HOH   HOH A . 
F 5 HOH   25  325 661  HOH   HOH A . 
F 5 HOH   26  326 39   HOH   HOH A . 
F 5 HOH   27  327 15   HOH   HOH A . 
F 5 HOH   28  328 241  HOH   HOH A . 
F 5 HOH   29  329 192  HOH   HOH A . 
F 5 HOH   30  330 225  HOH   HOH A . 
F 5 HOH   31  331 105  HOH   HOH A . 
F 5 HOH   32  332 86   HOH   HOH A . 
F 5 HOH   33  333 124  HOH   HOH A . 
F 5 HOH   34  334 1300 HOH   HOH A . 
F 5 HOH   35  335 6    HOH   HOH A . 
F 5 HOH   36  336 5    HOH   HOH A . 
F 5 HOH   37  337 236  HOH   HOH A . 
F 5 HOH   38  338 140  HOH   HOH A . 
F 5 HOH   39  339 34   HOH   HOH A . 
F 5 HOH   40  340 165  HOH   HOH A . 
F 5 HOH   41  341 964  HOH   HOH A . 
F 5 HOH   42  342 405  HOH   HOH A . 
F 5 HOH   43  343 92   HOH   HOH A . 
F 5 HOH   44  344 140  HOH   HOH A . 
F 5 HOH   45  345 164  HOH   HOH A . 
F 5 HOH   46  346 115  HOH   HOH A . 
F 5 HOH   47  347 33   HOH   HOH A . 
F 5 HOH   48  348 8    HOH   HOH A . 
F 5 HOH   49  349 469  HOH   HOH A . 
F 5 HOH   50  350 169  HOH   HOH A . 
F 5 HOH   51  351 102  HOH   HOH A . 
F 5 HOH   52  352 320  HOH   HOH A . 
F 5 HOH   53  353 21   HOH   HOH A . 
F 5 HOH   54  354 42   HOH   HOH A . 
F 5 HOH   55  355 17   HOH   HOH A . 
F 5 HOH   56  356 49   HOH   HOH A . 
F 5 HOH   57  357 162  HOH   HOH A . 
F 5 HOH   58  358 630  HOH   HOH A . 
F 5 HOH   59  359 939  HOH   HOH A . 
F 5 HOH   60  360 93   HOH   HOH A . 
F 5 HOH   61  361 396  HOH   HOH A . 
F 5 HOH   62  362 81   HOH   HOH A . 
F 5 HOH   63  363 354  HOH   HOH A . 
F 5 HOH   64  364 18   HOH   HOH A . 
F 5 HOH   65  365 1308 HOH   HOH A . 
F 5 HOH   66  366 2    HOH   HOH A . 
F 5 HOH   67  367 186  HOH   HOH A . 
F 5 HOH   68  368 19   HOH   HOH A . 
F 5 HOH   69  369 159  HOH   HOH A . 
F 5 HOH   70  370 36   HOH   HOH A . 
F 5 HOH   71  371 381  HOH   HOH A . 
F 5 HOH   72  372 138  HOH   HOH A . 
F 5 HOH   73  373 66   HOH   HOH A . 
F 5 HOH   74  374 139  HOH   HOH A . 
F 5 HOH   75  375 1238 HOH   HOH A . 
F 5 HOH   76  376 56   HOH   HOH A . 
F 5 HOH   77  377 9    HOH   HOH A . 
F 5 HOH   78  378 45   HOH   HOH A . 
F 5 HOH   79  379 5    HOH   HOH A . 
F 5 HOH   80  380 366  HOH   HOH A . 
F 5 HOH   81  381 134  HOH   HOH A . 
F 5 HOH   82  382 18   HOH   HOH A . 
F 5 HOH   83  383 662  HOH   HOH A . 
F 5 HOH   84  384 10   HOH   HOH A . 
F 5 HOH   85  385 461  HOH   HOH A . 
F 5 HOH   86  386 351  HOH   HOH A . 
F 5 HOH   87  387 26   HOH   HOH A . 
F 5 HOH   88  388 1309 HOH   HOH A . 
F 5 HOH   89  389 493  HOH   HOH A . 
F 5 HOH   90  390 35   HOH   HOH A . 
F 5 HOH   91  391 11   HOH   HOH A . 
F 5 HOH   92  392 62   HOH   HOH A . 
F 5 HOH   93  393 1275 HOH   HOH A . 
F 5 HOH   94  394 393  HOH   HOH A . 
F 5 HOH   95  395 116  HOH   HOH A . 
F 5 HOH   96  396 148  HOH   HOH A . 
F 5 HOH   97  397 46   HOH   HOH A . 
F 5 HOH   98  398 218  HOH   HOH A . 
F 5 HOH   99  399 303  HOH   HOH A . 
F 5 HOH   100 400 27   HOH   HOH A . 
F 5 HOH   101 401 58   HOH   HOH A . 
F 5 HOH   102 402 4    HOH   HOH A . 
F 5 HOH   103 403 195  HOH   HOH A . 
F 5 HOH   104 404 121  HOH   HOH A . 
F 5 HOH   105 405 154  HOH   HOH A . 
F 5 HOH   106 406 1289 HOH   HOH A . 
F 5 HOH   107 407 1310 HOH   HOH A . 
F 5 HOH   108 408 12   HOH   HOH A . 
F 5 HOH   109 409 78   HOH   HOH A . 
F 5 HOH   110 410 333  HOH   HOH A . 
F 5 HOH   111 411 85   HOH   HOH A . 
F 5 HOH   112 412 1315 HOH   HOH A . 
F 5 HOH   113 413 68   HOH   HOH A . 
F 5 HOH   114 414 24   HOH   HOH A . 
F 5 HOH   115 415 296  HOH   HOH A . 
F 5 HOH   116 416 199  HOH   HOH A . 
F 5 HOH   117 417 83   HOH   HOH A . 
F 5 HOH   118 418 25   HOH   HOH A . 
F 5 HOH   119 419 6    HOH   HOH A . 
F 5 HOH   120 420 1313 HOH   HOH A . 
F 5 HOH   121 421 67   HOH   HOH A . 
F 5 HOH   122 422 3    HOH   HOH A . 
F 5 HOH   123 423 15   HOH   HOH A . 
F 5 HOH   124 424 123  HOH   HOH A . 
F 5 HOH   125 425 3    HOH   HOH A . 
F 5 HOH   126 426 1279 HOH   HOH A . 
F 5 HOH   127 427 4    HOH   HOH A . 
F 5 HOH   128 428 1068 HOH   HOH A . 
F 5 HOH   129 429 125  HOH   HOH A . 
F 5 HOH   130 430 8    HOH   HOH A . 
F 5 HOH   131 431 278  HOH   HOH A . 
F 5 HOH   132 432 53   HOH   HOH A . 
F 5 HOH   133 433 397  HOH   HOH A . 
F 5 HOH   134 434 1222 HOH   HOH A . 
F 5 HOH   135 435 95   HOH   HOH A . 
F 5 HOH   136 436 132  HOH   HOH A . 
F 5 HOH   137 437 582  HOH   HOH A . 
F 5 HOH   138 438 7    HOH   HOH A . 
F 5 HOH   139 439 122  HOH   HOH A . 
F 5 HOH   140 440 156  HOH   HOH A . 
F 5 HOH   141 441 51   HOH   HOH A . 
F 5 HOH   142 442 212  HOH   HOH A . 
F 5 HOH   143 443 1301 HOH   HOH A . 
F 5 HOH   144 444 70   HOH   HOH A . 
F 5 HOH   145 445 952  HOH   HOH A . 
F 5 HOH   146 446 71   HOH   HOH A . 
F 5 HOH   147 447 944  HOH   HOH A . 
F 5 HOH   148 448 79   HOH   HOH A . 
F 5 HOH   149 449 16   HOH   HOH A . 
F 5 HOH   150 450 80   HOH   HOH A . 
F 5 HOH   151 451 40   HOH   HOH A . 
F 5 HOH   152 452 1189 HOH   HOH A . 
F 5 HOH   153 453 94   HOH   HOH A . 
F 5 HOH   154 454 1296 HOH   HOH A . 
F 5 HOH   155 455 1286 HOH   HOH A . 
F 5 HOH   156 456 576  HOH   HOH A . 
F 5 HOH   157 457 188  HOH   HOH A . 
F 5 HOH   158 458 97   HOH   HOH A . 
F 5 HOH   159 459 73   HOH   HOH A . 
F 5 HOH   160 460 104  HOH   HOH A . 
F 5 HOH   161 461 12   HOH   HOH A . 
F 5 HOH   162 462 330  HOH   HOH A . 
F 5 HOH   163 463 726  HOH   HOH A . 
F 5 HOH   164 464 1094 HOH   HOH A . 
F 5 HOH   165 465 1119 HOH   HOH A . 
F 5 HOH   166 466 509  HOH   HOH A . 
F 5 HOH   167 467 107  HOH   HOH A . 
F 5 HOH   168 468 163  HOH   HOH A . 
F 5 HOH   169 469 1134 HOH   HOH A . 
F 5 HOH   170 470 408  HOH   HOH A . 
F 5 HOH   171 471 801  HOH   HOH A . 
F 5 HOH   172 472 756  HOH   HOH A . 
F 5 HOH   173 473 280  HOH   HOH A . 
F 5 HOH   174 474 342  HOH   HOH A . 
F 5 HOH   175 475 126  HOH   HOH A . 
F 5 HOH   176 476 556  HOH   HOH A . 
F 5 HOH   177 477 319  HOH   HOH A . 
F 5 HOH   178 478 361  HOH   HOH A . 
F 5 HOH   179 479 1276 HOH   HOH A . 
F 5 HOH   180 480 63   HOH   HOH A . 
F 5 HOH   181 481 370  HOH   HOH A . 
F 5 HOH   182 482 1307 HOH   HOH A . 
F 5 HOH   183 483 224  HOH   HOH A . 
F 5 HOH   184 484 250  HOH   HOH A . 
F 5 HOH   185 485 267  HOH   HOH A . 
F 5 HOH   186 486 1287 HOH   HOH A . 
F 5 HOH   187 487 1306 HOH   HOH A . 
F 5 HOH   188 488 202  HOH   HOH A . 
F 5 HOH   189 489 695  HOH   HOH A . 
F 5 HOH   190 490 135  HOH   HOH A . 
F 5 HOH   191 491 674  HOH   HOH A . 
F 5 HOH   192 492 711  HOH   HOH A . 
F 5 HOH   193 493 919  HOH   HOH A . 
F 5 HOH   194 494 941  HOH   HOH A . 
F 5 HOH   195 495 318  HOH   HOH A . 
F 5 HOH   196 496 1314 HOH   HOH A . 
F 5 HOH   197 497 1299 HOH   HOH A . 
F 5 HOH   198 498 208  HOH   HOH A . 
F 5 HOH   199 499 309  HOH   HOH A . 
F 5 HOH   200 500 331  HOH   HOH A . 
F 5 HOH   201 501 805  HOH   HOH A . 
F 5 HOH   202 502 263  HOH   HOH A . 
F 5 HOH   203 503 152  HOH   HOH A . 
F 5 HOH   204 504 521  HOH   HOH A . 
F 5 HOH   205 505 315  HOH   HOH A . 
F 5 HOH   206 506 356  HOH   HOH A . 
F 5 HOH   207 507 1071 HOH   HOH A . 
F 5 HOH   208 508 180  HOH   HOH A . 
F 5 HOH   209 509 7    HOH   HOH A . 
F 5 HOH   210 510 350  HOH   HOH A . 
F 5 HOH   211 511 16   HOH   HOH A . 
F 5 HOH   212 512 363  HOH   HOH A . 
F 5 HOH   213 513 326  HOH   HOH A . 
F 5 HOH   214 514 313  HOH   HOH A . 
F 5 HOH   215 515 371  HOH   HOH A . 
F 5 HOH   216 516 1284 HOH   HOH A . 
F 5 HOH   217 517 185  HOH   HOH A . 
F 5 HOH   218 518 429  HOH   HOH A . 
F 5 HOH   219 519 14   HOH   HOH A . 
F 5 HOH   220 520 772  HOH   HOH A . 
F 5 HOH   221 521 70   HOH   HOH A . 
F 5 HOH   222 522 13   HOH   HOH A . 
F 5 HOH   223 523 376  HOH   HOH A . 
F 5 HOH   224 524 1074 HOH   HOH A . 
F 5 HOH   225 525 1292 HOH   HOH A . 
F 5 HOH   226 526 346  HOH   HOH A . 
F 5 HOH   227 527 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 531  HOH   HOH B . 
G 5 HOH   3   203 549  HOH   HOH B . 
G 5 HOH   4   204 358  HOH   HOH B . 
G 5 HOH   5   205 240  HOH   HOH B . 
G 5 HOH   6   206 364  HOH   HOH B . 
G 5 HOH   7   207 758  HOH   HOH B . 
G 5 HOH   8   208 452  HOH   HOH B . 
G 5 HOH   9   209 353  HOH   HOH B . 
G 5 HOH   10  210 398  HOH   HOH B . 
G 5 HOH   11  211 1249 HOH   HOH B . 
G 5 HOH   12  212 654  HOH   HOH B . 
G 5 HOH   13  213 120  HOH   HOH B . 
G 5 HOH   14  214 50   HOH   HOH B . 
G 5 HOH   15  215 743  HOH   HOH B . 
G 5 HOH   16  216 264  HOH   HOH B . 
G 5 HOH   17  217 332  HOH   HOH B . 
G 5 HOH   18  218 900  HOH   HOH B . 
G 5 HOH   19  219 444  HOH   HOH B . 
G 5 HOH   20  220 131  HOH   HOH B . 
G 5 HOH   21  221 343  HOH   HOH B . 
G 5 HOH   22  222 1278 HOH   HOH B . 
G 5 HOH   23  223 75   HOH   HOH B . 
G 5 HOH   24  224 1140 HOH   HOH B . 
G 5 HOH   25  225 166  HOH   HOH B . 
G 5 HOH   26  226 282  HOH   HOH B . 
G 5 HOH   27  227 232  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  230 723  HOH   HOH B . 
G 5 HOH   31  231 60   HOH   HOH B . 
G 5 HOH   32  232 231  HOH   HOH B . 
G 5 HOH   33  233 82   HOH   HOH B . 
G 5 HOH   34  234 205  HOH   HOH B . 
G 5 HOH   35  235 1    HOH   HOH B . 
G 5 HOH   36  236 172  HOH   HOH B . 
G 5 HOH   37  237 272  HOH   HOH B . 
G 5 HOH   38  238 271  HOH   HOH B . 
G 5 HOH   39  239 128  HOH   HOH B . 
G 5 HOH   40  240 133  HOH   HOH B . 
G 5 HOH   41  241 127  HOH   HOH B . 
G 5 HOH   42  242 325  HOH   HOH B . 
G 5 HOH   43  243 1312 HOH   HOH B . 
G 5 HOH   44  244 181  HOH   HOH B . 
G 5 HOH   45  245 14   HOH   HOH B . 
G 5 HOH   46  246 300  HOH   HOH B . 
G 5 HOH   47  247 110  HOH   HOH B . 
G 5 HOH   48  248 69   HOH   HOH B . 
G 5 HOH   49  249 9    HOH   HOH B . 
G 5 HOH   50  250 143  HOH   HOH B . 
G 5 HOH   51  251 144  HOH   HOH B . 
G 5 HOH   52  252 276  HOH   HOH B . 
G 5 HOH   53  253 52   HOH   HOH B . 
G 5 HOH   54  254 391  HOH   HOH B . 
G 5 HOH   55  255 129  HOH   HOH B . 
G 5 HOH   56  256 72   HOH   HOH B . 
G 5 HOH   57  257 103  HOH   HOH B . 
G 5 HOH   58  258 30   HOH   HOH B . 
G 5 HOH   59  259 41   HOH   HOH B . 
G 5 HOH   60  260 47   HOH   HOH B . 
G 5 HOH   61  261 31   HOH   HOH B . 
G 5 HOH   62  262 59   HOH   HOH B . 
G 5 HOH   63  263 11   HOH   HOH B . 
G 5 HOH   64  264 10   HOH   HOH B . 
G 5 HOH   65  265 150  HOH   HOH B . 
G 5 HOH   66  266 347  HOH   HOH B . 
G 5 HOH   67  267 242  HOH   HOH B . 
G 5 HOH   68  268 20   HOH   HOH B . 
G 5 HOH   69  269 117  HOH   HOH B . 
G 5 HOH   70  270 77   HOH   HOH B . 
G 5 HOH   71  271 302  HOH   HOH B . 
G 5 HOH   72  272 61   HOH   HOH B . 
G 5 HOH   73  273 147  HOH   HOH B . 
G 5 HOH   74  274 221  HOH   HOH B . 
G 5 HOH   75  275 84   HOH   HOH B . 
G 5 HOH   76  276 216  HOH   HOH B . 
G 5 HOH   77  277 1277 HOH   HOH B . 
G 5 HOH   78  278 243  HOH   HOH B . 
G 5 HOH   79  279 43   HOH   HOH B . 
G 5 HOH   80  280 220  HOH   HOH B . 
G 5 HOH   81  281 235  HOH   HOH B . 
G 5 HOH   82  282 1106 HOH   HOH B . 
G 5 HOH   83  283 88   HOH   HOH B . 
G 5 HOH   84  284 114  HOH   HOH B . 
G 5 HOH   85  285 22   HOH   HOH B . 
G 5 HOH   86  286 106  HOH   HOH B . 
G 5 HOH   87  287 416  HOH   HOH B . 
G 5 HOH   88  288 175  HOH   HOH B . 
G 5 HOH   89  289 1066 HOH   HOH B . 
G 5 HOH   90  290 89   HOH   HOH B . 
G 5 HOH   91  291 287  HOH   HOH B . 
G 5 HOH   92  292 311  HOH   HOH B . 
G 5 HOH   93  293 137  HOH   HOH B . 
G 5 HOH   94  294 99   HOH   HOH B . 
G 5 HOH   95  295 387  HOH   HOH B . 
G 5 HOH   96  296 635  HOH   HOH B . 
G 5 HOH   97  297 13   HOH   HOH B . 
G 5 HOH   98  298 341  HOH   HOH B . 
G 5 HOH   99  299 112  HOH   HOH B . 
G 5 HOH   100 300 160  HOH   HOH B . 
G 5 HOH   101 301 141  HOH   HOH B . 
G 5 HOH   102 302 316  HOH   HOH B . 
G 5 HOH   103 303 215  HOH   HOH B . 
G 5 HOH   104 304 142  HOH   HOH B . 
G 5 HOH   105 305 1274 HOH   HOH B . 
G 5 HOH   106 306 1305 HOH   HOH B . 
G 5 HOH   107 307 101  HOH   HOH B . 
G 5 HOH   108 308 32   HOH   HOH B . 
G 5 HOH   109 309 38   HOH   HOH B . 
G 5 HOH   110 310 170  HOH   HOH B . 
G 5 HOH   111 311 299  HOH   HOH B . 
G 5 HOH   112 312 37   HOH   HOH B . 
G 5 HOH   113 313 91   HOH   HOH B . 
G 5 HOH   114 314 197  HOH   HOH B . 
G 5 HOH   115 315 23   HOH   HOH B . 
G 5 HOH   116 316 48   HOH   HOH B . 
G 5 HOH   117 317 297  HOH   HOH B . 
G 5 HOH   118 318 28   HOH   HOH B . 
G 5 HOH   119 319 118  HOH   HOH B . 
G 5 HOH   120 320 161  HOH   HOH B . 
G 5 HOH   121 321 1291 HOH   HOH B . 
G 5 HOH   122 322 177  HOH   HOH B . 
G 5 HOH   123 323 44   HOH   HOH B . 
G 5 HOH   124 324 334  HOH   HOH B . 
G 5 HOH   125 325 100  HOH   HOH B . 
G 5 HOH   126 326 29   HOH   HOH B . 
G 5 HOH   127 327 704  HOH   HOH B . 
G 5 HOH   128 328 182  HOH   HOH B . 
G 5 HOH   129 329 1126 HOH   HOH B . 
G 5 HOH   130 330 1285 HOH   HOH B . 
G 5 HOH   131 331 1294 HOH   HOH B . 
G 5 HOH   132 332 98   HOH   HOH B . 
G 5 HOH   133 333 55   HOH   HOH B . 
G 5 HOH   134 334 717  HOH   HOH B . 
G 5 HOH   135 335 207  HOH   HOH B . 
G 5 HOH   136 336 65   HOH   HOH B . 
G 5 HOH   137 337 234  HOH   HOH B . 
G 5 HOH   138 338 619  HOH   HOH B . 
G 5 HOH   139 339 1293 HOH   HOH B . 
G 5 HOH   140 340 445  HOH   HOH B . 
G 5 HOH   141 341 339  HOH   HOH B . 
G 5 HOH   142 342 362  HOH   HOH B . 
G 5 HOH   143 343 960  HOH   HOH B . 
G 5 HOH   144 344 90   HOH   HOH B . 
G 5 HOH   145 345 178  HOH   HOH B . 
G 5 HOH   146 346 1304 HOH   HOH B . 
G 5 HOH   147 347 463  HOH   HOH B . 
G 5 HOH   148 348 191  HOH   HOH B . 
G 5 HOH   149 349 335  HOH   HOH B . 
G 5 HOH   150 350 623  HOH   HOH B . 
G 5 HOH   151 351 1046 HOH   HOH B . 
G 5 HOH   152 352 1280 HOH   HOH B . 
G 5 HOH   153 353 87   HOH   HOH B . 
G 5 HOH   154 354 541  HOH   HOH B . 
G 5 HOH   155 355 304  HOH   HOH B . 
G 5 HOH   156 356 203  HOH   HOH B . 
G 5 HOH   157 357 290  HOH   HOH B . 
G 5 HOH   158 358 479  HOH   HOH B . 
G 5 HOH   159 359 1077 HOH   HOH B . 
G 5 HOH   160 360 389  HOH   HOH B . 
G 5 HOH   161 361 718  HOH   HOH B . 
G 5 HOH   162 362 283  HOH   HOH B . 
G 5 HOH   163 363 1072 HOH   HOH B . 
G 5 HOH   164 364 1316 HOH   HOH B . 
G 5 HOH   165 365 898  HOH   HOH B . 
G 5 HOH   166 366 340  HOH   HOH B . 
G 5 HOH   167 367 1303 HOH   HOH B . 
G 5 HOH   168 368 615  HOH   HOH B . 
G 5 HOH   169 369 291  HOH   HOH B . 
G 5 HOH   170 370 667  HOH   HOH B . 
G 5 HOH   171 371 373  HOH   HOH B . 
G 5 HOH   172 372 190  HOH   HOH B . 
G 5 HOH   173 373 310  HOH   HOH B . 
G 5 HOH   174 374 149  HOH   HOH B . 
G 5 HOH   175 375 431  HOH   HOH B . 
G 5 HOH   176 376 1163 HOH   HOH B . 
G 5 HOH   177 377 1173 HOH   HOH B . 
G 5 HOH   178 378 1000 HOH   HOH B . 
G 5 HOH   179 379 183  HOH   HOH B . 
G 5 HOH   180 380 1311 HOH   HOH B . 
G 5 HOH   181 381 418  HOH   HOH B . 
G 5 HOH   182 382 176  HOH   HOH B . 
G 5 HOH   183 383 424  HOH   HOH B . 
G 5 HOH   184 384 1298 HOH   HOH B . 
G 5 HOH   185 385 491  HOH   HOH B . 
G 5 HOH   186 386 981  HOH   HOH B . 
G 5 HOH   187 387 265  HOH   HOH B . 
G 5 HOH   188 388 248  HOH   HOH B . 
G 5 HOH   189 389 470  HOH   HOH B . 
G 5 HOH   190 390 184  HOH   HOH B . 
G 5 HOH   191 391 360  HOH   HOH B . 
G 5 HOH   192 392 355  HOH   HOH B . 
G 5 HOH   193 393 410  HOH   HOH B . 
G 5 HOH   194 394 566  HOH   HOH B . 
G 5 HOH   195 395 274  HOH   HOH B . 
G 5 HOH   196 396 314  HOH   HOH B . 
G 5 HOH   197 397 157  HOH   HOH B . 
G 5 HOH   198 398 792  HOH   HOH B . 
G 5 HOH   199 399 321  HOH   HOH B . 
G 5 HOH   200 400 558  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           7HE0 
_cell.length_a           88.704 
_cell.length_b           88.704 
_cell.length_c           39.559 
_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                         7HE0 
_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          7HE0 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.63 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HE0 
_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                   175774 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.044 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.000 
_reflns.B_iso_Wilson_estimate        11.910 
_reflns.pdbx_redundancy              6.200 
_reflns.pdbx_Rrim_I_all              0.048 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1088123 
_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  ? 27133 8249 ? 1.045 ? ? ? 3.300 ? 0.800  ? ? ? ? ? ? 95.500 1.239 0.641 0.574 
1 2 5.370 44.350 ? 7997  1165 ? 0.033 ? ? ? 6.900 ? 52.900 ? ? ? ? ? ? 99.800 0.035 0.013 0.998 
# 
_refine.entry_id                                 7HE0 
_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                    99.6600 
_refine.ls_number_reflns_obs                     175676 
_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                          0.1470 
_refine.ls_R_factor_R_work                       0.1463 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1600 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  8479 
_refine.ls_number_reflns_R_work                  167197 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.2061 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1200 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                63.130 
_refine.B_iso_min                                4.100 
_refine.pdbx_overall_phase_error                 19.0100 
_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         48 
_refine_hist.number_atoms_solvent             427 
_refine_hist.number_atoms_total               3017 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           12.58 
_refine_hist.pdbx_B_iso_mean_solvent          30.56 
_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  5211 . 0.4315 0.4447 . 273 0.0000 5484 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 98.0000  5408 . 0.3768 0.3538 . 279 0.0000 5687 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 100.0000 5558 . 0.3258 0.2902 . 278 0.0000 5836 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 100.0000 5581 . 0.2761 0.2793 . 253 0.0000 5834 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5586 . 0.2520 0.2642 . 302 0.0000 5888 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5497 . 0.2224 0.2120 . 300 0.0000 5797 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5548 . 0.2087 0.2272 . 311 0.0000 5859 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5533 . 0.1843 0.2039 . 255 0.0000 5788 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5591 . 0.1724 0.2132 . 286 0.0000 5877 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5586 . 0.1611 0.1873 . 294 0.0000 5880 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5589 . 0.1535 0.1855 . 246 0.0000 5835 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5573 . 0.1429 0.1517 . 266 0.0000 5839 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5568 . 0.1329 0.1674 . 289 0.0000 5857 . 'X-RAY DIFFRACTION' 
1.1800 1.2100  30 100.0000 5515 . 0.1269 0.1700 . 315 0.0000 5830 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5644 . 0.1224 0.1521 . 243 0.0000 5887 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5580 . 0.1234 0.1396 . 271 0.0000 5851 . 'X-RAY DIFFRACTION' 
1.2600 1.3000  30 100.0000 5549 . 0.1233 0.1311 . 292 0.0000 5841 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5569 . 0.1235 0.1312 . 304 0.0000 5873 . 'X-RAY DIFFRACTION' 
1.3300 1.3700  30 100.0000 5589 . 0.1301 0.1469 . 299 0.0000 5888 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5627 . 0.1257 0.1643 . 244 0.0000 5871 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5556 . 0.1281 0.1432 . 302 0.0000 5858 . 'X-RAY DIFFRACTION' 
1.4600 1.5200  30 100.0000 5585 . 0.1203 0.1374 . 265 0.0000 5850 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 5612 . 0.1190 0.1275 . 306 0.0000 5918 . 'X-RAY DIFFRACTION' 
1.5900 1.6800  30 100.0000 5584 . 0.1207 0.1298 . 275 0.0000 5859 . 'X-RAY DIFFRACTION' 
1.6800 1.7800  30 100.0000 5621 . 0.1324 0.1454 . 264 0.0000 5885 . 'X-RAY DIFFRACTION' 
1.7800 1.9200  30 100.0000 5592 . 0.1369 0.1409 . 304 0.0000 5896 . 'X-RAY DIFFRACTION' 
1.9200 2.1100  30 100.0000 5664 . 0.1392 0.1429 . 284 0.0000 5948 . 'X-RAY DIFFRACTION' 
2.1100 2.4200  30 100.0000 5592 . 0.1413 0.1386 . 308 0.0000 5900 . 'X-RAY DIFFRACTION' 
2.4200 3.0400  30 100.0000 5696 . 0.1492 0.1714 . 292 0.0000 5988 . 'X-RAY DIFFRACTION' 
3.0500 39.6700 30 100.0000 5793 . 0.1489 0.1692 . 279 0.0000 6072 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HE0 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003652' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HE0 
_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 7HE0 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HE0 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 7HE0 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HE0 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HE0 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HE0 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HE0 
_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_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 HH A TYR 42 ? B 1_555 OD1 B ASP 67 ? ? 2_654 1.59 
2 1 O  A ASP 66 ? ? 1_555 HG  B SER 1  ? B 2_655 1.60 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86 ? ? 55.29 -131.79 
2 1 HIS A 86 ? ? 55.29 -133.37 
3 1 HIS B 86 ? ? 57.25 -128.48 
# 
_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 525 ? 5.95 . 
2 1 O ? A HOH 526 ? 5.96 . 
3 1 O ? A HOH 527 ? 7.60 . 
4 1 O ? B HOH 400 ? 6.17 . 
# 
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 
A1A9A N2   N  Y N 1   
A1A9A C3   C  Y N 2   
A1A9A C6   C  Y N 3   
A1A9A C9   C  N N 4   
A1A9A C12  C  Y N 5   
A1A9A C14  C  Y N 6   
A1A9A C17  C  Y N 7   
A1A9A C1   C  N R 8   
A1A9A C10  C  N N 9   
A1A9A C11  C  N N 10  
A1A9A C13  C  Y N 11  
A1A9A C15  C  Y N 12  
A1A9A C16  C  Y N 13  
A1A9A C2   C  Y N 14  
A1A9A C4   C  Y N 15  
A1A9A C5   C  Y N 16  
A1A9A C7   C  Y N 17  
A1A9A C8   C  N R 18  
A1A9A N1   N  N N 19  
A1A9A N3   N  Y N 20  
A1A9A N4   N  Y N 21  
A1A9A O1   O  N N 22  
A1A9A H4   H  N N 23  
A1A9A H7   H  N N 24  
A1A9A H10  H  N N 25  
A1A9A H9   H  N N 26  
A1A9A H17  H  N N 27  
A1A9A H1   H  N N 28  
A1A9A H12  H  N N 29  
A1A9A H11  H  N N 30  
A1A9A H14  H  N N 31  
A1A9A H13  H  N N 32  
A1A9A H15  H  N N 33  
A1A9A H16  H  N N 34  
A1A9A H5   H  N N 35  
A1A9A H6   H  N N 36  
A1A9A H8   H  N N 37  
A1A9A H2   H  N N 38  
A1A9A H18  H  N N 39  
A1A9A H3   H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CL    CL   CL N N 114 
CYS   N    N  N N 115 
CYS   CA   C  N R 116 
CYS   C    C  N N 117 
CYS   O    O  N N 118 
CYS   CB   C  N N 119 
CYS   SG   S  N N 120 
CYS   OXT  O  N N 121 
CYS   H    H  N N 122 
CYS   H2   H  N N 123 
CYS   HA   H  N N 124 
CYS   HB2  H  N N 125 
CYS   HB3  H  N N 126 
CYS   HG   H  N N 127 
CYS   HXT  H  N N 128 
GLN   N    N  N N 129 
GLN   CA   C  N S 130 
GLN   C    C  N N 131 
GLN   O    O  N N 132 
GLN   CB   C  N N 133 
GLN   CG   C  N N 134 
GLN   CD   C  N N 135 
GLN   OE1  O  N N 136 
GLN   NE2  N  N N 137 
GLN   OXT  O  N N 138 
GLN   H    H  N N 139 
GLN   H2   H  N N 140 
GLN   HA   H  N N 141 
GLN   HB2  H  N N 142 
GLN   HB3  H  N N 143 
GLN   HG2  H  N N 144 
GLN   HG3  H  N N 145 
GLN   HE21 H  N N 146 
GLN   HE22 H  N N 147 
GLN   HXT  H  N N 148 
GLU   N    N  N N 149 
GLU   CA   C  N S 150 
GLU   C    C  N N 151 
GLU   O    O  N N 152 
GLU   CB   C  N N 153 
GLU   CG   C  N N 154 
GLU   CD   C  N N 155 
GLU   OE1  O  N N 156 
GLU   OE2  O  N N 157 
GLU   OXT  O  N N 158 
GLU   H    H  N N 159 
GLU   H2   H  N N 160 
GLU   HA   H  N N 161 
GLU   HB2  H  N N 162 
GLU   HB3  H  N N 163 
GLU   HG2  H  N N 164 
GLU   HG3  H  N N 165 
GLU   HE2  H  N N 166 
GLU   HXT  H  N N 167 
GLY   N    N  N N 168 
GLY   CA   C  N N 169 
GLY   C    C  N N 170 
GLY   O    O  N N 171 
GLY   OXT  O  N N 172 
GLY   H    H  N N 173 
GLY   H2   H  N N 174 
GLY   HA2  H  N N 175 
GLY   HA3  H  N N 176 
GLY   HXT  H  N N 177 
HIS   N    N  N N 178 
HIS   CA   C  N S 179 
HIS   C    C  N N 180 
HIS   O    O  N N 181 
HIS   CB   C  N N 182 
HIS   CG   C  Y N 183 
HIS   ND1  N  Y N 184 
HIS   CD2  C  Y N 185 
HIS   CE1  C  Y N 186 
HIS   NE2  N  Y N 187 
HIS   OXT  O  N N 188 
HIS   H    H  N N 189 
HIS   H2   H  N N 190 
HIS   HA   H  N N 191 
HIS   HB2  H  N N 192 
HIS   HB3  H  N N 193 
HIS   HD1  H  N N 194 
HIS   HD2  H  N N 195 
HIS   HE1  H  N N 196 
HIS   HE2  H  N N 197 
HIS   HXT  H  N N 198 
HOH   O    O  N N 199 
HOH   H1   H  N N 200 
HOH   H2   H  N N 201 
ILE   N    N  N N 202 
ILE   CA   C  N S 203 
ILE   C    C  N N 204 
ILE   O    O  N N 205 
ILE   CB   C  N S 206 
ILE   CG1  C  N N 207 
ILE   CG2  C  N N 208 
ILE   CD1  C  N N 209 
ILE   OXT  O  N N 210 
ILE   H    H  N N 211 
ILE   H2   H  N N 212 
ILE   HA   H  N N 213 
ILE   HB   H  N N 214 
ILE   HG12 H  N N 215 
ILE   HG13 H  N N 216 
ILE   HG21 H  N N 217 
ILE   HG22 H  N N 218 
ILE   HG23 H  N N 219 
ILE   HD11 H  N N 220 
ILE   HD12 H  N N 221 
ILE   HD13 H  N N 222 
ILE   HXT  H  N N 223 
LEU   N    N  N N 224 
LEU   CA   C  N S 225 
LEU   C    C  N N 226 
LEU   O    O  N N 227 
LEU   CB   C  N N 228 
LEU   CG   C  N N 229 
LEU   CD1  C  N N 230 
LEU   CD2  C  N N 231 
LEU   OXT  O  N N 232 
LEU   H    H  N N 233 
LEU   H2   H  N N 234 
LEU   HA   H  N N 235 
LEU   HB2  H  N N 236 
LEU   HB3  H  N N 237 
LEU   HG   H  N N 238 
LEU   HD11 H  N N 239 
LEU   HD12 H  N N 240 
LEU   HD13 H  N N 241 
LEU   HD21 H  N N 242 
LEU   HD22 H  N N 243 
LEU   HD23 H  N N 244 
LEU   HXT  H  N N 245 
LYS   N    N  N N 246 
LYS   CA   C  N S 247 
LYS   C    C  N N 248 
LYS   O    O  N N 249 
LYS   CB   C  N N 250 
LYS   CG   C  N N 251 
LYS   CD   C  N N 252 
LYS   CE   C  N N 253 
LYS   NZ   N  N N 254 
LYS   OXT  O  N N 255 
LYS   H    H  N N 256 
LYS   H2   H  N N 257 
LYS   HA   H  N N 258 
LYS   HB2  H  N N 259 
LYS   HB3  H  N N 260 
LYS   HG2  H  N N 261 
LYS   HG3  H  N N 262 
LYS   HD2  H  N N 263 
LYS   HD3  H  N N 264 
LYS   HE2  H  N N 265 
LYS   HE3  H  N N 266 
LYS   HZ1  H  N N 267 
LYS   HZ2  H  N N 268 
LYS   HZ3  H  N N 269 
LYS   HXT  H  N N 270 
MET   N    N  N N 271 
MET   CA   C  N S 272 
MET   C    C  N N 273 
MET   O    O  N N 274 
MET   CB   C  N N 275 
MET   CG   C  N N 276 
MET   SD   S  N N 277 
MET   CE   C  N N 278 
MET   OXT  O  N N 279 
MET   H    H  N N 280 
MET   H2   H  N N 281 
MET   HA   H  N N 282 
MET   HB2  H  N N 283 
MET   HB3  H  N N 284 
MET   HG2  H  N N 285 
MET   HG3  H  N N 286 
MET   HE1  H  N N 287 
MET   HE2  H  N N 288 
MET   HE3  H  N N 289 
MET   HXT  H  N N 290 
PHE   N    N  N N 291 
PHE   CA   C  N S 292 
PHE   C    C  N N 293 
PHE   O    O  N N 294 
PHE   CB   C  N N 295 
PHE   CG   C  Y N 296 
PHE   CD1  C  Y N 297 
PHE   CD2  C  Y N 298 
PHE   CE1  C  Y N 299 
PHE   CE2  C  Y N 300 
PHE   CZ   C  Y N 301 
PHE   OXT  O  N N 302 
PHE   H    H  N N 303 
PHE   H2   H  N N 304 
PHE   HA   H  N N 305 
PHE   HB2  H  N N 306 
PHE   HB3  H  N N 307 
PHE   HD1  H  N N 308 
PHE   HD2  H  N N 309 
PHE   HE1  H  N N 310 
PHE   HE2  H  N N 311 
PHE   HZ   H  N N 312 
PHE   HXT  H  N N 313 
PRO   N    N  N N 314 
PRO   CA   C  N S 315 
PRO   C    C  N N 316 
PRO   O    O  N N 317 
PRO   CB   C  N N 318 
PRO   CG   C  N N 319 
PRO   CD   C  N N 320 
PRO   OXT  O  N N 321 
PRO   H    H  N N 322 
PRO   HA   H  N N 323 
PRO   HB2  H  N N 324 
PRO   HB3  H  N N 325 
PRO   HG2  H  N N 326 
PRO   HG3  H  N N 327 
PRO   HD2  H  N N 328 
PRO   HD3  H  N N 329 
PRO   HXT  H  N N 330 
SER   N    N  N N 331 
SER   CA   C  N S 332 
SER   C    C  N N 333 
SER   O    O  N N 334 
SER   CB   C  N N 335 
SER   OG   O  N N 336 
SER   OXT  O  N N 337 
SER   H    H  N N 338 
SER   H2   H  N N 339 
SER   HA   H  N N 340 
SER   HB2  H  N N 341 
SER   HB3  H  N N 342 
SER   HG   H  N N 343 
SER   HXT  H  N N 344 
TFA   C1   C  N N 345 
TFA   C2   C  N N 346 
TFA   O    O  N N 347 
TFA   F1   F  N N 348 
TFA   F2   F  N N 349 
TFA   F3   F  N N 350 
TFA   OXT  O  N N 351 
TFA   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TYR   N    N  N N 370 
TYR   CA   C  N S 371 
TYR   C    C  N N 372 
TYR   O    O  N N 373 
TYR   CB   C  N N 374 
TYR   CG   C  Y N 375 
TYR   CD1  C  Y N 376 
TYR   CD2  C  Y N 377 
TYR   CE1  C  Y N 378 
TYR   CE2  C  Y N 379 
TYR   CZ   C  Y N 380 
TYR   OH   O  N N 381 
TYR   OXT  O  N N 382 
TYR   H    H  N N 383 
TYR   H2   H  N N 384 
TYR   HA   H  N N 385 
TYR   HB2  H  N N 386 
TYR   HB3  H  N N 387 
TYR   HD1  H  N N 388 
TYR   HD2  H  N N 389 
TYR   HE1  H  N N 390 
TYR   HE2  H  N N 391 
TYR   HH   H  N N 392 
TYR   HXT  H  N N 393 
VAL   N    N  N N 394 
VAL   CA   C  N S 395 
VAL   C    C  N N 396 
VAL   O    O  N N 397 
VAL   CB   C  N N 398 
VAL   CG1  C  N N 399 
VAL   CG2  C  N N 400 
VAL   OXT  O  N N 401 
VAL   H    H  N N 402 
VAL   H2   H  N N 403 
VAL   HA   H  N N 404 
VAL   HB   H  N N 405 
VAL   HG11 H  N N 406 
VAL   HG12 H  N N 407 
VAL   HG13 H  N N 408 
VAL   HG21 H  N N 409 
VAL   HG22 H  N N 410 
VAL   HG23 H  N N 411 
VAL   HXT  H  N N 412 
# 
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 
A1A9A C6  C5   doub Y N 1   
A1A9A C6  C7   sing Y N 2   
A1A9A C5  C4   sing Y N 3   
A1A9A C7  C2   doub Y N 4   
A1A9A C10 C9   sing N N 5   
A1A9A C10 C11  sing N N 6   
A1A9A C9  C8   sing N N 7   
A1A9A C4  C3   doub Y N 8   
A1A9A C2  C3   sing Y N 9   
A1A9A C2  C1   sing N N 10  
A1A9A O1  C1   sing N N 11  
A1A9A C11 N1   sing N N 12  
A1A9A C8  C1   sing N N 13  
A1A9A C8  N1   sing N N 14  
A1A9A N1  C12  sing N N 15  
A1A9A C12 N2   doub Y N 16  
A1A9A C12 C15  sing Y N 17  
A1A9A C16 C15  sing Y N 18  
A1A9A C16 C17  doub Y N 19  
A1A9A N2  C13  sing Y N 20  
A1A9A C15 C14  doub Y N 21  
A1A9A C17 N4   sing Y N 22  
A1A9A C13 N3   doub Y N 23  
A1A9A C14 N4   sing Y N 24  
A1A9A C14 N3   sing Y N 25  
A1A9A C3  H4   sing N N 26  
A1A9A C6  H7   sing N N 27  
A1A9A C9  H10  sing N N 28  
A1A9A C9  H9   sing N N 29  
A1A9A C17 H17  sing N N 30  
A1A9A C1  H1   sing N N 31  
A1A9A C10 H12  sing N N 32  
A1A9A C10 H11  sing N N 33  
A1A9A C11 H14  sing N N 34  
A1A9A C11 H13  sing N N 35  
A1A9A C13 H15  sing N N 36  
A1A9A C16 H16  sing N N 37  
A1A9A C4  H5   sing N N 38  
A1A9A C5  H6   sing N N 39  
A1A9A C7  H8   sing N N 40  
A1A9A C8  H2   sing N N 41  
A1A9A N4  H18  sing N N 42  
A1A9A O1  H3   sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
GLN   N   CA   sing N N 126 
GLN   N   H    sing N N 127 
GLN   N   H2   sing N N 128 
GLN   CA  C    sing N N 129 
GLN   CA  CB   sing N N 130 
GLN   CA  HA   sing N N 131 
GLN   C   O    doub N N 132 
GLN   C   OXT  sing N N 133 
GLN   CB  CG   sing N N 134 
GLN   CB  HB2  sing N N 135 
GLN   CB  HB3  sing N N 136 
GLN   CG  CD   sing N N 137 
GLN   CG  HG2  sing N N 138 
GLN   CG  HG3  sing N N 139 
GLN   CD  OE1  doub N N 140 
GLN   CD  NE2  sing N N 141 
GLN   NE2 HE21 sing N N 142 
GLN   NE2 HE22 sing N N 143 
GLN   OXT HXT  sing N N 144 
GLU   N   CA   sing N N 145 
GLU   N   H    sing N N 146 
GLU   N   H2   sing N N 147 
GLU   CA  C    sing N N 148 
GLU   CA  CB   sing N N 149 
GLU   CA  HA   sing N N 150 
GLU   C   O    doub N N 151 
GLU   C   OXT  sing N N 152 
GLU   CB  CG   sing N N 153 
GLU   CB  HB2  sing N N 154 
GLU   CB  HB3  sing N N 155 
GLU   CG  CD   sing N N 156 
GLU   CG  HG2  sing N N 157 
GLU   CG  HG3  sing N N 158 
GLU   CD  OE1  doub N N 159 
GLU   CD  OE2  sing N N 160 
GLU   OE2 HE2  sing N N 161 
GLU   OXT HXT  sing N N 162 
GLY   N   CA   sing N N 163 
GLY   N   H    sing N N 164 
GLY   N   H2   sing N N 165 
GLY   CA  C    sing N N 166 
GLY   CA  HA2  sing N N 167 
GLY   CA  HA3  sing N N 168 
GLY   C   O    doub N N 169 
GLY   C   OXT  sing N N 170 
GLY   OXT HXT  sing N N 171 
HIS   N   CA   sing N N 172 
HIS   N   H    sing N N 173 
HIS   N   H2   sing N N 174 
HIS   CA  C    sing N N 175 
HIS   CA  CB   sing N N 176 
HIS   CA  HA   sing N N 177 
HIS   C   O    doub N N 178 
HIS   C   OXT  sing N N 179 
HIS   CB  CG   sing N N 180 
HIS   CB  HB2  sing N N 181 
HIS   CB  HB3  sing N N 182 
HIS   CG  ND1  sing Y N 183 
HIS   CG  CD2  doub Y N 184 
HIS   ND1 CE1  doub Y N 185 
HIS   ND1 HD1  sing N N 186 
HIS   CD2 NE2  sing Y N 187 
HIS   CD2 HD2  sing N N 188 
HIS   CE1 NE2  sing Y N 189 
HIS   CE1 HE1  sing N N 190 
HIS   NE2 HE2  sing N N 191 
HIS   OXT HXT  sing N N 192 
HOH   O   H1   sing N N 193 
HOH   O   H2   sing N N 194 
ILE   N   CA   sing N N 195 
ILE   N   H    sing N N 196 
ILE   N   H2   sing N N 197 
ILE   CA  C    sing N N 198 
ILE   CA  CB   sing N N 199 
ILE   CA  HA   sing N N 200 
ILE   C   O    doub N N 201 
ILE   C   OXT  sing N N 202 
ILE   CB  CG1  sing N N 203 
ILE   CB  CG2  sing N N 204 
ILE   CB  HB   sing N N 205 
ILE   CG1 CD1  sing N N 206 
ILE   CG1 HG12 sing N N 207 
ILE   CG1 HG13 sing N N 208 
ILE   CG2 HG21 sing N N 209 
ILE   CG2 HG22 sing N N 210 
ILE   CG2 HG23 sing N N 211 
ILE   CD1 HD11 sing N N 212 
ILE   CD1 HD12 sing N N 213 
ILE   CD1 HD13 sing N N 214 
ILE   OXT HXT  sing N N 215 
LEU   N   CA   sing N N 216 
LEU   N   H    sing N N 217 
LEU   N   H2   sing N N 218 
LEU   CA  C    sing N N 219 
LEU   CA  CB   sing N N 220 
LEU   CA  HA   sing N N 221 
LEU   C   O    doub N N 222 
LEU   C   OXT  sing N N 223 
LEU   CB  CG   sing N N 224 
LEU   CB  HB2  sing N N 225 
LEU   CB  HB3  sing N N 226 
LEU   CG  CD1  sing N N 227 
LEU   CG  CD2  sing N N 228 
LEU   CG  HG   sing N N 229 
LEU   CD1 HD11 sing N N 230 
LEU   CD1 HD12 sing N N 231 
LEU   CD1 HD13 sing N N 232 
LEU   CD2 HD21 sing N N 233 
LEU   CD2 HD22 sing N N 234 
LEU   CD2 HD23 sing N N 235 
LEU   OXT HXT  sing N N 236 
LYS   N   CA   sing N N 237 
LYS   N   H    sing N N 238 
LYS   N   H2   sing N N 239 
LYS   CA  C    sing N N 240 
LYS   CA  CB   sing N N 241 
LYS   CA  HA   sing N N 242 
LYS   C   O    doub N N 243 
LYS   C   OXT  sing N N 244 
LYS   CB  CG   sing N N 245 
LYS   CB  HB2  sing N N 246 
LYS   CB  HB3  sing N N 247 
LYS   CG  CD   sing N N 248 
LYS   CG  HG2  sing N N 249 
LYS   CG  HG3  sing N N 250 
LYS   CD  CE   sing N N 251 
LYS   CD  HD2  sing N N 252 
LYS   CD  HD3  sing N N 253 
LYS   CE  NZ   sing N N 254 
LYS   CE  HE2  sing N N 255 
LYS   CE  HE3  sing N N 256 
LYS   NZ  HZ1  sing N N 257 
LYS   NZ  HZ2  sing N N 258 
LYS   NZ  HZ3  sing N N 259 
LYS   OXT HXT  sing N N 260 
MET   N   CA   sing N N 261 
MET   N   H    sing N N 262 
MET   N   H2   sing N N 263 
MET   CA  C    sing N N 264 
MET   CA  CB   sing N N 265 
MET   CA  HA   sing N N 266 
MET   C   O    doub N N 267 
MET   C   OXT  sing N N 268 
MET   CB  CG   sing N N 269 
MET   CB  HB2  sing N N 270 
MET   CB  HB3  sing N N 271 
MET   CG  SD   sing N N 272 
MET   CG  HG2  sing N N 273 
MET   CG  HG3  sing N N 274 
MET   SD  CE   sing N N 275 
MET   CE  HE1  sing N N 276 
MET   CE  HE2  sing N N 277 
MET   CE  HE3  sing N N 278 
MET   OXT HXT  sing N N 279 
PHE   N   CA   sing N N 280 
PHE   N   H    sing N N 281 
PHE   N   H2   sing N N 282 
PHE   CA  C    sing N N 283 
PHE   CA  CB   sing N N 284 
PHE   CA  HA   sing N N 285 
PHE   C   O    doub N N 286 
PHE   C   OXT  sing N N 287 
PHE   CB  CG   sing N N 288 
PHE   CB  HB2  sing N N 289 
PHE   CB  HB3  sing N N 290 
PHE   CG  CD1  doub Y N 291 
PHE   CG  CD2  sing Y N 292 
PHE   CD1 CE1  sing Y N 293 
PHE   CD1 HD1  sing N N 294 
PHE   CD2 CE2  doub Y N 295 
PHE   CD2 HD2  sing N N 296 
PHE   CE1 CZ   doub Y N 297 
PHE   CE1 HE1  sing N N 298 
PHE   CE2 CZ   sing Y N 299 
PHE   CE2 HE2  sing N N 300 
PHE   CZ  HZ   sing N N 301 
PHE   OXT HXT  sing N N 302 
PRO   N   CA   sing N N 303 
PRO   N   CD   sing N N 304 
PRO   N   H    sing N N 305 
PRO   CA  C    sing N N 306 
PRO   CA  CB   sing N N 307 
PRO   CA  HA   sing N N 308 
PRO   C   O    doub N N 309 
PRO   C   OXT  sing N N 310 
PRO   CB  CG   sing N N 311 
PRO   CB  HB2  sing N N 312 
PRO   CB  HB3  sing N N 313 
PRO   CG  CD   sing N N 314 
PRO   CG  HG2  sing N N 315 
PRO   CG  HG3  sing N N 316 
PRO   CD  HD2  sing N N 317 
PRO   CD  HD3  sing N N 318 
PRO   OXT HXT  sing N N 319 
SER   N   CA   sing N N 320 
SER   N   H    sing N N 321 
SER   N   H2   sing N N 322 
SER   CA  C    sing N N 323 
SER   CA  CB   sing N N 324 
SER   CA  HA   sing N N 325 
SER   C   O    doub N N 326 
SER   C   OXT  sing N N 327 
SER   CB  OG   sing N N 328 
SER   CB  HB2  sing N N 329 
SER   CB  HB3  sing N N 330 
SER   OG  HG   sing N N 331 
SER   OXT HXT  sing N N 332 
TFA   C1  C2   sing N N 333 
TFA   C1  O    doub N N 334 
TFA   C1  OXT  sing N N 335 
TFA   C2  F1   sing N N 336 
TFA   C2  F2   sing N N 337 
TFA   C2  F3   sing N N 338 
TFA   OXT HXT  sing N N 339 
THR   N   CA   sing N N 340 
THR   N   H    sing N N 341 
THR   N   H2   sing N N 342 
THR   CA  C    sing N N 343 
THR   CA  CB   sing N N 344 
THR   CA  HA   sing N N 345 
THR   C   O    doub N N 346 
THR   C   OXT  sing N N 347 
THR   CB  OG1  sing N N 348 
THR   CB  CG2  sing N N 349 
THR   CB  HB   sing N N 350 
THR   OG1 HG1  sing N N 351 
THR   CG2 HG21 sing N N 352 
THR   CG2 HG22 sing N N 353 
THR   CG2 HG23 sing N N 354 
THR   OXT HXT  sing N N 355 
TYR   N   CA   sing N N 356 
TYR   N   H    sing N N 357 
TYR   N   H2   sing N N 358 
TYR   CA  C    sing N N 359 
TYR   CA  CB   sing N N 360 
TYR   CA  HA   sing N N 361 
TYR   C   O    doub N N 362 
TYR   C   OXT  sing N N 363 
TYR   CB  CG   sing N N 364 
TYR   CB  HB2  sing N N 365 
TYR   CB  HB3  sing N N 366 
TYR   CG  CD1  doub Y N 367 
TYR   CG  CD2  sing Y N 368 
TYR   CD1 CE1  sing Y N 369 
TYR   CD1 HD1  sing N N 370 
TYR   CD2 CE2  doub Y N 371 
TYR   CD2 HD2  sing N N 372 
TYR   CE1 CZ   doub Y N 373 
TYR   CE1 HE1  sing N N 374 
TYR   CE2 CZ   sing Y N 375 
TYR   CE2 HE2  sing N N 376 
TYR   CZ  OH   sing N N 377 
TYR   OH  HH   sing N N 378 
TYR   OXT HXT  sing N N 379 
VAL   N   CA   sing N N 380 
VAL   N   H    sing N N 381 
VAL   N   H2   sing N N 382 
VAL   CA  C    sing N N 383 
VAL   CA  CB   sing N N 384 
VAL   CA  HA   sing N N 385 
VAL   C   O    doub N N 386 
VAL   C   OXT  sing N N 387 
VAL   CB  CG1  sing N N 388 
VAL   CB  CG2  sing N N 389 
VAL   CB  HB   sing N N 390 
VAL   CG1 HG11 sing N N 391 
VAL   CG1 HG12 sing N N 392 
VAL   CG1 HG13 sing N N 393 
VAL   CG2 HG21 sing N N 394 
VAL   CG2 HG22 sing N N 395 
VAL   CG2 HG23 sing N N 396 
VAL   OXT HXT  sing N N 397 
# 
_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                    7HE0 
_atom_sites.fract_transf_matrix[1][1]   0.011273 
_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]   0.011273 
_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]   0.025279 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
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    . VAL   A 1 3   ? 19.584 -16.178 22.300  1.00 52.13 ?  3   VAL   A N    1 
ATOM   2    C  CA   . VAL   A 1 3   ? 18.622 -15.094 22.458  1.00 51.44 ?  3   VAL   A CA   1 
ATOM   3    C  C    . VAL   A 1 3   ? 19.276 -13.756 22.126  1.00 49.33 ?  3   VAL   A C    1 
ATOM   4    O  O    . VAL   A 1 3   ? 20.401 -13.485 22.547  1.00 49.88 ?  3   VAL   A O    1 
ATOM   5    C  CB   . VAL   A 1 3   ? 18.012 -15.089 23.878  1.00 52.36 ?  3   VAL   A CB   1 
ATOM   6    C  CG1  . VAL   A 1 3   ? 16.995 -13.964 24.022  1.00 52.59 ?  3   VAL   A CG1  1 
ATOM   7    C  CG2  . VAL   A 1 3   ? 17.371 -16.435 24.189  1.00 52.61 ?  3   VAL   A CG2  1 
ATOM   8    H  HA   . VAL   A 1 3   ? 17.896 -15.228 21.834  1.00 61.73 ?  3   VAL   A HA   1 
ATOM   9    H  HB   . VAL   A 1 3   ? 18.717 -14.940 24.527  1.00 62.83 ?  3   VAL   A HB   1 
ATOM   10   H  HG11 . VAL   A 1 3   ? 16.504 -14.087 24.851  1.00 63.11 ?  3   VAL   A HG11 1 
ATOM   11   H  HG12 . VAL   A 1 3   ? 17.461 -13.114 24.039  1.00 63.11 ?  3   VAL   A HG12 1 
ATOM   12   H  HG13 . VAL   A 1 3   ? 16.382 -13.993 23.271  1.00 63.11 ?  3   VAL   A HG13 1 
ATOM   13   H  HG21 . VAL   A 1 3   ? 16.931 -16.383 25.052  1.00 63.13 ?  3   VAL   A HG21 1 
ATOM   14   H  HG22 . VAL   A 1 3   ? 16.722 -16.642 23.498  1.00 63.13 ?  3   VAL   A HG22 1 
ATOM   15   H  HG23 . VAL   A 1 3   ? 18.061 -17.117 24.210  1.00 63.13 ?  3   VAL   A HG23 1 
ATOM   16   N  N    . ASN   A 1 4   ? 18.570 -12.928 21.357  1.00 46.10 ?  4   ASN   A N    1 
ATOM   17   C  CA   . ASN   A 1 4   ? 19.004 -11.571 21.046  1.00 42.56 ?  4   ASN   A CA   1 
ATOM   18   C  C    . ASN   A 1 4   ? 17.844 -10.609 21.290  1.00 39.42 ?  4   ASN   A C    1 
ATOM   19   O  O    . ASN   A 1 4   ? 16.744 -11.013 21.678  1.00 39.16 ?  4   ASN   A O    1 
ATOM   20   C  CB   . ASN   A 1 4   ? 19.559 -11.455 19.619  1.00 41.80 ?  4   ASN   A CB   1 
ATOM   21   C  CG   . ASN   A 1 4   ? 18.553 -11.855 18.561  1.00 40.88 ?  4   ASN   A CG   1 
ATOM   22   O  OD1  . ASN   A 1 4   ? 17.438 -11.336 18.519  1.00 40.52 ?  4   ASN   A OD1  1 
ATOM   23   N  ND2  . ASN   A 1 4   ? 18.945 -12.786 17.697  1.00 40.56 ?  4   ASN   A ND2  1 
ATOM   24   H  H    . ASN   A 1 4   ? 17.817 -13.138 20.997  1.00 55.32 ?  4   ASN   A H    1 
ATOM   25   H  HA   . ASN   A 1 4   ? 19.719 -11.332 21.652  1.00 51.08 ?  4   ASN   A HA   1 
ATOM   26   H  HB2  . ASN   A 1 4   ? 19.813 -10.533 19.453  1.00 50.16 ?  4   ASN   A HB2  1 
ATOM   27   H  HB3  . ASN   A 1 4   ? 20.331 -12.033 19.533  1.00 50.16 ?  4   ASN   A HB3  1 
ATOM   28   H  HD21 . ASN   A 1 4   ? 18.413 -13.050 17.074  1.00 48.67 ?  4   ASN   A HD21 1 
ATOM   29   H  HD22 . ASN   A 1 4   ? 19.734 -13.125 17.760  1.00 48.67 ?  4   ASN   A HD22 1 
ATOM   30   N  N    . SER   A 1 5   ? 18.095 -9.321  21.053  1.00 36.32 ?  5   SER   A N    1 
ATOM   31   C  CA   . SER   A 1 5   ? 17.171 -8.261  21.436  1.00 33.35 ?  5   SER   A CA   1 
ATOM   32   C  C    . SER   A 1 5   ? 16.306 -7.754  20.282  1.00 29.87 ?  5   SER   A C    1 
ATOM   33   O  O    . SER   A 1 5   ? 15.582 -6.769  20.455  1.00 29.86 ?  5   SER   A O    1 
ATOM   34   C  CB   . SER   A 1 5   ? 17.930 -7.103  22.091  1.00 34.51 ?  5   SER   A CB   1 
ATOM   35   O  OG   . SER   A 1 5   ? 18.866 -6.529  21.195  1.00 35.19 ?  5   SER   A OG   1 
ATOM   36   H  H    . SER   A 1 5   ? 18.809 -9.037  20.665  1.00 43.58 ?  5   SER   A H    1 
ATOM   37   H  HA   . SER   A 1 5   ? 16.570 -8.614  22.105  1.00 40.01 ?  5   SER   A HA   1 
ATOM   38   H  HB2  . SER   A 1 5   ? 17.296 -6.419  22.358  1.00 41.41 ?  5   SER   A HB2  1 
ATOM   39   H  HB3  . SER   A 1 5   ? 18.402 -7.436  22.875  1.00 41.41 ?  5   SER   A HB3  1 
ATOM   40   H  HG   . SER   A 1 5   ? 19.281 -5.899  21.575  1.00 42.23 ?  5   SER   A HG   1 
ATOM   41   N  N    . PHE   A 1 6   ? 16.349 -8.400  19.120  1.00 26.01 ?  6   PHE   A N    1 
ATOM   42   C  CA   . PHE   A 1 6   ? 15.448 -8.025  18.035  1.00 22.66 ?  6   PHE   A CA   1 
ATOM   43   C  C    . PHE   A 1 6   ? 14.017 -8.392  18.415  1.00 22.67 ?  6   PHE   A C    1 
ATOM   44   O  O    . PHE   A 1 6   ? 13.757 -9.498  18.889  1.00 23.78 ?  6   PHE   A O    1 
ATOM   45   C  CB   . PHE   A 1 6   ? 15.855 -8.741  16.753  1.00 20.41 ?  6   PHE   A CB   1 
ATOM   46   C  CG   . PHE   A 1 6   ? 17.151 -8.239  16.165  1.00 19.11 ?  6   PHE   A CG   1 
ATOM   47   C  CD1  . PHE   A 1 6   ? 17.188 -7.051  15.459  1.00 18.59 ?  6   PHE   A CD1  1 
ATOM   48   C  CD2  . PHE   A 1 6   ? 18.323 -8.961  16.316  1.00 19.84 ?  6   PHE   A CD2  1 
ATOM   49   C  CE1  . PHE   A 1 6   ? 18.367 -6.587  14.916  1.00 18.61 ?  6   PHE   A CE1  1 
ATOM   50   C  CE2  . PHE   A 1 6   ? 19.506 -8.503  15.772  1.00 20.02 ?  6   PHE   A CE2  1 
ATOM   51   C  CZ   . PHE   A 1 6   ? 19.527 -7.312  15.071  1.00 19.02 ?  6   PHE   A CZ   1 
ATOM   52   H  H    . PHE   A 1 6   ? 16.876 -9.056  18.940  1.00 31.21 ?  6   PHE   A H    1 
ATOM   53   H  HA   . PHE   A 1 6   ? 15.492 -7.073  17.893  1.00 27.19 ?  6   PHE   A HA   1 
ATOM   54   H  HB2  . PHE   A 1 6   ? 15.955 -9.691  16.945  1.00 24.49 ?  6   PHE   A HB2  1 
ATOM   55   H  HB3  . PHE   A 1 6   ? 15.154 -8.617  16.094  1.00 24.49 ?  6   PHE   A HB3  1 
ATOM   56   H  HD1  . PHE   A 1 6   ? 16.402 -6.564  15.353  1.00 22.31 ?  6   PHE   A HD1  1 
ATOM   57   H  HD2  . PHE   A 1 6   ? 18.310 -9.767  16.791  1.00 23.80 ?  6   PHE   A HD2  1 
ATOM   58   H  HE1  . PHE   A 1 6   ? 18.376 -5.788  14.443  1.00 22.33 ?  6   PHE   A HE1  1 
ATOM   59   H  HE2  . PHE   A 1 6   ? 20.290 -8.994  15.881  1.00 24.02 ?  6   PHE   A HE2  1 
ATOM   60   H  HZ   . PHE   A 1 6   ? 20.321 -7.001  14.706  1.00 22.82 ?  6   PHE   A HZ   1 
ATOM   61   N  N    A SER   A 1 7   ? 13.078 -7.476  18.171  0.56 22.29 ?  7   SER   A N    1 
ATOM   62   N  N    B SER   A 1 7   ? 13.092 -7.450  18.219  0.44 22.36 ?  7   SER   A N    1 
ATOM   63   C  CA   A SER   A 1 7   ? 11.702 -7.639  18.628  0.56 22.26 ?  7   SER   A CA   1 
ATOM   64   C  CA   B SER   A 1 7   ? 11.743 -7.536  18.765  0.44 22.29 ?  7   SER   A CA   1 
ATOM   65   C  C    A SER   A 1 7   ? 10.718 -7.421  17.485  0.56 19.90 ?  7   SER   A C    1 
ATOM   66   C  C    B SER   A 1 7   ? 10.710 -7.314  17.670  0.44 20.48 ?  7   SER   A C    1 
ATOM   67   O  O    A SER   A 1 7   ? 10.898 -6.522  16.658  0.56 20.08 ?  7   SER   A O    1 
ATOM   68   O  O    B SER   A 1 7   ? 10.893 -6.468  16.790  0.44 20.59 ?  7   SER   A O    1 
ATOM   69   C  CB   A SER   A 1 7   ? 11.392 -6.650  19.763  0.56 24.26 ?  7   SER   A CB   1 
ATOM   70   C  CB   B SER   A 1 7   ? 11.545 -6.482  19.868  0.44 23.61 ?  7   SER   A CB   1 
ATOM   71   O  OG   A SER   A 1 7   ? 10.093 -6.862  20.289  0.56 25.81 ?  7   SER   A OG   1 
ATOM   72   O  OG   B SER   A 1 7   ? 10.183 -6.372  20.239  0.44 24.67 ?  7   SER   A OG   1 
ATOM   73   H  H    A SER   A 1 7   ? 13.218 -6.750  17.735  0.56 26.75 ?  7   SER   A H    1 
ATOM   74   H  H    B SER   A 1 7   ? 13.227 -6.741  17.756  0.44 26.83 ?  7   SER   A H    1 
ATOM   75   H  HA   A SER   A 1 7   ? 11.577 -8.537  18.972  0.56 26.72 ?  7   SER   A HA   1 
ATOM   76   H  HA   B SER   A 1 7   ? 11.596 -8.412  19.153  0.44 26.74 ?  7   SER   A HA   1 
ATOM   77   H  HB2  A SER   A 1 7   ? 12.041 -6.773  20.476  0.56 29.11 ?  7   SER   A HB2  1 
ATOM   78   H  HB2  B SER   A 1 7   ? 12.068 -6.737  20.647  0.44 28.33 ?  7   SER   A HB2  1 
ATOM   79   H  HB3  A SER   A 1 7   ? 11.454 -5.744  19.417  0.56 29.11 ?  7   SER   A HB3  1 
ATOM   80   H  HB3  B SER   A 1 7   ? 11.842 -5.620  19.540  0.44 28.33 ?  7   SER   A HB3  1 
ATOM   81   H  HG   A SER   A 1 7   ? 9.941  -6.305  20.902  0.56 30.97 ?  7   SER   A HG   1 
ATOM   82   H  HG   B SER   A 1 7   ? 10.093 -5.803  20.851  0.44 29.61 ?  7   SER   A HG   1 
ATOM   83   N  N    A GLY   A 1 8   ? 9.670  -8.247  17.449  0.56 17.90 ?  8   GLY   A N    1 
ATOM   84   N  N    B GLY   A 1 8   ? 9.619  -8.076  17.736  0.44 18.93 ?  8   GLY   A N    1 
ATOM   85   C  CA   A GLY   A 1 8   ? 8.579  -8.030  16.520  0.56 16.62 ?  8   GLY   A CA   1 
ATOM   86   C  CA   B GLY   A 1 8   ? 8.510  -7.886  16.826  0.44 17.89 ?  8   GLY   A CA   1 
ATOM   87   C  C    A GLY   A 1 8   ? 8.809  -8.508  15.106  0.56 15.34 ?  8   GLY   A C    1 
ATOM   88   C  C    B GLY   A 1 8   ? 8.741  -8.360  15.414  0.44 16.22 ?  8   GLY   A C    1 
ATOM   89   O  O    A GLY   A 1 8   ? 8.101  -8.064  14.194  0.56 15.73 ?  8   GLY   A O    1 
ATOM   90   O  O    B GLY   A 1 8   ? 7.928  -8.051  14.537  0.44 16.45 ?  8   GLY   A O    1 
ATOM   91   H  H    A GLY   A 1 8   ? 9.574  -8.936  17.958  0.56 21.48 ?  8   GLY   A H    1 
ATOM   92   H  H    B GLY   A 1 8   ? 9.504  -8.714  18.300  0.44 22.72 ?  8   GLY   A H    1 
ATOM   93   H  HA2  A GLY   A 1 8   ? 7.789  -8.477  16.866  0.56 19.94 ?  8   GLY   A HA2  1 
ATOM   94   H  HA2  B GLY   A 1 8   ? 7.740  -8.365  17.164  0.44 21.47 ?  8   GLY   A HA2  1 
ATOM   95   H  HA3  A GLY   A 1 8   ? 8.391  -7.081  16.482  0.56 19.94 ?  8   GLY   A HA3  1 
ATOM   96   H  HA3  B GLY   A 1 8   ? 8.289  -6.945  16.790  0.44 21.47 ?  8   GLY   A HA3  1 
ATOM   97   N  N    A TYR   A 1 9   ? 9.767  -9.405  14.890  0.56 14.38 ?  9   TYR   A N    1 
ATOM   98   N  N    B TYR   A 1 9   ? 9.815  -9.104  15.160  0.44 15.19 ?  9   TYR   A N    1 
ATOM   99   C  CA   A TYR   A 1 9   ? 10.048 -9.924  13.562  0.56 13.23 ?  9   TYR   A CA   1 
ATOM   100  C  CA   B TYR   A 1 9   ? 10.073 -9.604  13.819  0.44 14.06 ?  9   TYR   A CA   1 
ATOM   101  C  C    A TYR   A 1 9   ? 9.187  -11.146 13.265  0.56 12.78 ?  9   TYR   A C    1 
ATOM   102  C  C    B TYR   A 1 9   ? 9.252  -10.856 13.546  0.44 13.54 ?  9   TYR   A C    1 
ATOM   103  O  O    A TYR   A 1 9   ? 8.894  -11.962 14.145  0.56 14.03 ?  9   TYR   A O    1 
ATOM   104  O  O    B TYR   A 1 9   ? 9.093  -11.720 14.414  0.44 14.90 ?  9   TYR   A O    1 
ATOM   105  C  CB   A TYR   A 1 9   ? 11.525 -10.312 13.438  0.56 13.20 ?  9   TYR   A CB   1 
ATOM   106  C  CB   B TYR   A 1 9   ? 11.562 -9.910  13.634  0.44 14.14 ?  9   TYR   A CB   1 
ATOM   107  C  CG   A TYR   A 1 9   ? 12.442 -9.126  13.270  0.56 13.32 ?  9   TYR   A CG   1 
ATOM   108  C  CG   B TYR   A 1 9   ? 12.416 -8.674  13.436  0.44 14.12 ?  9   TYR   A CG   1 
ATOM   109  C  CD1  A TYR   A 1 9   ? 12.781 -8.332  14.354  0.56 13.19 ?  9   TYR   A CD1  1 
ATOM   110  C  CD1  B TYR   A 1 9   ? 12.645 -7.795  14.483  0.44 14.40 ?  9   TYR   A CD1  1 
ATOM   111  C  CD2  A TYR   A 1 9   ? 12.955 -8.793  12.023  0.56 13.52 ?  9   TYR   A CD2  1 
ATOM   112  C  CD2  B TYR   A 1 9   ? 12.984 -8.385  12.201  0.44 13.68 ?  9   TYR   A CD2  1 
ATOM   113  C  CE1  A TYR   A 1 9   ? 13.606 -7.236  14.206  0.56 13.94 ?  9   TYR   A CE1  1 
ATOM   114  C  CE1  B TYR   A 1 9   ? 13.411 -6.663  14.308  0.44 14.07 ?  9   TYR   A CE1  1 
ATOM   115  C  CE2  A TYR   A 1 9   ? 13.782 -7.702  11.863  0.56 13.81 ?  9   TYR   A CE2  1 
ATOM   116  C  CE2  B TYR   A 1 9   ? 13.755 -7.252  12.016  0.44 13.27 ?  9   TYR   A CE2  1 
ATOM   117  C  CZ   A TYR   A 1 9   ? 14.101 -6.924  12.957  0.56 14.18 ?  9   TYR   A CZ   1 
ATOM   118  C  CZ   B TYR   A 1 9   ? 13.964 -6.400  13.075  0.44 13.53 ?  9   TYR   A CZ   1 
ATOM   119  O  OH   A TYR   A 1 9   ? 14.922 -5.836  12.800  0.56 15.27 ?  9   TYR   A OH   1 
ATOM   120  O  OH   B TYR   A 1 9   ? 14.723 -5.271  12.898  0.44 14.03 ?  9   TYR   A OH   1 
ATOM   121  H  H    A TYR   A 1 9   ? 10.270 -9.738  15.503  0.56 17.26 ?  9   TYR   A H    1 
ATOM   122  H  H    B TYR   A 1 9   ? 10.408 -9.333  15.743  0.44 18.23 ?  9   TYR   A H    1 
ATOM   123  H  HA   A TYR   A 1 9   ? 9.861  -9.243  12.895  0.56 15.88 ?  9   TYR   A HA   1 
ATOM   124  H  HA   B TYR   A 1 9   ? 9.824  -8.925  13.170  0.44 16.87 ?  9   TYR   A HA   1 
ATOM   125  H  HB2  A TYR   A 1 9   ? 11.804 -10.792 14.234  0.56 15.84 ?  9   TYR   A HB2  1 
ATOM   126  H  HB2  B TYR   A 1 9   ? 11.889 -10.375 14.419  0.44 16.97 ?  9   TYR   A HB2  1 
ATOM   127  H  HB3  A TYR   A 1 9   ? 11.625 -10.875 12.659  0.56 15.84 ?  9   TYR   A HB3  1 
ATOM   128  H  HB3  B TYR   A 1 9   ? 11.670 -10.472 12.849  0.44 16.97 ?  9   TYR   A HB3  1 
ATOM   129  H  HD1  A TYR   A 1 9   ? 12.442 -8.537  15.195  0.56 15.82 ?  9   TYR   A HD1  1 
ATOM   130  H  HD1  B TYR   A 1 9   ? 12.273 -7.970  15.315  0.44 17.28 ?  9   TYR   A HD1  1 
ATOM   131  H  HD2  A TYR   A 1 9   ? 12.739 -9.319  11.283  0.56 16.23 ?  9   TYR   A HD2  1 
ATOM   132  H  HD2  B TYR   A 1 9   ? 12.841 -8.962  11.485  0.44 16.42 ?  9   TYR   A HD2  1 
ATOM   133  H  HE1  A TYR   A 1 9   ? 13.825 -6.714  14.940  0.56 16.72 ?  9   TYR   A HE1  1 
ATOM   134  H  HE1  B TYR   A 1 9   ? 13.558 -6.081  15.018  0.44 16.89 ?  9   TYR   A HE1  1 
ATOM   135  H  HE2  A TYR   A 1 9   ? 14.123 -7.497  11.021  0.56 16.57 ?  9   TYR   A HE2  1 
ATOM   136  H  HE2  B TYR   A 1 9   ? 14.131 -7.068  11.181  0.44 15.92 ?  9   TYR   A HE2  1 
ATOM   137  H  HH   A TYR   A 1 9   ? 15.044 -5.470  13.544  0.56 18.32 ?  9   TYR   A HH   1 
ATOM   138  H  HH   B TYR   A 1 9   ? 14.884 -4.905  13.638  0.44 16.84 ?  9   TYR   A HH   1 
ATOM   139  N  N    A LEU   A 1 10  ? 8.799  -11.273 12.002  0.56 12.47 ?  10  LEU   A N    1 
ATOM   140  N  N    B LEU   A 1 10  ? 8.719  -10.933 12.332  0.44 12.77 ?  10  LEU   A N    1 
ATOM   141  C  CA   A LEU   A 1 10  ? 8.208  -12.498 11.493  0.56 12.46 ?  10  LEU   A CA   1 
ATOM   142  C  CA   B LEU   A 1 10  ? 8.088  -12.145 11.837  0.44 12.42 ?  10  LEU   A CA   1 
ATOM   143  C  C    A LEU   A 1 10  ? 9.338  -13.432 11.078  0.56 12.56 ?  10  LEU   A C    1 
ATOM   144  C  C    B LEU   A 1 10  ? 9.173  -13.112 11.380  0.44 11.88 ?  10  LEU   A C    1 
ATOM   145  O  O    A LEU   A 1 10  ? 10.320 -13.000 10.470  0.56 13.10 ?  10  LEU   A O    1 
ATOM   146  O  O    B LEU   A 1 10  ? 10.074 -12.735 10.627  0.44 11.80 ?  10  LEU   A O    1 
ATOM   147  C  CB   A LEU   A 1 10  ? 7.344  -12.169 10.277  0.56 13.75 ?  10  LEU   A CB   1 
ATOM   148  C  CB   B LEU   A 1 10  ? 7.170  -11.785 10.670  0.44 13.04 ?  10  LEU   A CB   1 
ATOM   149  C  CG   A LEU   A 1 10  ? 6.615  -13.325 9.598   0.56 16.25 ?  10  LEU   A CG   1 
ATOM   150  C  CG   B LEU   A 1 10  ? 6.577  -12.936 9.858   0.44 14.46 ?  10  LEU   A CG   1 
ATOM   151  C  CD1  A LEU   A 1 10  ? 5.494  -13.839 10.482  0.56 17.67 ?  10  LEU   A CD1  1 
ATOM   152  C  CD1  B LEU   A 1 10  ? 5.673  -13.804 10.710  0.44 16.12 ?  10  LEU   A CD1  1 
ATOM   153  C  CD2  A LEU   A 1 10  ? 6.080  -12.889 8.249   0.56 17.34 ?  10  LEU   A CD2  1 
ATOM   154  C  CD2  B LEU   A 1 10  ? 5.834  -12.378 8.657   0.44 15.29 ?  10  LEU   A CD2  1 
ATOM   155  H  H    A LEU   A 1 10  ? 8.877  -10.656 11.397  0.56 14.97 ?  10  LEU   A H    1 
ATOM   156  H  H    B LEU   A 1 10  ? 8.705  -10.278 11.767  0.44 15.32 ?  10  LEU   A H    1 
ATOM   157  H  HA   A LEU   A 1 10  ? 7.664  -12.924 12.180  0.56 14.95 ?  10  LEU   A HA   1 
ATOM   158  H  HA   B LEU   A 1 10  ? 7.560  -12.558 12.539  0.44 14.90 ?  10  LEU   A HA   1 
ATOM   159  H  HB2  A LEU   A 1 10  ? 6.670  -11.534 10.552  0.56 16.50 ?  10  LEU   A HB2  1 
ATOM   160  H  HB2  B LEU   A 1 10  ? 6.422  -11.269 11.021  0.44 15.65 ?  10  LEU   A HB2  1 
ATOM   161  H  HB3  A LEU   A 1 10  ? 7.916  -11.766 9.608   0.56 16.50 ?  10  LEU   A HB3  1 
ATOM   162  H  HB3  B LEU   A 1 10  ? 7.670  -11.229 10.053  0.44 15.65 ?  10  LEU   A HB3  1 
ATOM   163  H  HG   A LEU   A 1 10  ? 7.237  -14.059 9.452   0.56 19.50 ?  10  LEU   A HG   1 
ATOM   164  H  HG   B LEU   A 1 10  ? 7.298  -13.492 9.530   0.44 17.35 ?  10  LEU   A HG   1 
ATOM   165  H  HD11 A LEU   A 1 10  ? 5.039  -14.567 10.030  0.56 21.20 ?  10  LEU   A HD11 1 
ATOM   166  H  HD11 B LEU   A 1 10  ? 5.352  -14.548 10.174  0.44 19.34 ?  10  LEU   A HD11 1 
ATOM   167  H  HD12 A LEU   A 1 10  ? 5.869  -14.155 11.320  0.56 21.20 ?  10  LEU   A HD12 1 
ATOM   168  H  HD12 B LEU   A 1 10  ? 6.176  -14.136 11.469  0.44 19.34 ?  10  LEU   A HD12 1 
ATOM   169  H  HD13 A LEU   A 1 10  ? 4.871  -13.115 10.653  0.56 21.20 ?  10  LEU   A HD13 1 
ATOM   170  H  HD13 B LEU   A 1 10  ? 4.924  -13.271 11.020  0.44 19.34 ?  10  LEU   A HD13 1 
ATOM   171  H  HD21 A LEU   A 1 10  ? 5.614  -13.636 7.842   0.56 20.80 ?  10  LEU   A HD21 1 
ATOM   172  H  HD21 B LEU   A 1 10  ? 5.459  -13.115 8.151   0.44 18.35 ?  10  LEU   A HD21 1 
ATOM   173  H  HD22 A LEU   A 1 10  ? 5.471  -12.149 8.382   0.56 20.80 ?  10  LEU   A HD22 1 
ATOM   174  H  HD22 B LEU   A 1 10  ? 5.124  -11.794 8.969   0.44 18.35 ?  10  LEU   A HD22 1 
ATOM   175  H  HD23 A LEU   A 1 10  ? 6.824  -12.617 7.693   0.56 20.80 ?  10  LEU   A HD23 1 
ATOM   176  H  HD23 B LEU   A 1 10  ? 6.457  -11.879 8.107   0.44 18.35 ?  10  LEU   A HD23 1 
ATOM   177  N  N    A LYS   A 1 11  ? 9.202  -14.712 11.412  0.56 12.61 ?  11  LYS   A N    1 
ATOM   178  N  N    B LYS   A 1 11  ? 9.094  -14.354 11.843  0.44 12.01 ?  11  LYS   A N    1 
ATOM   179  C  CA   A LYS   A 1 11  ? 10.209 -15.712 11.081  0.56 13.11 ?  11  LYS   A CA   1 
ATOM   180  C  CA   B LYS   A 1 11  ? 10.055 -15.377 11.457  0.44 12.12 ?  11  LYS   A CA   1 
ATOM   181  C  C    A LYS   A 1 11  ? 9.865  -16.308 9.722   0.56 13.41 ?  11  LYS   A C    1 
ATOM   182  C  C    B LYS   A 1 11  ? 9.688  -15.909 10.076  0.44 11.79 ?  11  LYS   A C    1 
ATOM   183  O  O    A LYS   A 1 11  ? 8.804  -16.916 9.564   0.56 15.03 ?  11  LYS   A O    1 
ATOM   184  O  O    B LYS   A 1 11  ? 8.560  -16.363 9.862   0.44 12.42 ?  11  LYS   A O    1 
ATOM   185  C  CB   A LYS   A 1 11  ? 10.244 -16.784 12.171  0.56 13.52 ?  11  LYS   A CB   1 
ATOM   186  C  CB   B LYS   A 1 11  ? 10.050 -16.498 12.494  0.44 12.13 ?  11  LYS   A CB   1 
ATOM   187  C  CG   A LYS   A 1 11  ? 11.267 -17.895 11.988  0.56 14.05 ?  11  LYS   A CG   1 
ATOM   188  C  CG   B LYS   A 1 11  ? 11.093 -17.581 12.277  0.44 12.47 ?  11  LYS   A CG   1 
ATOM   189  C  CD   A LYS   A 1 11  ? 11.348 -18.726 13.274  0.56 14.97 ?  11  LYS   A CD   1 
ATOM   190  C  CD   B LYS   A 1 11  ? 11.105 -18.555 13.449  0.44 13.12 ?  11  LYS   A CD   1 
ATOM   191  C  CE   A LYS   A 1 11  ? 12.330 -19.884 13.189  0.56 15.36 ?  11  LYS   A CE   1 
ATOM   192  C  CE   B LYS   A 1 11  ? 12.116 -19.681 13.254  0.44 13.22 ?  11  LYS   A CE   1 
ATOM   193  N  NZ   A LYS   A 1 11  ? 13.702 -19.422 12.863  0.56 15.30 ?  11  LYS   A NZ   1 
ATOM   194  N  NZ   B LYS   A 1 11  ? 13.523 -19.190 13.169  0.44 13.57 ?  11  LYS   A NZ   1 
ATOM   195  H  H    A LYS   A 1 11  ? 8.517  -15.034 11.824  0.56 15.13 ?  11  LYS   A H    1 
ATOM   196  H  H    B LYS   A 1 11  ? 8.480  -14.628 12.374  0.44 14.41 ?  11  LYS   A H    1 
ATOM   197  H  HA   A LYS   A 1 11  ? 11.080 -15.294 11.026  0.56 15.73 ?  11  LYS   A HA   1 
ATOM   198  H  HA   B LYS   A 1 11  ? 10.941 -14.985 11.411  0.44 14.55 ?  11  LYS   A HA   1 
ATOM   199  H  HB2  A LYS   A 1 11  ? 10.445 -16.350 13.015  0.56 16.22 ?  11  LYS   A HB2  1 
ATOM   200  H  HB2  B LYS   A 1 11  ? 10.211 -16.104 13.366  0.44 14.56 ?  11  LYS   A HB2  1 
ATOM   201  H  HB3  A LYS   A 1 11  ? 9.373  -17.201 12.221  0.56 16.22 ?  11  LYS   A HB3  1 
ATOM   202  H  HB3  B LYS   A 1 11  ? 9.179  -16.920 12.484  0.44 14.56 ?  11  LYS   A HB3  1 
ATOM   203  H  HG2  A LYS   A 1 11  ? 10.992 -18.476 11.260  0.56 16.86 ?  11  LYS   A HG2  1 
ATOM   204  H  HG2  B LYS   A 1 11  ? 10.880 -18.074 11.471  0.44 14.96 ?  11  LYS   A HG2  1 
ATOM   205  H  HG3  A LYS   A 1 11  ? 12.140 -17.514 11.810  0.56 16.86 ?  11  LYS   A HG3  1 
ATOM   206  H  HG3  B LYS   A 1 11  ? 11.971 -17.176 12.206  0.44 14.96 ?  11  LYS   A HG3  1 
ATOM   207  H  HD2  A LYS   A 1 11  ? 11.628 -18.153 14.003  0.56 17.96 ?  11  LYS   A HD2  1 
ATOM   208  H  HD2  B LYS   A 1 11  ? 11.338 -18.076 14.260  0.44 15.75 ?  11  LYS   A HD2  1 
ATOM   209  H  HD3  A LYS   A 1 11  ? 10.470 -19.097 13.465  0.56 17.96 ?  11  LYS   A HD3  1 
ATOM   210  H  HD3  B LYS   A 1 11  ? 10.223 -18.953 13.541  0.44 15.75 ?  11  LYS   A HD3  1 
ATOM   211  H  HE2  A LYS   A 1 11  ? 12.361 -20.344 14.046  0.56 18.44 ?  11  LYS   A HE2  1 
ATOM   212  H  HE2  B LYS   A 1 11  ? 12.058 -20.295 14.003  0.44 15.86 ?  11  LYS   A HE2  1 
ATOM   213  H  HE3  A LYS   A 1 11  ? 12.044 -20.499 12.495  0.56 18.44 ?  11  LYS   A HE3  1 
ATOM   214  H  HE3  B LYS   A 1 11  ? 11.913 -20.150 12.428  0.44 15.86 ?  11  LYS   A HE3  1 
ATOM   215  H  HZ1  A LYS   A 1 11  ? 14.258 -20.116 12.835  0.56 18.36 ?  11  LYS   A HZ1  1 
ATOM   216  H  HZ1  B LYS   A 1 11  ? 14.080 -19.877 13.058  0.44 16.28 ?  11  LYS   A HZ1  1 
ATOM   217  H  HZ2  A LYS   A 1 11  ? 13.703 -19.016 12.072  0.56 18.36 ?  11  LYS   A HZ2  1 
ATOM   218  H  HZ2  B LYS   A 1 11  ? 13.611 -18.634 12.480  0.44 16.28 ?  11  LYS   A HZ2  1 
ATOM   219  H  HZ3  A LYS   A 1 11  ? 13.984 -18.851 13.484  0.56 18.36 ?  11  LYS   A HZ3  1 
ATOM   220  H  HZ3  B LYS   A 1 11  ? 13.741 -18.761 13.917  0.44 16.28 ?  11  LYS   A HZ3  1 
ATOM   221  N  N    A LEU   A 1 12  ? 10.749 -16.130 8.739   0.56 12.36 ?  12  LEU   A N    1 
ATOM   222  N  N    B LEU   A 1 12  ? 10.623 -15.831 9.131   0.44 11.84 ?  12  LEU   A N    1 
ATOM   223  C  CA   A LEU   A 1 12  ? 10.499 -16.710 7.421   0.56 12.66 ?  12  LEU   A CA   1 
ATOM   224  C  CA   B LEU   A 1 12  ? 10.404 -16.367 7.791   0.44 12.06 ?  12  LEU   A CA   1 
ATOM   225  C  C    A LEU   A 1 12  ? 11.082 -18.109 7.277   0.56 12.64 ?  12  LEU   A C    1 
ATOM   226  C  C    B LEU   A 1 12  ? 10.961 -17.775 7.635   0.44 12.06 ?  12  LEU   A C    1 
ATOM   227  O  O    A LEU   A 1 12  ? 10.456 -18.980 6.663   0.56 12.66 ?  12  LEU   A O    1 
ATOM   228  O  O    B LEU   A 1 12  ? 10.290 -18.651 7.082   0.44 12.36 ?  12  LEU   A O    1 
ATOM   229  C  CB   A LEU   A 1 12  ? 11.053 -15.810 6.313   0.56 13.05 ?  12  LEU   A CB   1 
ATOM   230  C  CB   B LEU   A 1 12  ? 11.024 -15.450 6.730   0.44 12.99 ?  12  LEU   A CB   1 
ATOM   231  C  CG   A LEU   A 1 12  ? 10.396 -14.438 6.182   0.56 14.25 ?  12  LEU   A CG   1 
ATOM   232  C  CG   B LEU   A 1 12  ? 10.354 -14.102 6.472   0.44 13.72 ?  12  LEU   A CG   1 
ATOM   233  C  CD1  A LEU   A 1 12  ? 11.185 -13.578 5.215   0.56 15.10 ?  12  LEU   A CD1  1 
ATOM   234  C  CD1  B LEU   A 1 12  ? 10.951 -13.477 5.219   0.44 14.57 ?  12  LEU   A CD1  1 
ATOM   235  C  CD2  A LEU   A 1 12  ? 8.941  -14.570 5.732   0.56 14.77 ?  12  LEU   A CD2  1 
ATOM   236  C  CD2  B LEU   A 1 12  ? 8.847  -14.250 6.336   0.44 13.54 ?  12  LEU   A CD2  1 
ATOM   237  H  H    A LEU   A 1 12  ? 11.486 -15.674 8.803   0.56 14.83 ?  12  LEU   A H    1 
ATOM   238  H  H    B LEU   A 1 12  ? 11.392 -15.449 9.235   0.44 14.21 ?  12  LEU   A H    1 
ATOM   239  H  HA   A LEU   A 1 12  ? 9.545  -16.778 7.294   0.56 15.20 ?  12  LEU   A HA   1 
ATOM   240  H  HA   B LEU   A 1 12  ? 9.450  -16.409 7.624   0.44 14.47 ?  12  LEU   A HA   1 
ATOM   241  H  HB2  A LEU   A 1 12  ? 11.997 -15.667 6.474   0.56 15.66 ?  12  LEU   A HB2  1 
ATOM   242  H  HB2  B LEU   A 1 12  ? 11.939 -15.257 6.992   0.44 15.59 ?  12  LEU   A HB2  1 
ATOM   243  H  HB3  A LEU   A 1 12  ? 10.938 -16.270 5.464   0.56 15.66 ?  12  LEU   A HB3  1 
ATOM   244  H  HB3  B LEU   A 1 12  ? 11.029 -15.923 5.885   0.44 15.59 ?  12  LEU   A HB3  1 
ATOM   245  H  HG   A LEU   A 1 12  ? 10.403 -14.002 7.046   0.56 17.10 ?  12  LEU   A HG   1 
ATOM   246  H  HG   B LEU   A 1 12  ? 10.533 -13.506 7.216   0.44 16.47 ?  12  LEU   A HG   1 
ATOM   247  H  HD11 A LEU   A 1 12  ? 10.738 -12.723 5.119   0.56 18.12 ?  12  LEU   A HD11 1 
ATOM   248  H  HD11 B LEU   A 1 12  ? 10.534 -12.615 5.063   0.44 17.48 ?  12  LEU   A HD11 1 
ATOM   249  H  HD12 A LEU   A 1 12  ? 12.078 -13.448 5.569   0.56 18.12 ?  12  LEU   A HD12 1 
ATOM   250  H  HD12 B LEU   A 1 12  ? 11.907 -13.364 5.346   0.44 17.48 ?  12  LEU   A HD12 1 
ATOM   251  H  HD13 A LEU   A 1 12  ? 11.229 -14.028 4.357   0.56 18.12 ?  12  LEU   A HD13 1 
ATOM   252  H  HD13 B LEU   A 1 12  ? 10.787 -14.065 4.463   0.44 17.48 ?  12  LEU   A HD13 1 
ATOM   253  H  HD21 A LEU   A 1 12  ? 8.549  -13.687 5.667   0.56 17.72 ?  12  LEU   A HD21 1 
ATOM   254  H  HD21 B LEU   A 1 12  ? 8.481  -13.434 5.965   0.44 16.25 ?  12  LEU   A HD21 1 
ATOM   255  H  HD22 A LEU   A 1 12  ? 8.916  -15.006 4.866   0.56 17.72 ?  12  LEU   A HD22 1 
ATOM   256  H  HD22 B LEU   A 1 12  ? 8.658  -14.998 5.748   0.44 16.25 ?  12  LEU   A HD22 1 
ATOM   257  H  HD23 A LEU   A 1 12  ? 8.451  -15.101 6.382   0.56 17.72 ?  12  LEU   A HD23 1 
ATOM   258  H  HD23 B LEU   A 1 12  ? 8.468  -14.416 7.214   0.44 16.25 ?  12  LEU   A HD23 1 
ATOM   259  N  N    A THR   A 1 13  ? 12.278 -18.326 7.815   0.56 12.91 ?  13  THR   A N    1 
ATOM   260  N  N    B THR   A 1 13  ? 12.195 -17.994 8.080   0.44 12.02 ?  13  THR   A N    1 
ATOM   261  C  CA   A THR   A 1 13  ? 12.971 -19.601 7.715   0.56 13.11 ?  13  THR   A CA   1 
ATOM   262  C  CA   B THR   A 1 13  ? 12.844 -19.296 8.023   0.44 12.19 ?  13  THR   A CA   1 
ATOM   263  C  C    A THR   A 1 13  ? 13.738 -19.830 9.010   0.56 12.99 ?  13  THR   A C    1 
ATOM   264  C  C    B THR   A 1 13  ? 13.594 -19.512 9.334   0.44 12.75 ?  13  THR   A C    1 
ATOM   265  O  O    A THR   A 1 13  ? 13.635 -19.058 9.969   0.56 13.06 ?  13  THR   A O    1 
ATOM   266  O  O    B THR   A 1 13  ? 13.490 -18.722 10.279  0.44 13.20 ?  13  THR   A O    1 
ATOM   267  C  CB   A THR   A 1 13  ? 13.952 -19.623 6.532   0.56 14.66 ?  13  THR   A CB   1 
ATOM   268  C  CB   B THR   A 1 13  ? 13.807 -19.395 6.830   0.44 12.77 ?  13  THR   A CB   1 
ATOM   269  O  OG1  A THR   A 1 13  ? 14.981 -18.655 6.753   0.56 15.51 ?  13  THR   A OG1  1 
ATOM   270  O  OG1  B THR   A 1 13  ? 14.922 -18.527 7.053   0.44 12.93 ?  13  THR   A OG1  1 
ATOM   271  C  CG2  A THR   A 1 13  ? 13.256 -19.324 5.220   0.56 15.36 ?  13  THR   A CG2  1 
ATOM   272  C  CG2  B THR   A 1 13  ? 13.127 -19.028 5.507   0.44 13.29 ?  13  THR   A CG2  1 
ATOM   273  H  H    A THR   A 1 13  ? 12.724 -17.732 8.247   0.56 15.50 ?  13  THR   A H    1 
ATOM   274  H  H    B THR   A 1 13  ? 12.696 -17.372 8.407   0.44 14.43 ?  13  THR   A H    1 
ATOM   275  H  HA   A THR   A 1 13  ? 12.330 -20.323 7.602   0.56 15.73 ?  13  THR   A HA   1 
ATOM   276  H  HA   B THR   A 1 13  ? 12.169 -19.981 7.926   0.44 14.62 ?  13  THR   A HA   1 
ATOM   277  H  HB   A THR   A 1 13  ? 14.355 -20.504 6.467   0.56 17.60 ?  13  THR   A HB   1 
ATOM   278  H  HB   B THR   A 1 13  ? 14.122 -20.311 6.753   0.44 15.33 ?  13  THR   A HB   1 
ATOM   279  H  HG1  A THR   A 1 13  ? 15.526 -18.660 6.115   0.56 18.62 ?  13  THR   A HG1  1 
ATOM   280  H  HG1  B THR   A 1 13  ? 15.502 -18.923 7.513   0.44 15.51 ?  13  THR   A HG1  1 
ATOM   281  H  HG21 A THR   A 1 13  ? 13.833 -19.571 4.479   0.56 18.44 ?  13  THR   A HG21 1 
ATOM   282  H  HG21 B THR   A 1 13  ? 13.743 -19.163 4.765   0.44 15.94 ?  13  THR   A HG21 1 
ATOM   283  H  HG22 A THR   A 1 13  ? 12.434 -19.834 5.160   0.56 18.44 ?  13  THR   A HG22 1 
ATOM   284  H  HG22 B THR   A 1 13  ? 12.347 -19.591 5.367   0.44 15.94 ?  13  THR   A HG22 1 
ATOM   285  H  HG23 A THR   A 1 13  ? 13.049 -18.381 5.162   0.56 18.44 ?  13  THR   A HG23 1 
ATOM   286  H  HG23 B THR   A 1 13  ? 12.849 -18.102 5.519   0.44 15.94 ?  13  THR   A HG23 1 
ATOM   287  N  N    A ASP   A 1 14  ? 14.554 -20.885 9.019   0.56 13.77 ?  14  ASP   A N    1 
ATOM   288  N  N    B ASP   A 1 14  ? 14.382 -20.585 9.369   0.44 13.05 ?  14  ASP   A N    1 
ATOM   289  C  CA   A ASP   A 1 14  ? 15.394 -21.149 10.177  0.56 14.79 ?  14  ASP   A CA   1 
ATOM   290  C  CA   B ASP   A 1 14  ? 15.222 -20.873 10.525  0.44 14.16 ?  14  ASP   A CA   1 
ATOM   291  C  C    A ASP   A 1 14  ? 16.242 -19.943 10.562  0.56 13.85 ?  14  ASP   A C    1 
ATOM   292  C  C    B ASP   A 1 14  ? 16.056 -19.662 10.930  0.44 13.41 ?  14  ASP   A C    1 
ATOM   293  O  O    A ASP   A 1 14  ? 16.522 -19.741 11.750  0.56 14.27 ?  14  ASP   A O    1 
ATOM   294  O  O    B ASP   A 1 14  ? 16.226 -19.394 12.125  0.44 13.64 ?  14  ASP   A O    1 
ATOM   295  C  CB   A ASP   A 1 14  ? 16.302 -22.350 9.912   0.56 17.96 ?  14  ASP   A CB   1 
ATOM   296  C  CB   B ASP   A 1 14  ? 16.131 -22.055 10.185  0.44 16.67 ?  14  ASP   A CB   1 
ATOM   297  C  CG   A ASP   A 1 14  ? 17.220 -22.635 11.076  0.56 21.57 ?  14  ASP   A CG   1 
ATOM   298  C  CG   B ASP   A 1 14  ? 17.076 -22.424 11.317  0.44 19.85 ?  14  ASP   A CG   1 
ATOM   299  O  OD1  A ASP   A 1 14  ? 16.734 -23.180 12.091  0.56 22.49 ?  14  ASP   A OD1  1 
ATOM   300  O  OD1  B ASP   A 1 14  ? 16.602 -22.633 12.453  0.44 20.78 ?  14  ASP   A OD1  1 
ATOM   301  O  OD2  A ASP   A 1 14  ? 18.416 -22.283 10.984  0.56 23.99 -1 14  ASP   A OD2  1 
ATOM   302  O  OD2  B ASP   A 1 14  ? 18.290 -22.534 11.058  0.44 21.84 -1 14  ASP   A OD2  1 
ATOM   303  H  H    A ASP   A 1 14  ? 14.642 -21.453 8.374   0.56 16.52 ?  14  ASP   A H    1 
ATOM   304  H  H    B ASP   A 1 14  ? 14.448 -21.146 8.731   0.44 15.65 ?  14  ASP   A H    1 
ATOM   305  H  HA   A ASP   A 1 14  ? 14.835 -21.372 10.933  0.56 17.75 ?  14  ASP   A HA   1 
ATOM   306  H  HA   B ASP   A 1 14  ? 14.654 -21.116 11.276  0.44 16.99 ?  14  ASP   A HA   1 
ATOM   307  H  HB2  A ASP   A 1 14  ? 15.753 -23.145 9.753   0.56 21.56 ?  14  ASP   A HB2  1 
ATOM   308  H  HB2  B ASP   A 1 14  ? 15.572 -22.822 9.991   0.44 20.00 ?  14  ASP   A HB2  1 
ATOM   309  H  HB3  A ASP   A 1 14  ? 16.857 -22.182 9.136   0.56 21.56 ?  14  ASP   A HB3  1 
ATOM   310  H  HB3  B ASP   A 1 14  ? 16.656 -21.819 9.404   0.44 20.00 ?  14  ASP   A HB3  1 
ATOM   311  N  N    A ASN   A 1 15  ? 16.667 -19.132 9.583   0.56 12.82 ?  15  ASN   A N    1 
ATOM   312  N  N    B ASN   A 1 15  ? 16.571 -18.905 9.951   0.44 12.75 ?  15  ASN   A N    1 
ATOM   313  C  CA   A ASN   A 1 15  ? 17.656 -18.094 9.848   0.56 13.29 ?  15  ASN   A CA   1 
ATOM   314  C  CA   B ASN   A 1 15  ? 17.554 -17.863 10.220  0.44 12.84 ?  15  ASN   A CA   1 
ATOM   315  C  C    A ASN   A 1 15  ? 17.295 -16.702 9.337   0.56 13.65 ?  15  ASN   A C    1 
ATOM   316  C  C    B ASN   A 1 15  ? 17.180 -16.474 9.722   0.44 12.83 ?  15  ASN   A C    1 
ATOM   317  O  O    A ASN   A 1 15  ? 18.109 -15.786 9.501   0.56 13.93 ?  15  ASN   A O    1 
ATOM   318  O  O    B ASN   A 1 15  ? 17.888 -15.519 10.059  0.44 12.94 ?  15  ASN   A O    1 
ATOM   319  C  CB   A ASN   A 1 15  ? 19.026 -18.508 9.284   0.56 13.18 ?  15  ASN   A CB   1 
ATOM   320  C  CB   B ASN   A 1 15  ? 18.924 -18.232 9.621   0.44 13.15 ?  15  ASN   A CB   1 
ATOM   321  C  CG   A ASN   A 1 15  ? 19.031 -18.571 7.774   0.56 13.78 ?  15  ASN   A CG   1 
ATOM   322  C  CG   B ASN   A 1 15  ? 18.888 -18.391 8.110   0.44 13.59 ?  15  ASN   A CG   1 
ATOM   323  O  OD1  A ASN   A 1 15  ? 18.369 -19.416 7.170   0.56 14.34 ?  15  ASN   A OD1  1 
ATOM   324  O  OD1  B ASN   A 1 15  ? 18.104 -19.178 7.576   0.44 13.76 ?  15  ASN   A OD1  1 
ATOM   325  N  ND2  A ASN   A 1 15  ? 19.771 -17.667 7.153   0.56 14.34 ?  15  ASN   A ND2  1 
ATOM   326  N  ND2  B ASN   A 1 15  ? 19.732 -17.629 7.409   0.44 14.22 ?  15  ASN   A ND2  1 
ATOM   327  H  H    A ASN   A 1 15  ? 16.408 -19.183 8.763   0.56 15.39 ?  15  ASN   A H    1 
ATOM   328  H  H    B ASN   A 1 15  ? 16.356 -18.979 9.125   0.44 15.30 ?  15  ASN   A H    1 
ATOM   329  H  HA   A ASN   A 1 15  ? 17.767 -18.025 10.802  0.56 15.94 ?  15  ASN   A HA   1 
ATOM   330  H  HA   B ASN   A 1 15  ? 17.671 -17.803 11.182  0.44 15.41 ?  15  ASN   A HA   1 
ATOM   331  H  HB2  A ASN   A 1 15  ? 19.697 -17.857 9.562   0.56 15.81 ?  15  ASN   A HB2  1 
ATOM   332  H  HB2  B ASN   A 1 15  ? 19.556 -17.525 9.836   0.44 15.79 ?  15  ASN   A HB2  1 
ATOM   333  H  HB3  A ASN   A 1 15  ? 19.271 -19.388 9.629   0.56 15.81 ?  15  ASN   A HB3  1 
ATOM   334  H  HB3  B ASN   A 1 15  ? 19.217 -19.069 10.000  0.44 15.79 ?  15  ASN   A HB3  1 
ATOM   335  H  HD21 A ASN   A 1 15  ? 19.807 -17.661 6.297   0.56 17.21 ?  15  ASN   A HD21 1 
ATOM   336  H  HD21 B ASN   A 1 15  ? 19.753 -17.677 6.548   0.44 17.06 ?  15  ASN   A HD21 1 
ATOM   337  H  HD22 A ASN   A 1 15  ? 20.219 -17.087 7.608   0.56 17.21 ?  15  ASN   A HD22 1 
ATOM   338  H  HD22 B ASN   A 1 15  ? 20.266 -17.085 7.815   0.44 17.06 ?  15  ASN   A HD22 1 
ATOM   339  N  N    A VAL   A 1 16  ? 16.120 -16.508 8.739   0.56 13.67 ?  16  VAL   A N    1 
ATOM   340  N  N    B VAL   A 1 16  ? 16.114 -16.327 8.936   0.44 12.97 ?  16  VAL   A N    1 
ATOM   341  C  CA   A VAL   A 1 16  ? 15.735 -15.219 8.170   0.56 13.38 ?  16  VAL   A CA   1 
ATOM   342  C  CA   B VAL   A 1 16  ? 15.735 -15.048 8.344   0.44 13.29 ?  16  VAL   A CA   1 
ATOM   343  C  C    A VAL   A 1 16  ? 14.457 -14.713 8.834   0.56 12.73 ?  16  VAL   A C    1 
ATOM   344  C  C    B VAL   A 1 16  ? 14.469 -14.546 9.023   0.44 13.47 ?  16  VAL   A C    1 
ATOM   345  O  O    A VAL   A 1 16  ? 13.450 -15.431 8.900   0.56 12.76 ?  16  VAL   A O    1 
ATOM   346  O  O    B VAL   A 1 16  ? 13.479 -15.280 9.147   0.44 13.71 ?  16  VAL   A O    1 
ATOM   347  C  CB   A VAL   A 1 16  ? 15.573 -15.286 6.640   0.56 14.30 ?  16  VAL   A CB   1 
ATOM   348  C  CB   B VAL   A 1 16  ? 15.556 -15.144 6.818   0.44 13.78 ?  16  VAL   A CB   1 
ATOM   349  C  CG1  A VAL   A 1 16  ? 15.128 -13.928 6.102   0.56 14.94 ?  16  VAL   A CG1  1 
ATOM   350  C  CG1  B VAL   A 1 16  ? 15.170 -13.780 6.231   0.44 14.10 ?  16  VAL   A CG1  1 
ATOM   351  C  CG2  A VAL   A 1 16  ? 16.867 -15.735 5.973   0.56 14.84 ?  16  VAL   A CG2  1 
ATOM   352  C  CG2  B VAL   A 1 16  ? 16.821 -15.673 6.152   0.44 14.58 ?  16  VAL   A CG2  1 
ATOM   353  H  H    A VAL   A 1 16  ? 15.532 -17.131 8.642   0.56 16.40 ?  16  VAL   A H    1 
ATOM   354  H  H    B VAL   A 1 16  ? 15.583 -16.966 8.730   0.44 15.56 ?  16  VAL   A H    1 
ATOM   355  H  HA   A VAL   A 1 16  ? 16.446 -14.585 8.357   0.56 16.06 ?  16  VAL   A HA   1 
ATOM   356  H  HA   B VAL   A 1 16  ? 16.431 -14.397 8.518   0.44 15.95 ?  16  VAL   A HA   1 
ATOM   357  H  HB   A VAL   A 1 16  ? 14.889 -15.937 6.426   0.56 17.16 ?  16  VAL   A HB   1 
ATOM   358  H  HB   B VAL   A 1 16  ? 14.838 -15.763 6.623   0.44 16.54 ?  16  VAL   A HB   1 
ATOM   359  H  HG11 A VAL   A 1 16  ? 15.224 -13.926 5.138   0.56 17.93 ?  16  VAL   A HG11 1 
ATOM   360  H  HG11 B VAL   A 1 16  ? 15.237 -13.824 5.263   0.44 16.92 ?  16  VAL   A HG11 1 
ATOM   361  H  HG12 A VAL   A 1 16  ? 14.200 -13.782 6.342   0.56 17.93 ?  16  VAL   A HG12 1 
ATOM   362  H  HG12 B VAL   A 1 16  ? 14.258 -13.570 6.487   0.44 16.92 ?  16  VAL   A HG12 1 
ATOM   363  H  HG13 A VAL   A 1 16  ? 15.685 -13.237 6.491   0.56 17.93 ?  16  VAL   A HG13 1 
ATOM   364  H  HG13 B VAL   A 1 16  ? 15.775 -13.105 6.573   0.44 16.92 ?  16  VAL   A HG13 1 
ATOM   365  H  HG21 A VAL   A 1 16  ? 16.761 -15.680 5.011   0.56 17.81 ?  16  VAL   A HG21 1 
ATOM   366  H  HG21 B VAL   A 1 16  ? 16.706 -15.645 5.188   0.44 17.50 ?  16  VAL   A HG21 1 
ATOM   367  H  HG22 A VAL   A 1 16  ? 17.590 -15.155 6.260   0.56 17.81 ?  16  VAL   A HG22 1 
ATOM   368  H  HG22 B VAL   A 1 16  ? 17.572 -15.119 6.411   0.44 17.50 ?  16  VAL   A HG22 1 
ATOM   369  H  HG23 A VAL   A 1 16  ? 17.057 -16.651 6.233   0.56 17.81 ?  16  VAL   A HG23 1 
ATOM   370  H  HG23 B VAL   A 1 16  ? 16.970 -16.587 6.440   0.44 17.50 ?  16  VAL   A HG23 1 
ATOM   371  N  N    A TYR   A 1 17  ? 14.500 -13.457 9.279   0.56 12.39 ?  17  TYR   A N    1 
ATOM   372  N  N    B TYR   A 1 17  ? 14.505 -13.285 9.439   0.44 13.53 ?  17  TYR   A N    1 
ATOM   373  C  CA   A TYR   A 1 17  ? 13.410 -12.758 9.950   0.56 12.26 ?  17  TYR   A CA   1 
ATOM   374  C  CA   B TYR   A 1 17  ? 13.438 -12.628 10.171  0.44 13.22 ?  17  TYR   A CA   1 
ATOM   375  C  C    A TYR   A 1 17  ? 13.135 -11.440 9.231   0.56 11.87 ?  17  TYR   A C    1 
ATOM   376  C  C    B TYR   A 1 17  ? 13.192 -11.283 9.509   0.44 13.09 ?  17  TYR   A C    1 
ATOM   377  O  O    A TYR   A 1 17  ? 14.015 -10.909 8.549   0.56 10.56 ?  17  TYR   A O    1 
ATOM   378  O  O    B TYR   A 1 17  ? 14.139 -10.625 9.076   0.44 12.74 ?  17  TYR   A O    1 
ATOM   379  C  CB   A TYR   A 1 17  ? 13.807 -12.463 11.404  0.56 13.08 ?  17  TYR   A CB   1 
ATOM   380  C  CB   B TYR   A 1 17  ? 13.872 -12.431 11.627  0.44 13.63 ?  17  TYR   A CB   1 
ATOM   381  C  CG   A TYR   A 1 17  ? 13.955 -13.707 12.252  0.56 14.18 ?  17  TYR   A CG   1 
ATOM   382  C  CG   B TYR   A 1 17  ? 14.155 -13.726 12.364  0.44 14.53 ?  17  TYR   A CG   1 
ATOM   383  C  CD1  A TYR   A 1 17  ? 15.107 -14.488 12.196  0.56 14.92 ?  17  TYR   A CD1  1 
ATOM   384  C  CD1  B TYR   A 1 17  ? 15.376 -14.386 12.232  0.44 15.28 ?  17  TYR   A CD1  1 
ATOM   385  C  CD2  A TYR   A 1 17  ? 12.933 -14.115 13.099  0.56 14.37 ?  17  TYR   A CD2  1 
ATOM   386  C  CD2  B TYR   A 1 17  ? 13.198 -14.291 13.194  0.44 14.99 ?  17  TYR   A CD2  1 
ATOM   387  C  CE1  A TYR   A 1 17  ? 15.237 -15.642 12.964  0.56 15.06 ?  17  TYR   A CE1  1 
ATOM   388  C  CE1  B TYR   A 1 17  ? 15.627 -15.576 12.907  0.44 15.96 ?  17  TYR   A CE1  1 
ATOM   389  C  CE2  A TYR   A 1 17  ? 13.051 -15.274 13.872  0.56 14.80 ?  17  TYR   A CE2  1 
ATOM   390  C  CE2  B TYR   A 1 17  ? 13.438 -15.476 13.872  0.44 15.50 ?  17  TYR   A CE2  1 
ATOM   391  C  CZ   A TYR   A 1 17  ? 14.208 -16.031 13.803  0.56 14.70 ?  17  TYR   A CZ   1 
ATOM   392  C  CZ   B TYR   A 1 17  ? 14.651 -16.116 13.727  0.44 16.05 ?  17  TYR   A CZ   1 
ATOM   393  O  OH   A TYR   A 1 17  ? 14.332 -17.178 14.567  0.56 14.91 ?  17  TYR   A OH   1 
ATOM   394  O  OH   B TYR   A 1 17  ? 14.883 -17.294 14.404  0.44 16.91 ?  17  TYR   A OH   1 
ATOM   395  H  H    A TYR   A 1 17  ? 15.209 -12.979 9.195   0.56 14.87 ?  17  TYR   A H    1 
ATOM   396  H  H    B TYR   A 1 17  ? 15.170 -12.756 9.286   0.44 16.23 ?  17  TYR   A H    1 
ATOM   397  H  HA   A TYR   A 1 17  ? 12.618 -13.315 9.933   0.56 14.71 ?  17  TYR   A HA   1 
ATOM   398  H  HA   B TYR   A 1 17  ? 12.623 -13.153 10.139  0.44 15.86 ?  17  TYR   A HA   1 
ATOM   399  H  HB2  A TYR   A 1 17  ? 14.652 -11.994 11.409  0.56 15.70 ?  17  TYR   A HB2  1 
ATOM   400  H  HB2  B TYR   A 1 17  ? 14.682 -11.903 11.636  0.44 16.35 ?  17  TYR   A HB2  1 
ATOM   401  H  HB3  A TYR   A 1 17  ? 13.120 -11.912 11.797  0.56 15.70 ?  17  TYR   A HB3  1 
ATOM   402  H  HB3  B TYR   A 1 17  ? 13.166 -11.969 12.101  0.44 16.35 ?  17  TYR   A HB3  1 
ATOM   403  H  HD1  A TYR   A 1 17  ? 15.803 -14.237 11.634  0.56 17.90 ?  17  TYR   A HD1  1 
ATOM   404  H  HD1  B TYR   A 1 17  ? 16.033 -14.031 11.679  0.44 18.34 ?  17  TYR   A HD1  1 
ATOM   405  H  HD2  A TYR   A 1 17  ? 12.149 -13.617 13.150  0.56 17.25 ?  17  TYR   A HD2  1 
ATOM   406  H  HD2  B TYR   A 1 17  ? 12.375 -13.869 13.294  0.44 17.99 ?  17  TYR   A HD2  1 
ATOM   407  H  HE1  A TYR   A 1 17  ? 16.018 -16.153 12.918  0.56 18.07 ?  17  TYR   A HE1  1 
ATOM   408  H  HE1  B TYR   A 1 17  ? 16.448 -16.007 12.812  0.44 19.15 ?  17  TYR   A HE1  1 
ATOM   409  H  HE2  A TYR   A 1 17  ? 12.356 -15.532 14.437  0.56 17.76 ?  17  TYR   A HE2  1 
ATOM   410  H  HE2  B TYR   A 1 17  ? 12.785 -15.838 14.425  0.44 18.60 ?  17  TYR   A HE2  1 
ATOM   411  H  HH   A TYR   A 1 17  ? 13.585 -17.412 14.865  0.56 17.89 ?  17  TYR   A HH   1 
ATOM   412  H  HH   B TYR   A 1 17  ? 15.619 -17.623 14.168  0.44 20.30 ?  17  TYR   A HH   1 
ATOM   413  N  N    . ILE   A 1 18  ? 11.928 -10.880 9.408   1.00 12.97 ?  18  ILE   A N    1 
ATOM   414  C  CA   . ILE   A 1 18  ? 11.542 -9.665  8.687   1.00 12.69 ?  18  ILE   A CA   1 
ATOM   415  C  C    . ILE   A 1 18  ? 10.577 -8.801  9.497   1.00 13.12 ?  18  ILE   A C    1 
ATOM   416  O  O    . ILE   A 1 18  ? 9.751  -9.308  10.266  1.00 13.98 ?  18  ILE   A O    1 
ATOM   417  C  CB   . ILE   A 1 18  ? 10.973 -10.041 7.299   1.00 13.16 ?  18  ILE   A CB   1 
ATOM   418  C  CG1  . ILE   A 1 18  ? 10.944 -8.838  6.357   1.00 13.55 ?  18  ILE   A CG1  1 
ATOM   419  C  CG2  . ILE   A 1 18  ? 9.615  -10.731 7.431   1.00 14.13 ?  18  ILE   A CG2  1 
ATOM   420  C  CD1  . ILE   A 1 18  ? 10.729 -9.225  4.918   1.00 15.32 ?  18  ILE   A CD1  1 
ATOM   421  H  H    A ILE   A 1 18  ? 11.327 -11.185 9.938   0.56 15.56 ?  18  ILE   A H    1 
ATOM   422  H  H    B ILE   A 1 18  ? 11.260 -11.315 9.732   0.44 15.56 ?  18  ILE   A H    1 
ATOM   423  H  HA   . ILE   A 1 18  ? 12.346 -9.139  8.531   1.00 15.23 ?  18  ILE   A HA   1 
ATOM   424  H  HB   . ILE   A 1 18  ? 11.583 -10.679 6.905   1.00 15.79 ?  18  ILE   A HB   1 
ATOM   425  H  HG12 . ILE   A 1 18  ? 10.228 -8.242  6.614   1.00 16.26 ?  18  ILE   A HG12 1 
ATOM   426  H  HG13 . ILE   A 1 18  ? 11.798 -8.369  6.407   1.00 16.26 ?  18  ILE   A HG13 1 
ATOM   427  H  HG21 . ILE   A 1 18  ? 9.361  -11.090 6.565   1.00 16.96 ?  18  ILE   A HG21 1 
ATOM   428  H  HG22 . ILE   A 1 18  ? 9.691  -11.444 8.077   1.00 16.96 ?  18  ILE   A HG22 1 
ATOM   429  H  HG23 . ILE   A 1 18  ? 8.956  -10.082 7.724   1.00 16.96 ?  18  ILE   A HG23 1 
ATOM   430  H  HD11 . ILE   A 1 18  ? 10.787 -8.427  4.361   1.00 18.38 ?  18  ILE   A HD11 1 
ATOM   431  H  HD12 . ILE   A 1 18  ? 11.412 -9.857  4.651   1.00 18.38 ?  18  ILE   A HD12 1 
ATOM   432  H  HD13 . ILE   A 1 18  ? 9.851  -9.623  4.826   1.00 18.38 ?  18  ILE   A HD13 1 
ATOM   433  N  N    A LYS   A 1 19  ? 10.661 -7.484  9.291   0.56 13.45 ?  19  LYS   A N    1 
ATOM   434  N  N    B LYS   A 1 19  ? 10.699 -7.480  9.313   0.44 12.76 ?  19  LYS   A N    1 
ATOM   435  C  CA   A LYS   A 1 19  ? 9.867  -6.539  10.067  0.56 14.24 ?  19  LYS   A CA   1 
ATOM   436  C  CA   B LYS   A 1 19  ? 9.874  -6.497  10.006  0.44 12.83 ?  19  LYS   A CA   1 
ATOM   437  C  C    A LYS   A 1 19  ? 9.707  -5.252  9.268   0.56 14.04 ?  19  LYS   A C    1 
ATOM   438  C  C    B LYS   A 1 19  ? 9.657  -5.286  9.107   0.44 12.66 ?  19  LYS   A C    1 
ATOM   439  O  O    A LYS   A 1 19  ? 10.660 -4.801  8.630   0.56 13.31 ?  19  LYS   A O    1 
ATOM   440  O  O    B LYS   A 1 19  ? 10.493 -4.976  8.252   0.44 12.25 ?  19  LYS   A O    1 
ATOM   441  C  CB   A LYS   A 1 19  ? 10.576 -6.257  11.399  0.56 15.48 ?  19  LYS   A CB   1 
ATOM   442  C  CB   B LYS   A 1 19  ? 10.558 -6.026  11.296  0.44 13.46 ?  19  LYS   A CB   1 
ATOM   443  C  CG   A LYS   A 1 19  ? 9.898  -5.267  12.330  0.56 16.40 ?  19  LYS   A CG   1 
ATOM   444  C  CG   B LYS   A 1 19  ? 9.691  -5.201  12.238  0.44 14.87 ?  19  LYS   A CG   1 
ATOM   445  C  CD   A LYS   A 1 19  ? 10.786 -5.039  13.547  0.56 16.90 ?  19  LYS   A CD   1 
ATOM   446  C  CD   B LYS   A 1 19  ? 10.505 -4.772  13.452  0.44 15.89 ?  19  LYS   A CD   1 
ATOM   447  C  CE   A LYS   A 1 19  ? 10.157 -4.112  14.568  0.56 17.19 ?  19  LYS   A CE   1 
ATOM   448  C  CE   B LYS   A 1 19  ? 9.695  -3.933  14.426  0.44 16.57 ?  19  LYS   A CE   1 
ATOM   449  N  NZ   A LYS   A 1 19  ? 11.052 -3.935  15.748  0.56 17.24 ?  19  LYS   A NZ   1 
ATOM   450  N  NZ   B LYS   A 1 19  ? 10.538 -3.472  15.567  0.44 16.83 ?  19  LYS   A NZ   1 
ATOM   451  H  H    A LYS   A 1 19  ? 11.175 -7.113  8.701   0.56 16.15 ?  19  LYS   A H    1 
ATOM   452  H  H    B LYS   A 1 19  ? 11.281 -7.128  8.778   0.44 15.31 ?  19  LYS   A H    1 
ATOM   453  H  HA   A LYS   A 1 19  ? 8.993  -6.910  10.243  0.56 17.08 ?  19  LYS   A HA   1 
ATOM   454  H  HA   B LYS   A 1 19  ? 9.019  -6.895  10.223  0.44 15.39 ?  19  LYS   A HA   1 
ATOM   455  H  HB2  A LYS   A 1 19  ? 10.656 -7.097  11.881  0.56 18.57 ?  19  LYS   A HB2  1 
ATOM   456  H  HB2  B LYS   A 1 19  ? 10.851 -6.808  11.784  0.44 16.15 ?  19  LYS   A HB2  1 
ATOM   457  H  HB3  A LYS   A 1 19  ? 11.462 -5.913  11.208  0.56 18.57 ?  19  LYS   A HB3  1 
ATOM   458  H  HB3  B LYS   A 1 19  ? 11.327 -5.486  11.054  0.44 16.15 ?  19  LYS   A HB3  1 
ATOM   459  H  HG2  A LYS   A 1 19  ? 9.770  -4.421  11.874  0.56 19.68 ?  19  LYS   A HG2  1 
ATOM   460  H  HG2  B LYS   A 1 19  ? 9.377  -4.407  11.780  0.44 17.84 ?  19  LYS   A HG2  1 
ATOM   461  H  HG3  A LYS   A 1 19  ? 9.046  -5.628  12.627  0.56 19.68 ?  19  LYS   A HG3  1 
ATOM   462  H  HG3  B LYS   A 1 19  ? 8.942  -5.739  12.542  0.44 17.84 ?  19  LYS   A HG3  1 
ATOM   463  H  HD2  A LYS   A 1 19  ? 10.954 -5.891  13.978  0.56 20.28 ?  19  LYS   A HD2  1 
ATOM   464  H  HD2  B LYS   A 1 19  ? 10.816 -5.563  13.921  0.44 19.06 ?  19  LYS   A HD2  1 
ATOM   465  H  HD3  A LYS   A 1 19  ? 11.622 -4.643  13.256  0.56 20.28 ?  19  LYS   A HD3  1 
ATOM   466  H  HD3  B LYS   A 1 19  ? 11.263 -4.244  13.155  0.44 19.06 ?  19  LYS   A HD3  1 
ATOM   467  H  HE2  A LYS   A 1 19  ? 10.007 -3.240  14.166  0.56 20.62 ?  19  LYS   A HE2  1 
ATOM   468  H  HE2  B LYS   A 1 19  ? 9.349  -3.152  13.968  0.44 19.88 ?  19  LYS   A HE2  1 
ATOM   469  H  HE3  A LYS   A 1 19  ? 9.317  -4.489  14.876  0.56 20.62 ?  19  LYS   A HE3  1 
ATOM   470  H  HE3  B LYS   A 1 19  ? 8.967  -4.466  14.782  0.44 19.88 ?  19  LYS   A HE3  1 
ATOM   471  H  HZ1  A LYS   A 1 19  ? 10.690 -3.359  16.321  0.56 20.69 ?  19  LYS   A HZ1  1 
ATOM   472  H  HZ1  B LYS   A 1 19  ? 10.051 -2.983  16.128  0.44 20.20 ?  19  LYS   A HZ1  1 
ATOM   473  H  HZ2  A LYS   A 1 19  ? 11.171 -4.716  16.157  0.56 20.69 ?  19  LYS   A HZ2  1 
ATOM   474  H  HZ2  B LYS   A 1 19  ? 10.867 -4.174  16.005  0.44 20.20 ?  19  LYS   A HZ2  1 
ATOM   475  H  HZ3  A LYS   A 1 19  ? 11.842 -3.623  15.485  0.56 20.69 ?  19  LYS   A HZ3  1 
ATOM   476  H  HZ3  B LYS   A 1 19  ? 11.215 -2.978  15.265  0.44 20.20 ?  19  LYS   A HZ3  1 
ATOM   477  N  N    A ASN   A 1 20  ? 8.505  -4.669  9.292   0.56 14.84 ?  20  ASN   A N    1 
ATOM   478  N  N    B ASN   A 1 20  ? 8.533  -4.593  9.320   0.44 13.08 ?  20  ASN   A N    1 
ATOM   479  C  CA   A ASN   A 1 20  ? 8.314  -3.323  8.754   0.56 15.47 ?  20  ASN   A CA   1 
ATOM   480  C  CA   B ASN   A 1 20  ? 8.253  -3.305  8.677   0.44 13.51 ?  20  ASN   A CA   1 
ATOM   481  C  C    A ASN   A 1 20  ? 8.947  -2.336  9.723   0.56 15.42 ?  20  ASN   A C    1 
ATOM   482  C  C    B ASN   A 1 20  ? 8.820  -2.221  9.586   0.44 14.24 ?  20  ASN   A C    1 
ATOM   483  O  O    A ASN   A 1 20  ? 8.456  -2.151  10.842  0.56 15.27 ?  20  ASN   A O    1 
ATOM   484  O  O    B ASN   A 1 20  ? 8.165  -1.768  10.528  0.44 14.86 ?  20  ASN   A O    1 
ATOM   485  C  CB   A ASN   A 1 20  ? 6.826  -3.036  8.558   0.56 16.47 ?  20  ASN   A CB   1 
ATOM   486  C  CB   B ASN   A 1 20  ? 6.748  -3.137  8.479   0.44 13.61 ?  20  ASN   A CB   1 
ATOM   487  C  CG   A ASN   A 1 20  ? 6.537  -1.578  8.209   0.56 17.81 ?  20  ASN   A CG   1 
ATOM   488  C  CG   B ASN   A 1 20  ? 6.356  -1.787  7.876   0.44 13.55 ?  20  ASN   A CG   1 
ATOM   489  O  OD1  A ASN   A 1 20  ? 5.571  -1.005  8.709   0.56 19.70 ?  20  ASN   A OD1  1 
ATOM   490  O  OD1  B ASN   A 1 20  ? 5.210  -1.337  8.036   0.44 13.62 ?  20  ASN   A OD1  1 
ATOM   491  N  ND2  A ASN   A 1 20  ? 7.362  -0.979  7.350   0.56 17.85 ?  20  ASN   A ND2  1 
ATOM   492  N  ND2  B ASN   A 1 20  ? 7.286  -1.146  7.171   0.44 14.28 ?  20  ASN   A ND2  1 
ATOM   493  H  H    A ASN   A 1 20  ? 7.794  -5.033  9.607   0.56 17.81 ?  20  ASN   A H    1 
ATOM   494  H  H    B ASN   A 1 20  ? 7.910  -4.863  9.842   0.44 15.70 ?  20  ASN   A H    1 
ATOM   495  H  HA   A ASN   A 1 20  ? 8.757  -3.250  7.896   0.56 18.57 ?  20  ASN   A HA   1 
ATOM   496  H  HA   B ASN   A 1 20  ? 8.695  -3.272  7.810   0.44 16.21 ?  20  ASN   A HA   1 
ATOM   497  H  HB2  A ASN   A 1 20  ? 6.488  -3.590  7.836   0.56 19.77 ?  20  ASN   A HB2  1 
ATOM   498  H  HB2  B ASN   A 1 20  ? 6.420  -3.824  7.888   0.44 16.33 ?  20  ASN   A HB2  1 
ATOM   499  H  HB3  A ASN   A 1 20  ? 6.352  -3.244  9.380   0.56 19.77 ?  20  ASN   A HB3  1 
ATOM   500  H  HB3  B ASN   A 1 20  ? 6.311  -3.222  9.340   0.44 16.33 ?  20  ASN   A HB3  1 
ATOM   501  H  HD21 A ASN   A 1 20  ? 7.230  -0.160  7.123   0.56 21.42 ?  20  ASN   A HD21 1 
ATOM   502  H  HD21 B ASN   A 1 20  ? 7.106  -0.388  6.820   0.44 17.13 ?  20  ASN   A HD21 1 
ATOM   503  H  HD22 A ASN   A 1 20  ? 8.027  -1.414  7.021   0.56 21.42 ?  20  ASN   A HD22 1 
ATOM   504  H  HD22 B ASN   A 1 20  ? 8.069  -1.492  7.067   0.44 17.13 ?  20  ASN   A HD22 1 
ATOM   505  N  N    A ALA   A 1 21  ? 10.060 -1.730  9.316   0.56 15.63 ?  21  ALA   A N    1 
ATOM   506  N  N    B ALA   A 1 21  ? 10.058 -1.804  9.309   0.44 14.58 ?  21  ALA   A N    1 
ATOM   507  C  CA   A ALA   A 1 21  ? 10.780 -0.857  10.227  0.56 15.57 ?  21  ALA   A CA   1 
ATOM   508  C  CA   B ALA   A 1 21  ? 10.729 -0.841  10.171  0.44 14.78 ?  21  ALA   A CA   1 
ATOM   509  C  C    A ALA   A 1 21  ? 11.733 0.028   9.444   0.56 15.21 ?  21  ALA   A C    1 
ATOM   510  C  C    B ALA   A 1 21  ? 11.820 -0.118  9.393   0.44 13.86 ?  21  ALA   A C    1 
ATOM   511  O  O    A ALA   A 1 21  ? 12.212 -0.341  8.369   0.56 15.59 ?  21  ALA   A O    1 
ATOM   512  O  O    B ALA   A 1 21  ? 12.281 -0.584  8.348   0.44 13.95 ?  21  ALA   A O    1 
ATOM   513  C  CB   A ALA   A 1 21  ? 11.562 -1.671  11.260  0.56 16.14 ?  21  ALA   A CB   1 
ATOM   514  C  CB   B ALA   A 1 21  ? 11.324 -1.513  11.413  0.44 16.16 ?  21  ALA   A CB   1 
ATOM   515  H  H    A ALA   A 1 21  ? 10.411 -1.813  8.534   0.56 18.76 ?  21  ALA   A H    1 
ATOM   516  H  H    B ALA   A 1 21  ? 10.521 -2.060  8.629   0.44 17.50 ?  21  ALA   A H    1 
ATOM   517  H  HA   A ALA   A 1 21  ? 10.145 -0.290  10.693  0.56 18.68 ?  21  ALA   A HA   1 
ATOM   518  H  HA   B ALA   A 1 21  ? 10.084 -0.183  10.467  0.44 17.74 ?  21  ALA   A HA   1 
ATOM   519  H  HB1  A ALA   A 1 21  ? 11.992 -1.058  11.872  0.56 19.37 ?  21  ALA   A HB1  1 
ATOM   520  H  HB1  B ALA   A 1 21  ? 11.759 -0.839  11.958  0.44 19.39 ?  21  ALA   A HB1  1 
ATOM   521  H  HB2  A ALA   A 1 21  ? 10.939 -2.239  11.744  0.56 19.37 ?  21  ALA   A HB2  1 
ATOM   522  H  HB2  B ALA   A 1 21  ? 10.610 -1.935  11.917  0.44 19.39 ?  21  ALA   A HB2  1 
ATOM   523  H  HB3  A ALA   A 1 21  ? 12.219 -2.213  10.803  0.56 19.37 ?  21  ALA   A HB3  1 
ATOM   524  H  HB3  B ALA   A 1 21  ? 11.970 -2.181  11.134  0.44 19.39 ?  21  ALA   A HB3  1 
ATOM   525  N  N    A ASP   A 1 22  ? 11.980 1.211   10.001  0.56 15.13 ?  22  ASP   A N    1 
ATOM   526  N  N    B ASP   A 1 22  ? 12.217 1.037   9.930   0.44 13.82 ?  22  ASP   A N    1 
ATOM   527  C  CA   A ASP   A 1 22  ? 13.038 2.097   9.539   0.56 14.72 ?  22  ASP   A CA   1 
ATOM   528  C  CA   B ASP   A 1 22  ? 13.351 1.804   9.427   0.44 13.95 ?  22  ASP   A CA   1 
ATOM   529  C  C    A ASP   A 1 22  ? 14.358 1.593   10.112  0.56 13.63 ?  22  ASP   A C    1 
ATOM   530  C  C    B ASP   A 1 22  ? 14.623 1.216   10.026  0.44 12.67 ?  22  ASP   A C    1 
ATOM   531  O  O    A ASP   A 1 22  ? 14.545 1.583   11.333  0.56 14.00 ?  22  ASP   A O    1 
ATOM   532  O  O    B ASP   A 1 22  ? 14.746 1.115   11.251  0.44 12.92 ?  22  ASP   A O    1 
ATOM   533  C  CB   A ASP   A 1 22  ? 12.729 3.508   10.034  0.56 16.14 ?  22  ASP   A CB   1 
ATOM   534  C  CB   B ASP   A 1 22  ? 13.188 3.260   9.863   0.44 15.52 ?  22  ASP   A CB   1 
ATOM   535  C  CG   A ASP   A 1 22  ? 13.765 4.529   9.602   0.56 17.45 ?  22  ASP   A CG   1 
ATOM   536  C  CG   B ASP   A 1 22  ? 14.175 4.202   9.193   0.44 16.57 ?  22  ASP   A CG   1 
ATOM   537  O  OD1  A ASP   A 1 22  ? 14.857 4.143   9.137   0.56 17.61 ?  22  ASP   A OD1  1 
ATOM   538  O  OD1  B ASP   A 1 22  ? 15.248 3.738   8.755   0.44 15.72 ?  22  ASP   A OD1  1 
ATOM   539  O  OD2  A ASP   A 1 22  ? 13.481 5.737   9.733   0.56 18.84 -1 22  ASP   A OD2  1 
ATOM   540  O  OD2  B ASP   A 1 22  ? 13.881 5.416   9.118   0.44 18.25 -1 22  ASP   A OD2  1 
ATOM   541  H  H    A ASP   A 1 22  ? 11.524 1.531   10.660  0.56 18.16 ?  22  ASP   A H    1 
ATOM   542  H  H    B ASP   A 1 22  ? 11.831 1.401   10.607  0.44 16.58 ?  22  ASP   A H    1 
ATOM   543  H  HA   A ASP   A 1 22  ? 13.080 2.096   8.569   0.56 17.66 ?  22  ASP   A HA   1 
ATOM   544  H  HA   B ASP   A 1 22  ? 13.387 1.751   8.457   0.44 16.74 ?  22  ASP   A HA   1 
ATOM   545  H  HB2  A ASP   A 1 22  ? 11.865 3.784   9.684   0.56 19.37 ?  22  ASP   A HB2  1 
ATOM   546  H  HB2  B ASP   A 1 22  ? 12.291 3.554   9.648   0.44 18.62 ?  22  ASP   A HB2  1 
ATOM   547  H  HB3  A ASP   A 1 22  ? 12.700 3.501   11.005  0.56 19.37 ?  22  ASP   A HB3  1 
ATOM   548  H  HB3  B ASP   A 1 22  ? 13.338 3.317   10.818  0.44 18.62 ?  22  ASP   A HB3  1 
ATOM   549  N  N    A ILE   A 1 23  ? 15.269 1.167   9.231   0.56 13.30 ?  23  ILE   A N    1 
ATOM   550  N  N    B ILE   A 1 23  ? 15.565 0.818   9.166   0.44 12.25 ?  23  ILE   A N    1 
ATOM   551  C  CA   A ILE   A 1 23  ? 16.520 0.562   9.683   0.56 13.20 ?  23  ILE   A CA   1 
ATOM   552  C  CA   B ILE   A 1 23  ? 16.796 0.196   9.647   0.44 11.79 ?  23  ILE   A CA   1 
ATOM   553  C  C    A ILE   A 1 23  ? 17.309 1.517   10.566  0.56 13.21 ?  23  ILE   A C    1 
ATOM   554  C  C    B ILE   A 1 23  ? 17.540 1.122   10.600  0.44 12.42 ?  23  ILE   A C    1 
ATOM   555  O  O    A ILE   A 1 23  ? 18.028 1.082   11.474  0.56 13.49 ?  23  ILE   A O    1 
ATOM   556  O  O    B ILE   A 1 23  ? 18.209 0.659   11.533  0.44 12.53 ?  23  ILE   A O    1 
ATOM   557  C  CB   A ILE   A 1 23  ? 17.340 0.051   8.479   0.56 12.83 ?  23  ILE   A CB   1 
ATOM   558  C  CB   B ILE   A 1 23  ? 17.678 -0.274  8.469   0.44 11.33 ?  23  ILE   A CB   1 
ATOM   559  C  CG1  A ILE   A 1 23  ? 18.451 -0.895  8.945   0.56 12.93 ?  23  ILE   A CG1  1 
ATOM   560  C  CG1  B ILE   A 1 23  ? 18.748 -1.248  8.977   0.44 11.76 ?  23  ILE   A CG1  1 
ATOM   561  C  CG2  A ILE   A 1 23  ? 17.895 1.216   7.662   0.56 13.04 ?  23  ILE   A CG2  1 
ATOM   562  C  CG2  B ILE   A 1 23  ? 18.308 0.915   7.735   0.44 11.08 ?  23  ILE   A CG2  1 
ATOM   563  C  CD1  A ILE   A 1 23  ? 19.164 -1.595  7.808   0.56 13.11 ?  23  ILE   A CD1  1 
ATOM   564  C  CD1  B ILE   A 1 23  ? 19.607 -1.862  7.887   0.44 12.26 ?  23  ILE   A CD1  1 
ATOM   565  H  H    A ILE   A 1 23  ? 15.183 1.218   8.380   0.56 15.96 ?  23  ILE   A H    1 
ATOM   566  H  H    B ILE   A 1 23  ? 15.515 0.895   8.319   0.44 14.70 ?  23  ILE   A H    1 
ATOM   567  H  HA   A ILE   A 1 23  ? 16.301 -0.208  10.228  0.56 15.84 ?  23  ILE   A HA   1 
ATOM   568  H  HA   B ILE   A 1 23  ? 16.550 -0.597  10.146  0.44 14.15 ?  23  ILE   A HA   1 
ATOM   569  H  HB   A ILE   A 1 23  ? 16.743 -0.454  7.909   0.56 15.40 ?  23  ILE   A HB   1 
ATOM   570  H  HB   B ILE   A 1 23  ? 17.115 -0.753  7.840   0.44 13.60 ?  23  ILE   A HB   1 
ATOM   571  H  HG12 A ILE   A 1 23  ? 19.112 -0.388  9.441   0.56 15.52 ?  23  ILE   A HG12 1 
ATOM   572  H  HG12 B ILE   A 1 23  ? 19.337 -0.777  9.585   0.44 14.11 ?  23  ILE   A HG12 1 
ATOM   573  H  HG13 A ILE   A 1 23  ? 18.064 -1.579  9.516   0.56 15.52 ?  23  ILE   A HG13 1 
ATOM   574  H  HG13 B ILE   A 1 23  ? 18.308 -1.977  9.447   0.44 14.11 ?  23  ILE   A HG13 1 
ATOM   575  H  HG21 A ILE   A 1 23  ? 18.239 0.875   6.820   0.56 15.65 ?  23  ILE   A HG21 1 
ATOM   576  H  HG21 B ILE   A 1 23  ? 18.699 0.599   6.901   0.44 13.30 ?  23  ILE   A HG21 1 
ATOM   577  H  HG22 A ILE   A 1 23  ? 17.178 1.848   7.490   0.56 15.65 ?  23  ILE   A HG22 1 
ATOM   578  H  HG22 B ILE   A 1 23  ? 17.619 1.569   7.547   0.44 13.30 ?  23  ILE   A HG22 1 
ATOM   579  H  HG23 A ILE   A 1 23  ? 18.605 1.647   8.160   0.56 15.65 ?  23  ILE   A HG23 1 
ATOM   580  H  HG23 B ILE   A 1 23  ? 18.996 1.306   8.293   0.44 13.30 ?  23  ILE   A HG23 1 
ATOM   581  H  HD11 A ILE   A 1 23  ? 19.801 -2.227  8.176   0.56 15.73 ?  23  ILE   A HD11 1 
ATOM   582  H  HD11 B ILE   A 1 23  ? 20.199 -2.521  8.286   0.44 14.71 ?  23  ILE   A HD11 1 
ATOM   583  H  HD12 A ILE   A 1 23  ? 18.509 -2.062  7.266   0.56 15.73 ?  23  ILE   A HD12 1 
ATOM   584  H  HD12 B ILE   A 1 23  ? 19.032 -2.288  7.233   0.44 14.71 ?  23  ILE   A HD12 1 
ATOM   585  H  HD13 A ILE   A 1 23  ? 19.627 -0.933  7.271   0.56 15.73 ?  23  ILE   A HD13 1 
ATOM   586  H  HD13 B ILE   A 1 23  ? 20.129 -1.163  7.465   0.44 14.71 ?  23  ILE   A HD13 1 
ATOM   587  N  N    A VAL   A 1 24  ? 17.185 2.826   10.332  0.56 13.48 ?  24  VAL   A N    1 
ATOM   588  N  N    B VAL   A 1 24  ? 17.427 2.437   10.395  0.44 13.37 ?  24  VAL   A N    1 
ATOM   589  C  CA   A VAL   A 1 24  ? 17.855 3.798   11.192  0.56 14.66 ?  24  VAL   A CA   1 
ATOM   590  C  CA   B VAL   A 1 24  ? 18.075 3.398   11.287  0.44 14.27 ?  24  VAL   A CA   1 
ATOM   591  C  C    A VAL   A 1 24  ? 17.316 3.708   12.612  0.56 15.32 ?  24  VAL   A C    1 
ATOM   592  C  C    B VAL   A 1 24  ? 17.498 3.296   12.694  0.44 14.94 ?  24  VAL   A C    1 
ATOM   593  O  O    A VAL   A 1 24  ? 18.078 3.635   13.585  0.56 15.79 ?  24  VAL   A O    1 
ATOM   594  O  O    B VAL   A 1 24  ? 18.236 3.301   13.689  0.44 15.31 ?  24  VAL   A O    1 
ATOM   595  C  CB   A VAL   A 1 24  ? 17.707 5.220   10.619  0.56 15.47 ?  24  VAL   A CB   1 
ATOM   596  C  CB   B VAL   A 1 24  ? 17.940 4.820   10.710  0.44 15.24 ?  24  VAL   A CB   1 
ATOM   597  C  CG1  A VAL   A 1 24  ? 18.232 6.259   11.612  0.56 16.10 ?  24  VAL   A CG1  1 
ATOM   598  C  CG1  B VAL   A 1 24  ? 18.519 5.846   11.669  0.44 16.40 ?  24  VAL   A CG1  1 
ATOM   599  C  CG2  A VAL   A 1 24  ? 18.428 5.335   9.289   0.56 16.01 ?  24  VAL   A CG2  1 
ATOM   600  C  CG2  B VAL   A 1 24  ? 18.614 4.901   9.346   0.44 15.66 ?  24  VAL   A CG2  1 
ATOM   601  H  H    A VAL   A 1 24  ? 16.722 3.172   9.694   0.56 16.17 ?  24  VAL   A H    1 
ATOM   602  H  H    B VAL   A 1 24  ? 16.987 2.791   9.751   0.44 16.05 ?  24  VAL   A H    1 
ATOM   603  H  HA   A VAL   A 1 24  ? 18.799 3.594   11.222  0.56 17.59 ?  24  VAL   A HA   1 
ATOM   604  H  HA   B VAL   A 1 24  ? 19.020 3.189   11.336  0.44 17.12 ?  24  VAL   A HA   1 
ATOM   605  H  HB   A VAL   A 1 24  ? 16.767 5.407   10.462  0.56 18.56 ?  24  VAL   A HB   1 
ATOM   606  H  HB   B VAL   A 1 24  ? 16.999 5.023   10.588  0.44 18.29 ?  24  VAL   A HB   1 
ATOM   607  H  HG11 A VAL   A 1 24  ? 18.381 7.095   11.145  0.56 19.32 ?  24  VAL   A HG11 1 
ATOM   608  H  HG11 B VAL   A 1 24  ? 18.743 6.648   11.173  0.44 19.68 ?  24  VAL   A HG11 1 
ATOM   609  H  HG12 A VAL   A 1 24  ? 17.577 6.386   12.315  0.56 19.32 ?  24  VAL   A HG12 1 
ATOM   610  H  HG12 B VAL   A 1 24  ? 17.851 6.047   12.340  0.44 19.68 ?  24  VAL   A HG12 1 
ATOM   611  H  HG13 A VAL   A 1 24  ? 19.068 5.938   11.988  0.56 19.32 ?  24  VAL   A HG13 1 
ATOM   612  H  HG13 B VAL   A 1 24  ? 19.315 5.478   12.083  0.44 19.68 ?  24  VAL   A HG13 1 
ATOM   613  H  HG21 A VAL   A 1 24  ? 18.263 6.214   8.914   0.56 19.21 ?  24  VAL   A HG21 1 
ATOM   614  H  HG21 B VAL   A 1 24  ? 18.534 5.807   9.007   0.44 18.79 ?  24  VAL   A HG21 1 
ATOM   615  H  HG22 A VAL   A 1 24  ? 19.379 5.214   9.435   0.56 19.21 ?  24  VAL   A HG22 1 
ATOM   616  H  HG22 B VAL   A 1 24  ? 19.550 4.666   9.442   0.44 18.79 ?  24  VAL   A HG22 1 
ATOM   617  H  HG23 A VAL   A 1 24  ? 18.095 4.651   8.687   0.56 19.21 ?  24  VAL   A HG23 1 
ATOM   618  H  HG23 B VAL   A 1 24  ? 18.178 4.283   8.738   0.44 18.79 ?  24  VAL   A HG23 1 
ATOM   619  N  N    A GLU   A 1 25  ? 15.990 3.715   12.753  0.56 16.09 ?  25  GLU   A N    1 
ATOM   620  N  N    B GLU   A 1 25  ? 16.171 3.197   12.798  0.44 15.50 ?  25  GLU   A N    1 
ATOM   621  C  CA   A GLU   A 1 25  ? 15.399 3.668   14.085  0.56 17.19 ?  25  GLU   A CA   1 
ATOM   622  C  CA   B GLU   A 1 25  ? 15.526 3.090   14.103  0.44 16.80 ?  25  GLU   A CA   1 
ATOM   623  C  C    A GLU   A 1 25  ? 15.633 2.315   14.747  0.56 16.15 ?  25  GLU   A C    1 
ATOM   624  C  C    B GLU   A 1 25  ? 15.813 1.744   14.758  0.44 15.73 ?  25  GLU   A C    1 
ATOM   625  O  O    A GLU   A 1 25  ? 15.844 2.241   15.963  0.56 16.80 ?  25  GLU   A O    1 
ATOM   626  O  O    B GLU   A 1 25  ? 16.041 1.676   15.971  0.44 15.91 ?  25  GLU   A O    1 
ATOM   627  C  CB   A GLU   A 1 25  ? 13.911 4.017   14.013  0.56 19.72 ?  25  GLU   A CB   1 
ATOM   628  C  CB   B GLU   A 1 25  ? 14.022 3.330   13.959  0.44 18.53 ?  25  GLU   A CB   1 
ATOM   629  C  CG   A GLU   A 1 25  ? 13.656 5.486   13.682  0.56 22.75 ?  25  GLU   A CG   1 
ATOM   630  C  CG   B GLU   A 1 25  ? 13.683 4.702   13.405  0.44 21.14 ?  25  GLU   A CG   1 
ATOM   631  C  CD   A GLU   A 1 25  ? 14.476 6.442   14.540  0.56 25.32 ?  25  GLU   A CD   1 
ATOM   632  C  CD   B GLU   A 1 25  ? 14.194 5.819   14.288  0.44 23.47 ?  25  GLU   A CD   1 
ATOM   633  O  OE1  A GLU   A 1 25  ? 14.539 6.241   15.772  0.56 26.03 ?  25  GLU   A OE1  1 
ATOM   634  O  OE1  B GLU   A 1 25  ? 14.149 5.665   15.528  0.44 24.23 ?  25  GLU   A OE1  1 
ATOM   635  O  OE2  A GLU   A 1 25  ? 15.077 7.382   13.977  0.56 26.52 -1 25  GLU   A OE2  1 
ATOM   636  O  OE2  B GLU   A 1 25  ? 14.646 6.846   13.744  0.44 24.63 -1 25  GLU   A OE2  1 
ATOM   637  H  H    A GLU   A 1 25  ? 15.421 3.758   12.103  0.56 19.31 ?  25  GLU   A H    1 
ATOM   638  H  H    B GLU   A 1 25  ? 15.631 3.189   12.132  0.44 18.61 ?  25  GLU   A H    1 
ATOM   639  H  HA   A GLU   A 1 25  ? 15.835 4.331   14.637  0.56 20.63 ?  25  GLU   A HA   1 
ATOM   640  H  HA   B GLU   A 1 25  ? 15.884 3.774   14.686  0.44 20.16 ?  25  GLU   A HA   1 
ATOM   641  H  HB2  A GLU   A 1 25  ? 13.487 3.484   13.318  0.56 23.67 ?  25  GLU   A HB2  1 
ATOM   642  H  HB2  B GLU   A 1 25  ? 13.652 2.668   13.357  0.44 22.23 ?  25  GLU   A HB2  1 
ATOM   643  H  HB3  A GLU   A 1 25  ? 13.494 3.831   14.868  0.56 23.67 ?  25  GLU   A HB3  1 
ATOM   644  H  HB3  B GLU   A 1 25  ? 13.606 3.253   14.832  0.44 22.23 ?  25  GLU   A HB3  1 
ATOM   645  H  HG2  A GLU   A 1 25  ? 13.897 5.649   12.759  0.56 27.30 ?  25  GLU   A HG2  1 
ATOM   646  H  HG2  B GLU   A 1 25  ? 14.086 4.799   12.527  0.44 25.37 ?  25  GLU   A HG2  1 
ATOM   647  H  HG3  A GLU   A 1 25  ? 12.716 5.685   13.823  0.56 27.30 ?  25  GLU   A HG3  1 
ATOM   648  H  HG3  B GLU   A 1 25  ? 12.719 4.789   13.339  0.44 25.37 ?  25  GLU   A HG3  1 
ATOM   649  N  N    A GLU   A 1 26  ? 15.619 1.236   13.962  0.56 15.94 ?  26  GLU   A N    1 
ATOM   650  N  N    B GLU   A 1 26  ? 15.818 0.662   13.974  0.44 15.51 ?  26  GLU   A N    1 
ATOM   651  C  CA   A GLU   A 1 26  ? 15.925 -0.081  14.512  0.56 15.82 ?  26  GLU   A CA   1 
ATOM   652  C  CA   B GLU   A 1 26  ? 16.204 -0.636  14.520  0.44 15.50 ?  26  GLU   A CA   1 
ATOM   653  C  C    A GLU   A 1 26  ? 17.353 -0.138  15.035  0.56 15.59 ?  26  GLU   A C    1 
ATOM   654  C  C    B GLU   A 1 26  ? 17.624 -0.593  15.067  0.44 14.79 ?  26  GLU   A C    1 
ATOM   655  O  O    A GLU   A 1 26  ? 17.606 -0.637  16.137  0.56 16.16 ?  26  GLU   A O    1 
ATOM   656  O  O    B GLU   A 1 26  ? 17.901 -1.125  16.147  0.44 14.91 ?  26  GLU   A O    1 
ATOM   657  C  CB   A GLU   A 1 26  ? 15.725 -1.149  13.439  0.56 16.80 ?  26  GLU   A CB   1 
ATOM   658  C  CB   B GLU   A 1 26  ? 16.074 -1.723  13.449  0.44 16.75 ?  26  GLU   A CB   1 
ATOM   659  C  CG   A GLU   A 1 26  ? 14.300 -1.609  13.270  0.56 19.38 ?  26  GLU   A CG   1 
ATOM   660  C  CG   B GLU   A 1 26  ? 14.647 -2.081  13.083  0.44 17.54 ?  26  GLU   A CG   1 
ATOM   661  C  CD   A GLU   A 1 26  ? 13.833 -2.480  14.419  0.56 21.31 ?  26  GLU   A CD   1 
ATOM   662  C  CD   B GLU   A 1 26  ? 13.870 -2.656  14.246  0.44 18.02 ?  26  GLU   A CD   1 
ATOM   663  O  OE1  A GLU   A 1 26  ? 14.381 -3.590  14.593  0.56 22.06 ?  26  GLU   A OE1  1 
ATOM   664  O  OE1  B GLU   A 1 26  ? 14.288 -3.699  14.800  0.44 18.64 ?  26  GLU   A OE1  1 
ATOM   665  O  OE2  A GLU   A 1 26  ? 12.927 -2.042  15.156  0.56 22.56 -1 26  GLU   A OE2  1 
ATOM   666  O  OE2  B GLU   A 1 26  ? 12.838 -2.056  14.603  0.44 17.45 -1 26  GLU   A OE2  1 
ATOM   667  H  H    A GLU   A 1 26  ? 15.431 1.248   13.124  0.56 19.13 ?  26  GLU   A H    1 
ATOM   668  H  H    B GLU   A 1 26  ? 15.614 0.653   13.140  0.44 18.61 ?  26  GLU   A H    1 
ATOM   669  H  HA   A GLU   A 1 26  ? 15.318 -0.262  15.245  0.56 18.99 ?  26  GLU   A HA   1 
ATOM   670  H  HA   B GLU   A 1 26  ? 15.614 -0.866  15.251  0.44 18.61 ?  26  GLU   A HA   1 
ATOM   671  H  HB2  A GLU   A 1 26  ? 16.023 -0.794  12.588  0.56 20.16 ?  26  GLU   A HB2  1 
ATOM   672  H  HB2  B GLU   A 1 26  ? 16.511 -1.422  12.637  0.44 20.10 ?  26  GLU   A HB2  1 
ATOM   673  H  HB3  A GLU   A 1 26  ? 16.259 -1.921  13.678  0.56 20.16 ?  26  GLU   A HB3  1 
ATOM   674  H  HB3  B GLU   A 1 26  ? 16.503 -2.535  13.767  0.44 20.10 ?  26  GLU   A HB3  1 
ATOM   675  H  HG2  A GLU   A 1 26  ? 13.722 -0.833  13.236  0.56 23.26 ?  26  GLU   A HG2  1 
ATOM   676  H  HG2  B GLU   A 1 26  ? 14.187 -1.284  12.778  0.44 21.05 ?  26  GLU   A HG2  1 
ATOM   677  H  HG3  A GLU   A 1 26  ? 14.228 -2.113  12.443  0.56 23.26 ?  26  GLU   A HG3  1 
ATOM   678  H  HG3  B GLU   A 1 26  ? 14.651 -2.752  12.383  0.44 21.05 ?  26  GLU   A HG3  1 
ATOM   679  N  N    A ALA   A 1 27  ? 18.306 0.367   14.248  0.56 15.40 ?  27  ALA   A N    1 
ATOM   680  N  N    B ALA   A 1 27  ? 18.539 0.049   14.340  0.44 14.73 ?  27  ALA   A N    1 
ATOM   681  C  CA   A ALA   A 1 27  ? 19.702 0.315   14.662  0.56 15.83 ?  27  ALA   A CA   1 
ATOM   682  C  CA   B ALA   A 1 27  ? 19.916 0.140   14.815  0.44 15.32 ?  27  ALA   A CA   1 
ATOM   683  C  C    A ALA   A 1 27  ? 19.910 1.067   15.968  0.56 17.30 ?  27  ALA   A C    1 
ATOM   684  C  C    B ALA   A 1 27  ? 20.004 1.001   16.070  0.44 16.71 ?  27  ALA   A C    1 
ATOM   685  O  O    A ALA   A 1 27  ? 20.606 0.584   16.869  0.56 17.61 ?  27  ALA   A O    1 
ATOM   686  O  O    B ALA   A 1 27  ? 20.657 0.623   17.050  0.44 16.70 ?  27  ALA   A O    1 
ATOM   687  C  CB   A ALA   A 1 27  ? 20.594 0.886   13.559  0.56 15.41 ?  27  ALA   A CB   1 
ATOM   688  C  CB   B ALA   A 1 27  ? 20.819 0.683   13.706  0.44 15.18 ?  27  ALA   A CB   1 
ATOM   689  H  H    A ALA   A 1 27  ? 18.164 0.747   13.489  0.56 18.48 ?  27  ALA   A H    1 
ATOM   690  H  H    B ALA   A 1 27  ? 18.391 0.423   13.581  0.44 17.68 ?  27  ALA   A H    1 
ATOM   691  H  HA   A ALA   A 1 27  ? 19.949 -0.607  14.804  0.56 19.00 ?  27  ALA   A HA   1 
ATOM   692  H  HA   B ALA   A 1 27  ? 20.231 -0.749  15.041  0.44 18.39 ?  27  ALA   A HA   1 
ATOM   693  H  HB1  A ALA   A 1 27  ? 21.517 0.842   13.849  0.56 18.49 ?  27  ALA   A HB1  1 
ATOM   694  H  HB1  B ALA   A 1 27  ? 21.730 0.738   14.040  0.44 18.21 ?  27  ALA   A HB1  1 
ATOM   695  H  HB2  A ALA   A 1 27  ? 20.471 0.359   12.753  0.56 18.49 ?  27  ALA   A HB2  1 
ATOM   696  H  HB2  B ALA   A 1 27  ? 20.786 0.080   12.945  0.44 18.21 ?  27  ALA   A HB2  1 
ATOM   697  H  HB3  A ALA   A 1 27  ? 20.341 1.808   13.393  0.56 18.49 ?  27  ALA   A HB3  1 
ATOM   698  H  HB3  B ALA   A 1 27  ? 20.510 1.563   13.445  0.44 18.21 ?  27  ALA   A HB3  1 
ATOM   699  N  N    A LYS   A 1 28  ? 19.299 2.245   16.097  0.56 19.14 ?  28  LYS   A N    1 
ATOM   700  N  N    B LYS   A 1 28  ? 19.342 2.162   16.064  0.44 18.39 ?  28  LYS   A N    1 
ATOM   701  C  CA   A LYS   A 1 28  ? 19.468 3.026   17.317  0.56 21.62 ?  28  LYS   A CA   1 
ATOM   702  C  CA   B LYS   A 1 28  ? 19.376 3.038   17.232  0.44 20.62 ?  28  LYS   A CA   1 
ATOM   703  C  C    A LYS   A 1 28  ? 18.890 2.310   18.530  0.56 22.29 ?  28  LYS   A C    1 
ATOM   704  C  C    B LYS   A 1 28  ? 18.893 2.311   18.481  0.44 21.70 ?  28  LYS   A C    1 
ATOM   705  O  O    A LYS   A 1 28  ? 19.384 2.497   19.647  0.56 23.85 ?  28  LYS   A O    1 
ATOM   706  O  O    B LYS   A 1 28  ? 19.459 2.482   19.566  0.44 22.92 ?  28  LYS   A O    1 
ATOM   707  C  CB   A LYS   A 1 28  ? 18.853 4.417   17.147  0.56 23.77 ?  28  LYS   A CB   1 
ATOM   708  C  CB   B LYS   A 1 28  ? 18.541 4.297   16.978  0.44 22.15 ?  28  LYS   A CB   1 
ATOM   709  C  CG   A LYS   A 1 28  ? 19.634 5.296   16.181  0.56 26.01 ?  28  LYS   A CG   1 
ATOM   710  C  CG   B LYS   A 1 28  ? 19.266 5.361   16.166  0.44 24.11 ?  28  LYS   A CG   1 
ATOM   711  C  CD   A LYS   A 1 28  ? 19.186 6.746   16.225  0.56 28.47 ?  28  LYS   A CD   1 
ATOM   712  C  CD   B LYS   A 1 28  ? 18.613 6.733   16.301  0.44 26.53 ?  28  LYS   A CD   1 
ATOM   713  C  CE   A LYS   A 1 28  ? 17.866 6.945   15.511  0.56 30.29 ?  28  LYS   A CE   1 
ATOM   714  C  CE   B LYS   A 1 28  ? 17.776 7.081   15.083  0.44 28.46 ?  28  LYS   A CE   1 
ATOM   715  N  NZ   A LYS   A 1 28  ? 17.501 8.387   15.442  0.56 31.48 ?  28  LYS   A NZ   1 
ATOM   716  N  NZ   B LYS   A 1 28  ? 17.547 8.551   14.965  0.44 29.49 ?  28  LYS   A NZ   1 
ATOM   717  H  H    A LYS   A 1 28  ? 18.795 2.607   15.505  0.56 22.97 ?  28  LYS   A H    1 
ATOM   718  H  H    B LYS   A 1 28  ? 18.871 2.454   15.410  0.44 22.07 ?  28  LYS   A H    1 
ATOM   719  H  HA   A LYS   A 1 28  ? 20.414 3.145   17.479  0.56 25.94 ?  28  LYS   A HA   1 
ATOM   720  H  HA   B LYS   A 1 28  ? 20.287 3.316   17.394  0.44 24.74 ?  28  LYS   A HA   1 
ATOM   721  H  HB2  A LYS   A 1 28  ? 17.951 4.326   16.805  0.56 28.53 ?  28  LYS   A HB2  1 
ATOM   722  H  HB2  B LYS   A 1 28  ? 17.740 4.054   16.488  0.44 26.58 ?  28  LYS   A HB2  1 
ATOM   723  H  HB3  A LYS   A 1 28  ? 18.837 4.863   18.009  0.56 28.53 ?  28  LYS   A HB3  1 
ATOM   724  H  HB3  B LYS   A 1 28  ? 18.299 4.691   17.830  0.44 26.58 ?  28  LYS   A HB3  1 
ATOM   725  H  HG2  A LYS   A 1 28  ? 20.575 5.264   16.413  0.56 31.21 ?  28  LYS   A HG2  1 
ATOM   726  H  HG2  B LYS   A 1 28  ? 20.180 5.435   16.480  0.44 28.93 ?  28  LYS   A HG2  1 
ATOM   727  H  HG3  A LYS   A 1 28  ? 19.503 4.968   15.278  0.56 31.21 ?  28  LYS   A HG3  1 
ATOM   728  H  HG3  B LYS   A 1 28  ? 19.255 5.109   15.229  0.44 28.93 ?  28  LYS   A HG3  1 
ATOM   729  H  HD2  A LYS   A 1 28  ? 19.076 7.019   17.149  0.56 34.16 ?  28  LYS   A HD2  1 
ATOM   730  H  HD2  B LYS   A 1 28  ? 18.033 6.740   17.079  0.44 31.83 ?  28  LYS   A HD2  1 
ATOM   731  H  HD3  A LYS   A 1 28  ? 19.854 7.299   15.790  0.56 34.16 ?  28  LYS   A HD3  1 
ATOM   732  H  HD3  B LYS   A 1 28  ? 19.304 7.407   16.395  0.44 31.83 ?  28  LYS   A HD3  1 
ATOM   733  H  HE2  A LYS   A 1 28  ? 17.937 6.605   14.604  0.56 36.35 ?  28  LYS   A HE2  1 
ATOM   734  H  HE2  B LYS   A 1 28  ? 18.242 6.790   14.287  0.44 34.16 ?  28  LYS   A HE2  1 
ATOM   735  H  HE3  A LYS   A 1 28  ? 17.166 6.476   15.992  0.56 36.35 ?  28  LYS   A HE3  1 
ATOM   736  H  HE3  B LYS   A 1 28  ? 16.913 6.641   15.148  0.44 34.16 ?  28  LYS   A HE3  1 
ATOM   737  H  HZ1  A LYS   A 1 28  ? 16.725 8.485   15.020  0.56 37.77 ?  28  LYS   A HZ1  1 
ATOM   738  H  HZ1  B LYS   A 1 28  ? 17.056 8.726   14.244  0.44 35.39 ?  28  LYS   A HZ1  1 
ATOM   739  H  HZ2  A LYS   A 1 28  ? 17.429 8.721   16.264  0.56 37.77 ?  28  LYS   A HZ2  1 
ATOM   740  H  HZ2  B LYS   A 1 28  ? 17.122 8.852   15.686  0.44 35.39 ?  28  LYS   A HZ2  1 
ATOM   741  H  HZ3  A LYS   A 1 28  ? 18.130 8.838   15.001  0.56 37.77 ?  28  LYS   A HZ3  1 
ATOM   742  H  HZ3  B LYS   A 1 28  ? 18.328 8.974   14.892  0.44 35.39 ?  28  LYS   A HZ3  1 
ATOM   743  N  N    . LYS   A 1 29  ? 17.861 1.481   18.339  1.00 22.24 ?  29  LYS   A N    1 
ATOM   744  C  CA   . LYS   A 1 29  ? 17.283 0.768   19.475  1.00 24.70 ?  29  LYS   A CA   1 
ATOM   745  C  C    . LYS   A 1 29  ? 18.120 -0.449  19.862  1.00 24.38 ?  29  LYS   A C    1 
ATOM   746  O  O    . LYS   A 1 29  ? 18.412 -0.660  21.045  1.00 25.23 ?  29  LYS   A O    1 
ATOM   747  C  CB   . LYS   A 1 29  ? 15.852 0.338   19.138  1.00 27.98 ?  29  LYS   A CB   1 
ATOM   748  C  CG   . LYS   A 1 29  ? 15.083 -0.273  20.304  1.00 31.69 ?  29  LYS   A CG   1 
ATOM   749  C  CD   . LYS   A 1 29  ? 14.708 0.782   21.334  1.00 35.24 ?  29  LYS   A CD   1 
ATOM   750  C  CE   . LYS   A 1 29  ? 13.807 0.207   22.417  1.00 37.54 ?  29  LYS   A CE   1 
ATOM   751  N  NZ   . LYS   A 1 29  ? 13.404 1.242   23.409  1.00 38.97 ?  29  LYS   A NZ   1 
ATOM   752  H  H    A LYS   A 1 29  ? 17.484 1.321   17.582  0.56 26.69 ?  29  LYS   A H    1 
ATOM   753  H  H    B LYS   A 1 29  ? 17.480 1.304   17.588  0.44 26.69 ?  29  LYS   A H    1 
ATOM   754  H  HA   . LYS   A 1 29  ? 17.244 1.359   20.240  1.00 29.64 ?  29  LYS   A HA   1 
ATOM   755  H  HB2  . LYS   A 1 29  ? 15.355 1.116   18.839  1.00 33.57 ?  29  LYS   A HB2  1 
ATOM   756  H  HB3  . LYS   A 1 29  ? 15.881 -0.323  18.430  1.00 33.57 ?  29  LYS   A HB3  1 
ATOM   757  H  HG2  . LYS   A 1 29  ? 14.264 -0.676  19.973  1.00 38.03 ?  29  LYS   A HG2  1 
ATOM   758  H  HG3  . LYS   A 1 29  ? 15.631 -0.944  20.741  1.00 38.03 ?  29  LYS   A HG3  1 
ATOM   759  H  HD2  . LYS   A 1 29  ? 15.514 1.118   21.756  1.00 42.28 ?  29  LYS   A HD2  1 
ATOM   760  H  HD3  . LYS   A 1 29  ? 14.232 1.504   20.894  1.00 42.28 ?  29  LYS   A HD3  1 
ATOM   761  H  HE2  . LYS   A 1 29  ? 13.003 -0.149  22.007  1.00 45.04 ?  29  LYS   A HE2  1 
ATOM   762  H  HE3  . LYS   A 1 29  ? 14.282 -0.495  22.888  1.00 45.04 ?  29  LYS   A HE3  1 
ATOM   763  H  HZ1  . LYS   A 1 29  ? 12.879 0.880   24.030  1.00 46.77 ?  29  LYS   A HZ1  1 
ATOM   764  H  HZ2  . LYS   A 1 29  ? 14.126 1.582   23.803  1.00 46.77 ?  29  LYS   A HZ2  1 
ATOM   765  H  HZ3  . LYS   A 1 29  ? 12.961 1.897   23.001  1.00 46.77 ?  29  LYS   A HZ3  1 
ATOM   766  N  N    . VAL   A 1 30  ? 18.493 -1.270  18.880  1.00 23.44 ?  30  VAL   A N    1 
ATOM   767  C  CA   . VAL   A 1 30  ? 19.137 -2.549  19.166  1.00 22.67 ?  30  VAL   A CA   1 
ATOM   768  C  C    . VAL   A 1 30  ? 20.642 -2.398  19.383  1.00 21.79 ?  30  VAL   A C    1 
ATOM   769  O  O    . VAL   A 1 30  ? 21.233 -3.136  20.179  1.00 22.36 ?  30  VAL   A O    1 
ATOM   770  C  CB   . VAL   A 1 30  ? 18.819 -3.539  18.030  1.00 23.63 ?  30  VAL   A CB   1 
ATOM   771  C  CG1  . VAL   A 1 30  ? 19.589 -4.841  18.208  1.00 24.33 ?  30  VAL   A CG1  1 
ATOM   772  C  CG2  . VAL   A 1 30  ? 17.321 -3.807  17.966  1.00 24.30 ?  30  VAL   A CG2  1 
ATOM   773  H  H    . VAL   A 1 30  ? 18.372 -1.118  18.043  1.00 28.12 ?  30  VAL   A H    1 
ATOM   774  H  HA   . VAL   A 1 30  ? 18.755 -2.914  19.977  1.00 27.20 ?  30  VAL   A HA   1 
ATOM   775  H  HB   . VAL   A 1 30  ? 19.087 -3.153  17.183  1.00 28.36 ?  30  VAL   A HB   1 
ATOM   776  H  HG11 . VAL   A 1 30  ? 19.204 -5.517  17.626  1.00 29.20 ?  30  VAL   A HG11 1 
ATOM   777  H  HG12 . VAL   A 1 30  ? 20.518 -4.696  17.972  1.00 29.20 ?  30  VAL   A HG12 1 
ATOM   778  H  HG13 . VAL   A 1 30  ? 19.519 -5.125  19.132  1.00 29.20 ?  30  VAL   A HG13 1 
ATOM   779  H  HG21 . VAL   A 1 30  ? 17.145 -4.470  17.277  1.00 29.16 ?  30  VAL   A HG21 1 
ATOM   780  H  HG22 . VAL   A 1 30  ? 17.023 -4.144  18.827  1.00 29.16 ?  30  VAL   A HG22 1 
ATOM   781  H  HG23 . VAL   A 1 30  ? 16.861 -2.982  17.755  1.00 29.16 ?  30  VAL   A HG23 1 
ATOM   782  N  N    . LYS   A 1 31  ? 21.282 -1.457  18.699  1.00 21.07 ?  31  LYS   A N    1 
ATOM   783  C  CA   . LYS   A 1 31  ? 22.737 -1.355  18.658  1.00 21.97 ?  31  LYS   A CA   1 
ATOM   784  C  C    . LYS   A 1 31  ? 23.342 -2.710  18.281  1.00 19.64 ?  31  LYS   A C    1 
ATOM   785  O  O    . LYS   A 1 31  ? 24.134 -3.278  19.040  1.00 20.48 ?  31  LYS   A O    1 
ATOM   786  C  CB   . LYS   A 1 31  ? 23.309 -0.844  19.973  1.00 27.71 ?  31  LYS   A CB   1 
ATOM   787  C  CG   . LYS   A 1 31  ? 22.609 0.403   20.500  1.00 34.34 ?  31  LYS   A CG   1 
ATOM   788  C  CD   . LYS   A 1 31  ? 23.589 1.534   20.775  1.00 39.42 ?  31  LYS   A CD   1 
ATOM   789  C  CE   . LYS   A 1 31  ? 22.985 2.588   21.695  1.00 42.98 ?  31  LYS   A CE   1 
ATOM   790  N  NZ   . LYS   A 1 31  ? 21.714 3.161   21.172  1.00 44.79 ?  31  LYS   A NZ   1 
ATOM   791  H  H    . LYS   A 1 31  ? 20.887 -0.852  18.241  1.00 25.28 ?  31  LYS   A H    1 
ATOM   792  H  HA   . LYS   A 1 31  ? 22.982 -0.723  17.970  1.00 26.37 ?  31  LYS   A HA   1 
ATOM   793  H  HB2  . LYS   A 1 31  ? 23.230 -1.543  20.638  1.00 33.25 ?  31  LYS   A HB2  1 
ATOM   794  H  HB3  . LYS   A 1 31  ? 24.247 -0.626  19.837  1.00 33.25 ?  31  LYS   A HB3  1 
ATOM   795  H  HG2  . LYS   A 1 31  ? 21.982 0.714   19.834  1.00 41.21 ?  31  LYS   A HG2  1 
ATOM   796  H  HG3  . LYS   A 1 31  ? 22.136 0.192   21.319  1.00 41.21 ?  31  LYS   A HG3  1 
ATOM   797  H  HD2  . LYS   A 1 31  ? 24.383 1.177   21.203  1.00 47.30 ?  31  LYS   A HD2  1 
ATOM   798  H  HD3  . LYS   A 1 31  ? 23.825 1.961   19.936  1.00 47.30 ?  31  LYS   A HD3  1 
ATOM   799  H  HE2  . LYS   A 1 31  ? 22.797 2.183   22.555  1.00 51.57 ?  31  LYS   A HE2  1 
ATOM   800  H  HE3  . LYS   A 1 31  ? 23.619 3.314   21.802  1.00 51.57 ?  31  LYS   A HE3  1 
ATOM   801  H  HZ1  . LYS   A 1 31  ? 21.403 3.776   21.737  1.00 53.74 ?  31  LYS   A HZ1  1 
ATOM   802  H  HZ2  . LYS   A 1 31  ? 21.854 3.542   20.381  1.00 53.74 ?  31  LYS   A HZ2  1 
ATOM   803  H  HZ3  . LYS   A 1 31  ? 21.104 2.519   21.082  1.00 53.74 ?  31  LYS   A HZ3  1 
ATOM   804  N  N    . PRO   A 1 32  ? 22.987 -3.246  17.119  1.00 17.37 ?  32  PRO   A N    1 
ATOM   805  C  CA   . PRO   A 1 32  ? 23.452 -4.581  16.748  1.00 17.46 ?  32  PRO   A CA   1 
ATOM   806  C  C    . PRO   A 1 32  ? 24.953 -4.589  16.536  1.00 17.44 ?  32  PRO   A C    1 
ATOM   807  O  O    . PRO   A 1 32  ? 25.592 -3.553  16.328  1.00 17.65 ?  32  PRO   A O    1 
ATOM   808  C  CB   . PRO   A 1 32  ? 22.717 -4.847  15.430  1.00 17.29 ?  32  PRO   A CB   1 
ATOM   809  C  CG   . PRO   A 1 32  ? 22.526 -3.476  14.846  1.00 16.26 ?  32  PRO   A CG   1 
ATOM   810  C  CD   . PRO   A 1 32  ? 22.251 -2.595  16.024  1.00 16.40 ?  32  PRO   A CD   1 
ATOM   811  H  HA   . PRO   A 1 32  ? 23.202 -5.246  17.411  1.00 20.95 ?  32  PRO   A HA   1 
ATOM   812  H  HB2  . PRO   A 1 32  ? 23.262 -5.403  14.847  1.00 20.74 ?  32  PRO   A HB2  1 
ATOM   813  H  HB3  . PRO   A 1 32  ? 21.860 -5.275  15.606  1.00 20.74 ?  32  PRO   A HB3  1 
ATOM   814  H  HG2  . PRO   A 1 32  ? 23.333 -3.205  14.388  1.00 19.51 ?  32  PRO   A HG2  1 
ATOM   815  H  HG3  . PRO   A 1 32  ? 21.769 -3.486  14.237  1.00 19.51 ?  32  PRO   A HG3  1 
ATOM   816  H  HD2  . PRO   A 1 32  ? 22.605 -1.708  15.857  1.00 19.68 ?  32  PRO   A HD2  1 
ATOM   817  H  HD3  . PRO   A 1 32  ? 21.303 -2.576  16.211  1.00 19.68 ?  32  PRO   A HD3  1 
ATOM   818  N  N    . THR   A 1 33  ? 25.514 -5.795  16.577  1.00 17.44 ?  33  THR   A N    1 
ATOM   819  C  CA   . THR   A 1 33  ? 26.924 -5.950  16.250  1.00 17.76 ?  33  THR   A CA   1 
ATOM   820  C  C    . THR   A 1 33  ? 27.206 -5.480  14.830  1.00 16.04 ?  33  THR   A C    1 
ATOM   821  O  O    . THR   A 1 33  ? 28.234 -4.836  14.576  1.00 16.48 ?  33  THR   A O    1 
ATOM   822  C  CB   . THR   A 1 33  ? 27.333 -7.410  16.441  1.00 19.23 ?  33  THR   A CB   1 
ATOM   823  O  OG1  . THR   A 1 33  ? 27.029 -7.809  17.780  1.00 21.06 ?  33  THR   A OG1  1 
ATOM   824  C  CG2  . THR   A 1 33  ? 28.819 -7.598  16.191  1.00 20.10 ?  33  THR   A CG2  1 
ATOM   825  H  H    . THR   A 1 33  ? 25.107 -6.525  16.779  1.00 20.93 ?  33  THR   A H    1 
ATOM   826  H  HA   . THR   A 1 33  ? 27.453 -5.411  16.857  1.00 21.31 ?  33  THR   A HA   1 
ATOM   827  H  HB   . THR   A 1 33  ? 26.842 -7.974  15.819  1.00 23.08 ?  33  THR   A HB   1 
ATOM   828  H  HG1  . THR   A 1 33  ? 27.451 -7.332  18.330  1.00 25.27 ?  33  THR   A HG1  1 
ATOM   829  H  HG21 . THR   A 1 33  ? 29.090 -8.491  16.460  1.00 24.12 ?  33  THR   A HG21 1 
ATOM   830  H  HG22 . THR   A 1 33  ? 29.016 -7.481  15.250  1.00 24.12 ?  33  THR   A HG22 1 
ATOM   831  H  HG23 . THR   A 1 33  ? 29.323 -6.949  16.705  1.00 24.12 ?  33  THR   A HG23 1 
ATOM   832  N  N    . VAL   A 1 34  ? 26.303 -5.781  13.895  1.00 14.41 ?  34  VAL   A N    1 
ATOM   833  C  CA   . VAL   A 1 34  ? 26.486 -5.446  12.487  1.00 13.25 ?  34  VAL   A CA   1 
ATOM   834  C  C    . VAL   A 1 34  ? 25.183 -4.882  11.931  1.00 12.71 ?  34  VAL   A C    1 
ATOM   835  O  O    . VAL   A 1 34  ? 24.142 -5.550  11.980  1.00 13.20 ?  34  VAL   A O    1 
ATOM   836  C  CB   . VAL   A 1 34  ? 26.920 -6.661  11.648  1.00 14.08 ?  34  VAL   A CB   1 
ATOM   837  C  CG1  . VAL   A 1 34  ? 27.103 -6.261  10.192  1.00 14.29 ?  34  VAL   A CG1  1 
ATOM   838  C  CG2  . VAL   A 1 34  ? 28.192 -7.290  12.205  1.00 15.55 ?  34  VAL   A CG2  1 
ATOM   839  H  H    . VAL   A 1 34  ? 25.564 -6.191  14.059  1.00 17.29 ?  34  VAL   A H    1 
ATOM   840  H  HA   . VAL   A 1 34  ? 27.167 -4.762  12.404  1.00 15.90 ?  34  VAL   A HA   1 
ATOM   841  H  HB   . VAL   A 1 34  ? 26.218 -7.330  11.684  1.00 16.90 ?  34  VAL   A HB   1 
ATOM   842  H  HG11 . VAL   A 1 34  ? 27.583 -6.966  9.731   1.00 17.15 ?  34  VAL   A HG11 1 
ATOM   843  H  HG12 . VAL   A 1 34  ? 26.233 -6.134  9.783   1.00 17.15 ?  34  VAL   A HG12 1 
ATOM   844  H  HG13 . VAL   A 1 34  ? 27.612 -5.436  10.153  1.00 17.15 ?  34  VAL   A HG13 1 
ATOM   845  H  HG21 . VAL   A 1 34  ? 28.457 -8.027  11.630  1.00 18.66 ?  34  VAL   A HG21 1 
ATOM   846  H  HG22 . VAL   A 1 34  ? 28.892 -6.621  12.229  1.00 18.66 ?  34  VAL   A HG22 1 
ATOM   847  H  HG23 . VAL   A 1 34  ? 28.017 -7.619  13.101  1.00 18.66 ?  34  VAL   A HG23 1 
ATOM   848  N  N    . VAL   A 1 35  ? 25.243 -3.666  11.387  1.00 12.11 ?  35  VAL   A N    1 
ATOM   849  C  CA   . VAL   A 1 35  ? 24.212 -3.140  10.501  1.00 11.63 ?  35  VAL   A CA   1 
ATOM   850  C  C    . VAL   A 1 35  ? 24.764 -3.144  9.083   1.00 10.75 ?  35  VAL   A C    1 
ATOM   851  O  O    . VAL   A 1 35  ? 25.911 -2.748  8.848   1.00 11.55 ?  35  VAL   A O    1 
ATOM   852  C  CB   . VAL   A 1 35  ? 23.693 -1.746  10.914  1.00 12.16 ?  35  VAL   A CB   1 
ATOM   853  C  CG1  . VAL   A 1 35  ? 24.769 -0.662  10.774  1.00 12.94 ?  35  VAL   A CG1  1 
ATOM   854  C  CG2  . VAL   A 1 35  ? 22.457 -1.386  10.096  1.00 12.72 ?  35  VAL   A CG2  1 
ATOM   855  H  H    . VAL   A 1 35  ? 25.885 -3.110  11.521  1.00 14.53 ?  35  VAL   A H    1 
ATOM   856  H  HA   . VAL   A 1 35  ? 23.453 -3.747  10.516  1.00 13.96 ?  35  VAL   A HA   1 
ATOM   857  H  HB   . VAL   A 1 35  ? 23.420 -1.777  11.843  1.00 14.60 ?  35  VAL   A HB   1 
ATOM   858  H  HG11 . VAL   A 1 35  ? 24.433 0.168   11.156  1.00 15.52 ?  35  VAL   A HG11 1 
ATOM   859  H  HG12 . VAL   A 1 35  ? 25.563 -0.945  11.249  1.00 15.52 ?  35  VAL   A HG12 1 
ATOM   860  H  HG13 . VAL   A 1 35  ? 24.971 -0.531  9.834   1.00 15.52 ?  35  VAL   A HG13 1 
ATOM   861  H  HG21 . VAL   A 1 35  ? 22.105 -0.539  10.408  1.00 15.26 ?  35  VAL   A HG21 1 
ATOM   862  H  HG22 . VAL   A 1 35  ? 22.708 -1.313  9.159   1.00 15.26 ?  35  VAL   A HG22 1 
ATOM   863  H  HG23 . VAL   A 1 35  ? 21.791 -2.082  10.204  1.00 15.26 ?  35  VAL   A HG23 1 
ATOM   864  N  N    . VAL   A 1 36  ? 23.950 -3.599  8.138   1.00 10.40 ?  36  VAL   A N    1 
ATOM   865  C  CA   . VAL   A 1 36  ? 24.320 -3.614  6.729   1.00 10.16 ?  36  VAL   A CA   1 
ATOM   866  C  C    . VAL   A 1 36  ? 23.860 -2.322  6.070   1.00 10.27 ?  36  VAL   A C    1 
ATOM   867  O  O    . VAL   A 1 36  ? 22.698 -1.914  6.211   1.00 10.90 ?  36  VAL   A O    1 
ATOM   868  C  CB   . VAL   A 1 36  ? 23.703 -4.824  6.014   1.00 10.31 ?  36  VAL   A CB   1 
ATOM   869  C  CG1  . VAL   A 1 36  ? 23.957 -4.739  4.523   1.00 10.72 ?  36  VAL   A CG1  1 
ATOM   870  C  CG2  . VAL   A 1 36  ? 24.242 -6.113  6.590   1.00 11.30 ?  36  VAL   A CG2  1 
ATOM   871  H  H    . VAL   A 1 36  ? 23.164 -3.911  8.288   1.00 12.48 ?  36  VAL   A H    1 
ATOM   872  H  HA   . VAL   A 1 36  ? 25.289 -3.677  6.648   1.00 12.19 ?  36  VAL   A HA   1 
ATOM   873  H  HB   . VAL   A 1 36  ? 22.743 -4.810  6.153   1.00 12.37 ?  36  VAL   A HB   1 
ATOM   874  H  HG11 . VAL   A 1 36  ? 23.823 -5.615  4.132   1.00 12.86 ?  36  VAL   A HG11 1 
ATOM   875  H  HG12 . VAL   A 1 36  ? 23.336 -4.104  4.129   1.00 12.86 ?  36  VAL   A HG12 1 
ATOM   876  H  HG13 . VAL   A 1 36  ? 24.869 -4.446  4.375   1.00 12.86 ?  36  VAL   A HG13 1 
ATOM   877  H  HG21 . VAL   A 1 36  ? 23.854 -6.865  6.114   1.00 13.56 ?  36  VAL   A HG21 1 
ATOM   878  H  HG22 . VAL   A 1 36  ? 25.210 -6.127  6.490   1.00 13.56 ?  36  VAL   A HG22 1 
ATOM   879  H  HG23 . VAL   A 1 36  ? 24.011 -6.166  7.532   1.00 13.56 ?  36  VAL   A HG23 1 
ATOM   880  N  N    . ASN   A 1 37  ? 24.779 -1.684  5.344   1.00 9.95  ?  37  ASN   A N    1 
ATOM   881  C  CA   . ASN   A 1 37  ? 24.453 -0.569  4.473   1.00 9.59  ?  37  ASN   A CA   1 
ATOM   882  C  C    . ASN   A 1 37  ? 24.314 -1.041  3.034   1.00 9.79  ?  37  ASN   A C    1 
ATOM   883  O  O    . ASN   A 1 37  ? 25.098 -1.868  2.553   1.00 10.50 ?  37  ASN   A O    1 
ATOM   884  C  CB   . ASN   A 1 37  ? 25.528 0.511   4.551   1.00 9.98  ?  37  ASN   A CB   1 
ATOM   885  C  CG   . ASN   A 1 37  ? 25.203 1.708   3.693   1.00 9.93  ?  37  ASN   A CG   1 
ATOM   886  O  OD1  . ASN   A 1 37  ? 24.033 2.047   3.514   1.00 10.75 ?  37  ASN   A OD1  1 
ATOM   887  N  ND2  . ASN   A 1 37  ? 26.237 2.356   3.163   1.00 10.53 ?  37  ASN   A ND2  1 
ATOM   888  H  H    . ASN   A 1 37  ? 25.620 -1.874  5.354   1.00 11.94 ?  37  ASN   A H    1 
ATOM   889  H  HA   . ASN   A 1 37  ? 23.615 -0.174  4.755   1.00 11.51 ?  37  ASN   A HA   1 
ATOM   890  H  HB2  . ASN   A 1 37  ? 25.611 0.820   5.471   1.00 11.98 ?  37  ASN   A HB2  1 
ATOM   891  H  HB3  . ASN   A 1 37  ? 26.378 0.146   4.251   1.00 11.98 ?  37  ASN   A HB3  1 
ATOM   892  H  HD21 . ASN   A 1 37  ? 26.098 3.043   2.664   1.00 12.64 ?  37  ASN   A HD21 1 
ATOM   893  H  HD22 . ASN   A 1 37  ? 27.035 2.091   3.308   1.00 12.64 ?  37  ASN   A HD22 1 
ATOM   894  N  N    A ALA   A 1 38  ? 23.302 -0.502  2.352   0.56 10.16 ?  38  ALA   A N    1 
ATOM   895  N  N    B ALA   A 1 38  ? 23.304 -0.504  2.348   0.44 10.14 ?  38  ALA   A N    1 
ATOM   896  C  CA   A ALA   A 1 38  ? 23.111 -0.675  0.913   0.56 10.32 ?  38  ALA   A CA   1 
ATOM   897  C  CA   B ALA   A 1 38  ? 23.123 -0.698  0.909   0.44 10.34 ?  38  ALA   A CA   1 
ATOM   898  C  C    A ALA   A 1 38  ? 24.004 0.339   0.197   0.56 10.24 ?  38  ALA   A C    1 
ATOM   899  C  C    B ALA   A 1 38  ? 23.999 0.322   0.183   0.44 10.22 ?  38  ALA   A C    1 
ATOM   900  O  O    A ALA   A 1 38  ? 23.580 1.427   -0.203  0.56 10.50 ?  38  ALA   A O    1 
ATOM   901  O  O    B ALA   A 1 38  ? 23.557 1.394   -0.242  0.44 10.45 ?  38  ALA   A O    1 
ATOM   902  C  CB   A ALA   A 1 38  ? 21.641 -0.486  0.558   0.56 11.17 ?  38  ALA   A CB   1 
ATOM   903  C  CB   B ALA   A 1 38  ? 21.652 -0.556  0.537   0.44 11.18 ?  38  ALA   A CB   1 
ATOM   904  H  H    A ALA   A 1 38  ? 22.701 -0.007  2.718   0.56 12.19 ?  38  ALA   A H    1 
ATOM   905  H  H    B ALA   A 1 38  ? 22.700 -0.006  2.707   0.44 12.17 ?  38  ALA   A H    1 
ATOM   906  H  HA   A ALA   A 1 38  ? 23.383 -1.566  0.654   0.56 12.38 ?  38  ALA   A HA   1 
ATOM   907  H  HA   B ALA   A 1 38  ? 23.419 -1.587  0.665   0.44 12.41 ?  38  ALA   A HA   1 
ATOM   908  H  HB1  A ALA   A 1 38  ? 21.529 -0.607  -0.397  0.56 13.41 ?  38  ALA   A HB1  1 
ATOM   909  H  HB1  B ALA   A 1 38  ? 21.553 -0.703  -0.416  0.44 13.42 ?  38  ALA   A HB1  1 
ATOM   910  H  HB2  A ALA   A 1 38  ? 21.112 -1.145  1.039   0.56 13.41 ?  38  ALA   A HB2  1 
ATOM   911  H  HB2  B ALA   A 1 38  ? 21.137 -1.217  1.029   0.44 13.42 ?  38  ALA   A HB2  1 
ATOM   912  H  HB3  A ALA   A 1 38  ? 21.363 0.407   0.814   0.56 13.41 ?  38  ALA   A HB3  1 
ATOM   913  H  HB3  B ALA   A 1 38  ? 21.351 0.336   0.769   0.44 13.42 ?  38  ALA   A HB3  1 
ATOM   914  N  N    . ALA   A 1 39  ? 25.276 -0.025  0.049   1.00 10.24 ?  39  ALA   A N    1 
ATOM   915  C  CA   . ALA   A 1 39  ? 26.303 0.868   -0.457  1.00 10.32 ?  39  ALA   A CA   1 
ATOM   916  C  C    . ALA   A 1 39  ? 26.413 0.810   -1.975  1.00 10.06 ?  39  ALA   A C    1 
ATOM   917  O  O    . ALA   A 1 39  ? 25.929 -0.119  -2.630  1.00 10.85 ?  39  ALA   A O    1 
ATOM   918  C  CB   . ALA   A 1 39  ? 27.650 0.503   0.173   1.00 11.30 ?  39  ALA   A CB   1 
ATOM   919  H  H    A ALA   A 1 39  ? 25.569 -0.807  0.254   0.56 12.29 ?  39  ALA   A H    1 
ATOM   920  H  H    B ALA   A 1 39  ? 25.575 -0.802  0.263   0.44 12.29 ?  39  ALA   A H    1 
ATOM   921  H  HA   . ALA   A 1 39  ? 26.082 1.778   -0.202  1.00 12.38 ?  39  ALA   A HA   1 
ATOM   922  H  HB1  . ALA   A 1 39  ? 28.326 1.107   -0.169  1.00 13.56 ?  39  ALA   A HB1  1 
ATOM   923  H  HB2  . ALA   A 1 39  ? 27.579 0.604   1.140   1.00 13.56 ?  39  ALA   A HB2  1 
ATOM   924  H  HB3  . ALA   A 1 39  ? 27.866 -0.409  -0.050  1.00 13.56 ?  39  ALA   A HB3  1 
ATOM   925  N  N    . ASN   A 1 40  ? 27.095 1.819   -2.529  1.00 10.53 ?  40  ASN   A N    1 
ATOM   926  C  CA   . ASN   A 1 40  ? 27.630 1.770   -3.882  1.00 10.86 ?  40  ASN   A CA   1 
ATOM   927  C  C    . ASN   A 1 40  ? 29.154 1.647   -3.824  1.00 10.32 ?  40  ASN   A C    1 
ATOM   928  O  O    . ASN   A 1 40  ? 29.765 1.745   -2.754  1.00 10.58 ?  40  ASN   A O    1 
ATOM   929  C  CB   . ASN   A 1 40  ? 27.162 2.963   -4.732  1.00 11.39 ?  40  ASN   A CB   1 
ATOM   930  C  CG   . ASN   A 1 40  ? 27.534 4.296   -4.132  1.00 12.22 ?  40  ASN   A CG   1 
ATOM   931  O  OD1  . ASN   A 1 40  ? 28.705 4.556   -3.829  1.00 13.10 ?  40  ASN   A OD1  1 
ATOM   932  N  ND2  . ASN   A 1 40  ? 26.533 5.164   -3.966  1.00 13.19 ?  40  ASN   A ND2  1 
ATOM   933  H  H    . ASN   A 1 40  ? 27.273 2.546   -2.123  1.00 12.63 ?  40  ASN   A H    1 
ATOM   934  H  HA   . ASN   A 1 40  ? 27.296 0.967   -4.318  1.00 13.03 ?  40  ASN   A HA   1 
ATOM   935  H  HB2  . ASN   A 1 40  ? 27.569 2.905   -5.613  1.00 13.67 ?  40  ASN   A HB2  1 
ATOM   936  H  HB3  . ASN   A 1 40  ? 26.194 2.930   -4.817  1.00 13.67 ?  40  ASN   A HB3  1 
ATOM   937  H  HD21 . ASN   A 1 40  ? 26.687 5.945   -3.632  1.00 15.83 ?  40  ASN   A HD21 1 
ATOM   938  H  HD22 . ASN   A 1 40  ? 25.730 4.950   -4.191  1.00 15.83 ?  40  ASN   A HD22 1 
ATOM   939  N  N    . VAL   A 1 41  ? 29.766 1.392   -4.985  1.00 10.95 ?  41  VAL   A N    1 
ATOM   940  C  CA   . VAL   A 1 41  ? 31.196 1.077   -5.014  1.00 11.71 ?  41  VAL   A CA   1 
ATOM   941  C  C    . VAL   A 1 41  ? 32.062 2.229   -4.538  1.00 11.54 ?  41  VAL   A C    1 
ATOM   942  O  O    . VAL   A 1 41  ? 33.207 2.006   -4.128  1.00 12.12 ?  41  VAL   A O    1 
ATOM   943  C  CB   . VAL   A 1 41  ? 31.686 0.589   -6.399  1.00 12.41 ?  41  VAL   A CB   1 
ATOM   944  C  CG1  . VAL   A 1 41  ? 30.994 -0.710  -6.788  1.00 13.12 ?  41  VAL   A CG1  1 
ATOM   945  C  CG2  . VAL   A 1 41  ? 31.517 1.662   -7.467  1.00 13.22 ?  41  VAL   A CG2  1 
ATOM   946  H  H    . VAL   A 1 41  ? 29.380 1.393   -5.754  1.00 13.14 ?  41  VAL   A H    1 
ATOM   947  H  HA   . VAL   A 1 41  ? 31.346 0.344   -4.395  1.00 14.06 ?  41  VAL   A HA   1 
ATOM   948  H  HB   . VAL   A 1 41  ? 32.633 0.391   -6.332  1.00 14.89 ?  41  VAL   A HB   1 
ATOM   949  H  HG11 . VAL   A 1 41  ? 31.334 -1.008  -7.645  1.00 15.75 ?  41  VAL   A HG11 1 
ATOM   950  H  HG12 . VAL   A 1 41  ? 31.173 -1.382  -6.109  1.00 15.75 ?  41  VAL   A HG12 1 
ATOM   951  H  HG13 . VAL   A 1 41  ? 30.037 -0.553  -6.848  1.00 15.75 ?  41  VAL   A HG13 1 
ATOM   952  H  HG21 . VAL   A 1 41  ? 31.745 1.281   -8.332  1.00 15.86 ?  41  VAL   A HG21 1 
ATOM   953  H  HG22 . VAL   A 1 41  ? 30.600 1.965   -7.468  1.00 15.86 ?  41  VAL   A HG22 1 
ATOM   954  H  HG23 . VAL   A 1 41  ? 32.115 2.399   -7.266  1.00 15.86 ?  41  VAL   A HG23 1 
ATOM   955  N  N    A TYR   A 1 42  ? 31.547 3.459   -4.605  0.56 11.37 ?  42  TYR   A N    1 
ATOM   956  N  N    B TYR   A 1 42  ? 31.568 3.466   -4.607  0.44 11.31 ?  42  TYR   A N    1 
ATOM   957  C  CA   A TYR   A 1 42  ? 32.269 4.657   -4.199  0.56 11.47 ?  42  TYR   A CA   1 
ATOM   958  C  CA   B TYR   A 1 42  ? 32.337 4.626   -4.168  0.44 11.37 ?  42  TYR   A CA   1 
ATOM   959  C  C    A TYR   A 1 42  ? 32.032 5.019   -2.741  0.56 11.29 ?  42  TYR   A C    1 
ATOM   960  C  C    B TYR   A 1 42  ? 32.042 5.017   -2.729  0.44 11.15 ?  42  TYR   A C    1 
ATOM   961  O  O    A TYR   A 1 42  ? 32.615 5.999   -2.255  0.56 11.90 ?  42  TYR   A O    1 
ATOM   962  O  O    B TYR   A 1 42  ? 32.595 6.013   -2.244  0.44 11.58 ?  42  TYR   A O    1 
ATOM   963  C  CB   A TYR   A 1 42  ? 31.861 5.835   -5.099  0.56 11.91 ?  42  TYR   A CB   1 
ATOM   964  C  CB   B TYR   A 1 42  ? 32.085 5.820   -5.098  0.44 11.72 ?  42  TYR   A CB   1 
ATOM   965  C  CG   A TYR   A 1 42  ? 32.017 5.543   -6.576  0.56 12.45 ?  42  TYR   A CG   1 
ATOM   966  C  CG   B TYR   A 1 42  ? 32.322 5.484   -6.550  0.44 12.13 ?  42  TYR   A CG   1 
ATOM   967  C  CD1  A TYR   A 1 42  ? 33.270 5.335   -7.132  0.56 12.65 ?  42  TYR   A CD1  1 
ATOM   968  C  CD1  B TYR   A 1 42  ? 33.605 5.292   -7.034  0.44 12.54 ?  42  TYR   A CD1  1 
ATOM   969  C  CD2  A TYR   A 1 42  ? 30.909 5.459   -7.411  0.56 13.68 ?  42  TYR   A CD2  1 
ATOM   970  C  CD2  B TYR   A 1 42  ? 31.260 5.324   -7.428  0.44 12.53 ?  42  TYR   A CD2  1 
ATOM   971  C  CE1  A TYR   A 1 42  ? 33.421 5.052   -8.479  0.56 12.97 ?  42  TYR   A CE1  1 
ATOM   972  C  CE1  B TYR   A 1 42  ? 33.828 4.961   -8.360  0.44 12.46 ?  42  TYR   A CE1  1 
ATOM   973  C  CE2  A TYR   A 1 42  ? 31.049 5.185   -8.761  0.56 14.02 ?  42  TYR   A CE2  1 
ATOM   974  C  CE2  B TYR   A 1 42  ? 31.471 4.997   -8.755  0.44 12.74 ?  42  TYR   A CE2  1 
ATOM   975  C  CZ   A TYR   A 1 42  ? 32.306 4.980   -9.288  0.56 13.86 ?  42  TYR   A CZ   1 
ATOM   976  C  CZ   B TYR   A 1 42  ? 32.757 4.815   -9.216  0.44 12.49 ?  42  TYR   A CZ   1 
ATOM   977  O  OH   A TYR   A 1 42  ? 32.457 4.706   -10.628 0.56 15.22 ?  42  TYR   A OH   1 
ATOM   978  O  OH   B TYR   A 1 42  ? 32.974 4.484   -10.533 0.44 13.46 ?  42  TYR   A OH   1 
ATOM   979  H  H    A TYR   A 1 42  ? 30.756 3.624   -4.899  0.56 13.65 ?  42  TYR   A H    1 
ATOM   980  H  H    B TYR   A 1 42  ? 30.787 3.659   -4.913  0.44 13.57 ?  42  TYR   A H    1 
ATOM   981  H  HA   A TYR   A 1 42  ? 33.217 4.511   -4.324  0.56 13.77 ?  42  TYR   A HA   1 
ATOM   982  H  HA   B TYR   A 1 42  ? 33.281 4.411   -4.226  0.44 13.64 ?  42  TYR   A HA   1 
ATOM   983  H  HB2  A TYR   A 1 42  ? 30.926 6.050   -4.937  0.56 14.30 ?  42  TYR   A HB2  1 
ATOM   984  H  HB2  B TYR   A 1 42  ? 31.162 6.103   -5.003  0.44 14.07 ?  42  TYR   A HB2  1 
ATOM   985  H  HB3  A TYR   A 1 42  ? 32.414 6.602   -4.889  0.56 14.30 ?  42  TYR   A HB3  1 
ATOM   986  H  HB3  B TYR   A 1 42  ? 32.683 6.544   -4.853  0.44 14.07 ?  42  TYR   A HB3  1 
ATOM   987  H  HD1  A TYR   A 1 42  ? 34.023 5.380   -6.589  0.56 15.18 ?  42  TYR   A HD1  1 
ATOM   988  H  HD1  B TYR   A 1 42  ? 34.332 5.389   -6.456  0.44 15.05 ?  42  TYR   A HD1  1 
ATOM   989  H  HD2  A TYR   A 1 42  ? 30.058 5.596   -7.061  0.56 16.42 ?  42  TYR   A HD2  1 
ATOM   990  H  HD2  B TYR   A 1 42  ? 30.391 5.446   -7.117  0.44 15.04 ?  42  TYR   A HD2  1 
ATOM   991  H  HE1  A TYR   A 1 42  ? 34.268 4.914   -8.837  0.56 15.57 ?  42  TYR   A HE1  1 
ATOM   992  H  HE1  B TYR   A 1 42  ? 34.698 4.843   -8.670  0.44 14.95 ?  42  TYR   A HE1  1 
ATOM   993  H  HE2  A TYR   A 1 42  ? 30.299 5.130   -9.311  0.56 16.82 ?  42  TYR   A HE2  1 
ATOM   994  H  HE2  B TYR   A 1 42  ? 30.748 4.900   -9.332  0.44 15.29 ?  42  TYR   A HE2  1 
ATOM   995  H  HH   A TYR   A 1 42  ? 31.712 4.684   -11.009 0.56 18.27 ?  42  TYR   A HH   1 
ATOM   996  H  HH   B TYR   A 1 42  ? 33.785 4.309   -10.652 0.44 16.15 ?  42  TYR   A HH   1 
ATOM   997  N  N    . LEU   A 1 43  ? 31.178 4.265   -2.047  1.00 10.87 ?  43  LEU   A N    1 
ATOM   998  C  CA   . LEU   A 1 43  ? 30.747 4.604   -0.695  1.00 10.47 ?  43  LEU   A CA   1 
ATOM   999  C  C    . LEU   A 1 43  ? 30.267 6.052   -0.606  1.00 10.73 ?  43  LEU   A C    1 
ATOM   1000 O  O    . LEU   A 1 43  ? 30.533 6.756   0.370   1.00 11.65 ?  43  LEU   A O    1 
ATOM   1001 C  CB   . LEU   A 1 43  ? 31.801 4.294   0.365   1.00 10.80 ?  43  LEU   A CB   1 
ATOM   1002 C  CG   . LEU   A 1 43  ? 32.292 2.844   0.459   1.00 11.24 ?  43  LEU   A CG   1 
ATOM   1003 C  CD1  . LEU   A 1 43  ? 33.336 2.728   1.564   1.00 12.12 ?  43  LEU   A CD1  1 
ATOM   1004 C  CD2  . LEU   A 1 43  ? 31.146 1.870   0.697   1.00 12.04 ?  43  LEU   A CD2  1 
ATOM   1005 H  H    A LEU   A 1 43  ? 30.829 3.532   -2.343  0.56 13.04 ?  43  LEU   A H    1 
ATOM   1006 H  H    B LEU   A 1 43  ? 30.823 3.538   -2.350  0.44 13.04 ?  43  LEU   A H    1 
ATOM   1007 H  HA   . LEU   A 1 43  ? 29.978 4.048   -0.488  1.00 12.56 ?  43  LEU   A HA   1 
ATOM   1008 H  HB2  . LEU   A 1 43  ? 32.576 4.851   0.198   1.00 12.96 ?  43  LEU   A HB2  1 
ATOM   1009 H  HB3  . LEU   A 1 43  ? 31.427 4.522   1.235   1.00 12.96 ?  43  LEU   A HB3  1 
ATOM   1010 H  HG   . LEU   A 1 43  ? 32.721 2.603   -0.375  1.00 13.49 ?  43  LEU   A HG   1 
ATOM   1011 H  HD11 . LEU   A 1 43  ? 33.643 1.809   1.618   1.00 14.55 ?  43  LEU   A HD11 1 
ATOM   1012 H  HD12 . LEU   A 1 43  ? 34.082 3.314   1.360   1.00 14.55 ?  43  LEU   A HD12 1 
ATOM   1013 H  HD13 . LEU   A 1 43  ? 32.934 2.990   2.410   1.00 14.55 ?  43  LEU   A HD13 1 
ATOM   1014 H  HD21 . LEU   A 1 43  ? 31.514 0.983   0.844   1.00 14.45 ?  43  LEU   A HD21 1 
ATOM   1015 H  HD22 . LEU   A 1 43  ? 30.648 2.156   1.477   1.00 14.45 ?  43  LEU   A HD22 1 
ATOM   1016 H  HD23 . LEU   A 1 43  ? 30.573 1.865   -0.083  1.00 14.45 ?  43  LEU   A HD23 1 
ATOM   1017 N  N    A LYS   A 1 44  ? 29.534 6.494   -1.625  0.56 10.74 ?  44  LYS   A N    1 
ATOM   1018 N  N    B LYS   A 1 44  ? 29.549 6.491   -1.643  0.44 11.23 ?  44  LYS   A N    1 
ATOM   1019 C  CA   A LYS   A 1 44  ? 28.903 7.811   -1.615  0.56 10.77 ?  44  LYS   A CA   1 
ATOM   1020 C  CA   B LYS   A 1 44  ? 28.879 7.788   -1.655  0.44 11.82 ?  44  LYS   A CA   1 
ATOM   1021 C  C    A LYS   A 1 44  ? 27.471 7.635   -1.129  0.56 10.25 ?  44  LYS   A C    1 
ATOM   1022 C  C    B LYS   A 1 44  ? 27.474 7.571   -1.109  0.44 10.82 ?  44  LYS   A C    1 
ATOM   1023 O  O    A LYS   A 1 44  ? 26.600 7.166   -1.866  0.56 11.37 ?  44  LYS   A O    1 
ATOM   1024 O  O    B LYS   A 1 44  ? 26.620 6.991   -1.787  0.44 11.18 ?  44  LYS   A O    1 
ATOM   1025 C  CB   A LYS   A 1 44  ? 28.975 8.463   -2.990  0.56 11.94 ?  44  LYS   A CB   1 
ATOM   1026 C  CB   B LYS   A 1 44  ? 28.818 8.351   -3.072  0.44 14.16 ?  44  LYS   A CB   1 
ATOM   1027 C  CG   A LYS   A 1 44  ? 30.364 8.947   -3.371  0.56 14.23 ?  44  LYS   A CG   1 
ATOM   1028 C  CG   B LYS   A 1 44  ? 30.157 8.726   -3.682  0.44 17.29 ?  44  LYS   A CG   1 
ATOM   1029 C  CD   A LYS   A 1 44  ? 30.999 9.829   -2.297  0.56 18.76 ?  44  LYS   A CD   1 
ATOM   1030 C  CD   B LYS   A 1 44  ? 30.932 9.714   -2.827  0.44 20.85 ?  44  LYS   A CD   1 
ATOM   1031 C  CE   A LYS   A 1 44  ? 32.365 10.322  -2.733  0.56 21.24 ?  44  LYS   A CE   1 
ATOM   1032 C  CE   B LYS   A 1 44  ? 32.042 10.369  -3.635  0.44 22.84 ?  44  LYS   A CE   1 
ATOM   1033 N  NZ   A LYS   A 1 44  ? 33.151 10.887  -1.604  0.56 22.29 ?  44  LYS   A NZ   1 
ATOM   1034 N  NZ   B LYS   A 1 44  ? 33.193 10.794  -2.793  0.44 24.01 ?  44  LYS   A NZ   1 
ATOM   1035 H  H    A LYS   A 1 44  ? 29.396 6.048   -2.351  0.56 12.88 ?  44  LYS   A H    1 
ATOM   1036 H  H    B LYS   A 1 44  ? 29.429 6.040   -2.366  0.44 13.47 ?  44  LYS   A H    1 
ATOM   1037 H  HA   A LYS   A 1 44  ? 29.351 8.376   -0.967  0.56 12.92 ?  44  LYS   A HA   1 
ATOM   1038 H  HA   B LYS   A 1 44  ? 29.348 8.414   -1.082  0.44 14.19 ?  44  LYS   A HA   1 
ATOM   1039 H  HB2  A LYS   A 1 44  ? 28.694 7.819   -3.657  0.56 14.33 ?  44  LYS   A HB2  1 
ATOM   1040 H  HB2  B LYS   A 1 44  ? 28.413 7.688   -3.652  0.44 16.99 ?  44  LYS   A HB2  1 
ATOM   1041 H  HB3  A LYS   A 1 44  ? 28.383 9.232   -3.004  0.56 14.33 ?  44  LYS   A HB3  1 
ATOM   1042 H  HB3  B LYS   A 1 44  ? 28.271 9.153   -3.064  0.44 16.99 ?  44  LYS   A HB3  1 
ATOM   1043 H  HG2  A LYS   A 1 44  ? 30.939 8.179   -3.511  0.56 17.08 ?  44  LYS   A HG2  1 
ATOM   1044 H  HG2  B LYS   A 1 44  ? 30.697 7.927   -3.780  0.44 20.75 ?  44  LYS   A HG2  1 
ATOM   1045 H  HG3  A LYS   A 1 44  ? 30.303 9.469   -4.189  0.56 17.08 ?  44  LYS   A HG3  1 
ATOM   1046 H  HG3  B LYS   A 1 44  ? 30.009 9.135   -4.551  0.44 20.75 ?  44  LYS   A HG3  1 
ATOM   1047 H  HD2  A LYS   A 1 44  ? 30.420 10.590  -2.129  0.56 22.51 ?  44  LYS   A HD2  1 
ATOM   1048 H  HD2  B LYS   A 1 44  ? 30.332 10.406  -2.508  0.44 25.01 ?  44  LYS   A HD2  1 
ATOM   1049 H  HD3  A LYS   A 1 44  ? 31.119 9.309   -1.486  0.56 22.51 ?  44  LYS   A HD3  1 
ATOM   1050 H  HD3  B LYS   A 1 44  ? 31.334 9.244   -2.077  0.44 25.01 ?  44  LYS   A HD3  1 
ATOM   1051 H  HE2  A LYS   A 1 44  ? 32.864 9.577   -3.104  0.56 25.48 ?  44  LYS   A HE2  1 
ATOM   1052 H  HE2  B LYS   A 1 44  ? 32.368 9.736   -4.293  0.44 27.41 ?  44  LYS   A HE2  1 
ATOM   1053 H  HE3  A LYS   A 1 44  ? 32.250 11.013  -3.400  0.56 25.48 ?  44  LYS   A HE3  1 
ATOM   1054 H  HE3  B LYS   A 1 44  ? 31.686 11.156  -4.077  0.44 27.41 ?  44  LYS   A HE3  1 
ATOM   1055 H  HZ1  A LYS   A 1 44  ? 33.943 11.166  -1.898  0.56 26.75 ?  44  LYS   A HZ1  1 
ATOM   1056 H  HZ1  B LYS   A 1 44  ? 33.817 11.173  -3.303  0.44 28.81 ?  44  LYS   A HZ1  1 
ATOM   1057 H  HZ2  A LYS   A 1 44  ? 32.715 11.578  -1.248  0.56 26.75 ?  44  LYS   A HZ2  1 
ATOM   1058 H  HZ2  B LYS   A 1 44  ? 32.923 11.384  -2.184  0.44 28.81 ?  44  LYS   A HZ2  1 
ATOM   1059 H  HZ3  A LYS   A 1 44  ? 33.275 10.269  -0.978  0.56 26.75 ?  44  LYS   A HZ3  1 
ATOM   1060 H  HZ3  B LYS   A 1 44  ? 33.545 10.090  -2.380  0.44 28.81 ?  44  LYS   A HZ3  1 
ATOM   1061 N  N    . HIS   A 1 45  ? 27.237 8.004   0.127   1.00 10.37 ?  45  HIS   A N    1 
ATOM   1062 C  CA   . HIS   A 1 45  ? 26.001 7.661   0.825   1.00 10.78 ?  45  HIS   A CA   1 
ATOM   1063 C  C    . HIS   A 1 45  ? 24.968 8.773   0.650   1.00 11.51 ?  45  HIS   A C    1 
ATOM   1064 O  O    . HIS   A 1 45  ? 24.689 9.554   1.558   1.00 13.43 ?  45  HIS   A O    1 
ATOM   1065 C  CB   . HIS   A 1 45  ? 26.306 7.421   2.292   1.00 10.53 ?  45  HIS   A CB   1 
ATOM   1066 C  CG   . HIS   A 1 45  ? 27.414 6.449   2.523   1.00 10.10 ?  45  HIS   A CG   1 
ATOM   1067 N  ND1  . HIS   A 1 45  ? 27.410 5.166   2.014   1.00 10.57 ?  45  HIS   A ND1  1 
ATOM   1068 C  CD2  . HIS   A 1 45  ? 28.575 6.593   3.205   1.00 10.69 ?  45  HIS   A CD2  1 
ATOM   1069 C  CE1  . HIS   A 1 45  ? 28.529 4.566   2.381   1.00 10.49 ?  45  HIS   A CE1  1 
ATOM   1070 N  NE2  . HIS   A 1 45  ? 29.253 5.407   3.104   1.00 10.69 ?  45  HIS   A NE2  1 
ATOM   1071 H  H    A HIS   A 1 45  ? 27.781 8.473   0.601   0.56 12.44 ?  45  HIS   A H    1 
ATOM   1072 H  H    B HIS   A 1 45  ? 27.777 8.492   0.586   0.44 12.44 ?  45  HIS   A H    1 
ATOM   1073 H  HA   . HIS   A 1 45  ? 25.635 6.843   0.450   1.00 12.94 ?  45  HIS   A HA   1 
ATOM   1074 H  HB2  . HIS   A 1 45  ? 26.553 8.265   2.700   1.00 12.63 ?  45  HIS   A HB2  1 
ATOM   1075 H  HB3  . HIS   A 1 45  ? 25.506 7.072   2.722   1.00 12.63 ?  45  HIS   A HB3  1 
ATOM   1076 H  HD2  . HIS   A 1 45  ? 28.864 7.360   3.653   1.00 12.83 ?  45  HIS   A HD2  1 
ATOM   1077 H  HE1  . HIS   A 1 45  ? 28.759 3.688   2.184   1.00 12.59 ?  45  HIS   A HE1  1 
ATOM   1078 H  HE2  . HIS   A 1 45  ? 30.018 5.234   3.458   1.00 12.82 ?  45  HIS   A HE2  1 
ATOM   1079 N  N    A GLY   A 1 46  ? 24.415 8.854   -0.556  0.56 12.09 ?  46  GLY   A N    1 
ATOM   1080 N  N    B GLY   A 1 46  ? 24.330 8.772   -0.518  0.44 11.75 ?  46  GLY   A N    1 
ATOM   1081 C  CA   A GLY   A 1 46  ? 23.621 10.015  -0.916  0.56 12.75 ?  46  GLY   A CA   1 
ATOM   1082 C  CA   B GLY   A 1 46  ? 23.453 9.859   -0.907  0.44 12.08 ?  46  GLY   A CA   1 
ATOM   1083 C  C    A GLY   A 1 46  ? 22.132 9.901   -0.654  0.56 12.98 ?  46  GLY   A C    1 
ATOM   1084 C  C    B GLY   A 1 46  ? 21.992 9.710   -0.523  0.44 12.01 ?  46  GLY   A C    1 
ATOM   1085 O  O    A GLY   A 1 46  ? 21.473 10.904  -0.360  0.56 13.96 ?  46  GLY   A O    1 
ATOM   1086 O  O    B GLY   A 1 46  ? 21.366 10.685  -0.091  0.44 13.05 ?  46  GLY   A O    1 
ATOM   1087 H  H    A GLY   A 1 46  ? 24.480 8.258   -1.174  0.56 14.51 ?  46  GLY   A H    1 
ATOM   1088 H  H    B GLY   A 1 46  ? 24.381 8.140   -1.102  0.44 14.10 ?  46  GLY   A H    1 
ATOM   1089 H  HA2  A GLY   A 1 46  ? 23.961 10.790  -0.433  0.56 15.30 ?  46  GLY   A HA2  1 
ATOM   1090 H  HA2  B GLY   A 1 46  ? 23.767 10.675  -0.495  0.44 14.49 ?  46  GLY   A HA2  1 
ATOM   1091 H  HA3  A GLY   A 1 46  ? 23.727 10.189  -1.863  0.56 15.30 ?  46  GLY   A HA3  1 
ATOM   1092 H  HA3  B GLY   A 1 46  ? 23.513 9.974   -1.872  0.44 14.49 ?  46  GLY   A HA3  1 
ATOM   1093 N  N    A GLY   A 1 47  ? 21.586 8.701   -0.791  0.56 12.32 ?  47  GLY   A N    1 
ATOM   1094 N  N    B GLY   A 1 47  ? 21.429 8.513   -0.671  0.44 11.78 ?  47  GLY   A N    1 
ATOM   1095 C  CA   A GLY   A 1 47  ? 20.157 8.499   -0.693  0.56 12.38 ?  47  GLY   A CA   1 
ATOM   1096 C  CA   B GLY   A 1 47  ? 19.999 8.343   -0.520  0.44 11.94 ?  47  GLY   A CA   1 
ATOM   1097 C  C    A GLY   A 1 47  ? 19.848 7.066   -0.312  0.56 11.85 ?  47  GLY   A C    1 
ATOM   1098 C  C    B GLY   A 1 47  ? 19.648 6.939   -0.083  0.44 11.05 ?  47  GLY   A C    1 
ATOM   1099 O  O    A GLY   A 1 47  ? 20.747 6.266   -0.050  0.56 12.13 ?  47  GLY   A O    1 
ATOM   1100 O  O    B GLY   A 1 47  ? 20.521 6.085   0.088   0.44 10.76 ?  47  GLY   A O    1 
ATOM   1101 H  H    A GLY   A 1 47  ? 22.030 7.990   -0.937  0.56 14.78 ?  47  GLY   A H    1 
ATOM   1102 H  H    B GLY   A 1 47  ? 21.859 7.784   -0.844  0.44 14.13 ?  47  GLY   A H    1 
ATOM   1103 H  HA2  A GLY   A 1 47  ? 19.776 9.101   -0.029  0.56 14.85 ?  47  GLY   A HA2  1 
ATOM   1104 H  HA2  B GLY   A 1 47  ? 19.663 8.957   0.149   0.44 14.33 ?  47  GLY   A HA2  1 
ATOM   1105 H  HA3  A GLY   A 1 47  ? 19.743 8.689   -1.553  0.56 14.85 ?  47  GLY   A HA3  1 
ATOM   1106 H  HA3  B GLY   A 1 47  ? 19.550 8.526   -1.362  0.44 14.33 ?  47  GLY   A HA3  1 
ATOM   1107 N  N    A GLY   A 1 48  ? 18.560 6.740   -0.295  0.56 11.83 ?  48  GLY   A N    1 
ATOM   1108 N  N    B GLY   A 1 48  ? 18.349 6.703   0.092   0.44 11.05 ?  48  GLY   A N    1 
ATOM   1109 C  CA   A GLY   A 1 48  ? 18.164 5.403   0.102   0.56 11.43 ?  48  GLY   A CA   1 
ATOM   1110 C  CA   B GLY   A 1 48  ? 17.902 5.400   0.548   0.44 10.36 ?  48  GLY   A CA   1 
ATOM   1111 C  C    A GLY   A 1 48  ? 18.604 5.093   1.519   0.56 10.85 ?  48  GLY   A C    1 
ATOM   1112 C  C    B GLY   A 1 48  ? 18.524 5.041   1.882   0.44 10.62 ?  48  GLY   A C    1 
ATOM   1113 O  O    A GLY   A 1 48  ? 18.749 5.982   2.367   0.56 11.31 ?  48  GLY   A O    1 
ATOM   1114 O  O    B GLY   A 1 48  ? 18.686 5.884   2.774   0.44 10.91 ?  48  GLY   A O    1 
ATOM   1115 H  H    A GLY   A 1 48  ? 17.920 7.263   -0.493  0.56 14.20 ?  48  GLY   A H    1 
ATOM   1116 H  H    B GLY   A 1 48  ? 17.713 7.272   -0.047  0.44 13.26 ?  48  GLY   A H    1 
ATOM   1117 H  HA2  A GLY   A 1 48  ? 17.204 5.314   0.051   0.56 13.72 ?  48  GLY   A HA2  1 
ATOM   1118 H  HA2  B GLY   A 1 48  ? 16.931 5.393   0.633   0.44 12.43 ?  48  GLY   A HA2  1 
ATOM   1119 H  HA3  A GLY   A 1 48  ? 18.574 4.747   -0.485  0.56 13.72 ?  48  GLY   A HA3  1 
ATOM   1120 H  HA3  B GLY   A 1 48  ? 18.152 4.721   -0.102  0.44 12.43 ?  48  GLY   A HA3  1 
ATOM   1121 N  N    A VAL   A 1 49  ? 18.820 3.801   1.782   0.56 10.93 ?  49  VAL   A N    1 
ATOM   1122 N  N    B VAL   A 1 49  ? 18.874 3.763   2.023   0.44 10.34 ?  49  VAL   A N    1 
ATOM   1123 C  CA   A VAL   A 1 49  ? 19.314 3.375   3.090   0.56 11.23 ?  49  VAL   A CA   1 
ATOM   1124 C  CA   B VAL   A 1 49  ? 19.483 3.272   3.256   0.44 10.35 ?  49  VAL   A CA   1 
ATOM   1125 C  C    A VAL   A 1 49  ? 20.628 4.070   3.423   0.56 10.36 ?  49  VAL   A C    1 
ATOM   1126 C  C    B VAL   A 1 49  ? 20.750 4.055   3.582   0.44 10.05 ?  49  VAL   A C    1 
ATOM   1127 O  O    A VAL   A 1 49  ? 20.856 4.472   4.566   0.56 10.75 ?  49  VAL   A O    1 
ATOM   1128 O  O    B VAL   A 1 49  ? 20.951 4.494   4.720   0.44 10.46 ?  49  VAL   A O    1 
ATOM   1129 C  CB   A VAL   A 1 49  ? 19.473 1.842   3.130   0.56 12.30 ?  49  VAL   A CB   1 
ATOM   1130 C  CB   B VAL   A 1 49  ? 19.780 1.767   3.132   0.44 10.51 ?  49  VAL   A CB   1 
ATOM   1131 C  CG1  A VAL   A 1 49  ? 20.225 1.414   4.392   0.56 12.64 ?  49  VAL   A CG1  1 
ATOM   1132 C  CG1  B VAL   A 1 49  ? 20.626 1.296   4.309   0.44 9.81  ?  49  VAL   A CG1  1 
ATOM   1133 C  CG2  A VAL   A 1 49  ? 18.115 1.161   3.053   0.56 13.54 ?  49  VAL   A CG2  1 
ATOM   1134 C  CG2  B VAL   A 1 49  ? 18.494 0.962   3.019   0.44 11.38 ?  49  VAL   A CG2  1 
ATOM   1135 H  H    A VAL   A 1 49  ? 18.690 3.154   1.230   0.56 13.11 ?  49  VAL   A H    1 
ATOM   1136 H  H    B VAL   A 1 49  ? 18.774 3.164   1.418   0.44 12.40 ?  49  VAL   A H    1 
ATOM   1137 H  HA   A VAL   A 1 49  ? 18.667 3.615   3.771   0.56 13.47 ?  49  VAL   A HA   1 
ATOM   1138 H  HA   B VAL   A 1 49  ? 18.864 3.394   3.990   0.44 12.42 ?  49  VAL   A HA   1 
ATOM   1139 H  HB   A VAL   A 1 49  ? 19.999 1.556   2.366   0.56 14.76 ?  49  VAL   A HB   1 
ATOM   1140 H  HB   B VAL   A 1 49  ? 20.292 1.616   2.321   0.44 12.61 ?  49  VAL   A HB   1 
ATOM   1141 H  HG11 A VAL   A 1 49  ? 20.066 0.469   4.547   0.56 15.17 ?  49  VAL   A HG11 1 
ATOM   1142 H  HG11 B VAL   A 1 49  ? 20.554 0.331   4.385   0.44 11.77 ?  49  VAL   A HG11 1 
ATOM   1143 H  HG12 A VAL   A 1 49  ? 21.172 1.575   4.273   0.56 15.17 ?  49  VAL   A HG12 1 
ATOM   1144 H  HG12 B VAL   A 1 49  ? 21.553 1.543   4.158   0.44 11.77 ?  49  VAL   A HG12 1 
ATOM   1145 H  HG13 A VAL   A 1 49  ? 19.891 1.929   5.146   0.56 15.17 ?  49  VAL   A HG13 1 
ATOM   1146 H  HG13 B VAL   A 1 49  ? 20.300 1.713   5.122   0.44 11.77 ?  49  VAL   A HG13 1 
ATOM   1147 H  HG21 A VAL   A 1 49  ? 18.242 0.199   3.082   0.56 16.24 ?  49  VAL   A HG21 1 
ATOM   1148 H  HG21 B VAL   A 1 49  ? 18.714 0.023   2.924   0.44 13.66 ?  49  VAL   A HG21 1 
ATOM   1149 H  HG22 A VAL   A 1 49  ? 17.577 1.448   3.806   0.56 16.24 ?  49  VAL   A HG22 1 
ATOM   1150 H  HG22 B VAL   A 1 49  ? 17.965 1.098   3.822   0.44 13.66 ?  49  VAL   A HG22 1 
ATOM   1151 H  HG23 A VAL   A 1 49  ? 17.687 1.414   2.221   0.56 16.24 ?  49  VAL   A HG23 1 
ATOM   1152 H  HG23 B VAL   A 1 49  ? 17.997 1.265   2.242   0.44 13.66 ?  49  VAL   A HG23 1 
ATOM   1153 N  N    A ALA   A 1 50  ? 21.534 4.160   2.449   0.56 10.15 ?  50  ALA   A N    1 
ATOM   1154 N  N    B ALA   A 1 50  ? 21.646 4.194   2.602   0.44 9.92  ?  50  ALA   A N    1 
ATOM   1155 C  CA   A ALA   A 1 50  ? 22.855 4.723   2.709   0.56 10.06 ?  50  ALA   A CA   1 
ATOM   1156 C  CA   B ALA   A 1 50  ? 22.951 4.785   2.880   0.44 9.95  ?  50  ALA   A CA   1 
ATOM   1157 C  C    A ALA   A 1 50  ? 22.761 6.171   3.160   0.56 9.81  ?  50  ALA   A C    1 
ATOM   1158 C  C    B ALA   A 1 50  ? 22.818 6.248   3.270   0.44 9.80  ?  50  ALA   A C    1 
ATOM   1159 O  O    A ALA   A 1 50  ? 23.419 6.576   4.124   0.56 10.48 ?  50  ALA   A O    1 
ATOM   1160 O  O    B ALA   A 1 50  ? 23.427 6.697   4.248   0.44 10.06 ?  50  ALA   A O    1 
ATOM   1161 C  CB   A ALA   A 1 50  ? 23.712 4.613   1.453   0.56 9.87  ?  50  ALA   A CB   1 
ATOM   1162 C  CB   B ALA   A 1 50  ? 23.867 4.631   1.667   0.44 9.90  ?  50  ALA   A CB   1 
ATOM   1163 H  H    A ALA   A 1 50  ? 21.412 3.889   1.648   0.56 12.18 ?  50  ALA   A H    1 
ATOM   1164 H  H    B ALA   A 1 50  ? 21.524 3.962   1.781   0.44 11.90 ?  50  ALA   A H    1 
ATOM   1165 H  HA   A ALA   A 1 50  ? 23.286 4.220   3.421   0.56 12.08 ?  50  ALA   A HA   1 
ATOM   1166 H  HA   B ALA   A 1 50  ? 23.359 4.321   3.624   0.44 11.93 ?  50  ALA   A HA   1 
ATOM   1167 H  HB1  A ALA   A 1 50  ? 24.584 4.996   1.636   0.56 11.85 ?  50  ALA   A HB1  1 
ATOM   1168 H  HB1  B ALA   A 1 50  ? 24.729 5.030   1.868   0.44 11.88 ?  50  ALA   A HB1  1 
ATOM   1169 H  HB2  A ALA   A 1 50  ? 23.799 3.681   1.211   0.56 11.85 ?  50  ALA   A HB2  1 
ATOM   1170 H  HB2  B ALA   A 1 50  ? 23.977 3.688   1.472   0.44 11.88 ?  50  ALA   A HB2  1 
ATOM   1171 H  HB3  A ALA   A 1 50  ? 23.278 5.106   0.738   0.56 11.85 ?  50  ALA   A HB3  1 
ATOM   1172 H  HB3  B ALA   A 1 50  ? 23.465 5.082   0.907   0.44 11.88 ?  50  ALA   A HB3  1 
ATOM   1173 N  N    A GLY   A 1 51  ? 21.963 6.976   2.461   0.56 10.32 ?  51  GLY   A N    1 
ATOM   1174 N  N    B GLY   A 1 51  ? 22.034 7.010   2.508   0.44 10.50 ?  51  GLY   A N    1 
ATOM   1175 C  CA   A GLY   A 1 51  ? 21.816 8.363   2.862   0.56 10.65 ?  51  GLY   A CA   1 
ATOM   1176 C  CA   B GLY   A 1 51  ? 21.808 8.397   2.870   0.44 10.80 ?  51  GLY   A CA   1 
ATOM   1177 C  C    A GLY   A 1 51  ? 21.232 8.498   4.254   0.56 10.63 ?  51  GLY   A C    1 
ATOM   1178 C  C    B GLY   A 1 51  ? 21.200 8.531   4.250   0.44 10.86 ?  51  GLY   A C    1 
ATOM   1179 O  O    A GLY   A 1 51  ? 21.634 9.376   5.023   0.56 11.46 ?  51  GLY   A O    1 
ATOM   1180 O  O    B GLY   A 1 51  ? 21.559 9.434   5.010   0.44 11.37 ?  51  GLY   A O    1 
ATOM   1181 H  H    A GLY   A 1 51  ? 21.520 6.746   1.761   0.56 12.38 ?  51  GLY   A H    1 
ATOM   1182 H  H    B GLY   A 1 51  ? 21.638 6.752   1.788   0.44 12.60 ?  51  GLY   A H    1 
ATOM   1183 H  HA2  A GLY   A 1 51  ? 22.685 8.796   2.848   0.56 12.79 ?  51  GLY   A HA2  1 
ATOM   1184 H  HA2  B GLY   A 1 51  ? 22.652 8.877   2.855   0.44 12.97 ?  51  GLY   A HA2  1 
ATOM   1185 H  HA3  A GLY   A 1 51  ? 21.235 8.818   2.234   0.56 12.79 ?  51  GLY   A HA3  1 
ATOM   1186 H  HA3  B GLY   A 1 51  ? 21.210 8.806   2.225   0.44 12.97 ?  51  GLY   A HA3  1 
ATOM   1187 N  N    . ALA   A 1 52  ? 20.265 7.638   4.590   1.00 10.83 ?  52  ALA   A N    1 
ATOM   1188 C  CA   . ALA   A 1 52  ? 19.628 7.694   5.901   1.00 11.46 ?  52  ALA   A CA   1 
ATOM   1189 C  C    . ALA   A 1 52  ? 20.588 7.286   7.018   1.00 10.86 ?  52  ALA   A C    1 
ATOM   1190 O  O    . ALA   A 1 52  ? 20.664 7.956   8.055   1.00 12.00 ?  52  ALA   A O    1 
ATOM   1191 C  CB   . ALA   A 1 52  ? 18.366 6.826   5.900   1.00 12.89 ?  52  ALA   A CB   1 
ATOM   1192 H  H    A ALA   A 1 52  ? 19.972 7.009   4.075   0.56 12.99 ?  52  ALA   A H    1 
ATOM   1193 H  H    B ALA   A 1 52  ? 19.995 6.993   4.082   0.44 12.99 ?  52  ALA   A H    1 
ATOM   1194 H  HA   . ALA   A 1 52  ? 19.350 8.601   6.069   1.00 13.75 ?  52  ALA   A HA   1 
ATOM   1195 H  HB1  . ALA   A 1 52  ? 17.935 6.892   6.769   1.00 15.47 ?  52  ALA   A HB1  1 
ATOM   1196 H  HB2  . ALA   A 1 52  ? 17.760 7.147   5.211   1.00 15.47 ?  52  ALA   A HB2  1 
ATOM   1197 H  HB3  . ALA   A 1 52  ? 18.608 5.904   5.722   1.00 15.47 ?  52  ALA   A HB3  1 
ATOM   1198 N  N    A LEU   A 1 53  ? 21.320 6.183   6.834   0.56 11.00 ?  53  LEU   A N    1 
ATOM   1199 N  N    B LEU   A 1 53  ? 21.322 6.181   6.838   0.44 10.80 ?  53  LEU   A N    1 
ATOM   1200 C  CA   A LEU   A 1 53  ? 22.286 5.772   7.850   0.56 11.07 ?  53  LEU   A CA   1 
ATOM   1201 C  CA   B LEU   A 1 53  ? 22.313 5.797   7.843   0.44 10.67 ?  53  LEU   A CA   1 
ATOM   1202 C  C    A LEU   A 1 53  ? 23.358 6.832   8.035   0.56 11.03 ?  53  LEU   A C    1 
ATOM   1203 C  C    B LEU   A 1 53  ? 23.327 6.916   8.039   0.44 10.47 ?  53  LEU   A C    1 
ATOM   1204 O  O    A LEU   A 1 53  ? 23.760 7.137   9.163   0.56 11.88 ?  53  LEU   A O    1 
ATOM   1205 O  O    B LEU   A 1 53  ? 23.591 7.346   9.168   0.44 10.74 ?  53  LEU   A O    1 
ATOM   1206 C  CB   A LEU   A 1 53  ? 22.930 4.437   7.466   0.56 11.13 ?  53  LEU   A CB   1 
ATOM   1207 C  CB   B LEU   A 1 53  ? 23.026 4.494   7.447   0.44 10.61 ?  53  LEU   A CB   1 
ATOM   1208 C  CG   A LEU   A 1 53  ? 21.999 3.224   7.497   0.56 11.33 ?  53  LEU   A CG   1 
ATOM   1209 C  CG   B LEU   A 1 53  ? 22.318 3.136   7.584   0.44 10.70 ?  53  LEU   A CG   1 
ATOM   1210 C  CD1  A LEU   A 1 53  ? 22.709 2.012   6.919   0.56 11.31 ?  53  LEU   A CD1  1 
ATOM   1211 C  CD1  B LEU   A 1 53  ? 23.173 2.046   6.943   0.44 10.75 ?  53  LEU   A CD1  1 
ATOM   1212 C  CD2  A LEU   A 1 53  ? 21.535 2.944   8.913   0.56 12.30 ?  53  LEU   A CD2  1 
ATOM   1213 C  CD2  B LEU   A 1 53  ? 22.008 2.767   9.031   0.44 10.81 ?  53  LEU   A CD2  1 
ATOM   1214 H  H    A LEU   A 1 53  ? 21.275 5.666   6.145   0.56 13.20 ?  53  LEU   A H    1 
ATOM   1215 H  H    B LEU   A 1 53  ? 21.268 5.653   6.159   0.44 12.96 ?  53  LEU   A H    1 
ATOM   1216 H  HA   A LEU   A 1 53  ? 21.826 5.654   8.697   0.56 13.29 ?  53  LEU   A HA   1 
ATOM   1217 H  HA   B LEU   A 1 53  ? 21.864 5.647   8.689   0.44 12.81 ?  53  LEU   A HA   1 
ATOM   1218 H  HB2  A LEU   A 1 53  ? 23.281 4.513   6.564   0.56 13.36 ?  53  LEU   A HB2  1 
ATOM   1219 H  HB2  B LEU   A 1 53  ? 23.275 4.572   6.515   0.44 12.73 ?  53  LEU   A HB2  1 
ATOM   1220 H  HB3  A LEU   A 1 53  ? 23.658 4.258   8.082   0.56 13.36 ?  53  LEU   A HB3  1 
ATOM   1221 H  HB3  B LEU   A 1 53  ? 23.831 4.431   7.981   0.44 12.73 ?  53  LEU   A HB3  1 
ATOM   1222 H  HG   A LEU   A 1 53  ? 21.216 3.408   6.948   0.56 13.60 ?  53  LEU   A HG   1 
ATOM   1223 H  HG   B LEU   A 1 53  ? 21.481 3.167   7.101   0.44 12.84 ?  53  LEU   A HG   1 
ATOM   1224 H  HD11 A LEU   A 1 53  ? 22.106 1.254   6.943   0.56 13.58 ?  53  LEU   A HD11 1 
ATOM   1225 H  HD11 B LEU   A 1 53  ? 22.724 1.191   7.038   0.44 12.90 ?  53  LEU   A HD11 1 
ATOM   1226 H  HD12 A LEU   A 1 53  ? 22.964 2.204   6.002   0.56 13.58 ?  53  LEU   A HD12 1 
ATOM   1227 H  HD12 B LEU   A 1 53  ? 23.295 2.251   6.002   0.44 12.90 ?  53  LEU   A HD12 1 
ATOM   1228 H  HD13 A LEU   A 1 53  ? 23.497 1.829   7.451   0.56 13.58 ?  53  LEU   A HD13 1 
ATOM   1229 H  HD13 B LEU   A 1 53  ? 24.036 2.015   7.388   0.44 12.90 ?  53  LEU   A HD13 1 
ATOM   1230 H  HD21 A LEU   A 1 53  ? 21.025 2.122   8.922   0.56 14.76 ?  53  LEU   A HD21 1 
ATOM   1231 H  HD21 B LEU   A 1 53  ? 21.511 1.932   9.048   0.44 12.98 ?  53  LEU   A HD21 1 
ATOM   1232 H  HD22 A LEU   A 1 53  ? 22.315 2.857   9.485   0.56 14.76 ?  53  LEU   A HD22 1 
ATOM   1233 H  HD22 B LEU   A 1 53  ? 22.837 2.666   9.522   0.44 12.98 ?  53  LEU   A HD22 1 
ATOM   1234 H  HD23 A LEU   A 1 53  ? 20.983 3.680   9.221   0.56 14.76 ?  53  LEU   A HD23 1 
ATOM   1235 H  HD23 B LEU   A 1 53  ? 21.472 3.473   9.429   0.44 12.98 ?  53  LEU   A HD23 1 
ATOM   1236 N  N    A ASN   A 1 54  ? 23.844 7.401   6.935   0.56 10.42 ?  54  ASN   A N    1 
ATOM   1237 N  N    B ASN   A 1 54  ? 23.892 7.419   6.941   0.44 10.30 ?  54  ASN   A N    1 
ATOM   1238 C  CA   A ASN   A 1 54  ? 24.900 8.394   7.060   0.56 10.75 ?  54  ASN   A CA   1 
ATOM   1239 C  CA   B ASN   A 1 54  ? 24.934 8.429   7.065   0.44 10.65 ?  54  ASN   A CA   1 
ATOM   1240 C  C    A ASN   A 1 54  ? 24.397 9.639   7.785   0.56 11.17 ?  54  ASN   A C    1 
ATOM   1241 C  C    B ASN   A 1 54  ? 24.414 9.676   7.771   0.44 11.08 ?  54  ASN   A C    1 
ATOM   1242 O  O    A ASN   A 1 54  ? 25.086 10.176  8.662   0.56 11.42 ?  54  ASN   A O    1 
ATOM   1243 O  O    B ASN   A 1 54  ? 25.108 10.258  8.614   0.44 11.24 ?  54  ASN   A O    1 
ATOM   1244 C  CB   A ASN   A 1 54  ? 25.456 8.749   5.689   0.56 10.73 ?  54  ASN   A CB   1 
ATOM   1245 C  CB   B ASN   A 1 54  ? 25.503 8.789   5.698   0.44 10.63 ?  54  ASN   A CB   1 
ATOM   1246 C  CG   A ASN   A 1 54  ? 26.516 9.812   5.781   0.56 10.69 ?  54  ASN   A CG   1 
ATOM   1247 C  CG   B ASN   A 1 54  ? 26.474 9.938   5.786   0.44 10.56 ?  54  ASN   A CG   1 
ATOM   1248 O  OD1  A ASN   A 1 54  ? 27.511 9.638   6.487   0.56 10.81 ?  54  ASN   A OD1  1 
ATOM   1249 O  OD1  B ASN   A 1 54  ? 27.499 9.834   6.459   0.44 10.75 ?  54  ASN   A OD1  1 
ATOM   1250 N  ND2  A ASN   A 1 54  ? 26.309 10.926  5.098   0.56 11.40 ?  54  ASN   A ND2  1 
ATOM   1251 N  ND2  B ASN   A 1 54  ? 26.147 11.053  5.144   0.44 11.46 ?  54  ASN   A ND2  1 
ATOM   1252 H  H    A ASN   A 1 54  ? 23.586 7.227   6.133   0.56 12.50 ?  54  ASN   A H    1 
ATOM   1253 H  H    B ASN   A 1 54  ? 23.687 7.199   6.134   0.44 12.36 ?  54  ASN   A H    1 
ATOM   1254 H  HA   A ASN   A 1 54  ? 25.618 8.015   7.585   0.56 12.90 ?  54  ASN   A HA   1 
ATOM   1255 H  HA   B ASN   A 1 54  ? 25.652 8.068   7.602   0.44 12.78 ?  54  ASN   A HA   1 
ATOM   1256 H  HB2  A ASN   A 1 54  ? 25.852 7.950   5.293   0.56 12.87 ?  54  ASN   A HB2  1 
ATOM   1257 H  HB2  B ASN   A 1 54  ? 25.977 8.018   5.341   0.44 12.75 ?  54  ASN   A HB2  1 
ATOM   1258 H  HB3  A ASN   A 1 54  ? 24.739 9.075   5.126   0.56 12.87 ?  54  ASN   A HB3  1 
ATOM   1259 H  HB3  B ASN   A 1 54  ? 24.781 9.041   5.105   0.44 12.75 ?  54  ASN   A HB3  1 
ATOM   1260 H  HD21 A ASN   A 1 54  ? 26.888 11.555  5.129   0.56 13.68 ?  54  ASN   A HD21 1 
ATOM   1261 H  HD21 B ASN   A 1 54  ? 26.668 11.737  5.175   0.44 13.75 ?  54  ASN   A HD21 1 
ATOM   1262 H  HD22 A ASN   A 1 54  ? 25.598 11.011  4.622   0.56 13.68 ?  54  ASN   A HD22 1 
ATOM   1263 H  HD22 B ASN   A 1 54  ? 25.417 11.090  4.689   0.44 13.75 ?  54  ASN   A HD22 1 
ATOM   1264 N  N    . LYS   A 1 55  ? 23.191 10.102  7.442   1.00 11.26 ?  55  LYS   A N    1 
ATOM   1265 C  CA   . LYS   A 1 55  ? 22.610 11.258  8.115   1.00 12.04 ?  55  LYS   A CA   1 
ATOM   1266 C  C    . LYS   A 1 55  ? 22.527 11.023  9.616   1.00 12.13 ?  55  LYS   A C    1 
ATOM   1267 O  O    . LYS   A 1 55  ? 22.816 11.924  10.414  1.00 12.76 ?  55  LYS   A O    1 
ATOM   1268 C  CB   . LYS   A 1 55  ? 21.235 11.553  7.505   1.00 13.01 ?  55  LYS   A CB   1 
ATOM   1269 C  CG   . LYS   A 1 55  ? 20.479 12.720  8.109   1.00 14.74 ?  55  LYS   A CG   1 
ATOM   1270 C  CD   . LYS   A 1 55  ? 19.152 12.935  7.373   1.00 16.56 ?  55  LYS   A CD   1 
ATOM   1271 C  CE   . LYS   A 1 55  ? 18.298 14.011  8.024   1.00 18.59 ?  55  LYS   A CE   1 
ATOM   1272 N  NZ   . LYS   A 1 55  ? 16.975 14.156  7.346   1.00 19.14 ?  55  LYS   A NZ   1 
ATOM   1273 H  H    A LYS   A 1 55  ? 22.687 9.761   6.832   0.56 13.51 ?  55  LYS   A H    1 
ATOM   1274 H  H    B LYS   A 1 55  ? 22.680 9.738   6.852   0.44 13.51 ?  55  LYS   A H    1 
ATOM   1275 H  HA   . LYS   A 1 55  ? 23.172 12.030  7.968   1.00 14.45 ?  55  LYS   A HA   1 
ATOM   1276 H  HB2  . LYS   A 1 55  ? 21.351 11.747  6.564   1.00 15.61 ?  55  LYS   A HB2  1 
ATOM   1277 H  HB3  . LYS   A 1 55  ? 20.674 10.768  7.608   1.00 15.61 ?  55  LYS   A HB3  1 
ATOM   1278 H  HG2  . LYS   A 1 55  ? 20.281 12.533  9.041   1.00 17.69 ?  55  LYS   A HG2  1 
ATOM   1279 H  HG3  . LYS   A 1 55  ? 21.007 13.526  8.028   1.00 17.69 ?  55  LYS   A HG3  1 
ATOM   1280 H  HD2  . LYS   A 1 55  ? 19.337 13.206  6.459   1.00 19.87 ?  55  LYS   A HD2  1 
ATOM   1281 H  HD3  . LYS   A 1 55  ? 18.648 12.104  7.375   1.00 19.87 ?  55  LYS   A HD3  1 
ATOM   1282 H  HE2  . LYS   A 1 55  ? 18.138 13.773  8.950   1.00 22.31 ?  55  LYS   A HE2  1 
ATOM   1283 H  HE3  . LYS   A 1 55  ? 18.760 14.861  7.970   1.00 22.31 ?  55  LYS   A HE3  1 
ATOM   1284 H  HZ1  . LYS   A 1 55  ? 16.423 14.637  7.855   1.00 22.97 ?  55  LYS   A HZ1  1 
ATOM   1285 H  HZ2  . LYS   A 1 55  ? 17.075 14.570  6.564   1.00 22.97 ?  55  LYS   A HZ2  1 
ATOM   1286 H  HZ3  . LYS   A 1 55  ? 16.611 13.356  7.206   1.00 22.97 ?  55  LYS   A HZ3  1 
ATOM   1287 N  N    . ALA   A 1 56  ? 22.139 9.809   10.019  1.00 12.61 ?  56  ALA   A N    1 
ATOM   1288 C  CA   . ALA   A 1 56  ? 22.023 9.475   11.433  1.00 13.16 ?  56  ALA   A CA   1 
ATOM   1289 C  C    . ALA   A 1 56  ? 23.365 9.498   12.154  1.00 13.22 ?  56  ALA   A C    1 
ATOM   1290 O  O    . ALA   A 1 56  ? 23.391 9.665   13.375  1.00 14.35 ?  56  ALA   A O    1 
ATOM   1291 C  CB   . ALA   A 1 56  ? 21.333 8.115   11.609  1.00 13.96 ?  56  ALA   A CB   1 
ATOM   1292 H  H    . ALA   A 1 56  ? 21.934 9.165   9.489   1.00 15.14 ?  56  ALA   A H    1 
ATOM   1293 H  HA   . ALA   A 1 56  ? 21.458 10.130  11.861  1.00 15.80 ?  56  ALA   A HA   1 
ATOM   1294 H  HB1  . ALA   A 1 56  ? 21.265 7.910   12.557  1.00 16.75 ?  56  ALA   A HB1  1 
ATOM   1295 H  HB2  . ALA   A 1 56  ? 20.445 8.156   11.219  1.00 16.75 ?  56  ALA   A HB2  1 
ATOM   1296 H  HB3  . ALA   A 1 56  ? 21.856 7.428   11.162  1.00 16.75 ?  56  ALA   A HB3  1 
ATOM   1297 N  N    . THR   A 1 57  ? 24.474 9.314   11.434  1.00 12.17 ?  57  THR   A N    1 
ATOM   1298 C  CA   . THR   A 1 57  ? 25.815 9.444   12.010  1.00 12.10 ?  57  THR   A CA   1 
ATOM   1299 C  C    . THR   A 1 57  ? 26.369 10.864  11.920  1.00 12.48 ?  57  THR   A C    1 
ATOM   1300 O  O    . THR   A 1 57  ? 27.556 11.078  12.210  1.00 13.03 ?  57  THR   A O    1 
ATOM   1301 C  CB   . THR   A 1 57  ? 26.824 8.493   11.343  1.00 12.20 ?  57  THR   A CB   1 
ATOM   1302 O  OG1  . THR   A 1 57  ? 27.200 8.988   10.045  1.00 11.67 ?  57  THR   A OG1  1 
ATOM   1303 C  CG2  . THR   A 1 57  ? 26.288 7.080   11.234  1.00 12.25 ?  57  THR   A CG2  1 
ATOM   1304 H  H    . THR   A 1 57  ? 24.475 9.090   10.606  1.00 14.60 ?  57  THR   A H    1 
ATOM   1305 H  HA   . THR   A 1 57  ? 25.768 9.190   12.952  1.00 14.52 ?  57  THR   A HA   1 
ATOM   1306 H  HB   . THR   A 1 57  ? 27.622 8.452   11.898  1.00 14.64 ?  57  THR   A HB   1 
ATOM   1307 H  HG1  . THR   A 1 57  ? 26.521 9.049   9.555   1.00 14.00 ?  57  THR   A HG1  1 
ATOM   1308 H  HG21 . THR   A 1 57  ? 26.978 6.483   10.900  1.00 14.70 ?  57  THR   A HG21 1 
ATOM   1309 H  HG22 . THR   A 1 57  ? 25.997 6.765   12.106  1.00 14.70 ?  57  THR   A HG22 1 
ATOM   1310 H  HG23 . THR   A 1 57  ? 25.535 7.055   10.627  1.00 14.70 ?  57  THR   A HG23 1 
ATOM   1311 N  N    . ASN   A 1 58  ? 25.553 11.836  11.516  1.00 12.96 ?  58  ASN   A N    1 
ATOM   1312 C  CA   . ASN   A 1 58  ? 26.018 13.215  11.415  1.00 13.97 ?  58  ASN   A CA   1 
ATOM   1313 C  C    . ASN   A 1 58  ? 27.171 13.337  10.412  1.00 12.93 ?  58  ASN   A C    1 
ATOM   1314 O  O    . ASN   A 1 58  ? 28.074 14.165  10.576  1.00 13.46 ?  58  ASN   A O    1 
ATOM   1315 C  CB   . ASN   A 1 58  ? 26.388 13.757  12.808  1.00 17.06 ?  58  ASN   A CB   1 
ATOM   1316 C  CG   . ASN   A 1 58  ? 26.763 15.222  12.804  1.00 20.86 ?  58  ASN   A CG   1 
ATOM   1317 O  OD1  . ASN   A 1 58  ? 26.150 16.025  12.111  1.00 22.15 ?  58  ASN   A OD1  1 
ATOM   1318 N  ND2  . ASN   A 1 58  ? 27.775 15.580  13.590  1.00 22.72 ?  58  ASN   A ND2  1 
ATOM   1319 H  H    . ASN   A 1 58  ? 24.731 11.710  11.283  1.00 15.56 ?  58  ASN   A H    1 
ATOM   1320 H  HA   . ASN   A 1 58  ? 25.281 13.747  11.082  1.00 16.77 ?  58  ASN   A HA   1 
ATOM   1321 H  HB2  . ASN   A 1 58  ? 25.622 13.639  13.404  1.00 20.47 ?  58  ASN   A HB2  1 
ATOM   1322 H  HB3  . ASN   A 1 58  ? 27.144 13.265  13.152  1.00 20.47 ?  58  ASN   A HB3  1 
ATOM   1323 H  HD21 . ASN   A 1 58  ? 28.011 16.409  13.631  1.00 27.27 ?  58  ASN   A HD21 1 
ATOM   1324 H  HD22 . ASN   A 1 58  ? 28.173 14.992  14.063  1.00 27.27 ?  58  ASN   A HD22 1 
ATOM   1325 N  N    . ASN   A 1 59  ? 27.142 12.520  9.355   1.00 11.87 ?  59  ASN   A N    1 
ATOM   1326 C  CA   . ASN   A 1 59  ? 28.119 12.497  8.259   1.00 11.77 ?  59  ASN   A CA   1 
ATOM   1327 C  C    . ASN   A 1 59  ? 29.436 11.816  8.643   1.00 11.49 ?  59  ASN   A C    1 
ATOM   1328 O  O    . ASN   A 1 59  ? 30.349 11.769  7.815   1.00 11.50 ?  59  ASN   A O    1 
ATOM   1329 C  CB   . ASN   A 1 59  ? 28.408 13.884  7.656   1.00 12.01 ?  59  ASN   A CB   1 
ATOM   1330 C  CG   . ASN   A 1 59  ? 28.759 13.822  6.185   1.00 12.04 ?  59  ASN   A CG   1 
ATOM   1331 O  OD1  . ASN   A 1 59  ? 28.047 13.207  5.391   1.00 12.24 ?  59  ASN   A OD1  1 
ATOM   1332 N  ND2  . ASN   A 1 59  ? 29.850 14.475  5.806   1.00 12.68 ?  59  ASN   A ND2  1 
ATOM   1333 H  H    . ASN   A 1 59  ? 26.520 11.933  9.240   1.00 14.24 ?  59  ASN   A H    1 
ATOM   1334 H  HA   . ASN   A 1 59  ? 27.737 11.968  7.548   1.00 14.12 ?  59  ASN   A HA   1 
ATOM   1335 H  HB2  . ASN   A 1 59  ? 27.622 14.443  7.747   1.00 14.41 ?  59  ASN   A HB2  1 
ATOM   1336 H  HB3  . ASN   A 1 59  ? 29.159 14.285  8.120   1.00 14.41 ?  59  ASN   A HB3  1 
ATOM   1337 H  HD21 . ASN   A 1 59  ? 30.090 14.470  4.980   1.00 15.21 ?  59  ASN   A HD21 1 
ATOM   1338 H  HD22 . ASN   A 1 59  ? 30.328 14.893  6.388   1.00 15.21 ?  59  ASN   A HD22 1 
ATOM   1339 N  N    . ALA   A 1 60  ? 29.562 11.269  9.852   1.00 11.60 ?  60  ALA   A N    1 
ATOM   1340 C  CA   . ALA   A 1 60  ? 30.798 10.578  10.202  1.00 11.65 ?  60  ALA   A CA   1 
ATOM   1341 C  C    . ALA   A 1 60  ? 31.016 9.344   9.336   1.00 11.44 ?  60  ALA   A C    1 
ATOM   1342 O  O    . ALA   A 1 60  ? 32.161 9.025   9.000   1.00 11.68 ?  60  ALA   A O    1 
ATOM   1343 C  CB   . ALA   A 1 60  ? 30.800 10.215  11.682  1.00 12.35 ?  60  ALA   A CB   1 
ATOM   1344 H  H    . ALA   A 1 60  ? 28.965 11.281  10.470  1.00 13.93 ?  60  ALA   A H    1 
ATOM   1345 H  HA   . ALA   A 1 60  ? 31.543 11.179  10.044  1.00 13.98 ?  60  ALA   A HA   1 
ATOM   1346 H  HB1  . ALA   A 1 60  ? 31.632 9.759   11.895  1.00 14.82 ?  60  ALA   A HB1  1 
ATOM   1347 H  HB2  . ALA   A 1 60  ? 30.731 11.030  12.207  1.00 14.82 ?  60  ALA   A HB2  1 
ATOM   1348 H  HB3  . ALA   A 1 60  ? 30.048 9.636   11.869  1.00 14.82 ?  60  ALA   A HB3  1 
ATOM   1349 N  N    . MET   A 1 61  ? 29.941 8.648   8.960   1.00 11.01 ?  61  MET   A N    1 
ATOM   1350 C  CA   . MET   A 1 61  ? 30.071 7.512   8.051   1.00 10.81 ?  61  MET   A CA   1 
ATOM   1351 C  C    . MET   A 1 61  ? 30.699 7.939   6.725   1.00 10.68 ?  61  MET   A C    1 
ATOM   1352 O  O    . MET   A 1 61  ? 31.593 7.258   6.204   1.00 11.02 ?  61  MET   A O    1 
ATOM   1353 C  CB   . MET   A 1 61  ? 28.706 6.848   7.843   1.00 10.87 ?  61  MET   A CB   1 
ATOM   1354 C  CG   . MET   A 1 61  ? 28.718 5.692   6.862   1.00 11.50 ?  61  MET   A CG   1 
ATOM   1355 S  SD   . MET   A 1 61  ? 27.097 4.941   6.669   1.00 12.27 ?  61  MET   A SD   1 
ATOM   1356 C  CE   . MET   A 1 61  ? 26.985 4.042   8.225   1.00 13.65 ?  61  MET   A CE   1 
ATOM   1357 H  H    . MET   A 1 61  ? 29.136 8.808   9.217   1.00 13.21 ?  61  MET   A H    1 
ATOM   1358 H  HA   . MET   A 1 61  ? 30.651 6.854   8.464   1.00 12.97 ?  61  MET   A HA   1 
ATOM   1359 H  HB2  . MET   A 1 61  ? 28.395 6.508   8.695   1.00 13.05 ?  61  MET   A HB2  1 
ATOM   1360 H  HB3  . MET   A 1 61  ? 28.085 7.512   7.508   1.00 13.05 ?  61  MET   A HB3  1 
ATOM   1361 H  HG2  . MET   A 1 61  ? 29.001 6.009   5.991   1.00 13.80 ?  61  MET   A HG2  1 
ATOM   1362 H  HG3  . MET   A 1 61  ? 29.326 5.007   7.182   1.00 13.80 ?  61  MET   A HG3  1 
ATOM   1363 H  HE1  . MET   A 1 61  ? 26.153 3.543   8.249   1.00 16.38 ?  61  MET   A HE1  1 
ATOM   1364 H  HE2  . MET   A 1 61  ? 27.737 3.430   8.291   1.00 16.38 ?  61  MET   A HE2  1 
ATOM   1365 H  HE3  . MET   A 1 61  ? 27.012 4.674   8.961   1.00 16.38 ?  61  MET   A HE3  1 
ATOM   1366 N  N    . GLN   A 1 62  ? 30.255 9.074   6.170   1.00 10.63 ?  62  GLN   A N    1 
ATOM   1367 C  CA   . GLN   A 1 62  ? 30.819 9.550   4.910   1.00 10.90 ?  62  GLN   A CA   1 
ATOM   1368 C  C    . GLN   A 1 62  ? 32.291 9.923   5.053   1.00 10.84 ?  62  GLN   A C    1 
ATOM   1369 O  O    . GLN   A 1 62  ? 33.101 9.611   4.173   1.00 11.25 ?  62  GLN   A O    1 
ATOM   1370 C  CB   . GLN   A 1 62  ? 30.017 10.737  4.382   1.00 10.89 ?  62  GLN   A CB   1 
ATOM   1371 C  CG   . GLN   A 1 62  ? 30.399 11.101  2.959   1.00 10.85 ?  62  GLN   A CG   1 
ATOM   1372 C  CD   . GLN   A 1 62  ? 30.067 9.973   2.002   1.00 11.30 ?  62  GLN   A CD   1 
ATOM   1373 O  OE1  . GLN   A 1 62  ? 28.887 9.673   1.785   1.00 11.89 ?  62  GLN   A OE1  1 
ATOM   1374 N  NE2  . GLN   A 1 62  ? 31.086 9.297   1.478   1.00 11.72 ?  62  GLN   A NE2  1 
ATOM   1375 H  H    . GLN   A 1 62  ? 29.635 9.569   6.501   1.00 12.75 ?  62  GLN   A H    1 
ATOM   1376 H  HA   . GLN   A 1 62  ? 30.758 8.832   4.261   1.00 13.08 ?  62  GLN   A HA   1 
ATOM   1377 H  HB2  . GLN   A 1 62  ? 29.071 10.515  4.395   1.00 13.06 ?  62  GLN   A HB2  1 
ATOM   1378 H  HB3  . GLN   A 1 62  ? 30.183 11.509  4.948   1.00 13.06 ?  62  GLN   A HB3  1 
ATOM   1379 H  HG2  . GLN   A 1 62  ? 29.900 11.886  2.684   1.00 13.02 ?  62  GLN   A HG2  1 
ATOM   1380 H  HG3  . GLN   A 1 62  ? 31.351 11.273  2.912   1.00 13.02 ?  62  GLN   A HG3  1 
ATOM   1381 H  HE21 . GLN   A 1 62  ? 31.892 9.523   1.667   1.00 14.06 ?  62  GLN   A HE21 1 
ATOM   1382 H  HE22 . GLN   A 1 62  ? 30.934 8.642   0.943   1.00 14.06 ?  62  GLN   A HE22 1 
ATOM   1383 N  N    . VAL   A 1 63  ? 32.658 10.604  6.144   1.00 11.46 ?  63  VAL   A N    1 
ATOM   1384 C  CA   . VAL   A 1 63  ? 34.053 10.999  6.352   1.00 12.23 ?  63  VAL   A CA   1 
ATOM   1385 C  C    . VAL   A 1 63  ? 34.949 9.763   6.408   1.00 11.57 ?  63  VAL   A C    1 
ATOM   1386 O  O    . VAL   A 1 63  ? 36.000 9.696   5.752   1.00 12.00 ?  63  VAL   A O    1 
ATOM   1387 C  CB   . VAL   A 1 63  ? 34.169 11.866  7.618   1.00 13.57 ?  63  VAL   A CB   1 
ATOM   1388 C  CG1  . VAL   A 1 63  ? 35.619 12.109  7.976   1.00 15.58 ?  63  VAL   A CG1  1 
ATOM   1389 C  CG2  . VAL   A 1 63  ? 33.433 13.199  7.420   1.00 14.28 ?  63  VAL   A CG2  1 
ATOM   1390 H  H    . VAL   A 1 63  ? 32.117 10.848  6.772   1.00 13.75 ?  63  VAL   A H    1 
ATOM   1391 H  HA   . VAL   A 1 63  ? 34.332 11.537  5.597   1.00 14.67 ?  63  VAL   A HA   1 
ATOM   1392 H  HB   . VAL   A 1 63  ? 33.752 11.398  8.360   1.00 16.29 ?  63  VAL   A HB   1 
ATOM   1393 H  HG11 . VAL   A 1 63  ? 35.667 12.841  8.609   1.00 18.69 ?  63  VAL   A HG11 1 
ATOM   1394 H  HG12 . VAL   A 1 63  ? 35.991 11.305  8.370   1.00 18.69 ?  63  VAL   A HG12 1 
ATOM   1395 H  HG13 . VAL   A 1 63  ? 36.106 12.340  7.168   1.00 18.69 ?  63  VAL   A HG13 1 
ATOM   1396 H  HG21 . VAL   A 1 63  ? 33.527 13.736  8.225   1.00 17.13 ?  63  VAL   A HG21 1 
ATOM   1397 H  HG22 . VAL   A 1 63  ? 33.826 13.670  6.666   1.00 17.13 ?  63  VAL   A HG22 1 
ATOM   1398 H  HG23 . VAL   A 1 63  ? 32.495 13.026  7.248   1.00 17.13 ?  63  VAL   A HG23 1 
ATOM   1399 N  N    . GLU   A 1 64  ? 34.534 8.757   7.181   1.00 11.48 ?  64  GLU   A N    1 
ATOM   1400 C  CA   . GLU   A 1 64  ? 35.292 7.513   7.271   1.00 11.57 ?  64  GLU   A CA   1 
ATOM   1401 C  C    . GLU   A 1 64  ? 35.371 6.827   5.915   1.00 11.12 ?  64  GLU   A C    1 
ATOM   1402 O  O    . GLU   A 1 64  ? 36.421 6.284   5.534   1.00 11.60 ?  64  GLU   A O    1 
ATOM   1403 C  CB   . GLU   A 1 64  ? 34.606 6.604   8.289   1.00 12.06 ?  64  GLU   A CB   1 
ATOM   1404 C  CG   . GLU   A 1 64  ? 35.254 5.254   8.449   1.00 12.72 ?  64  GLU   A CG   1 
ATOM   1405 C  CD   . GLU   A 1 64  ? 34.365 4.259   9.163   1.00 13.12 ?  64  GLU   A CD   1 
ATOM   1406 O  OE1  . GLU   A 1 64  ? 33.126 4.350   9.018   1.00 13.96 ?  64  GLU   A OE1  1 
ATOM   1407 O  OE2  . GLU   A 1 64  ? 34.908 3.363   9.852   1.00 13.57 -1 64  GLU   A OE2  1 
ATOM   1408 H  H    . GLU   A 1 64  ? 33.817 8.769   7.655   1.00 13.78 ?  64  GLU   A H    1 
ATOM   1409 H  HA   . GLU   A 1 64  ? 36.194 7.710   7.582   1.00 13.88 ?  64  GLU   A HA   1 
ATOM   1410 H  HB2  . GLU   A 1 64  ? 34.619 7.048   9.157   1.00 14.47 ?  64  GLU   A HB2  1 
ATOM   1411 H  HB3  . GLU   A 1 64  ? 33.688 6.474   8.008   1.00 14.47 ?  64  GLU   A HB3  1 
ATOM   1412 H  HG2  . GLU   A 1 64  ? 35.463 4.886   7.574   1.00 15.26 ?  64  GLU   A HG2  1 
ATOM   1413 H  HG3  . GLU   A 1 64  ? 36.068 5.354   8.964   1.00 15.26 ?  64  GLU   A HG3  1 
ATOM   1414 N  N    . SER   A 1 65  ? 34.255 6.824   5.185   1.00 10.87 ?  65  SER   A N    1 
ATOM   1415 C  CA   . SER   A 1 65  ? 34.198 6.167   3.883   1.00 10.71 ?  65  SER   A CA   1 
ATOM   1416 C  C    . SER   A 1 65  ? 35.124 6.836   2.875   1.00 10.98 ?  65  SER   A C    1 
ATOM   1417 O  O    . SER   A 1 65  ? 35.763 6.159   2.061   1.00 11.96 ?  65  SER   A O    1 
ATOM   1418 C  CB   . SER   A 1 65  ? 32.764 6.185   3.352   1.00 10.60 ?  65  SER   A CB   1 
ATOM   1419 O  OG   . SER   A 1 65  ? 31.909 5.369   4.146   1.00 11.41 ?  65  SER   A OG   1 
ATOM   1420 H  H    . SER   A 1 65  ? 33.519 7.195   5.426   1.00 13.05 ?  65  SER   A H    1 
ATOM   1421 H  HA   . SER   A 1 65  ? 34.477 5.244   3.979   1.00 12.85 ?  65  SER   A HA   1 
ATOM   1422 H  HB2  . SER   A 1 65  ? 32.434 7.097   3.367   1.00 12.72 ?  65  SER   A HB2  1 
ATOM   1423 H  HB3  . SER   A 1 65  ? 32.764 5.848   2.443   1.00 12.72 ?  65  SER   A HB3  1 
ATOM   1424 H  HG   . SER   A 1 65  ? 31.907 5.654   4.943   1.00 13.69 ?  65  SER   A HG   1 
ATOM   1425 N  N    . ASP   A 1 66  ? 35.199 8.167   2.901   1.00 11.12 ?  66  ASP   A N    1 
ATOM   1426 C  CA   . ASP   A 1 66  ? 36.062 8.868   1.959   1.00 12.10 ?  66  ASP   A CA   1 
ATOM   1427 C  C    . ASP   A 1 66  ? 37.521 8.504   2.188   1.00 11.97 ?  66  ASP   A C    1 
ATOM   1428 O  O    . ASP   A 1 66  ? 38.286 8.330   1.231   1.00 12.95 ?  66  ASP   A O    1 
ATOM   1429 C  CB   . ASP   A 1 66  ? 35.848 10.374  2.079   1.00 13.30 ?  66  ASP   A CB   1 
ATOM   1430 C  CG   . ASP   A 1 66  ? 34.511 10.839  1.487   1.00 14.84 ?  66  ASP   A CG   1 
ATOM   1431 O  OD1  . ASP   A 1 66  ? 33.790 10.047  0.838   1.00 15.27 ?  66  ASP   A OD1  1 
ATOM   1432 O  OD2  . ASP   A 1 66  ? 34.208 12.037  1.651   1.00 17.86 -1 66  ASP   A OD2  1 
ATOM   1433 H  H    . ASP   A 1 66  ? 34.764 8.676   3.445   1.00 13.34 ?  66  ASP   A H    1 
ATOM   1434 H  HA   . ASP   A 1 66  ? 35.821 8.602   1.060   1.00 14.53 ?  66  ASP   A HA   1 
ATOM   1435 H  HB2  . ASP   A 1 66  ? 35.860 10.624  3.017   1.00 15.96 ?  66  ASP   A HB2  1 
ATOM   1436 H  HB3  . ASP   A 1 66  ? 36.563 10.831  1.607   1.00 15.96 ?  66  ASP   A HB3  1 
ATOM   1437 N  N    . ASP   A 1 67  ? 37.926 8.370   3.451   1.00 12.14 ?  67  ASP   A N    1 
ATOM   1438 C  CA   . ASP   A 1 67  ? 39.281 7.921   3.741   1.00 12.75 ?  67  ASP   A CA   1 
ATOM   1439 C  C    . ASP   A 1 67  ? 39.493 6.485   3.274   1.00 12.74 ?  67  ASP   A C    1 
ATOM   1440 O  O    . ASP   A 1 67  ? 40.548 6.159   2.717   1.00 13.36 ?  67  ASP   A O    1 
ATOM   1441 C  CB   . ASP   A 1 67  ? 39.555 8.052   5.235   1.00 14.23 ?  67  ASP   A CB   1 
ATOM   1442 C  CG   . ASP   A 1 67  ? 40.850 7.392   5.646   1.00 15.44 ?  67  ASP   A CG   1 
ATOM   1443 O  OD1  . ASP   A 1 67  ? 41.927 8.016   5.490   1.00 17.88 ?  67  ASP   A OD1  1 
ATOM   1444 O  OD2  . ASP   A 1 67  ? 40.799 6.236   6.121   1.00 15.17 -1 67  ASP   A OD2  1 
ATOM   1445 H  H    . ASP   A 1 67  ? 37.447 8.530   4.142   1.00 14.56 ?  67  ASP   A H    1 
ATOM   1446 H  HA   . ASP   A 1 67  ? 39.912 8.485   3.264   1.00 15.30 ?  67  ASP   A HA   1 
ATOM   1447 H  HB2  . ASP   A 1 67  ? 39.617 8.986   5.462   1.00 17.07 ?  67  ASP   A HB2  1 
ATOM   1448 H  HB3  . ASP   A 1 67  ? 38.832 7.628   5.723   1.00 17.07 ?  67  ASP   A HB3  1 
ATOM   1449 N  N    . TYR   A 1 68  ? 38.498 5.612   3.477   1.00 12.37 ?  68  TYR   A N    1 
ATOM   1450 C  CA   . TYR   A 1 68  ? 38.607 4.235   2.996   1.00 12.41 ?  68  TYR   A CA   1 
ATOM   1451 C  C    . TYR   A 1 68  ? 38.850 4.190   1.489   1.00 12.29 ?  68  TYR   A C    1 
ATOM   1452 O  O    . TYR   A 1 68  ? 39.723 3.452   1.013   1.00 12.92 ?  68  TYR   A O    1 
ATOM   1453 C  CB   . TYR   A 1 68  ? 37.350 3.420   3.367   1.00 12.89 ?  68  TYR   A CB   1 
ATOM   1454 C  CG   . TYR   A 1 68  ? 37.378 2.030   2.738   1.00 14.35 ?  68  TYR   A CG   1 
ATOM   1455 C  CD1  . TYR   A 1 68  ? 36.925 1.834   1.436   1.00 15.68 ?  68  TYR   A CD1  1 
ATOM   1456 C  CD2  . TYR   A 1 68  ? 37.918 0.941   3.409   1.00 16.00 ?  68  TYR   A CD2  1 
ATOM   1457 C  CE1  . TYR   A 1 68  ? 36.994 0.614   0.822   1.00 16.98 ?  68  TYR   A CE1  1 
ATOM   1458 C  CE2  . TYR   A 1 68  ? 37.981 -0.318  2.795   1.00 16.52 ?  68  TYR   A CE2  1 
ATOM   1459 C  CZ   . TYR   A 1 68  ? 37.529 -0.456  1.500   1.00 17.02 ?  68  TYR   A CZ   1 
ATOM   1460 O  OH   . TYR   A 1 68  ? 37.605 -1.667  0.870   1.00 18.11 ?  68  TYR   A OH   1 
ATOM   1461 H  H    . TYR   A 1 68  ? 37.759 5.789   3.884   1.00 14.85 ?  68  TYR   A H    1 
ATOM   1462 H  HA   . TYR   A 1 68  ? 39.362 3.812   3.429   1.00 14.90 ?  68  TYR   A HA   1 
ATOM   1463 H  HB2  . TYR   A 1 68  ? 37.309 3.312   4.331   1.00 15.47 ?  68  TYR   A HB2  1 
ATOM   1464 H  HB3  . TYR   A 1 68  ? 36.558 3.881   3.048   1.00 15.47 ?  68  TYR   A HB3  1 
ATOM   1465 H  HD1  . TYR   A 1 68  ? 36.577 2.562   0.966   1.00 18.82 ?  68  TYR   A HD1  1 
ATOM   1466 H  HD2  . TYR   A 1 68  ? 38.244 1.048   4.271   1.00 19.20 ?  68  TYR   A HD2  1 
ATOM   1467 H  HE1  . TYR   A 1 68  ? 36.681 0.511   -0.049  1.00 20.38 ?  68  TYR   A HE1  1 
ATOM   1468 H  HE2  . TYR   A 1 68  ? 38.350 -1.044  3.238   1.00 19.83 ?  68  TYR   A HE2  1 
ATOM   1469 H  HH   . TYR   A 1 68  ? 37.943 -2.235  1.389   1.00 21.73 ?  68  TYR   A HH   1 
ATOM   1470 N  N    . ILE   A 1 69  ? 38.063 4.947   0.718   1.00 11.83 ?  69  ILE   A N    1 
ATOM   1471 C  CA   . ILE   A 1 69  ? 38.201 4.933   -0.736  1.00 11.79 ?  69  ILE   A CA   1 
ATOM   1472 C  C    . ILE   A 1 69  ? 39.539 5.537   -1.160  1.00 11.82 ?  69  ILE   A C    1 
ATOM   1473 O  O    . ILE   A 1 69  ? 40.190 5.048   -2.091  1.00 12.27 ?  69  ILE   A O    1 
ATOM   1474 C  CB   . ILE   A 1 69  ? 37.007 5.649   -1.400  1.00 12.73 ?  69  ILE   A CB   1 
ATOM   1475 C  CG1  . ILE   A 1 69  ? 35.694 4.909   -1.132  1.00 13.19 ?  69  ILE   A CG1  1 
ATOM   1476 C  CG2  . ILE   A 1 69  ? 37.244 5.845   -2.900  1.00 14.10 ?  69  ILE   A CG2  1 
ATOM   1477 C  CD1  . ILE   A 1 69  ? 35.521 3.627   -1.910  1.00 13.69 ?  69  ILE   A CD1  1 
ATOM   1478 H  H    . ILE   A 1 69  ? 37.458 5.481   1.016   1.00 14.20 ?  69  ILE   A H    1 
ATOM   1479 H  HA   . ILE   A 1 69  ? 38.195 4.014   -1.031  1.00 14.14 ?  69  ILE   A HA   1 
ATOM   1480 H  HB   . ILE   A 1 69  ? 36.931 6.525   -1.000  1.00 15.28 ?  69  ILE   A HB   1 
ATOM   1481 H  HG12 . ILE   A 1 69  ? 35.652 4.682   -0.189  1.00 15.83 ?  69  ILE   A HG12 1 
ATOM   1482 H  HG13 . ILE   A 1 69  ? 34.957 5.491   -1.361  1.00 15.83 ?  69  ILE   A HG13 1 
ATOM   1483 H  HG21 . ILE   A 1 69  ? 36.398 6.063   -3.327  1.00 16.93 ?  69  ILE   A HG21 1 
ATOM   1484 H  HG22 . ILE   A 1 69  ? 37.870 6.580   -3.029  1.00 16.93 ?  69  ILE   A HG22 1 
ATOM   1485 H  HG23 . ILE   A 1 69  ? 37.605 5.032   -3.278  1.00 16.93 ?  69  ILE   A HG23 1 
ATOM   1486 H  HD11 . ILE   A 1 69  ? 34.723 3.172   -1.596  1.00 16.43 ?  69  ILE   A HD11 1 
ATOM   1487 H  HD12 . ILE   A 1 69  ? 35.426 3.837   -2.854  1.00 16.43 ?  69  ILE   A HD12 1 
ATOM   1488 H  HD13 . ILE   A 1 69  ? 36.296 3.060   -1.774  1.00 16.43 ?  69  ILE   A HD13 1 
ATOM   1489 N  N    . ALA   A 1 70  ? 39.959 6.624   -0.508  1.00 12.36 ?  70  ALA   A N    1 
ATOM   1490 C  CA   . ALA   A 1 70  ? 41.242 7.227   -0.857  1.00 13.41 ?  70  ALA   A CA   1 
ATOM   1491 C  C    . ALA   A 1 70  ? 42.383 6.233   -0.694  1.00 13.73 ?  70  ALA   A C    1 
ATOM   1492 O  O    . ALA   A 1 70  ? 43.349 6.263   -1.463  1.00 15.35 ?  70  ALA   A O    1 
ATOM   1493 C  CB   . ALA   A 1 70  ? 41.492 8.473   -0.003  1.00 14.13 ?  70  ALA   A CB   1 
ATOM   1494 H  H    . ALA   A 1 70  ? 39.532 7.018   0.126   1.00 14.83 ?  70  ALA   A H    1 
ATOM   1495 H  HA   . ALA   A 1 70  ? 41.212 7.510   -1.786  1.00 16.09 ?  70  ALA   A HA   1 
ATOM   1496 H  HB1  . ALA   A 1 70  ? 42.350 8.859   -0.253  1.00 16.96 ?  70  ALA   A HB1  1 
ATOM   1497 H  HB2  . ALA   A 1 70  ? 40.785 9.117   -0.157  1.00 16.96 ?  70  ALA   A HB2  1 
ATOM   1498 H  HB3  . ALA   A 1 70  ? 41.509 8.217   0.933   1.00 16.96 ?  70  ALA   A HB3  1 
ATOM   1499 N  N    . THR   A 1 71  ? 42.284 5.340   0.288   1.00 13.01 ?  71  THR   A N    1 
ATOM   1500 C  CA   . THR   A 1 71  ? 43.337 4.363   0.532   1.00 14.56 ?  71  THR   A CA   1 
ATOM   1501 C  C    . THR   A 1 71  ? 43.212 3.140   -0.370  1.00 14.60 ?  71  THR   A C    1 
ATOM   1502 O  O    . THR   A 1 71  ? 44.220 2.631   -0.879  1.00 16.30 ?  71  THR   A O    1 
ATOM   1503 C  CB   . THR   A 1 71  ? 43.269 3.912   1.985   1.00 16.19 ?  71  THR   A CB   1 
ATOM   1504 O  OG1  . THR   A 1 71  ? 43.514 5.033   2.840   1.00 17.37 ?  71  THR   A OG1  1 
ATOM   1505 C  CG2  . THR   A 1 71  ? 44.285 2.819   2.263   1.00 17.82 ?  71  THR   A CG2  1 
ATOM   1506 H  H    . THR   A 1 71  ? 41.612 5.280   0.820   1.00 15.62 ?  71  THR   A H    1 
ATOM   1507 H  HA   . THR   A 1 71  ? 44.199 4.773   0.373   1.00 17.48 ?  71  THR   A HA   1 
ATOM   1508 H  HB   . THR   A 1 71  ? 42.382 3.550   2.162   1.00 19.43 ?  71  THR   A HB   1 
ATOM   1509 H  HG1  . THR   A 1 71  ? 43.465 4.783   3.644   1.00 20.84 ?  71  THR   A HG1  1 
ATOM   1510 H  HG21 . THR   A 1 71  ? 44.427 2.738   3.219   1.00 21.38 ?  71  THR   A HG21 1 
ATOM   1511 H  HG22 . THR   A 1 71  ? 43.973 1.968   1.919   1.00 21.38 ?  71  THR   A HG22 1 
ATOM   1512 H  HG23 . THR   A 1 71  ? 45.132 3.040   1.840   1.00 21.38 ?  71  THR   A HG23 1 
ATOM   1513 N  N    . ASN   A 1 72  ? 41.987 2.641   -0.556  1.00 13.45 ?  72  ASN   A N    1 
ATOM   1514 C  CA   . ASN   A 1 72  ? 41.759 1.314   -1.110  1.00 13.64 ?  72  ASN   A CA   1 
ATOM   1515 C  C    . ASN   A 1 72  ? 41.136 1.297   -2.493  1.00 13.54 ?  72  ASN   A C    1 
ATOM   1516 O  O    . ASN   A 1 72  ? 41.148 0.238   -3.137  1.00 15.04 ?  72  ASN   A O    1 
ATOM   1517 C  CB   . ASN   A 1 72  ? 40.868 0.501   -0.163  1.00 14.18 ?  72  ASN   A CB   1 
ATOM   1518 C  CG   . ASN   A 1 72  ? 41.491 0.338   1.195   1.00 15.49 ?  72  ASN   A CG   1 
ATOM   1519 O  OD1  . ASN   A 1 72  ? 41.052 0.944   2.170   1.00 17.20 ?  72  ASN   A OD1  1 
ATOM   1520 N  ND2  . ASN   A 1 72  ? 42.537 -0.463  1.265   1.00 16.02 ?  72  ASN   A ND2  1 
ATOM   1521 H  H    . ASN   A 1 72  ? 41.263 3.067   -0.371  1.00 16.14 ?  72  ASN   A H    1 
ATOM   1522 H  HA   . ASN   A 1 72  ? 42.611 0.862   -1.179  1.00 16.37 ?  72  ASN   A HA   1 
ATOM   1523 H  HB2  . ASN   A 1 72  ? 40.022 0.956   -0.055  1.00 17.01 ?  72  ASN   A HB2  1 
ATOM   1524 H  HB3  . ASN   A 1 72  ? 40.734 -0.381  -0.540  1.00 17.01 ?  72  ASN   A HB3  1 
ATOM   1525 H  HD21 . ASN   A 1 72  ? 42.935 -0.584  2.019   1.00 19.22 ?  72  ASN   A HD21 1 
ATOM   1526 H  HD22 . ASN   A 1 72  ? 42.823 -0.865  0.561   1.00 19.22 ?  72  ASN   A HD22 1 
ATOM   1527 N  N    . GLY   A 1 73  ? 40.585 2.410   -2.960  1.00 13.34 ?  73  GLY   A N    1 
ATOM   1528 C  CA   . GLY   A 1 73  ? 39.852 2.417   -4.199  1.00 13.22 ?  73  GLY   A CA   1 
ATOM   1529 C  C    . GLY   A 1 73  ? 38.456 1.849   -4.024  1.00 12.69 ?  73  GLY   A C    1 
ATOM   1530 O  O    . GLY   A 1 73  ? 38.071 1.387   -2.945  1.00 13.22 ?  73  GLY   A O    1 
ATOM   1531 H  H    . GLY   A 1 73  ? 40.626 3.186   -2.576  1.00 16.01 ?  73  GLY   A H    1 
ATOM   1532 H  HA2  . GLY   A 1 73  ? 39.786 3.329   -4.533  1.00 15.86 ?  73  GLY   A HA2  1 
ATOM   1533 H  HA3  . GLY   A 1 73  ? 40.325 1.886   -4.863  1.00 15.86 ?  73  GLY   A HA3  1 
ATOM   1534 N  N    . PRO   A 1 74  ? 37.681 1.870   -5.105  1.00 13.21 ?  74  PRO   A N    1 
ATOM   1535 C  CA   . PRO   A 1 74  ? 36.284 1.444   -5.026  1.00 13.19 ?  74  PRO   A CA   1 
ATOM   1536 C  C    . PRO   A 1 74  ? 36.131 -0.036  -4.713  1.00 12.65 ?  74  PRO   A C    1 
ATOM   1537 O  O    . PRO   A 1 74  ? 36.998 -0.869  -5.002  1.00 13.38 ?  74  PRO   A O    1 
ATOM   1538 C  CB   . PRO   A 1 74  ? 35.743 1.757   -6.426  1.00 14.74 ?  74  PRO   A CB   1 
ATOM   1539 C  CG   . PRO   A 1 74  ? 36.693 2.743   -7.017  1.00 17.55 ?  74  PRO   A CG   1 
ATOM   1540 C  CD   . PRO   A 1 74  ? 38.027 2.398   -6.434  1.00 15.16 ?  74  PRO   A CD   1 
ATOM   1541 H  HA   . PRO   A 1 74  ? 35.805 1.970   -4.366  1.00 15.83 ?  74  PRO   A HA   1 
ATOM   1542 H  HB2  . PRO   A 1 74  ? 35.718 0.945   -6.953  1.00 17.69 ?  74  PRO   A HB2  1 
ATOM   1543 H  HB3  . PRO   A 1 74  ? 34.855 2.143   -6.350  1.00 17.69 ?  74  PRO   A HB3  1 
ATOM   1544 H  HG2  . PRO   A 1 74  ? 36.706 2.646   -7.982  1.00 21.06 ?  74  PRO   A HG2  1 
ATOM   1545 H  HG3  . PRO   A 1 74  ? 36.432 3.642   -6.765  1.00 21.06 ?  74  PRO   A HG3  1 
ATOM   1546 H  HD2  . PRO   A 1 74  ? 38.468 1.717   -6.969  1.00 18.19 ?  74  PRO   A HD2  1 
ATOM   1547 H  HD3  . PRO   A 1 74  ? 38.574 3.200   -6.365  1.00 18.19 ?  74  PRO   A HD3  1 
ATOM   1548 N  N    . LEU   A 1 75  ? 34.984 -0.355  -4.123  1.00 12.07 ?  75  LEU   A N    1 
ATOM   1549 C  CA   . LEU   A 1 75  ? 34.575 -1.743  -3.974  1.00 11.67 ?  75  LEU   A CA   1 
ATOM   1550 C  C    . LEU   A 1 75  ? 34.183 -2.319  -5.335  1.00 12.30 ?  75  LEU   A C    1 
ATOM   1551 O  O    . LEU   A 1 75  ? 34.069 -1.606  -6.336  1.00 13.42 ?  75  LEU   A O    1 
ATOM   1552 C  CB   . LEU   A 1 75  ? 33.392 -1.861  -3.011  1.00 12.00 ?  75  LEU   A CB   1 
ATOM   1553 C  CG   . LEU   A 1 75  ? 33.596 -1.425  -1.561  1.00 13.31 ?  75  LEU   A CG   1 
ATOM   1554 C  CD1  . LEU   A 1 75  ? 32.301 -1.587  -0.768  1.00 15.33 ?  75  LEU   A CD1  1 
ATOM   1555 C  CD2  . LEU   A 1 75  ? 34.731 -2.149  -0.887  1.00 16.41 ?  75  LEU   A CD2  1 
ATOM   1556 H  H    . LEU   A 1 75  ? 34.426 0.217   -3.806  1.00 14.49 ?  75  LEU   A H    1 
ATOM   1557 H  HA   . LEU   A 1 75  ? 35.314 -2.260  -3.629  1.00 14.00 ?  75  LEU   A HA   1 
ATOM   1558 H  HB2  . LEU   A 1 75  ? 32.665 -1.329  -3.363  1.00 14.40 ?  75  LEU   A HB2  1 
ATOM   1559 H  HB3  . LEU   A 1 75  ? 33.123 -2.793  -2.988  1.00 14.40 ?  75  LEU   A HB3  1 
ATOM   1560 H  HG   . LEU   A 1 75  ? 33.826 -0.481  -1.557  1.00 15.97 ?  75  LEU   A HG   1 
ATOM   1561 H  HD11 . LEU   A 1 75  ? 32.457 -1.302  0.148   1.00 18.40 ?  75  LEU   A HD11 1 
ATOM   1562 H  HD12 . LEU   A 1 75  ? 31.618 -1.033  -1.175  1.00 18.40 ?  75  LEU   A HD12 1 
ATOM   1563 H  HD13 . LEU   A 1 75  ? 32.036 -2.516  -0.787  1.00 18.40 ?  75  LEU   A HD13 1 
ATOM   1564 H  HD21 . LEU   A 1 75  ? 34.795 -1.851  0.035   1.00 19.69 ?  75  LEU   A HD21 1 
ATOM   1565 H  HD22 . LEU   A 1 75  ? 34.562 -3.102  -0.916  1.00 19.69 ?  75  LEU   A HD22 1 
ATOM   1566 H  HD23 . LEU   A 1 75  ? 35.561 -1.946  -1.353  1.00 19.69 ?  75  LEU   A HD23 1 
ATOM   1567 N  N    . LYS   A 1 76  ? 33.986 -3.638  -5.355  1.00 12.52 ?  76  LYS   A N    1 
ATOM   1568 C  CA   . LYS   A 1 76  ? 33.382 -4.346  -6.478  1.00 13.41 ?  76  LYS   A CA   1 
ATOM   1569 C  C    . LYS   A 1 76  ? 31.870 -4.422  -6.281  1.00 11.77 ?  76  LYS   A C    1 
ATOM   1570 O  O    . LYS   A 1 76  ? 31.387 -4.550  -5.158  1.00 11.76 ?  76  LYS   A O    1 
ATOM   1571 C  CB   . LYS   A 1 76  ? 33.916 -5.790  -6.544  1.00 15.37 ?  76  LYS   A CB   1 
ATOM   1572 C  CG   . LYS   A 1 76  ? 35.422 -5.903  -6.703  1.00 17.10 ?  76  LYS   A CG   1 
ATOM   1573 C  CD   . LYS   A 1 76  ? 35.932 -7.308  -6.519  1.00 18.64 ?  76  LYS   A CD   1 
ATOM   1574 C  CE   . LYS   A 1 76  ? 37.419 -7.370  -6.754  1.00 21.23 ?  76  LYS   A CE   1 
ATOM   1575 N  NZ   . LYS   A 1 76  ? 37.956 -8.715  -6.486  1.00 22.12 ?  76  LYS   A NZ   1 
ATOM   1576 H  H    . LYS   A 1 76  ? 34.204 -4.157  -4.703  1.00 15.02 ?  76  LYS   A H    1 
ATOM   1577 H  HA   . LYS   A 1 76  ? 33.579 -3.887  -7.310  1.00 16.09 ?  76  LYS   A HA   1 
ATOM   1578 H  HB2  . LYS   A 1 76  ? 33.667 -6.243  -5.722  1.00 18.45 ?  76  LYS   A HB2  1 
ATOM   1579 H  HB3  . LYS   A 1 76  ? 33.502 -6.232  -7.300  1.00 18.45 ?  76  LYS   A HB3  1 
ATOM   1580 H  HG2  . LYS   A 1 76  ? 35.665 -5.606  -7.592  1.00 20.51 ?  76  LYS   A HG2  1 
ATOM   1581 H  HG3  . LYS   A 1 76  ? 35.850 -5.340  -6.037  1.00 20.51 ?  76  LYS   A HG3  1 
ATOM   1582 H  HD2  . LYS   A 1 76  ? 35.747 -7.603  -5.614  1.00 22.36 ?  76  LYS   A HD2  1 
ATOM   1583 H  HD3  . LYS   A 1 76  ? 35.493 -7.893  -7.160  1.00 22.36 ?  76  LYS   A HD3  1 
ATOM   1584 H  HE2  . LYS   A 1 76  ? 37.603 -7.143  -7.678  1.00 25.47 ?  76  LYS   A HE2  1 
ATOM   1585 H  HE3  . LYS   A 1 76  ? 37.857 -6.742  -6.159  1.00 25.47 ?  76  LYS   A HE3  1 
ATOM   1586 H  HZ1  . LYS   A 1 76  ? 38.831 -8.728  -6.631  1.00 26.55 ?  76  LYS   A HZ1  1 
ATOM   1587 H  HZ2  . LYS   A 1 76  ? 37.796 -8.946  -5.641  1.00 26.55 ?  76  LYS   A HZ2  1 
ATOM   1588 H  HZ3  . LYS   A 1 76  ? 37.564 -9.311  -7.024  1.00 26.55 ?  76  LYS   A HZ3  1 
ATOM   1589 N  N    . VAL   A 1 77  ? 31.118 -4.387  -7.385  1.00 12.37 ?  77  VAL   A N    1 
ATOM   1590 C  CA   . VAL   A 1 77  ? 29.712 -4.774  -7.299  1.00 12.30 ?  77  VAL   A CA   1 
ATOM   1591 C  C    . VAL   A 1 77  ? 29.645 -6.230  -6.862  1.00 11.97 ?  77  VAL   A C    1 
ATOM   1592 O  O    . VAL   A 1 77  ? 30.304 -7.096  -7.447  1.00 12.41 ?  77  VAL   A O    1 
ATOM   1593 C  CB   . VAL   A 1 77  ? 28.983 -4.544  -8.631  1.00 13.44 ?  77  VAL   A CB   1 
ATOM   1594 C  CG1  . VAL   A 1 77  ? 27.517 -4.975  -8.520  1.00 14.17 ?  77  VAL   A CG1  1 
ATOM   1595 C  CG2  . VAL   A 1 77  ? 29.070 -3.081  -9.046  1.00 15.07 ?  77  VAL   A CG2  1 
ATOM   1596 H  H    . VAL   A 1 77  ? 31.396 -4.148  -8.165  1.00 14.85 ?  77  VAL   A H    1 
ATOM   1597 H  HA   . VAL   A 1 77  ? 29.280 -4.235  -6.619  1.00 14.76 ?  77  VAL   A HA   1 
ATOM   1598 H  HB   . VAL   A 1 77  ? 29.407 -5.077  -9.320  1.00 16.12 ?  77  VAL   A HB   1 
ATOM   1599 H  HG11 . VAL   A 1 77  ? 27.042 -4.677  -9.310  1.00 17.01 ?  77  VAL   A HG11 1 
ATOM   1600 H  HG12 . VAL   A 1 77  ? 27.475 -5.941  -8.451  1.00 17.01 ?  77  VAL   A HG12 1 
ATOM   1601 H  HG13 . VAL   A 1 77  ? 27.129 -4.568  -7.728  1.00 17.01 ?  77  VAL   A HG13 1 
ATOM   1602 H  HG21 . VAL   A 1 77  ? 28.560 -2.956  -9.861  1.00 18.09 ?  77  VAL   A HG21 1 
ATOM   1603 H  HG22 . VAL   A 1 77  ? 28.703 -2.529  -8.338  1.00 18.09 ?  77  VAL   A HG22 1 
ATOM   1604 H  HG23 . VAL   A 1 77  ? 29.999 -2.848  -9.198  1.00 18.09 ?  77  VAL   A HG23 1 
ATOM   1605 N  N    . GLY   A 1 78  ? 28.855 -6.503  -5.823  1.00 11.54 ?  78  GLY   A N    1 
ATOM   1606 C  CA   . GLY   A 1 78  ? 28.829 -7.792  -5.164  1.00 11.76 ?  78  GLY   A CA   1 
ATOM   1607 C  C    . GLY   A 1 78  ? 29.747 -7.889  -3.966  1.00 11.24 ?  78  GLY   A C    1 
ATOM   1608 O  O    . GLY   A 1 78  ? 29.688 -8.895  -3.242  1.00 11.97 ?  78  GLY   A O    1 
ATOM   1609 H  H    . GLY   A 1 78  ? 28.298 -5.934  -5.487  1.00 13.84 ?  78  GLY   A H    1 
ATOM   1610 H  HA2  . GLY   A 1 78  ? 27.925 -7.979  -4.870  1.00 14.11 ?  78  GLY   A HA2  1 
ATOM   1611 H  HA3  . GLY   A 1 78  ? 29.086 -8.477  -5.803  1.00 14.11 ?  78  GLY   A HA3  1 
ATOM   1612 N  N    . GLY   A 1 79  ? 30.597 -6.881  -3.744  1.00 11.38 ?  79  GLY   A N    1 
ATOM   1613 C  CA   . GLY   A 1 79  ? 31.566 -6.899  -2.674  1.00 11.66 ?  79  GLY   A CA   1 
ATOM   1614 C  C    . GLY   A 1 79  ? 31.128 -6.106  -1.458  1.00 11.05 ?  79  GLY   A C    1 
ATOM   1615 O  O    . GLY   A 1 79  ? 30.008 -5.598  -1.373  1.00 11.79 ?  79  GLY   A O    1 
ATOM   1616 H  H    . GLY   A 1 79  ? 30.627 -6.163  -4.221  1.00 13.66 ?  79  GLY   A H    1 
ATOM   1617 H  HA2  . GLY   A 1 79  ? 31.719 -7.820  -2.401  1.00 13.99 ?  79  GLY   A HA2  1 
ATOM   1618 H  HA3  . GLY   A 1 79  ? 32.402 -6.534  -2.992  1.00 13.99 ?  79  GLY   A HA3  1 
ATOM   1619 N  N    . SER   A 1 80  ? 32.043 -6.013  -0.493  1.00 11.76 ?  80  SER   A N    1 
ATOM   1620 C  CA   . SER   A 1 80  ? 31.733 -5.387  0.782   1.00 11.27 ?  80  SER   A CA   1 
ATOM   1621 C  C    . SER   A 1 80  ? 33.008 -4.942  1.476   1.00 11.23 ?  80  SER   A C    1 
ATOM   1622 O  O    . SER   A 1 80  ? 34.115 -5.379  1.143   1.00 12.57 ?  80  SER   A O    1 
ATOM   1623 C  CB   . SER   A 1 80  ? 30.970 -6.351  1.699   1.00 12.49 ?  80  SER   A CB   1 
ATOM   1624 O  OG   . SER   A 1 80  ? 31.804 -7.397  2.175   1.00 13.95 ?  80  SER   A OG   1 
ATOM   1625 H  H    . SER   A 1 80  ? 32.852 -6.305  -0.558  1.00 14.11 ?  80  SER   A H    1 
ATOM   1626 H  HA   . SER   A 1 80  ? 31.183 -4.610  0.611   1.00 13.53 ?  80  SER   A HA   1 
ATOM   1627 H  HB2  . SER   A 1 80  ? 30.625 -5.852  2.455   1.00 14.98 ?  80  SER   A HB2  1 
ATOM   1628 H  HB3  . SER   A 1 80  ? 30.233 -6.738  1.198   1.00 14.98 ?  80  SER   A HB3  1 
ATOM   1629 H  HG   . SER   A 1 80  ? 32.106 -7.836  1.527   1.00 16.74 ?  80  SER   A HG   1 
ATOM   1630 N  N    . CYS   A 1 81  ? 32.826 -4.093  2.484   1.00 10.88 ?  81  CYS   A N    1 
ATOM   1631 C  CA   . CYS   A 1 81  ? 33.882 -3.820  3.445   1.00 11.16 ?  81  CYS   A CA   1 
ATOM   1632 C  C    . CYS   A 1 81  ? 33.242 -3.587  4.806   1.00 11.08 ?  81  CYS   A C    1 
ATOM   1633 O  O    . CYS   A 1 81  ? 32.077 -3.186  4.901   1.00 12.27 ?  81  CYS   A O    1 
ATOM   1634 C  CB   . CYS   A 1 81  ? 34.759 -2.630  3.027   1.00 11.79 ?  81  CYS   A CB   1 
ATOM   1635 S  SG   . CYS   A 1 81  ? 33.871 -1.050  3.057   1.00 11.76 ?  81  CYS   A SG   1 
ATOM   1636 H  H    . CYS   A 1 81  ? 32.093 -3.659  2.635   1.00 13.05 ?  81  CYS   A H    1 
ATOM   1637 H  HA   . CYS   A 1 81  ? 34.450 -4.602  3.513   1.00 13.39 ?  81  CYS   A HA   1 
ATOM   1638 H  HB2  . CYS   A 1 81  ? 35.517 -2.574  3.636   1.00 14.15 ?  81  CYS   A HB2  1 
ATOM   1639 H  HB3  . CYS   A 1 81  ? 35.085 -2.788  2.122   1.00 14.15 ?  81  CYS   A HB3  1 
ATOM   1640 H  HG   . CYS   A 1 81  ? 34.622 -0.172  2.719   1.00 14.12 ?  81  CYS   A HG   1 
ATOM   1641 N  N    . VAL   A 1 82  ? 34.016 -3.846  5.858   1.00 11.33 ?  82  VAL   A N    1 
ATOM   1642 C  CA   . VAL   A 1 82  ? 33.592 -3.601  7.231   1.00 11.80 ?  82  VAL   A CA   1 
ATOM   1643 C  C    . VAL   A 1 82  ? 34.198 -2.288  7.700   1.00 11.86 ?  82  VAL   A C    1 
ATOM   1644 O  O    . VAL   A 1 82  ? 35.423 -2.121  7.683   1.00 12.76 ?  82  VAL   A O    1 
ATOM   1645 C  CB   . VAL   A 1 82  ? 34.017 -4.742  8.167   1.00 13.19 ?  82  VAL   A CB   1 
ATOM   1646 C  CG1  . VAL   A 1 82  ? 33.571 -4.440  9.591   1.00 14.68 ?  82  VAL   A CG1  1 
ATOM   1647 C  CG2  . VAL   A 1 82  ? 33.460 -6.070  7.689   1.00 14.17 ?  82  VAL   A CG2  1 
ATOM   1648 H  H    . VAL   A 1 82  ? 34.812 -4.188  5.799   1.00 13.60 ?  82  VAL   A H    1 
ATOM   1649 H  HA   . VAL   A 1 82  ? 32.625 -3.523  7.258   1.00 14.16 ?  82  VAL   A HA   1 
ATOM   1650 H  HB   . VAL   A 1 82  ? 34.981 -4.803  8.169   1.00 15.83 ?  82  VAL   A HB   1 
ATOM   1651 H  HG11 . VAL   A 1 82  ? 33.645 -5.248  10.124  1.00 17.62 ?  82  VAL   A HG11 1 
ATOM   1652 H  HG12 . VAL   A 1 82  ? 34.136 -3.746  9.966   1.00 17.62 ?  82  VAL   A HG12 1 
ATOM   1653 H  HG13 . VAL   A 1 82  ? 32.645 -4.141  9.580   1.00 17.62 ?  82  VAL   A HG13 1 
ATOM   1654 H  HG21 . VAL   A 1 82  ? 33.700 -6.761  8.328   1.00 17.01 ?  82  VAL   A HG21 1 
ATOM   1655 H  HG22 . VAL   A 1 82  ? 32.495 -6.005  7.622   1.00 17.01 ?  82  VAL   A HG22 1 
ATOM   1656 H  HG23 . VAL   A 1 82  ? 33.840 -6.277  6.822   1.00 17.01 ?  82  VAL   A HG23 1 
ATOM   1657 N  N    . LEU   A 1 83  ? 33.346 -1.360  8.121   1.00 11.37 ?  83  LEU   A N    1 
ATOM   1658 C  CA   . LEU   A 1 83  ? 33.770 -0.099  8.706   1.00 11.35 ?  83  LEU   A CA   1 
ATOM   1659 C  C    . LEU   A 1 83  ? 33.056 0.078   10.042  1.00 11.55 ?  83  LEU   A C    1 
ATOM   1660 O  O    . LEU   A 1 83  ? 32.341 -0.815  10.512  1.00 12.16 ?  83  LEU   A O    1 
ATOM   1661 C  CB   . LEU   A 1 83  ? 33.517 1.062   7.736   1.00 11.90 ?  83  LEU   A CB   1 
ATOM   1662 C  CG   . LEU   A 1 83  ? 34.415 1.051   6.495   1.00 12.56 ?  83  LEU   A CG   1 
ATOM   1663 C  CD1  . LEU   A 1 83  ? 33.988 2.097   5.482   1.00 13.39 ?  83  LEU   A CD1  1 
ATOM   1664 C  CD2  . LEU   A 1 83  ? 35.883 1.272   6.890   1.00 13.44 ?  83  LEU   A CD2  1 
ATOM   1665 H  H    . LEU   A 1 83  ? 32.492 -1.446  8.073   1.00 13.65 ?  83  LEU   A H    1 
ATOM   1666 H  HA   . LEU   A 1 83  ? 34.722 -0.138  8.883   1.00 13.62 ?  83  LEU   A HA   1 
ATOM   1667 H  HB2  . LEU   A 1 83  ? 32.600 1.020   7.426   1.00 14.28 ?  83  LEU   A HB2  1 
ATOM   1668 H  HB3  . LEU   A 1 83  ? 33.669 1.899   8.199   1.00 14.28 ?  83  LEU   A HB3  1 
ATOM   1669 H  HG   . LEU   A 1 83  ? 34.359 0.181   6.073   1.00 15.07 ?  83  LEU   A HG   1 
ATOM   1670 H  HD11 . LEU   A 1 83  ? 34.583 2.048   4.713   1.00 16.07 ?  83  LEU   A HD11 1 
ATOM   1671 H  HD12 . LEU   A 1 83  ? 33.080 1.909   5.208   1.00 16.07 ?  83  LEU   A HD12 1 
ATOM   1672 H  HD13 . LEU   A 1 83  ? 34.045 2.972   5.889   1.00 16.07 ?  83  LEU   A HD13 1 
ATOM   1673 H  HD21 . LEU   A 1 83  ? 36.406 1.444   6.088   1.00 16.13 ?  83  LEU   A HD21 1 
ATOM   1674 H  HD22 . LEU   A 1 83  ? 35.941 2.035   7.488   1.00 16.13 ?  83  LEU   A HD22 1 
ATOM   1675 H  HD23 . LEU   A 1 83  ? 36.220 0.479   7.336   1.00 16.13 ?  83  LEU   A HD23 1 
ATOM   1676 N  N    . SER   A 1 84  ? 33.269 1.225   10.675  1.00 12.10 ?  84  SER   A N    1 
ATOM   1677 C  CA   . SER   A 1 84  ? 32.634 1.481   11.957  1.00 12.49 ?  84  SER   A CA   1 
ATOM   1678 C  C    . SER   A 1 84  ? 31.113 1.568   11.819  1.00 12.43 ?  84  SER   A C    1 
ATOM   1679 O  O    . SER   A 1 84  ? 30.584 2.038   10.812  1.00 12.41 ?  84  SER   A O    1 
ATOM   1680 C  CB   . SER   A 1 84  ? 33.146 2.795   12.535  1.00 13.41 ?  84  SER   A CB   1 
ATOM   1681 O  OG   . SER   A 1 84  ? 32.515 3.074   13.767  1.00 14.36 ?  84  SER   A OG   1 
ATOM   1682 H  H    . SER   A 1 84  ? 33.777 1.864   10.381  1.00 14.53 ?  84  SER   A H    1 
ATOM   1683 H  HA   . SER   A 1 84  ? 32.858 0.767   12.569  1.00 14.99 ?  84  SER   A HA   1 
ATOM   1684 H  HB2  . SER   A 1 84  ? 34.110 2.732   12.670  1.00 16.09 ?  84  SER   A HB2  1 
ATOM   1685 H  HB3  . SER   A 1 84  ? 32.955 3.516   11.909  1.00 16.09 ?  84  SER   A HB3  1 
ATOM   1686 H  HG   . SER   A 1 84  ? 32.809 3.798   14.081  1.00 17.24 ?  84  SER   A HG   1 
ATOM   1687 N  N    . GLY   A 1 85  ? 30.412 1.148   12.869  1.00 13.39 ?  85  GLY   A N    1 
ATOM   1688 C  CA   . GLY   A 1 85  ? 28.992 1.393   12.969  1.00 13.78 ?  85  GLY   A CA   1 
ATOM   1689 C  C    . GLY   A 1 85  ? 28.639 2.708   13.620  1.00 13.58 ?  85  GLY   A C    1 
ATOM   1690 O  O    . GLY   A 1 85  ? 27.451 3.027   13.745  1.00 14.18 ?  85  GLY   A O    1 
ATOM   1691 H  H    . GLY   A 1 85  ? 30.752 0.723   13.539  1.00 16.06 ?  85  GLY   A H    1 
ATOM   1692 H  HA2  . GLY   A 1 85  ? 28.612 1.383   12.077  1.00 16.54 ?  85  GLY   A HA2  1 
ATOM   1693 H  HA3  . GLY   A 1 85  ? 28.586 0.682   13.480  1.00 16.54 ?  85  GLY   A HA3  1 
ATOM   1694 N  N    . HIS   A 1 86  ? 29.637 3.474   14.053  1.00 13.21 ?  86  HIS   A N    1 
ATOM   1695 C  CA   . HIS   A 1 86  ? 29.434 4.807   14.630  1.00 13.82 ?  86  HIS   A CA   1 
ATOM   1696 C  C    . HIS   A 1 86  ? 28.458 4.694   15.793  1.00 14.66 ?  86  HIS   A C    1 
ATOM   1697 O  O    . HIS   A 1 86  ? 28.631 3.809   16.647  1.00 15.55 ?  86  HIS   A O    1 
ATOM   1698 C  CB   . HIS   A 1 86  ? 29.052 5.795   13.538  1.00 13.63 ?  86  HIS   A CB   1 
ATOM   1699 C  CG   . HIS   A 1 86  ? 30.096 5.898   12.490  1.00 13.48 ?  86  HIS   A CG   1 
ATOM   1700 N  ND1  . HIS   A 1 86  ? 31.188 6.726   12.618  1.00 14.53 ?  86  HIS   A ND1  1 
ATOM   1701 C  CD2  . HIS   A 1 86  ? 30.264 5.218   11.335  1.00 12.96 ?  86  HIS   A CD2  1 
ATOM   1702 C  CE1  . HIS   A 1 86  ? 31.968 6.575   11.564  1.00 14.12 ?  86  HIS   A CE1  1 
ATOM   1703 N  NE2  . HIS   A 1 86  ? 31.440 5.652   10.781  1.00 13.34 ?  86  HIS   A NE2  1 
ATOM   1704 H  H    . HIS   A 1 86  ? 30.461 3.237   14.040  1.00 15.85 ?  86  HIS   A H    1 
ATOM   1705 H  HA   . HIS   A 1 86  ? 30.278 5.109   15.001  1.00 16.59 ?  86  HIS   A HA   1 
ATOM   1706 H  HB2  . HIS   A 1 86  ? 28.226 5.507   13.119  1.00 16.36 ?  86  HIS   A HB2  1 
ATOM   1707 H  HB3  . HIS   A 1 86  ? 28.931 6.678   13.931  1.00 16.36 ?  86  HIS   A HB3  1 
ATOM   1708 H  HD2  . HIS   A 1 86  ? 29.699 4.563   10.988  1.00 15.55 ?  86  HIS   A HD2  1 
ATOM   1709 H  HE1  . HIS   A 1 86  ? 32.761 7.032   11.397  1.00 16.95 ?  86  HIS   A HE1  1 
ATOM   1710 H  HE2  . HIS   A 1 86  ? 31.768 5.384   10.025  1.00 16.01 ?  86  HIS   A HE2  1 
ATOM   1711 N  N    A ASN   A 1 87  ? 27.439 5.543   15.863  0.56 15.53 ?  87  ASN   A N    1 
ATOM   1712 N  N    B ASN   A 1 87  ? 27.458 5.557   15.886  0.44 15.27 ?  87  ASN   A N    1 
ATOM   1713 C  CA   A ASN   A 1 87  ? 26.449 5.552   16.926  0.56 16.19 ?  87  ASN   A CA   1 
ATOM   1714 C  CA   B ASN   A 1 87  ? 26.524 5.537   16.998  0.44 15.84 ?  87  ASN   A CA   1 
ATOM   1715 C  C    A ASN   A 1 87  ? 25.286 4.605   16.660  0.56 16.67 ?  87  ASN   A C    1 
ATOM   1716 C  C    B ASN   A 1 87  ? 25.429 4.493   16.835  0.44 15.92 ?  87  ASN   A C    1 
ATOM   1717 O  O    A ASN   A 1 87  ? 24.304 4.628   17.407  0.56 18.09 ?  87  ASN   A O    1 
ATOM   1718 O  O    B ASN   A 1 87  ? 24.645 4.300   17.769  0.44 16.25 ?  87  ASN   A O    1 
ATOM   1719 C  CB   A ASN   A 1 87  ? 25.893 6.969   17.085  0.56 17.03 ?  87  ASN   A CB   1 
ATOM   1720 C  CB   B ASN   A 1 87  ? 25.912 6.932   17.174  0.44 16.79 ?  87  ASN   A CB   1 
ATOM   1721 C  CG   A ASN   A 1 87  ? 25.310 7.516   15.787  0.56 17.92 ?  87  ASN   A CG   1 
ATOM   1722 C  CG   B ASN   A 1 87  ? 25.455 7.541   15.859  0.44 17.40 ?  87  ASN   A CG   1 
ATOM   1723 O  OD1  A ASN   A 1 87  ? 25.882 7.347   14.711  0.56 18.15 ?  87  ASN   A OD1  1 
ATOM   1724 O  OD1  B ASN   A 1 87  ? 26.160 7.478   14.851  0.44 17.73 ?  87  ASN   A OD1  1 
ATOM   1725 N  ND2  A ASN   A 1 87  ? 24.162 8.163   15.886  0.56 18.86 ?  87  ASN   A ND2  1 
ATOM   1726 N  ND2  B ASN   A 1 87  ? 24.272 8.136   15.864  0.44 18.10 ?  87  ASN   A ND2  1 
ATOM   1727 H  H    A ASN   A 1 87  ? 27.294 6.147   15.276  0.56 18.63 ?  87  ASN   A H    1 
ATOM   1728 H  H    B ASN   A 1 87  ? 27.298 6.167   15.306  0.44 18.33 ?  87  ASN   A H    1 
ATOM   1729 H  HA   A ASN   A 1 87  ? 26.872 5.299   17.765  0.56 19.43 ?  87  ASN   A HA   1 
ATOM   1730 H  HA   B ASN   A 1 87  ? 26.995 5.315   17.812  0.44 19.01 ?  87  ASN   A HA   1 
ATOM   1731 H  HB2  A ASN   A 1 87  ? 25.186 6.958   17.755  0.56 20.44 ?  87  ASN   A HB2  1 
ATOM   1732 H  HB2  B ASN   A 1 87  ? 25.143 6.872   17.763  0.44 20.14 ?  87  ASN   A HB2  1 
ATOM   1733 H  HB3  A ASN   A 1 87  ? 26.607 7.559   17.372  0.56 20.44 ?  87  ASN   A HB3  1 
ATOM   1734 H  HB3  B ASN   A 1 87  ? 26.580 7.520   17.560  0.44 20.14 ?  87  ASN   A HB3  1 
ATOM   1735 H  HD21 A ASN   A 1 87  ? 23.795 8.486   15.182  0.56 22.64 ?  87  ASN   A HD21 1 
ATOM   1736 H  HD21 B ASN   A 1 87  ? 23.968 8.493   15.146  0.44 21.73 ?  87  ASN   A HD21 1 
ATOM   1737 H  HD22 A ASN   A 1 87  ? 23.788 8.260   16.654  0.56 22.64 ?  87  ASN   A HD22 1 
ATOM   1738 H  HD22 B ASN   A 1 87  ? 23.810 8.167   16.591  0.44 21.73 ?  87  ASN   A HD22 1 
ATOM   1739 N  N    A LEU   A 1 88  ? 25.362 3.789   15.610  0.56 16.06 ?  88  LEU   A N    1 
ATOM   1740 N  N    B LEU   A 1 88  ? 25.388 3.785   15.707  0.44 15.67 ?  88  LEU   A N    1 
ATOM   1741 C  CA   A LEU   A 1 88  ? 24.257 2.925   15.211  0.56 16.06 ?  88  LEU   A CA   1 
ATOM   1742 C  CA   B LEU   A 1 88  ? 24.251 2.942   15.354  0.44 15.75 ?  88  LEU   A CA   1 
ATOM   1743 C  C    A LEU   A 1 88  ? 24.472 1.452   15.519  0.56 15.84 ?  88  LEU   A C    1 
ATOM   1744 C  C    B LEU   A 1 88  ? 24.476 1.460   15.623  0.44 15.57 ?  88  LEU   A C    1 
ATOM   1745 O  O    A LEU   A 1 88  ? 23.492 0.726   15.710  0.56 16.47 ?  88  LEU   A O    1 
ATOM   1746 O  O    B LEU   A 1 88  ? 23.509 0.738   15.895  0.44 16.18 ?  88  LEU   A O    1 
ATOM   1747 C  CB   A LEU   A 1 88  ? 24.013 3.059   13.705  0.56 16.50 ?  88  LEU   A CB   1 
ATOM   1748 C  CB   B LEU   A 1 88  ? 23.912 3.131   13.871  0.44 16.04 ?  88  LEU   A CB   1 
ATOM   1749 C  CG   A LEU   A 1 88  ? 23.709 4.462   13.185  0.56 17.83 ?  88  LEU   A CG   1 
ATOM   1750 C  CG   B LEU   A 1 88  ? 23.621 4.565   13.418  0.44 16.95 ?  88  LEU   A CG   1 
ATOM   1751 C  CD1  A LEU   A 1 88  ? 23.552 4.429   11.677  0.56 18.22 ?  88  LEU   A CD1  1 
ATOM   1752 C  CD1  B LEU   A 1 88  ? 23.412 4.616   11.911  0.44 16.96 ?  88  LEU   A CD1  1 
ATOM   1753 C  CD2  A LEU   A 1 88  ? 22.459 5.019   13.849  0.56 19.11 ?  88  LEU   A CD2  1 
ATOM   1754 C  CD2  B LEU   A 1 88  ? 22.413 5.131   14.148  0.44 17.97 ?  88  LEU   A CD2  1 
ATOM   1755 H  H    A LEU   A 1 88  ? 26.049 3.728   15.103  0.56 19.27 ?  88  LEU   A H    1 
ATOM   1756 H  H    B LEU   A 1 88  ? 26.027 3.764   15.131  0.44 18.80 ?  88  LEU   A H    1 
ATOM   1757 H  HA   A LEU   A 1 88  ? 23.452 3.207   15.671  0.56 19.27 ?  88  LEU   A HA   1 
ATOM   1758 H  HA   B LEU   A 1 88  ? 23.481 3.218   15.869  0.44 18.90 ?  88  LEU   A HA   1 
ATOM   1759 H  HB2  A LEU   A 1 88  ? 24.803 2.747   13.240  0.56 19.80 ?  88  LEU   A HB2  1 
ATOM   1760 H  HB2  B LEU   A 1 88  ? 24.657 2.811   13.341  0.44 19.25 ?  88  LEU   A HB2  1 
ATOM   1761 H  HB3  A LEU   A 1 88  ? 23.258 2.498   13.469  0.56 19.80 ?  88  LEU   A HB3  1 
ATOM   1762 H  HB3  B LEU   A 1 88  ? 23.123 2.605   13.669  0.44 19.25 ?  88  LEU   A HB3  1 
ATOM   1763 H  HG   A LEU   A 1 88  ? 24.452 5.048   13.398  0.56 21.39 ?  88  LEU   A HG   1 
ATOM   1764 H  HG   B LEU   A 1 88  ? 24.385 5.124   13.625  0.44 20.34 ?  88  LEU   A HG   1 
ATOM   1765 H  HD11 A LEU   A 1 88  ? 23.404 5.332   11.354  0.56 21.86 ?  88  LEU   A HD11 1 
ATOM   1766 H  HD11 B LEU   A 1 88  ? 23.232 5.532   11.646  0.44 20.36 ?  88  LEU   A HD11 1 
ATOM   1767 H  HD12 A LEU   A 1 88  ? 24.359 4.064   11.282  0.56 21.86 ?  88  LEU   A HD12 1 
ATOM   1768 H  HD12 B LEU   A 1 88  ? 24.215 4.297   11.469  0.44 20.36 ?  88  LEU   A HD12 1 
ATOM   1769 H  HD13 A LEU   A 1 88  ? 22.791 3.869   11.452  0.56 21.86 ?  88  LEU   A HD13 1 
ATOM   1770 H  HD13 B LEU   A 1 88  ? 22.659 4.050   11.676  0.44 20.36 ?  88  LEU   A HD13 1 
ATOM   1771 H  HD21 A LEU   A 1 88  ? 22.224 5.858   13.424  0.56 22.93 ?  88  LEU   A HD21 1 
ATOM   1772 H  HD21 B LEU   A 1 88  ? 22.202 6.003   13.778  0.44 21.57 ?  88  LEU   A HD21 1 
ATOM   1773 H  HD22 A LEU   A 1 88  ? 21.736 4.381   13.745  0.56 22.93 ?  88  LEU   A HD22 1 
ATOM   1774 H  HD22 B LEU   A 1 88  ? 21.662 4.530   14.026  0.44 21.57 ?  88  LEU   A HD22 1 
ATOM   1775 H  HD23 A LEU   A 1 88  ? 22.639 5.164   14.791  0.56 22.93 ?  88  LEU   A HD23 1 
ATOM   1776 H  HD23 B LEU   A 1 88  ? 22.626 5.212   15.089  0.44 21.57 ?  88  LEU   A HD23 1 
ATOM   1777 N  N    . ALA   A 1 89  ? 25.721 0.999   15.555  1.00 15.07 ?  89  ALA   A N    1 
ATOM   1778 C  CA   . ALA   A 1 89  ? 26.050 -0.413  15.665  1.00 14.73 ?  89  ALA   A CA   1 
ATOM   1779 C  C    . ALA   A 1 89  ? 27.539 -0.491  15.959  1.00 15.06 ?  89  ALA   A C    1 
ATOM   1780 O  O    . ALA   A 1 89  ? 28.256 0.499   15.825  1.00 15.90 ?  89  ALA   A O    1 
ATOM   1781 C  CB   . ALA   A 1 89  ? 25.747 -1.129  14.351  1.00 14.27 ?  89  ALA   A CB   1 
ATOM   1782 H  H    A ALA   A 1 89  ? 26.415 1.509   15.504  0.56 18.08 ?  89  ALA   A H    1 
ATOM   1783 H  H    B ALA   A 1 89  ? 26.411 1.503   15.439  0.44 18.08 ?  89  ALA   A H    1 
ATOM   1784 H  HA   . ALA   A 1 89  ? 25.551 -0.821  16.390  1.00 17.68 ?  89  ALA   A HA   1 
ATOM   1785 H  HB1  . ALA   A 1 89  ? 25.991 -2.065  14.440  1.00 17.12 ?  89  ALA   A HB1  1 
ATOM   1786 H  HB2  . ALA   A 1 89  ? 24.797 -1.055  14.161  1.00 17.12 ?  89  ALA   A HB2  1 
ATOM   1787 H  HB3  . ALA   A 1 89  ? 26.260 -0.719  13.641  1.00 17.12 ?  89  ALA   A HB3  1 
ATOM   1788 N  N    . LYS   A 1 90  ? 28.012 -1.668  16.358  1.00 15.73 ?  90  LYS   A N    1 
ATOM   1789 C  CA   . LYS   A 1 90  ? 29.455 -1.834  16.490  1.00 16.66 ?  90  LYS   A CA   1 
ATOM   1790 C  C    . LYS   A 1 90  ? 30.143 -1.641  15.142  1.00 15.38 ?  90  LYS   A C    1 
ATOM   1791 O  O    . LYS   A 1 90  ? 31.084 -0.841  15.012  1.00 16.65 ?  90  LYS   A O    1 
ATOM   1792 C  CB   . LYS   A 1 90  ? 29.781 -3.204  17.085  1.00 19.20 ?  90  LYS   A CB   1 
ATOM   1793 C  CG   . LYS   A 1 90  ? 31.252 -3.359  17.438  1.00 23.56 ?  90  LYS   A CG   1 
ATOM   1794 C  CD   . LYS   A 1 90  ? 31.485 -4.571  18.322  1.00 27.88 ?  90  LYS   A CD   1 
ATOM   1795 C  CE   . LYS   A 1 90  ? 32.908 -4.615  18.853  1.00 31.58 ?  90  LYS   A CE   1 
ATOM   1796 N  NZ   . LYS   A 1 90  ? 33.898 -4.948  17.794  1.00 33.63 ?  90  LYS   A NZ   1 
ATOM   1797 H  H    . LYS   A 1 90  ? 27.534 -2.353  16.557  1.00 18.88 ?  90  LYS   A H    1 
ATOM   1798 H  HA   . LYS   A 1 90  ? 29.793 -1.159  17.096  1.00 19.99 ?  90  LYS   A HA   1 
ATOM   1799 H  HB2  . LYS   A 1 90  ? 29.262 -3.329  17.896  1.00 23.03 ?  90  LYS   A HB2  1 
ATOM   1800 H  HB3  . LYS   A 1 90  ? 29.553 -3.892  16.439  1.00 23.03 ?  90  LYS   A HB3  1 
ATOM   1801 H  HG2  . LYS   A 1 90  ? 31.768 -3.473  16.624  1.00 28.27 ?  90  LYS   A HG2  1 
ATOM   1802 H  HG3  . LYS   A 1 90  ? 31.552 -2.571  17.918  1.00 28.27 ?  90  LYS   A HG3  1 
ATOM   1803 H  HD2  . LYS   A 1 90  ? 30.879 -4.537  19.080  1.00 33.45 ?  90  LYS   A HD2  1 
ATOM   1804 H  HD3  . LYS   A 1 90  ? 31.328 -5.379  17.807  1.00 33.45 ?  90  LYS   A HD3  1 
ATOM   1805 H  HE2  . LYS   A 1 90  ? 33.137 -3.745  19.216  1.00 37.89 ?  90  LYS   A HE2  1 
ATOM   1806 H  HE3  . LYS   A 1 90  ? 32.969 -5.291  19.546  1.00 37.89 ?  90  LYS   A HE3  1 
ATOM   1807 H  HZ1  . LYS   A 1 90  ? 34.717 -4.980  18.142  1.00 40.36 ?  90  LYS   A HZ1  1 
ATOM   1808 H  HZ2  . LYS   A 1 90  ? 33.705 -5.741  17.437  1.00 40.36 ?  90  LYS   A HZ2  1 
ATOM   1809 H  HZ3  . LYS   A 1 90  ? 33.879 -4.331  17.154  1.00 40.36 ?  90  LYS   A HZ3  1 
ATOM   1810 N  N    . HIS   A 1 91  ? 29.666 -2.356  14.123  1.00 13.73 ?  91  HIS   A N    1 
ATOM   1811 C  CA   . HIS   A 1 91  ? 30.238 -2.342  12.789  1.00 13.19 ?  91  HIS   A CA   1 
ATOM   1812 C  C    . HIS   A 1 91  ? 29.150 -2.058  11.770  1.00 12.36 ?  91  HIS   A C    1 
ATOM   1813 O  O    . HIS   A 1 91  ? 27.982 -2.407  11.973  1.00 12.79 ?  91  HIS   A O    1 
ATOM   1814 C  CB   . HIS   A 1 91  ? 30.820 -3.715  12.420  1.00 15.71 ?  91  HIS   A CB   1 
ATOM   1815 C  CG   . HIS   A 1 91  ? 31.808 -4.247  13.409  1.00 19.78 ?  91  HIS   A CG   1 
ATOM   1816 N  ND1  . HIS   A 1 91  ? 33.089 -3.752  13.524  1.00 21.83 ?  91  HIS   A ND1  1 
ATOM   1817 C  CD2  . HIS   A 1 91  ? 31.709 -5.247  14.316  1.00 21.56 ?  91  HIS   A CD2  1 
ATOM   1818 C  CE1  . HIS   A 1 91  ? 33.734 -4.419  14.465  1.00 22.87 ?  91  HIS   A CE1  1 
ATOM   1819 N  NE2  . HIS   A 1 91  ? 32.919 -5.332  14.961  1.00 23.01 ?  91  HIS   A NE2  1 
ATOM   1820 H  H    . HIS   A 1 91  ? 28.985 -2.890  14.193  1.00 16.47 ?  91  HIS   A H    1 
ATOM   1821 H  HA   . HIS   A 1 91  ? 30.930 -1.670  12.726  1.00 15.83 ?  91  HIS   A HA   1 
ATOM   1822 H  HB2  . HIS   A 1 91  ? 30.094 -4.358  12.358  1.00 18.85 ?  91  HIS   A HB2  1 
ATOM   1823 H  HB3  . HIS   A 1 91  ? 31.267 -3.644  11.563  1.00 18.85 ?  91  HIS   A HB3  1 
ATOM   1824 H  HD1  . HIS   A 1 91  ? 33.417 -3.108  13.054  1.00 26.19 ?  91  HIS   A HD1  1 
ATOM   1825 H  HD2  . HIS   A 1 91  ? 30.966 -5.777  14.476  1.00 25.87 ?  91  HIS   A HD2  1 
ATOM   1826 H  HE1  . HIS   A 1 91  ? 34.616 -4.266  14.730  1.00 27.44 ?  91  HIS   A HE1  1 
ATOM   1827 N  N    . CYS   A 1 92  ? 29.556 -1.471  10.649  1.00 11.90 ?  92  CYS   A N    1 
ATOM   1828 C  CA   . CYS   A 1 92  ? 28.717 -1.384  9.461   1.00 11.55 ?  92  CYS   A CA   1 
ATOM   1829 C  C    . CYS   A 1 92  ? 29.357 -2.207  8.352   1.00 11.03 ?  92  CYS   A C    1 
ATOM   1830 O  O    . CYS   A 1 92  ? 30.517 -1.968  7.985   1.00 11.64 ?  92  CYS   A O    1 
ATOM   1831 C  CB   . CYS   A 1 92  ? 28.512 0.061   9.000   1.00 11.87 ?  92  CYS   A CB   1 
ATOM   1832 S  SG   . CYS   A 1 92  ? 27.490 0.172   7.499   1.00 11.15 ?  92  CYS   A SG   1 
ATOM   1833 H  H    . CYS   A 1 92  ? 30.328 -1.104  10.553  1.00 14.28 ?  92  CYS   A H    1 
ATOM   1834 H  HA   . CYS   A 1 92  ? 27.848 -1.761  9.657   1.00 13.86 ?  92  CYS   A HA   1 
ATOM   1835 H  HB2  . CYS   A 1 92  ? 28.066 0.562   9.703   1.00 14.24 ?  92  CYS   A HB2  1 
ATOM   1836 H  HB3  . CYS   A 1 92  ? 29.376 0.462   8.807   1.00 14.24 ?  92  CYS   A HB3  1 
ATOM   1837 H  HG   . CYS   A 1 92  ? 27.359 1.326   7.201   1.00 13.38 ?  92  CYS   A HG   1 
ATOM   1838 N  N    . LEU   A 1 93  ? 28.614 -3.186  7.844   1.00 10.72 ?  93  LEU   A N    1 
ATOM   1839 C  CA   . LEU   A 1 93  ? 29.018 -3.946  6.667   1.00 10.46 ?  93  LEU   A CA   1 
ATOM   1840 C  C    . LEU   A 1 93  ? 28.422 -3.250  5.448   1.00 10.19 ?  93  LEU   A C    1 
ATOM   1841 O  O    . LEU   A 1 93  ? 27.207 -3.294  5.230   1.00 10.59 ?  93  LEU   A O    1 
ATOM   1842 C  CB   . LEU   A 1 93  ? 28.530 -5.390  6.773   1.00 11.23 ?  93  LEU   A CB   1 
ATOM   1843 C  CG   . LEU   A 1 93  ? 28.913 -6.290  5.597   1.00 11.53 ?  93  LEU   A CG   1 
ATOM   1844 C  CD1  . LEU   A 1 93  ? 30.415 -6.551  5.577   1.00 12.49 ?  93  LEU   A CD1  1 
ATOM   1845 C  CD2  . LEU   A 1 93  ? 28.144 -7.613  5.621   1.00 12.22 ?  93  LEU   A CD2  1 
ATOM   1846 H  H    . LEU   A 1 93  ? 27.853 -3.427  8.170   1.00 12.86 ?  93  LEU   A H    1 
ATOM   1847 H  HA   . LEU   A 1 93  ? 29.982 -3.942  6.596   1.00 12.55 ?  93  LEU   A HA   1 
ATOM   1848 H  HB2  . LEU   A 1 93  ? 28.905 -5.780  7.581   1.00 13.47 ?  93  LEU   A HB2  1 
ATOM   1849 H  HB3  . LEU   A 1 93  ? 27.563 -5.384  6.836   1.00 13.47 ?  93  LEU   A HB3  1 
ATOM   1850 H  HG   . LEU   A 1 93  ? 28.689 -5.838  4.778   1.00 13.84 ?  93  LEU   A HG   1 
ATOM   1851 H  HD11 . LEU   A 1 93  ? 30.624 -7.165  4.856   1.00 14.99 ?  93  LEU   A HD11 1 
ATOM   1852 H  HD12 . LEU   A 1 93  ? 30.887 -5.713  5.444   1.00 14.99 ?  93  LEU   A HD12 1 
ATOM   1853 H  HD13 . LEU   A 1 93  ? 30.687 -6.944  6.428   1.00 14.99 ?  93  LEU   A HD13 1 
ATOM   1854 H  HD21 . LEU   A 1 93  ? 28.426 -8.151  4.859   1.00 14.66 ?  93  LEU   A HD21 1 
ATOM   1855 H  HD22 . LEU   A 1 93  ? 28.344 -8.085  6.445   1.00 14.66 ?  93  LEU   A HD22 1 
ATOM   1856 H  HD23 . LEU   A 1 93  ? 27.197 -7.430  5.562   1.00 14.66 ?  93  LEU   A HD23 1 
ATOM   1857 N  N    . HIS   A 1 94  ? 29.274 -2.563  4.685   1.00 9.91  ?  94  HIS   A N    1 
ATOM   1858 C  CA   . HIS   A 1 94  ? 28.850 -1.884  3.464   1.00 10.08 ?  94  HIS   A CA   1 
ATOM   1859 C  C    . HIS   A 1 94  ? 28.847 -2.918  2.353   1.00 10.06 ?  94  HIS   A C    1 
ATOM   1860 O  O    . HIS   A 1 94  ? 29.905 -3.440  2.003   1.00 11.59 ?  94  HIS   A O    1 
ATOM   1861 C  CB   . HIS   A 1 94  ? 29.813 -0.742  3.132   1.00 10.06 ?  94  HIS   A CB   1 
ATOM   1862 C  CG   . HIS   A 1 94  ? 29.804 0.348   4.148   1.00 10.00 ?  94  HIS   A CG   1 
ATOM   1863 N  ND1  . HIS   A 1 94  ? 28.935 1.418   4.092   1.00 10.23 ?  94  HIS   A ND1  1 
ATOM   1864 C  CD2  . HIS   A 1 94  ? 30.545 0.513   5.269   1.00 10.66 ?  94  HIS   A CD2  1 
ATOM   1865 C  CE1  . HIS   A 1 94  ? 29.148 2.193   5.139   1.00 10.44 ?  94  HIS   A CE1  1 
ATOM   1866 N  NE2  . HIS   A 1 94  ? 30.116 1.666   5.869   1.00 10.90 ?  94  HIS   A NE2  1 
ATOM   1867 H  H    . HIS   A 1 94  ? 30.118 -2.474  4.856   1.00 11.89 ?  94  HIS   A H    1 
ATOM   1868 H  HA   . HIS   A 1 94  ? 27.956 -1.531  3.573   1.00 12.10 ?  94  HIS   A HA   1 
ATOM   1869 H  HB2  . HIS   A 1 94  ? 30.712 -1.094  3.077   1.00 12.07 ?  94  HIS   A HB2  1 
ATOM   1870 H  HB3  . HIS   A 1 94  ? 29.553 -0.355  2.280   1.00 12.07 ?  94  HIS   A HB3  1 
ATOM   1871 H  HD2  . HIS   A 1 94  ? 31.214 -0.050  5.578   1.00 12.80 ?  94  HIS   A HD2  1 
ATOM   1872 H  HE1  . HIS   A 1 94  ? 28.686 2.979   5.327   1.00 12.53 ?  94  HIS   A HE1  1 
ATOM   1873 H  HE2  . HIS   A 1 94  ? 30.430 2.007   6.594   1.00 13.08 ?  94  HIS   A HE2  1 
ATOM   1874 N  N    . VAL   A 1 95  ? 27.673 -3.234  1.812   1.00 9.61  ?  95  VAL   A N    1 
ATOM   1875 C  CA   . VAL   A 1 95  ? 27.520 -4.269  0.791   1.00 9.72  ?  95  VAL   A CA   1 
ATOM   1876 C  C    . VAL   A 1 95  ? 26.970 -3.630  -0.473  1.00 9.34  ?  95  VAL   A C    1 
ATOM   1877 O  O    . VAL   A 1 95  ? 25.972 -2.900  -0.414  1.00 10.33 ?  95  VAL   A O    1 
ATOM   1878 C  CB   . VAL   A 1 95  ? 26.584 -5.403  1.247   1.00 10.70 ?  95  VAL   A CB   1 
ATOM   1879 C  CG1  . VAL   A 1 95  ? 26.458 -6.438  0.143   1.00 11.31 ?  95  VAL   A CG1  1 
ATOM   1880 C  CG2  . VAL   A 1 95  ? 27.092 -6.028  2.530   1.00 10.81 ?  95  VAL   A CG2  1 
ATOM   1881 H  H    . VAL   A 1 95  ? 26.926 -2.863  2.032   1.00 11.53 ?  95  VAL   A H    1 
ATOM   1882 H  HA   . VAL   A 1 95  ? 28.383 -4.652  0.587   1.00 11.67 ?  95  VAL   A HA   1 
ATOM   1883 H  HB   . VAL   A 1 95  ? 25.702 -5.038  1.420   1.00 12.84 ?  95  VAL   A HB   1 
ATOM   1884 H  HG11 . VAL   A 1 95  ? 26.072 -7.250  0.512   1.00 13.57 ?  95  VAL   A HG11 1 
ATOM   1885 H  HG12 . VAL   A 1 95  ? 25.881 -6.093  -0.558  1.00 13.57 ?  95  VAL   A HG12 1 
ATOM   1886 H  HG13 . VAL   A 1 95  ? 27.339 -6.630  -0.217  1.00 13.57 ?  95  VAL   A HG13 1 
ATOM   1887 H  HG21 . VAL   A 1 95  ? 26.528 -6.782  2.755   1.00 12.97 ?  95  VAL   A HG21 1 
ATOM   1888 H  HG22 . VAL   A 1 95  ? 28.005 -6.320  2.395   1.00 12.97 ?  95  VAL   A HG22 1 
ATOM   1889 H  HG23 . VAL   A 1 95  ? 27.055 -5.363  3.236   1.00 12.97 ?  95  VAL   A HG23 1 
ATOM   1890 N  N    . VAL   A 1 96  ? 27.598 -3.917  -1.613  1.00 9.71  ?  96  VAL   A N    1 
ATOM   1891 C  CA   . VAL   A 1 96  ? 27.190 -3.356  -2.895  1.00 10.22 ?  96  VAL   A CA   1 
ATOM   1892 C  C    . VAL   A 1 96  ? 26.374 -4.397  -3.656  1.00 10.37 ?  96  VAL   A C    1 
ATOM   1893 O  O    . VAL   A 1 96  ? 26.923 -5.340  -4.227  1.00 11.62 ?  96  VAL   A O    1 
ATOM   1894 C  CB   . VAL   A 1 96  ? 28.383 -2.889  -3.728  1.00 10.58 ?  96  VAL   A CB   1 
ATOM   1895 C  CG1  . VAL   A 1 96  ? 27.882 -2.246  -5.007  1.00 10.95 ?  96  VAL   A CG1  1 
ATOM   1896 C  CG2  . VAL   A 1 96  ? 29.260 -1.924  -2.941  1.00 11.01 ?  96  VAL   A CG2  1 
ATOM   1897 H  H    . VAL   A 1 96  ? 28.280 -4.450  -1.668  1.00 11.65 ?  96  VAL   A H    1 
ATOM   1898 H  HA   . VAL   A 1 96  ? 26.624 -2.589  -2.732  1.00 12.26 ?  96  VAL   A HA   1 
ATOM   1899 H  HB   . VAL   A 1 96  ? 28.924 -3.654  -3.971  1.00 12.69 ?  96  VAL   A HB   1 
ATOM   1900 H  HG11 . VAL   A 1 96  ? 28.621 -1.775  -5.431  1.00 13.14 ?  96  VAL   A HG11 1 
ATOM   1901 H  HG12 . VAL   A 1 96  ? 27.549 -2.934  -5.600  1.00 13.14 ?  96  VAL   A HG12 1 
ATOM   1902 H  HG13 . VAL   A 1 96  ? 27.177 -1.617  -4.790  1.00 13.14 ?  96  VAL   A HG13 1 
ATOM   1903 H  HG21 . VAL   A 1 96  ? 29.970 -1.596  -3.515  1.00 13.21 ?  96  VAL   A HG21 1 
ATOM   1904 H  HG22 . VAL   A 1 96  ? 28.718 -1.182  -2.629  1.00 13.21 ?  96  VAL   A HG22 1 
ATOM   1905 H  HG23 . VAL   A 1 96  ? 29.643 -2.393  -2.180  1.00 13.21 ?  96  VAL   A HG23 1 
ATOM   1906 N  N    A GLY   A 1 97  ? 25.056 -4.233  -3.671  0.56 10.79 ?  97  GLY   A N    1 
ATOM   1907 N  N    B GLY   A 1 97  ? 25.057 -4.229  -3.672  0.44 10.67 ?  97  GLY   A N    1 
ATOM   1908 C  CA   A GLY   A 1 97  ? 24.227 -4.972  -4.588  0.56 11.35 ?  97  GLY   A CA   1 
ATOM   1909 C  CA   B GLY   A 1 97  ? 24.223 -4.998  -4.558  0.44 11.03 ?  97  GLY   A CA   1 
ATOM   1910 C  C    A GLY   A 1 97  ? 24.224 -4.285  -5.939  0.56 11.69 ?  97  GLY   A C    1 
ATOM   1911 C  C    B GLY   A 1 97  ? 24.236 -4.381  -5.941  0.44 11.29 ?  97  GLY   A C    1 
ATOM   1912 O  O    A GLY   A 1 97  ? 24.497 -3.086  -6.043  0.56 12.52 ?  97  GLY   A O    1 
ATOM   1913 O  O    B GLY   A 1 97  ? 24.561 -3.202  -6.111  0.44 11.59 ?  97  GLY   A O    1 
ATOM   1914 H  H    A GLY   A 1 97  ? 24.622 -3.691  -3.154  0.56 12.95 ?  97  GLY   A H    1 
ATOM   1915 H  H    B GLY   A 1 97  ? 24.627 -3.665  -3.177  0.44 12.80 ?  97  GLY   A H    1 
ATOM   1916 H  HA2  A GLY   A 1 97  ? 24.573 -5.874  -4.677  0.56 13.62 ?  97  GLY   A HA2  1 
ATOM   1917 H  HA2  B GLY   A 1 97  ? 24.564 -5.901  -4.620  0.44 13.24 ?  97  GLY   A HA2  1 
ATOM   1918 H  HA3  A GLY   A 1 97  ? 23.317 -5.015  -4.252  0.56 13.62 ?  97  GLY   A HA3  1 
ATOM   1919 H  HA3  B GLY   A 1 97  ? 23.314 -5.026  -4.216  0.44 13.24 ?  97  GLY   A HA3  1 
ATOM   1920 N  N    A PRO   A 1 98  ? 23.911 -5.019  -7.003  0.56 11.58 ?  98  PRO   A N    1 
ATOM   1921 N  N    B PRO   A 1 98  ? 23.891 -5.162  -6.960  0.44 11.55 ?  98  PRO   A N    1 
ATOM   1922 C  CA   A PRO   A 1 98  ? 23.801 -4.378  -8.319  0.56 12.33 ?  98  PRO   A CA   1 
ATOM   1923 C  CA   B PRO   A 1 98  ? 23.810 -4.600  -8.312  0.44 12.49 ?  98  PRO   A CA   1 
ATOM   1924 C  C    A PRO   A 1 98  ? 22.675 -3.350  -8.354  0.56 12.69 ?  98  PRO   A C    1 
ATOM   1925 C  C    B PRO   A 1 98  ? 22.708 -3.554  -8.401  0.44 12.75 ?  98  PRO   A C    1 
ATOM   1926 O  O    A PRO   A 1 98  ? 21.595 -3.562  -7.800  0.56 12.35 ?  98  PRO   A O    1 
ATOM   1927 O  O    B PRO   A 1 98  ? 21.621 -3.719  -7.843  0.44 13.01 ?  98  PRO   A O    1 
ATOM   1928 C  CB   A PRO   A 1 98  ? 23.521 -5.554  -9.262  0.56 13.16 ?  98  PRO   A CB   1 
ATOM   1929 C  CB   B PRO   A 1 98  ? 23.493 -5.821  -9.183  0.44 12.80 ?  98  PRO   A CB   1 
ATOM   1930 C  CG   A PRO   A 1 98  ? 22.930 -6.620  -8.378  0.56 13.10 ?  98  PRO   A CG   1 
ATOM   1931 C  CG   B PRO   A 1 98  ? 22.792 -6.762  -8.253  0.44 12.56 ?  98  PRO   A CG   1 
ATOM   1932 C  CD   A PRO   A 1 98  ? 23.648 -6.468  -7.064  0.56 12.07 ?  98  PRO   A CD   1 
ATOM   1933 C  CD   B PRO   A 1 98  ? 23.484 -6.577  -6.926  0.44 11.66 ?  98  PRO   A CD   1 
ATOM   1934 H  HA   A PRO   A 1 98  ? 24.642 -3.960  -8.555  0.56 14.80 ?  98  PRO   A HA   1 
ATOM   1935 H  HA   B PRO   A 1 98  ? 24.658 -4.209  -8.579  0.44 14.99 ?  98  PRO   A HA   1 
ATOM   1936 H  HB2  A PRO   A 1 98  ? 22.887 -5.284  -9.942  0.56 15.80 ?  98  PRO   A HB2  1 
ATOM   1937 H  HB2  B PRO   A 1 98  ? 22.913 -5.560  -9.916  0.44 15.36 ?  98  PRO   A HB2  1 
ATOM   1938 H  HB3  A PRO   A 1 98  ? 24.349 -5.862  -9.659  0.56 15.80 ?  98  PRO   A HB3  1 
ATOM   1939 H  HB3  B PRO   A 1 98  ? 24.317 -6.209  -9.514  0.44 15.36 ?  98  PRO   A HB3  1 
ATOM   1940 H  HG2  A PRO   A 1 98  ? 21.977 -6.466  -8.267  0.56 15.72 ?  98  PRO   A HG2  1 
ATOM   1941 H  HG2  B PRO   A 1 98  ? 21.854 -6.519  -8.191  0.44 15.07 ?  98  PRO   A HG2  1 
ATOM   1942 H  HG3  A PRO   A 1 98  ? 23.094 -7.496  -8.759  0.56 15.72 ?  98  PRO   A HG3  1 
ATOM   1943 H  HG3  B PRO   A 1 98  ? 22.894 -7.670  -8.573  0.44 15.07 ?  98  PRO   A HG3  1 
ATOM   1944 H  HD2  A PRO   A 1 98  ? 23.076 -6.750  -6.329  0.56 14.49 ?  98  PRO   A HD2  1 
ATOM   1945 H  HD2  B PRO   A 1 98  ? 22.863 -6.736  -6.197  0.44 13.99 ?  98  PRO   A HD2  1 
ATOM   1946 H  HD3  A PRO   A 1 98  ? 24.483 -6.962  -7.072  0.56 14.49 ?  98  PRO   A HD3  1 
ATOM   1947 H  HD3  B PRO   A 1 98  ? 24.263 -7.148  -6.866  0.44 13.99 ?  98  PRO   A HD3  1 
ATOM   1948 N  N    A ASN   A 1 99  ? 22.941 -2.220  -9.012  0.56 13.58 ?  99  ASN   A N    1 
ATOM   1949 N  N    B ASN   A 1 99  ? 23.002 -2.461  -9.097  0.44 13.55 ?  99  ASN   A N    1 
ATOM   1950 C  CA   A ASN   A 1 99  ? 21.953 -1.158  -9.214  0.56 14.57 ?  99  ASN   A CA   1 
ATOM   1951 C  CA   B ASN   A 1 99  ? 22.027 -1.408  -9.348  0.44 14.89 ?  99  ASN   A CA   1 
ATOM   1952 C  C    A ASN   A 1 99  ? 21.428 -1.310  -10.641 0.56 15.42 ?  99  ASN   A C    1 
ATOM   1953 C  C    B ASN   A 1 99  ? 21.452 -1.608  -10.743 0.44 15.55 ?  99  ASN   A C    1 
ATOM   1954 O  O    A ASN   A 1 99  ? 22.048 -0.840  -11.601 0.56 15.21 ?  99  ASN   A O    1 
ATOM   1955 O  O    B ASN   A 1 99  ? 22.201 -1.676  -11.728 0.44 16.05 ?  99  ASN   A O    1 
ATOM   1956 C  CB   A ASN   A 1 99  ? 22.578 0.215   -8.960  0.56 15.04 ?  99  ASN   A CB   1 
ATOM   1957 C  CB   B ASN   A 1 99  ? 22.667 -0.024  -9.225  0.44 16.51 ?  99  ASN   A CB   1 
ATOM   1958 C  CG   A ASN   A 1 99  ? 21.549 1.349   -8.964  0.56 15.64 ?  99  ASN   A CG   1 
ATOM   1959 C  CG   B ASN   A 1 99  ? 21.643 1.096   -9.267  0.44 18.25 ?  99  ASN   A CG   1 
ATOM   1960 O  OD1  A ASN   A 1 99  ? 20.546 1.292   -9.677  0.56 16.09 ?  99  ASN   A OD1  1 
ATOM   1961 O  OD1  B ASN   A 1 99  ? 20.726 1.076   -10.085 0.44 18.62 ?  99  ASN   A OD1  1 
ATOM   1962 N  ND2  A ASN   A 1 99  ? 21.807 2.389   -8.168  0.56 15.90 ?  99  ASN   A ND2  1 
ATOM   1963 N  ND2  B ASN   A 1 99  ? 21.790 2.074   -8.372  0.44 18.91 ?  99  ASN   A ND2  1 
ATOM   1964 H  H    A ASN   A 1 99  ? 23.710 -2.040  -9.350  0.56 16.29 ?  99  ASN   A H    1 
ATOM   1965 H  H    B ASN   A 1 99  ? 23.780 -2.294  -9.425  0.44 16.26 ?  99  ASN   A H    1 
ATOM   1966 H  HA   A ASN   A 1 99  ? 21.216 -1.278  -8.586  0.56 17.49 ?  99  ASN   A HA   1 
ATOM   1967 H  HA   B ASN   A 1 99  ? 21.306 -1.471  -8.696  0.44 17.86 ?  99  ASN   A HA   1 
ATOM   1968 H  HB2  A ASN   A 1 99  ? 23.017 0.214   -8.089  0.56 18.05 ?  99  ASN   A HB2  1 
ATOM   1969 H  HB2  B ASN   A 1 99  ? 23.144 0.035   -8.383  0.44 19.82 ?  99  ASN   A HB2  1 
ATOM   1970 H  HB3  A ASN   A 1 99  ? 23.230 0.399   -9.652  0.56 18.05 ?  99  ASN   A HB3  1 
ATOM   1971 H  HB3  B ASN   A 1 99  ? 23.277 0.108   -9.964  0.44 19.82 ?  99  ASN   A HB3  1 
ATOM   1972 H  HD21 A ASN   A 1 99  ? 21.261 3.053   -8.133  0.56 19.07 ?  99  ASN   A HD21 1 
ATOM   1973 H  HD21 B ASN   A 1 99  ? 21.233 2.729   -8.346  0.44 22.69 ?  99  ASN   A HD21 1 
ATOM   1974 H  HD22 A ASN   A 1 99  ? 22.517 2.394   -7.680  0.56 19.07 ?  99  ASN   A HD22 1 
ATOM   1975 H  HD22 B ASN   A 1 99  ? 22.446 2.051   -7.812  0.44 22.69 ?  99  ASN   A HD22 1 
ATOM   1976 N  N    A VAL   A 1 100 ? 20.295 -2.016  -10.760 0.56 17.04 ?  100 VAL   A N    1 
ATOM   1977 N  N    B VAL   A 1 100 ? 20.126 -1.713  -10.823 0.44 15.50 ?  100 VAL   A N    1 
ATOM   1978 C  CA   A VAL   A 1 100 ? 19.656 -2.285  -12.049 0.56 19.57 ?  100 VAL   A CA   1 
ATOM   1979 C  CA   B VAL   A 1 100 ? 19.491 -1.878  -12.122 0.44 16.16 ?  100 VAL   A CA   1 
ATOM   1980 C  C    A VAL   A 1 100 ? 19.563 -1.024  -12.893 0.56 20.63 ?  100 VAL   A C    1 
ATOM   1981 C  C    B VAL   A 1 100 ? 19.312 -0.534  -12.816 0.44 15.02 ?  100 VAL   A C    1 
ATOM   1982 O  O    A VAL   A 1 100 ? 19.680 -1.074  -14.123 0.56 21.38 ?  100 VAL   A O    1 
ATOM   1983 O  O    B VAL   A 1 100 ? 19.321 -0.465  -14.050 0.44 15.12 ?  100 VAL   A O    1 
ATOM   1984 C  CB   A VAL   A 1 100 ? 18.272 -2.928  -11.821 0.56 20.93 ?  100 VAL   A CB   1 
ATOM   1985 C  CB   B VAL   A 1 100 ? 18.172 -2.656  -11.985 0.44 17.99 ?  100 VAL   A CB   1 
ATOM   1986 C  CG1  A VAL   A 1 100 ? 17.514 -3.089  -13.135 0.56 21.63 ?  100 VAL   A CG1  1 
ATOM   1987 C  CG1  B VAL   A 1 100 ? 17.479 -2.787  -13.335 0.44 18.92 ?  100 VAL   A CG1  1 
ATOM   1988 C  CG2  A VAL   A 1 100 ? 18.426 -4.269  -11.124 0.56 21.70 ?  100 VAL   A CG2  1 
ATOM   1989 C  CG2  B VAL   A 1 100 ? 18.444 -4.024  -11.388 0.44 18.56 ?  100 VAL   A CG2  1 
ATOM   1990 H  H    A VAL   A 1 100 ? 19.878 -2.367  -10.099 0.56 20.45 ?  100 VAL   A H    1 
ATOM   1991 H  H    B VAL   A 1 100 ? 19.582 -1.695  -10.149 0.44 18.60 ?  100 VAL   A H    1 
ATOM   1992 H  HA   A VAL   A 1 100 ? 20.197 -2.914  -12.545 0.56 23.49 ?  100 VAL   A HA   1 
ATOM   1993 H  HA   B VAL   A 1 100 ? 20.080 -2.408  -12.674 0.44 19.40 ?  100 VAL   A HA   1 
ATOM   1994 H  HB   A VAL   A 1 100 ? 17.748 -2.348  -11.247 0.56 25.12 ?  100 VAL   A HB   1 
ATOM   1995 H  HB   B VAL   A 1 100 ? 17.578 -2.175  -11.388 0.44 21.59 ?  100 VAL   A HB   1 
ATOM   1996 H  HG11 A VAL   A 1 100 ? 16.759 -3.681  -12.991 0.56 25.96 ?  100 VAL   A HG11 1 
ATOM   1997 H  HG11 B VAL   A 1 100 ? 16.750 -3.421  -13.252 0.44 22.70 ?  100 VAL   A HG11 1 
ATOM   1998 H  HG12 A VAL   A 1 100 ? 17.195 -2.220  -13.431 0.56 25.96 ?  100 VAL   A HG12 1 
ATOM   1999 H  HG12 B VAL   A 1 100 ? 17.136 -1.922  -13.604 0.44 22.70 ?  100 VAL   A HG12 1 
ATOM   2000 H  HG13 A VAL   A 1 100 ? 18.108 -3.468  -13.800 0.56 25.96 ?  100 VAL   A HG13 1 
ATOM   2001 H  HG13 B VAL   A 1 100 ? 18.122 -3.109  -13.988 0.44 22.70 ?  100 VAL   A HG13 1 
ATOM   2002 H  HG21 A VAL   A 1 100 ? 17.558 -4.697  -11.073 0.56 26.05 ?  100 VAL   A HG21 1 
ATOM   2003 H  HG21 B VAL   A 1 100 ? 17.620 -4.533  -11.378 0.44 22.27 ?  100 VAL   A HG21 1 
ATOM   2004 H  HG22 A VAL   A 1 100 ? 19.039 -4.819  -11.635 0.56 26.05 ?  100 VAL   A HG22 1 
ATOM   2005 H  HG22 B VAL   A 1 100 ? 19.108 -4.477  -11.931 0.44 22.27 ?  100 VAL   A HG22 1 
ATOM   2006 H  HG23 A VAL   A 1 100 ? 18.777 -4.122  -10.233 0.56 26.05 ?  100 VAL   A HG23 1 
ATOM   2007 H  HG23 B VAL   A 1 100 ? 18.777 -3.913  -10.483 0.44 22.27 ?  100 VAL   A HG23 1 
ATOM   2008 N  N    A ASN   A 1 101 ? 19.330 0.124   -12.254 0.56 22.00 ?  101 ASN   A N    1 
ATOM   2009 N  N    B ASN   A 1 101 ? 19.149 0.550   -12.056 0.44 15.17 ?  101 ASN   A N    1 
ATOM   2010 C  CA   A ASN   A 1 101 ? 19.264 1.395   -12.966 0.56 23.30 ?  101 ASN   A CA   1 
ATOM   2011 C  CA   B ASN   A 1 101 ? 19.013 1.864   -12.671 0.44 15.85 ?  101 ASN   A CA   1 
ATOM   2012 C  C    A ASN   A 1 101 ? 20.610 1.822   -13.540 0.56 24.86 ?  101 ASN   A C    1 
ATOM   2013 C  C    B ASN   A 1 101 ? 20.335 2.411   -13.195 0.44 17.43 ?  101 ASN   A C    1 
ATOM   2014 O  O    A ASN   A 1 101 ? 20.660 2.810   -14.280 0.56 25.98 ?  101 ASN   A O    1 
ATOM   2015 O  O    B ASN   A 1 101 ? 20.323 3.394   -13.946 0.44 18.27 ?  101 ASN   A O    1 
ATOM   2016 C  CB   A ASN   A 1 101 ? 18.674 2.464   -12.042 0.56 23.10 ?  101 ASN   A CB   1 
ATOM   2017 C  CB   B ASN   A 1 101 ? 18.339 2.833   -11.699 0.44 16.28 ?  101 ASN   A CB   1 
ATOM   2018 C  CG   A ASN   A 1 101 ? 17.324 2.052   -11.479 0.56 22.76 ?  101 ASN   A CG   1 
ATOM   2019 C  CG   B ASN   A 1 101 ? 16.944 2.375   -11.321 0.44 16.46 ?  101 ASN   A CG   1 
ATOM   2020 O  OD1  A ASN   A 1 101 ? 16.490 1.493   -12.193 0.56 22.51 ?  101 ASN   A OD1  1 
ATOM   2021 O  OD1  B ASN   A 1 101 ? 16.199 1.881   -12.170 0.44 16.85 ?  101 ASN   A OD1  1 
ATOM   2022 N  ND2  A ASN   A 1 101 ? 17.111 2.301   -10.193 0.56 22.63 ?  101 ASN   A ND2  1 
ATOM   2023 N  ND2  B ASN   A 1 101 ? 16.593 2.509   -10.046 0.44 16.11 ?  101 ASN   A ND2  1 
ATOM   2024 H  H    A ASN   A 1 101 ? 19.194 0.192   -11.413 0.56 26.40 ?  101 ASN   A H    1 
ATOM   2025 H  H    B ASN   A 1 101 ? 19.100 0.553   -11.193 0.44 18.20 ?  101 ASN   A H    1 
ATOM   2026 H  HA   A ASN   A 1 101 ? 18.663 1.309   -13.718 0.56 27.96 ?  101 ASN   A HA   1 
ATOM   2027 H  HA   B ASN   A 1 101 ? 18.425 1.779   -13.433 0.44 19.02 ?  101 ASN   A HA   1 
ATOM   2028 H  HB2  A ASN   A 1 101 ? 19.272 2.621   -11.296 0.56 27.72 ?  101 ASN   A HB2  1 
ATOM   2029 H  HB2  B ASN   A 1 101 ? 18.864 2.900   -10.889 0.44 19.53 ?  101 ASN   A HB2  1 
ATOM   2030 H  HB3  A ASN   A 1 101 ? 18.549 3.293   -12.543 0.56 27.72 ?  101 ASN   A HB3  1 
ATOM   2031 H  HB3  B ASN   A 1 101 ? 18.265 3.711   -12.120 0.44 19.53 ?  101 ASN   A HB3  1 
ATOM   2032 H  HD21 A ASN   A 1 101 ? 16.359 2.087   -9.830  0.56 27.15 ?  101 ASN   A HD21 1 
ATOM   2033 H  HD21 B ASN   A 1 101 ? 15.809 2.263   -9.784  0.44 19.34 ?  101 ASN   A HD21 1 
ATOM   2034 H  HD22 A ASN   A 1 101 ? 17.719 2.685   -9.723  0.56 27.15 ?  101 ASN   A HD22 1 
ATOM   2035 H  HD22 B ASN   A 1 101 ? 17.144 2.852   -9.482  0.44 19.34 ?  101 ASN   A HD22 1 
ATOM   2036 N  N    A LYS   A 1 102 ? 21.689 1.101   -13.229 0.56 25.68 ?  102 LYS   A N    1 
ATOM   2037 N  N    B LYS   A 1 102 ? 21.462 1.794   -12.821 0.44 18.75 ?  102 LYS   A N    1 
ATOM   2038 C  CA   A LYS   A 1 102 ? 22.983 1.289   -13.874 0.56 26.43 ?  102 LYS   A CA   1 
ATOM   2039 C  CA   B LYS   A 1 102 ? 22.756 2.033   -13.447 0.44 20.40 ?  102 LYS   A CA   1 
ATOM   2040 C  C    A LYS   A 1 102 ? 23.305 0.163   -14.851 0.56 26.51 ?  102 LYS   A C    1 
ATOM   2041 C  C    B LYS   A 1 102 ? 23.081 1.018   -14.536 0.44 21.07 ?  102 LYS   A C    1 
ATOM   2042 O  O    A LYS   A 1 102 ? 24.419 0.115   -15.381 0.56 26.59 ?  102 LYS   A O    1 
ATOM   2043 O  O    B LYS   A 1 102 ? 24.094 1.179   -15.226 0.44 20.88 ?  102 LYS   A O    1 
ATOM   2044 C  CB   A LYS   A 1 102 ? 24.102 1.378   -12.830 0.56 27.54 ?  102 LYS   A CB   1 
ATOM   2045 C  CB   B LYS   A 1 102 ? 23.874 1.984   -12.396 0.44 21.66 ?  102 LYS   A CB   1 
ATOM   2046 C  CG   A LYS   A 1 102 ? 23.975 2.519   -11.835 0.56 28.59 ?  102 LYS   A CG   1 
ATOM   2047 C  CG   B LYS   A 1 102 ? 23.816 3.081   -11.349 0.44 22.96 ?  102 LYS   A CG   1 
ATOM   2048 C  CD   A LYS   A 1 102 ? 25.137 2.512   -10.848 0.56 29.87 ?  102 LYS   A CD   1 
ATOM   2049 C  CD   B LYS   A 1 102 ? 24.849 2.837   -10.256 0.44 24.34 ?  102 LYS   A CD   1 
ATOM   2050 C  CE   A LYS   A 1 102 ? 25.020 3.642   -9.838  0.56 31.01 ?  102 LYS   A CE   1 
ATOM   2051 C  CE   B LYS   A 1 102 ? 24.870 3.966   -9.239  0.44 25.28 ?  102 LYS   A CE   1 
ATOM   2052 N  NZ   A LYS   A 1 102 ? 26.123 3.611   -8.834  0.56 31.57 ?  102 LYS   A NZ   1 
ATOM   2053 N  NZ   B LYS   A 1 102 ? 25.795 3.664   -8.110  0.44 25.84 ?  102 LYS   A NZ   1 
ATOM   2054 H  H    A LYS   A 1 102 ? 21.693 0.482   -12.635 0.56 30.82 ?  102 LYS   A H    1 
ATOM   2055 H  H    B LYS   A 1 102 ? 21.499 1.216   -12.185 0.44 22.50 ?  102 LYS   A H    1 
ATOM   2056 H  HA   A LYS   A 1 102 ? 22.967 2.128   -14.366 0.56 31.72 ?  102 LYS   A HA   1 
ATOM   2057 H  HA   B LYS   A 1 102 ? 22.762 2.912   -13.852 0.44 24.48 ?  102 LYS   A HA   1 
ATOM   2058 H  HB2  A LYS   A 1 102 ? 24.120 0.550   -12.325 0.56 33.05 ?  102 LYS   A HB2  1 
ATOM   2059 H  HB2  B LYS   A 1 102 ? 23.826 1.134   -11.931 0.44 25.99 ?  102 LYS   A HB2  1 
ATOM   2060 H  HB3  A LYS   A 1 102 ? 24.949 1.490   -13.295 0.56 33.05 ?  102 LYS   A HB3  1 
ATOM   2061 H  HB3  B LYS   A 1 102 ? 24.730 2.058   -12.848 0.44 25.99 ?  102 LYS   A HB3  1 
ATOM   2062 H  HG2  A LYS   A 1 102 ? 23.985 3.365   -12.309 0.56 34.30 ?  102 LYS   A HG2  1 
ATOM   2063 H  HG2  B LYS   A 1 102 ? 24.007 3.936   -11.766 0.44 27.55 ?  102 LYS   A HG2  1 
ATOM   2064 H  HG3  A LYS   A 1 102 ? 23.151 2.421   -11.334 0.56 34.30 ?  102 LYS   A HG3  1 
ATOM   2065 H  HG3  B LYS   A 1 102 ? 22.936 3.092   -10.942 0.44 27.55 ?  102 LYS   A HG3  1 
ATOM   2066 H  HD2  A LYS   A 1 102 ? 25.142 1.672   -10.363 0.56 35.85 ?  102 LYS   A HD2  1 
ATOM   2067 H  HD2  B LYS   A 1 102 ? 24.633 2.013   -9.790  0.44 29.21 ?  102 LYS   A HD2  1 
ATOM   2068 H  HD3  A LYS   A 1 102 ? 25.971 2.624   -11.332 0.56 35.85 ?  102 LYS   A HD3  1 
ATOM   2069 H  HD3  B LYS   A 1 102 ? 25.730 2.773   -10.657 0.44 29.21 ?  102 LYS   A HD3  1 
ATOM   2070 H  HE2  A LYS   A 1 102 ? 25.060 4.491   -10.306 0.56 37.21 ?  102 LYS   A HE2  1 
ATOM   2071 H  HE2  B LYS   A 1 102 ? 25.173 4.780   -9.671  0.44 30.34 ?  102 LYS   A HE2  1 
ATOM   2072 H  HE3  A LYS   A 1 102 ? 24.177 3.560   -9.366  0.56 37.21 ?  102 LYS   A HE3  1 
ATOM   2073 H  HE3  B LYS   A 1 102 ? 23.978 4.089   -8.878  0.44 30.34 ?  102 LYS   A HE3  1 
ATOM   2074 H  HZ1  A LYS   A 1 102 ? 26.028 4.283   -8.258  0.56 37.88 ?  102 LYS   A HZ1  1 
ATOM   2075 H  HZ1  B LYS   A 1 102 ? 25.793 4.335   -7.527  0.44 31.01 ?  102 LYS   A HZ1  1 
ATOM   2076 H  HZ2  A LYS   A 1 102 ? 26.105 2.842   -8.387  0.56 37.88 ?  102 LYS   A HZ2  1 
ATOM   2077 H  HZ2  B LYS   A 1 102 ? 25.535 2.920   -7.695  0.44 31.01 ?  102 LYS   A HZ2  1 
ATOM   2078 H  HZ3  A LYS   A 1 102 ? 26.909 3.690   -9.243  0.56 37.88 ?  102 LYS   A HZ3  1 
ATOM   2079 H  HZ3  B LYS   A 1 102 ? 26.622 3.549   -8.417  0.44 31.01 ?  102 LYS   A HZ3  1 
ATOM   2080 N  N    A GLY   A 1 103 ? 22.371 -0.757  -15.083 0.56 27.01 ?  103 GLY   A N    1 
ATOM   2081 N  N    B GLY   A 1 103 ? 22.262 -0.021  -14.695 0.44 22.58 ?  103 GLY   A N    1 
ATOM   2082 C  CA   A GLY   A 1 103 ? 22.610 -1.875  -15.973 0.56 26.56 ?  103 GLY   A CA   1 
ATOM   2083 C  CA   B GLY   A 1 103 ? 22.492 -1.037  -15.705 0.44 24.09 ?  103 GLY   A CA   1 
ATOM   2084 C  C    A GLY   A 1 103 ? 23.421 -3.009  -15.384 0.56 26.15 ?  103 GLY   A C    1 
ATOM   2085 C  C    B GLY   A 1 103 ? 23.478 -2.119  -15.313 0.44 25.56 ?  103 GLY   A C    1 
ATOM   2086 O  O    A GLY   A 1 103 ? 23.867 -3.885  -16.133 0.56 26.43 ?  103 GLY   A O    1 
ATOM   2087 O  O    B GLY   A 1 103 ? 24.380 -2.442  -16.091 0.44 26.07 ?  103 GLY   A O    1 
ATOM   2088 H  H    A GLY   A 1 103 ? 21.586 -0.753  -14.733 0.56 32.41 ?  103 GLY   A H    1 
ATOM   2089 H  H    B GLY   A 1 103 ? 21.555 -0.157  -14.224 0.44 27.10 ?  103 GLY   A H    1 
ATOM   2090 H  HA2  A GLY   A 1 103 ? 21.757 -2.234  -16.259 0.56 31.87 ?  103 GLY   A HA2  1 
ATOM   2091 H  HA2  B GLY   A 1 103 ? 21.649 -1.462  -15.933 0.44 28.90 ?  103 GLY   A HA2  1 
ATOM   2092 H  HA3  A GLY   A 1 103 ? 23.073 -1.543  -16.761 0.56 31.87 ?  103 GLY   A HA3  1 
ATOM   2093 H  HA3  B GLY   A 1 103 ? 22.842 -0.609  -16.496 0.44 28.90 ?  103 GLY   A HA3  1 
ATOM   2094 N  N    A GLU   A 1 104 ? 23.610 -3.036  -14.068 0.56 24.61 ?  104 GLU   A N    1 
ATOM   2095 N  N    B GLU   A 1 104 ? 23.315 -2.701  -14.128 0.44 26.12 ?  104 GLU   A N    1 
ATOM   2096 C  CA   A GLU   A 1 104 ? 24.491 -4.011  -13.439 0.56 23.26 ?  104 GLU   A CA   1 
ATOM   2097 C  CA   B GLU   A 1 104 ? 24.194 -3.754  -13.641 0.44 26.54 ?  104 GLU   A CA   1 
ATOM   2098 C  C    A GLU   A 1 104 ? 23.812 -5.375  -13.321 0.56 23.56 ?  104 GLU   A C    1 
ATOM   2099 C  C    B GLU   A 1 104 ? 23.445 -5.080  -13.553 0.44 26.92 ?  104 GLU   A C    1 
ATOM   2100 O  O    A GLU   A 1 104 ? 22.602 -5.473  -13.093 0.56 23.16 ?  104 GLU   A O    1 
ATOM   2101 O  O    B GLU   A 1 104 ? 22.213 -5.129  -13.581 0.44 27.04 ?  104 GLU   A O    1 
ATOM   2102 C  CB   A GLU   A 1 104 ? 24.956 -3.482  -12.077 0.56 21.64 ?  104 GLU   A CB   1 
ATOM   2103 C  CB   B GLU   A 1 104 ? 24.798 -3.378  -12.282 0.44 26.37 ?  104 GLU   A CB   1 
ATOM   2104 C  CG   A GLU   A 1 104 ? 25.829 -2.221  -12.237 0.56 20.95 ?  104 GLU   A CG   1 
ATOM   2105 C  CG   B GLU   A 1 104 ? 25.639 -2.107  -12.344 0.44 26.37 ?  104 GLU   A CG   1 
ATOM   2106 C  CD   A GLU   A 1 104 ? 26.143 -1.467  -10.953 0.56 19.92 ?  104 GLU   A CD   1 
ATOM   2107 C  CD   B GLU   A 1 104 ? 26.104 -1.615  -10.986 0.44 26.24 ?  104 GLU   A CD   1 
ATOM   2108 O  OE1  A GLU   A 1 104 ? 25.559 -1.768  -9.891  0.56 18.44 ?  104 GLU   A OE1  1 
ATOM   2109 O  OE1  B GLU   A 1 104 ? 25.609 -2.118  -9.956  0.44 25.76 ?  104 GLU   A OE1  1 
ATOM   2110 O  OE2  A GLU   A 1 104 ? 26.995 -0.548  -11.028 0.56 20.65 -1 104 GLU   A OE2  1 
ATOM   2111 O  OE2  B GLU   A 1 104 ? 26.965 -0.709  -10.953 0.44 26.72 -1 104 GLU   A OE2  1 
ATOM   2112 H  H    A GLU   A 1 104 ? 23.230 -2.495  -13.518 0.56 29.54 ?  104 GLU   A H    1 
ATOM   2113 H  H    B GLU   A 1 104 ? 22.686 -2.497  -13.580 0.44 31.34 ?  104 GLU   A H    1 
ATOM   2114 H  HA   A GLU   A 1 104 ? 25.277 -4.118  -13.997 0.56 27.92 ?  104 GLU   A HA   1 
ATOM   2115 H  HA   B GLU   A 1 104 ? 24.924 -3.868  -14.266 0.44 31.85 ?  104 GLU   A HA   1 
ATOM   2116 H  HB2  A GLU   A 1 104 ? 24.180 -3.255  -11.540 0.56 25.97 ?  104 GLU   A HB2  1 
ATOM   2117 H  HB2  B GLU   A 1 104 ? 24.083 -3.238  -11.646 0.44 31.64 ?  104 GLU   A HB2  1 
ATOM   2118 H  HB3  A GLU   A 1 104 ? 25.483 -4.165  -11.635 0.56 25.97 ?  104 GLU   A HB3  1 
ATOM   2119 H  HB3  B GLU   A 1 104 ? 25.370 -4.104  -11.984 0.44 31.64 ?  104 GLU   A HB3  1 
ATOM   2120 H  HG2  A GLU   A 1 104 ? 26.678 -2.481  -12.616 0.56 25.14 ?  104 GLU   A HG2  1 
ATOM   2121 H  HG2  B GLU   A 1 104 ? 26.420 -2.278  -12.896 0.44 31.64 ?  104 GLU   A HG2  1 
ATOM   2122 H  HG3  A GLU   A 1 104 ? 25.375 -1.606  -12.833 0.56 25.14 ?  104 GLU   A HG3  1 
ATOM   2123 H  HG3  B GLU   A 1 104 ? 25.107 -1.400  -12.736 0.44 31.64 ?  104 GLU   A HG3  1 
ATOM   2124 N  N    A ASP   A 1 105 ? 24.609 -6.431  -13.488 0.56 24.93 ?  105 ASP   A N    1 
ATOM   2125 N  N    B ASP   A 1 105 ? 24.216 -6.161  -13.430 0.44 27.26 ?  105 ASP   A N    1 
ATOM   2126 C  CA   A ASP   A 1 105 ? 24.085 -7.788  -13.611 0.56 26.33 ?  105 ASP   A CA   1 
ATOM   2127 C  CA   B ASP   A 1 105 ? 23.706 -7.519  -13.583 0.44 28.29 ?  105 ASP   A CA   1 
ATOM   2128 C  C    A ASP   A 1 105 ? 23.366 -8.214  -12.337 0.56 23.90 ?  105 ASP   A C    1 
ATOM   2129 C  C    B ASP   A 1 105 ? 23.137 -8.021  -12.261 0.44 26.76 ?  105 ASP   A C    1 
ATOM   2130 O  O    A ASP   A 1 105 ? 23.976 -8.295  -11.267 0.56 21.56 ?  105 ASP   A O    1 
ATOM   2131 O  O    B ASP   A 1 105 ? 23.844 -8.061  -11.249 0.44 25.93 ?  105 ASP   A O    1 
ATOM   2132 C  CB   A ASP   A 1 105 ? 25.248 -8.737  -13.902 0.56 29.71 ?  105 ASP   A CB   1 
ATOM   2133 C  CB   B ASP   A 1 105 ? 24.820 -8.446  -14.069 0.44 30.57 ?  105 ASP   A CB   1 
ATOM   2134 C  CG   A ASP   A 1 105 ? 24.790 -10.133 -14.271 0.56 32.58 ?  105 ASP   A CG   1 
ATOM   2135 C  CG   B ASP   A 1 105 ? 24.506 -9.906  -13.828 0.44 32.53 ?  105 ASP   A CG   1 
ATOM   2136 O  OD1  A ASP   A 1 105 ? 23.570 -10.340 -14.422 0.56 33.64 ?  105 ASP   A OD1  1 
ATOM   2137 O  OD1  B ASP   A 1 105 ? 23.412 -10.350 -14.232 0.44 33.20 ?  105 ASP   A OD1  1 
ATOM   2138 O  OD2  A ASP   A 1 105 ? 25.657 -11.024 -14.413 0.56 33.63 -1 105 ASP   A OD2  1 
ATOM   2139 O  OD2  B ASP   A 1 105 ? 25.355 -10.611 -13.243 0.44 33.37 -1 105 ASP   A OD2  1 
ATOM   2140 H  H    A ASP   A 1 105 ? 25.467 -6.382  -13.539 0.56 29.92 ?  105 ASP   A H    1 
ATOM   2141 H  H    B ASP   A 1 105 ? 25.052 -6.132  -13.239 0.44 32.71 ?  105 ASP   A H    1 
ATOM   2142 H  HA   A ASP   A 1 105 ? 23.458 -7.829  -14.349 0.56 31.60 ?  105 ASP   A HA   1 
ATOM   2143 H  HA   B ASP   A 1 105 ? 22.997 -7.532  -14.239 0.44 33.95 ?  105 ASP   A HA   1 
ATOM   2144 H  HB2  A ASP   A 1 105 ? 25.761 -8.389  -14.647 0.56 35.65 ?  105 ASP   A HB2  1 
ATOM   2145 H  HB2  B ASP   A 1 105 ? 24.934 -8.333  -15.025 0.44 36.68 ?  105 ASP   A HB2  1 
ATOM   2146 H  HB3  A ASP   A 1 105 ? 25.808 -8.799  -13.112 0.56 35.65 ?  105 ASP   A HB3  1 
ATOM   2147 H  HB3  B ASP   A 1 105 ? 25.646 -8.223  -13.609 0.44 36.68 ?  105 ASP   A HB3  1 
ATOM   2148 N  N    A ILE   A 1 106 ? 22.070 -8.514  -12.458 0.56 23.91 ?  106 ILE   A N    1 
ATOM   2149 N  N    B ILE   A 1 106 ? 21.864 -8.428  -12.282 0.44 26.28 ?  106 ILE   A N    1 
ATOM   2150 C  CA   A ILE   A 1 106 ? 21.286 -8.927  -11.299 0.56 23.45 ?  106 ILE   A CA   1 
ATOM   2151 C  CA   B ILE   A 1 106 ? 21.188 -8.864  -11.065 0.44 25.81 ?  106 ILE   A CA   1 
ATOM   2152 C  C    A ILE   A 1 106 ? 21.812 -10.220 -10.702 0.56 22.52 ?  106 ILE   A C    1 
ATOM   2153 C  C    B ILE   A 1 106 ? 21.738 -10.182 -10.536 0.44 24.96 ?  106 ILE   A C    1 
ATOM   2154 O  O    A ILE   A 1 106 ? 21.591 -10.485 -9.517  0.56 21.67 ?  106 ILE   A O    1 
ATOM   2155 O  O    B ILE   A 1 106 ? 21.558 -10.485 -9.351  0.44 24.46 ?  106 ILE   A O    1 
ATOM   2156 C  CB   A ILE   A 1 106 ? 19.783 -9.027  -11.651 0.56 24.59 ?  106 ILE   A CB   1 
ATOM   2157 C  CB   B ILE   A 1 106 ? 19.660 -8.912  -11.279 0.44 26.66 ?  106 ILE   A CB   1 
ATOM   2158 C  CG1  A ILE   A 1 106 ? 18.931 -9.058  -10.379 0.56 25.09 ?  106 ILE   A CG1  1 
ATOM   2159 C  CG1  B ILE   A 1 106 ? 18.924 -9.035  -9.940  0.44 27.25 ?  106 ILE   A CG1  1 
ATOM   2160 C  CG2  A ILE   A 1 106 ? 19.505 -10.269 -12.475 0.56 25.10 ?  106 ILE   A CG2  1 
ATOM   2161 C  CG2  B ILE   A 1 106 ? 19.280 -10.066 -12.193 0.44 26.97 ?  106 ILE   A CG2  1 
ATOM   2162 C  CD1  A ILE   A 1 106 ? 19.044 -7.810  -9.534  0.56 25.48 ?  106 ILE   A CD1  1 
ATOM   2163 C  CD1  B ILE   A 1 106 ? 19.274 -7.946  -8.947  0.44 27.60 ?  106 ILE   A CD1  1 
ATOM   2164 H  H    A ILE   A 1 106 ? 21.632 -8.483  -13.192 0.56 28.69 ?  106 ILE   A H    1 
ATOM   2165 H  H    B ILE   A 1 106 ? 21.372 -8.451  -12.982 0.44 31.54 ?  106 ILE   A H    1 
ATOM   2166 H  HA   A ILE   A 1 106 ? 21.385 -8.251  -10.618 0.56 28.14 ?  106 ILE   A HA   1 
ATOM   2167 H  HA   B ILE   A 1 106 ? 21.367 -8.207  -10.384 0.44 30.97 ?  106 ILE   A HA   1 
ATOM   2168 H  HB   A ILE   A 1 106 ? 19.536 -8.247  -12.171 0.56 29.51 ?  106 ILE   A HB   1 
ATOM   2169 H  HB   B ILE   A 1 106 ? 19.385 -8.085  -11.701 0.44 32.00 ?  106 ILE   A HB   1 
ATOM   2170 H  HG12 A ILE   A 1 106 ? 18.001 -9.159  -10.629 0.56 30.10 ?  106 ILE   A HG12 1 
ATOM   2171 H  HG12 B ILE   A 1 106 ? 17.967 -8.986  -10.102 0.44 32.70 ?  106 ILE   A HG12 1 
ATOM   2172 H  HG13 A ILE   A 1 106 ? 19.209 -9.810  -9.833  0.56 30.10 ?  106 ILE   A HG13 1 
ATOM   2173 H  HG13 B ILE   A 1 106 ? 19.143 -9.888  -9.535  0.44 32.70 ?  106 ILE   A HG13 1 
ATOM   2174 H  HG21 A ILE   A 1 106 ? 18.635 -10.178 -12.892 0.56 30.12 ?  106 ILE   A HG21 1 
ATOM   2175 H  HG21 B ILE   A 1 106 ? 18.354 -9.962  -12.462 0.44 32.36 ?  106 ILE   A HG21 1 
ATOM   2176 H  HG22 A ILE   A 1 106 ? 20.192 -10.354 -13.152 0.56 30.12 ?  106 ILE   A HG22 1 
ATOM   2177 H  HG22 B ILE   A 1 106 ? 19.855 -10.049 -12.973 0.44 32.36 ?  106 ILE   A HG22 1 
ATOM   2178 H  HG23 A ILE   A 1 106 ? 19.515 -11.043 -11.892 0.56 30.12 ?  106 ILE   A HG23 1 
ATOM   2179 H  HG23 B ILE   A 1 106 ? 19.394 -10.901 -11.714 0.44 32.36 ?  106 ILE   A HG23 1 
ATOM   2180 H  HD11 A ILE   A 1 106 ? 18.295 -7.777  -8.921  0.56 30.57 ?  106 ILE   A HD11 1 
ATOM   2181 H  HD11 B ILE   A 1 106 ? 18.588 -7.909  -8.265  0.44 33.12 ?  106 ILE   A HD11 1 
ATOM   2182 H  HD12 A ILE   A 1 106 ? 19.877 -7.838  -9.035  0.56 30.57 ?  106 ILE   A HD12 1 
ATOM   2183 H  HD12 B ILE   A 1 106 ? 20.132 -8.152  -8.542  0.44 33.12 ?  106 ILE   A HD12 1 
ATOM   2184 H  HD13 A ILE   A 1 106 ? 19.031 -7.033  -10.115 0.56 30.57 ?  106 ILE   A HD13 1 
ATOM   2185 H  HD13 B ILE   A 1 106 ? 19.323 -7.098  -9.415  0.44 33.12 ?  106 ILE   A HD13 1 
ATOM   2186 N  N    A GLN   A 1 107 ? 22.517 -11.035 -11.495 0.56 23.33 ?  107 GLN   A N    1 
ATOM   2187 N  N    B GLN   A 1 107 ? 22.416 -10.976 -11.372 0.44 25.41 ?  107 GLN   A N    1 
ATOM   2188 C  CA   A GLN   A 1 107 ? 23.129 -12.247 -10.965 0.56 25.44 ?  107 GLN   A CA   1 
ATOM   2189 C  CA   B GLN   A 1 107 ? 23.018 -12.207 -10.871 0.44 26.05 ?  107 GLN   A CA   1 
ATOM   2190 C  C    A GLN   A 1 107 ? 24.095 -11.939 -9.832  0.56 23.70 ?  107 GLN   A C    1 
ATOM   2191 C  C    B GLN   A 1 107 ? 24.068 -11.928 -9.805  0.44 23.86 ?  107 GLN   A C    1 
ATOM   2192 O  O    A GLN   A 1 107 ? 24.330 -12.801 -8.978  0.56 25.08 ?  107 GLN   A O    1 
ATOM   2193 O  O    B GLN   A 1 107 ? 24.349 -12.805 -8.981  0.44 24.97 ?  107 GLN   A O    1 
ATOM   2194 C  CB   A GLN   A 1 107 ? 23.850 -13.004 -12.088 0.56 29.28 ?  107 GLN   A CB   1 
ATOM   2195 C  CB   B GLN   A 1 107 ? 23.613 -13.035 -12.016 0.44 29.04 ?  107 GLN   A CB   1 
ATOM   2196 C  CG   A GLN   A 1 107 ? 22.984 -13.271 -13.314 0.56 33.05 ?  107 GLN   A CG   1 
ATOM   2197 C  CG   B GLN   A 1 107 ? 22.655 -13.278 -13.177 0.44 31.89 ?  107 GLN   A CG   1 
ATOM   2198 C  CD   A GLN   A 1 107 ? 21.761 -14.107 -12.995 0.56 36.17 ?  107 GLN   A CD   1 
ATOM   2199 C  CD   B GLN   A 1 107 ? 21.257 -13.656 -12.726 0.44 34.22 ?  107 GLN   A CD   1 
ATOM   2200 O  OE1  A GLN   A 1 107 ? 21.859 -15.151 -12.349 0.56 37.32 ?  107 GLN   A OE1  1 
ATOM   2201 O  OE1  B GLN   A 1 107 ? 21.079 -14.492 -11.840 0.44 35.12 ?  107 GLN   A OE1  1 
ATOM   2202 N  NE2  A GLN   A 1 107 ? 20.597 -13.649 -13.442 0.56 37.30 ?  107 GLN   A NE2  1 
ATOM   2203 N  NE2  B GLN   A 1 107 ? 20.253 -13.033 -13.336 0.44 34.90 ?  107 GLN   A NE2  1 
ATOM   2204 H  H    A GLN   A 1 107 ? 22.656 -10.907 -12.332 0.56 28.00 ?  107 GLN   A H    1 
ATOM   2205 H  H    B GLN   A 1 107 ? 22.540 -10.829 -12.209 0.44 30.49 ?  107 GLN   A H    1 
ATOM   2206 H  HA   A GLN   A 1 107 ? 22.443 -12.830 -10.613 0.56 30.52 ?  107 GLN   A HA   1 
ATOM   2207 H  HA   B GLN   A 1 107 ? 22.331 -12.743 -10.454 0.44 31.26 ?  107 GLN   A HA   1 
ATOM   2208 H  HB2  A GLN   A 1 107 ? 24.616 -12.486 -12.380 0.56 35.14 ?  107 GLN   A HB2  1 
ATOM   2209 H  HB2  B GLN   A 1 107 ? 24.390 -12.575 -12.369 0.44 34.85 ?  107 GLN   A HB2  1 
ATOM   2210 H  HB3  A GLN   A 1 107 ? 24.147 -13.865 -11.750 0.56 35.14 ?  107 GLN   A HB3  1 
ATOM   2211 H  HB3  B GLN   A 1 107 ? 23.878 -13.904 -11.670 0.44 34.85 ?  107 GLN   A HB3  1 
ATOM   2212 H  HG2  A GLN   A 1 107 ? 22.682 -12.427 -13.684 0.56 39.66 ?  107 GLN   A HG2  1 
ATOM   2213 H  HG2  B GLN   A 1 107 ? 22.586 -12.473 -13.708 0.44 38.27 ?  107 GLN   A HG2  1 
ATOM   2214 H  HG3  A GLN   A 1 107 ? 23.509 -13.750 -13.973 0.56 39.66 ?  107 GLN   A HG3  1 
ATOM   2215 H  HG3  B GLN   A 1 107 ? 22.998 -14.004 -13.722 0.44 38.27 ?  107 GLN   A HG3  1 
ATOM   2216 H  HE21 A GLN   A 1 107 ? 20.567 -12.914 -13.889 0.56 44.76 ?  107 GLN   A HE21 1 
ATOM   2217 H  HE21 B GLN   A 1 107 ? 20.417 -12.453 -13.949 0.44 41.88 ?  107 GLN   A HE21 1 
ATOM   2218 H  HE22 A GLN   A 1 107 ? 19.874 -14.087 -13.286 0.56 44.76 ?  107 GLN   A HE22 1 
ATOM   2219 H  HE22 B GLN   A 1 107 ? 19.440 -13.210 -13.118 0.44 41.88 ?  107 GLN   A HE22 1 
ATOM   2220 N  N    . LEU   A 1 108 ? 24.637 -10.721 -9.785  1.00 20.43 ?  108 LEU   A N    1 
ATOM   2221 C  CA   . LEU   A 1 108 ? 25.560 -10.348 -8.725  1.00 16.98 ?  108 LEU   A CA   1 
ATOM   2222 C  C    . LEU   A 1 108 ? 24.867 -10.204 -7.379  1.00 14.38 ?  108 LEU   A C    1 
ATOM   2223 O  O    . LEU   A 1 108 ? 25.556 -10.052 -6.368  1.00 14.29 ?  108 LEU   A O    1 
ATOM   2224 C  CB   . LEU   A 1 108 ? 26.300 -9.055  -9.093  1.00 16.53 ?  108 LEU   A CB   1 
ATOM   2225 C  CG   . LEU   A 1 108 ? 27.288 -9.240  -10.246 1.00 18.11 ?  108 LEU   A CG   1 
ATOM   2226 C  CD1  . LEU   A 1 108 ? 27.764 -7.895  -10.766 1.00 18.59 ?  108 LEU   A CD1  1 
ATOM   2227 C  CD2  . LEU   A 1 108 ? 28.468 -10.093 -9.804  1.00 20.12 ?  108 LEU   A CD2  1 
ATOM   2228 H  H    A LEU   A 1 108 ? 24.480 -10.098 -10.352 0.56 24.51 ?  108 LEU   A H    1 
ATOM   2229 H  H    B LEU   A 1 108 ? 24.506 -10.111 -10.372 0.44 24.51 ?  108 LEU   A H    1 
ATOM   2230 H  HA   . LEU   A 1 108 ? 26.222 -11.048 -8.628  1.00 20.37 ?  108 LEU   A HA   1 
ATOM   2231 H  HB2  . LEU   A 1 108 ? 25.650 -8.386  -9.363  1.00 19.84 ?  108 LEU   A HB2  1 
ATOM   2232 H  HB3  . LEU   A 1 108 ? 26.795 -8.743  -8.321  1.00 19.84 ?  108 LEU   A HB3  1 
ATOM   2233 H  HG   . LEU   A 1 108 ? 26.840 -9.704  -10.972 1.00 21.73 ?  108 LEU   A HG   1 
ATOM   2234 H  HD11 . LEU   A 1 108 ? 28.360 -8.042  -11.520 1.00 22.31 ?  108 LEU   A HD11 1 
ATOM   2235 H  HD12 . LEU   A 1 108 ? 26.998 -7.374  -11.048 1.00 22.31 ?  108 LEU   A HD12 1 
ATOM   2236 H  HD13 . LEU   A 1 108 ? 28.238 -7.432  -10.057 1.00 22.31 ?  108 LEU   A HD13 1 
ATOM   2237 H  HD21 . LEU   A 1 108 ? 29.162 -10.038 -10.475 1.00 24.14 ?  108 LEU   A HD21 1 
ATOM   2238 H  HD22 . LEU   A 1 108 ? 28.796 -9.757  -8.956  1.00 24.14 ?  108 LEU   A HD22 1 
ATOM   2239 H  HD23 . LEU   A 1 108 ? 28.174 -11.013 -9.703  1.00 24.14 ?  108 LEU   A HD23 1 
ATOM   2240 N  N    . LEU   A 1 109 ? 23.535 -10.262 -7.333  1.00 13.68 ?  109 LEU   A N    1 
ATOM   2241 C  CA   . LEU   A 1 109 ? 22.850 -10.133 -6.056  1.00 12.76 ?  109 LEU   A CA   1 
ATOM   2242 C  C    . LEU   A 1 109 ? 23.200 -11.283 -5.118  1.00 12.41 ?  109 LEU   A C    1 
ATOM   2243 O  O    . LEU   A 1 109 ? 23.337 -11.080 -3.907  1.00 12.78 ?  109 LEU   A O    1 
ATOM   2244 C  CB   . LEU   A 1 109 ? 21.345 -10.043 -6.296  1.00 13.58 ?  109 LEU   A CB   1 
ATOM   2245 C  CG   . LEU   A 1 109 ? 20.458 -9.753  -5.089  1.00 13.35 ?  109 LEU   A CG   1 
ATOM   2246 C  CD1  . LEU   A 1 109 ? 20.903 -8.482  -4.384  1.00 13.60 ?  109 LEU   A CD1  1 
ATOM   2247 C  CD2  . LEU   A 1 109 ? 19.002 -9.635  -5.530  1.00 14.61 ?  109 LEU   A CD2  1 
ATOM   2248 H  H    . LEU   A 1 109 ? 23.017 -10.369 -8.013  1.00 16.41 ?  109 LEU   A H    1 
ATOM   2249 H  HA   . LEU   A 1 109 ? 23.137 -9.308  -5.634  1.00 15.31 ?  109 LEU   A HA   1 
ATOM   2250 H  HB2  . LEU   A 1 109 ? 21.186 -9.332  -6.938  1.00 16.29 ?  109 LEU   A HB2  1 
ATOM   2251 H  HB3  . LEU   A 1 109 ? 21.047 -10.883 -6.671  1.00 16.29 ?  109 LEU   A HB3  1 
ATOM   2252 H  HG   . LEU   A 1 109 ? 20.521 -10.488 -4.461  1.00 16.02 ?  109 LEU   A HG   1 
ATOM   2253 H  HD11 . LEU   A 1 109 ? 20.224 -8.224  -3.740  1.00 16.32 ?  109 LEU   A HD11 1 
ATOM   2254 H  HD12 . LEU   A 1 109 ? 21.743 -8.647  -3.934  1.00 16.32 ?  109 LEU   A HD12 1 
ATOM   2255 H  HD13 . LEU   A 1 109 ? 21.011 -7.777  -5.045  1.00 16.32 ?  109 LEU   A HD13 1 
ATOM   2256 H  HD21 . LEU   A 1 109 ? 18.464 -9.348  -4.774  1.00 17.53 ?  109 LEU   A HD21 1 
ATOM   2257 H  HD22 . LEU   A 1 109 ? 18.938 -8.986  -6.246  1.00 17.53 ?  109 LEU   A HD22 1 
ATOM   2258 H  HD23 . LEU   A 1 109 ? 18.693 -10.503 -5.842  1.00 17.53 ?  109 LEU   A HD23 1 
ATOM   2259 N  N    . LYS   A 1 110 ? 23.345 -12.499 -5.650  1.00 12.08 ?  110 LYS   A N    1 
ATOM   2260 C  CA   . LYS   A 1 110 ? 23.719 -13.614 -4.786  1.00 12.21 ?  110 LYS   A CA   1 
ATOM   2261 C  C    . LYS   A 1 110 ? 25.102 -13.391 -4.184  1.00 11.84 ?  110 LYS   A C    1 
ATOM   2262 O  O    . LYS   A 1 110 ? 25.302 -13.584 -2.982  1.00 11.78 ?  110 LYS   A O    1 
ATOM   2263 C  CB   . LYS   A 1 110 ? 23.636 -14.940 -5.544  1.00 13.04 ?  110 LYS   A CB   1 
ATOM   2264 C  CG   . LYS   A 1 110 ? 23.843 -16.156 -4.635  1.00 12.96 ?  110 LYS   A CG   1 
ATOM   2265 C  CD   . LYS   A 1 110 ? 23.601 -17.473 -5.349  1.00 13.93 ?  110 LYS   A CD   1 
ATOM   2266 C  CE   . LYS   A 1 110 ? 23.723 -18.655 -4.397  1.00 14.46 ?  110 LYS   A CE   1 
ATOM   2267 N  NZ   . LYS   A 1 110 ? 22.533 -18.788 -3.517  1.00 14.94 ?  110 LYS   A NZ   1 
ATOM   2268 H  H    . LYS   A 1 110 ? 23.228 -12.700 -6.477  1.00 14.50 ?  110 LYS   A H    1 
ATOM   2269 H  HA   . LYS   A 1 110 ? 23.085 -13.662 -4.053  1.00 14.65 ?  110 LYS   A HA   1 
ATOM   2270 H  HB2  . LYS   A 1 110 ? 22.757 -15.019 -5.949  1.00 15.65 ?  110 LYS   A HB2  1 
ATOM   2271 H  HB3  . LYS   A 1 110 ? 24.321 -14.960 -6.227  1.00 15.65 ?  110 LYS   A HB3  1 
ATOM   2272 H  HG2  . LYS   A 1 110 ? 24.754 -16.154 -4.306  1.00 15.55 ?  110 LYS   A HG2  1 
ATOM   2273 H  HG3  . LYS   A 1 110 ? 23.222 -16.101 -3.889  1.00 15.55 ?  110 LYS   A HG3  1 
ATOM   2274 H  HD2  . LYS   A 1 110 ? 22.707 -17.478 -5.720  1.00 16.72 ?  110 LYS   A HD2  1 
ATOM   2275 H  HD3  . LYS   A 1 110 ? 24.261 -17.581 -6.050  1.00 16.72 ?  110 LYS   A HD3  1 
ATOM   2276 H  HE2  . LYS   A 1 110 ? 23.815 -19.472 -4.909  1.00 17.35 ?  110 LYS   A HE2  1 
ATOM   2277 H  HE3  . LYS   A 1 110 ? 24.502 -18.529 -3.828  1.00 17.35 ?  110 LYS   A HE3  1 
ATOM   2278 H  HZ1  . LYS   A 1 110 ? 22.627 -19.482 -2.974  1.00 17.93 ?  110 LYS   A HZ1  1 
ATOM   2279 H  HZ2  . LYS   A 1 110 ? 22.428 -18.049 -3.032  1.00 17.93 ?  110 LYS   A HZ2  1 
ATOM   2280 H  HZ3  . LYS   A 1 110 ? 21.802 -18.907 -4.017  1.00 17.93 ?  110 LYS   A HZ3  1 
ATOM   2281 N  N    . SER   A 1 111 ? 26.061 -12.954 -5.001  1.00 12.12 ?  111 SER   A N    1 
ATOM   2282 C  CA   . SER   A 1 111 ? 27.391 -12.645 -4.485  1.00 12.16 ?  111 SER   A CA   1 
ATOM   2283 C  C    . SER   A 1 111 ? 27.321 -11.597 -3.379  1.00 11.75 ?  111 SER   A C    1 
ATOM   2284 O  O    . SER   A 1 111 ? 28.013 -11.702 -2.360  1.00 12.11 ?  111 SER   A O    1 
ATOM   2285 C  CB   . SER   A 1 111 ? 28.277 -12.149 -5.627  1.00 13.34 ?  111 SER   A CB   1 
ATOM   2286 O  OG   . SER   A 1 111 ? 28.407 -13.154 -6.618  1.00 15.19 ?  111 SER   A OG   1 
ATOM   2287 H  H    . SER   A 1 111 ? 25.967 -12.831 -5.844  1.00 14.54 ?  111 SER   A H    1 
ATOM   2288 H  HA   . SER   A 1 111 ? 27.791 -13.451 -4.117  1.00 14.59 ?  111 SER   A HA   1 
ATOM   2289 H  HB2  . SER   A 1 111 ? 27.866 -11.368 -6.029  1.00 16.01 ?  111 SER   A HB2  1 
ATOM   2290 H  HB3  . SER   A 1 111 ? 29.151 -11.922 -5.275  1.00 16.01 ?  111 SER   A HB3  1 
ATOM   2291 H  HG   . SER   A 1 111 ? 28.912 -12.872 -7.239  1.00 18.22 ?  111 SER   A HG   1 
ATOM   2292 N  N    . ALA   A 1 112 ? 26.481 -10.578 -3.563  1.00 11.87 ?  112 ALA   A N    1 
ATOM   2293 C  CA   . ALA   A 1 112 ? 26.329 -9.541  -2.545  1.00 11.73 ?  112 ALA   A CA   1 
ATOM   2294 C  C    . ALA   A 1 112 ? 25.844 -10.137 -1.223  1.00 11.53 ?  112 ALA   A C    1 
ATOM   2295 O  O    . ALA   A 1 112 ? 26.394 -9.847  -0.154  1.00 11.71 ?  112 ALA   A O    1 
ATOM   2296 C  CB   . ALA   A 1 112 ? 25.372 -8.453  -3.043  1.00 12.03 ?  112 ALA   A CB   1 
ATOM   2297 H  H    . ALA   A 1 112 ? 25.999 -10.459 -4.261  1.00 14.24 ?  112 ALA   A H    1 
ATOM   2298 H  HA   . ALA   A 1 112 ? 27.187 -9.121  -2.383  1.00 14.07 ?  112 ALA   A HA   1 
ATOM   2299 H  HB1  . ALA   A 1 112 ? 25.290 -7.760  -2.362  1.00 14.43 ?  112 ALA   A HB1  1 
ATOM   2300 H  HB2  . ALA   A 1 112 ? 25.727 -8.063  -3.859  1.00 14.43 ?  112 ALA   A HB2  1 
ATOM   2301 H  HB3  . ALA   A 1 112 ? 24.501 -8.843  -3.216  1.00 14.43 ?  112 ALA   A HB3  1 
ATOM   2302 N  N    . TYR   A 1 113 ? 24.811 -10.984 -1.274  1.00 11.59 ?  113 TYR   A N    1 
ATOM   2303 C  CA   . TYR   A 1 113 ? 24.303 -11.590 -0.045  1.00 11.65 ?  113 TYR   A CA   1 
ATOM   2304 C  C    . TYR   A 1 113 ? 25.309 -12.538 0.606   1.00 11.14 ?  113 TYR   A C    1 
ATOM   2305 O  O    . TYR   A 1 113 ? 25.266 -12.722 1.827   1.00 11.71 ?  113 TYR   A O    1 
ATOM   2306 C  CB   . TYR   A 1 113 ? 22.988 -12.321 -0.310  1.00 11.87 ?  113 TYR   A CB   1 
ATOM   2307 C  CG   . TYR   A 1 113 ? 21.770 -11.427 -0.236  1.00 11.57 ?  113 TYR   A CG   1 
ATOM   2308 C  CD1  . TYR   A 1 113 ? 21.397 -10.833 0.968   1.00 11.78 ?  113 TYR   A CD1  1 
ATOM   2309 C  CD2  . TYR   A 1 113 ? 20.972 -11.207 -1.349  1.00 11.84 ?  113 TYR   A CD2  1 
ATOM   2310 C  CE1  . TYR   A 1 113 ? 20.268 -10.033 1.055   1.00 12.07 ?  113 TYR   A CE1  1 
ATOM   2311 C  CE2  . TYR   A 1 113 ? 19.822 -10.410 -1.268  1.00 11.99 ?  113 TYR   A CE2  1 
ATOM   2312 C  CZ   . TYR   A 1 113 ? 19.483 -9.829  -0.063  1.00 11.79 ?  113 TYR   A CZ   1 
ATOM   2313 O  OH   . TYR   A 1 113 ? 18.347 -9.046  0.041   1.00 12.43 ?  113 TYR   A OH   1 
ATOM   2314 H  H    . TYR   A 1 113 ? 24.401 -11.214 -1.993  1.00 13.91 ?  113 TYR   A H    1 
ATOM   2315 H  HA   . TYR   A 1 113 ? 24.127 -10.882 0.590   1.00 13.98 ?  113 TYR   A HA   1 
ATOM   2316 H  HB2  . TYR   A 1 113 ? 23.014 -12.704 -1.200  1.00 14.24 ?  113 TYR   A HB2  1 
ATOM   2317 H  HB3  . TYR   A 1 113 ? 22.884 -13.022 0.349   1.00 14.24 ?  113 TYR   A HB3  1 
ATOM   2318 H  HD1  . TYR   A 1 113 ? 21.918 -10.977 1.727   1.00 14.14 ?  113 TYR   A HD1  1 
ATOM   2319 H  HD2  . TYR   A 1 113 ? 21.196 -11.605 -2.156  1.00 14.20 ?  113 TYR   A HD2  1 
ATOM   2320 H  HE1  . TYR   A 1 113 ? 20.032 -9.648  1.870   1.00 14.48 ?  113 TYR   A HE1  1 
ATOM   2321 H  HE2  . TYR   A 1 113 ? 19.289 -10.263 -2.016  1.00 14.39 ?  113 TYR   A HE2  1 
ATOM   2322 H  HH   . TYR   A 1 113 ? 17.962 -9.003  -0.714  1.00 14.91 ?  113 TYR   A HH   1 
ATOM   2323 N  N    . GLU   A 1 114 ? 26.207 -13.155 -0.175  1.00 11.32 ?  114 GLU   A N    1 
ATOM   2324 C  CA   . GLU   A 1 114 ? 27.200 -14.055 0.417   1.00 11.40 ?  114 GLU   A CA   1 
ATOM   2325 C  C    . GLU   A 1 114 ? 28.052 -13.349 1.465   1.00 11.57 ?  114 GLU   A C    1 
ATOM   2326 O  O    . GLU   A 1 114 ? 28.529 -13.985 2.414   1.00 11.89 ?  114 GLU   A O    1 
ATOM   2327 C  CB   . GLU   A 1 114 ? 28.070 -14.693 -0.674  1.00 11.82 ?  114 GLU   A CB   1 
ATOM   2328 C  CG   . GLU   A 1 114 ? 27.304 -15.748 -1.455  1.00 12.23 ?  114 GLU   A CG   1 
ATOM   2329 C  CD   . GLU   A 1 114 ? 28.016 -16.284 -2.689  1.00 12.44 ?  114 GLU   A CD   1 
ATOM   2330 O  OE1  . GLU   A 1 114 ? 28.975 -15.663 -3.182  1.00 12.63 ?  114 GLU   A OE1  1 
ATOM   2331 O  OE2  . GLU   A 1 114 ? 27.570 -17.353 -3.174  1.00 13.67 -1 114 GLU   A OE2  1 
ATOM   2332 H  H    . GLU   A 1 114 ? 26.262 -13.069 -1.039  1.00 13.58 ?  114 GLU   A H    1 
ATOM   2333 H  HA   . GLU   A 1 114 ? 26.730 -14.768 0.860   1.00 13.68 ?  114 GLU   A HA   1 
ATOM   2334 H  HB2  . GLU   A 1 114 ? 28.359 -14.008 -1.302  1.00 14.19 ?  114 GLU   A HB2  1 
ATOM   2335 H  HB3  . GLU   A 1 114 ? 28.838 -15.117 -0.265  1.00 14.19 ?  114 GLU   A HB3  1 
ATOM   2336 H  HG2  . GLU   A 1 114 ? 27.133 -16.499 -0.863  1.00 14.68 ?  114 GLU   A HG2  1 
ATOM   2337 H  HG3  . GLU   A 1 114 ? 26.459 -15.365 -1.742  1.00 14.68 ?  114 GLU   A HG3  1 
ATOM   2338 N  N    . ASN   A 1 115 ? 28.235 -12.033 1.335   1.00 11.37 ?  115 ASN   A N    1 
ATOM   2339 C  CA   . ASN   A 1 115 ? 29.001 -11.304 2.342   1.00 11.69 ?  115 ASN   A CA   1 
ATOM   2340 C  C    . ASN   A 1 115 ? 28.388 -11.434 3.730   1.00 11.58 ?  115 ASN   A C    1 
ATOM   2341 O  O    . ASN   A 1 115 ? 29.101 -11.367 4.738   1.00 11.97 ?  115 ASN   A O    1 
ATOM   2342 C  CB   . ASN   A 1 115 ? 29.109 -9.824  1.965   1.00 11.73 ?  115 ASN   A CB   1 
ATOM   2343 C  CG   . ASN   A 1 115 ? 29.907 -9.601  0.700   1.00 12.33 ?  115 ASN   A CG   1 
ATOM   2344 O  OD1  . ASN   A 1 115 ? 31.128 -9.682  0.716   1.00 15.63 ?  115 ASN   A OD1  1 
ATOM   2345 N  ND2  . ASN   A 1 115 ? 29.231 -9.309  -0.394  1.00 11.84 ?  115 ASN   A ND2  1 
ATOM   2346 H  H    . ASN   A 1 115 ? 27.929 -11.542 0.692   1.00 13.64 ?  115 ASN   A H    1 
ATOM   2347 H  HA   . ASN   A 1 115 ? 29.899 -11.667 2.377   1.00 14.02 ?  115 ASN   A HA   1 
ATOM   2348 H  HB2  . ASN   A 1 115 ? 28.215 -9.468  1.832   1.00 14.08 ?  115 ASN   A HB2  1 
ATOM   2349 H  HB3  . ASN   A 1 115 ? 29.546 -9.346  2.692   1.00 14.08 ?  115 ASN   A HB3  1 
ATOM   2350 H  HD21 . ASN   A 1 115 ? 29.650 -9.169  -1.129  1.00 14.21 ?  115 ASN   A HD21 1 
ATOM   2351 H  HD22 . ASN   A 1 115 ? 28.372 -9.283  -0.373  1.00 14.21 ?  115 ASN   A HD22 1 
ATOM   2352 N  N    . PHE   A 1 116 ? 27.065 -11.599 3.806   1.00 11.59 ?  116 PHE   A N    1 
ATOM   2353 C  CA   . PHE   A 1 116 ? 26.417 -11.696 5.109   1.00 11.84 ?  116 PHE   A CA   1 
ATOM   2354 C  C    . PHE   A 1 116 ? 26.896 -12.925 5.878   1.00 11.85 ?  116 PHE   A C    1 
ATOM   2355 O  O    . PHE   A 1 116 ? 26.814 -12.949 7.108   1.00 12.32 ?  116 PHE   A O    1 
ATOM   2356 C  CB   . PHE   A 1 116 ? 24.891 -11.822 4.969   1.00 11.95 ?  116 PHE   A CB   1 
ATOM   2357 C  CG   . PHE   A 1 116 ? 24.137 -10.574 4.509   1.00 11.34 ?  116 PHE   A CG   1 
ATOM   2358 C  CD1  . PHE   A 1 116 ? 24.712 -9.548  3.773   1.00 11.43 ?  116 PHE   A CD1  1 
ATOM   2359 C  CD2  . PHE   A 1 116 ? 22.783 -10.475 4.816   1.00 11.99 ?  116 PHE   A CD2  1 
ATOM   2360 C  CE1  . PHE   A 1 116 ? 23.943 -8.470  3.356   1.00 11.58 ?  116 PHE   A CE1  1 
ATOM   2361 C  CE2  . PHE   A 1 116 ? 22.020 -9.401  4.409   1.00 12.50 ?  116 PHE   A CE2  1 
ATOM   2362 C  CZ   . PHE   A 1 116 ? 22.595 -8.397  3.680   1.00 11.67 ?  116 PHE   A CZ   1 
ATOM   2363 H  H    . PHE   A 1 116 ? 26.532 -11.652 3.130   1.00 13.90 ?  116 PHE   A H    1 
ATOM   2364 H  HA   . PHE   A 1 116 ? 26.612 -10.908 5.634   1.00 14.21 ?  116 PHE   A HA   1 
ATOM   2365 H  HB2  . PHE   A 1 116 ? 24.701 -12.524 4.324   1.00 14.34 ?  116 PHE   A HB2  1 
ATOM   2366 H  HB3  . PHE   A 1 116 ? 24.527 -12.076 5.831   1.00 14.34 ?  116 PHE   A HB3  1 
ATOM   2367 H  HD1  . PHE   A 1 116 ? 25.608 -9.597  3.546   1.00 13.71 ?  116 PHE   A HD1  1 
ATOM   2368 H  HD2  . PHE   A 1 116 ? 22.374 -11.162 5.298   1.00 14.39 ?  116 PHE   A HD2  1 
ATOM   2369 H  HE1  . PHE   A 1 116 ? 24.343 -7.783  2.871   1.00 13.89 ?  116 PHE   A HE1  1 
ATOM   2370 H  HE2  . PHE   A 1 116 ? 21.114 -9.362  4.630   1.00 15.00 ?  116 PHE   A HE2  1 
ATOM   2371 H  HZ   . PHE   A 1 116 ? 22.092 -7.663  3.412   1.00 14.00 ?  116 PHE   A HZ   1 
ATOM   2372 N  N    . ASN   A 1 117 ? 27.333 -13.979 5.175   1.00 12.03 ?  117 ASN   A N    1 
ATOM   2373 C  CA   . ASN   A 1 117 ? 27.698 -15.225 5.847   1.00 12.28 ?  117 ASN   A CA   1 
ATOM   2374 C  C    . ASN   A 1 117 ? 28.961 -15.110 6.676   1.00 12.85 ?  117 ASN   A C    1 
ATOM   2375 O  O    . ASN   A 1 117 ? 29.257 -16.033 7.443   1.00 13.84 ?  117 ASN   A O    1 
ATOM   2376 C  CB   . ASN   A 1 117 ? 27.811 -16.353 4.828   1.00 12.58 ?  117 ASN   A CB   1 
ATOM   2377 C  CG   . ASN   A 1 117 ? 26.459 -16.732 4.291   1.00 12.46 ?  117 ASN   A CG   1 
ATOM   2378 O  OD1  . ASN   A 1 117 ? 25.481 -16.751 5.042   1.00 13.46 ?  117 ASN   A OD1  1 
ATOM   2379 N  ND2  . ASN   A 1 117 ? 26.373 -16.995 3.002   1.00 12.57 ?  117 ASN   A ND2  1 
ATOM   2380 H  H    . ASN   A 1 117 ? 27.402 -14.005 4.312   1.00 14.44 ?  117 ASN   A H    1 
ATOM   2381 H  HA   . ASN   A 1 117 ? 26.973 -15.460 6.452   1.00 14.74 ?  117 ASN   A HA   1 
ATOM   2382 H  HB2  . ASN   A 1 117 ? 28.362 -16.062 4.084   1.00 15.09 ?  117 ASN   A HB2  1 
ATOM   2383 H  HB3  . ASN   A 1 117 ? 28.196 -17.132 5.252   1.00 15.09 ?  117 ASN   A HB3  1 
ATOM   2384 H  HD21 . ASN   A 1 117 ? 25.617 -17.213 2.661   1.00 15.08 ?  117 ASN   A HD21 1 
ATOM   2385 H  HD22 . ASN   A 1 117 ? 27.079 -16.967 2.512   1.00 15.08 ?  117 ASN   A HD22 1 
ATOM   2386 N  N    . GLN   A 1 118 ? 29.687 -14.000 6.559   1.00 12.67 ?  118 GLN   A N    1 
ATOM   2387 C  CA   . GLN   A 1 118 ? 30.870 -13.772 7.374   1.00 13.19 ?  118 GLN   A CA   1 
ATOM   2388 C  C    . GLN   A 1 118 ? 30.536 -13.200 8.747   1.00 13.08 ?  118 GLN   A C    1 
ATOM   2389 O  O    . GLN   A 1 118 ? 31.454 -12.914 9.526   1.00 14.58 ?  118 GLN   A O    1 
ATOM   2390 C  CB   . GLN   A 1 118 ? 31.860 -12.871 6.630   1.00 13.38 ?  118 GLN   A CB   1 
ATOM   2391 C  CG   . GLN   A 1 118 ? 32.332 -13.451 5.307   1.00 13.50 ?  118 GLN   A CG   1 
ATOM   2392 C  CD   . GLN   A 1 118 ? 33.156 -14.717 5.483   1.00 13.72 ?  118 GLN   A CD   1 
ATOM   2393 O  OE1  . GLN   A 1 118 ? 34.017 -14.793 6.371   1.00 14.86 ?  118 GLN   A OE1  1 
ATOM   2394 N  NE2  . GLN   A 1 118 ? 32.902 -15.715 4.633   1.00 13.86 ?  118 GLN   A NE2  1 
ATOM   2395 H  H    . GLN   A 1 118 ? 29.509 -13.357 6.008   1.00 15.21 ?  118 GLN   A H    1 
ATOM   2396 H  HA   . GLN   A 1 118 ? 31.302 -14.623 7.516   1.00 15.82 ?  118 GLN   A HA   1 
ATOM   2397 H  HB2  . GLN   A 1 118 ? 31.432 -12.020 6.446   1.00 16.05 ?  118 GLN   A HB2  1 
ATOM   2398 H  HB3  . GLN   A 1 118 ? 32.637 -12.737 7.191   1.00 16.05 ?  118 GLN   A HB3  1 
ATOM   2399 H  HG2  . GLN   A 1 118 ? 31.559 -13.664 4.756   1.00 16.20 ?  118 GLN   A HG2  1 
ATOM   2400 H  HG3  . GLN   A 1 118 ? 32.887 -12.798 4.854   1.00 16.20 ?  118 GLN   A HG3  1 
ATOM   2401 H  HE21 . GLN   A 1 118 ? 32.290 -15.624 4.024   1.00 16.63 ?  118 GLN   A HE21 1 
ATOM   2402 H  HE22 . GLN   A 1 118 ? 33.335 -16.454 4.685   1.00 16.63 ?  118 GLN   A HE22 1 
ATOM   2403 N  N    . HIS   A 1 119 ? 29.250 -13.047 9.067   1.00 12.93 ?  119 HIS   A N    1 
ATOM   2404 C  CA   . HIS   A 1 119 ? 28.808 -12.443 10.318  1.00 13.37 ?  119 HIS   A CA   1 
ATOM   2405 C  C    . HIS   A 1 119 ? 27.669 -13.267 10.891  1.00 13.66 ?  119 HIS   A C    1 
ATOM   2406 O  O    . HIS   A 1 119 ? 26.716 -13.587 10.178  1.00 14.03 ?  119 HIS   A O    1 
ATOM   2407 C  CB   . HIS   A 1 119 ? 28.353 -11.009 10.055  1.00 13.95 ?  119 HIS   A CB   1 
ATOM   2408 C  CG   . HIS   A 1 119 ? 29.431 -10.194 9.439   1.00 15.27 ?  119 HIS   A CG   1 
ATOM   2409 N  ND1  . HIS   A 1 119 ? 30.413 -9.595  10.191  1.00 17.39 ?  119 HIS   A ND1  1 
ATOM   2410 C  CD2  . HIS   A 1 119 ? 29.765 -9.993  8.144   1.00 15.87 ?  119 HIS   A CD2  1 
ATOM   2411 C  CE1  . HIS   A 1 119 ? 31.274 -9.002  9.385   1.00 17.39 ?  119 HIS   A CE1  1 
ATOM   2412 N  NE2  . HIS   A 1 119 ? 30.914 -9.242  8.138   1.00 17.31 ?  119 HIS   A NE2  1 
ATOM   2413 H  H    . HIS   A 1 119 ? 28.593 -13.305 8.566   1.00 15.52 ?  119 HIS   A H    1 
ATOM   2414 H  HA   . HIS   A 1 119 ? 29.543 -12.438 10.954  1.00 16.04 ?  119 HIS   A HA   1 
ATOM   2415 H  HB2  . HIS   A 1 119 ? 27.597 -11.026 9.448   1.00 16.74 ?  119 HIS   A HB2  1 
ATOM   2416 H  HB3  . HIS   A 1 119 ? 28.104 -10.601 10.896  1.00 16.74 ?  119 HIS   A HB3  1 
ATOM   2417 H  HD1  . HIS   A 1 119 ? 30.446 -9.585  11.049  1.00 20.87 ?  119 HIS   A HD1  1 
ATOM   2418 H  HD2  . HIS   A 1 119 ? 29.301 -10.305 7.398   1.00 19.04 ?  119 HIS   A HD2  1 
ATOM   2419 H  HE1  . HIS   A 1 119 ? 32.014 -8.505  9.649   1.00 20.86 ?  119 HIS   A HE1  1 
ATOM   2420 N  N    . GLU   A 1 120 ? 27.752 -13.585 12.181  1.00 14.92 ?  120 GLU   A N    1 
ATOM   2421 C  CA   . GLU   A 1 120 ? 26.789 -14.517 12.767  1.00 17.48 ?  120 GLU   A CA   1 
ATOM   2422 C  C    . GLU   A 1 120 ? 25.376 -13.943 12.848  1.00 15.61 ?  120 GLU   A C    1 
ATOM   2423 O  O    . GLU   A 1 120 ? 24.400 -14.702 12.742  1.00 15.56 ?  120 GLU   A O    1 
ATOM   2424 C  CB   . GLU   A 1 120 ? 27.259 -14.959 14.153  1.00 23.00 ?  120 GLU   A CB   1 
ATOM   2425 C  CG   . GLU   A 1 120 ? 28.455 -15.899 14.134  1.00 30.87 ?  120 GLU   A CG   1 
ATOM   2426 C  CD   . GLU   A 1 120 ? 28.660 -16.603 15.459  1.00 38.43 ?  120 GLU   A CD   1 
ATOM   2427 O  OE1  . GLU   A 1 120 ? 28.141 -16.110 16.483  1.00 40.20 ?  120 GLU   A OE1  1 
ATOM   2428 O  OE2  . GLU   A 1 120 ? 29.337 -17.653 15.475  1.00 42.11 -1 120 GLU   A OE2  1 
ATOM   2429 H  H    . GLU   A 1 120 ? 28.359 -13.298 12.722  1.00 17.91 ?  120 GLU   A H    1 
ATOM   2430 H  HA   . GLU   A 1 120 ? 26.751 -15.309 12.213  1.00 20.97 ?  120 GLU   A HA   1 
ATOM   2431 H  HB2  . GLU   A 1 120 ? 27.514 -14.182 14.671  1.00 27.60 ?  120 GLU   A HB2  1 
ATOM   2432 H  HB3  . GLU   A 1 120 ? 26.534 -15.427 14.599  1.00 27.60 ?  120 GLU   A HB3  1 
ATOM   2433 H  HG2  . GLU   A 1 120 ? 28.324 -16.570 13.445  1.00 37.04 ?  120 GLU   A HG2  1 
ATOM   2434 H  HG3  . GLU   A 1 120 ? 29.260 -15.391 13.957  1.00 37.04 ?  120 GLU   A HG3  1 
ATOM   2435 N  N    . VAL   A 1 121 ? 25.250 -12.635 13.077  1.00 14.72 ?  121 VAL   A N    1 
ATOM   2436 C  CA   . VAL   A 1 121 ? 23.961 -11.959 13.206  1.00 14.81 ?  121 VAL   A CA   1 
ATOM   2437 C  C    . VAL   A 1 121 ? 24.077 -10.583 12.560  1.00 13.59 ?  121 VAL   A C    1 
ATOM   2438 O  O    . VAL   A 1 121 ? 25.054 -9.864  12.792  1.00 14.17 ?  121 VAL   A O    1 
ATOM   2439 C  CB   . VAL   A 1 121 ? 23.543 -11.795 14.685  1.00 17.50 ?  121 VAL   A CB   1 
ATOM   2440 C  CG1  . VAL   A 1 121 ? 22.167 -11.144 14.786  1.00 17.98 ?  121 VAL   A CG1  1 
ATOM   2441 C  CG2  . VAL   A 1 121 ? 23.560 -13.123 15.418  1.00 19.35 ?  121 VAL   A CG2  1 
ATOM   2442 H  H    . VAL   A 1 121 ? 25.923 -12.099 13.161  1.00 17.67 ?  121 VAL   A H    1 
ATOM   2443 H  HA   . VAL   A 1 121 ? 23.281 -12.470 12.742  1.00 17.77 ?  121 VAL   A HA   1 
ATOM   2444 H  HB   . VAL   A 1 121 ? 24.178 -11.210 15.123  1.00 20.99 ?  121 VAL   A HB   1 
ATOM   2445 H  HG11 . VAL   A 1 121 ? 21.860 -11.194 15.705  1.00 21.57 ?  121 VAL   A HG11 1 
ATOM   2446 H  HG12 . VAL   A 1 121 ? 22.232 -10.214 14.513  1.00 21.57 ?  121 VAL   A HG12 1 
ATOM   2447 H  HG13 . VAL   A 1 121 ? 21.548 -11.615 14.206  1.00 21.57 ?  121 VAL   A HG13 1 
ATOM   2448 H  HG21 . VAL   A 1 121 ? 23.224 -12.988 16.322  1.00 23.22 ?  121 VAL   A HG21 1 
ATOM   2449 H  HG22 . VAL   A 1 121 ? 22.987 -13.752 14.949  1.00 23.22 ?  121 VAL   A HG22 1 
ATOM   2450 H  HG23 . VAL   A 1 121 ? 24.466 -13.459 15.451  1.00 23.22 ?  121 VAL   A HG23 1 
ATOM   2451 N  N    . LEU   A 1 122 ? 23.065 -10.192 11.778  1.00 12.86 ?  122 LEU   A N    1 
ATOM   2452 C  CA   . LEU   A 1 122 ? 23.066 -8.892  11.113  1.00 12.43 ?  122 LEU   A CA   1 
ATOM   2453 C  C    . LEU   A 1 122 ? 21.673 -8.289  11.071  1.00 12.26 ?  122 LEU   A C    1 
ATOM   2454 O  O    . LEU   A 1 122 ? 20.680 -9.005  10.933  1.00 13.45 ?  122 LEU   A O    1 
ATOM   2455 C  CB   . LEU   A 1 122 ? 23.488 -8.982  9.644   1.00 13.88 ?  122 LEU   A CB   1 
ATOM   2456 C  CG   . LEU   A 1 122 ? 24.689 -9.840  9.270   1.00 13.88 ?  122 LEU   A CG   1 
ATOM   2457 C  CD1  . LEU   A 1 122 ? 24.278 -11.286 9.031   1.00 14.60 ?  122 LEU   A CD1  1 
ATOM   2458 C  CD2  . LEU   A 1 122 ? 25.374 -9.259  8.046   1.00 13.46 ?  122 LEU   A CD2  1 
ATOM   2459 H  H    . LEU   A 1 122 ? 22.362 -10.663 11.619  1.00 15.43 ?  122 LEU   A H    1 
ATOM   2460 H  HA   . LEU   A 1 122 ? 23.661 -8.280  11.577  1.00 14.92 ?  122 LEU   A HA   1 
ATOM   2461 H  HB2  . LEU   A 1 122 ? 22.741 -9.327  9.140   1.00 16.66 ?  122 LEU   A HB2  1 
ATOM   2462 H  HB3  . LEU   A 1 122 ? 23.693 -8.086  9.338   1.00 16.66 ?  122 LEU   A HB3  1 
ATOM   2463 H  HG   . LEU   A 1 122 ? 25.333 -9.834  9.997   1.00 16.65 ?  122 LEU   A HG   1 
ATOM   2464 H  HD11 . LEU   A 1 122 ? 25.055 -11.800 8.756   1.00 17.53 ?  122 LEU   A HD11 1 
ATOM   2465 H  HD12 . LEU   A 1 122 ? 23.918 -11.654 9.854   1.00 17.53 ?  122 LEU   A HD12 1 
ATOM   2466 H  HD13 . LEU   A 1 122 ? 23.603 -11.313 8.335   1.00 17.53 ?  122 LEU   A HD13 1 
ATOM   2467 H  HD21 . LEU   A 1 122 ? 26.111 -9.835  7.780   1.00 16.15 ?  122 LEU   A HD21 1 
ATOM   2468 H  HD22 . LEU   A 1 122 ? 24.732 -9.193  7.321   1.00 16.15 ?  122 LEU   A HD22 1 
ATOM   2469 H  HD23 . LEU   A 1 122 ? 25.715 -8.374  8.262   1.00 16.15 ?  122 LEU   A HD23 1 
ATOM   2470 N  N    A LEU   A 1 123 ? 21.620 -6.964  11.157  0.56 12.12 ?  123 LEU   A N    1 
ATOM   2471 N  N    B LEU   A 1 123 ? 21.620 -6.963  11.210  0.44 11.93 ?  123 LEU   A N    1 
ATOM   2472 C  CA   A LEU   A 1 123 ? 20.460 -6.172  10.764  0.56 11.69 ?  123 LEU   A CA   1 
ATOM   2473 C  CA   B LEU   A 1 123 ? 20.450 -6.152  10.895  0.44 11.57 ?  123 LEU   A CA   1 
ATOM   2474 C  C    A LEU   A 1 123 ? 20.711 -5.664  9.351   0.56 11.11 ?  123 LEU   A C    1 
ATOM   2475 C  C    B LEU   A 1 123 ? 20.678 -5.584  9.502   0.44 10.74 ?  123 LEU   A C    1 
ATOM   2476 O  O    A LEU   A 1 123 ? 21.806 -5.170  9.066   0.56 10.95 ?  123 LEU   A O    1 
ATOM   2477 O  O    B LEU   A 1 123 ? 21.652 -4.855  9.289   0.44 10.84 ?  123 LEU   A O    1 
ATOM   2478 C  CB   A LEU   A 1 123 ? 20.317 -4.980  11.709  0.56 12.01 ?  123 LEU   A CB   1 
ATOM   2479 C  CB   B LEU   A 1 123 ? 20.320 -5.009  11.905  0.44 12.05 ?  123 LEU   A CB   1 
ATOM   2480 C  CG   A LEU   A 1 123 ? 19.240 -3.949  11.369  0.56 12.73 ?  123 LEU   A CG   1 
ATOM   2481 C  CG   B LEU   A 1 123 ? 19.352 -3.876  11.541  0.44 12.29 ?  123 LEU   A CG   1 
ATOM   2482 C  CD1  A LEU   A 1 123 ? 17.872 -4.601  11.371  0.56 13.34 ?  123 LEU   A CD1  1 
ATOM   2483 C  CD1  B LEU   A 1 123 ? 17.911 -4.368  11.498  0.44 12.77 ?  123 LEU   A CD1  1 
ATOM   2484 C  CD2  A LEU   A 1 123 ? 19.290 -2.775  12.344  0.56 13.28 ?  123 LEU   A CD2  1 
ATOM   2485 C  CD2  B LEU   A 1 123 ? 19.497 -2.699  12.494  0.44 12.57 ?  123 LEU   A CD2  1 
ATOM   2486 H  H    A LEU   A 1 123 ? 22.274 -6.488  11.453  0.56 14.55 ?  123 LEU   A H    1 
ATOM   2487 H  H    B LEU   A 1 123 ? 22.286 -6.490  11.481  0.44 14.31 ?  123 LEU   A H    1 
ATOM   2488 H  HA   A LEU   A 1 123 ? 19.659 -6.717  10.780  0.56 14.03 ?  123 LEU   A HA   1 
ATOM   2489 H  HA   B LEU   A 1 123 ? 19.642 -6.683  10.898  0.44 13.89 ?  123 LEU   A HA   1 
ATOM   2490 H  HB2  A LEU   A 1 123 ? 20.109 -5.322  12.592  0.56 14.41 ?  123 LEU   A HB2  1 
ATOM   2491 H  HB2  B LEU   A 1 123 ? 20.012 -5.383  12.748  0.44 14.46 ?  123 LEU   A HB2  1 
ATOM   2492 H  HB3  A LEU   A 1 123 ? 21.162 -4.513  11.735  0.56 14.41 ?  123 LEU   A HB3  1 
ATOM   2493 H  HB3  B LEU   A 1 123 ? 21.192 -4.608  12.033  0.44 14.46 ?  123 LEU   A HB3  1 
ATOM   2494 H  HG   A LEU   A 1 123 ? 19.405 -3.598  10.479  0.56 15.28 ?  123 LEU   A HG   1 
ATOM   2495 H  HG   B LEU   A 1 123 ? 19.570 -3.544  10.658  0.44 14.75 ?  123 LEU   A HG   1 
ATOM   2496 H  HD11 A LEU   A 1 123 ? 17.199 -3.916  11.253  0.56 16.00 ?  123 LEU   A HD11 1 
ATOM   2497 H  HD11 B LEU   A 1 123 ? 17.329 -3.625  11.275  0.44 15.33 ?  123 LEU   A HD11 1 
ATOM   2498 H  HD12 A LEU   A 1 123 ? 17.830 -5.240  10.644  0.56 16.00 ?  123 LEU   A HD12 1 
ATOM   2499 H  HD12 B LEU   A 1 123 ? 17.836 -5.061  10.822  0.44 15.33 ?  123 LEU   A HD12 1 
ATOM   2500 H  HD13 A LEU   A 1 123 ? 17.744 -5.053  12.220  0.56 16.00 ?  123 LEU   A HD13 1 
ATOM   2501 H  HD13 B LEU   A 1 123 ? 17.673 -4.727  12.367  0.44 15.33 ?  123 LEU   A HD13 1 
ATOM   2502 H  HD21 A LEU   A 1 123 ? 18.600 -2.134  12.108  0.56 15.94 ?  123 LEU   A HD21 1 
ATOM   2503 H  HD21 B LEU   A 1 123 ? 18.871 -2.005  12.232  0.44 15.08 ?  123 LEU   A HD21 1 
ATOM   2504 H  HD22 A LEU   A 1 123 ? 19.136 -3.105  13.246  0.56 15.94 ?  123 LEU   A HD22 1 
ATOM   2505 H  HD22 B LEU   A 1 123 ? 19.300 -2.999  13.395  0.44 15.08 ?  123 LEU   A HD22 1 
ATOM   2506 H  HD23 A LEU   A 1 123 ? 20.163 -2.354  12.295  0.56 15.94 ?  123 LEU   A HD23 1 
ATOM   2507 H  HD23 B LEU   A 1 123 ? 20.404 -2.364  12.444  0.44 15.08 ?  123 LEU   A HD23 1 
ATOM   2508 N  N    A ALA   A 1 124 ? 19.710 -5.753  8.471   0.56 10.85 ?  124 ALA   A N    1 
ATOM   2509 N  N    B ALA   A 1 124 ? 19.802 -5.910  8.559   0.44 10.64 ?  124 ALA   A N    1 
ATOM   2510 C  CA   A ALA   A 1 124 ? 19.997 -5.502  7.065   0.56 10.72 ?  124 ALA   A CA   1 
ATOM   2511 C  CA   B ALA   A 1 124 ? 20.060 -5.605  7.161   0.44 10.95 ?  124 ALA   A CA   1 
ATOM   2512 C  C    A ALA   A 1 124 ? 18.749 -5.096  6.291   0.56 10.46 ?  124 ALA   A C    1 
ATOM   2513 C  C    B ALA   A 1 124 ? 18.834 -5.051  6.456   0.44 10.76 ?  124 ALA   A C    1 
ATOM   2514 O  O    A ALA   A 1 124 ? 17.629 -5.489  6.652   0.56 10.68 ?  124 ALA   A O    1 
ATOM   2515 O  O    B ALA   A 1 124 ? 17.694 -5.302  6.867   0.44 11.56 ?  124 ALA   A O    1 
ATOM   2516 C  CB   A ALA   A 1 124 ? 20.622 -6.741  6.414   0.56 11.49 ?  124 ALA   A CB   1 
ATOM   2517 C  CB   B ALA   A 1 124 ? 20.529 -6.850  6.398   0.44 11.37 ?  124 ALA   A CB   1 
ATOM   2518 H  H    A ALA   A 1 124 ? 18.897 -5.936  8.664   0.56 13.02 ?  124 ALA   A H    1 
ATOM   2519 H  H    B ALA   A 1 124 ? 19.060 -6.313  8.701   0.44 12.77 ?  124 ALA   A H    1 
ATOM   2520 H  HA   A ALA   A 1 124 ? 20.642 -4.780  7.012   0.56 12.86 ?  124 ALA   A HA   1 
ATOM   2521 H  HA   B ALA   A 1 124 ? 20.766 -4.943  7.114   0.44 13.15 ?  124 ALA   A HA   1 
ATOM   2522 H  HB1  A ALA   A 1 124 ? 20.807 -6.552  5.480   0.56 13.79 ?  124 ALA   A HB1  1 
ATOM   2523 H  HB1  B ALA   A 1 124 ? 20.689 -6.611  5.470   0.44 13.65 ?  124 ALA   A HB1  1 
ATOM   2524 H  HB2  A ALA   A 1 124 ? 21.455 -6.956  6.873   0.56 13.79 ?  124 ALA   A HB2  1 
ATOM   2525 H  HB2  B ALA   A 1 124 ? 21.353 -7.173  6.799   0.44 13.65 ?  124 ALA   A HB2  1 
ATOM   2526 H  HB3  A ALA   A 1 124 ? 20.008 -7.485  6.487   0.56 13.79 ?  124 ALA   A HB3  1 
ATOM   2527 H  HB3  B ALA   A 1 124 ? 19.844 -7.531  6.452   0.44 13.65 ?  124 ALA   A HB3  1 
ATOM   2528 N  N    A PRO   A 1 125 ? 18.921 -4.346  5.203   0.56 10.77 ?  125 PRO   A N    1 
ATOM   2529 N  N    B PRO   A 1 125 ? 19.046 -4.304  5.359   0.44 9.99  ?  125 PRO   A N    1 
ATOM   2530 C  CA   A PRO   A 1 125 ? 17.851 -4.132  4.230   0.56 10.75 ?  125 PRO   A CA   1 
ATOM   2531 C  CA   B PRO   A 1 125 ? 17.953 -3.942  4.458   0.44 10.32 ?  125 PRO   A CA   1 
ATOM   2532 C  C    A PRO   A 1 125 ? 17.926 -5.188  3.135   0.56 10.41 ?  125 PRO   A C    1 
ATOM   2533 C  C    B PRO   A 1 125 ? 17.846 -4.988  3.364   0.44 11.07 ?  125 PRO   A C    1 
ATOM   2534 O  O    A PRO   A 1 125 ? 18.905 -5.926  3.009   0.56 10.39 ?  125 PRO   A O    1 
ATOM   2535 O  O    B PRO   A 1 125 ? 18.685 -5.893  3.288   0.44 11.49 ?  125 PRO   A O    1 
ATOM   2536 C  CB   A PRO   A 1 125 ? 18.236 -2.773  3.640   0.56 11.18 ?  125 PRO   A CB   1 
ATOM   2537 C  CB   B PRO   A 1 125 ? 18.444 -2.614  3.878   0.44 10.11 ?  125 PRO   A CB   1 
ATOM   2538 C  CG   A PRO   A 1 125 ? 19.742 -2.870  3.563   0.56 11.33 ?  125 PRO   A CG   1 
ATOM   2539 C  CG   B PRO   A 1 125 ? 19.939 -2.883  3.698   0.44 9.85  ?  125 PRO   A CG   1 
ATOM   2540 C  CD   A PRO   A 1 125 ? 20.148 -3.617  4.821   0.56 11.23 ?  125 PRO   A CD   1 
ATOM   2541 C  CD   B PRO   A 1 125 ? 20.338 -3.797  4.856   0.44 9.91  ?  125 PRO   A CD   1 
ATOM   2542 H  HA   A PRO   A 1 125 ? 16.975 -4.115  4.646   0.56 12.90 ?  125 PRO   A HA   1 
ATOM   2543 H  HA   B PRO   A 1 125 ? 17.110 -3.831  4.927   0.44 12.39 ?  125 PRO   A HA   1 
ATOM   2544 H  HB2  A PRO   A 1 125 ? 17.842 -2.673  2.759   0.56 13.42 ?  125 PRO   A HB2  1 
ATOM   2545 H  HB2  B PRO   A 1 125 ? 18.008 -2.436  3.027   0.44 12.13 ?  125 PRO   A HB2  1 
ATOM   2546 H  HB3  A PRO   A 1 125 ? 17.956 -2.066  4.237   0.56 13.42 ?  125 PRO   A HB3  1 
ATOM   2547 H  HB3  B PRO   A 1 125 ? 18.287 -1.888  4.508   0.44 12.13 ?  125 PRO   A HB3  1 
ATOM   2548 H  HG2  A PRO   A 1 125 ? 19.997 -3.372  2.771   0.56 13.59 ?  125 PRO   A HG2  1 
ATOM   2549 H  HG2  B PRO   A 1 125 ? 20.088 -3.329  2.848   0.44 11.82 ?  125 PRO   A HG2  1 
ATOM   2550 H  HG3  A PRO   A 1 125 ? 20.124 -1.983  3.548   0.56 13.59 ?  125 PRO   A HG3  1 
ATOM   2551 H  HG3  B PRO   A 1 125 ? 20.429 -2.049  3.736   0.44 11.82 ?  125 PRO   A HG3  1 
ATOM   2552 H  HD2  A PRO   A 1 125 ? 20.872 -4.233  4.633   0.56 13.47 ?  125 PRO   A HD2  1 
ATOM   2553 H  HD2  B PRO   A 1 125 ? 20.888 -4.526  4.532   0.44 11.89 ?  125 PRO   A HD2  1 
ATOM   2554 H  HD3  A PRO   A 1 125 ? 20.390 -2.988  5.521   0.56 13.47 ?  125 PRO   A HD3  1 
ATOM   2555 H  HD3  B PRO   A 1 125 ? 20.796 -3.283  5.540   0.44 11.89 ?  125 PRO   A HD3  1 
ATOM   2556 N  N    A LEU   A 1 126 ? 16.876 -5.226  2.319   0.56 10.81 ?  126 LEU   A N    1 
ATOM   2557 N  N    B LEU   A 1 126 ? 16.846 -4.860  2.497   0.44 12.00 ?  126 LEU   A N    1 
ATOM   2558 C  CA   A LEU   A 1 126 ? 16.888 -6.043  1.113   0.56 10.85 ?  126 LEU   A CA   1 
ATOM   2559 C  CA   B LEU   A 1 126 ? 16.700 -5.746  1.345   0.44 12.75 ?  126 LEU   A CA   1 
ATOM   2560 C  C    A LEU   A 1 126 ? 17.807 -5.414  0.072   0.56 11.08 ?  126 LEU   A C    1 
ATOM   2561 C  C    B LEU   A 1 126 ? 17.606 -5.250  0.224   0.44 12.43 ?  126 LEU   A C    1 
ATOM   2562 O  O    A LEU   A 1 126 ? 17.569 -4.291  -0.388  0.56 12.04 ?  126 LEU   A O    1 
ATOM   2563 O  O    B LEU   A 1 126 ? 17.345 -4.202  -0.375  0.44 13.34 ?  126 LEU   A O    1 
ATOM   2564 C  CB   A LEU   A 1 126 ? 15.477 -6.167  0.559   0.56 11.29 ?  126 LEU   A CB   1 
ATOM   2565 C  CB   B LEU   A 1 126 ? 15.243 -5.746  0.897   0.44 14.62 ?  126 LEU   A CB   1 
ATOM   2566 C  CG   A LEU   A 1 126 ? 14.555 -7.077  1.369   0.56 11.81 ?  126 LEU   A CG   1 
ATOM   2567 C  CG   B LEU   A 1 126 ? 14.743 -6.831  -0.056  0.44 15.88 ?  126 LEU   A CG   1 
ATOM   2568 C  CD1  A LEU   A 1 126 ? 13.127 -6.933  0.881   0.56 13.20 ?  126 LEU   A CD1  1 
ATOM   2569 C  CD1  B LEU   A 1 126 ? 14.889 -8.203  0.565   0.44 16.01 ?  126 LEU   A CD1  1 
ATOM   2570 C  CD2  A LEU   A 1 126 ? 15.007 -8.530  1.271   0.56 11.99 ?  126 LEU   A CD2  1 
ATOM   2571 C  CD2  B LEU   A 1 126 ? 13.289 -6.568  -0.417  0.44 16.24 ?  126 LEU   A CD2  1 
ATOM   2572 H  H    A LEU   A 1 126 ? 16.152 -4.784  2.435   0.56 12.98 ?  126 LEU   A H    1 
ATOM   2573 H  H    B LEU   A 1 126 ? 16.228 -4.259  2.556   0.44 14.40 ?  126 LEU   A H    1 
ATOM   2574 H  HA   A LEU   A 1 126 ? 17.224 -6.930  1.320   0.56 13.01 ?  126 LEU   A HA   1 
ATOM   2575 H  HA   B LEU   A 1 126 ? 16.965 -6.644  1.590   0.44 15.30 ?  126 LEU   A HA   1 
ATOM   2576 H  HB2  A LEU   A 1 126 ? 15.074 -5.286  0.537   0.56 13.55 ?  126 LEU   A HB2  1 
ATOM   2577 H  HB2  B LEU   A 1 126 ? 14.698 -5.806  1.691   0.44 17.55 ?  126 LEU   A HB2  1 
ATOM   2578 H  HB3  A LEU   A 1 126 ? 15.525 -6.527  -0.340  0.56 13.55 ?  126 LEU   A HB3  1 
ATOM   2579 H  HB3  B LEU   A 1 126 ? 15.075 -4.896  0.461   0.44 17.55 ?  126 LEU   A HB3  1 
ATOM   2580 H  HG   A LEU   A 1 126 ? 14.577 -6.812  2.301   0.56 14.17 ?  126 LEU   A HG   1 
ATOM   2581 H  HG   B LEU   A 1 126 ? 15.267 -6.804  -0.875  0.44 19.06 ?  126 LEU   A HG   1 
ATOM   2582 H  HD11 A LEU   A 1 126 ? 12.552 -7.518  1.404   0.56 15.84 ?  126 LEU   A HD11 1 
ATOM   2583 H  HD11 B LEU   A 1 126 ? 14.460 -8.854  -0.010  0.44 19.21 ?  126 LEU   A HD11 1 
ATOM   2584 H  HD12 A LEU   A 1 126 ? 12.844 -6.012  0.987   0.56 15.84 ?  126 LEU   A HD12 1 
ATOM   2585 H  HD12 B LEU   A 1 126 ? 15.831 -8.409  0.657   0.44 19.21 ?  126 LEU   A HD12 1 
ATOM   2586 H  HD13 A LEU   A 1 126 ? 13.085 -7.186  -0.056  0.56 15.84 ?  126 LEU   A HD13 1 
ATOM   2587 H  HD13 B LEU   A 1 126 ? 14.462 -8.198  1.436   0.44 19.21 ?  126 LEU   A HD13 1 
ATOM   2588 H  HD21 A LEU   A 1 126 ? 14.322 -9.101  1.654   0.56 14.39 ?  126 LEU   A HD21 1 
ATOM   2589 H  HD21 B LEU   A 1 126 ? 12.985 -7.262  -1.023  0.44 19.48 ?  126 LEU   A HD21 1 
ATOM   2590 H  HD22 A LEU   A 1 126 ? 15.141 -8.756  0.337   0.56 14.39 ?  126 LEU   A HD22 1 
ATOM   2591 H  HD22 B LEU   A 1 126 ? 12.757 -6.581  0.394   0.44 19.48 ?  126 LEU   A HD22 1 
ATOM   2592 H  HD23 A LEU   A 1 126 ? 15.837 -8.635  1.760   0.56 14.39 ?  126 LEU   A HD23 1 
ATOM   2593 H  HD23 B LEU   A 1 126 ? 13.218 -5.700  -0.845  0.44 19.48 ?  126 LEU   A HD23 1 
ATOM   2594 N  N    A LEU   A 1 127 ? 18.852 -6.142  -0.306  0.56 10.77 ?  127 LEU   A N    1 
ATOM   2595 N  N    B LEU   A 1 127 ? 18.662 -6.005  -0.078  0.44 12.19 ?  127 LEU   A N    1 
ATOM   2596 C  CA   A LEU   A 1 127 ? 19.834 -5.618  -1.242  0.56 10.39 ?  127 LEU   A CA   1 
ATOM   2597 C  CA   B LEU   A 1 127 ? 19.662 -5.531  -1.026  0.44 12.38 ?  127 LEU   A CA   1 
ATOM   2598 C  C    A LEU   A 1 127 ? 19.221 -5.437  -2.623  0.56 9.99  ?  127 LEU   A C    1 
ATOM   2599 C  C    B LEU   A 1 127 ? 19.064 -5.353  -2.413  0.44 11.81 ?  127 LEU   A C    1 
ATOM   2600 O  O    A LEU   A 1 127 ? 18.403 -6.243  -3.079  0.56 10.16 ?  127 LEU   A O    1 
ATOM   2601 O  O    B LEU   A 1 127 ? 18.196 -6.118  -2.844  0.44 12.46 ?  127 LEU   A O    1 
ATOM   2602 C  CB   A LEU   A 1 127 ? 21.032 -6.562  -1.330  0.56 11.33 ?  127 LEU   A CB   1 
ATOM   2603 C  CB   B LEU   A 1 127 ? 20.847 -6.496  -1.103  0.44 13.25 ?  127 LEU   A CB   1 
ATOM   2604 C  CG   A LEU   A 1 127 ? 21.790 -6.858  -0.036  0.56 11.94 ?  127 LEU   A CG   1 
ATOM   2605 C  CG   B LEU   A 1 127 ? 21.691 -6.630  0.166   0.44 13.81 ?  127 LEU   A CG   1 
ATOM   2606 C  CD1  A LEU   A 1 127 ? 22.855 -7.898  -0.307  0.56 12.19 ?  127 LEU   A CD1  1 
ATOM   2607 C  CD1  B LEU   A 1 127 ? 22.944 -7.458  -0.097  0.44 14.13 ?  127 LEU   A CD1  1 
ATOM   2608 C  CD2  A LEU   A 1 127 ? 22.414 -5.597  0.523   0.56 12.08 ?  127 LEU   A CD2  1 
ATOM   2609 C  CD2  B LEU   A 1 127 ? 22.054 -5.273  0.736   0.44 14.23 ?  127 LEU   A CD2  1 
ATOM   2610 H  H    A LEU   A 1 127 ? 19.022 -6.940  -0.024  0.56 12.92 ?  127 LEU   A H    1 
ATOM   2611 H  H    B LEU   A 1 127 ? 18.822 -6.787  0.247   0.44 14.62 ?  127 LEU   A H    1 
ATOM   2612 H  HA   A LEU   A 1 127 ? 20.152 -4.759  -0.930  0.56 12.46 ?  127 LEU   A HA   1 
ATOM   2613 H  HA   B LEU   A 1 127 ? 19.988 -4.669  -0.738  0.44 14.86 ?  127 LEU   A HA   1 
ATOM   2614 H  HB2  A LEU   A 1 127 ? 20.728 -7.412  -1.677  0.56 13.59 ?  127 LEU   A HB2  1 
ATOM   2615 H  HB2  B LEU   A 1 127 ? 20.510 -7.378  -1.323  0.44 15.90 ?  127 LEU   A HB2  1 
ATOM   2616 H  HB3  A LEU   A 1 127 ? 21.678 -6.177  -1.943  0.56 13.59 ?  127 LEU   A HB3  1 
ATOM   2617 H  HB3  B LEU   A 1 127 ? 21.438 -6.194  -1.815  0.44 15.90 ?  127 LEU   A HB3  1 
ATOM   2618 H  HG   A LEU   A 1 127 ? 21.174 -7.221  0.627   0.56 14.33 ?  127 LEU   A HG   1 
ATOM   2619 H  HG   B LEU   A 1 127 ? 21.171 -7.100  0.831   0.44 16.57 ?  127 LEU   A HG   1 
ATOM   2620 H  HD11 A LEU   A 1 127 ? 23.304 -8.118  0.525   0.56 14.63 ?  127 LEU   A HD11 1 
ATOM   2621 H  HD11 B LEU   A 1 127 ? 23.462 -7.514  0.722   0.44 16.96 ?  127 LEU   A HD11 1 
ATOM   2622 H  HD12 A LEU   A 1 127 ? 22.434 -8.695  -0.673  0.56 14.63 ?  127 LEU   A HD12 1 
ATOM   2623 H  HD12 B LEU   A 1 127 ? 22.681 -8.348  -0.383  0.44 16.96 ?  127 LEU   A HD12 1 
ATOM   2624 H  HD13 A LEU   A 1 127 ? 23.490 -7.538  -0.942  0.56 14.63 ?  127 LEU   A HD13 1 
ATOM   2625 H  HD13 B LEU   A 1 127 ? 23.469 -7.030  -0.791  0.44 16.96 ?  127 LEU   A HD13 1 
ATOM   2626 H  HD21 A LEU   A 1 127 ? 22.941 -5.823  1.307   0.56 14.49 ?  127 LEU   A HD21 1 
ATOM   2627 H  HD21 B LEU   A 1 127 ? 22.743 -5.387  1.408   0.44 17.08 ?  127 LEU   A HD21 1 
ATOM   2628 H  HD22 A LEU   A 1 127 ? 22.985 -5.204  -0.156  0.56 14.49 ?  127 LEU   A HD22 1 
ATOM   2629 H  HD22 B LEU   A 1 127 ? 22.376 -4.705  0.021   0.44 17.08 ?  127 LEU   A HD22 1 
ATOM   2630 H  HD23 A LEU   A 1 127 ? 21.710 -4.977  0.764   0.56 14.49 ?  127 LEU   A HD23 1 
ATOM   2631 H  HD23 B LEU   A 1 127 ? 21.261 -4.882  1.138   0.44 17.08 ?  127 LEU   A HD23 1 
ATOM   2632 N  N    A SER   A 1 128 ? 19.641 -4.367  -3.292  0.56 10.47 ?  128 SER   A N    1 
ATOM   2633 N  N    B SER   A 1 128 ? 19.548 -4.327  -3.108  0.44 11.58 ?  128 SER   A N    1 
ATOM   2634 C  CA   A SER   A 1 128 ? 19.262 -3.990  -4.646  0.56 10.83 ?  128 SER   A CA   1 
ATOM   2635 C  CA   B SER   A 1 128 ? 19.146 -3.955  -4.461  0.44 11.55 ?  128 SER   A CA   1 
ATOM   2636 C  C    A SER   A 1 128 ? 17.810 -3.527  -4.766  0.56 10.64 ?  128 SER   A C    1 
ATOM   2637 C  C    B SER   A 1 128 ? 17.679 -3.548  -4.568  0.44 11.74 ?  128 SER   A C    1 
ATOM   2638 O  O    A SER   A 1 128 ? 17.384 -3.181  -5.870  0.56 11.48 ?  128 SER   A O    1 
ATOM   2639 O  O    B SER   A 1 128 ? 17.182 -3.343  -5.678  0.44 12.81 ?  128 SER   A O    1 
ATOM   2640 C  CB   A SER   A 1 128 ? 19.599 -5.065  -5.693  0.56 11.16 ?  128 SER   A CB   1 
ATOM   2641 C  CB   B SER   A 1 128 ? 19.521 -5.014  -5.507  0.44 11.56 ?  128 SER   A CB   1 
ATOM   2642 O  OG   A SER   A 1 128 ? 20.998 -5.313  -5.723  0.56 11.77 ?  128 SER   A OG   1 
ATOM   2643 O  OG   B SER   A 1 128 ? 20.933 -5.112  -5.626  0.44 11.92 ?  128 SER   A OG   1 
ATOM   2644 H  H    A SER   A 1 128 ? 20.212 -3.814  -2.950  0.56 12.56 ?  128 SER   A H    1 
ATOM   2645 H  H    B SER   A 1 128 ? 20.156 -3.800  -2.800  0.44 13.90 ?  128 SER   A H    1 
ATOM   2646 H  HA   A SER   A 1 128 ? 19.809 -3.229  -4.875  0.56 13.00 ?  128 SER   A HA   1 
ATOM   2647 H  HA   B SER   A 1 128 ? 19.655 -3.169  -4.693  0.44 13.86 ?  128 SER   A HA   1 
ATOM   2648 H  HB2  A SER   A 1 128 ? 19.137 -5.886  -5.473  0.56 13.40 ?  128 SER   A HB2  1 
ATOM   2649 H  HB2  B SER   A 1 128 ? 19.164 -5.871  -5.239  0.44 13.87 ?  128 SER   A HB2  1 
ATOM   2650 H  HB3  A SER   A 1 128 ? 19.313 -4.748  -6.568  0.56 13.40 ?  128 SER   A HB3  1 
ATOM   2651 H  HB3  B SER   A 1 128 ? 19.148 -4.754  -6.370  0.44 13.87 ?  128 SER   A HB3  1 
ATOM   2652 H  HG   A SER   A 1 128 ? 21.411 -4.610  -5.927  0.56 14.13 ?  128 SER   A HG   1 
ATOM   2653 H  HG   B SER   A 1 128 ? 21.252 -4.368  -5.862  0.44 14.30 ?  128 SER   A HG   1 
ATOM   2654 N  N    A ALA   A 1 129 ? 17.056 -3.477  -3.667  0.56 11.16 ?  129 ALA   A N    1 
ATOM   2655 N  N    B ALA   A 1 129 ? 16.982 -3.405  -3.444  0.44 12.28 ?  129 ALA   A N    1 
ATOM   2656 C  CA   A ALA   A 1 129 ? 15.673 -3.015  -3.693  0.56 11.59 ?  129 ALA   A CA   1 
ATOM   2657 C  CA   B ALA   A 1 129 ? 15.623 -2.894  -3.446  0.44 12.54 ?  129 ALA   A CA   1 
ATOM   2658 C  C    A ALA   A 1 129 ? 15.633 -1.486  -3.596  0.56 11.56 ?  129 ALA   A C    1 
ATOM   2659 C  C    B ALA   A 1 129 ? 15.644 -1.371  -3.566  0.44 13.00 ?  129 ALA   A C    1 
ATOM   2660 O  O    A ALA   A 1 129 ? 16.662 -0.803  -3.661  0.56 12.39 ?  129 ALA   A O    1 
ATOM   2661 O  O    B ALA   A 1 129 ? 16.700 -0.730  -3.580  0.44 13.57 ?  129 ALA   A O    1 
ATOM   2662 C  CB   A ALA   A 1 129 ? 14.860 -3.716  -2.603  0.56 12.22 ?  129 ALA   A CB   1 
ATOM   2663 C  CB   B ALA   A 1 129 ? 14.878 -3.357  -2.194  0.44 12.74 ?  129 ALA   A CB   1 
ATOM   2664 H  H    A ALA   A 1 129 ? 17.332 -3.715  -2.880  0.56 13.39 ?  129 ALA   A H    1 
ATOM   2665 H  H    B ALA   A 1 129 ? 17.277 -3.600  -2.664  0.44 14.73 ?  129 ALA   A H    1 
ATOM   2666 H  HA   A ALA   A 1 129 ? 15.289 -3.271  -4.544  0.56 13.91 ?  129 ALA   A HA   1 
ATOM   2667 H  HA   B ALA   A 1 129 ? 15.156 -3.242  -4.220  0.44 15.05 ?  129 ALA   A HA   1 
ATOM   2668 H  HB1  A ALA   A 1 129 ? 13.943 -3.406  -2.644  0.56 14.67 ?  129 ALA   A HB1  1 
ATOM   2669 H  HB1  B ALA   A 1 129 ? 13.974 -3.007  -2.218  0.44 15.28 ?  129 ALA   A HB1  1 
ATOM   2670 H  HB2  A ALA   A 1 129 ? 14.890 -4.677  -2.748  0.56 14.67 ?  129 ALA   A HB2  1 
ATOM   2671 H  HB2  B ALA   A 1 129 ? 14.857 -4.328  -2.181  0.44 15.28 ?  129 ALA   A HB2  1 
ATOM   2672 H  HB3  A ALA   A 1 129 ? 15.242 -3.505  -1.735  0.56 14.67 ?  129 ALA   A HB3  1 
ATOM   2673 H  HB3  B ALA   A 1 129 ? 15.342 -3.026  -1.409  0.44 15.28 ?  129 ALA   A HB3  1 
ATOM   2674 N  N    A GLY   A 1 130 ? 14.430 -0.932  -3.462  0.56 11.96 ?  130 GLY   A N    1 
ATOM   2675 N  N    B GLY   A 1 130 ? 14.459 -0.786  -3.667  0.44 13.79 ?  130 GLY   A N    1 
ATOM   2676 C  CA   A GLY   A 1 130 ? 14.293 0.513   -3.388  0.56 11.64 ?  130 GLY   A CA   1 
ATOM   2677 C  CA   B GLY   A 1 130 ? 14.372 0.659   -3.775  0.44 14.50 ?  130 GLY   A CA   1 
ATOM   2678 C  C    A GLY   A 1 130 ? 14.904 1.173   -4.613  0.56 10.82 ?  130 GLY   A C    1 
ATOM   2679 C  C    B GLY   A 1 130 ? 15.018 1.164   -5.047  0.44 14.92 ?  130 GLY   A C    1 
ATOM   2680 O  O    A GLY   A 1 130 ? 14.692 0.747   -5.751  0.56 11.19 ?  130 GLY   A O    1 
ATOM   2681 O  O    B GLY   A 1 130 ? 14.789 0.643   -6.145  0.44 14.92 ?  130 GLY   A O    1 
ATOM   2682 H  H    A GLY   A 1 130 ? 13.688 -1.370  -3.423  0.56 14.35 ?  130 GLY   A H    1 
ATOM   2683 H  H    B GLY   A 1 130 ? 13.705 -1.202  -3.665  0.44 16.54 ?  130 GLY   A H    1 
ATOM   2684 H  HA2  A GLY   A 1 130 ? 13.351 0.745   -3.319  0.56 13.97 ?  130 GLY   A HA2  1 
ATOM   2685 H  HA2  B GLY   A 1 130 ? 13.447 0.929   -3.787  0.44 17.40 ?  130 GLY   A HA2  1 
ATOM   2686 H  HA3  A GLY   A 1 130 ? 14.750 0.839   -2.597  0.56 13.97 ?  130 GLY   A HA3  1 
ATOM   2687 H  HA3  B GLY   A 1 130 ? 14.815 1.071   -3.017  0.44 17.40 ?  130 GLY   A HA3  1 
ATOM   2688 N  N    A ILE   A 1 131 ? 15.682 2.236   -4.383  0.56 10.92 ?  131 ILE   A N    1 
ATOM   2689 N  N    B ILE   A 1 131 ? 15.854 2.198   -4.901  0.44 15.95 ?  131 ILE   A N    1 
ATOM   2690 C  CA   A ILE   A 1 131 ? 16.254 3.009   -5.484  0.56 10.30 ?  131 ILE   A CA   1 
ATOM   2691 C  CA   B ILE   A 1 131 ? 16.392 2.894   -6.067  0.44 17.31 ?  131 ILE   A CA   1 
ATOM   2692 C  C    A ILE   A 1 131 ? 17.315 2.258   -6.281  0.56 10.14 ?  131 ILE   A C    1 
ATOM   2693 C  C    B ILE   A 1 131 ? 17.488 2.104   -6.759  0.44 16.54 ?  131 ILE   A C    1 
ATOM   2694 O  O    A ILE   A 1 131 ? 17.761 2.766   -7.318  0.56 10.71 ?  131 ILE   A O    1 
ATOM   2695 O  O    B ILE   A 1 131 ? 17.980 2.541   -7.808  0.44 16.88 ?  131 ILE   A O    1 
ATOM   2696 C  CB   A ILE   A 1 131 ? 16.800 4.374   -5.010  0.56 12.02 ?  131 ILE   A CB   1 
ATOM   2697 C  CB   B ILE   A 1 131 ? 16.808 4.346   -5.746  0.44 19.59 ?  131 ILE   A CB   1 
ATOM   2698 C  CG1  A ILE   A 1 131 ? 18.011 4.201   -4.089  0.56 13.18 ?  131 ILE   A CG1  1 
ATOM   2699 C  CG1  B ILE   A 1 131 ? 18.134 4.396   -4.990  0.44 21.38 ?  131 ILE   A CG1  1 
ATOM   2700 C  CG2  A ILE   A 1 131 ? 15.711 5.180   -4.309  0.56 12.82 ?  131 ILE   A CG2  1 
ATOM   2701 C  CG2  B ILE   A 1 131 ? 15.715 5.054   -4.955  0.44 19.77 ?  131 ILE   A CG2  1 
ATOM   2702 C  CD1  A ILE   A 1 131 ? 18.636 5.518   -3.651  0.56 14.67 ?  131 ILE   A CD1  1 
ATOM   2703 C  CD1  B ILE   A 1 131 ? 18.678 5.799   -4.866  0.44 22.37 ?  131 ILE   A CD1  1 
ATOM   2704 H  H    A ILE   A 1 131 ? 15.873 2.532   -3.596  0.56 13.11 ?  131 ILE   A H    1 
ATOM   2705 H  H    B ILE   A 1 131 ? 16.143 2.488   -4.147  0.44 19.14 ?  131 ILE   A H    1 
ATOM   2706 H  HA   A ILE   A 1 131 ? 15.528 3.211   -6.094  0.56 12.36 ?  131 ILE   A HA   1 
ATOM   2707 H  HA   B ILE   A 1 131 ? 15.678 2.953   -6.713  0.44 20.77 ?  131 ILE   A HA   1 
ATOM   2708 H  HB   A ILE   A 1 131 ? 17.078 4.874   -5.790  0.56 14.43 ?  131 ILE   A HB   1 
ATOM   2709 H  HB   B ILE   A 1 131 ? 16.920 4.816   -6.578  0.44 23.51 ?  131 ILE   A HB   1 
ATOM   2710 H  HG12 A ILE   A 1 131 ? 17.734 3.724   -3.292  0.56 15.82 ?  131 ILE   A HG12 1 
ATOM   2711 H  HG12 B ILE   A 1 131 ? 18.002 4.042   -4.098  0.44 25.65 ?  131 ILE   A HG12 1 
ATOM   2712 H  HG13 A ILE   A 1 131 ? 18.692 3.696   -4.557  0.56 15.82 ?  131 ILE   A HG13 1 
ATOM   2713 H  HG13 B ILE   A 1 131 ? 18.797 3.871   -5.463  0.44 25.65 ?  131 ILE   A HG13 1 
ATOM   2714 H  HG21 A ILE   A 1 131 ? 16.019 6.094   -4.184  0.56 15.39 ?  131 ILE   A HG21 1 
ATOM   2715 H  HG21 B ILE   A 1 131 ? 15.928 5.998   -4.900  0.44 23.72 ?  131 ILE   A HG21 1 
ATOM   2716 H  HG22 A ILE   A 1 131 ? 14.911 5.177   -4.857  0.56 15.39 ?  131 ILE   A HG22 1 
ATOM   2717 H  HG22 B ILE   A 1 131 ? 14.870 4.931   -5.412  0.44 23.72 ?  131 ILE   A HG22 1 
ATOM   2718 H  HG23 A ILE   A 1 131 ? 15.521 4.777   -3.447  0.56 15.39 ?  131 ILE   A HG23 1 
ATOM   2719 H  HG23 B ILE   A 1 131 ? 15.668 4.671   -4.065  0.44 23.72 ?  131 ILE   A HG23 1 
ATOM   2720 H  HD11 A ILE   A 1 131 ? 19.474 5.335   -3.195  0.56 17.60 ?  131 ILE   A HD11 1 
ATOM   2721 H  HD11 B ILE   A 1 131 ? 19.591 5.755   -4.552  0.44 26.84 ?  131 ILE   A HD11 1 
ATOM   2722 H  HD12 A ILE   A 1 131 ? 18.801 6.067   -4.434  0.56 17.60 ?  131 ILE   A HD12 1 
ATOM   2723 H  HD12 B ILE   A 1 131 ? 18.649 6.224   -5.740  0.44 26.84 ?  131 ILE   A HD12 1 
ATOM   2724 H  HD13 A ILE   A 1 131 ? 18.028 5.977   -3.049  0.56 17.60 ?  131 ILE   A HD13 1 
ATOM   2725 H  HD13 B ILE   A 1 131 ? 18.130 6.296   -4.241  0.44 26.84 ?  131 ILE   A HD13 1 
ATOM   2726 N  N    A PHE   A 1 132 ? 17.735 1.068   -5.838  0.56 10.22 ?  132 PHE   A N    1 
ATOM   2727 N  N    B PHE   A 1 132 ? 17.887 0.954   -6.208  0.44 15.36 ?  132 PHE   A N    1 
ATOM   2728 C  CA   A PHE   A 1 132 ? 18.616 0.251   -6.663  0.56 10.60 ?  132 PHE   A CA   1 
ATOM   2729 C  CA   B PHE   A 1 132 ? 18.783 0.061   -6.933  0.44 15.06 ?  132 PHE   A CA   1 
ATOM   2730 C  C    A PHE   A 1 132 ? 17.855 -0.501  -7.756  0.56 11.03 ?  132 PHE   A C    1 
ATOM   2731 C  C    B PHE   A 1 132 ? 18.066 -0.721  -8.032  0.44 15.26 ?  132 PHE   A C    1 
ATOM   2732 O  O    A PHE   A 1 132 ? 18.483 -1.131  -8.611  0.56 12.11 ?  132 PHE   A O    1 
ATOM   2733 O  O    B PHE   A 1 132 ? 18.733 -1.348  -8.864  0.44 16.01 ?  132 PHE   A O    1 
ATOM   2734 C  CB   A PHE   A 1 132 ? 19.429 -0.723  -5.801  0.56 10.30 ?  132 PHE   A CB   1 
ATOM   2735 C  CB   B PHE   A 1 132 ? 19.502 -0.893  -5.974  0.44 14.54 ?  132 PHE   A CB   1 
ATOM   2736 C  CG   A PHE   A 1 132 ? 20.675 -0.129  -5.164  0.56 10.58 ?  132 PHE   A CG   1 
ATOM   2737 C  CG   B PHE   A 1 132 ? 20.677 -0.279  -5.252  0.44 14.29 ?  132 PHE   A CG   1 
ATOM   2738 C  CD1  A PHE   A 1 132 ? 20.595 0.917   -4.257  0.56 11.64 ?  132 PHE   A CD1  1 
ATOM   2739 C  CD1  B PHE   A 1 132 ? 20.501 0.772   -4.365  0.44 14.47 ?  132 PHE   A CD1  1 
ATOM   2740 C  CD2  A PHE   A 1 132 ? 21.924 -0.675  -5.429  0.56 11.38 ?  132 PHE   A CD2  1 
ATOM   2741 C  CD2  B PHE   A 1 132 ? 21.954 -0.783  -5.437  0.44 14.46 ?  132 PHE   A CD2  1 
ATOM   2742 C  CE1  A PHE   A 1 132 ? 21.744 1.426   -3.656  0.56 11.92 ?  132 PHE   A CE1  1 
ATOM   2743 C  CE1  B PHE   A 1 132 ? 21.583 1.320   -3.693  0.44 14.36 ?  132 PHE   A CE1  1 
ATOM   2744 C  CE2  A PHE   A 1 132 ? 23.070 -0.172  -4.830  0.56 11.86 ?  132 PHE   A CE2  1 
ATOM   2745 C  CE2  B PHE   A 1 132 ? 23.037 -0.243  -4.767  0.44 14.28 ?  132 PHE   A CE2  1 
ATOM   2746 C  CZ   A PHE   A 1 132 ? 22.978 0.878   -3.943  0.56 12.01 ?  132 PHE   A CZ   1 
ATOM   2747 C  CZ   B PHE   A 1 132 ? 22.851 0.811   -3.893  0.44 14.18 ?  132 PHE   A CZ   1 
ATOM   2748 H  H    A PHE   A 1 132 ? 17.521 0.724   -5.073  0.56 12.26 ?  132 PHE   A H    1 
ATOM   2749 H  H    B PHE   A 1 132 ? 17.651 0.675   -5.416  0.44 18.43 ?  132 PHE   A H    1 
ATOM   2750 H  HA   A PHE   A 1 132 ? 19.240 0.846   -7.098  0.56 12.71 ?  132 PHE   A HA   1 
ATOM   2751 H  HA   B PHE   A 1 132 ? 19.463 0.602   -7.352  0.44 18.08 ?  132 PHE   A HA   1 
ATOM   2752 H  HB2  A PHE   A 1 132 ? 18.863 -1.045  -5.081  0.56 12.36 ?  132 PHE   A HB2  1 
ATOM   2753 H  HB2  B PHE   A 1 132 ? 18.876 -1.192  -5.298  0.44 17.45 ?  132 PHE   A HB2  1 
ATOM   2754 H  HB3  A PHE   A 1 132 ? 19.708 -1.463  -6.357  0.56 12.36 ?  132 PHE   A HB3  1 
ATOM   2755 H  HB3  B PHE   A 1 132 ? 19.834 -1.653  -6.476  0.44 17.45 ?  132 PHE   A HB3  1 
ATOM   2756 H  HD1  A PHE   A 1 132 ? 19.768 1.292   -4.054  0.56 13.97 ?  132 PHE   A HD1  1 
ATOM   2757 H  HD1  B PHE   A 1 132 ? 19.651 1.120   -4.223  0.44 17.37 ?  132 PHE   A HD1  1 
ATOM   2758 H  HD2  A PHE   A 1 132 ? 21.995 -1.386  -6.026  0.56 13.66 ?  132 PHE   A HD2  1 
ATOM   2759 H  HD2  B PHE   A 1 132 ? 22.087 -1.494  -6.023  0.44 17.36 ?  132 PHE   A HD2  1 
ATOM   2760 H  HE1  A PHE   A 1 132 ? 21.681 2.139   -3.058  0.56 14.30 ?  132 PHE   A HE1  1 
ATOM   2761 H  HE1  B PHE   A 1 132 ? 21.455 2.031   -3.104  0.44 17.23 ?  132 PHE   A HE1  1 
ATOM   2762 H  HE2  A PHE   A 1 132 ? 23.899 -0.543  -5.034  0.56 14.23 ?  132 PHE   A HE2  1 
ATOM   2763 H  HE2  B PHE   A 1 132 ? 23.888 -0.589  -4.911  0.44 17.14 ?  132 PHE   A HE2  1 
ATOM   2764 H  HZ   A PHE   A 1 132 ? 23.746 1.224   -3.548  0.56 14.42 ?  132 PHE   A HZ   1 
ATOM   2765 H  HZ   B PHE   A 1 132 ? 23.578 1.179   -3.447  0.44 17.02 ?  132 PHE   A HZ   1 
ATOM   2766 N  N    A GLY   A 1 133 ? 16.523 -0.461  -7.746  0.56 11.23 ?  133 GLY   A N    1 
ATOM   2767 N  N    B GLY   A 1 133 ? 16.733 -0.717  -8.046  0.44 14.82 ?  133 GLY   A N    1 
ATOM   2768 C  CA   A GLY   A 1 133 ? 15.737 -0.797  -8.915  0.56 11.87 ?  133 GLY   A CA   1 
ATOM   2769 C  CA   B GLY   A 1 133 ? 15.979 -1.107  -9.219  0.44 14.58 ?  133 GLY   A CA   1 
ATOM   2770 C  C    A GLY   A 1 133 ? 15.376 -2.254  -9.121  0.56 12.64 ?  133 GLY   A C    1 
ATOM   2771 C  C    B GLY   A 1 133 ? 15.638 -2.577  -9.362  0.44 14.72 ?  133 GLY   A C    1 
ATOM   2772 O  O    A GLY   A 1 133 ? 14.697 -2.557  -10.108 0.56 13.35 ?  133 GLY   A O    1 
ATOM   2773 O  O    B GLY   A 1 133 ? 15.047 -2.951  -10.382 0.44 15.76 ?  133 GLY   A O    1 
ATOM   2774 H  H    A GLY   A 1 133 ? 16.048 -0.229  -7.067  0.56 13.48 ?  133 GLY   A H    1 
ATOM   2775 H  H    B GLY   A 1 133 ? 16.242 -0.486  -7.375  0.44 17.79 ?  133 GLY   A H    1 
ATOM   2776 H  HA2  A GLY   A 1 133 ? 14.898 -0.311  -8.869  0.56 14.24 ?  133 GLY   A HA2  1 
ATOM   2777 H  HA2  B GLY   A 1 133 ? 15.150 -0.608  -9.228  0.44 17.50 ?  133 GLY   A HA2  1 
ATOM   2778 H  HA3  A GLY   A 1 133 ? 16.208 -0.493  -9.709  0.56 14.24 ?  133 GLY   A HA3  1 
ATOM   2779 H  HA3  B GLY   A 1 133 ? 16.486 -0.850  -10.004 0.44 17.50 ?  133 GLY   A HA3  1 
ATOM   2780 N  N    A ALA   A 1 134 ? 15.783 -3.163  -8.239  0.56 12.99 ?  134 ALA   A N    1 
ATOM   2781 N  N    B ALA   A 1 134 ? 15.988 -3.424  -8.398  0.44 14.20 ?  134 ALA   A N    1 
ATOM   2782 C  CA   A ALA   A 1 134 ? 15.434 -4.565  -8.414  0.56 13.48 ?  134 ALA   A CA   1 
ATOM   2783 C  CA   B ALA   A 1 134 ? 15.699 -4.845  -8.518  0.44 14.41 ?  134 ALA   A CA   1 
ATOM   2784 C  C    A ALA   A 1 134 ? 14.093 -4.868  -7.754  0.56 13.60 ?  134 ALA   A C    1 
ATOM   2785 C  C    B ALA   A 1 134 ? 14.293 -5.171  -8.020  0.44 14.70 ?  134 ALA   A C    1 
ATOM   2786 O  O    A ALA   A 1 134 ? 13.570 -4.083  -6.959  0.56 14.79 ?  134 ALA   A O    1 
ATOM   2787 O  O    B ALA   A 1 134 ? 13.655 -4.390  -7.312  0.44 15.66 ?  134 ALA   A O    1 
ATOM   2788 C  CB   A ALA   A 1 134 ? 16.510 -5.482  -7.837  0.56 14.37 ?  134 ALA   A CB   1 
ATOM   2789 C  CB   B ALA   A 1 134 ? 16.715 -5.675  -7.735  0.44 14.90 ?  134 ALA   A CB   1 
ATOM   2790 H  H    A ALA   A 1 134 ? 16.252 -2.990  -7.540  0.56 15.59 ?  134 ALA   A H    1 
ATOM   2791 H  H    B ALA   A 1 134 ? 16.406 -3.202  -7.676  0.44 17.04 ?  134 ALA   A H    1 
ATOM   2792 H  HA   A ALA   A 1 134 ? 15.349 -4.753  -9.360  0.56 16.18 ?  134 ALA   A HA   1 
ATOM   2793 H  HA   B ALA   A 1 134 ? 15.758 -5.100  -9.453  0.44 17.30 ?  134 ALA   A HA   1 
ATOM   2794 H  HB1  A ALA   A 1 134 ? 16.247 -6.401  -7.985  0.56 17.24 ?  134 ALA   A HB1  1 
ATOM   2795 H  HB1  B ALA   A 1 134 ? 16.515 -6.615  -7.863  0.44 17.88 ?  134 ALA   A HB1  1 
ATOM   2796 H  HB2  A ALA   A 1 134 ? 17.347 -5.296  -8.288  0.56 17.24 ?  134 ALA   A HB2  1 
ATOM   2797 H  HB2  B ALA   A 1 134 ? 17.605 -5.477  -8.065  0.44 17.88 ?  134 ALA   A HB2  1 
ATOM   2798 H  HB3  A ALA   A 1 134 ? 16.595 -5.305  -6.889  0.56 17.24 ?  134 ALA   A HB3  1 
ATOM   2799 H  HB3  B ALA   A 1 134 ? 16.650 -5.446  -6.796  0.44 17.88 ?  134 ALA   A HB3  1 
ATOM   2800 N  N    A ASP   A 1 135 ? 13.535 -6.022  -8.113  0.56 13.75 ?  135 ASP   A N    1 
ATOM   2801 N  N    B ASP   A 1 135 ? 13.823 -6.352  -8.408  0.44 14.72 ?  135 ASP   A N    1 
ATOM   2802 C  CA   A ASP   A 1 135 ? 12.287 -6.495  -7.528  0.56 14.43 ?  135 ASP   A CA   1 
ATOM   2803 C  CA   B ASP   A 1 135 ? 12.555 -6.891  -7.930  0.44 15.06 ?  135 ASP   A CA   1 
ATOM   2804 C  C    A ASP   A 1 135 ? 12.543 -6.948  -6.094  0.56 13.80 ?  135 ASP   A C    1 
ATOM   2805 C  C    B ASP   A 1 135 ? 12.702 -7.269  -6.462  0.44 14.49 ?  135 ASP   A C    1 
ATOM   2806 O  O    A ASP   A 1 135 ? 13.314 -7.894  -5.882  0.56 13.67 ?  135 ASP   A O    1 
ATOM   2807 O  O    B ASP   A 1 135 ? 13.526 -8.133  -6.136  0.44 14.80 ?  135 ASP   A O    1 
ATOM   2808 C  CB   A ASP   A 1 135 ? 11.772 -7.663  -8.364  0.56 16.64 ?  135 ASP   A CB   1 
ATOM   2809 C  CB   B ASP   A 1 135 ? 12.232 -8.136  -8.752  0.44 16.94 ?  135 ASP   A CB   1 
ATOM   2810 C  CG   A ASP   A 1 135 ? 10.410 -8.164  -7.902  0.56 19.02 ?  135 ASP   A CG   1 
ATOM   2811 C  CG   B ASP   A 1 135 ? 10.908 -8.780  -8.364  0.44 18.66 ?  135 ASP   A CG   1 
ATOM   2812 O  OD1  A ASP   A 1 135 ? 9.961  -7.769  -6.804  0.56 18.95 ?  135 ASP   A OD1  1 
ATOM   2813 O  OD1  B ASP   A 1 135 ? 10.374 -8.487  -7.274  0.44 19.01 ?  135 ASP   A OD1  1 
ATOM   2814 O  OD2  A ASP   A 1 135 ? 9.775  -8.934  -8.655  0.56 21.32 -1 135 ASP   A OD2  1 
ATOM   2815 O  OD2  B ASP   A 1 135 ? 10.411 -9.610  -9.151  0.44 20.01 -1 135 ASP   A OD2  1 
ATOM   2816 H  H    A ASP   A 1 135 ? 13.853 -6.549  -8.710  0.56 16.50 ?  135 ASP   A H    1 
ATOM   2817 H  H    B ASP   A 1 135 ? 14.229 -6.869  -8.961  0.44 17.66 ?  135 ASP   A H    1 
ATOM   2818 H  HA   A ASP   A 1 135 ? 11.614 -5.787  -7.549  0.56 17.32 ?  135 ASP   A HA   1 
ATOM   2819 H  HA   B ASP   A 1 135 ? 11.848 -6.238  -8.045  0.44 18.08 ?  135 ASP   A HA   1 
ATOM   2820 H  HB2  A ASP   A 1 135 ? 11.664 -7.375  -9.284  0.56 19.97 ?  135 ASP   A HB2  1 
ATOM   2821 H  HB2  B ASP   A 1 135 ? 12.205 -7.894  -9.693  0.44 20.33 ?  135 ASP   A HB2  1 
ATOM   2822 H  HB3  A ASP   A 1 135 ? 12.425 -8.386  -8.323  0.56 19.97 ?  135 ASP   A HB3  1 
ATOM   2823 H  HB3  B ASP   A 1 135 ? 12.922 -8.801  -8.604  0.44 20.33 ?  135 ASP   A HB3  1 
ATOM   2824 N  N    A PRO   A 1 136 ? 11.939 -6.310  -5.087  0.56 13.24 ?  136 PRO   A N    1 
ATOM   2825 N  N    B PRO   A 1 136 ? 11.937 -6.664  -5.549  0.44 13.94 ?  136 PRO   A N    1 
ATOM   2826 C  CA   A PRO   A 1 136 ? 12.207 -6.719  -3.696  0.56 13.27 ?  136 PRO   A CA   1 
ATOM   2827 C  CA   B PRO   A 1 136 ? 12.129 -6.985  -4.123  0.44 13.70 ?  136 PRO   A CA   1 
ATOM   2828 C  C    A PRO   A 1 136 ? 11.781 -8.142  -3.376  0.56 12.77 ?  136 PRO   A C    1 
ATOM   2829 C  C    B PRO   A 1 136 ? 11.745 -8.409  -3.758  0.44 13.60 ?  136 PRO   A C    1 
ATOM   2830 O  O    A PRO   A 1 136 ? 12.364 -8.765  -2.481  0.56 11.89 ?  136 PRO   A O    1 
ATOM   2831 O  O    B PRO   A 1 136 ? 12.394 -9.010  -2.895  0.44 13.80 ?  136 PRO   A O    1 
ATOM   2832 C  CB   A PRO   A 1 136 ? 11.437 -5.677  -2.869  0.56 14.04 ?  136 PRO   A CB   1 
ATOM   2833 C  CB   B PRO   A 1 136 ? 11.265 -5.936  -3.408  0.44 13.69 ?  136 PRO   A CB   1 
ATOM   2834 C  CG   A PRO   A 1 136 ? 10.397 -5.148  -3.798  0.56 14.76 ?  136 PRO   A CG   1 
ATOM   2835 C  CG   B PRO   A 1 136 ? 10.227 -5.557  -4.420  0.44 13.80 ?  136 PRO   A CG   1 
ATOM   2836 C  CD   A PRO   A 1 136 ? 11.010 -5.169  -5.158  0.56 14.08 ?  136 PRO   A CD   1 
ATOM   2837 C  CD   B PRO   A 1 136 ? 10.901 -5.639  -5.757  0.44 13.85 ?  136 PRO   A CD   1 
ATOM   2838 H  HA   A PRO   A 1 136 ? 13.153 -6.621  -3.501  0.56 15.92 ?  136 PRO   A HA   1 
ATOM   2839 H  HA   B PRO   A 1 136 ? 13.059 -6.846  -3.872  0.44 16.43 ?  136 PRO   A HA   1 
ATOM   2840 H  HB2  A PRO   A 1 136 ? 11.023 -6.103  -2.103  0.56 16.85 ?  136 PRO   A HB2  1 
ATOM   2841 H  HB2  B PRO   A 1 136 ? 10.855 -6.330  -2.621  0.44 16.43 ?  136 PRO   A HB2  1 
ATOM   2842 H  HB3  A PRO   A 1 136 ? 12.034 -4.965  -2.587  0.56 16.85 ?  136 PRO   A HB3  1 
ATOM   2843 H  HB3  B PRO   A 1 136 ? 11.812 -5.172  -3.165  0.44 16.43 ?  136 PRO   A HB3  1 
ATOM   2844 H  HG2  A PRO   A 1 136 ? 9.617  -5.723  -3.772  0.56 17.71 ?  136 PRO   A HG2  1 
ATOM   2845 H  HG2  B PRO   A 1 136 ? 9.488  -6.182  -4.376  0.44 16.56 ?  136 PRO   A HG2  1 
ATOM   2846 H  HG3  A PRO   A 1 136 ? 10.162 -4.242  -3.545  0.56 17.71 ?  136 PRO   A HG3  1 
ATOM   2847 H  HG3  B PRO   A 1 136 ? 9.925  -4.653  -4.251  0.44 16.56 ?  136 PRO   A HG3  1 
ATOM   2848 H  HD2  A PRO   A 1 136 ? 10.326 -5.329  -5.832  0.56 16.90 ?  136 PRO   A HD2  1 
ATOM   2849 H  HD2  B PRO   A 1 136 ? 10.277 -5.933  -6.439  0.44 16.62 ?  136 PRO   A HD2  1 
ATOM   2850 H  HD3  A PRO   A 1 136 ? 11.488 -4.341  -5.331  0.56 16.90 ?  136 PRO   A HD3  1 
ATOM   2851 H  HD3  B PRO   A 1 136 ? 11.309 -4.789  -5.991  0.44 16.62 ?  136 PRO   A HD3  1 
ATOM   2852 N  N    A ILE   A 1 137 ? 10.759 -8.666  -4.057  0.56 13.33 ?  137 ILE   A N    1 
ATOM   2853 N  N    B ILE   A 1 137 ? 10.697 -8.964  -4.372  0.44 13.68 ?  137 ILE   A N    1 
ATOM   2854 C  CA   A ILE   A 1 137 ? 10.367 -10.058 -3.847  0.56 13.59 ?  137 ILE   A CA   1 
ATOM   2855 C  CA   B ILE   A 1 137 ? 10.365 -10.367 -4.138  0.44 14.07 ?  137 ILE   A CA   1 
ATOM   2856 C  C    A ILE   A 1 137 ? 11.503 -10.988 -4.254  0.56 13.49 ?  137 ILE   A C    1 
ATOM   2857 C  C    B ILE   A 1 137 ? 11.560 -11.239 -4.480  0.44 14.16 ?  137 ILE   A C    1 
ATOM   2858 O  O    A ILE   A 1 137 ? 11.821 -11.956 -3.551  0.56 13.73 ?  137 ILE   A O    1 
ATOM   2859 O  O    B ILE   A 1 137 ? 11.877 -12.201 -3.769  0.44 14.50 ?  137 ILE   A O    1 
ATOM   2860 C  CB   A ILE   A 1 137 ? 9.061  -10.364 -4.609  0.56 14.37 ?  137 ILE   A CB   1 
ATOM   2861 C  CB   B ILE   A 1 137 ? 9.111  -10.774 -4.938  0.44 14.50 ?  137 ILE   A CB   1 
ATOM   2862 C  CG1  A ILE   A 1 137 ? 7.920  -9.468  -4.109  0.56 15.73 ?  137 ILE   A CG1  1 
ATOM   2863 C  CG1  B ILE   A 1 137 ? 7.866  -10.058 -4.413  0.44 15.16 ?  137 ILE   A CG1  1 
ATOM   2864 C  CG2  A ILE   A 1 137 ? 8.692  -11.839 -4.472  0.56 14.69 ?  137 ILE   A CG2  1 
ATOM   2865 C  CG2  B ILE   A 1 137 ? 8.905  -12.284 -4.881  0.44 14.99 ?  137 ILE   A CG2  1 
ATOM   2866 C  CD1  A ILE   A 1 137 ? 6.629  -9.639  -4.876  0.56 16.99 ?  137 ILE   A CD1  1 
ATOM   2867 C  CD1  B ILE   A 1 137 ? 6.636  -10.302 -5.260  0.44 15.79 ?  137 ILE   A CD1  1 
ATOM   2868 H  H    A ILE   A 1 137 ? 10.283 -8.235  -4.635  0.56 16.00 ?  137 ILE   A H    1 
ATOM   2869 H  H    B ILE   A 1 137 ? 10.180 -8.563  -4.922  0.44 16.42 ?  137 ILE   A H    1 
ATOM   2870 H  HA   A ILE   A 1 137 ? 10.195 -10.187 -2.904  0.56 16.31 ?  137 ILE   A HA   1 
ATOM   2871 H  HA   B ILE   A 1 137 ? 10.174 -10.500 -3.200  0.44 16.88 ?  137 ILE   A HA   1 
ATOM   2872 H  HB   A ILE   A 1 137 ? 9.203  -10.169 -5.547  0.56 17.24 ?  137 ILE   A HB   1 
ATOM   2873 H  HB   B ILE   A 1 137 ? 9.240  -10.522 -5.864  0.44 17.40 ?  137 ILE   A HB   1 
ATOM   2874 H  HG12 A ILE   A 1 137 ? 7.743  -9.671  -3.179  0.56 18.88 ?  137 ILE   A HG12 1 
ATOM   2875 H  HG12 B ILE   A 1 137 ? 7.678  -10.374 -3.515  0.44 18.19 ?  137 ILE   A HG12 1 
ATOM   2876 H  HG13 A ILE   A 1 137 ? 8.189  -8.536  -4.195  0.56 18.88 ?  137 ILE   A HG13 1 
ATOM   2877 H  HG13 B ILE   A 1 137 ? 8.036  -9.105  -4.400  0.44 18.19 ?  137 ILE   A HG13 1 
ATOM   2878 H  HG21 A ILE   A 1 137 ? 7.821  -11.996 -4.868  0.56 17.63 ?  137 ILE   A HG21 1 
ATOM   2879 H  HG21 B ILE   A 1 137 ? 8.031  -12.507 -5.239  0.44 17.99 ?  137 ILE   A HG21 1 
ATOM   2880 H  HG22 A ILE   A 1 137 ? 9.357  -12.372 -4.931  0.56 17.63 ?  137 ILE   A HG22 1 
ATOM   2881 H  HG22 B ILE   A 1 137 ? 9.588  -12.720 -5.411  0.44 17.99 ?  137 ILE   A HG22 1 
ATOM   2882 H  HG23 A ILE   A 1 137 ? 8.671  -12.069 -3.532  0.56 17.63 ?  137 ILE   A HG23 1 
ATOM   2883 H  HG23 B ILE   A 1 137 ? 8.963  -12.575 -3.958  0.44 17.99 ?  137 ILE   A HG23 1 
ATOM   2884 H  HD11 A ILE   A 1 137 ? 5.942  -9.968  -4.274  0.56 20.39 ?  137 ILE   A HD11 1 
ATOM   2885 H  HD11 B ILE   A 1 137 ? 5.986  -9.610  -5.077  0.44 18.94 ?  137 ILE   A HD11 1 
ATOM   2886 H  HD12 A ILE   A 1 137 ? 6.372  -8.779  -5.238  0.56 20.39 ?  137 ILE   A HD12 1 
ATOM   2887 H  HD12 B ILE   A 1 137 ? 6.891  -10.280 -6.197  0.44 18.94 ?  137 ILE   A HD12 1 
ATOM   2888 H  HD13 A ILE   A 1 137 ? 6.765  -10.268 -5.602  0.56 20.39 ?  137 ILE   A HD13 1 
ATOM   2889 H  HD13 B ILE   A 1 137 ? 6.267  -11.173 -5.041  0.44 18.94 ?  137 ILE   A HD13 1 
ATOM   2890 N  N    A HIS   A 1 138 ? 12.141 -10.697 -5.391  0.56 13.98 ?  138 HIS   A N    1 
ATOM   2891 N  N    B HIS   A 1 138 ? 12.247 -10.912 -5.574  0.44 14.17 ?  138 HIS   A N    1 
ATOM   2892 C  CA   A HIS   A 1 138 ? 13.282 -11.490 -5.844  0.56 14.19 ?  138 HIS   A CA   1 
ATOM   2893 C  CA   B HIS   A 1 138 ? 13.460 -11.635 -5.923  0.44 14.41 ?  138 HIS   A CA   1 
ATOM   2894 C  C    A HIS   A 1 138 ? 14.443 -11.390 -4.862  0.56 13.92 ?  138 HIS   A C    1 
ATOM   2895 C  C    B HIS   A 1 138 ? 14.559 -11.412 -4.891  0.44 13.81 ?  138 HIS   A C    1 
ATOM   2896 O  O    A HIS   A 1 138 ? 15.080 -12.394 -4.521  0.56 13.95 ?  138 HIS   A O    1 
ATOM   2897 O  O    B HIS   A 1 138 ? 15.257 -12.361 -4.517  0.44 13.60 ?  138 HIS   A O    1 
ATOM   2898 C  CB   A HIS   A 1 138 ? 13.705 -11.018 -7.237  0.56 14.30 ?  138 HIS   A CB   1 
ATOM   2899 C  CB   B HIS   A 1 138 ? 13.924 -11.244 -7.323  0.44 15.52 ?  138 HIS   A CB   1 
ATOM   2900 C  CG   A HIS   A 1 138 ? 14.999 -11.606 -7.707  0.56 15.09 ?  138 HIS   A CG   1 
ATOM   2901 C  CG   B HIS   A 1 138 ? 15.163 -11.956 -7.761  0.44 16.50 ?  138 HIS   A CG   1 
ATOM   2902 N  ND1  A HIS   A 1 138 ? 15.157 -12.951 -7.963  0.56 16.38 ?  138 HIS   A ND1  1 
ATOM   2903 N  ND1  B HIS   A 1 138 ? 15.199 -13.314 -8.001  0.44 17.50 ?  138 HIS   A ND1  1 
ATOM   2904 C  CD2  A HIS   A 1 138 ? 16.200 -11.032 -7.959  0.56 15.06 ?  138 HIS   A CD2  1 
ATOM   2905 C  CD2  B HIS   A 1 138 ? 16.417 -11.501 -7.987  0.44 16.87 ?  138 HIS   A CD2  1 
ATOM   2906 C  CE1  A HIS   A 1 138 ? 16.397 -13.180 -8.358  0.56 16.41 ?  138 HIS   A CE1  1 
ATOM   2907 C  CE1  B HIS   A 1 138 ? 16.421 -13.661 -8.365  0.44 17.86 ?  138 HIS   A CE1  1 
ATOM   2908 N  NE2  A HIS   A 1 138 ? 17.053 -12.033 -8.363  0.56 15.47 ?  138 HIS   A NE2  1 
ATOM   2909 N  NE2  B HIS   A 1 138 ? 17.179 -12.579 -8.365  0.44 17.20 ?  138 HIS   A NE2  1 
ATOM   2910 H  H    A HIS   A 1 138 ? 11.932 -10.040 -5.916  0.56 16.77 ?  138 HIS   A H    1 
ATOM   2911 H  H    B HIS   A 1 138 ? 12.031 -10.284 -6.124  0.44 17.00 ?  138 HIS   A H    1 
ATOM   2912 H  HA   A HIS   A 1 138 ? 13.016 -12.414 -5.907  0.56 17.03 ?  138 HIS   A HA   1 
ATOM   2913 H  HA   B HIS   A 1 138 ? 13.261 -12.582 -5.940  0.44 17.29 ?  138 HIS   A HA   1 
ATOM   2914 H  HB2  A HIS   A 1 138 ? 13.016 -11.271 -7.876  0.56 17.16 ?  138 HIS   A HB2  1 
ATOM   2915 H  HB2  B HIS   A 1 138 ? 13.223 -11.455 -7.960  0.44 18.62 ?  138 HIS   A HB2  1 
ATOM   2916 H  HB3  A HIS   A 1 138 ? 13.802 -10.052 -7.230  0.56 17.16 ?  138 HIS   A HB3  1 
ATOM   2917 H  HB3  B HIS   A 1 138 ? 14.111 -10.293 -7.340  0.44 18.62 ?  138 HIS   A HB3  1 
ATOM   2918 H  HD1  A HIS   A 1 138 ? 14.542 -13.547 -7.882  0.56 19.65 ?  138 HIS   A HD1  1 
ATOM   2919 H  HD1  B HIS   A 1 138 ? 14.530 -13.850 -7.929  0.44 21.00 ?  138 HIS   A HD1  1 
ATOM   2920 H  HD2  A HIS   A 1 138 ? 16.406 -10.128 -7.877  0.56 18.08 ?  138 HIS   A HD2  1 
ATOM   2921 H  HD2  B HIS   A 1 138 ? 16.708 -10.623 -7.905  0.44 20.24 ?  138 HIS   A HD2  1 
ATOM   2922 H  HE1  A HIS   A 1 138 ? 16.749 -14.008 -8.590  0.56 19.69 ?  138 HIS   A HE1  1 
ATOM   2923 H  HE1  B HIS   A 1 138 ? 16.699 -14.523 -8.582  0.44 21.44 ?  138 HIS   A HE1  1 
ATOM   2924 N  N    . SER   A 1 139 ? 14.737 -10.177 -4.408  1.00 13.28 ?  139 SER   A N    1 
ATOM   2925 C  CA   . SER   A 1 139 ? 15.801 -9.971  -3.436  1.00 13.10 ?  139 SER   A CA   1 
ATOM   2926 C  C    . SER   A 1 139 ? 15.580 -10.795 -2.174  1.00 12.60 ?  139 SER   A C    1 
ATOM   2927 O  O    . SER   A 1 139 ? 16.530 -11.376 -1.630  1.00 12.84 ?  139 SER   A O    1 
ATOM   2928 C  CB   . SER   A 1 139 ? 15.940 -8.490  -3.103  1.00 12.98 ?  139 SER   A CB   1 
ATOM   2929 O  OG   . SER   A 1 139 ? 17.012 -8.324  -2.191  1.00 13.47 ?  139 SER   A OG   1 
ATOM   2930 H  H    A SER   A 1 139 ? 14.336 -9.455  -4.644  0.56 15.94 ?  139 SER   A H    1 
ATOM   2931 H  H    B SER   A 1 139 ? 14.289 -9.477  -4.624  0.44 15.94 ?  139 SER   A H    1 
ATOM   2932 H  HA   . SER   A 1 139 ? 16.643 -10.257 -3.825  1.00 15.73 ?  139 SER   A HA   1 
ATOM   2933 H  HB2  . SER   A 1 139 ? 16.131 -7.990  -3.916  1.00 15.57 ?  139 SER   A HB2  1 
ATOM   2934 H  HB3  . SER   A 1 139 ? 15.115 -8.169  -2.701  1.00 15.57 ?  139 SER   A HB3  1 
ATOM   2935 H  HG   . SER   A 1 139 ? 17.099 -7.508  -1.991  1.00 16.17 ?  139 SER   A HG   1 
ATOM   2936 N  N    . LEU   A 1 140 ? 14.339 -10.859 -1.691  1.00 12.59 ?  140 LEU   A N    1 
ATOM   2937 C  CA   . LEU   A 1 140 ? 14.065 -11.656 -0.498  1.00 12.59 ?  140 LEU   A CA   1 
ATOM   2938 C  C    . LEU   A 1 140 ? 14.329 -13.136 -0.758  1.00 12.77 ?  140 LEU   A C    1 
ATOM   2939 O  O    . LEU   A 1 140 ? 14.872 -13.844 0.102   1.00 13.65 ?  140 LEU   A O    1 
ATOM   2940 C  CB   . LEU   A 1 140 ? 12.629 -11.419 -0.038  1.00 13.03 ?  140 LEU   A CB   1 
ATOM   2941 C  CG   . LEU   A 1 140 ? 12.165 -12.219 1.176   1.00 13.48 ?  140 LEU   A CG   1 
ATOM   2942 C  CD1  . LEU   A 1 140 ? 13.085 -12.034 2.375   1.00 14.20 ?  140 LEU   A CD1  1 
ATOM   2943 C  CD2  . LEU   A 1 140 ? 10.722 -11.865 1.531   1.00 14.45 ?  140 LEU   A CD2  1 
ATOM   2944 H  H    . LEU   A 1 140 ? 13.651 -10.458 -2.025  1.00 15.11 ?  140 LEU   A H    1 
ATOM   2945 H  HA   . LEU   A 1 140 ? 14.656 -11.370 0.212   1.00 15.11 ?  140 LEU   A HA   1 
ATOM   2946 H  HB2  . LEU   A 1 140 ? 12.529 -10.485 0.180   1.00 15.64 ?  140 LEU   A HB2  1 
ATOM   2947 H  HB3  . LEU   A 1 140 ? 12.035 -11.647 -0.772  1.00 15.64 ?  140 LEU   A HB3  1 
ATOM   2948 H  HG   . LEU   A 1 140 ? 12.166 -13.161 0.946   1.00 16.17 ?  140 LEU   A HG   1 
ATOM   2949 H  HD11 . LEU   A 1 140 ? 12.699 -12.493 3.141   1.00 17.04 ?  140 LEU   A HD11 1 
ATOM   2950 H  HD12 . LEU   A 1 140 ? 13.949 -12.426 2.163   1.00 17.04 ?  140 LEU   A HD12 1 
ATOM   2951 H  HD13 . LEU   A 1 140 ? 13.179 -11.094 2.561   1.00 17.04 ?  140 LEU   A HD13 1 
ATOM   2952 H  HD21 . LEU   A 1 140 ? 10.447 -12.386 2.305   1.00 17.34 ?  140 LEU   A HD21 1 
ATOM   2953 H  HD22 . LEU   A 1 140 ? 10.667 -10.919 1.735   1.00 17.34 ?  140 LEU   A HD22 1 
ATOM   2954 H  HD23 . LEU   A 1 140 ? 10.147 -12.074 0.776   1.00 17.34 ?  140 LEU   A HD23 1 
ATOM   2955 N  N    . ARG   A 1 141 ? 13.941 -13.619 -1.941  1.00 13.20 ?  141 ARG   A N    1 
ATOM   2956 C  CA   . ARG   A 1 141 ? 14.186 -15.011 -2.302  1.00 14.12 ?  141 ARG   A CA   1 
ATOM   2957 C  C    . ARG   A 1 141 ? 15.681 -15.311 -2.315  1.00 13.86 ?  141 ARG   A C    1 
ATOM   2958 O  O    . ARG   A 1 141 ? 16.131 -16.319 -1.757  1.00 14.32 ?  141 ARG   A O    1 
ATOM   2959 C  CB   . ARG   A 1 141 ? 13.571 -15.277 -3.678  1.00 15.75 ?  141 ARG   A CB   1 
ATOM   2960 C  CG   . ARG   A 1 141 ? 13.569 -16.727 -4.122  1.00 18.06 ?  141 ARG   A CG   1 
ATOM   2961 C  CD   . ARG   A 1 141 ? 12.538 -17.500 -3.362  1.00 19.64 ?  141 ARG   A CD   1 
ATOM   2962 N  NE   . ARG   A 1 141 ? 13.136 -18.246 -2.269  1.00 20.59 ?  141 ARG   A NE   1 
ATOM   2963 C  CZ   . ARG   A 1 141 ? 12.445 -18.779 -1.271  1.00 21.26 ?  141 ARG   A CZ   1 
ATOM   2964 N  NH1  . ARG   A 1 141 ? 11.156 -18.525 -1.111  1.00 20.69 ?  141 ARG   A NH1  1 
ATOM   2965 N  NH2  . ARG   A 1 141 ? 13.061 -19.588 -0.413  1.00 22.51 ?  141 ARG   A NH2  1 
ATOM   2966 H  H    . ARG   A 1 141 ? 13.542 -13.158 -2.554  1.00 15.84 ?  141 ARG   A H    1 
ATOM   2967 H  HA   . ARG   A 1 141 ? 13.761 -15.592 -1.656  1.00 16.94 ?  141 ARG   A HA   1 
ATOM   2968 H  HB2  . ARG   A 1 141 ? 12.653 -14.966 -3.674  1.00 18.90 ?  141 ARG   A HB2  1 
ATOM   2969 H  HB3  . ARG   A 1 141 ? 14.075 -14.774 -4.340  1.00 18.90 ?  141 ARG   A HB3  1 
ATOM   2970 H  HG2  . ARG   A 1 141 ? 13.359 -16.779 -5.069  1.00 21.68 ?  141 ARG   A HG2  1 
ATOM   2971 H  HG3  . ARG   A 1 141 ? 14.441 -17.124 -3.950  1.00 21.68 ?  141 ARG   A HG3  1 
ATOM   2972 H  HD2  . ARG   A 1 141 ? 11.886 -16.885 -2.987  1.00 23.57 ?  141 ARG   A HD2  1 
ATOM   2973 H  HD3  . ARG   A 1 141 ? 12.098 -18.125 -3.961  1.00 23.57 ?  141 ARG   A HD3  1 
ATOM   2974 H  HE   . ARG   A 1 141 ? 13.969 -18.445 -2.329  1.00 24.71 ?  141 ARG   A HE   1 
ATOM   2975 H  HH11 . ARG   A 1 141 ? 10.739 -18.014 -1.663  1.00 24.83 ?  141 ARG   A HH11 1 
ATOM   2976 H  HH12 . ARG   A 1 141 ? 10.725 -18.880 -0.452  1.00 24.83 ?  141 ARG   A HH12 1 
ATOM   2977 H  HH21 . ARG   A 1 141 ? 13.899 -19.756 -0.508  1.00 27.01 ?  141 ARG   A HH21 1 
ATOM   2978 H  HH22 . ARG   A 1 141 ? 12.626 -19.930 0.246   1.00 27.01 ?  141 ARG   A HH22 1 
ATOM   2979 N  N    . VAL   A 1 142 ? 16.472 -14.445 -2.955  1.00 13.22 ?  142 VAL   A N    1 
ATOM   2980 C  CA   . VAL   A 1 142 ? 17.919 -14.649 -2.982  1.00 13.41 ?  142 VAL   A CA   1 
ATOM   2981 C  C    . VAL   A 1 142 ? 18.484 -14.623 -1.569  1.00 12.89 ?  142 VAL   A C    1 
ATOM   2982 O  O    . VAL   A 1 142 ? 19.349 -15.435 -1.221  1.00 13.09 ?  142 VAL   A O    1 
ATOM   2983 C  CB   . VAL   A 1 142 ? 18.617 -13.635 -3.911  1.00 13.51 ?  142 VAL   A CB   1 
ATOM   2984 C  CG1  . VAL   A 1 142 ? 20.128 -13.852 -3.875  1.00 13.39 ?  142 VAL   A CG1  1 
ATOM   2985 C  CG2  . VAL   A 1 142 ? 18.106 -13.788 -5.335  1.00 14.49 ?  142 VAL   A CG2  1 
ATOM   2986 H  H    . VAL   A 1 142 ? 16.202 -13.737 -3.372  1.00 15.86 ?  142 VAL   A H    1 
ATOM   2987 H  HA   . VAL   A 1 142 ? 18.095 -15.524 -3.348  1.00 16.09 ?  142 VAL   A HA   1 
ATOM   2988 H  HB   . VAL   A 1 142 ? 18.432 -12.726 -3.614  1.00 16.21 ?  142 VAL   A HB   1 
ATOM   2989 H  HG11 . VAL   A 1 142 ? 20.536 -13.372 -4.614  1.00 16.07 ?  142 VAL   A HG11 1 
ATOM   2990 H  HG12 . VAL   A 1 142 ? 20.479 -13.518 -3.034  1.00 16.07 ?  142 VAL   A HG12 1 
ATOM   2991 H  HG13 . VAL   A 1 142 ? 20.310 -14.800 -3.959  1.00 16.07 ?  142 VAL   A HG13 1 
ATOM   2992 H  HG21 . VAL   A 1 142 ? 18.560 -13.146 -5.905  1.00 17.38 ?  142 VAL   A HG21 1 
ATOM   2993 H  HG22 . VAL   A 1 142 ? 18.296 -14.689 -5.638  1.00 17.38 ?  142 VAL   A HG22 1 
ATOM   2994 H  HG23 . VAL   A 1 142 ? 17.153 -13.626 -5.347  1.00 17.38 ?  142 VAL   A HG23 1 
ATOM   2995 N  N    . CYS   A 1 143 ? 18.017 -13.690 -0.736  1.00 12.67 ?  143 CYS   A N    1 
ATOM   2996 C  CA   . CYS   A 1 143 ? 18.472 -13.638 0.649   1.00 12.57 ?  143 CYS   A CA   1 
ATOM   2997 C  C    . CYS   A 1 143 ? 18.258 -14.976 1.350   1.00 13.08 ?  143 CYS   A C    1 
ATOM   2998 O  O    . CYS   A 1 143 ? 19.187 -15.559 1.921   1.00 13.12 ?  143 CYS   A O    1 
ATOM   2999 C  CB   . CYS   A 1 143 ? 17.731 -12.527 1.389   1.00 12.91 ?  143 CYS   A CB   1 
ATOM   3000 S  SG   . CYS   A 1 143 ? 18.234 -12.346 3.101   1.00 13.26 ?  143 CYS   A SG   1 
ATOM   3001 H  H    . CYS   A 1 143 ? 17.446 -13.086 -0.952  1.00 15.20 ?  143 CYS   A H    1 
ATOM   3002 H  HA   . CYS   A 1 143 ? 19.417 -13.441 0.665   1.00 15.08 ?  143 CYS   A HA   1 
ATOM   3003 H  HB2  . CYS   A 1 143 ? 17.894 -11.685 0.934   1.00 15.49 ?  143 CYS   A HB2  1 
ATOM   3004 H  HB3  . CYS   A 1 143 ? 16.782 -12.722 1.376   1.00 15.49 ?  143 CYS   A HB3  1 
ATOM   3005 H  HG   . CYS   A 1 143 ? 17.650 -11.413 3.575   1.00 15.91 ?  143 CYS   A HG   1 
ATOM   3006 N  N    . VAL   A 1 144 ? 17.029 -15.483 1.302   1.00 13.77 ?  144 VAL   A N    1 
ATOM   3007 C  CA   . VAL   A 1 144 ? 16.700 -16.712 2.012   1.00 15.23 ?  144 VAL   A CA   1 
ATOM   3008 C  C    . VAL   A 1 144 ? 17.512 -17.884 1.479   1.00 14.87 ?  144 VAL   A C    1 
ATOM   3009 O  O    . VAL   A 1 144 ? 17.881 -18.796 2.232   1.00 15.38 ?  144 VAL   A O    1 
ATOM   3010 C  CB   . VAL   A 1 144 ? 15.181 -16.949 1.917   1.00 18.38 ?  144 VAL   A CB   1 
ATOM   3011 C  CG1  . VAL   A 1 144 ? 14.822 -18.380 2.238   1.00 20.41 ?  144 VAL   A CG1  1 
ATOM   3012 C  CG2  . VAL   A 1 144 ? 14.450 -15.950 2.827   1.00 17.97 ?  144 VAL   A CG2  1 
ATOM   3013 H  H    . VAL   A 1 144 ? 16.370 -15.136 0.862   1.00 16.53 ?  144 VAL   A H    1 
ATOM   3014 H  HA   . VAL   A 1 144 ? 16.919 -16.600 2.942   1.00 18.27 ?  144 VAL   A HA   1 
ATOM   3015 H  HB   . VAL   A 1 144 ? 14.891 -16.770 1.004   1.00 22.05 ?  144 VAL   A HB   1 
ATOM   3016 H  HG11 . VAL   A 1 144 ? 13.871 -18.429 2.435   1.00 24.49 ?  144 VAL   A HG11 1 
ATOM   3017 H  HG12 . VAL   A 1 144 ? 15.025 -18.938 1.472   1.00 24.49 ?  144 VAL   A HG12 1 
ATOM   3018 H  HG13 . VAL   A 1 144 ? 15.332 -18.666 3.008   1.00 24.49 ?  144 VAL   A HG13 1 
ATOM   3019 H  HG21 . VAL   A 1 144 ? 13.495 -16.119 2.790   1.00 21.56 ?  144 VAL   A HG21 1 
ATOM   3020 H  HG22 . VAL   A 1 144 ? 14.768 -16.057 3.737   1.00 21.56 ?  144 VAL   A HG22 1 
ATOM   3021 H  HG23 . VAL   A 1 144 ? 14.633 -15.044 2.520   1.00 21.56 ?  144 VAL   A HG23 1 
ATOM   3022 N  N    . ASP   A 1 145 ? 17.771 -17.902 0.174   1.00 15.16 ?  145 ASP   A N    1 
ATOM   3023 C  CA   . ASP   A 1 145 ? 18.479 -19.009 -0.461  1.00 15.59 ?  145 ASP   A CA   1 
ATOM   3024 C  C    . ASP   A 1 145 ? 20.000 -18.863 -0.425  1.00 15.05 ?  145 ASP   A C    1 
ATOM   3025 O  O    . ASP   A 1 145 ? 20.701 -19.753 -0.920  1.00 16.70 ?  145 ASP   A O    1 
ATOM   3026 C  CB   . ASP   A 1 145 ? 18.023 -19.150 -1.915  1.00 17.56 ?  145 ASP   A CB   1 
ATOM   3027 C  CG   . ASP   A 1 145 ? 16.569 -19.583 -2.035  1.00 19.73 ?  145 ASP   A CG   1 
ATOM   3028 O  OD1  . ASP   A 1 145 ? 16.017 -20.141 -1.062  1.00 20.19 ?  145 ASP   A OD1  1 
ATOM   3029 O  OD2  . ASP   A 1 145 ? 15.977 -19.358 -3.109  1.00 21.08 -1 145 ASP   A OD2  1 
ATOM   3030 H  H    . ASP   A 1 145 ? 17.529 -17.284 -0.378  1.00 18.19 ?  145 ASP   A H    1 
ATOM   3031 H  HA   . ASP   A 1 145 ? 18.245 -19.830 -0.001  1.00 18.71 ?  145 ASP   A HA   1 
ATOM   3032 H  HB2  . ASP   A 1 145 ? 18.127 -18.297 -2.366  1.00 21.08 ?  145 ASP   A HB2  1 
ATOM   3033 H  HB3  . ASP   A 1 145 ? 18.564 -19.825 -2.353  1.00 21.08 ?  145 ASP   A HB3  1 
ATOM   3034 N  N    . THR   A 1 146 ? 20.527 -17.777 0.134   1.00 13.27 ?  146 THR   A N    1 
ATOM   3035 C  CA   . THR   A 1 146 ? 21.968 -17.532 0.154   1.00 12.94 ?  146 THR   A CA   1 
ATOM   3036 C  C    . THR   A 1 146 ? 22.520 -17.339 1.554   1.00 12.96 ?  146 THR   A C    1 
ATOM   3037 O  O    . THR   A 1 146 ? 23.597 -17.865 1.868   1.00 13.88 ?  146 THR   A O    1 
ATOM   3038 C  CB   . THR   A 1 146 ? 22.293 -16.280 -0.685  1.00 13.05 ?  146 THR   A CB   1 
ATOM   3039 O  OG1  . THR   A 1 146 ? 21.762 -16.439 -2.004  1.00 13.47 ?  146 THR   A OG1  1 
ATOM   3040 C  CG2  . THR   A 1 146 ? 23.793 -16.052 -0.779  1.00 13.43 ?  146 THR   A CG2  1 
ATOM   3041 H  H    . THR   A 1 146 ? 20.067 -17.156 0.513   1.00 15.93 ?  146 THR   A H    1 
ATOM   3042 H  HA   . THR   A 1 146 ? 22.429 -18.288 -0.240  1.00 15.53 ?  146 THR   A HA   1 
ATOM   3043 H  HB   . THR   A 1 146 ? 21.898 -15.498 -0.266  1.00 15.65 ?  146 THR   A HB   1 
ATOM   3044 H  HG1  . THR   A 1 146 ? 20.926 -16.514 -1.966  1.00 16.16 ?  146 THR   A HG1  1 
ATOM   3045 H  HG21 . THR   A 1 146 ? 23.983 -15.382 -1.451  1.00 16.11 ?  146 THR   A HG21 1 
ATOM   3046 H  HG22 . THR   A 1 146 ? 24.142 -15.753 0.074   1.00 16.11 ?  146 THR   A HG22 1 
ATOM   3047 H  HG23 . THR   A 1 146 ? 24.236 -16.881 -1.028  1.00 16.11 ?  146 THR   A HG23 1 
ATOM   3048 N  N    . VAL   A 1 147 ? 21.840 -16.555 2.385   1.00 12.75 ?  147 VAL   A N    1 
ATOM   3049 C  CA   . VAL   A 1 147 ? 22.325 -16.261 3.724   1.00 13.14 ?  147 VAL   A CA   1 
ATOM   3050 C  C    . VAL   A 1 147 ? 22.007 -17.432 4.639   1.00 13.46 ?  147 VAL   A C    1 
ATOM   3051 O  O    . VAL   A 1 147 ? 20.867 -17.906 4.695   1.00 14.27 ?  147 VAL   A O    1 
ATOM   3052 C  CB   . VAL   A 1 147 ? 21.707 -14.956 4.249   1.00 13.22 ?  147 VAL   A CB   1 
ATOM   3053 C  CG1  . VAL   A 1 147 ? 22.242 -14.648 5.633   1.00 14.06 ?  147 VAL   A CG1  1 
ATOM   3054 C  CG2  . VAL   A 1 147 ? 21.959 -13.805 3.283   1.00 13.25 ?  147 VAL   A CG2  1 
ATOM   3055 H  H    . VAL   A 1 147 ? 21.086 -16.182 2.196   1.00 15.30 ?  147 VAL   A H    1 
ATOM   3056 H  HA   . VAL   A 1 147 ? 23.289 -16.148 3.693   1.00 15.77 ?  147 VAL   A HA   1 
ATOM   3057 H  HB   . VAL   A 1 147 ? 20.749 -15.074 4.328   1.00 15.86 ?  147 VAL   A HB   1 
ATOM   3058 H  HG11 . VAL   A 1 147 ? 21.997 -13.746 5.874   1.00 16.88 ?  147 VAL   A HG11 1 
ATOM   3059 H  HG12 . VAL   A 1 147 ? 21.856 -15.277 6.268   1.00 16.88 ?  147 VAL   A HG12 1 
ATOM   3060 H  HG13 . VAL   A 1 147 ? 23.208 -14.742 5.626   1.00 16.88 ?  147 VAL   A HG13 1 
ATOM   3061 H  HG21 . VAL   A 1 147 ? 21.634 -12.984 3.682   1.00 15.90 ?  147 VAL   A HG21 1 
ATOM   3062 H  HG22 . VAL   A 1 147 ? 22.911 -13.740 3.115   1.00 15.90 ?  147 VAL   A HG22 1 
ATOM   3063 H  HG23 . VAL   A 1 147 ? 21.485 -13.983 2.456   1.00 15.90 ?  147 VAL   A HG23 1 
ATOM   3064 N  N    . ARG   A 1 148 ? 23.030 -17.904 5.348   1.00 13.58 ?  148 ARG   A N    1 
ATOM   3065 C  CA   . ARG   A 1 148 ? 22.902 -18.985 6.309   1.00 13.80 ?  148 ARG   A CA   1 
ATOM   3066 C  C    . ARG   A 1 148 ? 23.029 -18.514 7.744   1.00 14.16 ?  148 ARG   A C    1 
ATOM   3067 O  O    . ARG   A 1 148 ? 22.617 -19.239 8.658   1.00 15.78 ?  148 ARG   A O    1 
ATOM   3068 C  CB   . ARG   A 1 148 ? 23.947 -20.077 6.028   1.00 14.30 ?  148 ARG   A CB   1 
ATOM   3069 C  CG   . ARG   A 1 148 ? 23.779 -20.728 4.663   1.00 15.69 ?  148 ARG   A CG   1 
ATOM   3070 C  CD   . ARG   A 1 148 ? 24.854 -21.769 4.362   1.00 16.25 ?  148 ARG   A CD   1 
ATOM   3071 N  NE   . ARG   A 1 148 ? 26.194 -21.188 4.390   1.00 16.10 ?  148 ARG   A NE   1 
ATOM   3072 C  CZ   . ARG   A 1 148 ? 26.703 -20.434 3.424   1.00 15.43 ?  148 ARG   A CZ   1 
ATOM   3073 N  NH1  . ARG   A 1 148 ? 26.028 -20.191 2.312   1.00 15.83 ?  148 ARG   A NH1  1 
ATOM   3074 N  NH2  . ARG   A 1 148 ? 27.924 -19.917 3.575   1.00 16.00 ?  148 ARG   A NH2  1 
ATOM   3075 H  H    . ARG   A 1 148 ? 23.837 -17.601 5.274   1.00 16.30 ?  148 ARG   A H    1 
ATOM   3076 H  HA   . ARG   A 1 148 ? 22.030 -19.384 6.204   1.00 16.56 ?  148 ARG   A HA   1 
ATOM   3077 H  HB2  . ARG   A 1 148 ? 24.836 -19.694 6.066   1.00 17.16 ?  148 ARG   A HB2  1 
ATOM   3078 H  HB3  . ARG   A 1 148 ? 23.860 -20.777 6.698   1.00 17.16 ?  148 ARG   A HB3  1 
ATOM   3079 H  HG2  . ARG   A 1 148 ? 22.915 -21.165 4.628   1.00 18.83 ?  148 ARG   A HG2  1 
ATOM   3080 H  HG3  . ARG   A 1 148 ? 23.830 -20.038 3.982   1.00 18.83 ?  148 ARG   A HG3  1 
ATOM   3081 H  HD2  . ARG   A 1 148 ? 24.813 -22.474 5.027   1.00 19.50 ?  148 ARG   A HD2  1 
ATOM   3082 H  HD3  . ARG   A 1 148 ? 24.699 -22.141 3.475   1.00 19.50 ?  148 ARG   A HD3  1 
ATOM   3083 H  HE   . ARG   A 1 148 ? 26.683 -21.348 5.074   1.00 19.32 ?  148 ARG   A HE   1 
ATOM   3084 H  HH11 . ARG   A 1 148 ? 25.237 -20.509 2.204   1.00 19.00 ?  148 ARG   A HH11 1 
ATOM   3085 H  HH12 . ARG   A 1 148 ? 26.374 -19.691 1.701   1.00 19.00 ?  148 ARG   A HH12 1 
ATOM   3086 H  HH21 . ARG   A 1 148 ? 28.366 -20.070 4.294   1.00 19.20 ?  148 ARG   A HH21 1 
ATOM   3087 H  HH22 . ARG   A 1 148 ? 28.260 -19.424 2.956   1.00 19.20 ?  148 ARG   A HH22 1 
ATOM   3088 N  N    . THR   A 1 149 ? 23.578 -17.320 7.957   1.00 14.13 ?  149 THR   A N    1 
ATOM   3089 C  CA   . THR   A 1 149 ? 23.656 -16.726 9.277   1.00 14.30 ?  149 THR   A CA   1 
ATOM   3090 C  C    . THR   A 1 149 ? 22.336 -16.022 9.587   1.00 13.88 ?  149 THR   A C    1 
ATOM   3091 O  O    . THR   A 1 149 ? 21.399 -16.014 8.782   1.00 14.27 ?  149 THR   A O    1 
ATOM   3092 C  CB   . THR   A 1 149 ? 24.858 -15.790 9.341   1.00 14.55 ?  149 THR   A CB   1 
ATOM   3093 O  OG1  . THR   A 1 149 ? 24.737 -14.854 8.269   1.00 14.39 ?  149 THR   A OG1  1 
ATOM   3094 C  CG2  . THR   A 1 149 ? 26.163 -16.582 9.207   1.00 14.90 ?  149 THR   A CG2  1 
ATOM   3095 H  H    . THR   A 1 149 ? 23.922 -16.827 7.337   1.00 16.96 ?  149 THR   A H    1 
ATOM   3096 H  HA   . THR   A 1 149 ? 23.780 -17.430 9.931   1.00 17.16 ?  149 THR   A HA   1 
ATOM   3097 H  HB   . THR   A 1 149 ? 24.853 -15.320 10.190  1.00 17.45 ?  149 THR   A HB   1 
ATOM   3098 H  HG1  . THR   A 1 149 ? 25.385 -14.325 8.276   1.00 17.27 ?  149 THR   A HG1  1 
ATOM   3099 H  HG21 . THR   A 1 149 ? 26.919 -15.979 9.270   1.00 17.88 ?  149 THR   A HG21 1 
ATOM   3100 H  HG22 . THR   A 1 149 ? 26.225 -17.244 9.912   1.00 17.88 ?  149 THR   A HG22 1 
ATOM   3101 H  HG23 . THR   A 1 149 ? 26.190 -17.033 8.348   1.00 17.88 ?  149 THR   A HG23 1 
ATOM   3102 N  N    . ASN   A 1 150 ? 22.219 -15.489 10.796  1.00 13.97 ?  150 ASN   A N    1 
ATOM   3103 C  CA   . ASN   A 1 150 ? 20.940 -14.972 11.282  1.00 14.69 ?  150 ASN   A CA   1 
ATOM   3104 C  C    . ASN   A 1 150 ? 20.769 -13.527 10.834  1.00 13.68 ?  150 ASN   A C    1 
ATOM   3105 O  O    . ASN   A 1 150 ? 21.516 -12.638 11.266  1.00 14.84 ?  150 ASN   A O    1 
ATOM   3106 C  CB   . ASN   A 1 150 ? 20.874 -15.092 12.799  1.00 17.39 ?  150 ASN   A CB   1 
ATOM   3107 C  CG   . ASN   A 1 150 ? 20.766 -16.526 13.255  1.00 21.30 ?  150 ASN   A CG   1 
ATOM   3108 O  OD1  . ASN   A 1 150 ? 20.172 -17.356 12.568  1.00 22.65 ?  150 ASN   A OD1  1 
ATOM   3109 N  ND2  . ASN   A 1 150 ? 21.346 -16.832 14.410  1.00 23.50 ?  150 ASN   A ND2  1 
ATOM   3110 H  H    . ASN   A 1 150 ? 22.862 -15.423 11.360  1.00 16.77 ?  150 ASN   A H    1 
ATOM   3111 H  HA   . ASN   A 1 150 ? 20.214 -15.505 10.906  1.00 17.63 ?  150 ASN   A HA   1 
ATOM   3112 H  HB2  . ASN   A 1 150 ? 21.677 -14.715 13.184  1.00 20.86 ?  150 ASN   A HB2  1 
ATOM   3113 H  HB3  . ASN   A 1 150 ? 20.091 -14.616 13.122  1.00 20.86 ?  150 ASN   A HB3  1 
ATOM   3114 H  HD21 . ASN   A 1 150 ? 21.312 -17.639 14.714  1.00 28.19 ?  150 ASN   A HD21 1 
ATOM   3115 H  HD22 . ASN   A 1 150 ? 21.752 -16.224 14.864  1.00 28.19 ?  150 ASN   A HD22 1 
ATOM   3116 N  N    . VAL   A 1 151 ? 19.789 -13.290 9.968   1.00 13.32 ?  151 VAL   A N    1 
ATOM   3117 C  CA   . VAL   A 1 151 ? 19.579 -11.978 9.377   1.00 13.10 ?  151 VAL   A CA   1 
ATOM   3118 C  C    . VAL   A 1 151 ? 18.191 -11.465 9.740   1.00 13.04 ?  151 VAL   A C    1 
ATOM   3119 O  O    . VAL   A 1 151 ? 17.185 -12.174 9.586   1.00 14.27 ?  151 VAL   A O    1 
ATOM   3120 C  CB   . VAL   A 1 151 ? 19.869 -11.965 7.861   1.00 14.37 ?  151 VAL   A CB   1 
ATOM   3121 C  CG1  . VAL   A 1 151 ? 19.042 -12.986 7.107   1.00 15.47 ?  151 VAL   A CG1  1 
ATOM   3122 C  CG2  . VAL   A 1 151 ? 19.676 -10.563 7.284   1.00 14.62 ?  151 VAL   A CG2  1 
ATOM   3123 H  H    . VAL   A 1 151 ? 19.228 -13.888 9.696   1.00 15.99 ?  151 VAL   A H    1 
ATOM   3124 H  HA   . VAL   A 1 151 ? 20.222 -11.369 9.775   1.00 15.72 ?  151 VAL   A HA   1 
ATOM   3125 H  HB   . VAL   A 1 151 ? 20.804 -12.197 7.720   1.00 17.24 ?  151 VAL   A HB   1 
ATOM   3126 H  HG11 . VAL   A 1 151 ? 19.242 -12.925 6.157   1.00 18.57 ?  151 VAL   A HG11 1 
ATOM   3127 H  HG12 . VAL   A 1 151 ? 19.268 -13.876 7.429   1.00 18.57 ?  151 VAL   A HG12 1 
ATOM   3128 H  HG13 . VAL   A 1 151 ? 18.102 -12.810 7.258   1.00 18.57 ?  151 VAL   A HG13 1 
ATOM   3129 H  HG21 . VAL   A 1 151 ? 19.996 -10.549 6.366   1.00 17.55 ?  151 VAL   A HG21 1 
ATOM   3130 H  HG22 . VAL   A 1 151 ? 18.731 -10.339 7.303   1.00 17.55 ?  151 VAL   A HG22 1 
ATOM   3131 H  HG23 . VAL   A 1 151 ? 20.178 -9.929  7.816   1.00 17.55 ?  151 VAL   A HG23 1 
ATOM   3132 N  N    . TYR   A 1 152 ? 18.169 -10.221 10.225  1.00 12.97 ?  152 TYR   A N    1 
ATOM   3133 C  CA   . TYR   A 1 152 ? 16.973 -9.485  10.602  1.00 12.71 ?  152 TYR   A CA   1 
ATOM   3134 C  C    . TYR   A 1 152 ? 16.791 -8.380  9.574   1.00 12.14 ?  152 TYR   A C    1 
ATOM   3135 O  O    . TYR   A 1 152 ? 17.563 -7.413  9.541   1.00 12.54 ?  152 TYR   A O    1 
ATOM   3136 C  CB   . TYR   A 1 152 ? 17.139 -8.942  12.019  1.00 13.44 ?  152 TYR   A CB   1 
ATOM   3137 C  CG   . TYR   A 1 152 ? 17.102 -10.073 13.010  1.00 14.14 ?  152 TYR   A CG   1 
ATOM   3138 C  CD1  . TYR   A 1 152 ? 18.235 -10.829 13.282  1.00 15.53 ?  152 TYR   A CD1  1 
ATOM   3139 C  CD2  . TYR   A 1 152 ? 15.918 -10.431 13.634  1.00 14.45 ?  152 TYR   A CD2  1 
ATOM   3140 C  CE1  . TYR   A 1 152 ? 18.195 -11.893 14.162  1.00 17.04 ?  152 TYR   A CE1  1 
ATOM   3141 C  CE2  . TYR   A 1 152 ? 15.864 -11.502 14.519  1.00 16.24 ?  152 TYR   A CE2  1 
ATOM   3142 C  CZ   . TYR   A 1 152 ? 17.007 -12.226 14.782  1.00 16.89 ?  152 TYR   A CZ   1 
ATOM   3143 O  OH   . TYR   A 1 152 ? 16.959 -13.293 15.656  1.00 19.05 ?  152 TYR   A OH   1 
ATOM   3144 H  H    . TYR   A 1 152 ? 18.889 -9.753  10.334  1.00 15.57 ?  152 TYR   A H    1 
ATOM   3145 H  HA   . TYR   A 1 152 ? 16.206 -10.075 10.575  1.00 15.25 ?  152 TYR   A HA   1 
ATOM   3146 H  HB2  . TYR   A 1 152 ? 17.994 -8.495  12.095  1.00 16.13 ?  152 TYR   A HB2  1 
ATOM   3147 H  HB3  . TYR   A 1 152 ? 16.416 -8.331  12.217  1.00 16.13 ?  152 TYR   A HB3  1 
ATOM   3148 H  HD1  . TYR   A 1 152 ? 19.035 -10.607 12.859  1.00 18.64 ?  152 TYR   A HD1  1 
ATOM   3149 H  HD2  . TYR   A 1 152 ? 15.140 -9.947  13.458  1.00 17.34 ?  152 TYR   A HD2  1 
ATOM   3150 H  HE1  . TYR   A 1 152 ? 18.966 -12.377 14.335  1.00 20.45 ?  152 TYR   A HE1  1 
ATOM   3151 H  HE2  . TYR   A 1 152 ? 15.066 -11.722 14.939  1.00 19.49 ?  152 TYR   A HE2  1 
ATOM   3152 H  HH   . TYR   A 1 152 ? 16.183 -13.370 15.963  1.00 22.86 ?  152 TYR   A HH   1 
ATOM   3153 N  N    . LEU   A 1 153 ? 15.785 -8.549  8.721   1.00 12.14 ?  153 LEU   A N    1 
ATOM   3154 C  CA   . LEU   A 1 153 ? 15.520 -7.649  7.609   1.00 12.01 ?  153 LEU   A CA   1 
ATOM   3155 C  C    . LEU   A 1 153 ? 14.528 -6.569  8.015   1.00 12.12 ?  153 LEU   A C    1 
ATOM   3156 O  O    . LEU   A 1 153 ? 13.421 -6.869  8.477   1.00 13.16 ?  153 LEU   A O    1 
ATOM   3157 C  CB   . LEU   A 1 153 ? 14.964 -8.418  6.410   1.00 12.16 ?  153 LEU   A CB   1 
ATOM   3158 C  CG   . LEU   A 1 153 ? 15.891 -9.438  5.746   1.00 12.59 ?  153 LEU   A CG   1 
ATOM   3159 C  CD1  . LEU   A 1 153 ? 15.101 -10.304 4.778   1.00 13.06 ?  153 LEU   A CD1  1 
ATOM   3160 C  CD2  . LEU   A 1 153 ? 17.036 -8.753  5.012   1.00 13.46 ?  153 LEU   A CD2  1 
ATOM   3161 H  H    . LEU   A 1 153 ? 15.219 -9.202  8.776   1.00 14.56 ?  153 LEU   A H    1 
ATOM   3162 H  HA   . LEU   A 1 153 ? 16.347 -7.231  7.348   1.00 14.42 ?  153 LEU   A HA   1 
ATOM   3163 H  HB2  . LEU   A 1 153 ? 14.174 -8.896  6.697   1.00 14.59 ?  153 LEU   A HB2  1 
ATOM   3164 H  HB3  . LEU   A 1 153 ? 14.721 -7.772  5.729   1.00 14.59 ?  153 LEU   A HB3  1 
ATOM   3165 H  HG   . LEU   A 1 153 ? 16.276 -10.015 6.430   1.00 15.11 ?  153 LEU   A HG   1 
ATOM   3166 H  HD11 . LEU   A 1 153 ? 15.662 -11.025 4.467   1.00 15.67 ?  153 LEU   A HD11 1 
ATOM   3167 H  HD12 . LEU   A 1 153 ? 14.325 -10.656 5.239   1.00 15.67 ?  153 LEU   A HD12 1 
ATOM   3168 H  HD13 . LEU   A 1 153 ? 14.818 -9.752  4.030   1.00 15.67 ?  153 LEU   A HD13 1 
ATOM   3169 H  HD21 . LEU   A 1 153 ? 17.619 -9.437  4.645   1.00 16.15 ?  153 LEU   A HD21 1 
ATOM   3170 H  HD22 . LEU   A 1 153 ? 16.665 -8.214  4.300   1.00 16.15 ?  153 LEU   A HD22 1 
ATOM   3171 H  HD23 . LEU   A 1 153 ? 17.523 -8.201  5.637   1.00 16.15 ?  153 LEU   A HD23 1 
ATOM   3172 N  N    A ALA   A 1 154 ? 14.921 -5.316  7.813   0.56 11.98 ?  154 ALA   A N    1 
ATOM   3173 N  N    B ALA   A 1 154 ? 14.929 -5.314  7.848   0.44 12.08 ?  154 ALA   A N    1 
ATOM   3174 C  CA   A ALA   A 1 154 ? 14.042 -4.169  8.002   0.56 12.07 ?  154 ALA   A CA   1 
ATOM   3175 C  CA   B ALA   A 1 154 ? 14.089 -4.161  8.145   0.44 12.17 ?  154 ALA   A CA   1 
ATOM   3176 C  C    A ALA   A 1 154 ? 13.560 -3.697  6.637   0.56 12.20 ?  154 ALA   A C    1 
ATOM   3177 C  C    B ALA   A 1 154 ? 13.626 -3.572  6.823   0.44 11.81 ?  154 ALA   A C    1 
ATOM   3178 O  O    A ALA   A 1 154 ? 14.370 -3.319  5.784   0.56 12.79 ?  154 ALA   A O    1 
ATOM   3179 O  O    B ALA   A 1 154 ? 14.452 -3.126  6.020   0.44 11.84 ?  154 ALA   A O    1 
ATOM   3180 C  CB   A ALA   A 1 154 ? 14.779 -3.035  8.713   0.56 12.79 ?  154 ALA   A CB   1 
ATOM   3181 C  CB   B ALA   A 1 154 ? 14.871 -3.115  8.942   0.44 12.77 ?  154 ALA   A CB   1 
ATOM   3182 H  H    A ALA   A 1 154 ? 15.718 -5.099  7.565   0.56 14.38 ?  154 ALA   A H    1 
ATOM   3183 H  H    B ALA   A 1 154 ? 15.706 -5.099  7.548   0.44 14.50 ?  154 ALA   A H    1 
ATOM   3184 H  HA   A ALA   A 1 154 ? 13.276 -4.429  8.539   0.56 14.48 ?  154 ALA   A HA   1 
ATOM   3185 H  HA   B ALA   A 1 154 ? 13.315 -4.432  8.660   0.44 14.61 ?  154 ALA   A HA   1 
ATOM   3186 H  HB1  A ALA   A 1 154 ? 14.170 -2.286  8.824   0.56 15.35 ?  154 ALA   A HB1  1 
ATOM   3187 H  HB1  B ALA   A 1 154 ? 14.292 -2.357  9.126   0.44 15.32 ?  154 ALA   A HB1  1 
ATOM   3188 H  HB2  A ALA   A 1 154 ? 15.084 -3.344  9.580   0.56 15.35 ?  154 ALA   A HB2  1 
ATOM   3189 H  HB2  B ALA   A 1 154 ? 15.171 -3.510  9.776   0.44 15.32 ?  154 ALA   A HB2  1 
ATOM   3190 H  HB3  A ALA   A 1 154 ? 15.538 -2.764  8.172   0.56 15.35 ?  154 ALA   A HB3  1 
ATOM   3191 H  HB3  B ALA   A 1 154 ? 15.636 -2.823  8.420   0.44 15.32 ?  154 ALA   A HB3  1 
ATOM   3192 N  N    A VAL   A 1 155 ? 12.246 -3.724  6.437   0.46 12.09 ?  155 VAL   A N    1 
ATOM   3193 N  N    B VAL   A 1 155 ? 12.315 -3.573  6.597   0.44 11.69 ?  155 VAL   A N    1 
ATOM   3194 C  CA   A VAL   A 1 155 ? 11.606 -3.231  5.223   0.46 13.14 ?  155 VAL   A CA   1 
ATOM   3195 C  CA   B VAL   A 1 155 ? 11.726 -3.083  5.355   0.44 12.63 ?  155 VAL   A CA   1 
ATOM   3196 C  CA   T VAL   A 1 155 ? 11.556 -3.261  5.334   0.10 13.31 ?  155 VAL   A CA   1 
ATOM   3197 C  C    A VAL   A 1 155 ? 10.908 -1.925  5.574   0.46 13.91 ?  155 VAL   A C    1 
ATOM   3198 C  C    B VAL   A 1 155 ? 10.998 -1.779  5.661   0.44 13.07 ?  155 VAL   A C    1 
ATOM   3199 C  C    T VAL   A 1 155 ? 10.952 -1.893  5.642   0.10 13.31 ?  155 VAL   A C    1 
ATOM   3200 O  O    A VAL   A 1 155 ? 9.969  -1.917  6.378   0.46 14.20 ?  155 VAL   A O    1 
ATOM   3201 O  O    B VAL   A 1 155 ? 9.988  -1.765  6.374   0.44 13.62 ?  155 VAL   A O    1 
ATOM   3202 O  O    T VAL   A 1 155 ? 10.124 -1.754  6.542   0.10 13.22 ?  155 VAL   A O    1 
ATOM   3203 C  CB   A VAL   A 1 155 ? 10.606 -4.255  4.668   0.46 13.69 ?  155 VAL   A CB   1 
ATOM   3204 C  CB   B VAL   A 1 155 ? 10.807 -4.125  4.704   0.44 13.48 ?  155 VAL   A CB   1 
ATOM   3205 C  CB   T VAL   A 1 155 ? 10.522 -4.233  4.732   0.10 13.41 ?  155 VAL   A CB   1 
ATOM   3206 C  CG1  A VAL   A 1 155 ? 9.935  -3.720  3.413   0.46 14.23 ?  155 VAL   A CG1  1 
ATOM   3207 C  CG1  B VAL   A 1 155 ? 10.152 -3.549  3.459   0.44 14.05 ?  155 VAL   A CG1  1 
ATOM   3208 C  CG1  T VAL   A 1 155 ? 9.856  -3.617  3.513   0.10 13.59 ?  155 VAL   A CG1  1 
ATOM   3209 C  CG2  A VAL   A 1 155 ? 11.306 -5.575  4.388   0.46 14.51 ?  155 VAL   A CG2  1 
ATOM   3210 C  CG2  B VAL   A 1 155 ? 11.614 -5.373  4.348   0.44 14.33 ?  155 VAL   A CG2  1 
ATOM   3211 C  CG2  T VAL   A 1 155 ? 11.189 -5.554  4.372   0.10 13.53 ?  155 VAL   A CG2  1 
ATOM   3212 H  H    A VAL   A 1 155 ? 11.688 -4.041  7.013   0.46 14.51 ?  155 VAL   A H    1 
ATOM   3213 H  H    B VAL   A 1 155 ? 11.731 -3.860  7.164   0.44 14.03 ?  155 VAL   A H    1 
ATOM   3214 H  HA   A VAL   A 1 155 ? 12.280 -3.053  4.552   0.46 15.77 ?  155 VAL   A HA   1 
ATOM   3215 H  HA   B VAL   A 1 155 ? 12.440 -2.887  4.729   0.44 15.15 ?  155 VAL   A HA   1 
ATOM   3216 H  HB   A VAL   A 1 155 ? 9.918  -4.414  5.335   0.46 16.42 ?  155 VAL   A HB   1 
ATOM   3217 H  HB   B VAL   A 1 155 ? 10.111 -4.378  5.332   0.44 16.18 ?  155 VAL   A HB   1 
ATOM   3218 H  HB   T VAL   A 1 155 ? 9.836  -4.415  5.393   0.10 16.09 ?  155 VAL   A HB   1 
ATOM   3219 H  HG11 A VAL   A 1 155 ? 9.430  -4.435  3.000   0.46 17.07 ?  155 VAL   A HG11 1 
ATOM   3220 H  HG11 B VAL   A 1 155 ? 9.739  -4.271  2.960   0.44 16.86 ?  155 VAL   A HG11 1 
ATOM   3221 H  HG11 T VAL   A 1 155 ? 9.376  -4.310  3.033   0.10 16.31 ?  155 VAL   A HG11 1 
ATOM   3222 H  HG12 A VAL   A 1 155 ? 9.339  -2.992  3.656   0.46 17.07 ?  155 VAL   A HG12 1 
ATOM   3223 H  HG12 B VAL   A 1 155 ? 9.476  -2.904  3.725   0.44 16.86 ?  155 VAL   A HG12 1 
ATOM   3224 H  HG12 T VAL   A 1 155 ? 9.239  -2.927  3.802   0.10 16.31 ?  155 VAL   A HG12 1 
ATOM   3225 H  HG13 A VAL   A 1 155 ? 10.617 -3.399  2.804   0.46 17.07 ?  155 VAL   A HG13 1 
ATOM   3226 H  HG13 B VAL   A 1 155 ? 10.829 -3.118  2.917   0.44 16.86 ?  155 VAL   A HG13 1 
ATOM   3227 H  HG13 T VAL   A 1 155 ? 10.540 -3.234  2.941   0.10 16.31 ?  155 VAL   A HG13 1 
ATOM   3228 H  HG21 A VAL   A 1 155 ? 10.685 -6.171  3.948   0.46 17.42 ?  155 VAL   A HG21 1 
ATOM   3229 H  HG21 B VAL   A 1 155 ? 11.028 -6.014  3.913   0.44 17.19 ?  155 VAL   A HG21 1 
ATOM   3230 H  HG21 T VAL   A 1 155 ? 10.527 -6.146  3.983   0.10 16.23 ?  155 VAL   A HG21 1 
ATOM   3231 H  HG22 A VAL   A 1 155 ? 12.072 -5.408  3.814   0.46 17.42 ?  155 VAL   A HG22 1 
ATOM   3232 H  HG22 B VAL   A 1 155 ? 12.333 -5.124  3.747   0.44 17.19 ?  155 VAL   A HG22 1 
ATOM   3233 H  HG22 T VAL   A 1 155 ? 11.899 -5.384  3.732   0.10 16.23 ?  155 VAL   A HG22 1 
ATOM   3234 H  HG23 A VAL   A 1 155 ? 11.603 -5.961  5.228   0.46 17.42 ?  155 VAL   A HG23 1 
ATOM   3235 H  HG23 B VAL   A 1 155 ? 11.979 -5.759  5.159   0.44 17.19 ?  155 VAL   A HG23 1 
ATOM   3236 H  HG23 T VAL   A 1 155 ? 11.559 -5.952  5.176   0.10 16.23 ?  155 VAL   A HG23 1 
ATOM   3237 N  N    A PHE   A 1 156 ? 11.358 -0.821  4.968   0.46 15.08 ?  156 PHE   A N    1 
ATOM   3238 N  N    B PHE   A 1 156 ? 11.526 -0.682  5.112   0.44 13.76 ?  156 PHE   A N    1 
ATOM   3239 N  N    T PHE   A 1 156 ? 11.382 -0.881  4.886   0.10 13.56 ?  156 PHE   A N    1 
ATOM   3240 C  CA   A PHE   A 1 156 ? 10.840 0.491   5.352   0.46 16.87 ?  156 PHE   A CA   1 
ATOM   3241 C  CA   B PHE   A 1 156 ? 11.061 0.664   5.444   0.44 14.84 ?  156 PHE   A CA   1 
ATOM   3242 C  CA   T PHE   A 1 156 ? 10.945 0.487   5.151   0.10 13.92 ?  156 PHE   A CA   1 
ATOM   3243 C  C    A PHE   A 1 156 ? 9.391  0.672   4.920   0.46 17.05 ?  156 PHE   A C    1 
ATOM   3244 C  C    B PHE   A 1 156 ? 9.625  0.901   4.989   0.44 14.69 ?  156 PHE   A C    1 
ATOM   3245 C  C    T PHE   A 1 156 ? 9.493  0.703   4.741   0.10 14.36 ?  156 PHE   A C    1 
ATOM   3246 O  O    A PHE   A 1 156 ? 8.575  1.209   5.678   0.46 17.48 ?  156 PHE   A O    1 
ATOM   3247 O  O    B PHE   A 1 156 ? 8.835  1.525   5.707   0.44 15.23 ?  156 PHE   A O    1 
ATOM   3248 O  O    T PHE   A 1 156 ? 8.721  1.327   5.478   0.10 14.41 ?  156 PHE   A O    1 
ATOM   3249 C  CB   A PHE   A 1 156 ? 11.725 1.598   4.774   0.46 19.01 ?  156 PHE   A CB   1 
ATOM   3250 C  CB   B PHE   A 1 156 ? 12.015 1.650   4.766   0.44 15.81 ?  156 PHE   A CB   1 
ATOM   3251 C  CB   T PHE   A 1 156 ? 11.862 1.466   4.418   0.10 13.89 ?  156 PHE   A CB   1 
ATOM   3252 C  CG   A PHE   A 1 156 ? 11.233 2.989   5.081   0.46 21.24 ?  156 PHE   A CG   1 
ATOM   3253 C  CG   B PHE   A 1 156 ? 11.650 3.105   4.933   0.44 16.14 ?  156 PHE   A CG   1 
ATOM   3254 C  CG   T PHE   A 1 156 ? 11.492 2.911   4.613   0.10 13.99 ?  156 PHE   A CG   1 
ATOM   3255 C  CD1  A PHE   A 1 156 ? 11.226 3.461   6.384   0.46 22.18 ?  156 PHE   A CD1  1 
ATOM   3256 C  CD1  B PHE   A 1 156 ? 12.061 3.813   6.054   0.44 16.39 ?  156 PHE   A CD1  1 
ATOM   3257 C  CD1  T PHE   A 1 156 ? 11.823 3.573   5.785   0.10 14.18 ?  156 PHE   A CD1  1 
ATOM   3258 C  CD2  A PHE   A 1 156 ? 10.781 3.824   4.069   0.46 22.40 ?  156 PHE   A CD2  1 
ATOM   3259 C  CD2  B PHE   A 1 156 ? 10.949 3.783   3.944   0.44 16.89 ?  156 PHE   A CD2  1 
ATOM   3260 C  CD2  T PHE   A 1 156 ? 10.824 3.609   3.620   0.10 14.25 ?  156 PHE   A CD2  1 
ATOM   3261 C  CE1  A PHE   A 1 156 ? 10.773 4.736   6.676   0.46 22.98 ?  156 PHE   A CE1  1 
ATOM   3262 C  CE1  B PHE   A 1 156 ? 11.749 5.151   6.203   0.44 16.65 ?  156 PHE   A CE1  1 
ATOM   3263 C  CE1  T PHE   A 1 156 ? 11.489 4.903   5.965   0.10 14.39 ?  156 PHE   A CE1  1 
ATOM   3264 C  CE2  A PHE   A 1 156 ? 10.327 5.102   4.354   0.46 23.11 ?  156 PHE   A CE2  1 
ATOM   3265 C  CE2  B PHE   A 1 156 ? 10.636 5.126   4.089   0.44 17.08 ?  156 PHE   A CE2  1 
ATOM   3266 C  CE2  T PHE   A 1 156 ? 10.486 4.939   3.795   0.10 14.41 ?  156 PHE   A CE2  1 
ATOM   3267 C  CZ   A PHE   A 1 156 ? 10.326 5.559   5.659   0.46 23.32 ?  156 PHE   A CZ   1 
ATOM   3268 C  CZ   B PHE   A 1 156 ? 11.037 5.807   5.221   0.44 16.84 ?  156 PHE   A CZ   1 
ATOM   3269 C  CZ   T PHE   A 1 156 ? 10.820 5.587   4.969   0.10 14.45 ?  156 PHE   A CZ   1 
ATOM   3270 H  H    A PHE   A 1 156 ? 11.952 -0.806  4.344   0.46 18.10 ?  156 PHE   A H    1 
ATOM   3271 H  H    B PHE   A 1 156 ? 12.183 -0.692  4.549   0.44 16.51 ?  156 PHE   A H    1 
ATOM   3272 H  H    T PHE   A 1 156 ? 11.931 -0.960  4.228   0.10 16.27 ?  156 PHE   A H    1 
ATOM   3273 H  HA   A PHE   A 1 156 ? 10.873 0.572   6.317   0.46 20.24 ?  156 PHE   A HA   1 
ATOM   3274 H  HA   B PHE   A 1 156 ? 11.129 0.805   6.405   0.44 17.81 ?  156 PHE   A HA   1 
ATOM   3275 H  HA   T PHE   A 1 156 ? 11.019 0.661   6.102   0.10 16.71 ?  156 PHE   A HA   1 
ATOM   3276 H  HB2  A PHE   A 1 156 ? 12.620 1.517   5.144   0.46 22.81 ?  156 PHE   A HB2  1 
ATOM   3277 H  HB2  B PHE   A 1 156 ? 12.903 1.534   5.140   0.44 18.97 ?  156 PHE   A HB2  1 
ATOM   3278 H  HB2  T PHE   A 1 156 ? 12.769 1.347   4.743   0.10 16.66 ?  156 PHE   A HB2  1 
ATOM   3279 H  HB3  A PHE   A 1 156 ? 11.761 1.506   3.809   0.46 22.81 ?  156 PHE   A HB3  1 
ATOM   3280 H  HB3  B PHE   A 1 156 ? 12.042 1.459   3.819   0.44 18.97 ?  156 PHE   A HB3  1 
ATOM   3281 H  HB3  T PHE   A 1 156 ? 11.827 1.276   3.468   0.10 16.66 ?  156 PHE   A HB3  1 
ATOM   3282 H  HD1  A PHE   A 1 156 ? 11.526 2.912   7.072   0.46 26.62 ?  156 PHE   A HD1  1 
ATOM   3283 H  HD1  B PHE   A 1 156 ? 12.545 3.374   6.721   0.44 19.67 ?  156 PHE   A HD1  1 
ATOM   3284 H  HD1  T PHE   A 1 156 ? 12.273 3.117   6.460   0.10 17.02 ?  156 PHE   A HD1  1 
ATOM   3285 H  HD2  A PHE   A 1 156 ? 10.782 3.523   3.190   0.46 26.87 ?  156 PHE   A HD2  1 
ATOM   3286 H  HD2  B PHE   A 1 156 ? 10.680 3.325   3.182   0.44 20.26 ?  156 PHE   A HD2  1 
ATOM   3287 H  HD2  T PHE   A 1 156 ? 10.598 3.178   2.828   0.10 17.10 ?  156 PHE   A HD2  1 
ATOM   3288 H  HE1  A PHE   A 1 156 ? 10.772 5.040   7.556   0.46 27.58 ?  156 PHE   A HE1  1 
ATOM   3289 H  HE1  B PHE   A 1 156 ? 12.021 5.606   6.969   0.44 19.98 ?  156 PHE   A HE1  1 
ATOM   3290 H  HE1  T PHE   A 1 156 ? 11.713 5.337   6.758   0.10 17.27 ?  156 PHE   A HE1  1 
ATOM   3291 H  HE2  A PHE   A 1 156 ? 10.027 5.654   3.668   0.46 27.73 ?  156 PHE   A HE2  1 
ATOM   3292 H  HE2  B PHE   A 1 156 ? 10.154 5.564   3.429   0.44 20.50 ?  156 PHE   A HE2  1 
ATOM   3293 H  HE2  T PHE   A 1 156 ? 10.036 5.398   3.123   0.10 17.29 ?  156 PHE   A HE2  1 
ATOM   3294 H  HZ   A PHE   A 1 156 ? 10.021 6.417   5.854   0.46 27.98 ?  156 PHE   A HZ   1 
ATOM   3295 H  HZ   B PHE   A 1 156 ? 10.825 6.704   5.326   0.44 20.21 ?  156 PHE   A HZ   1 
ATOM   3296 H  HZ   T PHE   A 1 156 ? 10.593 6.481   5.089   0.10 17.34 ?  156 PHE   A HZ   1 
ATOM   3297 N  N    A ASP   A 1 157 ? 9.048  0.225   3.716   0.46 17.24 ?  157 ASP   A N    1 
ATOM   3298 N  N    B ASP   A 1 157 ? 9.277  0.422   3.801   0.44 13.78 ?  157 ASP   A N    1 
ATOM   3299 N  N    T ASP   A 1 157 ? 9.104  0.200   3.573   0.10 14.80 ?  157 ASP   A N    1 
ATOM   3300 C  CA   A ASP   A 1 157 ? 7.734  0.494   3.143   0.46 18.14 ?  157 ASP   A CA   1 
ATOM   3301 C  CA   B ASP   A 1 157 ? 8.014  0.742   3.148   0.44 13.83 ?  157 ASP   A CA   1 
ATOM   3302 C  CA   T ASP   A 1 157 ? 7.774  0.452   3.034   0.10 15.33 ?  157 ASP   A CA   1 
ATOM   3303 C  C    A ASP   A 1 157 ? 6.736  -0.530  3.672   0.46 18.17 ?  157 ASP   A C    1 
ATOM   3304 C  C    B ASP   A 1 157 ? 6.931  -0.226  3.615   0.44 14.09 ?  157 ASP   A C    1 
ATOM   3305 C  C    T ASP   A 1 157 ? 6.783  -0.540  3.632   0.10 15.88 ?  157 ASP   A C    1 
ATOM   3306 O  O    A ASP   A 1 157 ? 6.856  -1.727  3.389   0.46 17.87 ?  157 ASP   A O    1 
ATOM   3307 O  O    B ASP   A 1 157 ? 7.051  -1.443  3.422   0.44 14.14 ?  157 ASP   A O    1 
ATOM   3308 O  O    T ASP   A 1 157 ? 6.962  -1.757  3.506   0.10 15.79 ?  157 ASP   A O    1 
ATOM   3309 C  CB   A ASP   A 1 157 ? 7.825  0.438   1.622   0.46 19.49 ?  157 ASP   A CB   1 
ATOM   3310 C  CB   B ASP   A 1 157 ? 8.221  0.639   1.638   0.44 13.60 ?  157 ASP   A CB   1 
ATOM   3311 C  CB   T ASP   A 1 157 ? 7.811  0.322   1.514   0.10 15.46 ?  157 ASP   A CB   1 
ATOM   3312 C  CG   A ASP   A 1 157 ? 6.593  0.993   0.944   0.46 21.17 ?  157 ASP   A CG   1 
ATOM   3313 C  CG   B ASP   A 1 157 ? 7.007  1.069   0.846   0.44 13.79 ?  157 ASP   A CG   1 
ATOM   3314 C  CG   T ASP   A 1 157 ? 6.622  0.975   0.843   0.10 15.65 ?  157 ASP   A CG   1 
ATOM   3315 O  OD1  A ASP   A 1 157 ? 6.405  2.226   0.982   0.46 22.61 ?  157 ASP   A OD1  1 
ATOM   3316 O  OD1  B ASP   A 1 157 ? 5.960  0.384   0.926   0.44 14.31 ?  157 ASP   A OD1  1 
ATOM   3317 O  OD1  T ASP   A 1 157 ? 5.511  0.407   0.910   0.10 15.74 ?  157 ASP   A OD1  1 
ATOM   3318 O  OD2  A ASP   A 1 157 ? 5.810  0.198   0.378   0.46 21.19 -1 157 ASP   A OD2  1 
ATOM   3319 O  OD2  B ASP   A 1 157 ? 7.101  2.095   0.143   0.44 14.34 -1 157 ASP   A OD2  1 
ATOM   3320 O  OD2  T ASP   A 1 157 ? 6.797  2.064   0.257   0.10 15.69 -1 157 ASP   A OD2  1 
ATOM   3321 H  H    A ASP   A 1 157 ? 9.567  -0.246  3.209   0.46 20.69 ?  157 ASP   A H    1 
ATOM   3322 H  H    B ASP   A 1 157 ? 9.789  -0.097  3.343   0.44 16.53 ?  157 ASP   A H    1 
ATOM   3323 H  H    T ASP   A 1 157 ? 9.599  -0.294  3.071   0.10 17.76 ?  157 ASP   A H    1 
ATOM   3324 H  HA   A ASP   A 1 157 ? 7.448  1.381   3.410   0.46 21.77 ?  157 ASP   A HA   1 
ATOM   3325 H  HA   B ASP   A 1 157 ? 7.761  1.656   3.375   0.44 16.59 ?  157 ASP   A HA   1 
ATOM   3326 H  HA   T ASP   A 1 157 ? 7.494  1.352   3.263   0.10 18.40 ?  157 ASP   A HA   1 
ATOM   3327 H  HB2  A ASP   A 1 157 ? 8.596  0.952   1.339   0.46 23.39 ?  157 ASP   A HB2  1 
ATOM   3328 H  HB2  B ASP   A 1 157 ? 8.973  1.205   1.392   0.44 16.32 ?  157 ASP   A HB2  1 
ATOM   3329 H  HB2  T ASP   A 1 157 ? 8.623  0.732   1.183   0.10 18.55 ?  157 ASP   A HB2  1 
ATOM   3330 H  HB3  A ASP   A 1 157 ? 7.929  -0.483  1.351   0.46 23.39 ?  157 ASP   A HB3  1 
ATOM   3331 H  HB3  B ASP   A 1 157 ? 8.423  -0.282  1.414   0.44 16.32 ?  157 ASP   A HB3  1 
ATOM   3332 H  HB3  T ASP   A 1 157 ? 7.798  -0.616  1.280   0.10 18.55 ?  157 ASP   A HB3  1 
ATOM   3333 N  N    A LYS   A 1 158 ? 5.751  -0.060  4.445   0.46 19.18 ?  158 LYS   A N    1 
ATOM   3334 N  N    B LYS   A 1 158 ? 5.871  0.318   4.220   0.44 14.52 ?  158 LYS   A N    1 
ATOM   3335 N  N    T LYS   A 1 158 ? 5.737  -0.022  4.280   0.10 16.61 ?  158 LYS   A N    1 
ATOM   3336 C  CA   A LYS   A 1 158 ? 4.765  -0.972  5.021   0.46 20.41 ?  158 LYS   A CA   1 
ATOM   3337 C  CA   B LYS   A 1 158 ? 4.846  -0.535  4.814   0.44 15.59 ?  158 LYS   A CA   1 
ATOM   3338 C  CA   T LYS   A 1 158 ? 4.749  -0.897  4.904   0.10 17.44 ?  158 LYS   A CA   1 
ATOM   3339 C  C    A LYS   A 1 158 ? 3.987  -1.701  3.934   0.46 19.76 ?  158 LYS   A C    1 
ATOM   3340 C  C    B LYS   A 1 158 ? 4.132  -1.366  3.754   0.44 15.28 ?  158 LYS   A C    1 
ATOM   3341 C  C    T LYS   A 1 158 ? 3.991  -1.708  3.858   0.10 17.52 ?  158 LYS   A C    1 
ATOM   3342 O  O    A LYS   A 1 158 ? 3.761  -2.914  4.030   0.46 19.69 ?  158 LYS   A O    1 
ATOM   3343 O  O    B LYS   A 1 158 ? 3.905  -2.568  3.938   0.44 15.74 ?  158 LYS   A O    1 
ATOM   3344 O  O    T LYS   A 1 158 ? 3.792  -2.917  4.022   0.10 17.53 ?  158 LYS   A O    1 
ATOM   3345 C  CB   A LYS   A 1 158 ? 3.815  -0.216  5.955   0.46 21.98 ?  158 LYS   A CB   1 
ATOM   3346 C  CB   B LYS   A 1 158 ? 3.837  0.296   5.608   0.44 17.52 ?  158 LYS   A CB   1 
ATOM   3347 C  CB   T LYS   A 1 158 ? 3.786  -0.077  5.769   0.10 18.17 ?  158 LYS   A CB   1 
ATOM   3348 C  CG   A LYS   A 1 158 ? 2.564  -1.000  6.371   0.46 23.54 ?  158 LYS   A CG   1 
ATOM   3349 C  CG   B LYS   A 1 158 ? 2.494  -0.408  5.765   0.44 19.32 ?  158 LYS   A CG   1 
ATOM   3350 C  CG   T LYS   A 1 158 ? 2.563  -0.849  6.260   0.10 18.87 ?  158 LYS   A CG   1 
ATOM   3351 C  CD   A LYS   A 1 158 ? 2.892  -2.282  7.142   0.46 24.99 ?  158 LYS   A CD   1 
ATOM   3352 C  CD   B LYS   A 1 158 ? 1.698  0.107   6.946   0.44 21.00 ?  158 LYS   A CD   1 
ATOM   3353 C  CD   T LYS   A 1 158 ? 2.947  -2.047  7.117   0.10 19.60 ?  158 LYS   A CD   1 
ATOM   3354 C  CE   A LYS   A 1 158 ? 1.617  -2.972  7.634   0.46 25.74 ?  158 LYS   A CE   1 
ATOM   3355 C  CE   B LYS   A 1 158 ? 0.206  -0.139  6.758   0.44 22.04 ?  158 LYS   A CE   1 
ATOM   3356 C  CE   T LYS   A 1 158 ? 1.718  -2.847  7.523   0.10 20.09 ?  158 LYS   A CE   1 
ATOM   3357 N  NZ   A LYS   A 1 158 ? 1.877  -4.293  8.282   0.46 26.12 ?  158 LYS   A NZ   1 
ATOM   3358 N  NZ   B LYS   A 1 158 ? -0.119 -1.534  6.355   0.44 22.41 ?  158 LYS   A NZ   1 
ATOM   3359 N  NZ   T LYS   A 1 158 ? 2.070  -4.050  8.327   0.10 20.36 ?  158 LYS   A NZ   1 
ATOM   3360 H  H    A LYS   A 1 158 ? 5.641  0.768   4.649   0.46 23.01 ?  158 LYS   A H    1 
ATOM   3361 H  H    B LYS   A 1 158 ? 5.731  1.167   4.294   0.44 17.43 ?  158 LYS   A H    1 
ATOM   3362 H  H    T LYS   A 1 158 ? 5.583  0.820   4.373   0.10 19.93 ?  158 LYS   A H    1 
ATOM   3363 H  HA   A LYS   A 1 158 ? 5.228  -1.636  5.550   0.46 24.49 ?  158 LYS   A HA   1 
ATOM   3364 H  HA   B LYS   A 1 158 ? 5.276  -1.145  5.432   0.44 18.71 ?  158 LYS   A HA   1 
ATOM   3365 H  HA   T LYS   A 1 158 ? 5.208  -1.520  5.485   0.10 20.93 ?  158 LYS   A HA   1 
ATOM   3366 H  HB2  A LYS   A 1 158 ? 4.295  0.017   6.768   0.46 26.38 ?  158 LYS   A HB2  1 
ATOM   3367 H  HB2  B LYS   A 1 158 ? 4.195  0.464   6.496   0.44 21.02 ?  158 LYS   A HB2  1 
ATOM   3368 H  HB2  T LYS   A 1 158 ? 4.265  0.240   6.554   0.10 21.81 ?  158 LYS   A HB2  1 
ATOM   3369 H  HB3  A LYS   A 1 158 ? 3.518  0.595   5.513   0.46 26.38 ?  158 LYS   A HB3  1 
ATOM   3370 H  HB3  B LYS   A 1 158 ? 3.687  1.137   5.149   0.44 21.02 ?  158 LYS   A HB3  1 
ATOM   3371 H  HB3  T LYS   A 1 158 ? 3.469  0.681   5.255   0.10 21.81 ?  158 LYS   A HB3  1 
ATOM   3372 H  HG2  A LYS   A 1 158 ? 2.023  -0.440  6.949   0.46 28.24 ?  158 LYS   A HG2  1 
ATOM   3373 H  HG2  B LYS   A 1 158 ? 1.968  -0.266  4.961   0.44 23.18 ?  158 LYS   A HG2  1 
ATOM   3374 H  HG2  T LYS   A 1 158 ? 2.017  -0.260  6.802   0.10 22.64 ?  158 LYS   A HG2  1 
ATOM   3375 H  HG3  A LYS   A 1 158 ? 2.050  -1.242  5.583   0.46 28.24 ?  158 LYS   A HG3  1 
ATOM   3376 H  HG3  B LYS   A 1 158 ? 2.646  -1.356  5.902   0.44 23.18 ?  158 LYS   A HG3  1 
ATOM   3377 H  HG3  T LYS   A 1 158 ? 2.048  -1.168  5.501   0.10 22.64 ?  158 LYS   A HG3  1 
ATOM   3378 H  HD2  A LYS   A 1 158 ? 3.365  -2.897  6.562   0.46 29.99 ?  158 LYS   A HD2  1 
ATOM   3379 H  HD2  B LYS   A 1 158 ? 1.987  -0.356  7.749   0.44 25.20 ?  158 LYS   A HD2  1 
ATOM   3380 H  HD2  T LYS   A 1 158 ? 3.536  -2.631  6.615   0.10 23.51 ?  158 LYS   A HD2  1 
ATOM   3381 H  HD3  A LYS   A 1 158 ? 3.434  -2.062  7.916   0.46 29.99 ?  158 LYS   A HD3  1 
ATOM   3382 H  HD3  B LYS   A 1 158 ? 1.843  1.061   7.037   0.44 25.20 ?  158 LYS   A HD3  1 
ATOM   3383 H  HD3  T LYS   A 1 158 ? 3.388  -1.736  7.924   0.10 23.51 ?  158 LYS   A HD3  1 
ATOM   3384 H  HE2  A LYS   A 1 158 ? 1.180  -2.402  8.287   0.46 30.89 ?  158 LYS   A HE2  1 
ATOM   3385 H  HE2  B LYS   A 1 158 ? -0.248 0.042   7.594   0.44 26.45 ?  158 LYS   A HE2  1 
ATOM   3386 H  HE2  T LYS   A 1 158 ? 1.134  -2.286  8.058   0.10 24.11 ?  158 LYS   A HE2  1 
ATOM   3387 H  HE3  A LYS   A 1 158 ? 1.027  -3.122  6.879   0.46 30.89 ?  158 LYS   A HE3  1 
ATOM   3388 H  HE3  B LYS   A 1 158 ? -0.124 0.454   6.065   0.44 26.45 ?  158 LYS   A HE3  1 
ATOM   3389 H  HE3  T LYS   A 1 158 ? 1.254  -3.144  6.724   0.10 24.11 ?  158 LYS   A HE3  1 
ATOM   3390 H  HZ1  A LYS   A 1 158 ? 1.110  -4.657  8.551   0.46 31.35 ?  158 LYS   A HZ1  1 
ATOM   3391 H  HZ1  B LYS   A 1 158 ? -1.001 -1.637  6.297   0.44 26.89 ?  158 LYS   A HZ1  1 
ATOM   3392 H  HZ1  T LYS   A 1 158 ? 1.332  -4.495  8.548   0.10 24.43 ?  158 LYS   A HZ1  1 
ATOM   3393 H  HZ2  A LYS   A 1 158 ? 2.270  -4.844  7.703   0.46 31.35 ?  158 LYS   A HZ2  1 
ATOM   3394 H  HZ2  B LYS   A 1 158 ? 0.245  -1.717  5.562   0.44 26.89 ?  158 LYS   A HZ2  1 
ATOM   3395 H  HZ2  T LYS   A 1 158 ? 2.601  -4.586  7.855   0.10 24.43 ?  158 LYS   A HZ2  1 
ATOM   3396 H  HZ3  A LYS   A 1 158 ? 2.410  -4.187  8.987   0.46 31.35 ?  158 LYS   A HZ3  1 
ATOM   3397 H  HZ3  B LYS   A 1 158 ? 0.199  -2.108  6.957   0.44 26.89 ?  158 LYS   A HZ3  1 
ATOM   3398 H  HZ3  T LYS   A 1 158 ? 2.493  -3.805  9.071   0.10 24.43 ?  158 LYS   A HZ3  1 
ATOM   3399 N  N    A ASN   A 1 159 ? 3.558  -0.982  2.897   0.46 19.48 ?  159 ASN   A N    1 
ATOM   3400 N  N    B ASN   A 1 159 ? 3.751  -0.740  2.641   0.44 15.86 ?  159 ASN   A N    1 
ATOM   3401 N  N    T ASN   A 1 159 ? 3.559  -1.062  2.780   0.10 17.68 ?  159 ASN   A N    1 
ATOM   3402 C  CA   A ASN   A 1 159 ? 2.857  -1.645  1.804   0.46 19.11 ?  159 ASN   A CA   1 
ATOM   3403 C  CA   B ASN   A 1 159 ? 3.053  -1.491  1.604   0.44 16.92 ?  159 ASN   A CA   1 
ATOM   3404 C  CA   T ASN   A 1 159 ? 2.814  -1.749  1.729   0.10 17.78 ?  159 ASN   A CA   1 
ATOM   3405 C  C    A ASN   A 1 159 ? 3.733  -2.712  1.157   0.46 18.20 ?  159 ASN   A C    1 
ATOM   3406 C  C    B ASN   A 1 159 ? 3.930  -2.608  1.050   0.44 16.28 ?  159 ASN   A C    1 
ATOM   3407 C  C    T ASN   A 1 159 ? 3.649  -2.849  1.078   0.10 17.66 ?  159 ASN   A C    1 
ATOM   3408 O  O    A ASN   A 1 159 ? 3.255  -3.805  0.833   0.46 17.93 ?  159 ASN   A O    1 
ATOM   3409 O  O    B ASN   A 1 159 ? 3.449  -3.717  0.792   0.44 15.54 ?  159 ASN   A O    1 
ATOM   3410 O  O    T ASN   A 1 159 ? 3.123  -3.897  0.705   0.10 17.67 ?  159 ASN   A O    1 
ATOM   3411 C  CB   A ASN   A 1 159 ? 2.360  -0.616  0.786   0.46 20.26 ?  159 ASN   A CB   1 
ATOM   3412 C  CB   B ASN   A 1 159 ? 2.568  -0.547  0.503   0.44 19.07 ?  159 ASN   A CB   1 
ATOM   3413 C  CB   T ASN   A 1 159 ? 2.326  -0.753  0.673   0.10 18.11 ?  159 ASN   A CB   1 
ATOM   3414 C  CG   A ASN   A 1 159 ? 1.107  0.109   1.257   0.46 21.43 ?  159 ASN   A CG   1 
ATOM   3415 C  CG   B ASN   A 1 159 ? 1.348  0.255   0.924   0.44 20.95 ?  159 ASN   A CG   1 
ATOM   3416 C  CG   T ASN   A 1 159 ? 1.139  0.064   1.149   0.10 18.44 ?  159 ASN   A CG   1 
ATOM   3417 O  OD1  A ASN   A 1 159 ? 0.288  -0.459  1.982   0.46 22.54 ?  159 ASN   A OD1  1 
ATOM   3418 O  OD1  B ASN   A 1 159 ? 0.570  -0.183  1.767   0.44 21.87 ?  159 ASN   A OD1  1 
ATOM   3419 O  OD1  T ASN   A 1 159 ? 0.314  -0.416  1.928   0.10 18.76 ?  159 ASN   A OD1  1 
ATOM   3420 N  ND2  A ASN   A 1 159 ? 0.953  1.364   0.846   0.46 21.64 ?  159 ASN   A ND2  1 
ATOM   3421 N  ND2  B ASN   A 1 159 ? 1.178  1.433   0.338   0.44 21.63 ?  159 ASN   A ND2  1 
ATOM   3422 N  ND2  T ASN   A 1 159 ? 1.046  1.303   0.683   0.10 18.50 ?  159 ASN   A ND2  1 
ATOM   3423 H  H    A ASN   A 1 159 ? 3.652  -0.130  2.809   0.46 23.38 ?  159 ASN   A H    1 
ATOM   3424 H  H    B ASN   A 1 159 ? 3.881  0.094   2.469   0.44 19.03 ?  159 ASN   A H    1 
ATOM   3425 H  H    T ASN   A 1 159 ? 3.680  -0.225  2.633   0.10 21.22 ?  159 ASN   A H    1 
ATOM   3426 H  HA   A ASN   A 1 159 ? 2.079  -2.093  2.165   0.46 22.93 ?  159 ASN   A HA   1 
ATOM   3427 H  HA   B ASN   A 1 159 ? 2.271  -1.904  1.998   0.44 20.31 ?  159 ASN   A HA   1 
ATOM   3428 H  HA   T ASN   A 1 159 ? 2.035  -2.170  2.120   0.10 21.33 ?  159 ASN   A HA   1 
ATOM   3429 H  HB2  A ASN   A 1 159 ? 3.052  0.048   0.638   0.46 24.31 ?  159 ASN   A HB2  1 
ATOM   3430 H  HB2  B ASN   A 1 159 ? 3.270  0.083   0.285   0.44 22.89 ?  159 ASN   A HB2  1 
ATOM   3431 H  HB2  T ASN   A 1 159 ? 3.046  -0.140  0.458   0.10 21.73 ?  159 ASN   A HB2  1 
ATOM   3432 H  HB3  A ASN   A 1 159 ? 2.150  -1.067  -0.047  0.46 24.31 ?  159 ASN   A HB3  1 
ATOM   3433 H  HB3  B ASN   A 1 159 ? 2.329  -1.068  -0.281  0.44 22.89 ?  159 ASN   A HB3  1 
ATOM   3434 H  HB3  T ASN   A 1 159 ? 2.057  -1.241  -0.123  0.10 21.73 ?  159 ASN   A HB3  1 
ATOM   3435 H  HD21 A ASN   A 1 159 ? 0.261  1.816   1.085   0.46 25.97 ?  159 ASN   A HD21 1 
ATOM   3436 H  HD21 B ASN   A 1 159 ? 0.494  1.918   0.541   0.44 25.95 ?  159 ASN   A HD21 1 
ATOM   3437 H  HD21 T ASN   A 1 159 ? 0.389  1.804   0.924   0.10 22.21 ?  159 ASN   A HD21 1 
ATOM   3438 H  HD22 A ASN   A 1 159 ? 1.547  1.728   0.339   0.46 25.97 ?  159 ASN   A HD22 1 
ATOM   3439 H  HD22 B ASN   A 1 159 ? 1.742  1.708   -0.245  0.44 25.95 ?  159 ASN   A HD22 1 
ATOM   3440 H  HD22 T ASN   A 1 159 ? 1.641  1.604   0.141   0.10 22.21 ?  159 ASN   A HD22 1 
ATOM   3441 N  N    A LEU   A 1 160 ? 5.028  -2.435  0.996   0.46 17.42 ?  160 LEU   A N    1 
ATOM   3442 N  N    B LEU   A 1 160 ? 5.229  -2.348  0.893   0.44 15.93 ?  160 LEU   A N    1 
ATOM   3443 N  N    T LEU   A 1 160 ? 4.949  -2.611  0.948   0.10 17.50 ?  160 LEU   A N    1 
ATOM   3444 C  CA   A LEU   A 1 160 ? 5.916  -3.450  0.438   0.46 17.00 ?  160 LEU   A CA   1 
ATOM   3445 C  CA   B LEU   A 1 160 ? 6.126  -3.393  0.407   0.44 16.02 ?  160 LEU   A CA   1 
ATOM   3446 C  CA   T LEU   A 1 160 ? 5.845  -3.606  0.370   0.10 17.42 ?  160 LEU   A CA   1 
ATOM   3447 C  C    A LEU   A 1 160 ? 6.095  -4.619  1.400   0.46 16.28 ?  160 LEU   A C    1 
ATOM   3448 C  C    B LEU   A 1 160 ? 6.241  -4.535  1.412   0.44 15.19 ?  160 LEU   A C    1 
ATOM   3449 O  O    A LEU   A 1 160 ? 6.114  -5.782  0.978   0.46 16.51 ?  160 LEU   A O    1 
ATOM   3450 O  O    B LEU   A 1 160 ? 6.203  -5.711  1.030   0.44 15.60 ?  160 LEU   A O    1 
ATOM   3451 C  CB   A LEU   A 1 160 ? 7.265  -2.836  0.071   0.46 17.11 ?  160 LEU   A CB   1 
ATOM   3452 C  CB   B LEU   A 1 160 ? 7.501  -2.806  0.092   0.44 16.78 ?  160 LEU   A CB   1 
ATOM   3453 C  CB   T LEU   A 1 160 ? 7.227  -3.003  0.116   0.10 17.33 ?  160 LEU   A CB   1 
ATOM   3454 C  CG   A LEU   A 1 160 ? 8.314  -3.845  -0.395  0.46 17.89 ?  160 LEU   A CG   1 
ATOM   3455 C  CG   B LEU   A 1 160 ? 8.548  -3.830  -0.356  0.44 17.79 ?  160 LEU   A CG   1 
ATOM   3456 C  CG   T LEU   A 1 160 ? 8.312  -3.991  -0.312  0.10 17.34 ?  160 LEU   A CG   1 
ATOM   3457 C  CD1  A LEU   A 1 160 ? 7.788  -4.682  -1.549  0.46 18.65 ?  160 LEU   A CD1  1 
ATOM   3458 C  CD1  B LEU   A 1 160 ? 8.100  -4.553  -1.616  0.44 18.10 ?  160 LEU   A CD1  1 
ATOM   3459 C  CD1  T LEU   A 1 160 ? 7.886  -4.764  -1.546  0.10 17.43 ?  160 LEU   A CD1  1 
ATOM   3460 C  CD2  A LEU   A 1 160 ? 9.583  -3.124  -0.793  0.46 17.89 ?  160 LEU   A CD2  1 
ATOM   3461 C  CD2  B LEU   A 1 160 ? 9.893  -3.167  -0.574  0.44 18.24 ?  160 LEU   A CD2  1 
ATOM   3462 C  CD2  T LEU   A 1 160 ? 9.621  -3.263  -0.559  0.10 17.31 ?  160 LEU   A CD2  1 
ATOM   3463 H  H    A LEU   A 1 160 ? 5.410  -1.689  1.205   0.46 20.91 ?  160 LEU   A H    1 
ATOM   3464 H  H    B LEU   A 1 160 ? 5.604  -1.594  1.071   0.44 19.12 ?  160 LEU   A H    1 
ATOM   3465 H  H    T LEU   A 1 160 ? 5.338  -1.881  1.188   0.10 21.00 ?  160 LEU   A H    1 
ATOM   3466 H  HA   A LEU   A 1 160 ? 5.520  -3.790  -0.372  0.46 20.40 ?  160 LEU   A HA   1 
ATOM   3467 H  HA   B LEU   A 1 160 ? 5.759  -3.748  -0.416  0.44 19.23 ?  160 LEU   A HA   1 
ATOM   3468 H  HB2  A LEU   A 1 160 ? 7.143  -2.177  -0.639  0.46 20.54 ?  160 LEU   A HB2  1 
ATOM   3469 H  HB2  B LEU   A 1 160 ? 7.406  -2.150  -0.618  0.44 20.14 ?  160 LEU   A HB2  1 
ATOM   3470 H  HB2  T LEU   A 1 160 ? 7.147  -2.324  -0.576  0.10 20.80 ?  160 LEU   A HB2  1 
ATOM   3471 H  HB3  A LEU   A 1 160 ? 7.629  -2.407  0.857   0.46 20.54 ?  160 LEU   A HB3  1 
ATOM   3472 H  HB3  B LEU   A 1 160 ? 7.841  -2.372  0.890   0.44 20.14 ?  160 LEU   A HB3  1 
ATOM   3473 H  HB3  T LEU   A 1 160 ? 7.535  -2.598  0.939   0.10 20.80 ?  160 LEU   A HB3  1 
ATOM   3474 H  HG   A LEU   A 1 160 ? 8.533  -4.441  0.339   0.46 21.47 ?  160 LEU   A HG   1 
ATOM   3475 H  HG   B LEU   A 1 160 ? 8.660  -4.492  0.342   0.44 21.35 ?  160 LEU   A HG   1 
ATOM   3476 H  HG   T LEU   A 1 160 ? 8.458  -4.626  0.408   0.10 20.81 ?  160 LEU   A HG   1 
ATOM   3477 H  HD11 A LEU   A 1 160 ? 8.497  -5.260  -1.864  0.46 22.38 ?  160 LEU   A HD11 1 
ATOM   3478 H  HD11 B LEU   A 1 160 ? 8.829  -5.105  -1.937  0.44 21.73 ?  160 LEU   A HD11 1 
ATOM   3479 H  HD11 T LEU   A 1 160 ? 8.631  -5.303  -1.852  0.10 20.92 ?  160 LEU   A HD11 1 
ATOM   3480 H  HD12 A LEU   A 1 160 ? 7.041  -5.218  -1.240  0.46 22.38 ?  160 LEU   A HD12 1 
ATOM   3481 H  HD12 B LEU   A 1 160 ? 7.332  -5.109  -1.405  0.44 21.73 ?  160 LEU   A HD12 1 
ATOM   3482 H  HD12 T LEU   A 1 160 ? 7.136  -5.335  -1.318  0.10 20.92 ?  160 LEU   A HD12 1 
ATOM   3483 H  HD13 A LEU   A 1 160 ? 7.499  -4.090  -2.261  0.46 22.38 ?  160 LEU   A HD13 1 
ATOM   3484 H  HD13 B LEU   A 1 160 ? 7.860  -3.897  -2.288  0.44 21.73 ?  160 LEU   A HD13 1 
ATOM   3485 H  HD13 T LEU   A 1 160 ? 7.627  -4.134  -2.237  0.10 20.92 ?  160 LEU   A HD13 1 
ATOM   3486 H  HD21 A LEU   A 1 160 ? 10.239 -3.777  -1.081  0.46 21.46 ?  160 LEU   A HD21 1 
ATOM   3487 H  HD21 B LEU   A 1 160 ? 10.534 -3.840  -0.853  0.44 21.89 ?  160 LEU   A HD21 1 
ATOM   3488 H  HD21 T LEU   A 1 160 ? 10.294 -3.908  -0.825  0.10 20.77 ?  160 LEU   A HD21 1 
ATOM   3489 H  HD22 A LEU   A 1 160 ? 9.383  -2.513  -1.519  0.46 21.46 ?  160 LEU   A HD22 1 
ATOM   3490 H  HD22 B LEU   A 1 160 ? 9.804  -2.489  -1.262  0.44 21.89 ?  160 LEU   A HD22 1 
ATOM   3491 H  HD22 T LEU   A 1 160 ? 9.490  -2.611  -1.265  0.10 20.77 ?  160 LEU   A HD22 1 
ATOM   3492 H  HD23 A LEU   A 1 160 ? 9.920  -2.631  -0.028  0.46 21.46 ?  160 LEU   A HD23 1 
ATOM   3493 H  HD23 B LEU   A 1 160 ? 10.183 -2.759  0.257   0.44 21.89 ?  160 LEU   A HD23 1 
ATOM   3494 H  HD23 T LEU   A 1 160 ? 9.895  -2.816  0.257   0.10 20.77 ?  160 LEU   A HD23 1 
ATOM   3495 N  N    A TYR   A 1 161 ? 6.229  -4.332  2.695   0.56 15.82 ?  161 TYR   A N    1 
ATOM   3496 N  N    B TYR   A 1 161 ? 6.394  -4.211  2.697   0.44 14.41 ?  161 TYR   A N    1 
ATOM   3497 C  CA   A TYR   A 1 161 ? 6.365  -5.397  3.684   0.56 15.72 ?  161 TYR   A CA   1 
ATOM   3498 C  CA   B TYR   A 1 161 ? 6.438  -5.251  3.721   0.44 14.28 ?  161 TYR   A CA   1 
ATOM   3499 C  C    A TYR   A 1 161 ? 5.218  -6.399  3.587   0.56 15.94 ?  161 TYR   A C    1 
ATOM   3500 C  C    B TYR   A 1 161 ? 5.209  -6.146  3.643   0.44 14.43 ?  161 TYR   A C    1 
ATOM   3501 O  O    A TYR   A 1 161 ? 5.436  -7.616  3.585   0.56 15.71 ?  161 TYR   A O    1 
ATOM   3502 O  O    B TYR   A 1 161 ? 5.316  -7.378  3.635   0.44 14.16 ?  161 TYR   A O    1 
ATOM   3503 C  CB   A TYR   A 1 161 ? 6.435  -4.792  5.086   0.56 15.67 ?  161 TYR   A CB   1 
ATOM   3504 C  CB   B TYR   A 1 161 ? 6.548  -4.624  5.111   0.44 14.15 ?  161 TYR   A CB   1 
ATOM   3505 C  CG   A TYR   A 1 161 ? 6.367  -5.833  6.168   0.56 15.17 ?  161 TYR   A CG   1 
ATOM   3506 C  CG   B TYR   A 1 161 ? 6.445  -5.658  6.208   0.44 13.75 ?  161 TYR   A CG   1 
ATOM   3507 C  CD1  A TYR   A 1 161 ? 7.503  -6.517  6.571   0.56 15.18 ?  161 TYR   A CD1  1 
ATOM   3508 C  CD1  B TYR   A 1 161 ? 7.544  -6.418  6.571   0.44 14.14 ?  161 TYR   A CD1  1 
ATOM   3509 C  CD2  A TYR   A 1 161 ? 5.161  -6.148  6.777   0.56 14.96 ?  161 TYR   A CD2  1 
ATOM   3510 C  CD2  B TYR   A 1 161 ? 5.247  -5.877  6.879   0.44 13.37 ?  161 TYR   A CD2  1 
ATOM   3511 C  CE1  A TYR   A 1 161 ? 7.441  -7.480  7.550   0.56 14.79 ?  161 TYR   A CE1  1 
ATOM   3512 C  CE1  B TYR   A 1 161 ? 7.459  -7.368  7.565   0.44 14.02 ?  161 TYR   A CE1  1 
ATOM   3513 C  CE2  A TYR   A 1 161 ? 5.089  -7.110  7.754   0.56 14.47 ?  161 TYR   A CE2  1 
ATOM   3514 C  CE2  B TYR   A 1 161 ? 5.153  -6.828  7.879   0.44 13.31 ?  161 TYR   A CE2  1 
ATOM   3515 C  CZ   A TYR   A 1 161 ? 6.232  -7.774  8.139   0.56 14.58 ?  161 TYR   A CZ   1 
ATOM   3516 C  CZ   B TYR   A 1 161 ? 6.264  -7.570  8.217   0.44 13.92 ?  161 TYR   A CZ   1 
ATOM   3517 O  OH   A TYR   A 1 161 ? 6.183  -8.738  9.116   0.56 15.11 ?  161 TYR   A OH   1 
ATOM   3518 O  OH   B TYR   A 1 161 ? 6.197  -8.522  9.208   0.44 14.82 ?  161 TYR   A OH   1 
ATOM   3519 H  H    A TYR   A 1 161 ? 6.236  -3.537  3.024   0.56 18.98 ?  161 TYR   A H    1 
ATOM   3520 H  H    B TYR   A 1 161 ? 6.469  -3.407  2.991   0.44 17.30 ?  161 TYR   A H    1 
ATOM   3521 H  HA   A TYR   A 1 161 ? 7.191  -5.874  3.521   0.56 18.87 ?  161 TYR   A HA   1 
ATOM   3522 H  HA   B TYR   A 1 161 ? 7.223  -5.797  3.577   0.44 17.14 ?  161 TYR   A HA   1 
ATOM   3523 H  HB2  A TYR   A 1 161 ? 7.275  -4.316  5.183   0.56 18.80 ?  161 TYR   A HB2  1 
ATOM   3524 H  HB2  B TYR   A 1 161 ? 7.409  -4.179  5.195   0.44 16.98 ?  161 TYR   A HB2  1 
ATOM   3525 H  HB3  A TYR   A 1 161 ? 5.691  -4.183  5.209   0.56 18.80 ?  161 TYR   A HB3  1 
ATOM   3526 H  HB3  B TYR   A 1 161 ? 5.832  -3.980  5.232   0.44 16.98 ?  161 TYR   A HB3  1 
ATOM   3527 H  HD1  A TYR   A 1 161 ? 8.321  -6.322  6.173   0.56 18.22 ?  161 TYR   A HD1  1 
ATOM   3528 H  HD1  B TYR   A 1 161 ? 8.354  -6.286  6.133   0.44 16.96 ?  161 TYR   A HD1  1 
ATOM   3529 H  HD2  A TYR   A 1 161 ? 4.386  -5.707  6.518   0.56 17.95 ?  161 TYR   A HD2  1 
ATOM   3530 H  HD2  B TYR   A 1 161 ? 4.495  -5.376  6.658   0.44 16.05 ?  161 TYR   A HD2  1 
ATOM   3531 H  HE1  A TYR   A 1 161 ? 8.213  -7.930  7.812   0.56 17.74 ?  161 TYR   A HE1  1 
ATOM   3532 H  HE1  B TYR   A 1 161 ? 8.209  -7.871  7.796   0.44 16.83 ?  161 TYR   A HE1  1 
ATOM   3533 H  HE2  A TYR   A 1 161 ? 4.272  -7.312  8.155   0.56 17.36 ?  161 TYR   A HE2  1 
ATOM   3534 H  HE2  B TYR   A 1 161 ? 4.345  -6.963  8.324   0.44 15.97 ?  161 TYR   A HE2  1 
ATOM   3535 H  HH   A TYR   A 1 161 ? 5.392  -8.827  9.396   0.56 18.13 ?  161 TYR   A HH   1 
ATOM   3536 H  HH   B TYR   A 1 161 ? 5.415  -8.554  9.527   0.44 17.78 ?  161 TYR   A HH   1 
ATOM   3537 N  N    A ASP   A 1 162 ? 3.983  -5.903  3.512   0.56 16.62 ?  162 ASP   A N    1 
ATOM   3538 N  N    B ASP   A 1 162 ? 4.023  -5.536  3.598   0.44 14.50 ?  162 ASP   A N    1 
ATOM   3539 C  CA   A ASP   A 1 162 ? 2.833  -6.803  3.476   0.56 17.30 ?  162 ASP   A CA   1 
ATOM   3540 C  CA   B ASP   A 1 162 ? 2.800  -6.324  3.472   0.44 14.99 ?  162 ASP   A CA   1 
ATOM   3541 C  C    A ASP   A 1 162 ? 2.870  -7.693  2.241   0.56 17.50 ?  162 ASP   A C    1 
ATOM   3542 C  C    B ASP   A 1 162 ? 2.843  -7.204  2.228   0.44 15.08 ?  162 ASP   A C    1 
ATOM   3543 O  O    A ASP   A 1 162 ? 2.519  -8.877  2.310   0.56 17.60 ?  162 ASP   A O    1 
ATOM   3544 O  O    B ASP   A 1 162 ? 2.482  -8.388  2.277   0.44 15.31 ?  162 ASP   A O    1 
ATOM   3545 C  CB   A ASP   A 1 162 ? 1.529  -6.006  3.515   0.56 18.34 ?  162 ASP   A CB   1 
ATOM   3546 C  CB   B ASP   A 1 162 ? 1.586  -5.395  3.426   0.44 15.54 ?  162 ASP   A CB   1 
ATOM   3547 C  CG   A ASP   A 1 162 ? 1.246  -5.403  4.876   0.56 19.94 ?  162 ASP   A CG   1 
ATOM   3548 C  CG   B ASP   A 1 162 ? 1.321  -4.701  4.749   0.44 15.56 ?  162 ASP   A CG   1 
ATOM   3549 O  OD1  A ASP   A 1 162 ? 1.837  -5.865  5.874   0.56 20.84 ?  162 ASP   A OD1  1 
ATOM   3550 O  OD1  B ASP   A 1 162 ? 1.828  -5.161  5.790   0.44 15.80 ?  162 ASP   A OD1  1 
ATOM   3551 O  OD2  A ASP   A 1 162 ? 0.404  -4.481  4.949   0.56 20.71 -1 162 ASP   A OD2  1 
ATOM   3552 O  OD2  B ASP   A 1 162 ? 0.591  -3.687  4.749   0.44 15.71 -1 162 ASP   A OD2  1 
ATOM   3553 H  H    A ASP   A 1 162 ? 3.783  -5.067  3.477   0.56 19.95 ?  162 ASP   A H    1 
ATOM   3554 H  H    B ASP   A 1 162 ? 3.905  -4.680  3.640   0.44 17.40 ?  162 ASP   A H    1 
ATOM   3555 H  HA   A ASP   A 1 162 ? 2.856  -7.380  4.253   0.56 20.76 ?  162 ASP   A HA   1 
ATOM   3556 H  HA   B ASP   A 1 162 ? 2.711  -6.892  4.250   0.44 17.98 ?  162 ASP   A HA   1 
ATOM   3557 H  HB2  A ASP   A 1 162 ? 1.578  -5.284  2.873   0.56 22.01 ?  162 ASP   A HB2  1 
ATOM   3558 H  HB2  B ASP   A 1 162 ? 1.731  -4.708  2.754   0.44 18.64 ?  162 ASP   A HB2  1 
ATOM   3559 H  HB3  A ASP   A 1 162 ? 0.790  -6.597  3.295   0.56 22.01 ?  162 ASP   A HB3  1 
ATOM   3560 H  HB3  B ASP   A 1 162 ? 0.798  -5.910  3.210   0.44 18.64 ?  162 ASP   A HB3  1 
ATOM   3561 N  N    A LYS   A 1 163 ? 3.291  -7.142  1.102   0.56 18.03 ?  163 LYS   A N    1 
ATOM   3562 N  N    B LYS   A 1 163 ? 3.287  -6.640  1.101   0.44 15.81 ?  163 LYS   A N    1 
ATOM   3563 C  CA   A LYS   A 1 163 ? 3.367  -7.937  -0.118  0.56 19.21 ?  163 LYS   A CA   1 
ATOM   3564 C  CA   B LYS   A 1 163 ? 3.381  -7.420  -0.128  0.44 16.77 ?  163 LYS   A CA   1 
ATOM   3565 C  C    A LYS   A 1 163 ? 4.464  -8.993  -0.024  0.56 17.95 ?  163 LYS   A C    1 
ATOM   3566 C  C    B LYS   A 1 163 ? 4.407  -8.540  0.007   0.44 15.52 ?  163 LYS   A C    1 
ATOM   3567 O  O    A LYS   A 1 163 ? 4.292  -10.120 -0.503  0.56 18.39 ?  163 LYS   A O    1 
ATOM   3568 O  O    B LYS   A 1 163 ? 4.197  -9.650  -0.498  0.44 15.02 ?  163 LYS   A O    1 
ATOM   3569 C  CB   A LYS   A 1 163 ? 3.605  -7.016  -1.313  0.56 22.24 ?  163 LYS   A CB   1 
ATOM   3570 C  CB   B LYS   A 1 163 ? 3.733  -6.508  -1.308  0.44 19.60 ?  163 LYS   A CB   1 
ATOM   3571 C  CG   A LYS   A 1 163 ? 3.611  -7.715  -2.656  0.56 25.26 ?  163 LYS   A CG   1 
ATOM   3572 C  CG   B LYS   A 1 163 ? 3.849  -7.258  -2.630  0.44 22.76 ?  163 LYS   A CG   1 
ATOM   3573 C  CD   A LYS   A 1 163 ? 4.066  -6.764  -3.746  0.56 27.90 ?  163 LYS   A CD   1 
ATOM   3574 C  CD   B LYS   A 1 163 ? 4.092  -6.333  -3.811  0.44 25.77 ?  163 LYS   A CD   1 
ATOM   3575 C  CE   A LYS   A 1 163 ? 3.948  -7.393  -5.121  0.56 29.71 ?  163 LYS   A CE   1 
ATOM   3576 C  CE   B LYS   A 1 163 ? 3.761  -7.035  -5.124  0.44 27.92 ?  163 LYS   A CE   1 
ATOM   3577 N  NZ   A LYS   A 1 163 ? 4.669  -6.601  -6.155  0.56 30.60 ?  163 LYS   A NZ   1 
ATOM   3578 N  NZ   B LYS   A 1 163 ? 4.065  -6.194  -6.315  0.44 29.03 ?  163 LYS   A NZ   1 
ATOM   3579 H  H    A LYS   A 1 163 ? 3.533  -6.320  1.012   0.56 21.64 ?  163 LYS   A H    1 
ATOM   3580 H  H    B LYS   A 1 163 ? 3.532  -5.815  1.026   0.44 18.98 ?  163 LYS   A H    1 
ATOM   3581 H  HA   A LYS   A 1 163 ? 2.521  -8.392  -0.254  0.56 23.06 ?  163 LYS   A HA   1 
ATOM   3582 H  HA   B LYS   A 1 163 ? 2.520  -7.824  -0.308  0.44 20.12 ?  163 LYS   A HA   1 
ATOM   3583 H  HB2  A LYS   A 1 163 ? 2.898  -6.348  -1.335  0.56 26.68 ?  163 LYS   A HB2  1 
ATOM   3584 H  HB2  B LYS   A 1 163 ? 3.036  -5.836  -1.407  0.44 23.51 ?  163 LYS   A HB2  1 
ATOM   3585 H  HB3  A LYS   A 1 163 ? 4.462  -6.579  -1.205  0.56 26.68 ?  163 LYS   A HB3  1 
ATOM   3586 H  HB3  B LYS   A 1 163 ? 4.582  -6.076  -1.132  0.44 23.51 ?  163 LYS   A HB3  1 
ATOM   3587 H  HG2  A LYS   A 1 163 ? 4.224  -8.466  -2.631  0.56 30.31 ?  163 LYS   A HG2  1 
ATOM   3588 H  HG2  B LYS   A 1 163 ? 4.594  -7.877  -2.579  0.44 27.31 ?  163 LYS   A HG2  1 
ATOM   3589 H  HG3  A LYS   A 1 163 ? 2.713  -8.019  -2.867  0.56 30.31 ?  163 LYS   A HG3  1 
ATOM   3590 H  HG3  B LYS   A 1 163 ? 3.025  -7.743  -2.792  0.44 27.31 ?  163 LYS   A HG3  1 
ATOM   3591 H  HD2  A LYS   A 1 163 ? 3.511  -5.968  -3.726  0.56 33.49 ?  163 LYS   A HD2  1 
ATOM   3592 H  HD2  B LYS   A 1 163 ? 3.527  -5.551  -3.730  0.44 30.93 ?  163 LYS   A HD2  1 
ATOM   3593 H  HD3  A LYS   A 1 163 ? 4.995  -6.528  -3.595  0.56 33.49 ?  163 LYS   A HD3  1 
ATOM   3594 H  HD3  B LYS   A 1 163 ? 5.028  -6.076  -3.830  0.44 30.93 ?  163 LYS   A HD3  1 
ATOM   3595 H  HE2  A LYS   A 1 163 ? 4.315  -8.289  -5.099  0.56 35.65 ?  163 LYS   A HE2  1 
ATOM   3596 H  HE2  B LYS   A 1 163 ? 4.283  -7.851  -5.189  0.44 33.50 ?  163 LYS   A HE2  1 
ATOM   3597 H  HE3  A LYS   A 1 163 ? 3.013  -7.426  -5.370  0.56 35.65 ?  163 LYS   A HE3  1 
ATOM   3598 H  HE3  B LYS   A 1 163 ? 2.813  -7.248  -5.139  0.44 33.50 ?  163 LYS   A HE3  1 
ATOM   3599 H  HZ1  A LYS   A 1 163 ? 4.585  -6.991  -6.950  0.56 36.72 ?  163 LYS   A HZ1  1 
ATOM   3600 H  HZ1  B LYS   A 1 163 ? 3.859  -6.636  -7.060  0.44 34.83 ?  163 LYS   A HZ1  1 
ATOM   3601 H  HZ2  A LYS   A 1 163 ? 4.329  -5.779  -6.199  0.56 36.72 ?  163 LYS   A HZ2  1 
ATOM   3602 H  HZ2  B LYS   A 1 163 ? 3.592  -5.442  -6.284  0.44 34.83 ?  163 LYS   A HZ2  1 
ATOM   3603 H  HZ3  A LYS   A 1 163 ? 5.533  -6.545  -5.950  0.56 36.72 ?  163 LYS   A HZ3  1 
ATOM   3604 H  HZ3  B LYS   A 1 163 ? 4.931  -5.992  -6.330  0.44 34.83 ?  163 LYS   A HZ3  1 
ATOM   3605 N  N    A LEU   A 1 164 ? 5.604  -8.643  0.574   0.56 15.99 ?  164 LEU   A N    1 
ATOM   3606 N  N    B LEU   A 1 164 ? 5.527  -8.267  0.681   0.44 15.10 ?  164 LEU   A N    1 
ATOM   3607 C  CA   A LEU   A 1 164 ? 6.682  -9.615  0.741   0.56 15.49 ?  164 LEU   A CA   1 
ATOM   3608 C  CA   B LEU   A 1 164 ? 6.572  -9.277  0.811   0.44 15.19 ?  164 LEU   A CA   1 
ATOM   3609 C  C    A LEU   A 1 164 ? 6.236  -10.786 1.609   0.56 15.66 ?  164 LEU   A C    1 
ATOM   3610 C  C    B LEU   A 1 164 ? 6.109  -10.448 1.671   0.44 15.07 ?  164 LEU   A C    1 
ATOM   3611 O  O    A LEU   A 1 164 ? 6.527  -11.948 1.299   0.56 15.59 ?  164 LEU   A O    1 
ATOM   3612 O  O    B LEU   A 1 164 ? 6.343  -11.612 1.324   0.44 15.29 ?  164 LEU   A O    1 
ATOM   3613 C  CB   A LEU   A 1 164 ? 7.897  -8.935  1.369   0.56 15.16 ?  164 LEU   A CB   1 
ATOM   3614 C  CB   B LEU   A 1 164 ? 7.835  -8.642  1.390   0.44 15.57 ?  164 LEU   A CB   1 
ATOM   3615 C  CG   A LEU   A 1 164 ? 8.651  -7.933  0.497   0.56 15.53 ?  164 LEU   A CG   1 
ATOM   3616 C  CG   B LEU   A 1 164 ? 8.659  -7.794  0.420   0.44 16.12 ?  164 LEU   A CG   1 
ATOM   3617 C  CD1  A LEU   A 1 164 ? 9.528  -7.047  1.368   0.56 15.33 ?  164 LEU   A CD1  1 
ATOM   3618 C  CD1  B LEU   A 1 164 ? 9.749  -7.071  1.182   0.44 16.11 ?  164 LEU   A CD1  1 
ATOM   3619 C  CD2  A LEU   A 1 164 ? 9.489  -8.657  -0.541  0.56 16.08 ?  164 LEU   A CD2  1 
ATOM   3620 C  CD2  B LEU   A 1 164 ? 9.258  -8.646  -0.693  0.44 16.47 ?  164 LEU   A CD2  1 
ATOM   3621 H  H    A LEU   A 1 164 ? 5.779  -7.856  0.881   0.56 19.19 ?  164 LEU   A H    1 
ATOM   3622 H  H    B LEU   A 1 164 ? 5.704  -7.508  1.064   0.44 18.12 ?  164 LEU   A H    1 
ATOM   3623 H  HA   A LEU   A 1 164 ? 6.944  -9.958  -0.128  0.56 18.59 ?  164 LEU   A HA   1 
ATOM   3624 H  HA   B LEU   A 1 164 ? 6.788  -9.614  -0.070  0.44 18.23 ?  164 LEU   A HA   1 
ATOM   3625 H  HB2  A LEU   A 1 164 ? 7.605  -8.458  2.159   0.56 18.19 ?  164 LEU   A HB2  1 
ATOM   3626 H  HB2  B LEU   A 1 164 ? 7.582  -8.064  2.128   0.44 18.69 ?  164 LEU   A HB2  1 
ATOM   3627 H  HB3  A LEU   A 1 164 ? 8.534  -9.620  1.620   0.56 18.19 ?  164 LEU   A HB3  1 
ATOM   3628 H  HB3  B LEU   A 1 164 ? 8.413  -9.347  1.715   0.44 18.69 ?  164 LEU   A HB3  1 
ATOM   3629 H  HG   A LEU   A 1 164 ? 8.013  -7.364  0.033   0.56 18.64 ?  164 LEU   A HG   1 
ATOM   3630 H  HG   B LEU   A 1 164 ? 8.085  -7.125  0.012   0.44 19.35 ?  164 LEU   A HG   1 
ATOM   3631 H  HD11 A LEU   A 1 164 ? 10.012 -6.426  0.804   0.56 18.40 ?  164 LEU   A HD11 1 
ATOM   3632 H  HD11 B LEU   A 1 164 ? 10.269 -6.539  0.561   0.44 19.33 ?  164 LEU   A HD11 1 
ATOM   3633 H  HD12 A LEU   A 1 164 ? 8.963  -6.558  1.990   0.56 18.40 ?  164 LEU   A HD12 1 
ATOM   3634 H  HD12 B LEU   A 1 164 ? 9.339  -6.498  1.849   0.44 19.33 ?  164 LEU   A HD12 1 
ATOM   3635 H  HD13 A LEU   A 1 164 ? 10.149 -7.607  1.859   0.56 18.40 ?  164 LEU   A HD13 1 
ATOM   3636 H  HD13 B LEU   A 1 164 ? 10.317 -7.728  1.614   0.44 19.33 ?  164 LEU   A HD13 1 
ATOM   3637 H  HD21 A LEU   A 1 164 ? 9.968  -8.002  -1.074  0.56 19.30 ?  164 LEU   A HD21 1 
ATOM   3638 H  HD21 B LEU   A 1 164 ? 9.900  -8.113  -1.190  0.44 19.76 ?  164 LEU   A HD21 1 
ATOM   3639 H  HD22 A LEU   A 1 164 ? 10.120 -9.237  -0.087  0.56 19.30 ?  164 LEU   A HD22 1 
ATOM   3640 H  HD22 B LEU   A 1 164 ? 9.703  -9.413  -0.299  0.44 19.76 ?  164 LEU   A HD22 1 
ATOM   3641 H  HD23 A LEU   A 1 164 ? 8.905  -9.181  -1.109  0.56 19.30 ?  164 LEU   A HD23 1 
ATOM   3642 H  HD23 B LEU   A 1 164 ? 8.549  -8.943  -1.284  0.44 19.76 ?  164 LEU   A HD23 1 
ATOM   3643 N  N    A VAL   A 1 165 ? 5.545  -10.495 2.710   0.56 15.32 ?  165 VAL   A N    1 
ATOM   3644 N  N    B VAL   A 1 165 ? 5.461  -10.158 2.800   0.44 14.88 ?  165 VAL   A N    1 
ATOM   3645 C  CA   A VAL   A 1 165 ? 5.072  -11.555 3.595   0.56 15.50 ?  165 VAL   A CA   1 
ATOM   3646 C  CA   B VAL   A 1 165 ? 4.952  -11.227 3.656   0.44 15.08 ?  165 VAL   A CA   1 
ATOM   3647 C  C    A VAL   A 1 165 ? 4.032  -12.412 2.888   0.56 15.33 ?  165 VAL   A C    1 
ATOM   3648 C  C    B VAL   A 1 165 ? 3.917  -12.058 2.908   0.44 14.58 ?  165 VAL   A C    1 
ATOM   3649 O  O    A VAL   A 1 165 ? 4.140  -13.643 2.846   0.56 15.50 ?  165 VAL   A O    1 
ATOM   3650 O  O    B VAL   A 1 165 ? 3.966  -13.295 2.903   0.44 14.73 ?  165 VAL   A O    1 
ATOM   3651 C  CB   A VAL   A 1 165 ? 4.529  -10.954 4.904   0.56 15.96 ?  165 VAL   A CB   1 
ATOM   3652 C  CB   B VAL   A 1 165 ? 4.380  -10.643 4.961   0.44 15.98 ?  165 VAL   A CB   1 
ATOM   3653 C  CG1  A VAL   A 1 165 ? 3.776  -12.005 5.706   0.56 16.00 ?  165 VAL   A CG1  1 
ATOM   3654 C  CG1  B VAL   A 1 165 ? 3.638  -11.715 5.745   0.44 16.31 ?  165 VAL   A CG1  1 
ATOM   3655 C  CG2  A VAL   A 1 165 ? 5.668  -10.348 5.722   0.56 16.14 ?  165 VAL   A CG2  1 
ATOM   3656 C  CG2  B VAL   A 1 165 ? 5.497  -10.031 5.800   0.44 16.13 ?  165 VAL   A CG2  1 
ATOM   3657 H  H    A VAL   A 1 165 ? 5.336  -9.697  2.958   0.56 18.39 ?  165 VAL   A H    1 
ATOM   3658 H  H    B VAL   A 1 165 ? 5.310  -9.357  3.088   0.44 17.85 ?  165 VAL   A H    1 
ATOM   3659 H  HA   A VAL   A 1 165 ? 5.825  -12.123 3.824   0.56 18.60 ?  165 VAL   A HA   1 
ATOM   3660 H  HA   B VAL   A 1 165 ? 5.690  -11.806 3.892   0.44 18.10 ?  165 VAL   A HA   1 
ATOM   3661 H  HB   A VAL   A 1 165 ? 3.911  -10.238 4.687   0.56 19.15 ?  165 VAL   A HB   1 
ATOM   3662 H  HB   B VAL   A 1 165 ? 3.753  -9.934  4.745   0.44 19.18 ?  165 VAL   A HB   1 
ATOM   3663 H  HG11 A VAL   A 1 165 ? 3.692  -11.697 6.621   0.56 19.21 ?  165 VAL   A HG11 1 
ATOM   3664 H  HG11 B VAL   A 1 165 ? 3.529  -11.415 6.661   0.44 19.57 ?  165 VAL   A HG11 1 
ATOM   3665 H  HG12 A VAL   A 1 165 ? 2.895  -12.125 5.316   0.56 19.21 ?  165 VAL   A HG12 1 
ATOM   3666 H  HG12 B VAL   A 1 165 ? 2.770  -11.859 5.340   0.44 19.57 ?  165 VAL   A HG12 1 
ATOM   3667 H  HG13 A VAL   A 1 165 ? 4.272  -12.835 5.679   0.56 19.21 ?  165 VAL   A HG13 1 
ATOM   3668 H  HG13 B VAL   A 1 165 ? 4.157  -12.534 5.726   0.44 19.57 ?  165 VAL   A HG13 1 
ATOM   3669 H  HG21 A VAL   A 1 165 ? 5.306  -9.979  6.543   0.56 19.36 ?  165 VAL   A HG21 1 
ATOM   3670 H  HG21 B VAL   A 1 165 ? 5.119  -9.678  6.621   0.44 19.36 ?  165 VAL   A HG21 1 
ATOM   3671 H  HG22 A VAL   A 1 165 ? 6.315  -11.039 5.925   0.56 19.36 ?  165 VAL   A HG22 1 
ATOM   3672 H  HG22 B VAL   A 1 165 ? 6.150  -10.718 6.005   0.44 19.36 ?  165 VAL   A HG22 1 
ATOM   3673 H  HG23 A VAL   A 1 165 ? 6.090  -9.642  5.203   0.56 19.36 ?  165 VAL   A HG23 1 
ATOM   3674 H  HG23 B VAL   A 1 165 ? 5.918  -9.315  5.296   0.44 19.36 ?  165 VAL   A HG23 1 
ATOM   3675 N  N    A SER   A 1 166 ? 3.015  -11.772 2.308   0.56 15.87 ?  166 SER   A N    1 
ATOM   3676 N  N    B SER   A 1 166 ? 2.969  -11.386 2.254   0.44 14.52 ?  166 SER   A N    1 
ATOM   3677 C  CA   A SER   A 1 166 ? 1.910  -12.522 1.721   0.56 16.90 ?  166 SER   A CA   1 
ATOM   3678 C  CA   B SER   A 1 166 ? 1.852  -12.084 1.628   0.44 15.34 ?  166 SER   A CA   1 
ATOM   3679 C  C    A SER   A 1 166 ? 2.359  -13.362 0.537   0.56 17.67 ?  166 SER   A C    1 
ATOM   3680 C  C    B SER   A 1 166 ? 2.276  -12.930 0.433   0.44 15.67 ?  166 SER   A C    1 
ATOM   3681 O  O    A SER   A 1 166 ? 1.754  -14.404 0.257   0.56 18.92 ?  166 SER   A O    1 
ATOM   3682 O  O    B SER   A 1 166 ? 1.521  -13.826 0.031   0.44 15.89 ?  166 SER   A O    1 
ATOM   3683 C  CB   A SER   A 1 166 ? 0.798  -11.570 1.281   0.56 18.13 ?  166 SER   A CB   1 
ATOM   3684 C  CB   B SER   A 1 166 ? 0.785  -11.078 1.190   0.44 16.63 ?  166 SER   A CB   1 
ATOM   3685 O  OG   A SER   A 1 166 ? 0.172  -10.967 2.398   0.56 19.78 ?  166 SER   A OG   1 
ATOM   3686 O  OG   B SER   A 1 166 ? 0.128  -10.491 2.304   0.44 18.13 ?  166 SER   A OG   1 
ATOM   3687 H  H    A SER   A 1 166 ? 2.939  -10.923 2.252   0.56 19.04 ?  166 SER   A H    1 
ATOM   3688 H  H    B SER   A 1 166 ? 2.949  -10.526 2.168   0.44 17.42 ?  166 SER   A H    1 
ATOM   3689 H  HA   A SER   A 1 166 ? 1.543  -13.127 2.385   0.56 20.28 ?  166 SER   A HA   1 
ATOM   3690 H  HA   B SER   A 1 166 ? 1.452  -12.674 2.280   0.44 18.41 ?  166 SER   A HA   1 
ATOM   3691 H  HB2  A SER   A 1 166 ? 1.179  -10.882 0.716   0.56 21.75 ?  166 SER   A HB2  1 
ATOM   3692 H  HB2  B SER   A 1 166 ? 1.204  -10.371 0.676   0.44 19.96 ?  166 SER   A HB2  1 
ATOM   3693 H  HB3  A SER   A 1 166 ? 0.132  -12.073 0.783   0.56 21.75 ?  166 SER   A HB3  1 
ATOM   3694 H  HB3  B SER   A 1 166 ? 0.125  -11.536 0.647   0.44 19.96 ?  166 SER   A HB3  1 
ATOM   3695 H  HG   A SER   A 1 166 ? 0.736  -10.520 2.834   0.56 23.74 ?  166 SER   A HG   1 
ATOM   3696 H  HG   B SER   A 1 166 ? 0.686  -10.094 2.792   0.44 21.76 ?  166 SER   A HG   1 
ATOM   3697 N  N    A SER   A 1 167 ? 3.395  -12.928 -0.178  0.56 17.38 ?  167 SER   A N    1 
ATOM   3698 N  N    B SER   A 1 167 ? 3.450  -12.667 -0.146  0.44 16.15 ?  167 SER   A N    1 
ATOM   3699 C  CA   A SER   A 1 167 ? 3.860  -13.646 -1.355  0.56 17.94 ?  167 SER   A CA   1 
ATOM   3700 C  CA   B SER   A 1 167 ? 3.910  -13.388 -1.325  0.44 17.36 ?  167 SER   A CA   1 
ATOM   3701 C  C    A SER   A 1 167 ? 5.014  -14.592 -1.054  0.56 18.07 ?  167 SER   A C    1 
ATOM   3702 C  C    B SER   A 1 167 ? 5.057  -14.350 -1.037  0.44 18.32 ?  167 SER   A C    1 
ATOM   3703 O  O    A SER   A 1 167 ? 5.510  -15.256 -1.971  0.56 18.69 ?  167 SER   A O    1 
ATOM   3704 O  O    B SER   A 1 167 ? 5.543  -15.007 -1.964  0.44 18.95 ?  167 SER   A O    1 
ATOM   3705 C  CB   A SER   A 1 167 ? 4.265  -12.657 -2.457  0.56 18.25 ?  167 SER   A CB   1 
ATOM   3706 C  CB   B SER   A 1 167 ? 4.324  -12.402 -2.427  0.44 17.75 ?  167 SER   A CB   1 
ATOM   3707 O  OG   A SER   A 1 167 ? 5.387  -11.887 -2.063  0.56 18.60 ?  167 SER   A OG   1 
ATOM   3708 O  OG   B SER   A 1 167 ? 5.364  -11.549 -1.980  0.44 18.07 ?  167 SER   A OG   1 
ATOM   3709 H  H    A SER   A 1 167 ? 3.841  -12.207 -0.003  0.56 20.86 ?  167 SER   A H    1 
ATOM   3710 H  H    B SER   A 1 167 ? 4.001  -12.058 0.129   0.44 19.38 ?  167 SER   A H    1 
ATOM   3711 H  HA   A SER   A 1 167 ? 3.129  -14.175 -1.700  0.56 21.52 ?  167 SER   A HA   1 
ATOM   3712 H  HA   B SER   A 1 167 ? 3.171  -13.903 -1.672  0.44 20.83 ?  167 SER   A HA   1 
ATOM   3713 H  HB2  A SER   A 1 167 ? 4.490  -13.153 -3.260  0.56 21.91 ?  167 SER   A HB2  1 
ATOM   3714 H  HB2  B SER   A 1 167 ? 4.640  -12.904 -3.197  0.44 21.30 ?  167 SER   A HB2  1 
ATOM   3715 H  HB3  A SER   A 1 167 ? 3.515  -12.062 -2.641  0.56 21.91 ?  167 SER   A HB3  1 
ATOM   3716 H  HB3  B SER   A 1 167 ? 3.552  -11.866 -2.682  0.44 21.30 ?  167 SER   A HB3  1 
ATOM   3717 H  HG   A SER   A 1 167 ? 5.196  -11.439 -1.377  0.56 22.31 ?  167 SER   A HG   1 
ATOM   3718 H  HG   B SER   A 1 167 ? 5.095  -11.088 -1.330  0.44 21.68 ?  167 SER   A HG   1 
ATOM   3719 N  N    A PHE   A 1 168 ? 5.451  -14.685 0.199   0.56 18.00 ?  168 PHE   A N    1 
ATOM   3720 N  N    B PHE   A 1 168 ? 5.505  -14.454 0.210   0.44 18.94 ?  168 PHE   A N    1 
ATOM   3721 C  CA   A PHE   A 1 168 ? 6.634  -15.477 0.503   0.56 18.49 ?  168 PHE   A CA   1 
ATOM   3722 C  CA   B PHE   A 1 168 ? 6.664  -15.285 0.510   0.44 20.01 ?  168 PHE   A CA   1 
ATOM   3723 C  C    A PHE   A 1 168 ? 6.325  -16.960 0.397   0.56 20.37 ?  168 PHE   A C    1 
ATOM   3724 C  C    B PHE   A 1 168 ? 6.317  -16.763 0.396   0.44 21.59 ?  168 PHE   A C    1 
ATOM   3725 O  O    A PHE   A 1 168 ? 5.356  -17.448 0.988   0.56 21.14 ?  168 PHE   A O    1 
ATOM   3726 O  O    B PHE   A 1 168 ? 5.266  -17.210 0.866   0.44 22.35 ?  168 PHE   A O    1 
ATOM   3727 C  CB   A PHE   A 1 168 ? 7.154  -15.185 1.905   0.56 18.07 ?  168 PHE   A CB   1 
ATOM   3728 C  CB   B PHE   A 1 168 ? 7.176  -15.001 1.919   0.44 19.91 ?  168 PHE   A CB   1 
ATOM   3729 C  CG   A PHE   A 1 168 ? 8.408  -15.947 2.235   0.56 17.55 ?  168 PHE   A CG   1 
ATOM   3730 C  CG   B PHE   A 1 168 ? 8.425  -15.760 2.261   0.44 19.85 ?  168 PHE   A CG   1 
ATOM   3731 C  CD1  A PHE   A 1 168 ? 9.597  -15.629 1.606   0.56 17.67 ?  168 PHE   A CD1  1 
ATOM   3732 C  CD1  B PHE   A 1 168 ? 9.641  -15.373 1.731   0.44 19.98 ?  168 PHE   A CD1  1 
ATOM   3733 C  CD2  A PHE   A 1 168 ? 8.397  -16.996 3.140   0.56 17.49 ?  168 PHE   A CD2  1 
ATOM   3734 C  CD2  B PHE   A 1 168 ? 8.384  -16.867 3.092   0.44 19.90 ?  168 PHE   A CD2  1 
ATOM   3735 C  CE1  A PHE   A 1 168 ? 10.754 -16.330 1.883   0.56 17.08 ?  168 PHE   A CE1  1 
ATOM   3736 C  CE1  B PHE   A 1 168 ? 10.794 -16.068 2.029   0.44 19.89 ?  168 PHE   A CE1  1 
ATOM   3737 C  CE2  A PHE   A 1 168 ? 9.558  -17.699 3.425   0.56 17.67 ?  168 PHE   A CE2  1 
ATOM   3738 C  CE2  B PHE   A 1 168 ? 9.538  -17.567 3.396   0.44 20.01 ?  168 PHE   A CE2  1 
ATOM   3739 C  CZ   A PHE   A 1 168 ? 10.736 -17.362 2.794   0.56 17.35 ?  168 PHE   A CZ   1 
ATOM   3740 C  CZ   B PHE   A 1 168 ? 10.744 -17.165 2.863   0.44 19.89 ?  168 PHE   A CZ   1 
ATOM   3741 H  H    A PHE   A 1 168 ? 5.081  -14.313 0.878   0.56 21.60 ?  168 PHE   A H    1 
ATOM   3742 H  H    B PHE   A 1 168 ? 5.162  -14.055 0.889   0.44 22.72 ?  168 PHE   A H    1 
ATOM   3743 H  HA   A PHE   A 1 168 ? 7.334  -15.264 -0.136  0.56 22.19 ?  168 PHE   A HA   1 
ATOM   3744 H  HA   B PHE   A 1 168 ? 7.373  -15.084 -0.122  0.44 24.01 ?  168 PHE   A HA   1 
ATOM   3745 H  HB2  A PHE   A 1 168 ? 7.351  -14.239 1.975   0.56 21.69 ?  168 PHE   A HB2  1 
ATOM   3746 H  HB2  B PHE   A 1 168 ? 7.369  -14.054 1.998   0.44 23.90 ?  168 PHE   A HB2  1 
ATOM   3747 H  HB3  A PHE   A 1 168 ? 6.473  -15.433 2.549   0.56 21.69 ?  168 PHE   A HB3  1 
ATOM   3748 H  HB3  B PHE   A 1 168 ? 6.489  -15.252 2.557   0.44 23.90 ?  168 PHE   A HB3  1 
ATOM   3749 H  HD1  A PHE   A 1 168 ? 9.620  -14.934 0.989   0.56 21.21 ?  168 PHE   A HD1  1 
ATOM   3750 H  HD1  B PHE   A 1 168 ? 9.681  -14.634 1.167   0.44 23.97 ?  168 PHE   A HD1  1 
ATOM   3751 H  HD2  A PHE   A 1 168 ? 7.602  -17.227 3.567   0.56 20.99 ?  168 PHE   A HD2  1 
ATOM   3752 H  HD2  B PHE   A 1 168 ? 7.570  -17.141 3.453   0.44 23.88 ?  168 PHE   A HD2  1 
ATOM   3753 H  HE1  A PHE   A 1 168 ? 11.551 -16.102 1.457   0.56 20.49 ?  168 PHE   A HE1  1 
ATOM   3754 H  HE1  B PHE   A 1 168 ? 11.608 -15.795 1.668   0.44 23.87 ?  168 PHE   A HE1  1 
ATOM   3755 H  HE2  A PHE   A 1 168 ? 9.536  -18.399 4.038   0.56 21.20 ?  168 PHE   A HE2  1 
ATOM   3756 H  HE2  B PHE   A 1 168 ? 9.498  -18.307 3.957   0.44 24.02 ?  168 PHE   A HE2  1 
ATOM   3757 H  HZ   A PHE   A 1 168 ? 11.516 -17.835 2.981   0.56 20.82 ?  168 PHE   A HZ   1 
ATOM   3758 H  HZ   B PHE   A 1 168 ? 11.522 -17.633 3.064   0.44 23.87 ?  168 PHE   A HZ   1 
ATOM   3759 N  N    A LEU   A 1 169 ? 7.173  -17.683 -0.329  0.56 23.21 ?  169 LEU   A N    1 
ATOM   3760 N  N    B LEU   A 1 169 ? 7.217  -17.526 -0.220  0.44 23.14 ?  169 LEU   A N    1 
ATOM   3761 C  CA   A LEU   A 1 169 ? 6.984  -19.115 -0.492  0.56 27.28 ?  169 LEU   A CA   1 
ATOM   3762 C  CA   B LEU   A 1 169 ? 7.007  -18.959 -0.384  0.44 25.57 ?  169 LEU   A CA   1 
ATOM   3763 C  C    A LEU   A 1 169 ? 7.859  -19.884 0.489   0.56 28.61 ?  169 LEU   A C    1 
ATOM   3764 C  C    B LEU   A 1 169 ? 7.816  -19.747 0.642   0.44 25.72 ?  169 LEU   A C    1 
ATOM   3765 O  O    A LEU   A 1 169 ? 7.376  -20.333 1.529   0.56 29.02 ?  169 LEU   A O    1 
ATOM   3766 O  O    B LEU   A 1 169 ? 7.242  -20.375 1.535   0.44 25.90 ?  169 LEU   A O    1 
ATOM   3767 C  CB   A LEU   A 1 169 ? 7.284  -19.541 -1.931  0.56 29.32 ?  169 LEU   A CB   1 
ATOM   3768 C  CB   B LEU   A 1 169 ? 7.366  -19.402 -1.806  0.44 27.34 ?  169 LEU   A CB   1 
ATOM   3769 C  CG   A LEU   A 1 169 ? 6.983  -21.005 -2.266  0.56 31.00 ?  169 LEU   A CG   1 
ATOM   3770 C  CG   B LEU   A 1 169 ? 7.128  -20.880 -2.139  0.44 28.90 ?  169 LEU   A CG   1 
ATOM   3771 C  CD1  A LEU   A 1 169 ? 5.558  -21.372 -1.874  0.56 31.59 ?  169 LEU   A CD1  1 
ATOM   3772 C  CD1  B LEU   A 1 169 ? 5.725  -21.312 -1.739  0.44 29.45 ?  169 LEU   A CD1  1 
ATOM   3773 C  CD2  A LEU   A 1 169 ? 7.214  -21.274 -3.746  0.56 31.50 ?  169 LEU   A CD2  1 
ATOM   3774 C  CD2  B LEU   A 1 169 ? 7.363  -21.147 -3.621  0.44 29.45 ?  169 LEU   A CD2  1 
ATOM   3775 O  OXT  A LEU   A 1 169 ? 9.059  -20.065 0.273   0.56 28.85 -1 169 LEU   A OXT  1 
ATOM   3776 O  OXT  B LEU   A 1 169 ? 9.049  -19.771 0.611   0.44 25.20 -1 169 LEU   A OXT  1 
ATOM   3777 H  H    A LEU   A 1 169 ? 7.868  -17.368 -0.736  0.56 27.85 ?  169 LEU   A H    1 
ATOM   3778 H  H    B LEU   A 1 169 ? 7.959  -17.236 -0.549  0.44 27.77 ?  169 LEU   A H    1 
ATOM   3779 H  HA   A LEU   A 1 169 ? 6.063  -19.331 -0.296  0.56 32.74 ?  169 LEU   A HA   1 
ATOM   3780 H  HA   B LEU   A 1 169 ? 6.071  -19.153 -0.237  0.44 30.69 ?  169 LEU   A HA   1 
ATOM   3781 H  HB2  A LEU   A 1 169 ? 6.752  -18.993 -2.528  0.56 35.18 ?  169 LEU   A HB2  1 
ATOM   3782 H  HB2  B LEU   A 1 169 ? 6.837  -18.880 -2.429  0.44 32.81 ?  169 LEU   A HB2  1 
ATOM   3783 H  HB3  A LEU   A 1 169 ? 8.225  -19.393 -2.107  0.56 35.18 ?  169 LEU   A HB3  1 
ATOM   3784 H  HB3  B LEU   A 1 169 ? 8.307  -19.224 -1.953  0.44 32.81 ?  169 LEU   A HB3  1 
ATOM   3785 H  HG   A LEU   A 1 169 ? 7.586  -21.574 -1.764  0.56 37.20 ?  169 LEU   A HG   1 
ATOM   3786 H  HG   B LEU   A 1 169 ? 7.758  -21.421 -1.639  0.44 34.68 ?  169 LEU   A HG   1 
ATOM   3787 H  HD11 A LEU   A 1 169 ? 5.330  -22.224 -2.276  0.56 37.90 ?  169 LEU   A HD11 1 
ATOM   3788 H  HD11 B LEU   A 1 169 ? 5.547  -22.189 -2.112  0.44 35.34 ?  169 LEU   A HD11 1 
ATOM   3789 H  HD12 A LEU   A 1 169 ? 5.503  -21.439 -0.907  0.56 37.90 ?  169 LEU   A HD12 1 
ATOM   3790 H  HD12 B LEU   A 1 169 ? 5.669  -21.348 -0.771  0.44 35.34 ?  169 LEU   A HD12 1 
ATOM   3791 H  HD13 A LEU   A 1 169 ? 4.955  -20.683 -2.194  0.56 37.90 ?  169 LEU   A HD13 1 
ATOM   3792 H  HD13 B LEU   A 1 169 ? 5.086  -20.670 -2.086  0.44 35.34 ?  169 LEU   A HD13 1 
ATOM   3793 H  HD21 A LEU   A 1 169 ? 7.022  -22.207 -3.931  0.56 37.80 ?  169 LEU   A HD21 1 
ATOM   3794 H  HD21 B LEU   A 1 169 ? 7.209  -22.089 -3.801  0.44 35.34 ?  169 LEU   A HD21 1 
ATOM   3795 H  HD22 A LEU   A 1 169 ? 6.623  -20.706 -4.265  0.56 37.80 ?  169 LEU   A HD22 1 
ATOM   3796 H  HD22 B LEU   A 1 169 ? 6.746  -20.608 -4.141  0.44 35.34 ?  169 LEU   A HD22 1 
ATOM   3797 H  HD23 A LEU   A 1 169 ? 8.138  -21.076 -3.962  0.56 37.80 ?  169 LEU   A HD23 1 
ATOM   3798 H  HD23 B LEU   A 1 169 ? 8.277  -20.913 -3.843  0.44 35.34 ?  169 LEU   A HD23 1 
ATOM   3799 N  N    A SER   B 1 1   ? 50.757 -9.201  -23.681 0.56 30.17 ?  1   SER   B N    1 
ATOM   3800 N  N    B SER   B 1 1   ? 50.686 -9.225  -23.707 0.44 28.39 ?  1   SER   B N    1 
ATOM   3801 C  CA   A SER   B 1 1   ? 51.260 -10.278 -22.805 0.56 30.20 ?  1   SER   B CA   1 
ATOM   3802 C  CA   B SER   B 1 1   ? 51.148 -10.244 -22.742 0.44 28.35 ?  1   SER   B CA   1 
ATOM   3803 C  C    A SER   B 1 1   ? 50.186 -11.326 -22.566 0.56 29.16 ?  1   SER   B C    1 
ATOM   3804 C  C    B SER   B 1 1   ? 50.064 -11.285 -22.499 0.44 27.10 ?  1   SER   B C    1 
ATOM   3805 O  O    A SER   B 1 1   ? 48.998 -11.106 -22.824 0.56 29.06 ?  1   SER   B O    1 
ATOM   3806 O  O    B SER   B 1 1   ? 48.903 -11.112 -22.887 0.44 26.49 ?  1   SER   B O    1 
ATOM   3807 C  CB   A SER   B 1 1   ? 51.736 -9.712  -21.470 0.56 30.75 ?  1   SER   B CB   1 
ATOM   3808 C  CB   B SER   B 1 1   ? 51.544 -9.593  -21.421 0.44 29.08 ?  1   SER   B CB   1 
ATOM   3809 O  OG   A SER   B 1 1   ? 50.639 -9.391  -20.636 0.56 32.10 ?  1   SER   B OG   1 
ATOM   3810 O  OG   B SER   B 1 1   ? 50.400 -9.342  -20.626 0.44 30.36 ?  1   SER   B OG   1 
ATOM   3811 H  H1   A SER   B 1 1   ? 50.587 -9.539  -24.485 0.56 36.21 ?  1   SER   B H1   1 
ATOM   3812 H  H1   B SER   B 1 1   ? 50.579 -9.607  -24.501 0.44 34.07 ?  1   SER   B H1   1 
ATOM   3813 H  H2   A SER   B 1 1   ? 50.017 -8.865  -23.330 0.56 36.21 ?  1   SER   B H2   1 
ATOM   3814 H  H2   B SER   B 1 1   ? 49.917 -8.888  -23.425 0.44 34.07 ?  1   SER   B H2   1 
ATOM   3815 H  H3   A SER   B 1 1   ? 51.378 -8.570  -23.744 0.56 36.21 ?  1   SER   B H3   1 
ATOM   3816 H  H3   B SER   B 1 1   ? 51.297 -8.583  -23.761 0.44 34.07 ?  1   SER   B H3   1 
ATOM   3817 H  HA   A SER   B 1 1   ? 52.009 -10.701 -23.243 0.56 36.24 ?  1   SER   B HA   1 
ATOM   3818 H  HA   B SER   B 1 1   ? 51.924 -10.686 -23.113 0.44 34.02 ?  1   SER   B HA   1 
ATOM   3819 H  HB2  A SER   B 1 1   ? 52.286 -10.378 -21.031 0.56 36.90 ?  1   SER   B HB2  1 
ATOM   3820 H  HB2  B SER   B 1 1   ? 52.144 -10.191 -20.950 0.44 34.90 ?  1   SER   B HB2  1 
ATOM   3821 H  HB3  A SER   B 1 1   ? 52.253 -8.908  -21.633 0.56 36.90 ?  1   SER   B HB3  1 
ATOM   3822 H  HB3  B SER   B 1 1   ? 51.991 -8.751  -21.603 0.44 34.90 ?  1   SER   B HB3  1 
ATOM   3823 H  HG   A SER   B 1 1   ? 50.878 -8.832  -20.056 0.56 38.52 ?  1   SER   B HG   1 
ATOM   3824 H  HG   B SER   B 1 1   ? 50.559 -8.712  -20.094 0.44 36.43 ?  1   SER   B HG   1 
ATOM   3825 N  N    A MET   B 1 2   ? 50.626 -12.468 -22.055 0.56 27.92 ?  2   MET   B N    1 
ATOM   3826 N  N    B MET   B 1 2   ? 50.460 -12.363 -21.834 0.44 26.29 ?  2   MET   B N    1 
ATOM   3827 C  CA   A MET   B 1 2   ? 49.788 -13.644 -21.885 0.56 27.29 ?  2   MET   B CA   1 
ATOM   3828 C  CA   B MET   B 1 2   ? 49.639 -13.559 -21.683 0.44 25.91 ?  2   MET   B CA   1 
ATOM   3829 C  C    A MET   B 1 2   ? 49.543 -13.845 -20.397 0.56 24.00 ?  2   MET   B C    1 
ATOM   3830 C  C    B MET   B 1 2   ? 49.369 -13.770 -20.198 0.44 23.74 ?  2   MET   B C    1 
ATOM   3831 O  O    A MET   B 1 2   ? 50.490 -14.054 -19.632 0.56 23.49 ?  2   MET   B O    1 
ATOM   3832 O  O    B MET   B 1 2   ? 50.250 -14.220 -19.459 0.44 24.21 ?  2   MET   B O    1 
ATOM   3833 C  CB   A MET   B 1 2   ? 50.489 -14.856 -22.490 0.56 30.78 ?  2   MET   B CB   1 
ATOM   3834 C  CB   B MET   B 1 2   ? 50.383 -14.744 -22.278 0.44 28.35 ?  2   MET   B CB   1 
ATOM   3835 C  CG   A MET   B 1 2   ? 49.621 -16.095 -22.613 0.56 33.86 ?  2   MET   B CG   1 
ATOM   3836 C  CG   B MET   B 1 2   ? 49.511 -15.902 -22.732 0.44 30.40 ?  2   MET   B CG   1 
ATOM   3837 S  SD   A MET   B 1 2   ? 50.430 -17.369 -23.599 0.56 36.74 ?  2   MET   B SD   1 
ATOM   3838 S  SD   B MET   B 1 2   ? 50.412 -17.001 -23.837 0.44 32.37 ?  2   MET   B SD   1 
ATOM   3839 C  CE   A MET   B 1 2   ? 50.981 -16.372 -24.982 0.56 37.16 ?  2   MET   B CE   1 
ATOM   3840 C  CE   B MET   B 1 2   ? 51.247 -15.807 -24.865 0.44 32.63 ?  2   MET   B CE   1 
ATOM   3841 H  H    A MET   B 1 2   ? 51.435 -12.591 -21.787 0.56 33.51 ?  2   MET   B H    1 
ATOM   3842 H  H    B MET   B 1 2   ? 51.232 -12.433 -21.459 0.44 31.54 ?  2   MET   B H    1 
ATOM   3843 H  HA   A MET   B 1 2   ? 48.945 -13.524 -22.347 0.56 32.74 ?  2   MET   B HA   1 
ATOM   3844 H  HA   B MET   B 1 2   ? 48.805 -13.452 -22.165 0.44 31.10 ?  2   MET   B HA   1 
ATOM   3845 H  HB2  A MET   B 1 2   ? 50.788 -14.589 -23.372 0.56 36.94 ?  2   MET   B HB2  1 
ATOM   3846 H  HB2  B MET   B 1 2   ? 50.886 -14.397 -23.025 0.44 34.02 ?  2   MET   B HB2  1 
ATOM   3847 H  HB3  A MET   B 1 2   ? 51.254 -15.095 -21.947 0.56 36.94 ?  2   MET   B HB3  1 
ATOM   3848 H  HB3  B MET   B 1 2   ? 50.995 -15.106 -21.625 0.44 34.02 ?  2   MET   B HB3  1 
ATOM   3849 H  HG2  A MET   B 1 2   ? 49.452 -16.452 -21.725 0.56 40.64 ?  2   MET   B HG2  1 
ATOM   3850 H  HG2  B MET   B 1 2   ? 49.228 -16.414 -21.955 0.44 36.48 ?  2   MET   B HG2  1 
ATOM   3851 H  HG3  A MET   B 1 2   ? 48.787 -15.865 -23.050 0.56 40.64 ?  2   MET   B HG3  1 
ATOM   3852 H  HG3  B MET   B 1 2   ? 48.739 -15.571 -23.209 0.44 36.48 ?  2   MET   B HG3  1 
ATOM   3853 H  HE1  A MET   B 1 2   ? 51.131 -16.949 -25.735 0.56 44.59 ?  2   MET   B HE1  1 
ATOM   3854 H  HE1  B MET   B 1 2   ? 51.451 -16.230 -25.695 0.44 39.16 ?  2   MET   B HE1  1 
ATOM   3855 H  HE2  A MET   B 1 2   ? 50.287 -15.721 -25.189 0.56 44.59 ?  2   MET   B HE2  1 
ATOM   3856 H  HE2  B MET   B 1 2   ? 50.657 -15.048 -25.013 0.44 39.16 ?  2   MET   B HE2  1 
ATOM   3857 H  HE3  A MET   B 1 2   ? 51.804 -15.907 -24.745 0.56 44.59 ?  2   MET   B HE3  1 
ATOM   3858 H  HE3  B MET   B 1 2   ? 52.064 -15.512 -24.420 0.44 39.16 ?  2   MET   B HE3  1 
ATOM   3859 N  N    A VAL   B 1 3   ? 48.280 -13.749 -19.989 0.56 21.55 ?  3   VAL   B N    1 
ATOM   3860 N  N    B VAL   B 1 3   ? 48.156 -13.442 -19.759 0.44 21.38 ?  3   VAL   B N    1 
ATOM   3861 C  CA   A VAL   B 1 3   ? 47.879 -13.982 -18.610 0.56 20.13 ?  3   VAL   B CA   1 
ATOM   3862 C  CA   B VAL   B 1 3   ? 47.719 -13.705 -18.393 0.44 19.79 ?  3   VAL   B CA   1 
ATOM   3863 C  C    A VAL   B 1 3   ? 46.638 -14.864 -18.618 0.56 18.30 ?  3   VAL   B C    1 
ATOM   3864 C  C    B VAL   B 1 3   ? 46.471 -14.572 -18.436 0.44 18.11 ?  3   VAL   B C    1 
ATOM   3865 O  O    A VAL   B 1 3   ? 45.937 -14.983 -19.626 0.56 18.14 ?  3   VAL   B O    1 
ATOM   3866 O  O    B VAL   B 1 3   ? 45.634 -14.437 -19.333 0.44 17.89 ?  3   VAL   B O    1 
ATOM   3867 C  CB   A VAL   B 1 3   ? 47.595 -12.667 -17.851 0.56 21.38 ?  3   VAL   B CB   1 
ATOM   3868 C  CB   B VAL   B 1 3   ? 47.479 -12.418 -17.572 0.44 20.13 ?  3   VAL   B CB   1 
ATOM   3869 C  CG1  A VAL   B 1 3   ? 48.856 -11.814 -17.751 0.56 21.83 ?  3   VAL   B CG1  1 
ATOM   3870 C  CG1  B VAL   B 1 3   ? 48.768 -11.614 -17.449 0.44 20.25 ?  3   VAL   B CG1  1 
ATOM   3871 C  CG2  A VAL   B 1 3   ? 46.470 -11.900 -18.533 0.56 22.09 ?  3   VAL   B CG2  1 
ATOM   3872 C  CG2  B VAL   B 1 3   ? 46.369 -11.579 -18.184 0.44 20.48 ?  3   VAL   B CG2  1 
ATOM   3873 H  H    A VAL   B 1 3   ? 47.629 -13.543 -20.509 0.56 25.86 ?  3   VAL   B H    1 
ATOM   3874 H  H    B VAL   B 1 3   ? 47.557 -13.065 -20.252 0.44 25.66 ?  3   VAL   B H    1 
ATOM   3875 H  HA   A VAL   B 1 3   ? 48.594 -14.455 -18.147 0.56 24.16 ?  3   VAL   B HA   1 
ATOM   3876 H  HA   B VAL   B 1 3   ? 48.403 -14.213 -17.944 0.44 23.75 ?  3   VAL   B HA   1 
ATOM   3877 H  HB   A VAL   B 1 3   ? 47.307 -12.887 -16.951 0.56 25.66 ?  3   VAL   B HB   1 
ATOM   3878 H  HB   B VAL   B 1 3   ? 47.202 -12.669 -16.676 0.44 24.16 ?  3   VAL   B HB   1 
ATOM   3879 H  HG11 A VAL   B 1 3   ? 48.645 -11.004 -17.261 0.56 26.19 ?  3   VAL   B HG11 1 
ATOM   3880 H  HG11 B VAL   B 1 3   ? 48.595 -10.822 -16.917 0.44 24.31 ?  3   VAL   B HG11 1 
ATOM   3881 H  HG12 A VAL   B 1 3   ? 49.539 -12.318 -17.281 0.56 26.19 ?  3   VAL   B HG12 1 
ATOM   3882 H  HG12 B VAL   B 1 3   ? 49.441 -12.162 -17.018 0.44 24.31 ?  3   VAL   B HG12 1 
ATOM   3883 H  HG13 A VAL   B 1 3   ? 49.159 -11.595 -18.644 0.56 26.19 ?  3   VAL   B HG13 1 
ATOM   3884 H  HG13 B VAL   B 1 3   ? 49.065 -11.359 -18.336 0.44 24.31 ?  3   VAL   B HG13 1 
ATOM   3885 H  HG21 A VAL   B 1 3   ? 46.397 -11.026 -18.124 0.56 26.50 ?  3   VAL   B HG21 1 
ATOM   3886 H  HG21 B VAL   B 1 3   ? 46.336 -10.722 -17.731 0.44 24.57 ?  3   VAL   B HG21 1 
ATOM   3887 H  HG22 A VAL   B 1 3   ? 46.675 -11.809 -19.476 0.56 26.50 ?  3   VAL   B HG22 1 
ATOM   3888 H  HG22 B VAL   B 1 3   ? 46.555 -11.449 -19.126 0.44 24.57 ?  3   VAL   B HG22 1 
ATOM   3889 H  HG23 A VAL   B 1 3   ? 45.638 -12.388 -18.422 0.56 26.50 ?  3   VAL   B HG23 1 
ATOM   3890 H  HG23 B VAL   B 1 3   ? 45.524 -12.044 -18.074 0.44 24.57 ?  3   VAL   B HG23 1 
ATOM   3891 N  N    . ASN   B 1 4   ? 46.365 -15.479 -17.468 1.00 17.12 ?  4   ASN   B N    1 
ATOM   3892 C  CA   . ASN   B 1 4   ? 45.229 -16.393 -17.344 1.00 16.53 ?  4   ASN   B CA   1 
ATOM   3893 C  C    . ASN   B 1 4   ? 45.172 -17.363 -18.522 1.00 16.96 ?  4   ASN   B C    1 
ATOM   3894 O  O    . ASN   B 1 4   ? 44.110 -17.614 -19.086 1.00 17.63 ?  4   ASN   B O    1 
ATOM   3895 C  CB   . ASN   B 1 4   ? 43.903 -15.643 -17.179 1.00 16.16 ?  4   ASN   B CB   1 
ATOM   3896 C  CG   . ASN   B 1 4   ? 43.862 -14.815 -15.912 1.00 15.47 ?  4   ASN   B CG   1 
ATOM   3897 O  OD1  . ASN   B 1 4   ? 44.143 -15.316 -14.824 1.00 15.12 ?  4   ASN   B OD1  1 
ATOM   3898 N  ND2  . ASN   B 1 4   ? 43.526 -13.537 -16.048 1.00 16.16 ?  4   ASN   B ND2  1 
ATOM   3899 H  H    A ASN   B 1 4   ? 46.817 -15.375 -16.746 0.56 20.54 ?  4   ASN   B H    1 
ATOM   3900 H  H    B ASN   B 1 4   ? 46.964 -15.592 -16.864 0.44 20.54 ?  4   ASN   B H    1 
ATOM   3901 H  HA   . ASN   B 1 4   ? 45.362 -16.922 -16.543 1.00 19.84 ?  4   ASN   B HA   1 
ATOM   3902 H  HB2  . ASN   B 1 4   ? 43.769 -15.049 -17.931 1.00 19.39 ?  4   ASN   B HB2  1 
ATOM   3903 H  HB3  . ASN   B 1 4   ? 43.179 -16.292 -17.139 1.00 19.39 ?  4   ASN   B HB3  1 
ATOM   3904 H  HD21 . ASN   B 1 4   ? 43.493 -13.024 -15.357 1.00 19.40 ?  4   ASN   B HD21 1 
ATOM   3905 H  HD22 . ASN   B 1 4   ? 43.342 -13.218 -16.826 1.00 19.40 ?  4   ASN   B HD22 1 
ATOM   3906 N  N    . SER   B 1 5   ? 46.332 -17.897 -18.908 1.00 18.24 ?  5   SER   B N    1 
ATOM   3907 C  CA   . SER   B 1 5   ? 46.427 -18.811 -20.045 1.00 21.05 ?  5   SER   B CA   1 
ATOM   3908 C  C    . SER   B 1 5   ? 46.433 -20.232 -19.493 1.00 22.08 ?  5   SER   B C    1 
ATOM   3909 O  O    . SER   B 1 5   ? 47.468 -20.887 -19.387 1.00 23.79 ?  5   SER   B O    1 
ATOM   3910 C  CB   . SER   B 1 5   ? 47.668 -18.511 -20.879 1.00 22.87 ?  5   SER   B CB   1 
ATOM   3911 O  OG   . SER   B 1 5   ? 48.846 -18.687 -20.111 1.00 25.31 ?  5   SER   B OG   1 
ATOM   3912 H  H    . SER   B 1 5   ? 47.088 -17.750 -18.517 1.00 21.88 ?  5   SER   B H    1 
ATOM   3913 H  HA   . SER   B 1 5   ? 45.650 -18.706 -20.609 1.00 25.25 ?  5   SER   B HA   1 
ATOM   3914 H  HB2  . SER   B 1 5   ? 47.687 -19.106 -21.648 1.00 27.45 ?  5   SER   B HB2  1 
ATOM   3915 H  HB3  . SER   B 1 5   ? 47.617 -17.590 -21.181 1.00 27.45 ?  5   SER   B HB3  1 
ATOM   3916 H  HG   . SER   B 1 5   ? 48.922 -19.492 -19.883 1.00 30.38 ?  5   SER   B HG   1 
ATOM   3917 N  N    . PHE   B 1 6   ? 45.246 -20.694 -19.114 1.00 22.34 ?  6   PHE   B N    1 
ATOM   3918 C  CA   . PHE   B 1 6   ? 45.078 -22.035 -18.575 1.00 21.81 ?  6   PHE   B CA   1 
ATOM   3919 C  C    . PHE   B 1 6   ? 45.020 -23.032 -19.723 1.00 25.13 ?  6   PHE   B C    1 
ATOM   3920 O  O    . PHE   B 1 6   ? 44.333 -22.798 -20.721 1.00 27.00 ?  6   PHE   B O    1 
ATOM   3921 C  CB   . PHE   B 1 6   ? 43.789 -22.103 -17.756 1.00 19.63 ?  6   PHE   B CB   1 
ATOM   3922 C  CG   . PHE   B 1 6   ? 43.796 -21.224 -16.534 1.00 17.38 ?  6   PHE   B CG   1 
ATOM   3923 C  CD1  . PHE   B 1 6   ? 44.302 -21.693 -15.337 1.00 16.61 ?  6   PHE   B CD1  1 
ATOM   3924 C  CD2  . PHE   B 1 6   ? 43.298 -19.928 -16.585 1.00 16.89 ?  6   PHE   B CD2  1 
ATOM   3925 C  CE1  . PHE   B 1 6   ? 44.299 -20.889 -14.203 1.00 16.12 ?  6   PHE   B CE1  1 
ATOM   3926 C  CE2  . PHE   B 1 6   ? 43.301 -19.117 -15.462 1.00 17.27 ?  6   PHE   B CE2  1 
ATOM   3927 C  CZ   . PHE   B 1 6   ? 43.803 -19.593 -14.270 1.00 16.66 ?  6   PHE   B CZ   1 
ATOM   3928 H  H    . PHE   B 1 6   ? 44.515 -20.246 -19.168 1.00 26.81 ?  6   PHE   B H    1 
ATOM   3929 H  HA   . PHE   B 1 6   ? 45.826 -22.260 -18.005 1.00 26.18 ?  6   PHE   B HA   1 
ATOM   3930 H  HB2  . PHE   B 1 6   ? 43.046 -21.825 -18.315 1.00 23.56 ?  6   PHE   B HB2  1 
ATOM   3931 H  HB3  . PHE   B 1 6   ? 43.652 -23.016 -17.460 1.00 23.56 ?  6   PHE   B HB3  1 
ATOM   3932 H  HD1  . PHE   B 1 6   ? 44.643 -22.555 -15.284 1.00 19.93 ?  6   PHE   B HD1  1 
ATOM   3933 H  HD2  . PHE   B 1 6   ? 42.951 -19.603 -17.384 1.00 20.26 ?  6   PHE   B HD2  1 
ATOM   3934 H  HE1  . PHE   B 1 6   ? 44.651 -21.208 -13.401 1.00 19.35 ?  6   PHE   B HE1  1 
ATOM   3935 H  HE2  . PHE   B 1 6   ? 42.957 -18.253 -15.509 1.00 20.72 ?  6   PHE   B HE2  1 
ATOM   3936 H  HZ   . PHE   B 1 6   ? 43.805 -19.053 -13.512 1.00 19.99 ?  6   PHE   B HZ   1 
ATOM   3937 N  N    A SER   B 1 7   ? 45.742 -24.143 -19.587 0.56 25.54 ?  7   SER   B N    1 
ATOM   3938 N  N    B SER   B 1 7   ? 45.755 -24.135 -19.584 0.44 25.85 ?  7   SER   B N    1 
ATOM   3939 C  CA   A SER   B 1 7   ? 45.802 -25.144 -20.643 0.56 26.85 ?  7   SER   B CA   1 
ATOM   3940 C  CA   B SER   B 1 7   ? 45.866 -25.140 -20.631 0.44 27.18 ?  7   SER   B CA   1 
ATOM   3941 C  C    A SER   B 1 7   ? 45.777 -26.542 -20.042 0.56 26.16 ?  7   SER   B C    1 
ATOM   3942 C  C    B SER   B 1 7   ? 45.816 -26.531 -20.015 0.44 26.62 ?  7   SER   B C    1 
ATOM   3943 O  O    A SER   B 1 7   ? 46.388 -26.793 -18.999 0.56 26.50 ?  7   SER   B O    1 
ATOM   3944 O  O    B SER   B 1 7   ? 46.403 -26.774 -18.957 0.44 26.88 ?  7   SER   B O    1 
ATOM   3945 C  CB   A SER   B 1 7   ? 47.066 -24.965 -21.496 0.56 28.63 ?  7   SER   B CB   1 
ATOM   3946 C  CB   B SER   B 1 7   ? 47.179 -24.974 -21.408 0.44 28.79 ?  7   SER   B CB   1 
ATOM   3947 O  OG   A SER   B 1 7   ? 46.994 -25.735 -22.683 0.56 29.96 ?  7   SER   B OG   1 
ATOM   3948 O  OG   B SER   B 1 7   ? 47.321 -25.976 -22.399 0.44 29.96 ?  7   SER   B OG   1 
ATOM   3949 H  H    A SER   B 1 7   ? 46.212 -24.335 -18.892 0.56 30.65 ?  7   SER   B H    1 
ATOM   3950 H  H    B SER   B 1 7   ? 46.211 -24.322 -18.878 0.44 31.03 ?  7   SER   B H    1 
ATOM   3951 H  HA   A SER   B 1 7   ? 45.031 -25.050 -21.221 0.56 32.21 ?  7   SER   B HA   1 
ATOM   3952 H  HA   B SER   B 1 7   ? 45.127 -25.052 -21.251 0.44 32.62 ?  7   SER   B HA   1 
ATOM   3953 H  HB2  A SER   B 1 7   ? 47.153 -24.030 -21.740 0.56 34.36 ?  7   SER   B HB2  1 
ATOM   3954 H  HB2  B SER   B 1 7   ? 47.183 -24.102 -21.835 0.44 34.55 ?  7   SER   B HB2  1 
ATOM   3955 H  HB3  A SER   B 1 7   ? 47.839 -25.244 -20.979 0.56 34.36 ?  7   SER   B HB3  1 
ATOM   3956 H  HB3  B SER   B 1 7   ? 47.923 -25.040 -20.788 0.44 34.55 ?  7   SER   B HB3  1 
ATOM   3957 H  HG   A SER   B 1 7   ? 47.696 -25.636 -23.134 0.56 35.95 ?  7   SER   B HG   1 
ATOM   3958 H  HG   B SER   B 1 7   ? 48.041 -25.867 -22.817 0.44 35.95 ?  7   SER   B HG   1 
ATOM   3959 N  N    A GLY   B 1 8   ? 45.066 -27.448 -20.710 0.56 25.70 ?  8   GLY   B N    1 
ATOM   3960 N  N    B GLY   B 1 8   ? 45.111 -27.439 -20.687 0.44 26.17 ?  8   GLY   B N    1 
ATOM   3961 C  CA   A GLY   B 1 8   ? 45.044 -28.838 -20.304 0.56 25.06 ?  8   GLY   B CA   1 
ATOM   3962 C  CA   B GLY   B 1 8   ? 45.075 -28.824 -20.266 0.44 25.47 ?  8   GLY   B CA   1 
ATOM   3963 C  C    A GLY   B 1 8   ? 44.070 -29.171 -19.201 0.56 24.16 ?  8   GLY   B C    1 
ATOM   3964 C  C    B GLY   B 1 8   ? 44.120 -29.132 -19.140 0.44 24.48 ?  8   GLY   B C    1 
ATOM   3965 O  O    A GLY   B 1 8   ? 44.179 -30.247 -18.602 0.56 24.74 ?  8   GLY   B O    1 
ATOM   3966 O  O    B GLY   B 1 8   ? 44.295 -30.149 -18.460 0.44 25.15 ?  8   GLY   B O    1 
ATOM   3967 H  H    A GLY   B 1 8   ? 44.589 -27.275 -21.404 0.56 30.84 ?  8   GLY   B H    1 
ATOM   3968 H  H    B GLY   B 1 8   ? 44.645 -27.272 -21.390 0.44 31.41 ?  8   GLY   B H    1 
ATOM   3969 H  HA2  A GLY   B 1 8   ? 44.818 -29.384 -21.072 0.56 30.07 ?  8   GLY   B HA2  1 
ATOM   3970 H  HA2  B GLY   B 1 8   ? 44.829 -29.376 -21.025 0.44 30.57 ?  8   GLY   B HA2  1 
ATOM   3971 H  HA3  A GLY   B 1 8   ? 45.928 -29.092 -20.003 0.56 30.07 ?  8   GLY   B HA3  1 
ATOM   3972 H  HA3  B GLY   B 1 8   ? 45.960 -29.089 -19.977 0.44 30.57 ?  8   GLY   B HA3  1 
ATOM   3973 N  N    . TYR   B 1 9   ? 43.108 -28.296 -18.920 1.00 23.20 ?  9   TYR   B N    1 
ATOM   3974 C  CA   . TYR   B 1 9   ? 42.135 -28.549 -17.871 1.00 20.98 ?  9   TYR   B CA   1 
ATOM   3975 C  C    . TYR   B 1 9   ? 40.954 -29.336 -18.405 1.00 20.68 ?  9   TYR   B C    1 
ATOM   3976 O  O    . TYR   B 1 9   ? 40.554 -29.198 -19.564 1.00 22.46 ?  9   TYR   B O    1 
ATOM   3977 C  CB   . TYR   B 1 9   ? 41.626 -27.253 -17.246 1.00 20.10 ?  9   TYR   B CB   1 
ATOM   3978 C  CG   . TYR   B 1 9   ? 42.638 -26.628 -16.320 1.00 19.49 ?  9   TYR   B CG   1 
ATOM   3979 C  CD1  . TYR   B 1 9   ? 43.747 -25.965 -16.825 1.00 20.27 ?  9   TYR   B CD1  1 
ATOM   3980 C  CD2  . TYR   B 1 9   ? 42.501 -26.719 -14.941 1.00 18.73 ?  9   TYR   B CD2  1 
ATOM   3981 C  CE1  . TYR   B 1 9   ? 44.689 -25.405 -15.988 1.00 20.62 ?  9   TYR   B CE1  1 
ATOM   3982 C  CE2  . TYR   B 1 9   ? 43.442 -26.162 -14.093 1.00 18.90 ?  9   TYR   B CE2  1 
ATOM   3983 C  CZ   . TYR   B 1 9   ? 44.533 -25.502 -14.627 1.00 20.30 ?  9   TYR   B CZ   1 
ATOM   3984 O  OH   . TYR   B 1 9   ? 45.475 -24.947 -13.798 1.00 20.85 ?  9   TYR   B OH   1 
ATOM   3985 H  H    A TYR   B 1 9   ? 42.986 -27.555 -19.337 0.56 27.84 ?  9   TYR   B H    1 
ATOM   3986 H  H    B TYR   B 1 9   ? 42.955 -27.582 -19.374 0.44 27.84 ?  9   TYR   B H    1 
ATOM   3987 H  HA   . TYR   B 1 9   ? 42.544 -29.076 -17.172 1.00 25.18 ?  9   TYR   B HA   1 
ATOM   3988 H  HB2  . TYR   B 1 9   ? 41.419 -26.613 -17.947 1.00 24.13 ?  9   TYR   B HB2  1 
ATOM   3989 H  HB3  . TYR   B 1 9   ? 40.833 -27.452 -16.730 1.00 24.13 ?  9   TYR   B HB3  1 
ATOM   3990 H  HD1  . TYR   B 1 9   ? 43.855 -25.900 -17.746 1.00 24.32 ?  9   TYR   B HD1  1 
ATOM   3991 H  HD2  . TYR   B 1 9   ? 41.765 -27.168 -14.582 1.00 22.48 ?  9   TYR   B HD2  1 
ATOM   3992 H  HE1  . TYR   B 1 9   ? 45.422 -24.964 -16.342 1.00 24.74 ?  9   TYR   B HE1  1 
ATOM   3993 H  HE2  . TYR   B 1 9   ? 43.334 -26.231 -13.169 1.00 22.68 ?  9   TYR   B HE2  1 
ATOM   3994 H  HH   . TYR   B 1 9   ? 46.074 -24.583 -14.252 1.00 25.02 ?  9   TYR   B HH   1 
ATOM   3995 N  N    . LEU   B 1 10  ? 40.401 -30.170 -17.535 1.00 18.92 ?  10  LEU   B N    1 
ATOM   3996 C  CA   . LEU   B 1 10  ? 39.199 -30.931 -17.819 1.00 18.65 ?  10  LEU   B CA   1 
ATOM   3997 C  C    . LEU   B 1 10  ? 38.005 -30.169 -17.260 1.00 18.02 ?  10  LEU   B C    1 
ATOM   3998 O  O    . LEU   B 1 10  ? 38.014 -29.753 -16.098 1.00 17.65 ?  10  LEU   B O    1 
ATOM   3999 C  CB   . LEU   B 1 10  ? 39.302 -32.307 -17.162 1.00 19.42 ?  10  LEU   B CB   1 
ATOM   4000 C  CG   . LEU   B 1 10  ? 38.166 -33.269 -17.481 1.00 20.94 ?  10  LEU   B CG   1 
ATOM   4001 C  CD1  . LEU   B 1 10  ? 38.252 -33.736 -18.926 1.00 22.36 ?  10  LEU   B CD1  1 
ATOM   4002 C  CD2  . LEU   B 1 10  ? 38.186 -34.444 -16.525 1.00 21.98 ?  10  LEU   B CD2  1 
ATOM   4003 H  H    . LEU   B 1 10  ? 40.713 -30.318 -16.742 1.00 22.71 ?  10  LEU   B H    1 
ATOM   4004 H  HA   . LEU   B 1 10  ? 39.087 -31.044 -18.775 1.00 22.38 ?  10  LEU   B HA   1 
ATOM   4005 H  HB2  . LEU   B 1 10  ? 40.128 -32.727 -17.451 1.00 23.31 ?  10  LEU   B HB2  1 
ATOM   4006 H  HB3  . LEU   B 1 10  ? 39.320 -32.190 -16.198 1.00 23.31 ?  10  LEU   B HB3  1 
ATOM   4007 H  HG   . LEU   B 1 10  ? 37.321 -32.810 -17.366 1.00 25.12 ?  10  LEU   B HG   1 
ATOM   4008 H  HD11 . LEU   B 1 10  ? 37.562 -34.398 -19.083 1.00 26.83 ?  10  LEU   B HD11 1 
ATOM   4009 H  HD12 . LEU   B 1 10  ? 38.116 -32.972 -19.510 1.00 26.83 ?  10  LEU   B HD12 1 
ATOM   4010 H  HD13 . LEU   B 1 10  ? 39.126 -34.122 -19.081 1.00 26.83 ?  10  LEU   B HD13 1 
ATOM   4011 H  HD21 . LEU   B 1 10  ? 37.461 -35.045 -16.752 1.00 26.38 ?  10  LEU   B HD21 1 
ATOM   4012 H  HD22 . LEU   B 1 10  ? 39.037 -34.900 -16.607 1.00 26.38 ?  10  LEU   B HD22 1 
ATOM   4013 H  HD23 . LEU   B 1 10  ? 38.072 -34.111 -15.621 1.00 26.38 ?  10  LEU   B HD23 1 
ATOM   4014 N  N    . LYS   B 1 11  ? 36.984 -29.987 -18.089 1.00 19.43 ?  11  LYS   B N    1 
ATOM   4015 C  CA   . LYS   B 1 11  ? 35.787 -29.269 -17.680 1.00 21.62 ?  11  LYS   B CA   1 
ATOM   4016 C  C    . LYS   B 1 11  ? 34.906 -30.190 -16.842 1.00 20.54 ?  11  LYS   B C    1 
ATOM   4017 O  O    . LYS   B 1 11  ? 34.536 -31.280 -17.292 1.00 21.83 ?  11  LYS   B O    1 
ATOM   4018 C  CB   . LYS   B 1 11  ? 35.039 -28.809 -18.929 1.00 25.82 ?  11  LYS   B CB   1 
ATOM   4019 C  CG   . LYS   B 1 11  ? 33.874 -27.873 -18.680 1.00 29.42 ?  11  LYS   B CG   1 
ATOM   4020 C  CD   . LYS   B 1 11  ? 33.109 -27.626 -19.973 1.00 32.35 ?  11  LYS   B CD   1 
ATOM   4021 C  CE   . LYS   B 1 11  ? 32.116 -26.487 -19.831 1.00 34.46 ?  11  LYS   B CE   1 
ATOM   4022 N  NZ   . LYS   B 1 11  ? 32.804 -25.179 -19.673 1.00 35.59 ?  11  LYS   B NZ   1 
ATOM   4023 H  H    . LYS   B 1 11  ? 36.954 -30.284 -18.896 1.00 23.32 ?  11  LYS   B H    1 
ATOM   4024 H  HA   . LYS   B 1 11  ? 36.028 -28.499 -17.149 1.00 25.94 ?  11  LYS   B HA   1 
ATOM   4025 H  HB2  . LYS   B 1 11  ? 35.666 -28.346 -19.507 1.00 30.99 ?  11  LYS   B HB2  1 
ATOM   4026 H  HB3  . LYS   B 1 11  ? 34.692 -29.590 -19.389 1.00 30.99 ?  11  LYS   B HB3  1 
ATOM   4027 H  HG2  . LYS   B 1 11  ? 33.268 -28.273 -18.037 1.00 35.30 ?  11  LYS   B HG2  1 
ATOM   4028 H  HG3  . LYS   B 1 11  ? 34.207 -27.023 -18.352 1.00 35.30 ?  11  LYS   B HG3  1 
ATOM   4029 H  HD2  . LYS   B 1 11  ? 33.737 -27.396 -20.677 1.00 38.82 ?  11  LYS   B HD2  1 
ATOM   4030 H  HD3  . LYS   B 1 11  ? 32.620 -28.429 -20.213 1.00 38.82 ?  11  LYS   B HD3  1 
ATOM   4031 H  HE2  . LYS   B 1 11  ? 31.561 -26.446 -20.626 1.00 41.35 ?  11  LYS   B HE2  1 
ATOM   4032 H  HE3  . LYS   B 1 11  ? 31.567 -26.642 -19.047 1.00 41.35 ?  11  LYS   B HE3  1 
ATOM   4033 H  HZ1  . LYS   B 1 11  ? 32.205 -24.524 -19.623 1.00 42.71 ?  11  LYS   B HZ1  1 
ATOM   4034 H  HZ2  . LYS   B 1 11  ? 33.294 -25.180 -18.930 1.00 42.71 ?  11  LYS   B HZ2  1 
ATOM   4035 H  HZ3  . LYS   B 1 11  ? 33.338 -25.030 -20.370 1.00 42.71 ?  11  LYS   B HZ3  1 
ATOM   4036 N  N    . LEU   B 1 12  ? 34.568 -29.757 -15.626 1.00 18.71 ?  12  LEU   B N    1 
ATOM   4037 C  CA   . LEU   B 1 12  ? 33.617 -30.472 -14.781 1.00 18.13 ?  12  LEU   B CA   1 
ATOM   4038 C  C    . LEU   B 1 12  ? 32.223 -29.872 -14.865 1.00 17.85 ?  12  LEU   B C    1 
ATOM   4039 O  O    . LEU   B 1 12  ? 31.238 -30.596 -15.034 1.00 18.28 ?  12  LEU   B O    1 
ATOM   4040 C  CB   . LEU   B 1 12  ? 34.079 -30.490 -13.319 1.00 17.59 ?  12  LEU   B CB   1 
ATOM   4041 C  CG   . LEU   B 1 12  ? 35.416 -31.173 -13.040 1.00 17.31 ?  12  LEU   B CG   1 
ATOM   4042 C  CD1  . LEU   B 1 12  ? 35.754 -31.121 -11.563 1.00 17.43 ?  12  LEU   B CD1  1 
ATOM   4043 C  CD2  . LEU   B 1 12  ? 35.410 -32.613 -13.533 1.00 17.78 ?  12  LEU   B CD2  1 
ATOM   4044 H  H    . LEU   B 1 12  ? 34.873 -29.038 -15.271 1.00 22.45 ?  12  LEU   B H    1 
ATOM   4045 H  HA   . LEU   B 1 12  ? 33.544 -31.385 -15.089 1.00 21.76 ?  12  LEU   B HA   1 
ATOM   4046 H  HB2  . LEU   B 1 12  ? 34.150 -29.575 -13.014 1.00 21.11 ?  12  LEU   B HB2  1 
ATOM   4047 H  HB3  . LEU   B 1 12  ? 33.401 -30.951 -12.797 1.00 21.11 ?  12  LEU   B HB3  1 
ATOM   4048 H  HG   . LEU   B 1 12  ? 36.111 -30.702 -13.522 1.00 20.77 ?  12  LEU   B HG   1 
ATOM   4049 H  HD11 . LEU   B 1 12  ? 36.609 -31.559 -11.419 1.00 20.91 ?  12  LEU   B HD11 1 
ATOM   4050 H  HD12 . LEU   B 1 12  ? 35.807 -30.194 -11.284 1.00 20.91 ?  12  LEU   B HD12 1 
ATOM   4051 H  HD13 . LEU   B 1 12  ? 35.061 -31.579 -11.062 1.00 20.91 ?  12  LEU   B HD13 1 
ATOM   4052 H  HD21 . LEU   B 1 12  ? 36.216 -33.055 -13.228 1.00 21.33 ?  12  LEU   B HD21 1 
ATOM   4053 H  HD22 . LEU   B 1 12  ? 34.628 -33.066 -13.176 1.00 21.33 ?  12  LEU   B HD22 1 
ATOM   4054 H  HD23 . LEU   B 1 12  ? 35.376 -32.617 -14.503 1.00 21.33 ?  12  LEU   B HD23 1 
ATOM   4055 N  N    . THR   B 1 13  ? 32.126 -28.554 -14.744 1.00 18.05 ?  13  THR   B N    1 
ATOM   4056 C  CA   . THR   B 1 13  ? 30.897 -27.808 -14.958 1.00 18.19 ?  13  THR   B CA   1 
ATOM   4057 C  C    . THR   B 1 13  ? 31.227 -26.612 -15.841 1.00 19.98 ?  13  THR   B C    1 
ATOM   4058 O  O    . THR   B 1 13  ? 32.375 -26.415 -16.258 1.00 20.63 ?  13  THR   B O    1 
ATOM   4059 C  CB   . THR   B 1 13  ? 30.289 -27.333 -13.635 1.00 17.75 ?  13  THR   B CB   1 
ATOM   4060 O  OG1  . THR   B 1 13  ? 31.135 -26.315 -13.082 1.00 17.30 ?  13  THR   B OG1  1 
ATOM   4061 C  CG2  . THR   B 1 13  ? 30.165 -28.489 -12.648 1.00 18.29 ?  13  THR   B CG2  1 
ATOM   4062 H  H    . THR   B 1 13  ? 32.786 -28.046 -14.532 1.00 21.67 ?  13  THR   B H    1 
ATOM   4063 H  HA   . THR   B 1 13  ? 30.245 -28.362 -15.411 1.00 21.83 ?  13  THR   B HA   1 
ATOM   4064 H  HB   . THR   B 1 13  ? 29.400 -26.964 -13.793 1.00 21.30 ?  13  THR   B HB   1 
ATOM   4065 H  HG1  . THR   B 1 13  ? 30.822 -25.547 -13.261 1.00 20.76 ?  13  THR   B HG1  1 
ATOM   4066 H  HG21 . THR   B 1 13  ? 29.657 -28.210 -11.869 1.00 21.94 ?  13  THR   B HG21 1 
ATOM   4067 H  HG22 . THR   B 1 13  ? 29.709 -29.233 -13.070 1.00 21.94 ?  13  THR   B HG22 1 
ATOM   4068 H  HG23 . THR   B 1 13  ? 31.045 -28.777 -12.365 1.00 21.94 ?  13  THR   B HG23 1 
ATOM   4069 N  N    A ASP   B 1 14  ? 30.209 -25.794 -16.110 0.56 20.90 ?  14  ASP   B N    1 
ATOM   4070 N  N    B ASP   B 1 14  ? 30.215 -25.783 -16.109 0.44 20.84 ?  14  ASP   B N    1 
ATOM   4071 C  CA   A ASP   B 1 14  ? 30.415 -24.629 -16.960 0.56 22.33 ?  14  ASP   B CA   1 
ATOM   4072 C  CA   B ASP   B 1 14  ? 30.419 -24.626 -16.973 0.44 21.98 ?  14  ASP   B CA   1 
ATOM   4073 C  C    A ASP   B 1 14  ? 31.526 -23.732 -16.429 0.56 20.49 ?  14  ASP   B C    1 
ATOM   4074 C  C    B ASP   B 1 14  ? 31.415 -23.626 -16.403 0.44 20.24 ?  14  ASP   B C    1 
ATOM   4075 O  O    A ASP   B 1 14  ? 32.211 -23.075 -17.220 0.56 21.00 ?  14  ASP   B O    1 
ATOM   4076 O  O    B ASP   B 1 14  ? 31.865 -22.743 -17.140 0.44 20.47 ?  14  ASP   B O    1 
ATOM   4077 C  CB   A ASP   B 1 14  ? 29.107 -23.846 -17.114 0.56 25.57 ?  14  ASP   B CB   1 
ATOM   4078 C  CB   B ASP   B 1 14  ? 29.097 -23.905 -17.238 0.44 24.82 ?  14  ASP   B CB   1 
ATOM   4079 C  CG   A ASP   B 1 14  ? 28.122 -24.520 -18.053 0.56 28.76 ?  14  ASP   B CG   1 
ATOM   4080 C  CG   B ASP   B 1 14  ? 28.236 -24.626 -18.258 0.44 27.59 ?  14  ASP   B CG   1 
ATOM   4081 O  OD1  A ASP   B 1 14  ? 28.448 -25.578 -18.638 0.56 29.65 ?  14  ASP   B OD1  1 
ATOM   4082 O  OD1  B ASP   B 1 14  ? 28.803 -25.277 -19.162 0.44 28.45 ?  14  ASP   B OD1  1 
ATOM   4083 O  OD2  A ASP   B 1 14  ? 27.004 -23.985 -18.200 0.56 30.01 -1 14  ASP   B OD2  1 
ATOM   4084 O  OD2  B ASP   B 1 14  ? 26.994 -24.546 -18.159 0.44 28.55 -1 14  ASP   B OD2  1 
ATOM   4085 H  H    A ASP   B 1 14  ? 29.411 -25.877 -15.804 0.56 25.08 ?  14  ASP   B H    1 
ATOM   4086 H  H    B ASP   B 1 14  ? 29.415 -25.864 -15.805 0.44 25.01 ?  14  ASP   B H    1 
ATOM   4087 H  HA   A ASP   B 1 14  ? 30.691 -24.918 -17.836 0.56 26.79 ?  14  ASP   B HA   1 
ATOM   4088 H  HA   B ASP   B 1 14  ? 30.764 -24.931 -17.825 0.44 26.37 ?  14  ASP   B HA   1 
ATOM   4089 H  HB2  A ASP   B 1 14  ? 28.665 -23.781 -16.257 0.56 30.68 ?  14  ASP   B HB2  1 
ATOM   4090 H  HB2  B ASP   B 1 14  ? 28.600 -23.844 -16.407 0.44 29.79 ?  14  ASP   B HB2  1 
ATOM   4091 H  HB3  A ASP   B 1 14  ? 29.299 -22.959 -17.460 0.56 30.68 ?  14  ASP   B HB3  1 
ATOM   4092 H  HB3  B ASP   B 1 14  ? 29.289 -23.009 -17.571 0.44 29.79 ?  14  ASP   B HB3  1 
ATOM   4093 N  N    . ASN   B 1 15  ? 31.742 -23.713 -15.111 1.00 18.28 ?  15  ASN   B N    1 
ATOM   4094 C  CA   . ASN   B 1 15  ? 32.699 -22.789 -14.506 1.00 15.83 ?  15  ASN   B CA   1 
ATOM   4095 C  C    . ASN   B 1 15  ? 33.796 -23.440 -13.672 1.00 14.83 ?  15  ASN   B C    1 
ATOM   4096 O  O    . ASN   B 1 15  ? 34.636 -22.710 -13.135 1.00 15.24 ?  15  ASN   B O    1 
ATOM   4097 C  CB   . ASN   B 1 15  ? 31.981 -21.734 -13.646 1.00 16.00 ?  15  ASN   B CB   1 
ATOM   4098 C  CG   . ASN   B 1 15  ? 31.356 -22.334 -12.406 1.00 15.62 ?  15  ASN   B CG   1 
ATOM   4099 O  OD1  . ASN   B 1 15  ? 30.417 -23.131 -12.499 1.00 17.23 ?  15  ASN   B OD1  1 
ATOM   4100 N  ND2  . ASN   B 1 15  ? 31.872 -21.976 -11.242 1.00 14.88 ?  15  ASN   B ND2  1 
ATOM   4101 H  H    A ASN   B 1 15  ? 31.353 -24.235 -14.547 0.56 21.94 ?  15  ASN   B H    1 
ATOM   4102 H  H    B ASN   B 1 15  ? 31.395 -24.274 -14.557 0.44 21.94 ?  15  ASN   B H    1 
ATOM   4103 H  HA   . ASN   B 1 15  ? 33.148 -22.306 -15.206 1.00 18.99 ?  15  ASN   B HA   1 
ATOM   4104 H  HB2  . ASN   B 1 15  ? 32.622 -21.059 -13.364 1.00 19.20 ?  15  ASN   B HB2  1 
ATOM   4105 H  HB3  . ASN   B 1 15  ? 31.273 -21.320 -14.165 1.00 19.20 ?  15  ASN   B HB3  1 
ATOM   4106 H  HD21 . ASN   B 1 15  ? 31.547 -22.284 -10.506 1.00 17.85 ?  15  ASN   B HD21 1 
ATOM   4107 H  HD22 . ASN   B 1 15  ? 32.530 -21.414 -11.211 1.00 17.85 ?  15  ASN   B HD22 1 
ATOM   4108 N  N    . VAL   B 1 16  ? 33.821 -24.764 -13.540 1.00 14.71 ?  16  VAL   B N    1 
ATOM   4109 C  CA   . VAL   B 1 16  ? 34.816 -25.454 -12.725 1.00 14.35 ?  16  VAL   B CA   1 
ATOM   4110 C  C    . VAL   B 1 16  ? 35.609 -26.397 -13.614 1.00 14.64 ?  16  VAL   B C    1 
ATOM   4111 O  O    . VAL   B 1 16  ? 35.033 -27.277 -14.274 1.00 15.77 ?  16  VAL   B O    1 
ATOM   4112 C  CB   . VAL   B 1 16  ? 34.181 -26.213 -11.545 1.00 14.88 ?  16  VAL   B CB   1 
ATOM   4113 C  CG1  . VAL   B 1 16  ? 35.260 -26.942 -10.738 1.00 14.49 ?  16  VAL   B CG1  1 
ATOM   4114 C  CG2  . VAL   B 1 16  ? 33.376 -25.259 -10.660 1.00 15.48 ?  16  VAL   B CG2  1 
ATOM   4115 H  H    . VAL   B 1 16  ? 33.259 -25.299 -13.922 1.00 17.65 ?  16  VAL   B H    1 
ATOM   4116 H  HA   . VAL   B 1 16  ? 35.429 -24.797 -12.357 1.00 17.22 ?  16  VAL   B HA   1 
ATOM   4117 H  HB   . VAL   B 1 16  ? 33.574 -26.883 -11.895 1.00 17.85 ?  16  VAL   B HB   1 
ATOM   4118 H  HG11 . VAL   B 1 16  ? 34.874 -27.242 -9.900  1.00 17.38 ?  16  VAL   B HG11 1 
ATOM   4119 H  HG12 . VAL   B 1 16  ? 35.581 -27.701 -11.245 1.00 17.38 ?  16  VAL   B HG12 1 
ATOM   4120 H  HG13 . VAL   B 1 16  ? 35.990 -26.326 -10.561 1.00 17.38 ?  16  VAL   B HG13 1 
ATOM   4121 H  HG21 . VAL   B 1 16  ? 33.031 -25.751 -9.898  1.00 18.58 ?  16  VAL   B HG21 1 
ATOM   4122 H  HG22 . VAL   B 1 16  ? 33.952 -24.542 -10.359 1.00 18.58 ?  16  VAL   B HG22 1 
ATOM   4123 H  HG23 . VAL   B 1 16  ? 32.639 -24.897 -11.179 1.00 18.58 ?  16  VAL   B HG23 1 
ATOM   4124 N  N    . TYR   B 1 17  ? 36.934 -26.234 -13.581 1.00 14.75 ?  17  TYR   B N    1 
ATOM   4125 C  CA   . TYR   B 1 17  ? 37.884 -26.981 -14.389 1.00 15.10 ?  17  TYR   B CA   1 
ATOM   4126 C  C    . TYR   B 1 17  ? 38.930 -27.586 -13.465 1.00 14.29 ?  17  TYR   B C    1 
ATOM   4127 O  O    . TYR   B 1 17  ? 39.194 -27.052 -12.385 1.00 14.47 ?  17  TYR   B O    1 
ATOM   4128 C  CB   . TYR   B 1 17  ? 38.589 -26.047 -15.383 1.00 17.75 ?  17  TYR   B CB   1 
ATOM   4129 C  CG   . TYR   B 1 17  ? 37.657 -25.273 -16.285 1.00 21.17 ?  17  TYR   B CG   1 
ATOM   4130 C  CD1  . TYR   B 1 17  ? 37.061 -24.090 -15.862 1.00 22.67 ?  17  TYR   B CD1  1 
ATOM   4131 C  CD2  . TYR   B 1 17  ? 37.377 -25.725 -17.566 1.00 23.34 ?  17  TYR   B CD2  1 
ATOM   4132 C  CE1  . TYR   B 1 17  ? 36.207 -23.381 -16.695 1.00 24.29 ?  17  TYR   B CE1  1 
ATOM   4133 C  CE2  . TYR   B 1 17  ? 36.530 -25.025 -18.404 1.00 24.88 ?  17  TYR   B CE2  1 
ATOM   4134 C  CZ   . TYR   B 1 17  ? 35.946 -23.857 -17.963 1.00 25.61 ?  17  TYR   B CZ   1 
ATOM   4135 O  OH   . TYR   B 1 17  ? 35.103 -23.160 -18.798 1.00 26.96 ?  17  TYR   B OH   1 
ATOM   4136 H  H    . TYR   B 1 17  ? 37.327 -25.656 -13.069 1.00 17.70 ?  17  TYR   B H    1 
ATOM   4137 H  HA   . TYR   B 1 17  ? 37.431 -27.691 -14.873 1.00 18.12 ?  17  TYR   B HA   1 
ATOM   4138 H  HB2  . TYR   B 1 17  ? 39.123 -25.406 -14.889 1.00 21.30 ?  17  TYR   B HB2  1 
ATOM   4139 H  HB3  . TYR   B 1 17  ? 39.157 -26.579 -15.954 1.00 21.30 ?  17  TYR   B HB3  1 
ATOM   4140 H  HD1  . TYR   B 1 17  ? 37.236 -23.768 -15.008 1.00 27.21 ?  17  TYR   B HD1  1 
ATOM   4141 H  HD2  . TYR   B 1 17  ? 37.765 -26.512 -17.869 1.00 28.00 ?  17  TYR   B HD2  1 
ATOM   4142 H  HE1  . TYR   B 1 17  ? 35.813 -22.589 -16.401 1.00 29.14 ?  17  TYR   B HE1  1 
ATOM   4143 H  HE2  . TYR   B 1 17  ? 36.348 -25.342 -19.261 1.00 29.86 ?  17  TYR   B HE2  1 
ATOM   4144 H  HH   . TYR   B 1 17  ? 35.030 -23.554 -19.535 1.00 32.35 ?  17  TYR   B HH   1 
ATOM   4145 N  N    . ILE   B 1 18  ? 39.546 -28.692 -13.887 1.00 14.45 ?  18  ILE   B N    1 
ATOM   4146 C  CA   . ILE   B 1 18  ? 40.478 -29.403 -13.020 1.00 14.19 ?  18  ILE   B CA   1 
ATOM   4147 C  C    . ILE   B 1 18  ? 41.641 -29.951 -13.837 1.00 14.55 ?  18  ILE   B C    1 
ATOM   4148 O  O    . ILE   B 1 18  ? 41.478 -30.352 -14.995 1.00 15.93 ?  18  ILE   B O    1 
ATOM   4149 C  CB   . ILE   B 1 18  ? 39.726 -30.502 -12.230 1.00 14.71 ?  18  ILE   B CB   1 
ATOM   4150 C  CG1  . ILE   B 1 18  ? 40.581 -31.044 -11.081 1.00 15.30 ?  18  ILE   B CG1  1 
ATOM   4151 C  CG2  . ILE   B 1 18  ? 39.234 -31.615 -13.167 1.00 15.07 ?  18  ILE   B CG2  1 
ATOM   4152 C  CD1  . ILE   B 1 18  ? 39.765 -31.835 -10.063 1.00 16.56 ?  18  ILE   B CD1  1 
ATOM   4153 H  H    . ILE   B 1 18  ? 39.445 -29.046 -14.664 1.00 17.34 ?  18  ILE   B H    1 
ATOM   4154 H  HA   . ILE   B 1 18  ? 40.839 -28.782 -12.369 1.00 17.03 ?  18  ILE   B HA   1 
ATOM   4155 H  HB   . ILE   B 1 18  ? 38.941 -30.096 -11.834 1.00 17.65 ?  18  ILE   B HB   1 
ATOM   4156 H  HG12 . ILE   B 1 18  ? 41.261 -31.630 -11.439 1.00 18.36 ?  18  ILE   B HG12 1 
ATOM   4157 H  HG13 . ILE   B 1 18  ? 40.991 -30.297 -10.617 1.00 18.36 ?  18  ILE   B HG13 1 
ATOM   4158 H  HG21 . ILE   B 1 18  ? 38.643 -32.207 -12.672 1.00 18.09 ?  18  ILE   B HG21 1 
ATOM   4159 H  HG22 . ILE   B 1 18  ? 38.748 -31.209 -13.903 1.00 18.09 ?  18  ILE   B HG22 1 
ATOM   4160 H  HG23 . ILE   B 1 18  ? 39.994 -32.110 -13.503 1.00 18.09 ?  18  ILE   B HG23 1 
ATOM   4161 H  HD11 . ILE   B 1 18  ? 40.350 -32.122 -9.343  1.00 19.88 ?  18  ILE   B HD11 1 
ATOM   4162 H  HD12 . ILE   B 1 18  ? 39.062 -31.266 -9.708  1.00 19.88 ?  18  ILE   B HD12 1 
ATOM   4163 H  HD13 . ILE   B 1 18  ? 39.375 -32.608 -10.500 1.00 19.88 ?  18  ILE   B HD13 1 
ATOM   4164 N  N    . LYS   B 1 19  ? 42.824 -29.982 -13.215 1.00 14.96 ?  19  LYS   B N    1 
ATOM   4165 C  CA   . LYS   B 1 19  ? 44.037 -30.460 -13.863 1.00 15.61 ?  19  LYS   B CA   1 
ATOM   4166 C  C    . LYS   B 1 19  ? 44.928 -31.140 -12.836 1.00 15.62 ?  19  LYS   B C    1 
ATOM   4167 O  O    . LYS   B 1 19  ? 45.001 -30.712 -11.683 1.00 15.15 ?  19  LYS   B O    1 
ATOM   4168 C  CB   . LYS   B 1 19  ? 44.814 -29.298 -14.495 1.00 17.16 ?  19  LYS   B CB   1 
ATOM   4169 C  CG   . LYS   B 1 19  ? 46.028 -29.706 -15.314 1.00 18.87 ?  19  LYS   B CG   1 
ATOM   4170 C  CD   . LYS   B 1 19  ? 46.751 -28.472 -15.838 1.00 20.39 ?  19  LYS   B CD   1 
ATOM   4171 C  CE   . LYS   B 1 19  ? 47.897 -28.842 -16.756 1.00 22.30 ?  19  LYS   B CE   1 
ATOM   4172 N  NZ   . LYS   B 1 19  ? 48.623 -27.639 -17.246 1.00 23.37 ?  19  LYS   B NZ   1 
ATOM   4173 H  H    . LYS   B 1 19  ? 42.942 -29.720 -12.398 1.00 17.95 ?  19  LYS   B H    1 
ATOM   4174 H  HA   . LYS   B 1 19  ? 43.805 -31.098 -14.551 1.00 18.73 ?  19  LYS   B HA   1 
ATOM   4175 H  HB2  . LYS   B 1 19  ? 44.214 -28.815 -15.082 1.00 20.59 ?  19  LYS   B HB2  1 
ATOM   4176 H  HB3  . LYS   B 1 19  ? 45.119 -28.709 -13.785 1.00 20.59 ?  19  LYS   B HB3  1 
ATOM   4177 H  HG2  . LYS   B 1 19  ? 46.639 -30.213 -14.756 1.00 22.64 ?  19  LYS   B HG2  1 
ATOM   4178 H  HG3  . LYS   B 1 19  ? 45.737 -30.242 -16.070 1.00 22.64 ?  19  LYS   B HG3  1 
ATOM   4179 H  HD2  . LYS   B 1 19  ? 46.123 -27.923 -16.333 1.00 24.46 ?  19  LYS   B HD2  1 
ATOM   4180 H  HD3  . LYS   B 1 19  ? 47.110 -27.973 -15.085 1.00 24.46 ?  19  LYS   B HD3  1 
ATOM   4181 H  HE2  . LYS   B 1 19  ? 48.523 -29.402 -16.272 1.00 26.76 ?  19  LYS   B HE2  1 
ATOM   4182 H  HE3  . LYS   B 1 19  ? 47.544 -29.320 -17.524 1.00 26.76 ?  19  LYS   B HE3  1 
ATOM   4183 H  HZ1  . LYS   B 1 19  ? 49.261 -27.882 -17.818 1.00 28.05 ?  19  LYS   B HZ1  1 
ATOM   4184 H  HZ2  . LYS   B 1 19  ? 48.058 -27.090 -17.661 1.00 28.05 ?  19  LYS   B HZ2  1 
ATOM   4185 H  HZ3  . LYS   B 1 19  ? 48.995 -27.209 -16.563 1.00 28.05 ?  19  LYS   B HZ3  1 
ATOM   4186 N  N    . ASN   B 1 20  ? 45.612 -32.195 -13.264 1.00 16.84 ?  20  ASN   B N    1 
ATOM   4187 C  CA   . ASN   B 1 20  ? 46.636 -32.825 -12.438 1.00 17.85 ?  20  ASN   B CA   1 
ATOM   4188 C  C    . ASN   B 1 20  ? 47.909 -32.007 -12.631 1.00 18.17 ?  20  ASN   B C    1 
ATOM   4189 O  O    . ASN   B 1 20  ? 48.556 -32.084 -13.680 1.00 19.81 ?  20  ASN   B O    1 
ATOM   4190 C  CB   . ASN   B 1 20  ? 46.804 -34.282 -12.862 1.00 19.43 ?  20  ASN   B CB   1 
ATOM   4191 C  CG   . ASN   B 1 20  ? 47.976 -34.971 -12.194 1.00 20.88 ?  20  ASN   B CG   1 
ATOM   4192 O  OD1  . ASN   B 1 20  ? 48.644 -35.812 -12.807 1.00 23.11 ?  20  ASN   B OD1  1 
ATOM   4193 N  ND2  . ASN   B 1 20  ? 48.219 -34.648 -10.932 1.00 20.48 ?  20  ASN   B ND2  1 
ATOM   4194 H  H    . ASN   B 1 20  ? 45.505 -32.564 -14.032 1.00 20.21 ?  20  ASN   B H    1 
ATOM   4195 H  HA   . ASN   B 1 20  ? 46.363 -32.796 -11.506 1.00 21.42 ?  20  ASN   B HA   1 
ATOM   4196 H  HB2  . ASN   B 1 20  ? 46.002 -34.772 -12.626 1.00 23.31 ?  20  ASN   B HB2  1 
ATOM   4197 H  HB3  . ASN   B 1 20  ? 46.943 -34.312 -13.819 1.00 23.31 ?  20  ASN   B HB3  1 
ATOM   4198 H  HD21 . ASN   B 1 20  ? 48.879 -35.005 -10.517 1.00 24.57 ?  20  ASN   B HD21 1 
ATOM   4199 H  HD22 . ASN   B 1 20  ? 47.727 -34.063 -10.530 1.00 24.57 ?  20  ASN   B HD22 1 
ATOM   4200 N  N    . ALA   B 1 21  ? 48.261 -31.194 -11.631 1.00 17.52 ?  21  ALA   B N    1 
ATOM   4201 C  CA   . ALA   B 1 21  ? 49.377 -30.275 -11.783 1.00 18.05 ?  21  ALA   B CA   1 
ATOM   4202 C  C    . ALA   B 1 21  ? 49.829 -29.773 -10.420 1.00 16.99 ?  21  ALA   B C    1 
ATOM   4203 O  O    . ALA   B 1 21  ? 49.080 -29.799 -9.440  1.00 16.86 ?  21  ALA   B O    1 
ATOM   4204 C  CB   . ALA   B 1 21  ? 48.998 -29.099 -12.683 1.00 19.43 ?  21  ALA   B CB   1 
ATOM   4205 H  H    . ALA   B 1 21  ? 47.869 -31.159 -10.862 1.00 21.03 ?  21  ALA   B H    1 
ATOM   4206 H  HA   . ALA   B 1 21  ? 50.119 -30.747 -12.191 1.00 21.66 ?  21  ALA   B HA   1 
ATOM   4207 H  HB1  . ALA   B 1 21  ? 49.784 -28.555 -12.824 1.00 23.32 ?  21  ALA   B HB1  1 
ATOM   4208 H  HB2  . ALA   B 1 21  ? 48.677 -29.449 -13.529 1.00 23.32 ?  21  ALA   B HB2  1 
ATOM   4209 H  HB3  . ALA   B 1 21  ? 48.301 -28.584 -12.251 1.00 23.32 ?  21  ALA   B HB3  1 
ATOM   4210 N  N    . ASP   B 1 22  ? 51.087 -29.327 -10.393 1.00 16.52 ?  22  ASP   B N    1 
ATOM   4211 C  CA   . ASP   B 1 22  ? 51.692 -28.619 -9.270  1.00 15.85 ?  22  ASP   B CA   1 
ATOM   4212 C  C    . ASP   B 1 22  ? 51.279 -27.151 -9.363  1.00 14.46 ?  22  ASP   B C    1 
ATOM   4213 O  O    . ASP   B 1 22  ? 51.580 -26.485 -10.357 1.00 15.03 ?  22  ASP   B O    1 
ATOM   4214 C  CB   . ASP   B 1 22  ? 53.211 -28.793 -9.414  1.00 17.44 ?  22  ASP   B CB   1 
ATOM   4215 C  CG   . ASP   B 1 22  ? 54.031 -28.030 -8.376  1.00 19.11 ?  22  ASP   B CG   1 
ATOM   4216 O  OD1  . ASP   B 1 22  ? 53.660 -26.915 -7.975  1.00 19.20 ?  22  ASP   B OD1  1 
ATOM   4217 O  OD2  . ASP   B 1 22  ? 55.103 -28.540 -7.983  1.00 21.49 -1 22  ASP   B OD2  1 
ATOM   4218 H  H    . ASP   B 1 22  ? 51.634 -29.432 -11.051 1.00 19.83 ?  22  ASP   B H    1 
ATOM   4219 H  HA   . ASP   B 1 22  ? 51.401 -29.000 -8.424  1.00 19.02 ?  22  ASP   B HA   1 
ATOM   4220 H  HB2  . ASP   B 1 22  ? 53.434 -29.734 -9.331  1.00 20.93 ?  22  ASP   B HB2  1 
ATOM   4221 H  HB3  . ASP   B 1 22  ? 53.483 -28.468 -10.286 1.00 20.93 ?  22  ASP   B HB3  1 
ATOM   4222 N  N    . ILE   B 1 23  ? 50.562 -26.656 -8.348  1.00 13.92 ?  23  ILE   B N    1 
ATOM   4223 C  CA   . ILE   B 1 23  ? 49.967 -25.319 -8.425  1.00 13.17 ?  23  ILE   B CA   1 
ATOM   4224 C  C    . ILE   B 1 23  ? 51.019 -24.226 -8.565  1.00 12.96 ?  23  ILE   B C    1 
ATOM   4225 O  O    . ILE   B 1 23  ? 50.750 -23.187 -9.175  1.00 12.81 ?  23  ILE   B O    1 
ATOM   4226 C  CB   . ILE   B 1 23  ? 49.025 -25.070 -7.231  1.00 13.93 ?  23  ILE   B CB   1 
ATOM   4227 C  CG1  . ILE   B 1 23  ? 48.185 -23.807 -7.449  1.00 14.58 ?  23  ILE   B CG1  1 
ATOM   4228 C  CG2  . ILE   B 1 23  ? 49.794 -25.026 -5.927  1.00 15.07 ?  23  ILE   B CG2  1 
ATOM   4229 C  CD1  . ILE   B 1 23  ? 47.070 -23.631 -6.431  1.00 15.20 ?  23  ILE   B CD1  1 
ATOM   4230 H  H    . ILE   B 1 23  ? 50.414 -27.074 -7.612  1.00 16.70 ?  23  ILE   B H    1 
ATOM   4231 H  HA   . ILE   B 1 23  ? 49.427 -25.286 -9.226  1.00 15.81 ?  23  ILE   B HA   1 
ATOM   4232 H  HB   . ILE   B 1 23  ? 48.413 -25.824 -7.188  1.00 16.71 ?  23  ILE   B HB   1 
ATOM   4233 H  HG12 . ILE   B 1 23  ? 48.768 -23.032 -7.389  1.00 17.49 ?  23  ILE   B HG12 1 
ATOM   4234 H  HG13 . ILE   B 1 23  ? 47.782 -23.845 -8.332  1.00 17.49 ?  23  ILE   B HG13 1 
ATOM   4235 H  HG21 . ILE   B 1 23  ? 49.164 -25.021 -5.192  1.00 18.09 ?  23  ILE   B HG21 1 
ATOM   4236 H  HG22 . ILE   B 1 23  ? 50.362 -25.812 -5.870  1.00 18.09 ?  23  ILE   B HG22 1 
ATOM   4237 H  HG23 . ILE   B 1 23  ? 50.337 -24.224 -5.909  1.00 18.09 ?  23  ILE   B HG23 1 
ATOM   4238 H  HD11 . ILE   B 1 23  ? 46.543 -22.854 -6.672  1.00 18.24 ?  23  ILE   B HD11 1 
ATOM   4239 H  HD12 . ILE   B 1 23  ? 46.511 -24.425 -6.438  1.00 18.24 ?  23  ILE   B HD12 1 
ATOM   4240 H  HD13 . ILE   B 1 23  ? 47.460 -23.509 -5.553  1.00 18.24 ?  23  ILE   B HD13 1 
ATOM   4241 N  N    . VAL   B 1 24  ? 52.216 -24.425 -8.004  1.00 13.54 ?  24  VAL   B N    1 
ATOM   4242 C  CA   . VAL   B 1 24  ? 53.295 -23.449 -8.176  1.00 14.05 ?  24  VAL   B CA   1 
ATOM   4243 C  C    . VAL   B 1 24  ? 53.746 -23.407 -9.629  1.00 14.44 ?  24  VAL   B C    1 
ATOM   4244 O  O    . VAL   B 1 24  ? 53.892 -22.330 -10.226 1.00 14.60 ?  24  VAL   B O    1 
ATOM   4245 C  CB   . VAL   B 1 24  ? 54.472 -23.767 -7.232  1.00 14.77 ?  24  VAL   B CB   1 
ATOM   4246 C  CG1  . VAL   B 1 24  ? 55.684 -22.895 -7.569  1.00 15.52 ?  24  VAL   B CG1  1 
ATOM   4247 C  CG2  . VAL   B 1 24  ? 54.064 -23.579 -5.783  1.00 16.03 ?  24  VAL   B CG2  1 
ATOM   4248 H  H    . VAL   B 1 24  ? 52.427 -25.101 -7.519  1.00 16.25 ?  24  VAL   B H    1 
ATOM   4249 H  HA   . VAL   B 1 24  ? 52.968 -22.570 -7.943  1.00 16.86 ?  24  VAL   B HA   1 
ATOM   4250 H  HB   . VAL   B 1 24  ? 54.734 -24.698 -7.347  1.00 17.72 ?  24  VAL   B HB   1 
ATOM   4251 H  HG11 . VAL   B 1 24  ? 56.273 -22.862 -6.798  1.00 18.62 ?  24  VAL   B HG11 1 
ATOM   4252 H  HG12 . VAL   B 1 24  ? 56.152 -23.285 -8.323  1.00 18.62 ?  24  VAL   B HG12 1 
ATOM   4253 H  HG13 . VAL   B 1 24  ? 55.376 -22.003 -7.788  1.00 18.62 ?  24  VAL   B HG13 1 
ATOM   4254 H  HG21 . VAL   B 1 24  ? 54.799 -23.838 -5.206  1.00 19.23 ?  24  VAL   B HG21 1 
ATOM   4255 H  HG22 . VAL   B 1 24  ? 53.841 -22.647 -5.638  1.00 19.23 ?  24  VAL   B HG22 1 
ATOM   4256 H  HG23 . VAL   B 1 24  ? 53.289 -24.136 -5.597  1.00 19.23 ?  24  VAL   B HG23 1 
ATOM   4257 N  N    . GLU   B 1 25  ? 54.005 -24.580 -10.212 1.00 15.28 ?  25  GLU   B N    1 
ATOM   4258 C  CA   . GLU   B 1 25  ? 54.397 -24.621 -11.616 1.00 16.91 ?  25  GLU   B CA   1 
ATOM   4259 C  C    . GLU   B 1 25  ? 53.290 -24.074 -12.503 1.00 15.57 ?  25  GLU   B C    1 
ATOM   4260 O  O    . GLU   B 1 25  ? 53.558 -23.353 -13.473 1.00 16.25 ?  25  GLU   B O    1 
ATOM   4261 C  CB   . GLU   B 1 25  ? 54.783 -26.047 -12.010 1.00 21.31 ?  25  GLU   B CB   1 
ATOM   4262 C  CG   . GLU   B 1 25  ? 56.091 -26.494 -11.374 1.00 26.95 ?  25  GLU   B CG   1 
ATOM   4263 C  CD   . GLU   B 1 25  ? 57.198 -25.451 -11.477 1.00 31.93 ?  25  GLU   B CD   1 
ATOM   4264 O  OE1  . GLU   B 1 25  ? 57.553 -25.063 -12.611 1.00 34.01 ?  25  GLU   B OE1  1 
ATOM   4265 O  OE2  . GLU   B 1 25  ? 57.700 -25.000 -10.421 1.00 33.84 -1 25  GLU   B OE2  1 
ATOM   4266 H  H    . GLU   B 1 25  ? 53.958 -25.349 -9.825  1.00 18.33 ?  25  GLU   B H    1 
ATOM   4267 H  HA   . GLU   B 1 25  ? 55.158 -24.040 -11.742 1.00 20.29 ?  25  GLU   B HA   1 
ATOM   4268 H  HB2  . GLU   B 1 25  ? 54.085 -26.659 -11.716 1.00 25.57 ?  25  GLU   B HB2  1 
ATOM   4269 H  HB3  . GLU   B 1 25  ? 54.880 -26.096 -12.973 1.00 25.57 ?  25  GLU   B HB3  1 
ATOM   4270 H  HG2  . GLU   B 1 25  ? 55.945 -26.665 -10.436 1.00 32.34 ?  25  GLU   B HG2  1 
ATOM   4271 H  HG3  . GLU   B 1 25  ? 56.400 -27.296 -11.823 1.00 32.34 ?  25  GLU   B HG3  1 
ATOM   4272 N  N    . GLU   B 1 26  ? 52.038 -24.387 -12.169 1.00 14.75 ?  26  GLU   B N    1 
ATOM   4273 C  CA   . GLU   B 1 26  ? 50.910 -23.859 -12.927 1.00 15.15 ?  26  GLU   B CA   1 
ATOM   4274 C  C    . GLU   B 1 26  ? 50.865 -22.342 -12.853 1.00 14.41 ?  26  GLU   B C    1 
ATOM   4275 O  O    . GLU   B 1 26  ? 50.668 -21.668 -13.869 1.00 15.45 ?  26  GLU   B O    1 
ATOM   4276 C  CB   . GLU   B 1 26  ? 49.603 -24.439 -12.391 1.00 16.85 ?  26  GLU   B CB   1 
ATOM   4277 C  CG   . GLU   B 1 26  ? 49.180 -25.736 -13.039 1.00 20.14 ?  26  GLU   B CG   1 
ATOM   4278 C  CD   . GLU   B 1 26  ? 48.960 -25.619 -14.539 1.00 21.83 ?  26  GLU   B CD   1 
ATOM   4279 O  OE1  . GLU   B 1 26  ? 48.006 -24.940 -14.977 1.00 22.27 ?  26  GLU   B OE1  1 
ATOM   4280 O  OE2  . GLU   B 1 26  ? 49.745 -26.231 -15.279 1.00 23.78 -1 26  GLU   B OE2  1 
ATOM   4281 H  H    . GLU   B 1 26  ? 51.816 -24.910 -11.516 1.00 17.70 ?  26  GLU   B H    1 
ATOM   4282 H  HA   . GLU   B 1 26  ? 51.003 -24.113 -13.854 1.00 18.18 ?  26  GLU   B HA   1 
ATOM   4283 H  HB2  . GLU   B 1 26  ? 49.701 -24.607 -11.438 1.00 20.22 ?  26  GLU   B HB2  1 
ATOM   4284 H  HB3  . GLU   B 1 26  ? 48.894 -23.791 -12.532 1.00 20.22 ?  26  GLU   B HB3  1 
ATOM   4285 H  HG2  . GLU   B 1 26  ? 49.876 -26.388 -12.905 1.00 24.17 ?  26  GLU   B HG2  1 
ATOM   4286 H  HG3  . GLU   B 1 26  ? 48.350 -26.035 -12.633 1.00 24.17 ?  26  GLU   B HG3  1 
ATOM   4287 N  N    . ALA   B 1 27  ? 51.024 -21.787 -11.651 1.00 13.54 ?  27  ALA   B N    1 
ATOM   4288 C  CA   . ALA   B 1 27  ? 50.979 -20.336 -11.507 1.00 13.90 ?  27  ALA   B CA   1 
ATOM   4289 C  C    . ALA   B 1 27  ? 52.049 -19.668 -12.361 1.00 15.03 ?  27  ALA   B C    1 
ATOM   4290 O  O    . ALA   B 1 27  ? 51.788 -18.655 -13.030 1.00 15.66 ?  27  ALA   B O    1 
ATOM   4291 C  CB   . ALA   B 1 27  ? 51.123 -19.955 -10.033 1.00 14.11 ?  27  ALA   B CB   1 
ATOM   4292 H  H    . ALA   B 1 27  ? 51.150 -22.219 -10.914 1.00 16.25 ?  27  ALA   B H    1 
ATOM   4293 H  HA   . ALA   B 1 27  ? 50.119 -20.015 -11.808 1.00 16.68 ?  27  ALA   B HA   1 
ATOM   4294 H  HB1  . ALA   B 1 27  ? 51.083 -18.987 -9.951  1.00 16.93 ?  27  ALA   B HB1  1 
ATOM   4295 H  HB2  . ALA   B 1 27  ? 50.392 -20.354 -9.531  1.00 16.93 ?  27  ALA   B HB2  1 
ATOM   4296 H  HB3  . ALA   B 1 27  ? 51.970 -20.280 -9.698  1.00 16.93 ?  27  ALA   B HB3  1 
ATOM   4297 N  N    . LYS   B 1 28  ? 53.261 -20.223 -12.360 1.00 16.20 ?  28  LYS   B N    1 
ATOM   4298 C  CA   . LYS   B 1 28  ? 54.339 -19.612 -13.127 1.00 18.32 ?  28  LYS   B CA   1 
ATOM   4299 C  C    . LYS   B 1 28  ? 54.082 -19.692 -14.626 1.00 19.00 ?  28  LYS   B C    1 
ATOM   4300 O  O    . LYS   B 1 28  ? 54.491 -18.793 -15.369 1.00 20.05 ?  28  LYS   B O    1 
ATOM   4301 C  CB   . LYS   B 1 28  ? 55.693 -20.223 -12.739 1.00 21.42 ?  28  LYS   B CB   1 
ATOM   4302 C  CG   . LYS   B 1 28  ? 56.097 -19.883 -11.307 1.00 25.10 ?  28  LYS   B CG   1 
ATOM   4303 C  CD   . LYS   B 1 28  ? 57.513 -20.328 -10.957 1.00 30.08 ?  28  LYS   B CD   1 
ATOM   4304 C  CE   . LYS   B 1 28  ? 57.583 -21.807 -10.651 1.00 34.08 ?  28  LYS   B CE   1 
ATOM   4305 N  NZ   . LYS   B 1 28  ? 58.931 -22.195 -10.142 1.00 35.82 ?  28  LYS   B NZ   1 
ATOM   4306 H  H    . LYS   B 1 28  ? 53.481 -20.934 -11.932 1.00 19.44 ?  28  LYS   B H    1 
ATOM   4307 H  HA   . LYS   B 1 28  ? 54.379 -18.670 -12.904 1.00 21.98 ?  28  LYS   B HA   1 
ATOM   4308 H  HB2  . LYS   B 1 28  ? 55.643 -21.187 -12.813 1.00 25.71 ?  28  LYS   B HB2  1 
ATOM   4309 H  HB3  . LYS   B 1 28  ? 56.382 -19.877 -13.331 1.00 25.71 ?  28  LYS   B HB3  1 
ATOM   4310 H  HG2  . LYS   B 1 28  ? 56.046 -18.920 -11.190 1.00 30.12 ?  28  LYS   B HG2  1 
ATOM   4311 H  HG3  . LYS   B 1 28  ? 55.483 -20.321 -10.698 1.00 30.12 ?  28  LYS   B HG3  1 
ATOM   4312 H  HD2  . LYS   B 1 28  ? 58.097 -20.144 -11.708 1.00 36.10 ?  28  LYS   B HD2  1 
ATOM   4313 H  HD3  . LYS   B 1 28  ? 57.810 -19.840 -10.173 1.00 36.10 ?  28  LYS   B HD3  1 
ATOM   4314 H  HE2  . LYS   B 1 28  ? 56.927 -22.025 -9.971  1.00 40.90 ?  28  LYS   B HE2  1 
ATOM   4315 H  HE3  . LYS   B 1 28  ? 57.407 -22.312 -11.460 1.00 40.90 ?  28  LYS   B HE3  1 
ATOM   4316 H  HZ1  . LYS   B 1 28  ? 58.953 -23.068 -9.967  1.00 42.98 ?  28  LYS   B HZ1  1 
ATOM   4317 H  HZ2  . LYS   B 1 28  ? 59.552 -22.007 -10.751 1.00 42.98 ?  28  LYS   B HZ2  1 
ATOM   4318 H  HZ3  . LYS   B 1 28  ? 59.115 -21.747 -9.394  1.00 42.98 ?  28  LYS   B HZ3  1 
ATOM   4319 N  N    . LYS   B 1 29  ? 53.383 -20.734 -15.083 1.00 20.18 ?  29  LYS   B N    1 
ATOM   4320 C  CA   . LYS   B 1 29  ? 53.089 -20.863 -16.507 1.00 23.07 ?  29  LYS   B CA   1 
ATOM   4321 C  C    . LYS   B 1 29  ? 51.851 -20.067 -16.916 1.00 21.90 ?  29  LYS   B C    1 
ATOM   4322 O  O    . LYS   B 1 29  ? 51.864 -19.392 -17.950 1.00 22.95 ?  29  LYS   B O    1 
ATOM   4323 C  CB   . LYS   B 1 29  ? 52.922 -22.338 -16.875 1.00 27.85 ?  29  LYS   B CB   1 
ATOM   4324 C  CG   . LYS   B 1 29  ? 52.814 -22.594 -18.367 1.00 32.33 ?  29  LYS   B CG   1 
ATOM   4325 C  CD   . LYS   B 1 29  ? 53.104 -24.049 -18.699 1.00 35.79 ?  29  LYS   B CD   1 
ATOM   4326 C  CE   . LYS   B 1 29  ? 52.022 -24.980 -18.175 1.00 38.23 ?  29  LYS   B CE   1 
ATOM   4327 N  NZ   . LYS   B 1 29  ? 52.324 -26.407 -18.484 1.00 39.50 ?  29  LYS   B NZ   1 
ATOM   4328 H  H    . LYS   B 1 29  ? 53.079 -21.376 -14.591 1.00 24.21 ?  29  LYS   B H    1 
ATOM   4329 H  HA   . LYS   B 1 29  ? 53.836 -20.516 -17.008 1.00 27.68 ?  29  LYS   B HA   1 
ATOM   4330 H  HB2  . LYS   B 1 29  ? 53.693 -22.827 -16.548 1.00 33.41 ?  29  LYS   B HB2  1 
ATOM   4331 H  HB3  . LYS   B 1 29  ? 52.116 -22.676 -16.460 1.00 33.41 ?  29  LYS   B HB3  1 
ATOM   4332 H  HG2  . LYS   B 1 29  ? 51.913 -22.389 -18.664 1.00 38.79 ?  29  LYS   B HG2  1 
ATOM   4333 H  HG3  . LYS   B 1 29  ? 53.457 -22.040 -18.837 1.00 38.79 ?  29  LYS   B HG3  1 
ATOM   4334 H  HD2  . LYS   B 1 29  ? 53.154 -24.151 -19.661 1.00 42.95 ?  29  LYS   B HD2  1 
ATOM   4335 H  HD3  . LYS   B 1 29  ? 53.948 -24.304 -18.292 1.00 42.95 ?  29  LYS   B HD3  1 
ATOM   4336 H  HE2  . LYS   B 1 29  ? 51.956 -24.888 -17.211 1.00 45.88 ?  29  LYS   B HE2  1 
ATOM   4337 H  HE3  . LYS   B 1 29  ? 51.175 -24.752 -18.591 1.00 45.88 ?  29  LYS   B HE3  1 
ATOM   4338 H  HZ1  . LYS   B 1 29  ? 51.677 -26.931 -18.168 1.00 47.40 ?  29  LYS   B HZ1  1 
ATOM   4339 H  HZ2  . LYS   B 1 29  ? 52.384 -26.521 -19.365 1.00 47.40 ?  29  LYS   B HZ2  1 
ATOM   4340 H  HZ3  . LYS   B 1 29  ? 53.096 -26.642 -18.108 1.00 47.40 ?  29  LYS   B HZ3  1 
ATOM   4341 N  N    . VAL   B 1 30  ? 50.777 -20.147 -16.122 1.00 20.23 ?  30  VAL   B N    1 
ATOM   4342 C  CA   . VAL   B 1 30  ? 49.489 -19.545 -16.480 1.00 20.17 ?  30  VAL   B CA   1 
ATOM   4343 C  C    . VAL   B 1 30  ? 49.504 -18.031 -16.319 1.00 19.43 ?  30  VAL   B C    1 
ATOM   4344 O  O    . VAL   B 1 30  ? 48.773 -17.312 -17.017 1.00 20.54 ?  30  VAL   B O    1 
ATOM   4345 C  CB   . VAL   B 1 30  ? 48.383 -20.166 -15.601 1.00 20.87 ?  30  VAL   B CB   1 
ATOM   4346 C  CG1  . VAL   B 1 30  ? 47.087 -19.369 -15.700 1.00 21.18 ?  30  VAL   B CG1  1 
ATOM   4347 C  CG2  . VAL   B 1 30  ? 48.156 -21.620 -15.974 1.00 21.72 ?  30  VAL   B CG2  1 
ATOM   4348 H  H    . VAL   B 1 30  ? 50.759 -20.572 -15.366 1.00 24.27 ?  30  VAL   B H    1 
ATOM   4349 H  HA   . VAL   B 1 30  ? 49.285 -19.761 -17.404 1.00 24.21 ?  30  VAL   B HA   1 
ATOM   4350 H  HB   . VAL   B 1 30  ? 48.668 -20.149 -14.674 1.00 25.04 ?  30  VAL   B HB   1 
ATOM   4351 H  HG11 . VAL   B 1 30  ? 46.344 -19.960 -15.496 1.00 25.41 ?  30  VAL   B HG11 1 
ATOM   4352 H  HG12 . VAL   B 1 30  ? 47.109 -18.641 -15.062 1.00 25.41 ?  30  VAL   B HG12 1 
ATOM   4353 H  HG13 . VAL   B 1 30  ? 46.988 -19.032 -16.600 1.00 25.41 ?  30  VAL   B HG13 1 
ATOM   4354 H  HG21 . VAL   B 1 30  ? 47.465 -21.991 -15.399 1.00 26.07 ?  30  VAL   B HG21 1 
ATOM   4355 H  HG22 . VAL   B 1 30  ? 47.871 -21.666 -16.900 1.00 26.07 ?  30  VAL   B HG22 1 
ATOM   4356 H  HG23 . VAL   B 1 30  ? 48.982 -22.109 -15.854 1.00 26.07 ?  30  VAL   B HG23 1 
ATOM   4357 N  N    . LYS   B 1 31  ? 50.276 -17.535 -15.369 1.00 19.25 ?  31  LYS   B N    1 
ATOM   4358 C  CA   . LYS   B 1 31  ? 50.304 -16.127 -15.000 1.00 19.98 ?  31  LYS   B CA   1 
ATOM   4359 C  C    . LYS   B 1 31  ? 48.901 -15.650 -14.626 1.00 17.52 ?  31  LYS   B C    1 
ATOM   4360 O  O    . LYS   B 1 31  ? 48.366 -14.724 -15.251 1.00 18.74 ?  31  LYS   B O    1 
ATOM   4361 C  CB   . LYS   B 1 31  ? 50.944 -15.304 -16.123 1.00 23.67 ?  31  LYS   B CB   1 
ATOM   4362 C  CG   . LYS   B 1 31  ? 52.350 -15.792 -16.481 1.00 27.48 ?  31  LYS   B CG   1 
ATOM   4363 C  CD   . LYS   B 1 31  ? 52.927 -15.052 -17.675 1.00 31.71 ?  31  LYS   B CD   1 
ATOM   4364 C  CE   . LYS   B 1 31  ? 54.390 -15.398 -17.889 1.00 35.02 ?  31  LYS   B CE   1 
ATOM   4365 N  NZ   . LYS   B 1 31  ? 55.187 -15.073 -16.677 1.00 36.52 ?  31  LYS   B NZ   1 
ATOM   4366 H  H    . LYS   B 1 31  ? 50.814 -18.024 -14.914 1.00 23.10 ?  31  LYS   B H    1 
ATOM   4367 H  HA   . LYS   B 1 31  ? 50.852 -16.045 -14.214 1.00 23.98 ?  31  LYS   B HA   1 
ATOM   4368 H  HB2  . LYS   B 1 31  ? 50.395 -15.365 -16.921 1.00 28.41 ?  31  LYS   B HB2  1 
ATOM   4369 H  HB3  . LYS   B 1 31  ? 51.012 -14.383 -15.834 1.00 28.41 ?  31  LYS   B HB3  1 
ATOM   4370 H  HG2  . LYS   B 1 31  ? 52.928 -15.654 -15.715 1.00 32.98 ?  31  LYS   B HG2  1 
ATOM   4371 H  HG3  . LYS   B 1 31  ? 52.310 -16.739 -16.699 1.00 32.98 ?  31  LYS   B HG3  1 
ATOM   4372 H  HD2  . LYS   B 1 31  ? 52.433 -15.302 -18.470 1.00 38.05 ?  31  LYS   B HD2  1 
ATOM   4373 H  HD3  . LYS   B 1 31  ? 52.857 -14.100 -17.518 1.00 38.05 ?  31  LYS   B HD3  1 
ATOM   4374 H  HE2  . LYS   B 1 31  ? 54.480 -16.348 -18.069 1.00 42.03 ?  31  LYS   B HE2  1 
ATOM   4375 H  HE3  . LYS   B 1 31  ? 54.740 -14.881 -18.633 1.00 42.03 ?  31  LYS   B HE3  1 
ATOM   4376 H  HZ1  . LYS   B 1 31  ? 56.055 -15.136 -16.857 1.00 43.82 ?  31  LYS   B HZ1  1 
ATOM   4377 H  HZ2  . LYS   B 1 31  ? 55.005 -14.244 -16.410 1.00 43.82 ?  31  LYS   B HZ2  1 
ATOM   4378 H  HZ3  . LYS   B 1 31  ? 54.985 -15.639 -16.020 1.00 43.82 ?  31  LYS   B HZ3  1 
ATOM   4379 N  N    . PRO   B 1 32  ? 48.285 -16.254 -13.602 1.00 14.83 ?  32  PRO   B N    1 
ATOM   4380 C  CA   . PRO   B 1 32  ? 46.905 -15.899 -13.254 1.00 14.11 ?  32  PRO   B CA   1 
ATOM   4381 C  C    . PRO   B 1 32  ? 46.814 -14.551 -12.554 1.00 14.08 ?  32  PRO   B C    1 
ATOM   4382 O  O    . PRO   B 1 32  ? 47.730 -14.122 -11.847 1.00 15.20 ?  32  PRO   B O    1 
ATOM   4383 C  CB   . PRO   B 1 32  ? 46.498 -17.023 -12.295 1.00 14.37 ?  32  PRO   B CB   1 
ATOM   4384 C  CG   . PRO   B 1 32  ? 47.790 -17.368 -11.609 1.00 14.59 ?  32  PRO   B CG   1 
ATOM   4385 C  CD   . PRO   B 1 32  ? 48.846 -17.251 -12.667 1.00 14.88 ?  32  PRO   B CD   1 
ATOM   4386 H  HA   . PRO   B 1 32  ? 46.331 -15.906 -14.037 1.00 16.94 ?  32  PRO   B HA   1 
ATOM   4387 H  HB2  . PRO   B 1 32  ? 45.840 -16.700 -11.659 1.00 17.24 ?  32  PRO   B HB2  1 
ATOM   4388 H  HB3  . PRO   B 1 32  ? 46.156 -17.780 -12.797 1.00 17.24 ?  32  PRO   B HB3  1 
ATOM   4389 H  HG2  . PRO   B 1 32  ? 47.958 -16.742 -10.886 1.00 17.51 ?  32  PRO   B HG2  1 
ATOM   4390 H  HG3  . PRO   B 1 32  ? 47.750 -18.278 -11.267 1.00 17.51 ?  32  PRO   B HG3  1 
ATOM   4391 H  HD2  . PRO   B 1 32  ? 49.671 -16.923 -12.278 1.00 17.85 ?  32  PRO   B HD2  1 
ATOM   4392 H  HD3  . PRO   B 1 32  ? 48.969 -18.101 -13.109 1.00 17.85 ?  32  PRO   B HD3  1 
ATOM   4393 N  N    . THR   B 1 33  ? 45.662 -13.899 -12.731 1.00 13.58 ?  33  THR   B N    1 
ATOM   4394 C  CA   . THR   B 1 33  ? 45.355 -12.725 -11.924 1.00 13.62 ?  33  THR   B CA   1 
ATOM   4395 C  C    . THR   B 1 33  ? 45.302 -13.078 -10.445 1.00 13.61 ?  33  THR   B C    1 
ATOM   4396 O  O    . THR   B 1 33  ? 45.774 -12.302 -9.599  1.00 14.46 ?  33  THR   B O    1 
ATOM   4397 C  CB   . THR   B 1 33  ? 44.037 -12.098 -12.388 1.00 14.48 ?  33  THR   B CB   1 
ATOM   4398 O  OG1  . THR   B 1 33  ? 44.104 -11.841 -13.793 1.00 14.41 ?  33  THR   B OG1  1 
ATOM   4399 C  CG2  . THR   B 1 33  ? 43.759 -10.803 -11.638 1.00 15.58 ?  33  THR   B CG2  1 
ATOM   4400 H  H    . THR   B 1 33  ? 45.050 -14.116 -13.293 1.00 16.29 ?  33  THR   B H    1 
ATOM   4401 H  HA   . THR   B 1 33  ? 46.049 -12.065 -12.039 1.00 16.35 ?  33  THR   B HA   1 
ATOM   4402 H  HB   . THR   B 1 33  ? 43.301 -12.712 -12.209 1.00 17.37 ?  33  THR   B HB   1 
ATOM   4403 H  HG1  . THR   B 1 33  ? 43.390 -11.483 -14.057 1.00 17.30 ?  33  THR   B HG1  1 
ATOM   4404 H  HG21 . THR   B 1 33  ? 43.006 -10.342 -12.039 1.00 18.70 ?  33  THR   B HG21 1 
ATOM   4405 H  HG22 . THR   B 1 33  ? 43.555 -10.990 -10.709 1.00 18.70 ?  33  THR   B HG22 1 
ATOM   4406 H  HG23 . THR   B 1 33  ? 44.539 -10.227 -11.681 1.00 18.70 ?  33  THR   B HG23 1 
ATOM   4407 N  N    . VAL   B 1 34  ? 44.755 -14.251 -10.111 1.00 12.81 ?  34  VAL   B N    1 
ATOM   4408 C  CA   . VAL   B 1 34  ? 44.565 -14.655 -8.721  1.00 12.18 ?  34  VAL   B CA   1 
ATOM   4409 C  C    . VAL   B 1 34  ? 45.004 -16.103 -8.561  1.00 11.44 ?  34  VAL   B C    1 
ATOM   4410 O  O    . VAL   B 1 34  ? 44.485 -16.992 -9.248  1.00 12.01 ?  34  VAL   B O    1 
ATOM   4411 C  CB   . VAL   B 1 34  ? 43.097 -14.519 -8.268  1.00 13.28 ?  34  VAL   B CB   1 
ATOM   4412 C  CG1  . VAL   B 1 34  ? 42.944 -14.973 -6.821  1.00 13.88 ?  34  VAL   B CG1  1 
ATOM   4413 C  CG2  . VAL   B 1 34  ? 42.588 -13.094 -8.449  1.00 13.95 ?  34  VAL   B CG2  1 
ATOM   4414 H  H    . VAL   B 1 34  ? 44.483 -14.841 -10.679 1.00 15.37 ?  34  VAL   B H    1 
ATOM   4415 H  HA   . VAL   B 1 34  ? 45.112 -14.099 -8.141  1.00 14.62 ?  34  VAL   B HA   1 
ATOM   4416 H  HB   . VAL   B 1 34  ? 42.546 -15.102 -8.814  1.00 15.94 ?  34  VAL   B HB   1 
ATOM   4417 H  HG11 . VAL   B 1 34  ? 42.087 -14.668 -6.480  1.00 16.66 ?  34  VAL   B HG11 1 
ATOM   4418 H  HG12 . VAL   B 1 34  ? 42.983 -15.943 -6.780  1.00 16.66 ?  34  VAL   B HG12 1 
ATOM   4419 H  HG13 . VAL   B 1 34  ? 43.661 -14.592 -6.290  1.00 16.66 ?  34  VAL   B HG13 1 
ATOM   4420 H  HG21 . VAL   B 1 34  ? 41.673 -13.041 -8.128  1.00 16.74 ?  34  VAL   B HG21 1 
ATOM   4421 H  HG22 . VAL   B 1 34  ? 43.153 -12.491 -7.942  1.00 16.74 ?  34  VAL   B HG22 1 
ATOM   4422 H  HG23 . VAL   B 1 34  ? 42.620 -12.868 -9.391  1.00 16.74 ?  34  VAL   B HG23 1 
ATOM   4423 N  N    . VAL   B 1 35  ? 45.925 -16.348 -7.631  1.00 10.84 ?  35  VAL   B N    1 
ATOM   4424 C  CA   . VAL   B 1 35  ? 46.161 -17.688 -7.102  1.00 10.66 ?  35  VAL   B CA   1 
ATOM   4425 C  C    . VAL   B 1 35  ? 45.620 -17.741 -5.682  1.00 10.54 ?  35  VAL   B C    1 
ATOM   4426 O  O    . VAL   B 1 35  ? 45.830 -16.811 -4.893  1.00 10.95 ?  35  VAL   B O    1 
ATOM   4427 C  CB   . VAL   B 1 35  ? 47.642 -18.110 -7.184  1.00 11.63 ?  35  VAL   B CB   1 
ATOM   4428 C  CG1  . VAL   B 1 35  ? 48.536 -17.264 -6.269  1.00 11.96 ?  35  VAL   B CG1  1 
ATOM   4429 C  CG2  . VAL   B 1 35  ? 47.785 -19.607 -6.856  1.00 11.89 ?  35  VAL   B CG2  1 
ATOM   4430 H  H    . VAL   B 1 35  ? 46.438 -15.747 -7.289  1.00 13.01 ?  35  VAL   B H    1 
ATOM   4431 H  HA   . VAL   B 1 35  ? 45.643 -18.320 -7.631  1.00 12.79 ?  35  VAL   B HA   1 
ATOM   4432 H  HB   . VAL   B 1 35  ? 47.947 -17.990 -8.097  1.00 13.96 ?  35  VAL   B HB   1 
ATOM   4433 H  HG11 . VAL   B 1 35  ? 49.460 -17.492 -6.442  1.00 14.35 ?  35  VAL   B HG11 1 
ATOM   4434 H  HG12 . VAL   B 1 35  ? 48.374 -16.332 -6.456  1.00 14.35 ?  35  VAL   B HG12 1 
ATOM   4435 H  HG13 . VAL   B 1 35  ? 48.311 -17.466 -5.345  1.00 14.35 ?  35  VAL   B HG13 1 
ATOM   4436 H  HG21 . VAL   B 1 35  ? 48.709 -19.873 -6.961  1.00 14.27 ?  35  VAL   B HG21 1 
ATOM   4437 H  HG22 . VAL   B 1 35  ? 47.497 -19.763 -5.939  1.00 14.27 ?  35  VAL   B HG22 1 
ATOM   4438 H  HG23 . VAL   B 1 35  ? 47.223 -20.126 -7.462  1.00 14.27 ?  35  VAL   B HG23 1 
ATOM   4439 N  N    . VAL   B 1 36  ? 44.896 -18.819 -5.365  1.00 10.57 ?  36  VAL   B N    1 
ATOM   4440 C  CA   . VAL   B 1 36  ? 44.345 -19.020 -4.034  1.00 10.22 ?  36  VAL   B CA   1 
ATOM   4441 C  C    . VAL   B 1 36  ? 45.354 -19.782 -3.184  1.00 10.13 ?  36  VAL   B C    1 
ATOM   4442 O  O    . VAL   B 1 36  ? 45.893 -20.817 -3.608  1.00 11.07 ?  36  VAL   B O    1 
ATOM   4443 C  CB   . VAL   B 1 36  ? 43.012 -19.781 -4.110  1.00 10.48 ?  36  VAL   B CB   1 
ATOM   4444 C  CG1  . VAL   B 1 36  ? 42.514 -20.132 -2.720  1.00 11.36 ?  36  VAL   B CG1  1 
ATOM   4445 C  CG2  . VAL   B 1 36  ? 41.985 -18.957 -4.859  1.00 11.18 ?  36  VAL   B CG2  1 
ATOM   4446 H  H    . VAL   B 1 36  ? 44.717 -19.460 -5.913  1.00 12.68 ?  36  VAL   B H    1 
ATOM   4447 H  HA   . VAL   B 1 36  ? 44.180 -18.160 -3.619  1.00 12.27 ?  36  VAL   B HA   1 
ATOM   4448 H  HB   . VAL   B 1 36  ? 43.145 -20.608 -4.596  1.00 12.57 ?  36  VAL   B HB   1 
ATOM   4449 H  HG11 . VAL   B 1 36  ? 41.573 -20.350 -2.771  1.00 13.63 ?  36  VAL   B HG11 1 
ATOM   4450 H  HG12 . VAL   B 1 36  ? 43.017 -20.885 -2.385  1.00 13.63 ?  36  VAL   B HG12 1 
ATOM   4451 H  HG13 . VAL   B 1 36  ? 42.642 -19.359 -2.142  1.00 13.63 ?  36  VAL   B HG13 1 
ATOM   4452 H  HG21 . VAL   B 1 36  ? 41.145 -19.439 -4.878  1.00 13.41 ?  36  VAL   B HG21 1 
ATOM   4453 H  HG22 . VAL   B 1 36  ? 41.873 -18.107 -4.408  1.00 13.41 ?  36  VAL   B HG22 1 
ATOM   4454 H  HG23 . VAL   B 1 36  ? 42.302 -18.810 -5.766  1.00 13.41 ?  36  VAL   B HG23 1 
ATOM   4455 N  N    . ASN   B 1 37  ? 45.574 -19.290 -1.967  1.00 10.31 ?  37  ASN   B N    1 
ATOM   4456 C  CA   . ASN   B 1 37  ? 46.328 -20.012 -0.957  1.00 10.65 ?  37  ASN   B CA   1 
ATOM   4457 C  C    . ASN   B 1 37  ? 45.381 -20.685 0.028   1.00 10.72 ?  37  ASN   B C    1 
ATOM   4458 O  O    . ASN   B 1 37  ? 44.370 -20.107 0.440   1.00 11.20 ?  37  ASN   B O    1 
ATOM   4459 C  CB   . ASN   B 1 37  ? 47.252 -19.062 -0.194  1.00 10.64 ?  37  ASN   B CB   1 
ATOM   4460 C  CG   . ASN   B 1 37  ? 48.109 -19.782 0.815   1.00 11.26 ?  37  ASN   B CG   1 
ATOM   4461 O  OD1  . ASN   B 1 37  ? 48.449 -20.957 0.637   1.00 11.68 ?  37  ASN   B OD1  1 
ATOM   4462 N  ND2  . ASN   B 1 37  ? 48.464 -19.083 1.889   1.00 11.28 ?  37  ASN   B ND2  1 
ATOM   4463 H  H    . ASN   B 1 37  ? 45.288 -18.523 -1.692  1.00 12.38 ?  37  ASN   B H    1 
ATOM   4464 H  HA   . ASN   B 1 37  ? 46.868 -20.699 -1.374  1.00 12.78 ?  37  ASN   B HA   1 
ATOM   4465 H  HB2  . ASN   B 1 37  ? 47.842 -18.625 -0.823  1.00 12.76 ?  37  ASN   B HB2  1 
ATOM   4466 H  HB3  . ASN   B 1 37  ? 46.718 -18.406 0.280   1.00 12.76 ?  37  ASN   B HB3  1 
ATOM   4467 H  HD21 . ASN   B 1 37  ? 48.957 -19.445 2.493   1.00 13.54 ?  37  ASN   B HD21 1 
ATOM   4468 H  HD22 . ASN   B 1 37  ? 48.211 -18.271 1.978   1.00 13.54 ?  37  ASN   B HD22 1 
ATOM   4469 N  N    . ALA   B 1 38  ? 45.733 -21.917 0.404   1.00 10.83 ?  38  ALA   B N    1 
ATOM   4470 C  CA   . ALA   B 1 38  ? 45.075 -22.669 1.476   1.00 11.40 ?  38  ALA   B CA   1 
ATOM   4471 C  C    . ALA   B 1 38  ? 45.654 -22.182 2.804   1.00 11.17 ?  38  ALA   B C    1 
ATOM   4472 O  O    . ALA   B 1 38  ? 46.555 -22.787 3.394   1.00 12.20 ?  38  ALA   B O    1 
ATOM   4473 C  CB   . ALA   B 1 38  ? 45.303 -24.163 1.282   1.00 12.41 ?  38  ALA   B CB   1 
ATOM   4474 H  H    . ALA   B 1 38  ? 46.385 -22.350 0.053   1.00 13.00 ?  38  ALA   B H    1 
ATOM   4475 H  HA   . ALA   B 1 38  ? 44.119 -22.492 1.466   1.00 13.67 ?  38  ALA   B HA   1 
ATOM   4476 H  HB1  . ALA   B 1 38  ? 44.852 -24.649 1.998   1.00 14.89 ?  38  ALA   B HB1  1 
ATOM   4477 H  HB2  . ALA   B 1 38  ? 44.929 -24.432 0.426   1.00 14.89 ?  38  ALA   B HB2  1 
ATOM   4478 H  HB3  . ALA   B 1 38  ? 46.250 -24.348 1.304   1.00 14.89 ?  38  ALA   B HB3  1 
ATOM   4479 N  N    . ALA   B 1 39  ? 45.138 -21.040 3.261   1.00 11.06 ?  39  ALA   B N    1 
ATOM   4480 C  CA   . ALA   B 1 39  ? 45.689 -20.305 4.389   1.00 11.37 ?  39  ALA   B CA   1 
ATOM   4481 C  C    . ALA   B 1 39  ? 45.067 -20.744 5.714   1.00 11.41 ?  39  ALA   B C    1 
ATOM   4482 O  O    . ALA   B 1 39  ? 44.035 -21.414 5.761   1.00 12.41 ?  39  ALA   B O    1 
ATOM   4483 C  CB   . ALA   B 1 39  ? 45.464 -18.804 4.186   1.00 12.05 ?  39  ALA   B CB   1 
ATOM   4484 H  H    . ALA   B 1 39  ? 44.450 -20.662 2.913   1.00 13.27 ?  39  ALA   B H    1 
ATOM   4485 H  HA   . ALA   B 1 39  ? 46.641 -20.466 4.438   1.00 13.65 ?  39  ALA   B HA   1 
ATOM   4486 H  HB1  . ALA   B 1 39  ? 45.836 -18.328 4.944   1.00 14.46 ?  39  ALA   B HB1  1 
ATOM   4487 H  HB2  . ALA   B 1 39  ? 45.915 -18.529 3.370   1.00 14.46 ?  39  ALA   B HB2  1 
ATOM   4488 H  HB3  . ALA   B 1 39  ? 44.515 -18.633 4.115   1.00 14.46 ?  39  ALA   B HB3  1 
ATOM   4489 N  N    . ASN   B 1 40  ? 45.703 -20.319 6.804   1.00 12.28 ?  40  ASN   B N    1 
ATOM   4490 C  CA   . ASN   B 1 40  ? 45.136 -20.372 8.143   1.00 13.03 ?  40  ASN   B CA   1 
ATOM   4491 C  C    . ASN   B 1 40  ? 44.963 -18.948 8.669   1.00 12.53 ?  40  ASN   B C    1 
ATOM   4492 O  O    . ASN   B 1 40  ? 45.377 -17.969 8.036   1.00 12.55 ?  40  ASN   B O    1 
ATOM   4493 C  CB   . ASN   B 1 40  ? 45.984 -21.249 9.081   1.00 13.71 ?  40  ASN   B CB   1 
ATOM   4494 C  CG   . ASN   B 1 40  ? 47.443 -20.843 9.112   1.00 14.85 ?  40  ASN   B CG   1 
ATOM   4495 O  OD1  . ASN   B 1 40  ? 47.764 -19.662 9.173   1.00 16.70 ?  40  ASN   B OD1  1 
ATOM   4496 N  ND2  . ASN   B 1 40  ? 48.335 -21.820 9.080   1.00 14.75 ?  40  ASN   B ND2  1 
ATOM   4497 H  H    . ASN   B 1 40  ? 46.492 -19.985 6.784   1.00 14.74 ?  40  ASN   B H    1 
ATOM   4498 H  HA   . ASN   B 1 40  ? 44.251 -20.766 8.091   1.00 15.64 ?  40  ASN   B HA   1 
ATOM   4499 H  HB2  . ASN   B 1 40  ? 45.630 -21.175 9.981   1.00 16.46 ?  40  ASN   B HB2  1 
ATOM   4500 H  HB3  . ASN   B 1 40  ? 45.934 -22.167 8.778   1.00 16.46 ?  40  ASN   B HB3  1 
ATOM   4501 H  HD21 . ASN   B 1 40  ? 49.174 -21.635 9.098   1.00 17.70 ?  40  ASN   B HD21 1 
ATOM   4502 H  HD22 . ASN   B 1 40  ? 48.073 -22.636 9.040   1.00 17.70 ?  40  ASN   B HD22 1 
ATOM   4503 N  N    . VAL   B 1 41  ? 44.312 -18.824 9.829   1.00 13.10 ?  41  VAL   B N    1 
ATOM   4504 C  CA   . VAL   B 1 41  ? 43.853 -17.504 10.270  1.00 13.41 ?  41  VAL   B CA   1 
ATOM   4505 C  C    . VAL   B 1 41  ? 45.007 -16.554 10.570  1.00 13.50 ?  41  VAL   B C    1 
ATOM   4506 O  O    . VAL   B 1 41  ? 44.830 -15.334 10.490  1.00 13.83 ?  41  VAL   B O    1 
ATOM   4507 C  CB   . VAL   B 1 41  ? 42.865 -17.568 11.453  1.00 14.97 ?  41  VAL   B CB   1 
ATOM   4508 C  CG1  . VAL   B 1 41  ? 41.562 -18.248 11.043  1.00 15.53 ?  41  VAL   B CG1  1 
ATOM   4509 C  CG2  . VAL   B 1 41  ? 43.500 -18.252 12.653  1.00 16.11 ?  41  VAL   B CG2  1 
ATOM   4510 H  H    . VAL   B 1 41  ? 44.125 -19.468 10.360  1.00 15.72 ?  41  VAL   B H    1 
ATOM   4511 H  HA   . VAL   B 1 41  ? 43.364 -17.105 9.538   1.00 16.09 ?  41  VAL   B HA   1 
ATOM   4512 H  HB   . VAL   B 1 41  ? 42.644 -16.660 11.723  1.00 17.96 ?  41  VAL   B HB   1 
ATOM   4513 H  HG11 . VAL   B 1 41  ? 40.954 -18.247 11.799  1.00 18.63 ?  41  VAL   B HG11 1 
ATOM   4514 H  HG12 . VAL   B 1 41  ? 41.172 -17.758 10.303  1.00 18.63 ?  41  VAL   B HG12 1 
ATOM   4515 H  HG13 . VAL   B 1 41  ? 41.757 -19.158 10.774  1.00 18.63 ?  41  VAL   B HG13 1 
ATOM   4516 H  HG21 . VAL   B 1 41  ? 42.856 -18.283 13.377  1.00 19.34 ?  41  VAL   B HG21 1 
ATOM   4517 H  HG22 . VAL   B 1 41  ? 43.758 -19.153 12.401  1.00 19.34 ?  41  VAL   B HG22 1 
ATOM   4518 H  HG23 . VAL   B 1 41  ? 44.282 -17.748 12.927  1.00 19.34 ?  41  VAL   B HG23 1 
ATOM   4519 N  N    . TYR   B 1 42  ? 46.174 -17.070 10.959  1.00 13.84 ?  42  TYR   B N    1 
ATOM   4520 C  CA   . TYR   B 1 42  ? 47.333 -16.226 11.228  1.00 14.29 ?  42  TYR   B CA   1 
ATOM   4521 C  C    . TYR   B 1 42  ? 48.297 -16.150 10.046  1.00 13.63 ?  42  TYR   B C    1 
ATOM   4522 O  O    . TYR   B 1 42  ? 49.385 -15.581 10.181  1.00 14.77 ?  42  TYR   B O    1 
ATOM   4523 C  CB   . TYR   B 1 42  ? 48.031 -16.633 12.534  1.00 16.23 ?  42  TYR   B CB   1 
ATOM   4524 C  CG   . TYR   B 1 42  ? 47.420 -15.957 13.761  1.00 16.93 ?  42  TYR   B CG   1 
ATOM   4525 C  CD1  . TYR   B 1 42  ? 47.634 -14.604 14.003  1.00 16.25 ?  42  TYR   B CD1  1 
ATOM   4526 C  CD2  . TYR   B 1 42  ? 46.628 -16.659 14.656  1.00 18.85 ?  42  TYR   B CD2  1 
ATOM   4527 C  CE1  . TYR   B 1 42  ? 47.082 -13.970 15.103  1.00 17.50 ?  42  TYR   B CE1  1 
ATOM   4528 C  CE2  . TYR   B 1 42  ? 46.074 -16.033 15.766  1.00 19.33 ?  42  TYR   B CE2  1 
ATOM   4529 C  CZ   . TYR   B 1 42  ? 46.302 -14.686 15.982  1.00 19.55 ?  42  TYR   B CZ   1 
ATOM   4530 O  OH   . TYR   B 1 42  ? 45.760 -14.046 17.079  1.00 21.94 ?  42  TYR   B OH   1 
ATOM   4531 H  H    . TYR   B 1 42  ? 46.316 -17.913 11.067  1.00 16.60 ?  42  TYR   B H    1 
ATOM   4532 H  HA   . TYR   B 1 42  ? 47.009 -15.327 11.365  1.00 17.15 ?  42  TYR   B HA   1 
ATOM   4533 H  HB2  . TYR   B 1 42  ? 47.956 -17.592 12.651  1.00 19.48 ?  42  TYR   B HB2  1 
ATOM   4534 H  HB3  . TYR   B 1 42  ? 48.966 -16.376 12.485  1.00 19.48 ?  42  TYR   B HB3  1 
ATOM   4535 H  HD1  . TYR   B 1 42  ? 48.162 -14.116 13.407  1.00 19.50 ?  42  TYR   B HD1  1 
ATOM   4536 H  HD2  . TYR   B 1 42  ? 46.469 -17.566 14.511  1.00 22.62 ?  42  TYR   B HD2  1 
ATOM   4537 H  HE1  . TYR   B 1 42  ? 47.242 -13.066 15.243  1.00 21.00 ?  42  TYR   B HE1  1 
ATOM   4538 H  HE2  . TYR   B 1 42  ? 45.543 -16.517 16.356  1.00 23.19 ?  42  TYR   B HE2  1 
ATOM   4539 H  HH   . TYR   B 1 42  ? 45.985 -13.238 17.073  1.00 26.33 ?  42  TYR   B HH   1 
ATOM   4540 N  N    . LEU   B 1 43  ? 47.897 -16.660 8.883   1.00 12.77 ?  43  LEU   B N    1 
ATOM   4541 C  CA   . LEU   B 1 43  ? 48.708 -16.586 7.672   1.00 12.39 ?  43  LEU   B CA   1 
ATOM   4542 C  C    . LEU   B 1 43  ? 50.121 -17.098 7.929   1.00 12.66 ?  43  LEU   B C    1 
ATOM   4543 O  O    . LEU   B 1 43  ? 51.107 -16.507 7.487   1.00 13.45 ?  43  LEU   B O    1 
ATOM   4544 C  CB   . LEU   B 1 43  ? 48.722 -15.183 7.060   1.00 12.64 ?  43  LEU   B CB   1 
ATOM   4545 C  CG   . LEU   B 1 43  ? 47.371 -14.569 6.682   1.00 12.92 ?  43  LEU   B CG   1 
ATOM   4546 C  CD1  . LEU   B 1 43  ? 47.594 -13.176 6.095   1.00 13.77 ?  43  LEU   B CD1  1 
ATOM   4547 C  CD2  . LEU   B 1 43  ? 46.602 -15.453 5.706   1.00 13.24 ?  43  LEU   B CD2  1 
ATOM   4548 H  H    . LEU   B 1 43  ? 47.151 -17.072 8.766   1.00 15.32 ?  43  LEU   B H    1 
ATOM   4549 H  HA   . LEU   B 1 43  ? 48.309 -17.176 7.009   1.00 14.87 ?  43  LEU   B HA   1 
ATOM   4550 H  HB2  . LEU   B 1 43  ? 49.143 -14.584 7.692   1.00 15.17 ?  43  LEU   B HB2  1 
ATOM   4551 H  HB3  . LEU   B 1 43  ? 49.253 -15.217 6.248   1.00 15.17 ?  43  LEU   B HB3  1 
ATOM   4552 H  HG   . LEU   B 1 43  ? 46.834 -14.467 7.482   1.00 15.50 ?  43  LEU   B HG   1 
ATOM   4553 H  HD11 . LEU   B 1 43  ? 46.737 -12.787 5.858   1.00 16.53 ?  43  LEU   B HD11 1 
ATOM   4554 H  HD12 . LEU   B 1 43  ? 48.036 -12.618 6.757   1.00 16.53 ?  43  LEU   B HD12 1 
ATOM   4555 H  HD13 . LEU   B 1 43  ? 48.152 -13.249 5.304   1.00 16.53 ?  43  LEU   B HD13 1 
ATOM   4556 H  HD21 . LEU   B 1 43  ? 45.796 -14.988 5.425   1.00 15.89 ?  43  LEU   B HD21 1 
ATOM   4557 H  HD22 . LEU   B 1 43  ? 47.161 -15.636 4.937   1.00 15.89 ?  43  LEU   B HD22 1 
ATOM   4558 H  HD23 . LEU   B 1 43  ? 46.366 -16.281 6.151   1.00 15.89 ?  43  LEU   B HD23 1 
ATOM   4559 N  N    . LYS   B 1 44  ? 50.214 -18.224 8.641   1.00 12.67 ?  44  LYS   B N    1 
ATOM   4560 C  CA   . LYS   B 1 44  ? 51.477 -18.903 8.890   1.00 13.34 ?  44  LYS   B CA   1 
ATOM   4561 C  C    . LYS   B 1 44  ? 51.596 -20.019 7.862   1.00 12.94 ?  44  LYS   B C    1 
ATOM   4562 O  O    . LYS   B 1 44  ? 50.903 -21.036 7.951   1.00 14.15 ?  44  LYS   B O    1 
ATOM   4563 C  CB   . LYS   B 1 44  ? 51.534 -19.416 10.328  1.00 15.23 ?  44  LYS   B CB   1 
ATOM   4564 C  CG   . LYS   B 1 44  ? 51.738 -18.308 11.354  1.00 18.19 ?  44  LYS   B CG   1 
ATOM   4565 C  CD   . LYS   B 1 44  ? 52.944 -17.452 10.963  1.00 21.10 ?  44  LYS   B CD   1 
ATOM   4566 C  CE   . LYS   B 1 44  ? 53.438 -16.576 12.089  1.00 24.01 ?  44  LYS   B CE   1 
ATOM   4567 N  NZ   . LYS   B 1 44  ? 54.621 -15.768 11.702  1.00 25.06 ?  44  LYS   B NZ   1 
ATOM   4568 H  H    . LYS   B 1 44  ? 49.538 -18.617 8.997   1.00 15.20 ?  44  LYS   B H    1 
ATOM   4569 H  HA   . LYS   B 1 44  ? 52.210 -18.291 8.730   1.00 16.01 ?  44  LYS   B HA   1 
ATOM   4570 H  HB2  . LYS   B 1 44  ? 50.694 -19.860 10.540  1.00 18.27 ?  44  LYS   B HB2  1 
ATOM   4571 H  HB3  . LYS   B 1 44  ? 52.268 -20.041 10.417  1.00 18.27 ?  44  LYS   B HB3  1 
ATOM   4572 H  HG2  . LYS   B 1 44  ? 50.951 -17.744 11.387  1.00 21.83 ?  44  LYS   B HG2  1 
ATOM   4573 H  HG3  . LYS   B 1 44  ? 51.910 -18.703 12.228  1.00 21.83 ?  44  LYS   B HG3  1 
ATOM   4574 H  HD2  . LYS   B 1 44  ? 53.666 -18.041 10.681  1.00 25.32 ?  44  LYS   B HD2  1 
ATOM   4575 H  HD3  . LYS   B 1 44  ? 52.687 -16.871 10.230  1.00 25.32 ?  44  LYS   B HD3  1 
ATOM   4576 H  HE2  . LYS   B 1 44  ? 52.736 -15.957 12.317  1.00 28.81 ?  44  LYS   B HE2  1 
ATOM   4577 H  HE3  . LYS   B 1 44  ? 53.672 -17.131 12.849  1.00 28.81 ?  44  LYS   B HE3  1 
ATOM   4578 H  HZ1  . LYS   B 1 44  ? 54.878 -15.262 12.388  1.00 30.07 ?  44  LYS   B HZ1  1 
ATOM   4579 H  HZ2  . LYS   B 1 44  ? 55.294 -16.299 11.465  1.00 30.07 ?  44  LYS   B HZ2  1 
ATOM   4580 H  HZ3  . LYS   B 1 44  ? 54.417 -15.238 11.015  1.00 30.07 ?  44  LYS   B HZ3  1 
ATOM   4581 N  N    . HIS   B 1 45  ? 52.450 -19.804 6.864   1.00 12.73 ?  45  HIS   B N    1 
ATOM   4582 C  CA   . HIS   B 1 45  ? 52.478 -20.637 5.660   1.00 12.80 ?  45  HIS   B CA   1 
ATOM   4583 C  C    . HIS   B 1 45  ? 53.498 -21.759 5.825   1.00 14.69 ?  45  HIS   B C    1 
ATOM   4584 O  O    . HIS   B 1 45  ? 54.557 -21.780 5.206   1.00 16.81 ?  45  HIS   B O    1 
ATOM   4585 C  CB   . HIS   B 1 45  ? 52.796 -19.779 4.447   1.00 12.89 ?  45  HIS   B CB   1 
ATOM   4586 C  CG   . HIS   B 1 45  ? 51.927 -18.575 4.337   1.00 12.75 ?  45  HIS   B CG   1 
ATOM   4587 N  ND1  . HIS   B 1 45  ? 50.551 -18.654 4.286   1.00 12.61 ?  45  HIS   B ND1  1 
ATOM   4588 C  CD2  . HIS   B 1 45  ? 52.243 -17.261 4.283   1.00 13.26 ?  45  HIS   B CD2  1 
ATOM   4589 C  CE1  . HIS   B 1 45  ? 50.061 -17.430 4.194   1.00 12.43 ?  45  HIS   B CE1  1 
ATOM   4590 N  NE2  . HIS   B 1 45  ? 51.064 -16.567 4.185   1.00 12.93 ?  45  HIS   B NE2  1 
ATOM   4591 H  H    . HIS   B 1 45  ? 53.023 -19.163 6.852   1.00 15.27 ?  45  HIS   B H    1 
ATOM   4592 H  HA   . HIS   B 1 45  ? 51.596 -21.031 5.528   1.00 15.36 ?  45  HIS   B HA   1 
ATOM   4593 H  HB2  . HIS   B 1 45  ? 53.713 -19.480 4.509   1.00 15.47 ?  45  HIS   B HB2  1 
ATOM   4594 H  HB3  . HIS   B 1 45  ? 52.673 -20.314 3.645   1.00 15.47 ?  45  HIS   B HB3  1 
ATOM   4595 H  HD2  . HIS   B 1 45  ? 53.097 -16.897 4.306   1.00 15.91 ?  45  HIS   B HD2  1 
ATOM   4596 H  HE1  . HIS   B 1 45  ? 49.158 -17.213 4.130   1.00 14.92 ?  45  HIS   B HE1  1 
ATOM   4597 H  HE2  . HIS   B 1 45  ? 50.985 -15.712 4.141   1.00 15.52 ?  45  HIS   B HE2  1 
ATOM   4598 N  N    A GLY   B 1 46  ? 53.133 -22.725 6.663   0.56 15.85 ?  46  GLY   B N    1 
ATOM   4599 N  N    B GLY   B 1 46  ? 53.145 -22.709 6.682   0.44 15.66 ?  46  GLY   B N    1 
ATOM   4600 C  CA   A GLY   B 1 46  ? 54.057 -23.774 7.051   0.56 17.47 ?  46  GLY   B CA   1 
ATOM   4601 C  CA   B GLY   B 1 46  ? 54.065 -23.773 7.021   0.44 17.01 ?  46  GLY   B CA   1 
ATOM   4602 C  C    A GLY   B 1 46  ? 54.116 -24.995 6.155   0.56 18.77 ?  46  GLY   B C    1 
ATOM   4603 C  C    B GLY   B 1 46  ? 54.100 -24.909 6.020   0.44 18.22 ?  46  GLY   B C    1 
ATOM   4604 O  O    A GLY   B 1 46  ? 55.204 -25.437 5.773   0.56 21.09 ?  46  GLY   B O    1 
ATOM   4605 O  O    B GLY   B 1 46  ? 55.135 -25.177 5.401   0.44 19.54 ?  46  GLY   B O    1 
ATOM   4606 H  H    A GLY   B 1 46  ? 52.354 -22.781 7.031   0.56 19.02 ?  46  GLY   B H    1 
ATOM   4607 H  H    B GLY   B 1 46  ? 52.379 -22.750 7.080   0.44 18.80 ?  46  GLY   B H    1 
ATOM   4608 H  HA2  A GLY   B 1 46  ? 54.946 -23.394 7.099   0.56 20.96 ?  46  GLY   B HA2  1 
ATOM   4609 H  HA2  B GLY   B 1 46  ? 54.956 -23.400 7.088   0.44 20.41 ?  46  GLY   B HA2  1 
ATOM   4610 H  HA3  A GLY   B 1 46  ? 53.814 -24.084 7.935   0.56 20.96 ?  46  GLY   B HA3  1 
ATOM   4611 H  HA3  B GLY   B 1 46  ? 53.819 -24.129 7.888   0.44 20.41 ?  46  GLY   B HA3  1 
ATOM   4612 N  N    . GLY   B 1 47  ? 52.961 -25.573 5.830   1.00 18.20 ?  47  GLY   B N    1 
ATOM   4613 C  CA   . GLY   B 1 47  ? 52.910 -26.841 5.133   1.00 16.43 ?  47  GLY   B CA   1 
ATOM   4614 C  C    . GLY   B 1 47  ? 51.991 -26.823 3.929   1.00 14.08 ?  47  GLY   B C    1 
ATOM   4615 O  O    . GLY   B 1 47  ? 51.334 -25.825 3.635   1.00 14.10 ?  47  GLY   B O    1 
ATOM   4616 H  H    A GLY   B 1 47  ? 52.186 -25.254 6.028   0.56 21.84 ?  47  GLY   B H    1 
ATOM   4617 H  H    B GLY   B 1 47  ? 52.191 -25.295 6.100   0.44 21.84 ?  47  GLY   B H    1 
ATOM   4618 H  HA2  . GLY   B 1 47  ? 53.798 -27.086 4.831   1.00 19.72 ?  47  GLY   B HA2  1 
ATOM   4619 H  HA3  . GLY   B 1 47  ? 52.600 -27.528 5.746   1.00 19.72 ?  47  GLY   B HA3  1 
ATOM   4620 N  N    . GLY   B 1 48  ? 51.951 -27.962 3.242   1.00 13.40 ?  48  GLY   B N    1 
ATOM   4621 C  CA   . GLY   B 1 48  ? 51.030 -28.109 2.132   1.00 12.97 ?  48  GLY   B CA   1 
ATOM   4622 C  C    . GLY   B 1 48  ? 51.167 -26.999 1.118   1.00 12.58 ?  48  GLY   B C    1 
ATOM   4623 O  O    . GLY   B 1 48  ? 52.265 -26.531 0.811   1.00 13.18 ?  48  GLY   B O    1 
ATOM   4624 H  H    . GLY   B 1 48  ? 52.447 -28.644 3.391   1.00 16.08 ?  48  GLY   B H    1 
ATOM   4625 H  HA2  . GLY   B 1 48  ? 51.194 -28.957 1.687   1.00 15.57 ?  48  GLY   B HA2  1 
ATOM   4626 H  HA3  . GLY   B 1 48  ? 50.119 -28.107 2.463   1.00 15.57 ?  48  GLY   B HA3  1 
ATOM   4627 N  N    . VAL   B 1 49  ? 50.021 -26.577 0.580   1.00 12.45 ?  49  VAL   B N    1 
ATOM   4628 C  CA   . VAL   B 1 49  ? 49.996 -25.552 -0.460  1.00 12.65 ?  49  VAL   B CA   1 
ATOM   4629 C  C    . VAL   B 1 49  ? 50.653 -24.266 0.026   1.00 11.86 ?  49  VAL   B C    1 
ATOM   4630 O  O    . VAL   B 1 49  ? 51.438 -23.643 -0.695  1.00 12.53 ?  49  VAL   B O    1 
ATOM   4631 C  CB   . VAL   B 1 49  ? 48.549 -25.299 -0.926  1.00 13.77 ?  49  VAL   B CB   1 
ATOM   4632 C  CG1  . VAL   B 1 49  ? 48.482 -24.065 -1.820  1.00 13.88 ?  49  VAL   B CG1  1 
ATOM   4633 C  CG2  . VAL   B 1 49  ? 47.995 -26.522 -1.651  1.00 14.99 ?  49  VAL   B CG2  1 
ATOM   4634 H  H    . VAL   B 1 49  ? 49.243 -26.872 0.794   1.00 14.93 ?  49  VAL   B H    1 
ATOM   4635 H  HA   . VAL   B 1 49  ? 50.498 -25.866 -1.229  1.00 15.18 ?  49  VAL   B HA   1 
ATOM   4636 H  HB   . VAL   B 1 49  ? 47.993 -25.131 -0.149  1.00 16.52 ?  49  VAL   B HB   1 
ATOM   4637 H  HG11 . VAL   B 1 49  ? 47.652 -24.084 -2.321  1.00 16.65 ?  49  VAL   B HG11 1 
ATOM   4638 H  HG12 . VAL   B 1 49  ? 48.513 -23.266 -1.268  1.00 16.65 ?  49  VAL   B HG12 1 
ATOM   4639 H  HG13 . VAL   B 1 49  ? 49.235 -24.075 -2.431  1.00 16.65 ?  49  VAL   B HG13 1 
ATOM   4640 H  HG21 . VAL   B 1 49  ? 47.085 -26.336 -1.934  1.00 17.99 ?  49  VAL   B HG21 1 
ATOM   4641 H  HG22 . VAL   B 1 49  ? 48.549 -26.705 -2.427  1.00 17.99 ?  49  VAL   B HG22 1 
ATOM   4642 H  HG23 . VAL   B 1 49  ? 48.007 -27.278 -1.048  1.00 17.99 ?  49  VAL   B HG23 1 
ATOM   4643 N  N    . ALA   B 1 50  ? 50.310 -23.822 1.233   1.00 11.76 ?  50  ALA   B N    1 
ATOM   4644 C  CA   . ALA   B 1 50  ? 50.829 -22.543 1.705   1.00 11.52 ?  50  ALA   B CA   1 
ATOM   4645 C  C    . ALA   B 1 50  ? 52.349 -22.571 1.820   1.00 11.85 ?  50  ALA   B C    1 
ATOM   4646 O  O    . ALA   B 1 50  ? 53.029 -21.601 1.456   1.00 11.96 ?  50  ALA   B O    1 
ATOM   4647 C  CB   . ALA   B 1 50  ? 50.192 -22.178 3.045   1.00 12.07 ?  50  ALA   B CB   1 
ATOM   4648 H  H    . ALA   B 1 50  ? 49.790 -24.225 1.781   1.00 14.11 ?  50  ALA   B H    1 
ATOM   4649 H  HA   . ALA   B 1 50  ? 50.603 -21.850 1.072   1.00 13.82 ?  50  ALA   B HA   1 
ATOM   4650 H  HB1  . ALA   B 1 50  ? 50.550 -21.323 3.345   1.00 14.48 ?  50  ALA   B HB1  1 
ATOM   4651 H  HB2  . ALA   B 1 50  ? 49.231 -22.103 2.926   1.00 14.48 ?  50  ALA   B HB2  1 
ATOM   4652 H  HB3  . ALA   B 1 50  ? 50.394 -22.865 3.695   1.00 14.48 ?  50  ALA   B HB3  1 
ATOM   4653 N  N    . GLY   B 1 51  ? 52.901 -23.665 2.340   1.00 12.22 ?  51  GLY   B N    1 
ATOM   4654 C  CA   . GLY   B 1 51  ? 54.344 -23.766 2.413   1.00 12.99 ?  51  GLY   B CA   1 
ATOM   4655 C  C    . GLY   B 1 51  ? 54.989 -23.713 1.045   1.00 12.79 ?  51  GLY   B C    1 
ATOM   4656 O  O    . GLY   B 1 51  ? 56.031 -23.079 0.864   1.00 13.59 ?  51  GLY   B O    1 
ATOM   4657 H  H    . GLY   B 1 51  ? 52.475 -24.348 2.643   1.00 14.67 ?  51  GLY   B H    1 
ATOM   4658 H  HA2  . GLY   B 1 51  ? 54.698 -23.034 2.942   1.00 15.59 ?  51  GLY   B HA2  1 
ATOM   4659 H  HA3  . GLY   B 1 51  ? 54.594 -24.602 2.840   1.00 15.59 ?  51  GLY   B HA3  1 
ATOM   4660 N  N    . ALA   B 1 52  ? 54.384 -24.379 0.062   1.00 12.51 ?  52  ALA   B N    1 
ATOM   4661 C  CA   . ALA   B 1 52  ? 54.941 -24.385 -1.283  1.00 12.91 ?  52  ALA   B CA   1 
ATOM   4662 C  C    . ALA   B 1 52  ? 54.864 -23.007 -1.929  1.00 12.28 ?  52  ALA   B C    1 
ATOM   4663 O  O    . ALA   B 1 52  ? 55.833 -22.552 -2.552  1.00 13.07 ?  52  ALA   B O    1 
ATOM   4664 C  CB   . ALA   B 1 52  ? 54.230 -25.430 -2.140  1.00 13.54 ?  52  ALA   B CB   1 
ATOM   4665 H  H    . ALA   B 1 52  ? 53.652 -24.826 0.146   1.00 15.01 ?  52  ALA   B H    1 
ATOM   4666 H  HA   . ALA   B 1 52  ? 55.875 -24.635 -1.233  1.00 15.49 ?  52  ALA   B HA   1 
ATOM   4667 H  HB1  . ALA   B 1 52  ? 54.614 -25.426 -3.032  1.00 16.25 ?  52  ALA   B HB1  1 
ATOM   4668 H  HB2  . ALA   B 1 52  ? 54.355 -26.308 -1.736  1.00 16.25 ?  52  ALA   B HB2  1 
ATOM   4669 H  HB3  . ALA   B 1 52  ? 53.286 -25.221 -2.184  1.00 16.25 ?  52  ALA   B HB3  1 
ATOM   4670 N  N    . LEU   B 1 53  ? 53.721 -22.329 -1.806  1.00 11.79 ?  53  LEU   B N    1 
ATOM   4671 C  CA   . LEU   B 1 53  ? 53.607 -20.990 -2.375  1.00 12.00 ?  53  LEU   B CA   1 
ATOM   4672 C  C    . LEU   B 1 53  ? 54.614 -20.047 -1.730  1.00 11.90 ?  53  LEU   B C    1 
ATOM   4673 O  O    . LEU   B 1 53  ? 55.314 -19.297 -2.420  1.00 12.38 ?  53  LEU   B O    1 
ATOM   4674 C  CB   . LEU   B 1 53  ? 52.183 -20.451 -2.205  1.00 12.62 ?  53  LEU   B CB   1 
ATOM   4675 C  CG   . LEU   B 1 53  ? 51.049 -21.181 -2.937  1.00 12.99 ?  53  LEU   B CG   1 
ATOM   4676 C  CD1  . LEU   B 1 53  ? 49.713 -20.568 -2.560  1.00 14.38 ?  53  LEU   B CD1  1 
ATOM   4677 C  CD2  . LEU   B 1 53  ? 51.239 -21.166 -4.449  1.00 14.88 ?  53  LEU   B CD2  1 
ATOM   4678 H  H    . LEU   B 1 53  ? 53.019 -22.612 -1.405  1.00 14.15 ?  53  LEU   B H    1 
ATOM   4679 H  HA   . LEU   B 1 53  ? 53.803 -21.030 -3.326  1.00 14.40 ?  53  LEU   B HA   1 
ATOM   4680 H  HB2  . LEU   B 1 53  ? 51.968 -20.471 -1.262  1.00 15.15 ?  53  LEU   B HB2  1 
ATOM   4681 H  HB3  . LEU   B 1 53  ? 52.171 -19.532 -2.516  1.00 15.15 ?  53  LEU   B HB3  1 
ATOM   4682 H  HG   . LEU   B 1 53  ? 51.040 -22.105 -2.649  1.00 15.59 ?  53  LEU   B HG   1 
ATOM   4683 H  HD11 . LEU   B 1 53  ? 49.005 -21.045 -3.025  1.00 17.26 ?  53  LEU   B HD11 1 
ATOM   4684 H  HD12 . LEU   B 1 53  ? 49.586 -20.652 -1.599  1.00 17.26 ?  53  LEU   B HD12 1 
ATOM   4685 H  HD13 . LEU   B 1 53  ? 49.705 -19.634 -2.814  1.00 17.26 ?  53  LEU   B HD13 1 
ATOM   4686 H  HD21 . LEU   B 1 53  ? 50.546 -21.709 -4.858  1.00 17.86 ?  53  LEU   B HD21 1 
ATOM   4687 H  HD22 . LEU   B 1 53  ? 51.171 -20.253 -4.769  1.00 17.86 ?  53  LEU   B HD22 1 
ATOM   4688 H  HD23 . LEU   B 1 53  ? 52.111 -21.530 -4.666  1.00 17.86 ?  53  LEU   B HD23 1 
ATOM   4689 N  N    . ASN   B 1 54  ? 54.704 -20.071 -0.403  1.00 11.66 ?  54  ASN   B N    1 
ATOM   4690 C  CA   . ASN   B 1 54  ? 55.618 -19.162 0.269   1.00 12.21 ?  54  ASN   B CA   1 
ATOM   4691 C  C    . ASN   B 1 54  ? 57.060 -19.441 -0.129  1.00 12.90 ?  54  ASN   B C    1 
ATOM   4692 O  O    . ASN   B 1 54  ? 57.837 -18.504 -0.356  1.00 13.28 ?  54  ASN   B O    1 
ATOM   4693 C  CB   . ASN   B 1 54  ? 55.455 -19.247 1.778   1.00 12.93 ?  54  ASN   B CB   1 
ATOM   4694 C  CG   . ASN   B 1 54  ? 56.431 -18.340 2.492   1.00 13.13 ?  54  ASN   B CG   1 
ATOM   4695 O  OD1  . ASN   B 1 54  ? 56.449 -17.127 2.254   1.00 13.40 ?  54  ASN   B OD1  1 
ATOM   4696 N  ND2  . ASN   B 1 54  ? 57.271 -18.918 3.344   1.00 14.76 ?  54  ASN   B ND2  1 
ATOM   4697 H  H    . ASN   B 1 54  ? 54.254 -20.588 0.115   1.00 14.00 ?  54  ASN   B H    1 
ATOM   4698 H  HA   . ASN   B 1 54  ? 55.407 -18.254 0.001   1.00 14.65 ?  54  ASN   B HA   1 
ATOM   4699 H  HB2  . ASN   B 1 54  ? 54.555 -18.976 2.022   1.00 15.52 ?  54  ASN   B HB2  1 
ATOM   4700 H  HB3  . ASN   B 1 54  ? 55.620 -20.158 2.069   1.00 15.52 ?  54  ASN   B HB3  1 
ATOM   4701 H  HD21 . ASN   B 1 54  ? 57.848 -18.445 3.774   1.00 17.72 ?  54  ASN   B HD21 1 
ATOM   4702 H  HD22 . ASN   B 1 54  ? 57.236 -19.770 3.475   1.00 17.72 ?  54  ASN   B HD22 1 
ATOM   4703 N  N    . LYS   B 1 55  ? 57.443 -20.719 -0.202  1.00 13.30 ?  55  LYS   B N    1 
ATOM   4704 C  CA   . LYS   B 1 55  ? 58.800 -21.059 -0.615  1.00 14.37 ?  55  LYS   B CA   1 
ATOM   4705 C  C    . LYS   B 1 55  ? 59.099 -20.521 -2.007  1.00 13.89 ?  55  LYS   B C    1 
ATOM   4706 O  O    . LYS   B 1 55  ? 60.196 -20.013 -2.260  1.00 14.80 ?  55  LYS   B O    1 
ATOM   4707 C  CB   . LYS   B 1 55  ? 58.992 -22.576 -0.567  1.00 16.39 ?  55  LYS   B CB   1 
ATOM   4708 C  CG   . LYS   B 1 55  ? 60.366 -23.050 -1.006  1.00 20.43 ?  55  LYS   B CG   1 
ATOM   4709 C  CD   . LYS   B 1 55  ? 60.534 -24.544 -0.784  1.00 23.99 ?  55  LYS   B CD   1 
ATOM   4710 C  CE   . LYS   B 1 55  ? 60.689 -24.887 0.697   1.00 27.14 ?  55  LYS   B CE   1 
ATOM   4711 N  NZ   . LYS   B 1 55  ? 61.003 -26.322 0.906   1.00 28.60 ?  55  LYS   B NZ   1 
ATOM   4712 H  H    . LYS   B 1 55  ? 56.936 -21.395 -0.031  1.00 15.96 ?  55  LYS   B H    1 
ATOM   4713 H  HA   . LYS   B 1 55  ? 59.425 -20.655 0.005   1.00 17.24 ?  55  LYS   B HA   1 
ATOM   4714 H  HB2  . LYS   B 1 55  ? 58.854 -22.872 0.346   1.00 19.66 ?  55  LYS   B HB2  1 
ATOM   4715 H  HB3  . LYS   B 1 55  ? 58.339 -22.991 -1.148  1.00 19.66 ?  55  LYS   B HB3  1 
ATOM   4716 H  HG2  . LYS   B 1 55  ? 60.481 -22.872 -1.952  1.00 24.51 ?  55  LYS   B HG2  1 
ATOM   4717 H  HG3  . LYS   B 1 55  ? 61.046 -22.588 -0.492  1.00 24.51 ?  55  LYS   B HG3  1 
ATOM   4718 H  HD2  . LYS   B 1 55  ? 59.754 -25.012 -1.121  1.00 28.79 ?  55  LYS   B HD2  1 
ATOM   4719 H  HD3  . LYS   B 1 55  ? 61.332 -24.852 -1.247  1.00 28.79 ?  55  LYS   B HD3  1 
ATOM   4720 H  HE2  . LYS   B 1 55  ? 61.412 -24.355 1.070   1.00 32.57 ?  55  LYS   B HE2  1 
ATOM   4721 H  HE3  . LYS   B 1 55  ? 59.858 -24.684 1.157   1.00 32.57 ?  55  LYS   B HE3  1 
ATOM   4722 H  HZ1  . LYS   B 1 55  ? 61.034 -26.501 1.777   1.00 34.32 ?  55  LYS   B HZ1  1 
ATOM   4723 H  HZ2  . LYS   B 1 55  ? 60.374 -26.825 0.529   1.00 34.32 ?  55  LYS   B HZ2  1 
ATOM   4724 H  HZ3  . LYS   B 1 55  ? 61.789 -26.516 0.540   1.00 34.32 ?  55  LYS   B HZ3  1 
ATOM   4725 N  N    . ALA   B 1 56  ? 58.132 -20.609 -2.921  1.00 13.49 ?  56  ALA   B N    1 
ATOM   4726 C  CA   . ALA   B 1 56  ? 58.347 -20.104 -4.271  1.00 14.26 ?  56  ALA   B CA   1 
ATOM   4727 C  C    . ALA   B 1 56  ? 58.625 -18.607 -4.270  1.00 14.08 ?  56  ALA   B C    1 
ATOM   4728 O  O    . ALA   B 1 56  ? 59.352 -18.111 -5.141  1.00 15.04 ?  56  ALA   B O    1 
ATOM   4729 C  CB   . ALA   B 1 56  ? 57.146 -20.436 -5.156  1.00 14.92 ?  56  ALA   B CB   1 
ATOM   4730 H  H    . ALA   B 1 56  ? 57.352 -20.949 -2.785  1.00 16.18 ?  56  ALA   B H    1 
ATOM   4731 H  HA   . ALA   B 1 56  ? 59.123 -20.542 -4.647  1.00 17.11 ?  56  ALA   B HA   1 
ATOM   4732 H  HB1  . ALA   B 1 56  ? 57.312 -20.099 -6.052  1.00 17.90 ?  56  ALA   B HB1  1 
ATOM   4733 H  HB2  . ALA   B 1 56  ? 57.034 -21.400 -5.183  1.00 17.90 ?  56  ALA   B HB2  1 
ATOM   4734 H  HB3  . ALA   B 1 56  ? 56.353 -20.020 -4.787  1.00 17.90 ?  56  ALA   B HB3  1 
ATOM   4735 N  N    . THR   B 1 57  ? 58.066 -17.876 -3.303  1.00 13.87 ?  57  THR   B N    1 
ATOM   4736 C  CA   . THR   B 1 57  ? 58.298 -16.441 -3.183  1.00 14.05 ?  57  THR   B CA   1 
ATOM   4737 C  C    . THR   B 1 57  ? 59.546 -16.114 -2.373  1.00 14.78 ?  57  THR   B C    1 
ATOM   4738 O  O    . THR   B 1 57  ? 59.788 -14.937 -2.073  1.00 15.24 ?  57  THR   B O    1 
ATOM   4739 C  CB   . THR   B 1 57  ? 57.098 -15.713 -2.549  1.00 13.40 ?  57  THR   B CB   1 
ATOM   4740 O  OG1  . THR   B 1 57  ? 57.069 -15.929 -1.130  1.00 13.48 ?  57  THR   B OG1  1 
ATOM   4741 C  CG2  . THR   B 1 57  ? 55.781 -16.126 -3.186  1.00 13.47 ?  57  THR   B CG2  1 
ATOM   4742 H  H    . THR   B 1 57  ? 57.535 -18.191 -2.702  1.00 16.64 ?  57  THR   B H    1 
ATOM   4743 H  HA   . THR   B 1 57  ? 58.419 -16.078 -4.074  1.00 16.86 ?  57  THR   B HA   1 
ATOM   4744 H  HB   . THR   B 1 57  ? 57.205 -14.763 -2.709  1.00 16.08 ?  57  THR   B HB   1 
ATOM   4745 H  HG1  . THR   B 1 57  ? 56.996 -16.752 -0.967  1.00 16.18 ?  57  THR   B HG1  1 
ATOM   4746 H  HG21 . THR   B 1 57  ? 55.055 -15.602 -2.814  1.00 16.16 ?  57  THR   B HG21 1 
ATOM   4747 H  HG22 . THR   B 1 57  ? 55.816 -15.985 -4.144  1.00 16.16 ?  57  THR   B HG22 1 
ATOM   4748 H  HG23 . THR   B 1 57  ? 55.609 -17.065 -3.014  1.00 16.16 ?  57  THR   B HG23 1 
ATOM   4749 N  N    . ASN   B 1 58  ? 60.344 -17.118 -2.015  1.00 15.36 ?  58  ASN   B N    1 
ATOM   4750 C  CA   . ASN   B 1 58  ? 61.539 -16.899 -1.207  1.00 18.32 ?  58  ASN   B CA   1 
ATOM   4751 C  C    . ASN   B 1 58  ? 61.196 -16.189 0.104   1.00 16.35 ?  58  ASN   B C    1 
ATOM   4752 O  O    . ASN   B 1 58  ? 61.928 -15.310 0.570   1.00 16.95 ?  58  ASN   B O    1 
ATOM   4753 C  CB   . ASN   B 1 58  ? 62.626 -16.150 -1.988  1.00 27.13 ?  58  ASN   B CB   1 
ATOM   4754 C  CG   . ASN   B 1 58  ? 63.993 -16.269 -1.341  1.00 36.51 ?  58  ASN   B CG   1 
ATOM   4755 O  OD1  . ASN   B 1 58  ? 64.301 -17.271 -0.697  1.00 39.02 ?  58  ASN   B OD1  1 
ATOM   4756 N  ND2  . ASN   B 1 58  ? 64.820 -15.242 -1.508  1.00 41.02 ?  58  ASN   B ND2  1 
ATOM   4757 H  H    . ASN   B 1 58  ? 60.216 -17.944 -2.232  1.00 18.43 ?  58  ASN   B H    1 
ATOM   4758 H  HA   . ASN   B 1 58  ? 61.906 -17.767 -0.981  1.00 21.98 ?  58  ASN   B HA   1 
ATOM   4759 H  HB2  . ASN   B 1 58  ? 62.687 -16.517 -2.889  1.00 32.56 ?  58  ASN   B HB2  1 
ATOM   4760 H  HB3  . ASN   B 1 58  ? 62.400 -15.208 -2.033  1.00 32.56 ?  58  ASN   B HB3  1 
ATOM   4761 H  HD21 . ASN   B 1 58  ? 65.607 -15.264 -1.160  1.00 49.23 ?  58  ASN   B HD21 1 
ATOM   4762 H  HD22 . ASN   B 1 58  ? 64.570 -14.557 -1.962  1.00 49.23 ?  58  ASN   B HD22 1 
ATOM   4763 N  N    . ASN   B 1 59  ? 60.069 -16.573 0.705   1.00 15.58 ?  59  ASN   B N    1 
ATOM   4764 C  CA   . ASN   B 1 59  ? 59.592 -16.102 2.008   1.00 15.30 ?  59  ASN   B CA   1 
ATOM   4765 C  C    . ASN   B 1 59  ? 58.995 -14.696 1.955   1.00 14.47 ?  59  ASN   B C    1 
ATOM   4766 O  O    . ASN   B 1 59  ? 58.562 -14.194 3.004   1.00 14.79 ?  59  ASN   B O    1 
ATOM   4767 C  CB   . ASN   B 1 59  ? 60.662 -16.157 3.114   1.00 16.18 ?  59  ASN   B CB   1 
ATOM   4768 C  CG   . ASN   B 1 59  ? 60.070 -16.337 4.496   1.00 17.47 ?  59  ASN   B CG   1 
ATOM   4769 O  OD1  . ASN   B 1 59  ? 59.253 -17.233 4.720   1.00 17.67 ?  59  ASN   B OD1  1 
ATOM   4770 N  ND2  . ASN   B 1 59  ? 60.481 -15.487 5.435   1.00 18.24 ?  59  ASN   B ND2  1 
ATOM   4771 H  H    . ASN   B 1 59  ? 59.529 -17.150 0.354   1.00 18.69 ?  59  ASN   B H    1 
ATOM   4772 H  HA   . ASN   B 1 59  ? 58.883 -16.698 2.288   1.00 18.36 ?  59  ASN   B HA   1 
ATOM   4773 H  HB2  . ASN   B 1 59  ? 61.256 -16.907 2.954   1.00 19.42 ?  59  ASN   B HB2  1 
ATOM   4774 H  HB3  . ASN   B 1 59  ? 61.163 -15.329 3.118   1.00 19.42 ?  59  ASN   B HB3  1 
ATOM   4775 H  HD21 . ASN   B 1 59  ? 60.174 -15.546 6.239   1.00 21.88 ?  59  ASN   B HD21 1 
ATOM   4776 H  HD22 . ASN   B 1 59  ? 61.053 -14.876 5.241   1.00 21.88 ?  59  ASN   B HD22 1 
ATOM   4777 N  N    . ALA   B 1 60  ? 58.935 -14.049 0.786   1.00 14.19 ?  60  ALA   B N    1 
ATOM   4778 C  CA   . ALA   B 1 60  ? 58.337 -12.719 0.713   1.00 14.34 ?  60  ALA   B CA   1 
ATOM   4779 C  C    . ALA   B 1 60  ? 56.871 -12.749 1.120   1.00 13.39 ?  60  ALA   B C    1 
ATOM   4780 O  O    . ALA   B 1 60  ? 56.370 -11.801 1.740   1.00 13.64 ?  60  ALA   B O    1 
ATOM   4781 C  CB   . ALA   B 1 60  ? 58.497 -12.140 -0.693  1.00 15.23 ?  60  ALA   B CB   1 
ATOM   4782 H  H    . ALA   B 1 60  ? 59.225 -14.362 0.039   1.00 17.03 ?  60  ALA   B H    1 
ATOM   4783 H  HA   . ALA   B 1 60  ? 58.801 -12.137 1.332   1.00 17.20 ?  60  ALA   B HA   1 
ATOM   4784 H  HB1  . ALA   B 1 60  ? 58.096 -11.260 -0.717  1.00 18.28 ?  60  ALA   B HB1  1 
ATOM   4785 H  HB2  . ALA   B 1 60  ? 59.443 -12.081 -0.903  1.00 18.28 ?  60  ALA   B HB2  1 
ATOM   4786 H  HB3  . ALA   B 1 60  ? 58.054 -12.726 -1.328  1.00 18.28 ?  60  ALA   B HB3  1 
ATOM   4787 N  N    . MET   B 1 61  ? 56.165 -13.827 0.778   1.00 12.71 ?  61  MET   B N    1 
ATOM   4788 C  CA   . MET   B 1 61  ? 54.771 -13.951 1.174   1.00 12.34 ?  61  MET   B CA   1 
ATOM   4789 C  C    . MET   B 1 61  ? 54.634 -13.963 2.694   1.00 12.54 ?  61  MET   B C    1 
ATOM   4790 O  O    . MET   B 1 61  ? 53.737 -13.318 3.247   1.00 12.50 ?  61  MET   B O    1 
ATOM   4791 C  CB   . MET   B 1 61  ? 54.194 -15.224 0.551   1.00 12.54 ?  61  MET   B CB   1 
ATOM   4792 C  CG   . MET   B 1 61  ? 52.747 -15.507 0.939   1.00 12.41 ?  61  MET   B CG   1 
ATOM   4793 S  SD   . MET   B 1 61  ? 52.110 -17.018 0.180   1.00 12.72 ?  61  MET   B SD   1 
ATOM   4794 C  CE   . MET   B 1 61  ? 51.848 -16.435 -1.494  1.00 13.73 ?  61  MET   B CE   1 
ATOM   4795 H  H    . MET   B 1 61  ? 56.467 -14.495 0.322   1.00 15.25 ?  61  MET   B H    1 
ATOM   4796 H  HA   . MET   B 1 61  ? 54.271 -13.202 0.816   1.00 14.81 ?  61  MET   B HA   1 
ATOM   4797 H  HB2  . MET   B 1 61  ? 54.226 -15.147 -0.417  1.00 15.05 ?  61  MET   B HB2  1 
ATOM   4798 H  HB3  . MET   B 1 61  ? 54.726 -15.985 0.834   1.00 15.05 ?  61  MET   B HB3  1 
ATOM   4799 H  HG2  . MET   B 1 61  ? 52.684 -15.613 1.903   1.00 14.89 ?  61  MET   B HG2  1 
ATOM   4800 H  HG3  . MET   B 1 61  ? 52.186 -14.768 0.653   1.00 14.89 ?  61  MET   B HG3  1 
ATOM   4801 H  HE1  . MET   B 1 61  ? 51.475 -17.157 -2.024  1.00 16.48 ?  61  MET   B HE1  1 
ATOM   4802 H  HE2  . MET   B 1 61  ? 51.230 -15.685 -1.480  1.00 16.48 ?  61  MET   B HE2  1 
ATOM   4803 H  HE3  . MET   B 1 61  ? 52.698 -16.155 -1.866  1.00 16.48 ?  61  MET   B HE3  1 
ATOM   4804 N  N    . GLN   B 1 62  ? 55.512 -14.685 3.393   1.00 12.61 ?  62  GLN   B N    1 
ATOM   4805 C  CA   . GLN   B 1 62  ? 55.406 -14.744 4.848   1.00 12.95 ?  62  GLN   B CA   1 
ATOM   4806 C  C    . GLN   B 1 62  ? 55.689 -13.389 5.482   1.00 13.14 ?  62  GLN   B C    1 
ATOM   4807 O  O    . GLN   B 1 62  ? 54.996 -12.985 6.422   1.00 13.58 ?  62  GLN   B O    1 
ATOM   4808 C  CB   . GLN   B 1 62  ? 56.356 -15.803 5.411   1.00 13.38 ?  62  GLN   B CB   1 
ATOM   4809 C  CG   . GLN   B 1 62  ? 56.136 -16.067 6.889   1.00 13.51 ?  62  GLN   B CG   1 
ATOM   4810 C  CD   . GLN   B 1 62  ? 54.758 -16.655 7.132   1.00 12.94 ?  62  GLN   B CD   1 
ATOM   4811 O  OE1  . GLN   B 1 62  ? 54.496 -17.805 6.776   1.00 13.47 ?  62  GLN   B OE1  1 
ATOM   4812 N  NE2  . GLN   B 1 62  ? 53.851 -15.856 7.690   1.00 13.38 ?  62  GLN   B NE2  1 
ATOM   4813 H  H    . GLN   B 1 62  ? 56.156 -15.148 3.055   1.00 15.13 ?  62  GLN   B H    1 
ATOM   4814 H  HA   . GLN   B 1 62  ? 54.498 -15.000 5.083   1.00 15.54 ?  62  GLN   B HA   1 
ATOM   4815 H  HB2  . GLN   B 1 62  ? 56.220 -16.638 4.935   1.00 16.05 ?  62  GLN   B HB2  1 
ATOM   4816 H  HB3  . GLN   B 1 62  ? 57.271 -15.500 5.293   1.00 16.05 ?  62  GLN   B HB3  1 
ATOM   4817 H  HG2  . GLN   B 1 62  ? 56.797 -16.703 7.202   1.00 16.21 ?  62  GLN   B HG2  1 
ATOM   4818 H  HG3  . GLN   B 1 62  ? 56.210 -15.234 7.382   1.00 16.21 ?  62  GLN   B HG3  1 
ATOM   4819 H  HE21 . GLN   B 1 62  ? 54.067 -15.051 7.916   1.00 16.05 ?  62  GLN   B HE21 1 
ATOM   4820 H  HE22 . GLN   B 1 62  ? 53.058 -16.144 7.843   1.00 16.05 ?  62  GLN   B HE22 1 
ATOM   4821 N  N    . VAL   B 1 63  ? 56.707 -12.679 4.996   1.00 13.91 ?  63  VAL   B N    1 
ATOM   4822 C  CA   . VAL   B 1 63  ? 57.013 -11.361 5.548   1.00 14.92 ?  63  VAL   B CA   1 
ATOM   4823 C  C    . VAL   B 1 63  ? 55.824 -10.426 5.363   1.00 14.00 ?  63  VAL   B C    1 
ATOM   4824 O  O    . VAL   B 1 63  ? 55.410 -9.723  6.295   1.00 14.68 ?  63  VAL   B O    1 
ATOM   4825 C  CB   . VAL   B 1 63  ? 58.307 -10.809 4.924   1.00 16.25 ?  63  VAL   B CB   1 
ATOM   4826 C  CG1  . VAL   B 1 63  ? 58.541 -9.370  5.354   1.00 16.82 ?  63  VAL   B CG1  1 
ATOM   4827 C  CG2  . VAL   B 1 63  ? 59.491 -11.682 5.331   1.00 16.53 ?  63  VAL   B CG2  1 
ATOM   4828 H  H    . VAL   B 1 63  ? 57.219 -12.933 4.353   1.00 16.70 ?  63  VAL   B H    1 
ATOM   4829 H  HA   . VAL   B 1 63  ? 57.166 -11.457 6.499   1.00 17.90 ?  63  VAL   B HA   1 
ATOM   4830 H  HB   . VAL   B 1 63  ? 58.240 -10.835 3.958   1.00 19.51 ?  63  VAL   B HB   1 
ATOM   4831 H  HG11 . VAL   B 1 63  ? 59.459 -9.129  5.159   1.00 20.19 ?  63  VAL   B HG11 1 
ATOM   4832 H  HG12 . VAL   B 1 63  ? 57.935 -8.795  4.866   1.00 20.19 ?  63  VAL   B HG12 1 
ATOM   4833 H  HG13 . VAL   B 1 63  ? 58.377 -9.299  6.308   1.00 20.19 ?  63  VAL   B HG13 1 
ATOM   4834 H  HG21 . VAL   B 1 63  ? 60.304 -11.315 4.948   1.00 19.84 ?  63  VAL   B HG21 1 
ATOM   4835 H  HG22 . VAL   B 1 63  ? 59.560 -11.690 6.301   1.00 19.84 ?  63  VAL   B HG22 1 
ATOM   4836 H  HG23 . VAL   B 1 63  ? 59.350 -12.584 5.004   1.00 19.84 ?  63  VAL   B HG23 1 
ATOM   4837 N  N    . GLU   B 1 64  ? 55.252 -10.414 4.156   1.00 13.51 ?  64  GLU   B N    1 
ATOM   4838 C  CA   . GLU   B 1 64  ? 54.089 -9.576  3.881   1.00 13.30 ?  64  GLU   B CA   1 
ATOM   4839 C  C    . GLU   B 1 64  ? 52.908 -9.974  4.760   1.00 12.87 ?  64  GLU   B C    1 
ATOM   4840 O  O    . GLU   B 1 64  ? 52.166 -9.115  5.262   1.00 13.52 ?  64  GLU   B O    1 
ATOM   4841 C  CB   . GLU   B 1 64  ? 53.728 -9.727  2.403   1.00 13.45 ?  64  GLU   B CB   1 
ATOM   4842 C  CG   . GLU   B 1 64  ? 52.467 -8.992  1.973   1.00 13.59 ?  64  GLU   B CG   1 
ATOM   4843 C  CD   . GLU   B 1 64  ? 51.922 -9.491  0.646   1.00 14.29 ?  64  GLU   B CD   1 
ATOM   4844 O  OE1  . GLU   B 1 64  ? 52.098 -10.697 0.332   1.00 15.04 ?  64  GLU   B OE1  1 
ATOM   4845 O  OE2  . GLU   B 1 64  ? 51.304 -8.669  -0.072  1.00 14.75 -1 64  GLU   B OE2  1 
ATOM   4846 H  H    . GLU   B 1 64  ? 55.519 -10.885 3.481   1.00 16.21 ?  64  GLU   B H    1 
ATOM   4847 H  HA   . GLU   B 1 64  ? 54.308 -8.649  4.051   1.00 15.96 ?  64  GLU   B HA   1 
ATOM   4848 H  HB2  . GLU   B 1 64  ? 54.458 -9.379  1.862   1.00 16.14 ?  64  GLU   B HB2  1 
ATOM   4849 H  HB3  . GLU   B 1 64  ? 53.599 -10.666 2.206   1.00 16.14 ?  64  GLU   B HB3  1 
ATOM   4850 H  HG2  . GLU   B 1 64  ? 51.771 -9.114  2.639   1.00 16.30 ?  64  GLU   B HG2  1 
ATOM   4851 H  HG3  . GLU   B 1 64  ? 52.668 -8.047  1.879   1.00 16.30 ?  64  GLU   B HG3  1 
ATOM   4852 N  N    . SER   B 1 65  ? 52.722 -11.282 4.946   1.00 12.57 ?  65  SER   B N    1 
ATOM   4853 C  CA   . SER   B 1 65  ? 51.615 -11.793 5.746   1.00 12.69 ?  65  SER   B CA   1 
ATOM   4854 C  C    . SER   B 1 65  ? 51.753 -11.396 7.210   1.00 12.95 ?  65  SER   B C    1 
ATOM   4855 O  O    . SER   B 1 65  ? 50.759 -11.025 7.850   1.00 13.17 ?  65  SER   B O    1 
ATOM   4856 C  CB   . SER   B 1 65  ? 51.535 -13.313 5.611   1.00 12.86 ?  65  SER   B CB   1 
ATOM   4857 O  OG   . SER   B 1 65  ? 51.191 -13.698 4.289   1.00 13.00 ?  65  SER   B OG   1 
ATOM   4858 H  H    . SER   B 1 65  ? 53.226 -11.900 4.615   1.00 15.09 ?  65  SER   B H    1 
ATOM   4859 H  HA   . SER   B 1 65  ? 50.784 -11.420 5.410   1.00 15.22 ?  65  SER   B HA   1 
ATOM   4860 H  HB2  . SER   B 1 65  ? 52.391 -13.698 5.838   1.00 15.44 ?  65  SER   B HB2  1 
ATOM   4861 H  HB3  . SER   B 1 65  ? 50.851 -13.645 6.220   1.00 15.44 ?  65  SER   B HB3  1 
ATOM   4862 H  HG   . SER   B 1 65  ? 51.769 -13.413 3.747   1.00 15.60 ?  65  SER   B HG   1 
ATOM   4863 N  N    . ASP   B 1 66  ? 52.964 -11.495 7.768   1.00 13.40 ?  66  ASP   B N    1 
ATOM   4864 C  CA   . ASP   B 1 66  ? 53.152 -11.110 9.163   1.00 13.33 ?  66  ASP   B CA   1 
ATOM   4865 C  C    . ASP   B 1 66  ? 52.842 -9.633  9.368   1.00 13.57 ?  66  ASP   B C    1 
ATOM   4866 O  O    . ASP   B 1 66  ? 52.266 -9.249  10.393  1.00 13.95 ?  66  ASP   B O    1 
ATOM   4867 C  CB   . ASP   B 1 66  ? 54.579 -11.423 9.615   1.00 14.71 ?  66  ASP   B CB   1 
ATOM   4868 C  CG   . ASP   B 1 66  ? 54.842 -12.912 9.775   1.00 16.88 ?  66  ASP   B CG   1 
ATOM   4869 O  OD1  . ASP   B 1 66  ? 53.890 -13.719 9.698   1.00 17.64 ?  66  ASP   B OD1  1 
ATOM   4870 O  OD2  . ASP   B 1 66  ? 56.018 -13.281 9.987   1.00 19.27 -1 66  ASP   B OD2  1 
ATOM   4871 H  H    . ASP   B 1 66  ? 53.667 -11.790 7.372   1.00 16.07 ?  66  ASP   B H    1 
ATOM   4872 H  HA   . ASP   B 1 66  ? 52.546 -11.616 9.721   1.00 16.00 ?  66  ASP   B HA   1 
ATOM   4873 H  HB2  . ASP   B 1 66  ? 55.204 -11.087 8.956   1.00 17.66 ?  66  ASP   B HB2  1 
ATOM   4874 H  HB3  . ASP   B 1 66  ? 54.741 -10.996 10.474  1.00 17.66 ?  66  ASP   B HB3  1 
ATOM   4875 N  N    . ASP   B 1 67  ? 53.217 -8.786  8.404   1.00 13.10 ?  67  ASP   B N    1 
ATOM   4876 C  CA   . ASP   B 1 67  ? 52.874 -7.375  8.496   1.00 13.86 ?  67  ASP   B CA   1 
ATOM   4877 C  C    . ASP   B 1 67  ? 51.362 -7.169  8.416   1.00 14.12 ?  67  ASP   B C    1 
ATOM   4878 O  O    . ASP   B 1 67  ? 50.798 -6.368  9.169   1.00 14.61 ?  67  ASP   B O    1 
ATOM   4879 C  CB   . ASP   B 1 67  ? 53.594 -6.598  7.400   1.00 15.37 ?  67  ASP   B CB   1 
ATOM   4880 C  CG   . ASP   B 1 67  ? 53.162 -5.155  7.355   1.00 16.83 ?  67  ASP   B CG   1 
ATOM   4881 O  OD1  . ASP   B 1 67  ? 53.643 -4.348  8.184   1.00 17.66 ?  67  ASP   B OD1  1 
ATOM   4882 O  OD2  . ASP   B 1 67  ? 52.305 -4.852  6.508   1.00 17.92 -1 67  ASP   B OD2  1 
ATOM   4883 H  H    . ASP   B 1 67  ? 53.676 -9.004  7.707   1.00 15.73 ?  67  ASP   B H    1 
ATOM   4884 H  HA   . ASP   B 1 67  ? 53.185 -7.032  9.351   1.00 16.63 ?  67  ASP   B HA   1 
ATOM   4885 H  HB2  . ASP   B 1 67  ? 54.553 -6.618  7.567   1.00 18.44 ?  67  ASP   B HB2  1 
ATOM   4886 H  HB3  . ASP   B 1 67  ? 53.405 -7.014  6.540   1.00 18.44 ?  67  ASP   B HB3  1 
ATOM   4887 N  N    . TYR   B 1 68  ? 50.682 -7.897  7.526   1.00 13.81 ?  68  TYR   B N    1 
ATOM   4888 C  CA   . TYR   B 1 68  ? 49.225 -7.816  7.458   1.00 14.60 ?  68  TYR   B CA   1 
ATOM   4889 C  C    . TYR   B 1 68  ? 48.592 -8.159  8.805   1.00 14.15 ?  68  TYR   B C    1 
ATOM   4890 O  O    . TYR   B 1 68  ? 47.660 -7.481  9.256   1.00 14.94 ?  68  TYR   B O    1 
ATOM   4891 C  CB   . TYR   B 1 68  ? 48.689 -8.738  6.355   1.00 15.45 ?  68  TYR   B CB   1 
ATOM   4892 C  CG   . TYR   B 1 68  ? 47.185 -8.896  6.415   1.00 16.60 ?  68  TYR   B CG   1 
ATOM   4893 C  CD1  . TYR   B 1 68  ? 46.598 -9.848  7.245   1.00 17.50 ?  68  TYR   B CD1  1 
ATOM   4894 C  CD2  . TYR   B 1 68  ? 46.355 -8.065  5.686   1.00 17.89 ?  68  TYR   B CD2  1 
ATOM   4895 C  CE1  . TYR   B 1 68  ? 45.233 -9.972  7.335   1.00 18.78 ?  68  TYR   B CE1  1 
ATOM   4896 C  CE2  . TYR   B 1 68  ? 44.978 -8.191  5.762   1.00 18.55 ?  68  TYR   B CE2  1 
ATOM   4897 C  CZ   . TYR   B 1 68  ? 44.433 -9.143  6.589   1.00 18.69 ?  68  TYR   B CZ   1 
ATOM   4898 O  OH   . TYR   B 1 68  ? 43.066 -9.263  6.678   1.00 19.78 ?  68  TYR   B OH   1 
ATOM   4899 H  H    . TYR   B 1 68  ? 51.042 -8.438  6.959   1.00 16.57 ?  68  TYR   B H    1 
ATOM   4900 H  HA   . TYR   B 1 68  ? 48.977 -6.909  7.239   1.00 17.52 ?  68  TYR   B HA   1 
ATOM   4901 H  HB2  . TYR   B 1 68  ? 48.916 -8.360  5.493   1.00 18.54 ?  68  TYR   B HB2  1 
ATOM   4902 H  HB3  . TYR   B 1 68  ? 49.088 -9.616  6.453   1.00 18.54 ?  68  TYR   B HB3  1 
ATOM   4903 H  HD1  . TYR   B 1 68  ? 47.140 -10.411 7.754   1.00 21.00 ?  68  TYR   B HD1  1 
ATOM   4904 H  HD2  . TYR   B 1 68  ? 46.725 -7.417  5.137   1.00 21.47 ?  68  TYR   B HD2  1 
ATOM   4905 H  HE1  . TYR   B 1 68  ? 44.851 -10.625 7.885   1.00 22.54 ?  68  TYR   B HE1  1 
ATOM   4906 H  HE2  . TYR   B 1 68  ? 44.422 -7.632  5.268   1.00 22.26 ?  68  TYR   B HE2  1 
ATOM   4907 H  HH   . TYR   B 1 68  ? 42.681 -8.710  6.170   1.00 23.74 ?  68  TYR   B HH   1 
ATOM   4908 N  N    . ILE   B 1 69  ? 49.063 -9.238  9.442   1.00 13.85 ?  69  ILE   B N    1 
ATOM   4909 C  CA   . ILE   B 1 69  ? 48.508 -9.664  10.725  1.00 14.42 ?  69  ILE   B CA   1 
ATOM   4910 C  C    . ILE   B 1 69  ? 48.765 -8.619  11.805  1.00 14.45 ?  69  ILE   B C    1 
ATOM   4911 O  O    . ILE   B 1 69  ? 47.897 -8.345  12.642  1.00 14.81 ?  69  ILE   B O    1 
ATOM   4912 C  CB   . ILE   B 1 69  ? 49.083 -11.041 11.115  1.00 15.28 ?  69  ILE   B CB   1 
ATOM   4913 C  CG1  . ILE   B 1 69  ? 48.548 -12.136 10.183  1.00 15.65 ?  69  ILE   B CG1  1 
ATOM   4914 C  CG2  . ILE   B 1 69  ? 48.785 -11.366 12.575  1.00 16.18 ?  69  ILE   B CG2  1 
ATOM   4915 C  CD1  . ILE   B 1 69  ? 47.076 -12.442 10.346  1.00 15.96 ?  69  ILE   B CD1  1 
ATOM   4916 H  H    . ILE   B 1 69  ? 49.699 -9.738  9.154   1.00 16.62 ?  69  ILE   B H    1 
ATOM   4917 H  HA   . ILE   B 1 69  ? 47.550 -9.761  10.635  1.00 17.31 ?  69  ILE   B HA   1 
ATOM   4918 H  HB   . ILE   B 1 69  ? 50.048 -11.006 11.012  1.00 18.34 ?  69  ILE   B HB   1 
ATOM   4919 H  HG12 . ILE   B 1 69  ? 48.693 -11.854 9.265   1.00 18.78 ?  69  ILE   B HG12 1 
ATOM   4920 H  HG13 . ILE   B 1 69  ? 49.042 -12.954 10.352  1.00 18.78 ?  69  ILE   B HG13 1 
ATOM   4921 H  HG21 . ILE   B 1 69  ? 48.928 -12.316 12.721  1.00 19.42 ?  69  ILE   B HG21 1 
ATOM   4922 H  HG22 . ILE   B 1 69  ? 49.380 -10.856 13.146  1.00 19.42 ?  69  ILE   B HG22 1 
ATOM   4923 H  HG23 . ILE   B 1 69  ? 47.862 -11.141 12.767  1.00 19.42 ?  69  ILE   B HG23 1 
ATOM   4924 H  HD11 . ILE   B 1 69  ? 46.838 -13.145 9.725   1.00 19.16 ?  69  ILE   B HD11 1 
ATOM   4925 H  HD12 . ILE   B 1 69  ? 46.913 -12.735 11.255  1.00 19.16 ?  69  ILE   B HD12 1 
ATOM   4926 H  HD13 . ILE   B 1 69  ? 46.563 -11.643 10.154  1.00 19.16 ?  69  ILE   B HD13 1 
ATOM   4927 N  N    . ALA   B 1 70  ? 49.961 -8.036  11.822  1.00 14.26 ?  70  ALA   B N    1 
ATOM   4928 C  CA   . ALA   B 1 70  ? 50.247 -7.002  12.811  1.00 14.04 ?  70  ALA   B CA   1 
ATOM   4929 C  C    . ALA   B 1 70  ? 49.255 -5.854  12.702  1.00 14.70 ?  70  ALA   B C    1 
ATOM   4930 O  O    . ALA   B 1 70  ? 48.815 -5.306  13.718  1.00 14.96 ?  70  ALA   B O    1 
ATOM   4931 C  CB   . ALA   B 1 70  ? 51.674 -6.494  12.634  1.00 14.43 ?  70  ALA   B CB   1 
ATOM   4932 H  H    . ALA   B 1 70  ? 50.604 -8.219  11.290  1.00 17.12 ?  70  ALA   B H    1 
ATOM   4933 H  HA   . ALA   B 1 70  ? 50.171 -7.379  13.701  1.00 16.85 ?  70  ALA   B HA   1 
ATOM   4934 H  HB1  . ALA   B 1 70  ? 51.864 -5.835  13.321  1.00 17.32 ?  70  ALA   B HB1  1 
ATOM   4935 H  HB2  . ALA   B 1 70  ? 52.288 -7.240  12.714  1.00 17.32 ?  70  ALA   B HB2  1 
ATOM   4936 H  HB3  . ALA   B 1 70  ? 51.761 -6.089  11.755  1.00 17.32 ?  70  ALA   B HB3  1 
ATOM   4937 N  N    . THR   B 1 71  ? 48.876 -5.491  11.477  1.00 15.00 ?  71  THR   B N    1 
ATOM   4938 C  CA   . THR   B 1 71  ? 47.989 -4.352  11.269  1.00 15.92 ?  71  THR   B CA   1 
ATOM   4939 C  C    . THR   B 1 71  ? 46.522 -4.715  11.474  1.00 16.52 ?  71  THR   B C    1 
ATOM   4940 O  O    . THR   B 1 71  ? 45.747 -3.898  11.990  1.00 17.84 ?  71  THR   B O    1 
ATOM   4941 C  CB   . THR   B 1 71  ? 48.215 -3.779  9.867   1.00 17.73 ?  71  THR   B CB   1 
ATOM   4942 O  OG1  . THR   B 1 71  ? 49.546 -3.260  9.775   1.00 19.56 ?  71  THR   B OG1  1 
ATOM   4943 C  CG2  . THR   B 1 71  ? 47.217 -2.672  9.552   1.00 18.43 ?  71  THR   B CG2  1 
ATOM   4944 H  H    . THR   B 1 71  ? 49.121 -5.885  10.755  1.00 18.00 ?  71  THR   B H    1 
ATOM   4945 H  HA   . THR   B 1 71  ? 48.210 -3.659  11.907  1.00 19.10 ?  71  THR   B HA   1 
ATOM   4946 H  HB   . THR   B 1 71  ? 48.108 -4.482  9.206   1.00 21.27 ?  71  THR   B HB   1 
ATOM   4947 H  HG1  . THR   B 1 71  ? 49.681 -2.930  9.012   1.00 23.47 ?  71  THR   B HG1  1 
ATOM   4948 H  HG21 . THR   B 1 71  ? 47.521 -2.161  8.783   1.00 22.11 ?  71  THR   B HG21 1 
ATOM   4949 H  HG22 . THR   B 1 71  ? 46.348 -3.048  9.354   1.00 22.11 ?  71  THR   B HG22 1 
ATOM   4950 H  HG23 . THR   B 1 71  ? 47.140 -2.071  10.312  1.00 22.11 ?  71  THR   B HG23 1 
ATOM   4951 N  N    . ASN   B 1 72  ? 46.123 -5.930  11.086  1.00 16.32 ?  72  ASN   B N    1 
ATOM   4952 C  CA   . ASN   B 1 72  ? 44.719 -6.288  10.959  1.00 16.66 ?  72  ASN   B CA   1 
ATOM   4953 C  C    . ASN   B 1 72  ? 44.246 -7.387  11.899  1.00 17.07 ?  72  ASN   B C    1 
ATOM   4954 O  O    . ASN   B 1 72  ? 43.028 -7.553  12.055  1.00 18.18 ?  72  ASN   B O    1 
ATOM   4955 C  CB   . ASN   B 1 72  ? 44.416 -6.713  9.514   1.00 17.22 ?  72  ASN   B CB   1 
ATOM   4956 C  CG   . ASN   B 1 72  ? 44.676 -5.600  8.525   1.00 18.35 ?  72  ASN   B CG   1 
ATOM   4957 O  OD1  . ASN   B 1 72  ? 45.689 -5.591  7.816   1.00 19.57 ?  72  ASN   B OD1  1 
ATOM   4958 N  ND2  . ASN   B 1 72  ? 43.786 -4.630  8.501   1.00 19.84 ?  72  ASN   B ND2  1 
ATOM   4959 H  H    . ASN   B 1 72  ? 46.665 -6.575  10.888  1.00 19.58 ?  72  ASN   B H    1 
ATOM   4960 H  HA   . ASN   B 1 72  ? 44.188 -5.503  11.149  1.00 19.99 ?  72  ASN   B HA   1 
ATOM   4961 H  HB2  . ASN   B 1 72  ? 44.982 -7.466  9.280   1.00 20.67 ?  72  ASN   B HB2  1 
ATOM   4962 H  HB3  . ASN   B 1 72  ? 43.482 -6.965  9.451   1.00 20.67 ?  72  ASN   B HB3  1 
ATOM   4963 H  HD21 . ASN   B 1 72  ? 43.883 -3.970  7.960   1.00 23.81 ?  72  ASN   B HD21 1 
ATOM   4964 H  HD22 . ASN   B 1 72  ? 43.093 -4.665  9.014   1.00 23.81 ?  72  ASN   B HD22 1 
ATOM   4965 N  N    . GLY   B 1 73  ? 45.148 -8.141  12.522  1.00 16.73 ?  73  GLY   B N    1 
ATOM   4966 C  CA   . GLY   B 1 73  ? 44.749 -9.282  13.310  1.00 16.28 ?  73  GLY   B CA   1 
ATOM   4967 C  C    . GLY   B 1 73  ? 44.379 -10.459 12.434  1.00 15.15 ?  73  GLY   B C    1 
ATOM   4968 O  O    . GLY   B 1 73  ? 44.363 -10.368 11.201  1.00 14.85 ?  73  GLY   B O    1 
ATOM   4969 H  H    . GLY   B 1 73  ? 46.000 -8.006  12.502  1.00 20.07 ?  73  GLY   B H    1 
ATOM   4970 H  HA2  . GLY   B 1 73  ? 45.478 -9.542  13.898  1.00 19.54 ?  73  GLY   B HA2  1 
ATOM   4971 H  HA3  . GLY   B 1 73  ? 43.983 -9.046  13.859  1.00 19.54 ?  73  GLY   B HA3  1 
ATOM   4972 N  N    . PRO   B 1 74  ? 44.066 -11.587 13.065  1.00 15.20 ?  74  PRO   B N    1 
ATOM   4973 C  CA   . PRO   B 1 74  ? 43.812 -12.814 12.308  1.00 14.53 ?  74  PRO   B CA   1 
ATOM   4974 C  C    . PRO   B 1 74  ? 42.512 -12.754 11.517  1.00 14.10 ?  74  PRO   B C    1 
ATOM   4975 O  O    . PRO   B 1 74  ? 41.568 -12.021 11.840  1.00 15.11 ?  74  PRO   B O    1 
ATOM   4976 C  CB   . PRO   B 1 74  ? 43.742 -13.889 13.400  1.00 15.80 ?  74  PRO   B CB   1 
ATOM   4977 C  CG   . PRO   B 1 74  ? 43.303 -13.155 14.619  1.00 16.95 ?  74  PRO   B CG   1 
ATOM   4978 C  CD   . PRO   B 1 74  ? 43.959 -11.805 14.518  1.00 16.46 ?  74  PRO   B CD   1 
ATOM   4979 H  HA   . PRO   B 1 74  ? 44.554 -13.001 11.708  1.00 17.43 ?  74  PRO   B HA   1 
ATOM   4980 H  HB2  . PRO   B 1 74  ? 43.093 -14.566 13.148  1.00 18.95 ?  74  PRO   B HB2  1 
ATOM   4981 H  HB3  . PRO   B 1 74  ? 44.619 -14.283 13.529  1.00 18.95 ?  74  PRO   B HB3  1 
ATOM   4982 H  HG2  . PRO   B 1 74  ? 42.336 -13.071 14.616  1.00 20.34 ?  74  PRO   B HG2  1 
ATOM   4983 H  HG3  . PRO   B 1 74  ? 43.605 -13.629 15.409  1.00 20.34 ?  74  PRO   B HG3  1 
ATOM   4984 H  HD2  . PRO   B 1 74  ? 43.397 -11.127 14.929  1.00 19.75 ?  74  PRO   B HD2  1 
ATOM   4985 H  HD3  . PRO   B 1 74  ? 44.840 -11.827 14.920  1.00 19.75 ?  74  PRO   B HD3  1 
ATOM   4986 N  N    . LEU   B 1 75  ? 42.481 -13.566 10.464  1.00 13.36 ?  75  LEU   B N    1 
ATOM   4987 C  CA   . LEU   B 1 75  ? 41.272 -13.783 9.691   1.00 13.23 ?  75  LEU   B CA   1 
ATOM   4988 C  C    . LEU   B 1 75  ? 40.300 -14.646 10.490  1.00 13.56 ?  75  LEU   B C    1 
ATOM   4989 O  O    . LEU   B 1 75  ? 40.637 -15.192 11.540  1.00 14.86 ?  75  LEU   B O    1 
ATOM   4990 C  CB   . LEU   B 1 75  ? 41.602 -14.493 8.376   1.00 13.72 ?  75  LEU   B CB   1 
ATOM   4991 C  CG   . LEU   B 1 75  ? 42.452 -13.738 7.346   1.00 15.24 ?  75  LEU   B CG   1 
ATOM   4992 C  CD1  . LEU   B 1 75  ? 42.652 -14.573 6.081   1.00 16.60 ?  75  LEU   B CD1  1 
ATOM   4993 C  CD2  . LEU   B 1 75  ? 41.856 -12.400 7.004   1.00 18.13 ?  75  LEU   B CD2  1 
ATOM   4994 H  H    . LEU   B 1 75  ? 43.155 -14.017 10.180  1.00 16.03 ?  75  LEU   B H    1 
ATOM   4995 H  HA   . LEU   B 1 75  ? 40.848 -12.938 9.498   1.00 15.88 ?  75  LEU   B HA   1 
ATOM   4996 H  HB2  . LEU   B 1 75  ? 42.080 -15.312 8.590   1.00 16.46 ?  75  LEU   B HB2  1 
ATOM   4997 H  HB3  . LEU   B 1 75  ? 40.766 -14.722 7.942   1.00 16.46 ?  75  LEU   B HB3  1 
ATOM   4998 H  HG   . LEU   B 1 75  ? 43.327 -13.580 7.729   1.00 18.29 ?  75  LEU   B HG   1 
ATOM   4999 H  HD11 . LEU   B 1 75  ? 43.195 -14.068 5.452   1.00 19.92 ?  75  LEU   B HD11 1 
ATOM   5000 H  HD12 . LEU   B 1 75  ? 43.102 -15.400 6.312   1.00 19.92 ?  75  LEU   B HD12 1 
ATOM   5001 H  HD13 . LEU   B 1 75  ? 41.787 -14.766 5.686   1.00 19.92 ?  75  LEU   B HD13 1 
ATOM   5002 H  HD21 . LEU   B 1 75  ? 42.372 -12.000 6.290   1.00 21.75 ?  75  LEU   B HD21 1 
ATOM   5003 H  HD22 . LEU   B 1 75  ? 40.938 -12.529 6.722   1.00 21.75 ?  75  LEU   B HD22 1 
ATOM   5004 H  HD23 . LEU   B 1 75  ? 41.884 -11.834 7.792   1.00 21.75 ?  75  LEU   B HD23 1 
ATOM   5005 N  N    . LYS   B 1 76  ? 39.072 -14.748 9.983   1.00 14.67 ?  76  LYS   B N    1 
ATOM   5006 C  CA   . LYS   B 1 76  ? 38.089 -15.714 10.458  1.00 16.30 ?  76  LYS   B CA   1 
ATOM   5007 C  C    . LYS   B 1 76  ? 38.176 -16.982 9.612   1.00 14.63 ?  76  LYS   B C    1 
ATOM   5008 O  O    . LYS   B 1 76  ? 38.442 -16.919 8.413   1.00 14.39 ?  76  LYS   B O    1 
ATOM   5009 C  CB   . LYS   B 1 76  ? 36.665 -15.149 10.294  1.00 18.94 ?  76  LYS   B CB   1 
ATOM   5010 C  CG   . LYS   B 1 76  ? 36.383 -13.778 10.933  1.00 21.06 ?  76  LYS   B CG   1 
ATOM   5011 C  CD   . LYS   B 1 76  ? 34.985 -13.234 10.562  1.00 22.56 ?  76  LYS   B CD   1 
ATOM   5012 C  CE   . LYS   B 1 76  ? 34.730 -11.856 11.158  1.00 24.86 ?  76  LYS   B CE   1 
ATOM   5013 N  NZ   . LYS   B 1 76  ? 33.439 -11.265 10.696  1.00 25.46 ?  76  LYS   B NZ   1 
ATOM   5014 H  H    . LYS   B 1 76  ? 38.777 -14.255 9.347   1.00 17.60 ?  76  LYS   B H    1 
ATOM   5015 H  HA   . LYS   B 1 76  ? 38.240 -15.936 11.394  1.00 19.56 ?  76  LYS   B HA   1 
ATOM   5016 H  HB2  . LYS   B 1 76  ? 36.482 -15.065 9.345   1.00 22.73 ?  76  LYS   B HB2  1 
ATOM   5017 H  HB3  . LYS   B 1 76  ? 36.038 -15.779 10.685  1.00 22.73 ?  76  LYS   B HB3  1 
ATOM   5018 H  HG2  . LYS   B 1 76  ? 36.429 -13.862 11.897  1.00 25.27 ?  76  LYS   B HG2  1 
ATOM   5019 H  HG3  . LYS   B 1 76  ? 37.047 -13.142 10.621  1.00 25.27 ?  76  LYS   B HG3  1 
ATOM   5020 H  HD2  . LYS   B 1 76  ? 34.918 -13.163 9.596   1.00 27.07 ?  76  LYS   B HD2  1 
ATOM   5021 H  HD3  . LYS   B 1 76  ? 34.309 -13.840 10.900  1.00 27.07 ?  76  LYS   B HD3  1 
ATOM   5022 H  HE2  . LYS   B 1 76  ? 34.699 -11.930 12.124  1.00 29.83 ?  76  LYS   B HE2  1 
ATOM   5023 H  HE3  . LYS   B 1 76  ? 35.447 -11.259 10.892  1.00 29.83 ?  76  LYS   B HE3  1 
ATOM   5024 H  HZ1  . LYS   B 1 76  ? 33.323 -10.459 11.064  1.00 30.55 ?  76  LYS   B HZ1  1 
ATOM   5025 H  HZ2  . LYS   B 1 76  ? 33.441 -11.175 9.810   1.00 30.55 ?  76  LYS   B HZ2  1 
ATOM   5026 H  HZ3  . LYS   B 1 76  ? 32.759 -11.787 10.933  1.00 30.55 ?  76  LYS   B HZ3  1 
ATOM   5027 N  N    . VAL   B 1 77  ? 37.923 -18.140 10.233  1.00 15.17 ?  77  VAL   B N    1 
ATOM   5028 C  CA   . VAL   B 1 77  ? 37.713 -19.347 9.438   1.00 15.40 ?  77  VAL   B CA   1 
ATOM   5029 C  C    . VAL   B 1 77  ? 36.520 -19.105 8.525   1.00 14.43 ?  77  VAL   B C    1 
ATOM   5030 O  O    . VAL   B 1 77  ? 35.457 -18.655 8.972   1.00 14.56 ?  77  VAL   B O    1 
ATOM   5031 C  CB   . VAL   B 1 77  ? 37.517 -20.582 10.333  1.00 16.81 ?  77  VAL   B CB   1 
ATOM   5032 C  CG1  . VAL   B 1 77  ? 37.215 -21.804 9.476   1.00 17.33 ?  77  VAL   B CG1  1 
ATOM   5033 C  CG2  . VAL   B 1 77  ? 38.754 -20.831 11.192  1.00 18.21 ?  77  VAL   B CG2  1 
ATOM   5034 H  H    . VAL   B 1 77  ? 37.873 -18.250 11.081  1.00 18.20 ?  77  VAL   B H    1 
ATOM   5035 H  HA   . VAL   B 1 77  ? 38.488 -19.498 8.878   1.00 18.48 ?  77  VAL   B HA   1 
ATOM   5036 H  HB   . VAL   B 1 77  ? 36.760 -20.431 10.920  1.00 20.17 ?  77  VAL   B HB   1 
ATOM   5037 H  HG11 . VAL   B 1 77  ? 37.280 -22.597 10.029  1.00 20.80 ?  77  VAL   B HG11 1 
ATOM   5038 H  HG12 . VAL   B 1 77  ? 36.314 -21.728 9.118   1.00 20.80 ?  77  VAL   B HG12 1 
ATOM   5039 H  HG13 . VAL   B 1 77  ? 37.856 -21.850 8.752   1.00 20.80 ?  77  VAL   B HG13 1 
ATOM   5040 H  HG21 . VAL   B 1 77  ? 38.607 -21.628 11.723  1.00 21.85 ?  77  VAL   B HG21 1 
ATOM   5041 H  HG22 . VAL   B 1 77  ? 39.518 -20.952 10.611  1.00 21.85 ?  77  VAL   B HG22 1 
ATOM   5042 H  HG23 . VAL   B 1 77  ? 38.891 -20.065 11.770  1.00 21.85 ?  77  VAL   B HG23 1 
ATOM   5043 N  N    . GLY   B 1 78  ? 36.699 -19.382 7.235   1.00 13.90 ?  78  GLY   B N    1 
ATOM   5044 C  CA   . GLY   B 1 78  ? 35.723 -19.062 6.222   1.00 13.29 ?  78  GLY   B CA   1 
ATOM   5045 C  C    . GLY   B 1 78  ? 35.959 -17.742 5.526   1.00 12.91 ?  78  GLY   B C    1 
ATOM   5046 O  O    . GLY   B 1 78  ? 35.279 -17.459 4.534   1.00 13.26 ?  78  GLY   B O    1 
ATOM   5047 H  H    . GLY   B 1 78  ? 37.403 -19.763 6.917   1.00 16.68 ?  78  GLY   B H    1 
ATOM   5048 H  HA2  . GLY   B 1 78  ? 35.719 -19.760 5.549   1.00 15.95 ?  78  GLY   B HA2  1 
ATOM   5049 H  HA3  . GLY   B 1 78  ? 34.842 -19.028 6.625   1.00 15.95 ?  78  GLY   B HA3  1 
ATOM   5050 N  N    . GLY   B 1 79  ? 36.911 -16.938 6.009   1.00 12.89 ?  79  GLY   B N    1 
ATOM   5051 C  CA   . GLY   B 1 79  ? 37.212 -15.643 5.437   1.00 12.82 ?  79  GLY   B CA   1 
ATOM   5052 C  C    . GLY   B 1 79  ? 38.455 -15.663 4.553   1.00 12.15 ?  79  GLY   B C    1 
ATOM   5053 O  O    . GLY   B 1 79  ? 39.071 -16.699 4.303   1.00 12.67 ?  79  GLY   B O    1 
ATOM   5054 H  H    . GLY   B 1 79  ? 37.409 -17.136 6.675   1.00 15.47 ?  79  GLY   B H    1 
ATOM   5055 H  HA2  . GLY   B 1 79  ? 36.457 -15.339 4.901   1.00 15.38 ?  79  GLY   B HA2  1 
ATOM   5056 H  HA3  . GLY   B 1 79  ? 37.356 -15.001 6.148   1.00 15.38 ?  79  GLY   B HA3  1 
ATOM   5057 N  N    . SER   B 1 80  ? 38.825 -14.470 4.084   1.00 12.47 ?  80  SER   B N    1 
ATOM   5058 C  CA   . SER   B 1 80  ? 39.937 -14.335 3.153   1.00 12.21 ?  80  SER   B CA   1 
ATOM   5059 C  C    . SER   B 1 80  ? 40.515 -12.927 3.216   1.00 12.22 ?  80  SER   B C    1 
ATOM   5060 O  O    . SER   B 1 80  ? 39.895 -11.992 3.730   1.00 13.33 ?  80  SER   B O    1 
ATOM   5061 C  CB   . SER   B 1 80  ? 39.485 -14.623 1.718   1.00 12.43 ?  80  SER   B CB   1 
ATOM   5062 O  OG   . SER   B 1 80  ? 38.639 -13.597 1.223   1.00 13.34 ?  80  SER   B OG   1 
ATOM   5063 H  H    . SER   B 1 80  ? 38.453 -13.726 4.297   1.00 14.97 ?  80  SER   B H    1 
ATOM   5064 H  HA   . SER   B 1 80  ? 40.626 -14.969 3.397   1.00 14.65 ?  80  SER   B HA   1 
ATOM   5065 H  HB2  . SER   B 1 80  ? 40.263 -14.683 1.147   1.00 14.92 ?  80  SER   B HB2  1 
ATOM   5066 H  HB3  . SER   B 1 80  ? 38.996 -15.462 1.704   1.00 14.92 ?  80  SER   B HB3  1 
ATOM   5067 H  HG   . SER   B 1 80  ? 37.949 -13.530 1.710   1.00 16.01 ?  80  SER   B HG   1 
ATOM   5068 N  N    . CYS   B 1 81  ? 41.704 -12.782 2.634   1.00 11.75 ?  81  CYS   B N    1 
ATOM   5069 C  CA   . CYS   B 1 81  ? 42.251 -11.469 2.325   1.00 11.95 ?  81  CYS   B CA   1 
ATOM   5070 C  C    . CYS   B 1 81  ? 43.025 -11.552 1.020   1.00 11.43 ?  81  CYS   B C    1 
ATOM   5071 O  O    . CYS   B 1 81  ? 43.539 -12.614 0.647   1.00 12.27 ?  81  CYS   B O    1 
ATOM   5072 C  CB   . CYS   B 1 81  ? 43.138 -10.916 3.449   1.00 12.68 ?  81  CYS   B CB   1 
ATOM   5073 S  SG   . CYS   B 1 81  ? 44.653 -11.854 3.706   1.00 13.04 ?  81  CYS   B SG   1 
ATOM   5074 H  H    . CYS   B 1 81  ? 42.217 -13.438 2.406   1.00 14.10 ?  81  CYS   B H    1 
ATOM   5075 H  HA   . CYS   B 1 81  ? 41.517 -10.849 2.202   1.00 14.34 ?  81  CYS   B HA   1 
ATOM   5076 H  HB2  . CYS   B 1 81  ? 43.388 -10.004 3.232   1.00 15.22 ?  81  CYS   B HB2  1 
ATOM   5077 H  HB3  . CYS   B 1 81  ? 42.633 -10.924 4.282   1.00 15.22 ?  81  CYS   B HB3  1 
ATOM   5078 H  HG   . CYS   B 1 81  ? 45.276 -11.349 4.608   1.00 15.65 ?  81  CYS   B HG   1 
ATOM   5079 N  N    . VAL   B 1 82  ? 43.117 -10.411 0.341   1.00 11.79 ?  82  VAL   B N    1 
ATOM   5080 C  CA   . VAL   B 1 82  ? 43.883 -10.283 -0.896  1.00 12.01 ?  82  VAL   B CA   1 
ATOM   5081 C  C    . VAL   B 1 82  ? 45.222 -9.641  -0.571  1.00 12.20 ?  82  VAL   B C    1 
ATOM   5082 O  O    . VAL   B 1 82  ? 45.271 -8.523  -0.038  1.00 12.88 ?  82  VAL   B O    1 
ATOM   5083 C  CB   . VAL   B 1 82  ? 43.140 -9.440  -1.941  1.00 13.06 ?  82  VAL   B CB   1 
ATOM   5084 C  CG1  . VAL   B 1 82  ? 43.991 -9.283  -3.192  1.00 14.43 ?  82  VAL   B CG1  1 
ATOM   5085 C  CG2  . VAL   B 1 82  ? 41.786 -10.037 -2.263  1.00 13.64 ?  82  VAL   B CG2  1 
ATOM   5086 H  H    . VAL   B 1 82  ? 42.730 -9.677  0.581   1.00 14.15 ?  82  VAL   B H    1 
ATOM   5087 H  HA   . VAL   B 1 82  ? 44.046 -11.164 -1.265  1.00 14.41 ?  82  VAL   B HA   1 
ATOM   5088 H  HB   . VAL   B 1 82  ? 42.989 -8.559  -1.575  1.00 15.67 ?  82  VAL   B HB   1 
ATOM   5089 H  HG11 . VAL   B 1 82  ? 43.429 -8.973  -3.919  1.00 17.32 ?  82  VAL   B HG11 1 
ATOM   5090 H  HG12 . VAL   B 1 82  ? 44.692 -8.632  -3.020  1.00 17.32 ?  82  VAL   B HG12 1 
ATOM   5091 H  HG13 . VAL   B 1 82  ? 44.384 -10.140 -3.421  1.00 17.32 ?  82  VAL   B HG13 1 
ATOM   5092 H  HG21 . VAL   B 1 82  ? 41.358 -9.500  -2.951  1.00 16.37 ?  82  VAL   B HG21 1 
ATOM   5093 H  HG22 . VAL   B 1 82  ? 41.903 -10.946 -2.583  1.00 16.37 ?  82  VAL   B HG22 1 
ATOM   5094 H  HG23 . VAL   B 1 82  ? 41.238 -10.038 -1.461  1.00 16.37 ?  82  VAL   B HG23 1 
ATOM   5095 N  N    . LEU   B 1 83  ? 46.305 -10.328 -0.928  1.00 11.69 ?  83  LEU   B N    1 
ATOM   5096 C  CA   . LEU   B 1 83  ? 47.663 -9.810  -0.805  1.00 11.62 ?  83  LEU   B CA   1 
ATOM   5097 C  C    . LEU   B 1 83  ? 48.367 -9.944  -2.155  1.00 11.54 ?  83  LEU   B C    1 
ATOM   5098 O  O    . LEU   B 1 83  ? 47.769 -10.360 -3.155  1.00 11.85 ?  83  LEU   B O    1 
ATOM   5099 C  CB   . LEU   B 1 83  ? 48.412 -10.494 0.347   1.00 12.21 ?  83  LEU   B CB   1 
ATOM   5100 C  CG   . LEU   B 1 83  ? 47.900 -10.130 1.745   1.00 13.40 ?  83  LEU   B CG   1 
ATOM   5101 C  CD1  . LEU   B 1 83  ? 48.521 -11.000 2.820   1.00 14.12 ?  83  LEU   B CD1  1 
ATOM   5102 C  CD2  . LEU   B 1 83  ? 48.109 -8.649  2.066   1.00 14.58 ?  83  LEU   B CD2  1 
ATOM   5103 H  H    . LEU   B 1 83  ? 46.273 -11.125 -1.255  1.00 14.03 ?  83  LEU   B H    1 
ATOM   5104 H  HA   . LEU   B 1 83  ? 47.615 -8.870  -0.602  1.00 13.94 ?  83  LEU   B HA   1 
ATOM   5105 H  HB2  . LEU   B 1 83  ? 48.331 -11.454 0.249   1.00 14.65 ?  83  LEU   B HB2  1 
ATOM   5106 H  HB3  . LEU   B 1 83  ? 49.349 -10.241 0.302   1.00 14.65 ?  83  LEU   B HB3  1 
ATOM   5107 H  HG   . LEU   B 1 83  ? 46.948 -10.287 1.762   1.00 16.08 ?  83  LEU   B HG   1 
ATOM   5108 H  HD11 . LEU   B 1 83  ? 48.159 -10.740 3.683   1.00 16.94 ?  83  LEU   B HD11 1 
ATOM   5109 H  HD12 . LEU   B 1 83  ? 48.297 -11.928 2.637   1.00 16.94 ?  83  LEU   B HD12 1 
ATOM   5110 H  HD13 . LEU   B 1 83  ? 49.481 -10.884 2.813   1.00 16.94 ?  83  LEU   B HD13 1 
ATOM   5111 H  HD21 . LEU   B 1 83  ? 47.910 -8.501  3.004   1.00 17.49 ?  83  LEU   B HD21 1 
ATOM   5112 H  HD22 . LEU   B 1 83  ? 49.029 -8.410  1.880   1.00 17.49 ?  83  LEU   B HD22 1 
ATOM   5113 H  HD23 . LEU   B 1 83  ? 47.510 -8.119  1.515   1.00 17.49 ?  83  LEU   B HD23 1 
ATOM   5114 N  N    . SER   B 1 84  ? 49.644 -9.578  -2.199  1.00 12.51 ?  84  SER   B N    1 
ATOM   5115 C  CA   . SER   B 1 84  ? 50.378 -9.683  -3.450  1.00 12.89 ?  84  SER   B CA   1 
ATOM   5116 C  C    . SER   B 1 84  ? 50.529 -11.139 -3.876  1.00 12.14 ?  84  SER   B C    1 
ATOM   5117 O  O    . SER   B 1 84  ? 50.642 -12.047 -3.051  1.00 11.96 ?  84  SER   B O    1 
ATOM   5118 C  CB   . SER   B 1 84  ? 51.773 -9.080  -3.299  1.00 14.87 ?  84  SER   B CB   1 
ATOM   5119 O  OG   . SER   B 1 84  ? 52.525 -9.290  -4.477  1.00 16.39 ?  84  SER   B OG   1 
ATOM   5120 H  H    . SER   B 1 84  ? 50.097 -9.255  -1.537  1.00 15.01 ?  84  SER   B H    1 
ATOM   5121 H  HA   . SER   B 1 84  ? 49.907 -9.200  -4.148  1.00 15.47 ?  84  SER   B HA   1 
ATOM   5122 H  HB2  . SER   B 1 84  ? 51.692 -8.125  -3.126  1.00 17.84 ?  84  SER   B HB2  1 
ATOM   5123 H  HB3  . SER   B 1 84  ? 52.231 -9.511  -2.562  1.00 17.84 ?  84  SER   B HB3  1 
ATOM   5124 H  HG   . SER   B 1 84  ? 53.288 -8.936  -4.401  1.00 19.67 ?  84  SER   B HG   1 
ATOM   5125 N  N    . GLY   B 1 85  ? 50.591 -11.347 -5.186  1.00 13.08 ?  85  GLY   B N    1 
ATOM   5126 C  CA   . GLY   B 1 85  ? 50.934 -12.634 -5.744  1.00 13.79 ?  85  GLY   B CA   1 
ATOM   5127 C  C    . GLY   B 1 85  ? 52.405 -12.839 -6.040  1.00 13.19 ?  85  GLY   B C    1 
ATOM   5128 O  O    . GLY   B 1 85  ? 52.781 -13.921 -6.496  1.00 13.37 ?  85  GLY   B O    1 
ATOM   5129 H  H    . GLY   B 1 85  ? 50.444 -10.748 -5.778  1.00 15.70 ?  85  GLY   B H    1 
ATOM   5130 H  HA2  . GLY   B 1 85  ? 50.660 -13.331 -5.126  1.00 16.55 ?  85  GLY   B HA2  1 
ATOM   5131 H  HA3  . GLY   B 1 85  ? 50.450 -12.761 -6.570  1.00 16.55 ?  85  GLY   B HA3  1 
ATOM   5132 N  N    . HIS   B 1 86  ? 53.261 -11.847 -5.802  1.00 13.03 ?  86  HIS   B N    1 
ATOM   5133 C  CA   . HIS   B 1 86  ? 54.723 -12.023 -5.882  1.00 12.94 ?  86  HIS   B CA   1 
ATOM   5134 C  C    . HIS   B 1 86  ? 55.095 -12.527 -7.275  1.00 13.07 ?  86  HIS   B C    1 
ATOM   5135 O  O    . HIS   B 1 86  ? 54.706 -11.906 -8.276  1.00 14.09 ?  86  HIS   B O    1 
ATOM   5136 C  CB   . HIS   B 1 86  ? 55.215 -12.867 -4.709  1.00 13.25 ?  86  HIS   B CB   1 
ATOM   5137 C  CG   . HIS   B 1 86  ? 54.903 -12.262 -3.382  1.00 13.27 ?  86  HIS   B CG   1 
ATOM   5138 N  ND1  . HIS   B 1 86  ? 55.733 -11.353 -2.762  1.00 14.71 ?  86  HIS   B ND1  1 
ATOM   5139 C  CD2  . HIS   B 1 86  ? 53.824 -12.404 -2.576  1.00 13.44 ?  86  HIS   B CD2  1 
ATOM   5140 C  CE1  . HIS   B 1 86  ? 55.177 -10.965 -1.628  1.00 14.63 ?  86  HIS   B CE1  1 
ATOM   5141 N  NE2  . HIS   B 1 86  ? 54.017 -11.585 -1.493  1.00 13.84 ?  86  HIS   B NE2  1 
ATOM   5142 H  H    . HIS   B 1 86  ? 53.027 -11.049 -5.594  1.00 15.63 ?  86  HIS   B H    1 
ATOM   5143 H  HA   . HIS   B 1 86  ? 55.135 -11.153 -5.786  1.00 15.52 ?  86  HIS   B HA   1 
ATOM   5144 H  HB2  . HIS   B 1 86  ? 54.800 -13.739 -4.748  1.00 15.90 ?  86  HIS   B HB2  1 
ATOM   5145 H  HB3  . HIS   B 1 86  ? 56.183 -12.957 -4.769  1.00 15.90 ?  86  HIS   B HB3  1 
ATOM   5146 H  HD2  . HIS   B 1 86  ? 53.077 -12.941 -2.738  1.00 16.12 ?  86  HIS   B HD2  1 
ATOM   5147 H  HE1  . HIS   B 1 86  ? 55.546 -10.369 -1.019  1.00 17.55 ?  86  HIS   B HE1  1 
ATOM   5148 H  HE2  . HIS   B 1 86  ? 53.475 -11.501 -0.828  1.00 16.60 ?  86  HIS   B HE2  1 
ATOM   5149 N  N    . ASN   B 1 87  ? 55.864 -13.609 -7.389  1.00 13.71 ?  87  ASN   B N    1 
ATOM   5150 C  CA   . ASN   B 1 87  ? 56.256 -14.178 -8.671  1.00 14.41 ?  87  ASN   B CA   1 
ATOM   5151 C  C    . ASN   B 1 87  ? 55.275 -15.228 -9.170  1.00 13.92 ?  87  ASN   B C    1 
ATOM   5152 O  O    . ASN   B 1 87  ? 55.590 -15.948 -10.124 1.00 15.67 ?  87  ASN   B O    1 
ATOM   5153 C  CB   . ASN   B 1 87  ? 57.654 -14.797 -8.558  1.00 16.05 ?  87  ASN   B CB   1 
ATOM   5154 C  CG   . ASN   B 1 87  ? 57.719 -15.910 -7.518  1.00 16.98 ?  87  ASN   B CG   1 
ATOM   5155 O  OD1  . ASN   B 1 87  ? 57.072 -15.840 -6.467  1.00 16.14 ?  87  ASN   B OD1  1 
ATOM   5156 N  ND2  . ASN   B 1 87  ? 58.477 -16.964 -7.826  1.00 19.27 ?  87  ASN   B ND2  1 
ATOM   5157 H  H    . ASN   B 1 87  ? 56.179 -14.049 -6.717  1.00 16.45 ?  87  ASN   B H    1 
ATOM   5158 H  HA   . ASN   B 1 87  ? 56.296 -13.469 -9.328  1.00 17.29 ?  87  ASN   B HA   1 
ATOM   5159 H  HB2  . ASN   B 1 87  ? 57.904 -15.172 -9.420  1.00 19.27 ?  87  ASN   B HB2  1 
ATOM   5160 H  HB3  . ASN   B 1 87  ? 58.285 -14.109 -8.301  1.00 19.27 ?  87  ASN   B HB3  1 
ATOM   5161 H  HD21 . ASN   B 1 87  ? 58.548 -17.618 -7.275  1.00 23.12 ?  87  ASN   B HD21 1 
ATOM   5162 H  HD22 . ASN   B 1 87  ? 58.908 -16.982 -8.573  1.00 23.12 ?  87  ASN   B HD22 1 
ATOM   5163 N  N    . LEU   B 1 88  ? 54.095 -15.324 -8.555  1.00 12.87 ?  88  LEU   B N    1 
ATOM   5164 C  CA   . LEU   B 1 88  ? 53.116 -16.359 -8.873  1.00 13.39 ?  88  LEU   B CA   1 
ATOM   5165 C  C    . LEU   B 1 88  ? 51.881 -15.845 -9.592  1.00 12.97 ?  88  LEU   B C    1 
ATOM   5166 O  O    . LEU   B 1 88  ? 51.275 -16.597 -10.362 1.00 14.52 ?  88  LEU   B O    1 
ATOM   5167 C  CB   . LEU   B 1 88  ? 52.651 -17.048 -7.585  1.00 13.97 ?  88  LEU   B CB   1 
ATOM   5168 C  CG   . LEU   B 1 88  ? 53.772 -17.698 -6.784  1.00 16.40 ?  88  LEU   B CG   1 
ATOM   5169 C  CD1  . LEU   B 1 88  ? 53.263 -18.107 -5.412  1.00 17.95 ?  88  LEU   B CD1  1 
ATOM   5170 C  CD2  . LEU   B 1 88  ? 54.312 -18.893 -7.540  1.00 19.16 ?  88  LEU   B CD2  1 
ATOM   5171 H  H    . LEU   B 1 88  ? 53.835 -14.790 -7.927  1.00 15.45 ?  88  LEU   B H    1 
ATOM   5172 H  HA   . LEU   B 1 88  ? 53.533 -17.022 -9.436  1.00 16.07 ?  88  LEU   B HA   1 
ATOM   5173 H  HB2  . LEU   B 1 88  ? 52.224 -16.392 -7.012  1.00 16.77 ?  88  LEU   B HB2  1 
ATOM   5174 H  HB3  . LEU   B 1 88  ? 52.015 -17.743 -7.817  1.00 16.77 ?  88  LEU   B HB3  1 
ATOM   5175 H  HG   . LEU   B 1 88  ? 54.493 -17.061 -6.663  1.00 19.68 ?  88  LEU   B HG   1 
ATOM   5176 H  HD11 . LEU   B 1 88  ? 53.950 -18.621 -4.959  1.00 21.54 ?  88  LEU   B HD11 1 
ATOM   5177 H  HD12 . LEU   B 1 88  ? 53.053 -17.310 -4.901  1.00 21.54 ?  88  LEU   B HD12 1 
ATOM   5178 H  HD13 . LEU   B 1 88  ? 52.465 -18.648 -5.524  1.00 21.54 ?  88  LEU   B HD13 1 
ATOM   5179 H  HD21 . LEU   B 1 88  ? 54.944 -19.363 -6.975  1.00 22.99 ?  88  LEU   B HD21 1 
ATOM   5180 H  HD22 . LEU   B 1 88  ? 53.575 -19.478 -7.772  1.00 22.99 ?  88  LEU   B HD22 1 
ATOM   5181 H  HD23 . LEU   B 1 88  ? 54.756 -18.583 -8.345  1.00 22.99 ?  88  LEU   B HD23 1 
ATOM   5182 N  N    . ALA   B 1 89  ? 51.482 -14.604 -9.341  1.00 12.11 ?  89  ALA   B N    1 
ATOM   5183 C  CA   . ALA   B 1 89  ? 50.182 -14.115 -9.775  1.00 11.81 ?  89  ALA   B CA   1 
ATOM   5184 C  C    . ALA   B 1 89  ? 50.155 -12.621 -9.506  1.00 12.45 ?  89  ALA   B C    1 
ATOM   5185 O  O    . ALA   B 1 89  ? 50.999 -12.096 -8.779  1.00 13.22 ?  89  ALA   B O    1 
ATOM   5186 C  CB   . ALA   B 1 89  ? 49.053 -14.784 -8.996  1.00 12.33 ?  89  ALA   B CB   1 
ATOM   5187 H  H    . ALA   B 1 89  ? 51.942 -14.016 -8.910  1.00 14.54 ?  89  ALA   B H    1 
ATOM   5188 H  HA   . ALA   B 1 89  ? 50.051 -14.273 -10.724 1.00 14.18 ?  89  ALA   B HA   1 
ATOM   5189 H  HB1  . ALA   B 1 89  ? 48.198 -14.448 -9.318  1.00 14.79 ?  89  ALA   B HB1  1 
ATOM   5190 H  HB2  . ALA   B 1 89  ? 49.099 -15.744 -9.135  1.00 14.79 ?  89  ALA   B HB2  1 
ATOM   5191 H  HB3  . ALA   B 1 89  ? 49.152 -14.580 -8.054  1.00 14.79 ?  89  ALA   B HB3  1 
ATOM   5192 N  N    . LYS   B 1 90  ? 49.152 -11.936 -10.060 1.00 13.23 ?  90  LYS   B N    1 
ATOM   5193 C  CA   . LYS   B 1 90  ? 48.961 -10.547 -9.660  1.00 13.42 ?  90  LYS   B CA   1 
ATOM   5194 C  C    . LYS   B 1 90  ? 48.647 -10.470 -8.171  1.00 13.10 ?  90  LYS   B C    1 
ATOM   5195 O  O    . LYS   B 1 90  ? 49.290 -9.719  -7.422  1.00 14.52 ?  90  LYS   B O    1 
ATOM   5196 C  CB   . LYS   B 1 90  ? 47.879 -9.883  -10.513 1.00 14.82 ?  90  LYS   B CB   1 
ATOM   5197 C  CG   . LYS   B 1 90  ? 47.596 -8.433  -10.145 1.00 15.59 ?  90  LYS   B CG   1 
ATOM   5198 C  CD   . LYS   B 1 90  ? 48.814 -7.556  -10.246 1.00 18.84 ?  90  LYS   B CD   1 
ATOM   5199 C  CE   . LYS   B 1 90  ? 48.397 -6.118  -10.052 1.00 21.27 ?  90  LYS   B CE   1 
ATOM   5200 N  NZ   . LYS   B 1 90  ? 49.560 -5.213  -9.921  1.00 21.66 ?  90  LYS   B NZ   1 
ATOM   5201 H  H    . LYS   B 1 90  ? 48.588 -12.242 -10.636 1.00 15.88 ?  90  LYS   B H    1 
ATOM   5202 H  HA   . LYS   B 1 90  ? 49.786 -10.071 -9.809  1.00 16.10 ?  90  LYS   B HA   1 
ATOM   5203 H  HB2  . LYS   B 1 90  ? 48.163 -9.900  -11.444 1.00 17.79 ?  90  LYS   B HB2  1 
ATOM   5204 H  HB3  . LYS   B 1 90  ? 47.051 -10.381 -10.420 1.00 17.79 ?  90  LYS   B HB3  1 
ATOM   5205 H  HG2  . LYS   B 1 90  ? 46.921 -8.079  -10.748 1.00 18.71 ?  90  LYS   B HG2  1 
ATOM   5206 H  HG3  . LYS   B 1 90  ? 47.269 -8.394  -9.231  1.00 18.71 ?  90  LYS   B HG3  1 
ATOM   5207 H  HD2  . LYS   B 1 90  ? 49.450 -7.793  -9.551  1.00 22.61 ?  90  LYS   B HD2  1 
ATOM   5208 H  HD3  . LYS   B 1 90  ? 49.216 -7.651  -11.124 1.00 22.61 ?  90  LYS   B HD3  1 
ATOM   5209 H  HE2  . LYS   B 1 90  ? 47.880 -5.824  -10.821 1.00 25.52 ?  90  LYS   B HE2  1 
ATOM   5210 H  HE3  . LYS   B 1 90  ? 47.868 -6.038  -9.244  1.00 25.52 ?  90  LYS   B HE3  1 
ATOM   5211 H  HZ1  . LYS   B 1 90  ? 49.289 -4.370  -9.810  1.00 25.99 ?  90  LYS   B HZ1  1 
ATOM   5212 H  HZ2  . LYS   B 1 90  ? 50.057 -5.448  -9.220  1.00 25.99 ?  90  LYS   B HZ2  1 
ATOM   5213 H  HZ3  . LYS   B 1 90  ? 50.067 -5.253  -10.655 1.00 25.99 ?  90  LYS   B HZ3  1 
ATOM   5214 N  N    . HIS   B 1 91  ? 47.698 -11.294 -7.720  1.00 11.94 ?  91  HIS   B N    1 
ATOM   5215 C  CA   . HIS   B 1 91  ? 47.230 -11.312 -6.347  1.00 12.18 ?  91  HIS   B CA   1 
ATOM   5216 C  C    . HIS   B 1 91  ? 47.232 -12.739 -5.829  1.00 11.39 ?  91  HIS   B C    1 
ATOM   5217 O  O    . HIS   B 1 91  ? 47.011 -13.695 -6.584  1.00 11.72 ?  91  HIS   B O    1 
ATOM   5218 C  CB   . HIS   B 1 91  ? 45.776 -10.836 -6.237  1.00 13.68 ?  91  HIS   B CB   1 
ATOM   5219 C  CG   . HIS   B 1 91  ? 45.559 -9.431  -6.683  1.00 16.71 ?  91  HIS   B CG   1 
ATOM   5220 N  ND1  . HIS   B 1 91  ? 46.145 -8.348  -6.063  1.00 19.20 ?  91  HIS   B ND1  1 
ATOM   5221 C  CD2  . HIS   B 1 91  ? 44.791 -8.927  -7.674  1.00 18.98 ?  91  HIS   B CD2  1 
ATOM   5222 C  CE1  . HIS   B 1 91  ? 45.763 -7.235  -6.666  1.00 20.01 ?  91  HIS   B CE1  1 
ATOM   5223 N  NE2  . HIS   B 1 91  ? 44.936 -7.560  -7.645  1.00 20.15 ?  91  HIS   B NE2  1 
ATOM   5224 H  H    . HIS   B 1 91  ? 47.299 -11.880 -8.212  1.00 14.33 ?  91  HIS   B H    1 
ATOM   5225 H  HA   . HIS   B 1 91  ? 47.801 -10.752 -5.787  1.00 14.62 ?  91  HIS   B HA   1 
ATOM   5226 H  HB2  . HIS   B 1 91  ? 45.220 -11.407 -6.786  1.00 16.42 ?  91  HIS   B HB2  1 
ATOM   5227 H  HB3  . HIS   B 1 91  ? 45.497 -10.896 -5.309  1.00 16.42 ?  91  HIS   B HB3  1 
ATOM   5228 H  HD1  . HIS   B 1 91  ? 46.685 -8.390  -5.393  1.00 23.04 ?  91  HIS   B HD1  1 
ATOM   5229 H  HD2  . HIS   B 1 91  ? 44.268 -9.405  -8.270  1.00 22.78 ?  91  HIS   B HD2  1 
ATOM   5230 H  HE1  . HIS   B 1 91  ? 46.028 -6.371  -6.433  1.00 24.01 ?  91  HIS   B HE1  1 
ATOM   5231 N  N    . CYS   B 1 92  ? 47.429 -12.873 -4.524  1.00 10.96 ?  92  CYS   B N    1 
ATOM   5232 C  CA   . CYS   B 1 92  ? 47.133 -14.110 -3.815  1.00 10.72 ?  92  CYS   B CA   1 
ATOM   5233 C  C    . CYS   B 1 92  ? 45.915 -13.875 -2.932  1.00 10.50 ?  92  CYS   B C    1 
ATOM   5234 O  O    . CYS   B 1 92  ? 45.915 -12.972 -2.084  1.00 11.51 ?  92  CYS   B O    1 
ATOM   5235 C  CB   . CYS   B 1 92  ? 48.311 -14.566 -2.960  1.00 11.33 ?  92  CYS   B CB   1 
ATOM   5236 S  SG   . CYS   B 1 92  ? 47.955 -16.103 -2.064  1.00 11.34 ?  92  CYS   B SG   1 
ATOM   5237 H  H    . CYS   B 1 92  ? 47.749 -12.250 -4.014  1.00 13.16 ?  92  CYS   B H    1 
ATOM   5238 H  HA   . CYS   B 1 92  ? 46.936 -14.806 -4.461  1.00 12.87 ?  92  CYS   B HA   1 
ATOM   5239 H  HB2  . CYS   B 1 92  ? 49.082 -14.712 -3.526  1.00 13.59 ?  92  CYS   B HB2  1 
ATOM   5240 H  HB3  . CYS   B 1 92  ? 48.507 -13.875 -2.303  1.00 13.59 ?  92  CYS   B HB3  1 
ATOM   5241 H  HG   . CYS   B 1 92  ? 48.927 -16.422 -1.434  1.00 13.61 ?  92  CYS   B HG   1 
ATOM   5242 N  N    . LEU   B 1 93  ? 44.878 -14.683 -3.145  1.00 10.58 ?  93  LEU   B N    1 
ATOM   5243 C  CA   . LEU   B 1 93  ? 43.701 -14.698 -2.288  1.00 10.56 ?  93  LEU   B CA   1 
ATOM   5244 C  C    . LEU   B 1 93  ? 43.925 -15.765 -1.225  1.00 10.29 ?  93  LEU   B C    1 
ATOM   5245 O  O    . LEU   B 1 93  ? 43.876 -16.964 -1.523  1.00 11.05 ?  93  LEU   B O    1 
ATOM   5246 C  CB   . LEU   B 1 93  ? 42.438 -14.996 -3.094  1.00 11.33 ?  93  LEU   B CB   1 
ATOM   5247 C  CG   . LEU   B 1 93  ? 41.140 -15.016 -2.287  1.00 11.64 ?  93  LEU   B CG   1 
ATOM   5248 C  CD1  . LEU   B 1 93  ? 40.787 -13.628 -1.793  1.00 11.94 ?  93  LEU   B CD1  1 
ATOM   5249 C  CD2  . LEU   B 1 93  ? 40.005 -15.605 -3.116  1.00 12.16 ?  93  LEU   B CD2  1 
ATOM   5250 H  H    . LEU   B 1 93  ? 44.838 -15.257 -3.797  1.00 12.69 ?  93  LEU   B H    1 
ATOM   5251 H  HA   . LEU   B 1 93  ? 43.603 -13.836 -1.859  1.00 12.67 ?  93  LEU   B HA   1 
ATOM   5252 H  HB2  . LEU   B 1 93  ? 42.341 -14.313 -3.778  1.00 13.59 ?  93  LEU   B HB2  1 
ATOM   5253 H  HB3  . LEU   B 1 93  ? 42.538 -15.863 -3.516  1.00 13.59 ?  93  LEU   B HB3  1 
ATOM   5254 H  HG   . LEU   B 1 93  ? 41.260 -15.591 -1.515  1.00 13.96 ?  93  LEU   B HG   1 
ATOM   5255 H  HD11 . LEU   B 1 93  ? 39.929 -13.662 -1.346  1.00 14.32 ?  93  LEU   B HD11 1 
ATOM   5256 H  HD12 . LEU   B 1 93  ? 41.474 -13.330 -1.178  1.00 14.32 ?  93  LEU   B HD12 1 
ATOM   5257 H  HD13 . LEU   B 1 93  ? 40.741 -13.028 -2.556  1.00 14.32 ?  93  LEU   B HD13 1 
ATOM   5258 H  HD21 . LEU   B 1 93  ? 39.196 -15.606 -2.584  1.00 14.59 ?  93  LEU   B HD21 1 
ATOM   5259 H  HD22 . LEU   B 1 93  ? 39.881 -15.059 -3.909  1.00 14.59 ?  93  LEU   B HD22 1 
ATOM   5260 H  HD23 . LEU   B 1 93  ? 40.235 -16.512 -3.373  1.00 14.59 ?  93  LEU   B HD23 1 
ATOM   5261 N  N    . HIS   B 1 94  ? 44.203 -15.331 -0.000  1.00 10.36 ?  94  HIS   B N    1 
ATOM   5262 C  CA   . HIS   B 1 94  ? 44.421 -16.234 1.122   1.00 10.49 ?  94  HIS   B CA   1 
ATOM   5263 C  C    . HIS   B 1 94  ? 43.058 -16.590 1.697   1.00 10.85 ?  94  HIS   B C    1 
ATOM   5264 O  O    . HIS   B 1 94  ? 42.384 -15.720 2.249   1.00 12.13 ?  94  HIS   B O    1 
ATOM   5265 C  CB   . HIS   B 1 94  ? 45.291 -15.548 2.174   1.00 10.99 ?  94  HIS   B CB   1 
ATOM   5266 C  CG   . HIS   B 1 94  ? 46.675 -15.246 1.702   1.00 10.97 ?  94  HIS   B CG   1 
ATOM   5267 N  ND1  . HIS   B 1 94  ? 47.702 -16.160 1.788   1.00 11.22 ?  94  HIS   B ND1  1 
ATOM   5268 C  CD2  . HIS   B 1 94  ? 47.188 -14.138 1.116   1.00 11.13 ?  94  HIS   B CD2  1 
ATOM   5269 C  CE1  . HIS   B 1 94  ? 48.792 -15.614 1.279   1.00 11.41 ?  94  HIS   B CE1  1 
ATOM   5270 N  NE2  . HIS   B 1 94  ? 48.509 -14.389 0.864   1.00 11.53 ?  94  HIS   B NE2  1 
ATOM   5271 H  H    . HIS   B 1 94  ? 44.264 -14.496 0.210   1.00 12.43 ?  94  HIS   B H    1 
ATOM   5272 H  HA   . HIS   B 1 94  ? 44.860 -17.044 0.814   1.00 12.59 ?  94  HIS   B HA   1 
ATOM   5273 H  HB2  . HIS   B 1 94  ? 44.876 -14.716 2.427   1.00 13.19 ?  94  HIS   B HB2  1 
ATOM   5274 H  HB3  . HIS   B 1 94  ? 45.363 -16.136 2.943   1.00 13.19 ?  94  HIS   B HB3  1 
ATOM   5275 H  HD2  . HIS   B 1 94  ? 46.732 -13.357 0.920   1.00 13.35 ?  94  HIS   B HD2  1 
ATOM   5276 H  HE1  . HIS   B 1 94  ? 49.626 -16.031 1.224   1.00 13.70 ?  94  HIS   B HE1  1 
ATOM   5277 H  HE2  . HIS   B 1 94  ? 49.067 -13.849 0.503   1.00 13.84 ?  94  HIS   B HE2  1 
ATOM   5278 N  N    . VAL   B 1 95  ? 42.629 -17.844 1.544   1.00 10.82 ?  95  VAL   B N    1 
ATOM   5279 C  CA   . VAL   B 1 95  ? 41.303 -18.285 1.975   1.00 11.05 ?  95  VAL   B CA   1 
ATOM   5280 C  C    . VAL   B 1 95  ? 41.471 -19.321 3.069   1.00 11.34 ?  95  VAL   B C    1 
ATOM   5281 O  O    . VAL   B 1 95  ? 42.243 -20.274 2.912   1.00 11.84 ?  95  VAL   B O    1 
ATOM   5282 C  CB   . VAL   B 1 95  ? 40.486 -18.889 0.816   1.00 11.10 ?  95  VAL   B CB   1 
ATOM   5283 C  CG1  . VAL   B 1 95  ? 39.112 -19.333 1.303   1.00 12.72 ?  95  VAL   B CG1  1 
ATOM   5284 C  CG2  . VAL   B 1 95  ? 40.360 -17.903 -0.325  1.00 11.52 ?  95  VAL   B CG2  1 
ATOM   5285 H  H    . VAL   B 1 95  ? 43.091 -18.472 1.182   1.00 12.99 ?  95  VAL   B H    1 
ATOM   5286 H  HA   . VAL   B 1 95  ? 40.809 -17.532 2.341   1.00 13.26 ?  95  VAL   B HA   1 
ATOM   5287 H  HB   . VAL   B 1 95  ? 40.946 -19.669 0.484   1.00 13.32 ?  95  VAL   B HB   1 
ATOM   5288 H  HG11 . VAL   B 1 95  ? 38.548 -19.531 0.532   1.00 15.26 ?  95  VAL   B HG11 1 
ATOM   5289 H  HG12 . VAL   B 1 95  ? 39.202 -20.132 1.848   1.00 15.26 ?  95  VAL   B HG12 1 
ATOM   5290 H  HG13 . VAL   B 1 95  ? 38.705 -18.623 1.825   1.00 15.26 ?  95  VAL   B HG13 1 
ATOM   5291 H  HG21 . VAL   B 1 95  ? 39.778 -18.285 -1.004  1.00 13.82 ?  95  VAL   B HG21 1 
ATOM   5292 H  HG22 . VAL   B 1 95  ? 39.970 -17.079 0.012   1.00 13.82 ?  95  VAL   B HG22 1 
ATOM   5293 H  HG23 . VAL   B 1 95  ? 41.235 -17.734 -0.692  1.00 13.82 ?  95  VAL   B HG23 1 
ATOM   5294 N  N    . VAL   B 1 96  ? 40.730 -19.154 4.162   1.00 11.63 ?  96  VAL   B N    1 
ATOM   5295 C  CA   . VAL   B 1 96  ? 40.812 -20.069 5.301   1.00 11.93 ?  96  VAL   B CA   1 
ATOM   5296 C  C    . VAL   B 1 96  ? 39.623 -21.026 5.250   1.00 12.16 ?  96  VAL   B C    1 
ATOM   5297 O  O    . VAL   B 1 96  ? 38.502 -20.673 5.622   1.00 13.25 ?  96  VAL   B O    1 
ATOM   5298 C  CB   . VAL   B 1 96  ? 40.865 -19.325 6.638   1.00 12.81 ?  96  VAL   B CB   1 
ATOM   5299 C  CG1  . VAL   B 1 96  ? 41.051 -20.324 7.779   1.00 13.45 ?  96  VAL   B CG1  1 
ATOM   5300 C  CG2  . VAL   B 1 96  ? 41.971 -18.274 6.646   1.00 13.12 ?  96  VAL   B CG2  1 
ATOM   5301 H  H    . VAL   B 1 96  ? 40.167 -18.516 4.273   1.00 13.96 ?  96  VAL   B H    1 
ATOM   5302 H  HA   . VAL   B 1 96  ? 41.620 -20.597 5.226   1.00 14.32 ?  96  VAL   B HA   1 
ATOM   5303 H  HB   . VAL   B 1 96  ? 40.021 -18.869 6.783   1.00 15.37 ?  96  VAL   B HB   1 
ATOM   5304 H  HG11 . VAL   B 1 96  ? 41.237 -19.836 8.600   1.00 16.14 ?  96  VAL   B HG11 1 
ATOM   5305 H  HG12 . VAL   B 1 96  ? 40.245 -20.848 7.883   1.00 16.14 ?  96  VAL   B HG12 1 
ATOM   5306 H  HG13 . VAL   B 1 96  ? 41.803 -20.905 7.571   1.00 16.14 ?  96  VAL   B HG13 1 
ATOM   5307 H  HG21 . VAL   B 1 96  ? 42.018 -17.870 7.530   1.00 15.75 ?  96  VAL   B HG21 1 
ATOM   5308 H  HG22 . VAL   B 1 96  ? 42.814 -18.698 6.432   1.00 15.75 ?  96  VAL   B HG22 1 
ATOM   5309 H  HG23 . VAL   B 1 96  ? 41.764 -17.592 5.986   1.00 15.75 ?  96  VAL   B HG23 1 
ATOM   5310 N  N    . GLY   B 1 97  ? 39.863 -22.257 4.816   1.00 12.14 ?  97  GLY   B N    1 
ATOM   5311 C  CA   . GLY   B 1 97  ? 38.888 -23.312 4.966   1.00 12.95 ?  97  GLY   B CA   1 
ATOM   5312 C  C    . GLY   B 1 97  ? 39.000 -23.923 6.347   1.00 13.67 ?  97  GLY   B C    1 
ATOM   5313 O  O    . GLY   B 1 97  ? 40.036 -23.799 7.013   1.00 14.09 ?  97  GLY   B O    1 
ATOM   5314 H  H    . GLY   B 1 97  ? 40.599 -22.502 4.435   1.00 14.57 ?  97  GLY   B H    1 
ATOM   5315 H  HA2  . GLY   B 1 97  ? 37.997 -22.948 4.844   1.00 15.54 ?  97  GLY   B HA2  1 
ATOM   5316 H  HA3  . GLY   B 1 97  ? 39.041 -23.998 4.295   1.00 15.54 ?  97  GLY   B HA3  1 
ATOM   5317 N  N    . PRO   B 1 98  ? 37.954 -24.614 6.802   1.00 14.38 ?  98  PRO   B N    1 
ATOM   5318 C  CA   . PRO   B 1 98  ? 38.045 -25.306 8.091   1.00 15.13 ?  98  PRO   B CA   1 
ATOM   5319 C  C    . PRO   B 1 98  ? 39.069 -26.429 8.052   1.00 14.63 ?  98  PRO   B C    1 
ATOM   5320 O  O    . PRO   B 1 98  ? 39.182 -27.163 7.069   1.00 15.03 ?  98  PRO   B O    1 
ATOM   5321 C  CB   . PRO   B 1 98  ? 36.627 -25.852 8.296   1.00 15.46 ?  98  PRO   B CB   1 
ATOM   5322 C  CG   . PRO   B 1 98  ? 36.079 -25.996 6.918   1.00 14.98 ?  98  PRO   B CG   1 
ATOM   5323 C  CD   . PRO   B 1 98  ? 36.643 -24.817 6.162   1.00 14.60 ?  98  PRO   B CD   1 
ATOM   5324 H  HA   . PRO   B 1 98  ? 38.267 -24.682 8.797   1.00 18.16 ?  98  PRO   B HA   1 
ATOM   5325 H  HB2  . PRO   B 1 98  ? 36.672 -26.712 8.743   1.00 18.55 ?  98  PRO   B HB2  1 
ATOM   5326 H  HB3  . PRO   B 1 98  ? 36.107 -25.220 8.810   1.00 18.55 ?  98  PRO   B HB3  1 
ATOM   5327 H  HG2  . PRO   B 1 98  ? 36.386 -26.835 6.531   1.00 17.97 ?  98  PRO   B HG2  1 
ATOM   5328 H  HG3  . PRO   B 1 98  ? 35.113 -25.964 6.946   1.00 17.97 ?  98  PRO   B HG3  1 
ATOM   5329 H  HD2  . PRO   B 1 98  ? 36.747 -25.035 5.221   1.00 17.52 ?  98  PRO   B HD2  1 
ATOM   5330 H  HD3  . PRO   B 1 98  ? 36.085 -24.035 6.287   1.00 17.52 ?  98  PRO   B HD3  1 
ATOM   5331 N  N    . ASN   B 1 99  ? 39.823 -26.554 9.138   1.00 15.72 ?  99  ASN   B N    1 
ATOM   5332 C  CA   . ASN   B 1 99  ? 40.805 -27.624 9.298   1.00 16.81 ?  99  ASN   B CA   1 
ATOM   5333 C  C    . ASN   B 1 99  ? 40.172 -28.709 10.167  1.00 19.41 ?  99  ASN   B C    1 
ATOM   5334 O  O    . ASN   B 1 99  ? 40.092 -28.570 11.390  1.00 19.91 ?  99  ASN   B O    1 
ATOM   5335 C  CB   . ASN   B 1 99  ? 42.077 -27.070 9.926   1.00 16.98 ?  99  ASN   B CB   1 
ATOM   5336 C  CG   . ASN   B 1 99  ? 43.205 -28.077 9.937   1.00 17.78 ?  99  ASN   B CG   1 
ATOM   5337 O  OD1  . ASN   B 1 99  ? 42.976 -29.271 10.099  1.00 18.30 ?  99  ASN   B OD1  1 
ATOM   5338 N  ND2  . ASN   B 1 99  ? 44.428 -27.603 9.762   1.00 18.07 ?  99  ASN   B ND2  1 
ATOM   5339 H  H    . ASN   B 1 99  ? 39.789 -26.012 9.806   1.00 18.87 ?  99  ASN   B H    1 
ATOM   5340 H  HA   . ASN   B 1 99  ? 41.020 -28.005 8.432   1.00 20.17 ?  99  ASN   B HA   1 
ATOM   5341 H  HB2  . ASN   B 1 99  ? 42.368 -26.298 9.425   1.00 20.38 ?  99  ASN   B HB2  1 
ATOM   5342 H  HB3  . ASN   B 1 99  ? 41.888 -26.824 10.847  1.00 20.38 ?  99  ASN   B HB3  1 
ATOM   5343 H  HD21 . ASN   B 1 99  ? 45.102 -28.138 9.757   1.00 21.68 ?  99  ASN   B HD21 1 
ATOM   5344 H  HD22 . ASN   B 1 99  ? 44.546 -26.760 9.653   1.00 21.68 ?  99  ASN   B HD22 1 
ATOM   5345 N  N    A VAL   B 1 100 ? 39.702 -29.783 9.527   0.56 21.35 ?  100 VAL   B N    1 
ATOM   5346 N  N    B VAL   B 1 100 ? 39.714 -29.786 9.523   0.44 21.37 ?  100 VAL   B N    1 
ATOM   5347 C  CA   A VAL   B 1 100 ? 39.076 -30.877 10.268  0.56 23.94 ?  100 VAL   B CA   1 
ATOM   5348 C  CA   B VAL   B 1 100 ? 39.082 -30.887 10.247  0.44 23.77 ?  100 VAL   B CA   1 
ATOM   5349 C  C    A VAL   B 1 100 ? 40.074 -31.545 11.207  0.56 24.48 ?  100 VAL   B C    1 
ATOM   5350 C  C    B VAL   B 1 100 ? 40.070 -31.558 11.192  0.44 24.39 ?  100 VAL   B C    1 
ATOM   5351 O  O    A VAL   B 1 100 ? 39.695 -32.048 12.272  0.56 24.91 ?  100 VAL   B O    1 
ATOM   5352 O  O    B VAL   B 1 100 ? 39.681 -32.074 12.247  0.44 24.67 ?  100 VAL   B O    1 
ATOM   5353 C  CB   A VAL   B 1 100 ? 38.427 -31.886 9.298   0.56 25.96 ?  100 VAL   B CB   1 
ATOM   5354 C  CB   B VAL   B 1 100 ? 38.460 -31.887 9.250   0.44 25.49 ?  100 VAL   B CB   1 
ATOM   5355 C  CG1  A VAL   B 1 100 ? 37.940 -33.120 10.048  0.56 26.91 ?  100 VAL   B CG1  1 
ATOM   5356 C  CG1  B VAL   B 1 100 ? 37.928 -33.114 9.975   0.44 26.29 ?  100 VAL   B CG1  1 
ATOM   5357 C  CG2  A VAL   B 1 100 ? 37.275 -31.236 8.547   0.56 26.60 ?  100 VAL   B CG2  1 
ATOM   5358 C  CG2  B VAL   B 1 100 ? 37.352 -31.218 8.452   0.44 26.05 ?  100 VAL   B CG2  1 
ATOM   5359 H  H    A VAL   B 1 100 ? 39.721 -29.893 8.671   0.56 25.62 ?  100 VAL   B H    1 
ATOM   5360 H  H    B VAL   B 1 100 ? 39.752 -29.893 8.670   0.44 25.64 ?  100 VAL   B H    1 
ATOM   5361 H  HA   A VAL   B 1 100 ? 38.364 -30.506 10.811  0.56 28.73 ?  100 VAL   B HA   1 
ATOM   5362 H  HA   B VAL   B 1 100 ? 38.359 -30.527 10.782  0.44 28.53 ?  100 VAL   B HA   1 
ATOM   5363 H  HB   A VAL   B 1 100 ? 39.088 -32.172 8.651   0.56 31.15 ?  100 VAL   B HB   1 
ATOM   5364 H  HB   B VAL   B 1 100 ? 39.144 -32.182 8.628   0.44 30.59 ?  100 VAL   B HB   1 
ATOM   5365 H  HG11 A VAL   B 1 100 ? 37.354 -33.630 9.465   0.56 32.29 ?  100 VAL   B HG11 1 
ATOM   5366 H  HG11 B VAL   B 1 100 ? 37.366 -33.620 9.366   0.44 31.55 ?  100 VAL   B HG11 1 
ATOM   5367 H  HG12 A VAL   B 1 100 ? 38.703 -33.663 10.302  0.56 32.29 ?  100 VAL   B HG12 1 
ATOM   5368 H  HG12 B VAL   B 1 100 ? 38.673 -33.664 10.266  0.44 31.55 ?  100 VAL   B HG12 1 
ATOM   5369 H  HG13 A VAL   B 1 100 ? 37.453 -32.839 10.839  0.56 32.29 ?  100 VAL   B HG13 1 
ATOM   5370 H  HG13 B VAL   B 1 100 ? 37.406 -32.828 10.741  0.44 31.55 ?  100 VAL   B HG13 1 
ATOM   5371 H  HG21 A VAL   B 1 100 ? 36.876 -31.894 7.954   0.56 31.92 ?  100 VAL   B HG21 1 
ATOM   5372 H  HG21 B VAL   B 1 100 ? 36.954 -31.872 7.857   0.44 31.26 ?  100 VAL   B HG21 1 
ATOM   5373 H  HG22 A VAL   B 1 100 ? 36.615 -30.926 9.187   0.56 31.92 ?  100 VAL   B HG22 1 
ATOM   5374 H  HG22 B VAL   B 1 100 ? 36.682 -30.880 9.067   0.44 31.26 ?  100 VAL   B HG22 1 
ATOM   5375 H  HG23 A VAL   B 1 100 ? 37.615 -30.490 8.032   0.56 31.92 ?  100 VAL   B HG23 1 
ATOM   5376 H  HG23 B VAL   B 1 100 ? 37.730 -30.488 7.939   0.44 31.26 ?  100 VAL   B HG23 1 
ATOM   5377 N  N    . ASN   B 1 101 ? 41.354 -31.582 10.826  1.00 24.99 ?  101 ASN   B N    1 
ATOM   5378 C  CA   . ASN   B 1 101 ? 42.381 -32.126 11.713  1.00 26.95 ?  101 ASN   B CA   1 
ATOM   5379 C  C    . ASN   B 1 101 ? 42.567 -31.294 12.977  1.00 29.03 ?  101 ASN   B C    1 
ATOM   5380 O  O    . ASN   B 1 101 ? 43.187 -31.774 13.934  1.00 30.46 ?  101 ASN   B O    1 
ATOM   5381 C  CB   . ASN   B 1 101 ? 43.710 -32.257 10.965  1.00 27.08 ?  101 ASN   B CB   1 
ATOM   5382 C  CG   . ASN   B 1 101 ? 43.706 -33.396 9.962   1.00 26.95 ?  101 ASN   B CG   1 
ATOM   5383 O  OD1  . ASN   B 1 101 ? 43.035 -34.400 10.163  1.00 27.60 ?  101 ASN   B OD1  1 
ATOM   5384 N  ND2  . ASN   B 1 101 ? 44.448 -33.239 8.875   1.00 26.74 ?  101 ASN   B ND2  1 
ATOM   5385 H  H    A ASN   B 1 101 ? 41.642 -31.322 10.060  0.56 29.99 ?  101 ASN   B H    1 
ATOM   5386 H  H    B ASN   B 1 101 ? 41.648 -31.304 10.069  0.44 29.99 ?  101 ASN   B H    1 
ATOM   5387 H  HA   . ASN   B 1 101 ? 42.109 -33.010 11.989  1.00 32.33 ?  101 ASN   B HA   1 
ATOM   5388 H  HB2  . ASN   B 1 101 ? 43.893 -31.437 10.482  1.00 32.50 ?  101 ASN   B HB2  1 
ATOM   5389 H  HB3  . ASN   B 1 101 ? 44.418 -32.424 11.610  1.00 32.50 ?  101 ASN   B HB3  1 
ATOM   5390 H  HD21 . ASN   B 1 101 ? 44.481 -33.864 8.282   1.00 32.09 ?  101 ASN   B HD21 1 
ATOM   5391 H  HD22 . ASN   B 1 101 ? 44.896 -32.517 8.763   1.00 32.09 ?  101 ASN   B HD22 1 
ATOM   5392 N  N    . LYS   B 1 102 ? 42.061 -30.059 12.997  1.00 31.03 ?  102 LYS   B N    1 
ATOM   5393 C  CA   . LYS   B 1 102 ? 42.024 -29.228 14.193  1.00 33.41 ?  102 LYS   B CA   1 
ATOM   5394 C  C    . LYS   B 1 102 ? 40.638 -29.184 14.827  1.00 32.91 ?  102 LYS   B C    1 
ATOM   5395 O  O    . LYS   B 1 102 ? 40.408 -28.379 15.735  1.00 33.68 ?  102 LYS   B O    1 
ATOM   5396 C  CB   . LYS   B 1 102 ? 42.460 -27.798 13.866  1.00 36.58 ?  102 LYS   B CB   1 
ATOM   5397 C  CG   . LYS   B 1 102 ? 43.908 -27.631 13.448  1.00 39.67 ?  102 LYS   B CG   1 
ATOM   5398 C  CD   . LYS   B 1 102 ? 44.148 -26.201 12.980  1.00 42.51 ?  102 LYS   B CD   1 
ATOM   5399 C  CE   . LYS   B 1 102 ? 45.620 -25.910 12.751  1.00 44.64 ?  102 LYS   B CE   1 
ATOM   5400 N  NZ   . LYS   B 1 102 ? 45.827 -24.502 12.305  1.00 45.86 ?  102 LYS   B NZ   1 
ATOM   5401 H  H    . LYS   B 1 102 ? 41.721 -29.672 12.309  1.00 37.24 ?  102 LYS   B H    1 
ATOM   5402 H  HA   . LYS   B 1 102 ? 42.647 -29.587 14.845  1.00 40.09 ?  102 LYS   B HA   1 
ATOM   5403 H  HB2  . LYS   B 1 102 ? 41.909 -27.467 13.142  1.00 43.90 ?  102 LYS   B HB2  1 
ATOM   5404 H  HB3  . LYS   B 1 102 ? 42.322 -27.249 14.655  1.00 43.90 ?  102 LYS   B HB3  1 
ATOM   5405 H  HG2  . LYS   B 1 102 ? 44.490 -27.808 14.205  1.00 47.61 ?  102 LYS   B HG2  1 
ATOM   5406 H  HG3  . LYS   B 1 102 ? 44.108 -28.234 12.716  1.00 47.61 ?  102 LYS   B HG3  1 
ATOM   5407 H  HD2  . LYS   B 1 102 ? 43.678 -26.058 12.142  1.00 51.02 ?  102 LYS   B HD2  1 
ATOM   5408 H  HD3  . LYS   B 1 102 ? 43.819 -25.585 13.653  1.00 51.02 ?  102 LYS   B HD3  1 
ATOM   5409 H  HE2  . LYS   B 1 102 ? 46.106 -26.042 13.580  1.00 53.57 ?  102 LYS   B HE2  1 
ATOM   5410 H  HE3  . LYS   B 1 102 ? 45.961 -26.502 12.062  1.00 53.57 ?  102 LYS   B HE3  1 
ATOM   5411 H  HZ1  . LYS   B 1 102 ? 46.694 -24.348 12.176  1.00 55.03 ?  102 LYS   B HZ1  1 
ATOM   5412 H  HZ2  . LYS   B 1 102 ? 45.391 -24.357 11.543  1.00 55.03 ?  102 LYS   B HZ2  1 
ATOM   5413 H  HZ3  . LYS   B 1 102 ? 45.522 -23.939 12.924  1.00 55.03 ?  102 LYS   B HZ3  1 
ATOM   5414 N  N    . GLY   B 1 103 ? 39.706 -30.008 14.356  1.00 32.10 ?  103 GLY   B N    1 
ATOM   5415 C  CA   . GLY   B 1 103 ? 38.372 -30.048 14.921  1.00 31.62 ?  103 GLY   B CA   1 
ATOM   5416 C  C    . GLY   B 1 103 ? 37.443 -28.946 14.465  1.00 30.53 ?  103 GLY   B C    1 
ATOM   5417 O  O    . GLY   B 1 103 ? 36.350 -28.807 15.028  1.00 31.02 ?  103 GLY   B O    1 
ATOM   5418 H  H    . GLY   B 1 103 ? 39.826 -30.556 13.705  1.00 38.52 ?  103 GLY   B H    1 
ATOM   5419 H  HA2  . GLY   B 1 103 ? 37.961 -30.895 14.691  1.00 37.95 ?  103 GLY   B HA2  1 
ATOM   5420 H  HA3  . GLY   B 1 103 ? 38.440 -30.002 15.889  1.00 37.95 ?  103 GLY   B HA3  1 
ATOM   5421 N  N    A GLU   B 1 104 ? 37.843 -28.153 13.474  0.56 29.56 ?  104 GLU   B N    1 
ATOM   5422 N  N    B GLU   B 1 104 ? 37.825 -28.167 13.459  0.44 29.51 ?  104 GLU   B N    1 
ATOM   5423 C  CA   A GLU   B 1 104 ? 37.016 -27.048 13.014  0.56 28.40 ?  104 GLU   B CA   1 
ATOM   5424 C  CA   B GLU   B 1 104 ? 36.976 -27.084 12.986  0.44 28.27 ?  104 GLU   B CA   1 
ATOM   5425 C  C    A GLU   B 1 104 ? 35.834 -27.564 12.195  0.56 28.81 ?  104 GLU   B C    1 
ATOM   5426 C  C    B GLU   B 1 104 ? 35.820 -27.629 12.150  0.44 28.20 ?  104 GLU   B C    1 
ATOM   5427 O  O    A GLU   B 1 104 ? 35.878 -28.648 11.607  0.56 29.21 ?  104 GLU   B O    1 
ATOM   5428 O  O    B GLU   B 1 104 ? 35.907 -28.706 11.553  0.44 28.55 ?  104 GLU   B O    1 
ATOM   5429 C  CB   A GLU   B 1 104 ? 37.865 -26.058 12.213  0.56 27.05 ?  104 GLU   B CB   1 
ATOM   5430 C  CB   B GLU   B 1 104 ? 37.806 -26.073 12.195  0.44 27.21 ?  104 GLU   B CB   1 
ATOM   5431 C  CG   A GLU   B 1 104 ? 38.974 -25.432 13.055  0.56 25.76 ?  104 GLU   B CG   1 
ATOM   5432 C  CG   B GLU   B 1 104 ? 38.893 -25.434 13.050  0.44 26.26 ?  104 GLU   B CG   1 
ATOM   5433 C  CD   A GLU   B 1 104 ? 39.908 -24.537 12.267  0.56 24.32 ?  104 GLU   B CD   1 
ATOM   5434 C  CD   B GLU   B 1 104 ? 39.852 -24.561 12.264  0.44 25.27 ?  104 GLU   B CD   1 
ATOM   5435 O  OE1  A GLU   B 1 104 ? 39.889 -24.577 11.019  0.56 22.62 ?  104 GLU   B OE1  1 
ATOM   5436 O  OE1  B GLU   B 1 104 ? 39.803 -24.570 11.017  0.44 24.30 ?  104 GLU   B OE1  1 
ATOM   5437 O  OE2  A GLU   B 1 104 ? 40.671 -23.788 12.911  0.56 24.37 -1 104 GLU   B OE2  1 
ATOM   5438 O  OE2  B GLU   B 1 104 ? 40.664 -23.864 12.908  0.44 25.19 -1 104 GLU   B OE2  1 
ATOM   5439 H  H    A GLU   B 1 104 ? 38.592 -28.230 13.062  0.56 35.47 ?  104 GLU   B H    1 
ATOM   5440 H  H    B GLU   B 1 104 ? 38.574 -28.241 13.041  0.44 35.42 ?  104 GLU   B H    1 
ATOM   5441 H  HA   A GLU   B 1 104 ? 36.666 -26.577 13.785  0.56 34.08 ?  104 GLU   B HA   1 
ATOM   5442 H  HA   B GLU   B 1 104 ? 36.599 -26.625 13.752  0.44 33.92 ?  104 GLU   B HA   1 
ATOM   5443 H  HB2  A GLU   B 1 104 ? 38.280 -26.518 11.467  0.56 32.46 ?  104 GLU   B HB2  1 
ATOM   5444 H  HB2  B GLU   B 1 104 ? 38.232 -26.523 11.450  0.44 32.65 ?  104 GLU   B HB2  1 
ATOM   5445 H  HB3  A GLU   B 1 104 ? 37.298 -25.340 11.887  0.56 32.46 ?  104 GLU   B HB3  1 
ATOM   5446 H  HB3  B GLU   B 1 104 ? 37.222 -25.369 11.872  0.44 32.65 ?  104 GLU   B HB3  1 
ATOM   5447 H  HG2  A GLU   B 1 104 ? 38.575 -24.897 13.760  0.56 30.91 ?  104 GLU   B HG2  1 
ATOM   5448 H  HG2  B GLU   B 1 104 ? 38.474 -24.884 13.732  0.44 31.51 ?  104 GLU   B HG2  1 
ATOM   5449 H  HG3  A GLU   B 1 104 ? 39.513 -26.137 13.447  0.56 30.91 ?  104 GLU   B HG3  1 
ATOM   5450 H  HG3  B GLU   B 1 104 ? 39.416 -26.134 13.471  0.44 31.51 ?  104 GLU   B HG3  1 
ATOM   5451 N  N    A ASP   B 1 105 ? 34.764 -26.772 12.172  0.56 28.62 ?  105 ASP   B N    1 
ATOM   5452 N  N    B ASP   B 1 105 ? 34.726 -26.869 12.119  0.44 27.52 ?  105 ASP   B N    1 
ATOM   5453 C  CA   A ASP   B 1 105 ? 33.487 -27.228 11.634  0.56 29.05 ?  105 ASP   B CA   1 
ATOM   5454 C  CA   B ASP   B 1 105 ? 33.465 -27.352 11.568  0.44 27.35 ?  105 ASP   B CA   1 
ATOM   5455 C  C    A ASP   B 1 105 ? 33.535 -27.281 10.111  0.56 27.04 ?  105 ASP   B C    1 
ATOM   5456 C  C    B ASP   B 1 105 ? 33.522 -27.361 10.044  0.44 26.15 ?  105 ASP   B C    1 
ATOM   5457 O  O    A ASP   B 1 105 ? 33.689 -26.250 9.449   0.56 26.24 ?  105 ASP   B O    1 
ATOM   5458 O  O    B ASP   B 1 105 ? 33.692 -26.311 9.414   0.44 25.53 ?  105 ASP   B O    1 
ATOM   5459 C  CB   A ASP   B 1 105 ? 32.372 -26.292 12.096  0.56 31.68 ?  105 ASP   B CB   1 
ATOM   5460 C  CB   B ASP   B 1 105 ? 32.313 -26.475 12.056  0.44 28.52 ?  105 ASP   B CB   1 
ATOM   5461 C  CG   A ASP   B 1 105 ? 31.001 -26.745 11.634  0.56 33.99 ?  105 ASP   B CG   1 
ATOM   5462 C  CG   B ASP   B 1 105 ? 30.952 -27.070 11.742  0.44 29.47 ?  105 ASP   B CG   1 
ATOM   5463 O  OD1  A ASP   B 1 105 ? 30.885 -27.876 11.117  0.56 34.37 ?  105 ASP   B OD1  1 
ATOM   5464 O  OD1  B ASP   B 1 105 ? 30.888 -28.035 10.951  0.44 29.60 ?  105 ASP   B OD1  1 
ATOM   5465 O  OD2  A ASP   B 1 105 ? 30.038 -25.961 11.776  0.56 35.16 -1 105 ASP   B OD2  1 
ATOM   5466 O  OD2  B ASP   B 1 105 ? 29.944 -26.579 12.293  0.44 29.52 -1 105 ASP   B OD2  1 
ATOM   5467 H  H    A ASP   B 1 105 ? 34.756 -25.963 12.463  0.56 34.35 ?  105 ASP   B H    1 
ATOM   5468 H  H    B ASP   B 1 105 ? 34.691 -26.062 12.415  0.44 33.03 ?  105 ASP   B H    1 
ATOM   5469 H  HA   A ASP   B 1 105 ? 33.297 -28.119 11.966  0.56 34.87 ?  105 ASP   B HA   1 
ATOM   5470 H  HA   B ASP   B 1 105 ? 33.305 -28.258 11.872  0.44 32.82 ?  105 ASP   B HA   1 
ATOM   5471 H  HB2  A ASP   B 1 105 ? 32.384 -26.242 13.068  0.56 38.01 ?  105 ASP   B HB2  1 
ATOM   5472 H  HB2  B ASP   B 1 105 ? 32.380 -26.370 13.019  0.44 34.23 ?  105 ASP   B HB2  1 
ATOM   5473 H  HB3  A ASP   B 1 105 ? 32.516 -25.414 11.718  0.56 38.01 ?  105 ASP   B HB3  1 
ATOM   5474 H  HB3  B ASP   B 1 105 ? 32.371 -25.606 11.626  0.44 34.23 ?  105 ASP   B HB3  1 
ATOM   5475 N  N    A ILE   B 1 106 ? 33.373 -28.486 9.559   0.56 26.22 ?  106 ILE   B N    1 
ATOM   5476 N  N    B ILE   B 1 106 ? 33.357 -28.549 9.455   0.44 25.68 ?  106 ILE   B N    1 
ATOM   5477 C  CA   A ILE   B 1 106 ? 33.377 -28.674 8.113   0.56 25.30 ?  106 ILE   B CA   1 
ATOM   5478 C  CA   B ILE   B 1 106 ? 33.355 -28.694 8.004   0.44 25.24 ?  106 ILE   B CA   1 
ATOM   5479 C  C    A ILE   B 1 106 ? 32.285 -27.857 7.428   0.56 24.07 ?  106 ILE   B C    1 
ATOM   5480 C  C    B ILE   B 1 106 ? 32.258 -27.864 7.350   0.44 24.42 ?  106 ILE   B C    1 
ATOM   5481 O  O    A ILE   B 1 106 ? 32.404 -27.536 6.241   0.56 22.84 ?  106 ILE   B O    1 
ATOM   5482 O  O    B ILE   B 1 106 ? 32.345 -27.549 6.159   0.44 23.51 ?  106 ILE   B O    1 
ATOM   5483 C  CB   A ILE   B 1 106 ? 33.280 -30.182 7.787   0.56 26.12 ?  106 ILE   B CB   1 
ATOM   5484 C  CB   B ILE   B 1 106 ? 33.253 -30.193 7.633   0.44 25.94 ?  106 ILE   B CB   1 
ATOM   5485 C  CG1  A ILE   B 1 106 ? 33.524 -30.440 6.300   0.56 26.51 ?  106 ILE   B CG1  1 
ATOM   5486 C  CG1  B ILE   B 1 106 ? 33.531 -30.413 6.145   0.44 26.32 ?  106 ILE   B CG1  1 
ATOM   5487 C  CG2  A ILE   B 1 106 ? 31.926 -30.738 8.208   0.56 26.66 ?  106 ILE   B CG2  1 
ATOM   5488 C  CG2  B ILE   B 1 106 ? 31.884 -30.748 8.005   0.44 26.43 ?  106 ILE   B CG2  1 
ATOM   5489 C  CD1  A ILE   B 1 106 ? 34.880 -29.985 5.823   0.56 26.54 ?  106 ILE   B CD1  1 
ATOM   5490 C  CD1  B ILE   B 1 106 ? 34.901 -29.953 5.712   0.44 26.43 ?  106 ILE   B CD1  1 
ATOM   5491 H  H    A ILE   B 1 106 ? 33.265 -29.210 10.008  0.56 31.47 ?  106 ILE   B H    1 
ATOM   5492 H  H    B ILE   B 1 106 ? 33.252 -29.287 9.880   0.44 30.82 ?  106 ILE   B H    1 
ATOM   5493 H  HA   A ILE   B 1 106 ? 34.226 -28.358 7.777   0.56 30.36 ?  106 ILE   B HA   1 
ATOM   5494 H  HA   B ILE   B 1 106 ? 34.199 -28.365 7.669   0.44 30.29 ?  106 ILE   B HA   1 
ATOM   5495 H  HB   A ILE   B 1 106 ? 33.965 -30.649 8.293   0.56 31.34 ?  106 ILE   B HB   1 
ATOM   5496 H  HB   B ILE   B 1 106 ? 33.921 -30.677 8.141   0.44 31.13 ?  106 ILE   B HB   1 
ATOM   5497 H  HG12 A ILE   B 1 106 ? 33.460 -31.395 6.135   0.56 31.81 ?  106 ILE   B HG12 1 
ATOM   5498 H  HG12 B ILE   B 1 106 ? 33.465 -31.363 5.952   0.44 31.58 ?  106 ILE   B HG12 1 
ATOM   5499 H  HG13 A ILE   B 1 106 ? 32.853 -29.972 5.783   0.56 31.81 ?  106 ILE   B HG13 1 
ATOM   5500 H  HG13 B ILE   B 1 106 ? 32.875 -29.927 5.624   0.44 31.58 ?  106 ILE   B HG13 1 
ATOM   5501 H  HG21 A ILE   B 1 106 ? 31.937 -31.704 8.111   0.56 31.99 ?  106 ILE   B HG21 1 
ATOM   5502 H  HG21 B ILE   B 1 106 ? 31.900 -31.714 7.911   0.44 31.72 ?  106 ILE   B HG21 1 
ATOM   5503 H  HG22 A ILE   B 1 106 ? 31.762 -30.503 9.135   0.56 31.99 ?  106 ILE   B HG22 1 
ATOM   5504 H  HG22 B ILE   B 1 106 ? 31.686 -30.510 8.924   0.44 31.72 ?  106 ILE   B HG22 1 
ATOM   5505 H  HG23 A ILE   B 1 106 ? 31.236 -30.358 7.644   0.56 31.99 ?  106 ILE   B HG23 1 
ATOM   5506 H  HG23 B ILE   B 1 106 ? 31.215 -30.371 7.413   0.44 31.72 ?  106 ILE   B HG23 1 
ATOM   5507 H  HD11 A ILE   B 1 106 ? 35.063 -30.390 4.962   0.56 31.85 ?  106 ILE   B HD11 1 
ATOM   5508 H  HD11 B ILE   B 1 106 ? 35.108 -30.348 4.852   0.44 31.72 ?  106 ILE   B HD11 1 
ATOM   5509 H  HD12 A ILE   B 1 106 ? 34.878 -29.018 5.740   0.56 31.85 ?  106 ILE   B HD12 1 
ATOM   5510 H  HD12 B ILE   B 1 106 ? 34.902 -28.986 5.640   0.44 31.72 ?  106 ILE   B HD12 1 
ATOM   5511 H  HD13 A ILE   B 1 106 ? 35.551 -30.261 6.467   0.56 31.85 ?  106 ILE   B HD13 1 
ATOM   5512 H  HD13 B ILE   B 1 106 ? 35.553 -30.239 6.372   0.44 31.72 ?  106 ILE   B HD13 1 
ATOM   5513 N  N    A GLN   B 1 107 ? 31.222 -27.501 8.153   0.56 24.50 ?  107 GLN   B N    1 
ATOM   5514 N  N    B GLN   B 1 107 ? 31.223 -27.490 8.106   0.44 24.82 ?  107 GLN   B N    1 
ATOM   5515 C  CA   A GLN   B 1 107 ? 30.153 -26.695 7.571   0.56 25.18 ?  107 GLN   B CA   1 
ATOM   5516 C  CA   B GLN   B 1 107 ? 30.143 -26.682 7.552   0.44 25.37 ?  107 GLN   B CA   1 
ATOM   5517 C  C    A GLN   B 1 107 ? 30.650 -25.352 7.047   0.56 23.07 ?  107 GLN   B C    1 
ATOM   5518 C  C    B GLN   B 1 107 ? 30.623 -25.317 7.078   0.44 23.20 ?  107 GLN   B C    1 
ATOM   5519 O  O    A GLN   B 1 107 ? 30.019 -24.779 6.153   0.56 23.43 ?  107 GLN   B O    1 
ATOM   5520 O  O    B GLN   B 1 107 ? 29.950 -24.691 6.252   0.44 23.54 ?  107 GLN   B O    1 
ATOM   5521 C  CB   A GLN   B 1 107 ? 29.047 -26.482 8.610   0.56 28.92 ?  107 GLN   B CB   1 
ATOM   5522 C  CB   B GLN   B 1 107 ? 29.032 -26.523 8.594   0.44 28.71 ?  107 GLN   B CB   1 
ATOM   5523 C  CG   A GLN   B 1 107 ? 27.725 -25.962 8.049   0.56 32.55 ?  107 GLN   B CG   1 
ATOM   5524 C  CG   B GLN   B 1 107 ? 27.707 -26.005 8.044   0.44 31.91 ?  107 GLN   B CG   1 
ATOM   5525 C  CD   A GLN   B 1 107 ? 27.680 -24.447 7.930   0.56 35.37 ?  107 GLN   B CD   1 
ATOM   5526 C  CD   B GLN   B 1 107 ? 27.604 -24.491 8.078   0.44 34.42 ?  107 GLN   B CD   1 
ATOM   5527 O  OE1  A GLN   B 1 107 ? 28.520 -23.742 8.493   0.56 36.46 ?  107 GLN   B OE1  1 
ATOM   5528 O  OE1  B GLN   B 1 107 ? 28.455 -23.810 8.653   0.44 35.33 ?  107 GLN   B OE1  1 
ATOM   5529 N  NE2  A GLN   B 1 107 ? 26.692 -23.940 7.197   0.56 36.32 ?  107 GLN   B NE2  1 
ATOM   5530 N  NE2  B GLN   B 1 107 ? 26.553 -23.957 7.465   0.44 35.31 ?  107 GLN   B NE2  1 
ATOM   5531 H  H    A GLN   B 1 107 ? 31.097 -27.716 8.973   0.56 29.40 ?  107 GLN   B H    1 
ATOM   5532 H  H    B GLN   B 1 107 ? 31.124 -27.691 8.933   0.44 29.79 ?  107 GLN   B H    1 
ATOM   5533 H  HA   A GLN   B 1 107 ? 29.770 -27.180 6.822   0.56 30.22 ?  107 GLN   B HA   1 
ATOM   5534 H  HA   B GLN   B 1 107 ? 29.767 -27.144 6.789   0.44 30.44 ?  107 GLN   B HA   1 
ATOM   5535 H  HB2  A GLN   B 1 107 ? 28.865 -27.329 9.043   0.56 34.71 ?  107 GLN   B HB2  1 
ATOM   5536 H  HB2  B GLN   B 1 107 ? 28.861 -27.388 8.990   0.44 34.45 ?  107 GLN   B HB2  1 
ATOM   5537 H  HB3  A GLN   B 1 107 ? 29.360 -25.842 9.268   0.56 34.71 ?  107 GLN   B HB3  1 
ATOM   5538 H  HB3  B GLN   B 1 107 ? 29.331 -25.904 9.277   0.44 34.45 ?  107 GLN   B HB3  1 
ATOM   5539 H  HG2  A GLN   B 1 107 ? 27.588 -26.331 7.164   0.56 39.06 ?  107 GLN   B HG2  1 
ATOM   5540 H  HG2  B GLN   B 1 107 ? 27.612 -26.290 7.122   0.44 38.29 ?  107 GLN   B HG2  1 
ATOM   5541 H  HG3  A GLN   B 1 107 ? 27.002 -26.240 8.637   0.56 39.06 ?  107 GLN   B HG3  1 
ATOM   5542 H  HG3  B GLN   B 1 107 ? 26.981 -26.370 8.578   0.44 38.29 ?  107 GLN   B HG3  1 
ATOM   5543 H  HE21 A GLN   B 1 107 ? 26.124 -24.464 6.817   0.56 43.59 ?  107 GLN   B HE21 1 
ATOM   5544 H  HE21 B GLN   B 1 107 ? 25.979 -24.464 7.073   0.44 42.37 ?  107 GLN   B HE21 1 
ATOM   5545 H  HE22 A GLN   B 1 107 ? 26.617 -23.087 7.101   0.56 43.59 ?  107 GLN   B HE22 1 
ATOM   5546 H  HE22 B GLN   B 1 107 ? 26.447 -23.103 7.459   0.44 42.37 ?  107 GLN   B HE22 1 
ATOM   5547 N  N    . LEU   B 1 108 ? 31.769 -24.842 7.568   1.00 21.08 ?  108 LEU   B N    1 
ATOM   5548 C  CA   . LEU   B 1 108 ? 32.302 -23.545 7.157   1.00 18.47 ?  108 LEU   B CA   1 
ATOM   5549 C  C    . LEU   B 1 108 ? 32.950 -23.568 5.782   1.00 16.37 ?  108 LEU   B C    1 
ATOM   5550 O  O    . LEU   B 1 108 ? 33.375 -22.509 5.294   1.00 15.84 ?  108 LEU   B O    1 
ATOM   5551 C  CB   . LEU   B 1 108 ? 33.306 -23.040 8.192   1.00 18.80 ?  108 LEU   B CB   1 
ATOM   5552 C  CG   . LEU   B 1 108 ? 32.679 -22.631 9.524   1.00 20.47 ?  108 LEU   B CG   1 
ATOM   5553 C  CD1  . LEU   B 1 108 ? 33.724 -22.528 10.619  1.00 20.70 ?  108 LEU   B CD1  1 
ATOM   5554 C  CD2  . LEU   B 1 108 ? 31.954 -21.309 9.361   1.00 21.72 ?  108 LEU   B CD2  1 
ATOM   5555 H  H    A LEU   B 1 108 ? 32.239 -25.233 8.168   0.56 25.30 ?  108 LEU   B H    1 
ATOM   5556 H  H    B LEU   B 1 108 ? 32.251 -25.250 8.148   0.44 25.30 ?  108 LEU   B H    1 
ATOM   5557 H  HA   . LEU   B 1 108 ? 31.573 -22.913 7.116   1.00 22.16 ?  108 LEU   B HA   1 
ATOM   5558 H  HB2  . LEU   B 1 108 ? 33.945 -23.743 8.375   1.00 22.57 ?  108 LEU   B HB2  1 
ATOM   5559 H  HB3  . LEU   B 1 108 ? 33.759 -22.265 7.831   1.00 22.57 ?  108 LEU   B HB3  1 
ATOM   5560 H  HG   . LEU   B 1 108 ? 32.025 -23.299 9.792   1.00 24.57 ?  108 LEU   B HG   1 
ATOM   5561 H  HD11 . LEU   B 1 108 ? 33.289 -22.295 11.455  1.00 24.84 ?  108 LEU   B HD11 1 
ATOM   5562 H  HD12 . LEU   B 1 108 ? 34.173 -23.384 10.708  1.00 24.84 ?  108 LEU   B HD12 1 
ATOM   5563 H  HD13 . LEU   B 1 108 ? 34.366 -21.841 10.379  1.00 24.84 ?  108 LEU   B HD13 1 
ATOM   5564 H  HD21 . LEU   B 1 108 ? 31.637 -21.011 10.228  1.00 26.06 ?  108 LEU   B HD21 1 
ATOM   5565 H  HD22 . LEU   B 1 108 ? 32.569 -20.656 8.992   1.00 26.06 ?  108 LEU   B HD22 1 
ATOM   5566 H  HD23 . LEU   B 1 108 ? 31.202 -21.430 8.759   1.00 26.06 ?  108 LEU   B HD23 1 
ATOM   5567 N  N    . LEU   B 1 109 ? 33.017 -24.736 5.149   1.00 15.29 ?  109 LEU   B N    1 
ATOM   5568 C  CA   . LEU   B 1 109 ? 33.653 -24.841 3.845   1.00 14.37 ?  109 LEU   B CA   1 
ATOM   5569 C  C    . LEU   B 1 109 ? 32.893 -24.053 2.785   1.00 13.55 ?  109 LEU   B C    1 
ATOM   5570 O  O    . LEU   B 1 109 ? 33.510 -23.459 1.893   1.00 13.40 ?  109 LEU   B O    1 
ATOM   5571 C  CB   . LEU   B 1 109 ? 33.763 -26.316 3.465   1.00 14.48 ?  109 LEU   B CB   1 
ATOM   5572 C  CG   . LEU   B 1 109 ? 34.558 -26.653 2.210   1.00 14.38 ?  109 LEU   B CG   1 
ATOM   5573 C  CD1  . LEU   B 1 109 ? 35.935 -26.004 2.248   1.00 14.16 ?  109 LEU   B CD1  1 
ATOM   5574 C  CD2  . LEU   B 1 109 ? 34.688 -28.158 2.075   1.00 15.25 ?  109 LEU   B CD2  1 
ATOM   5575 H  H    . LEU   B 1 109 ? 32.705 -25.478 5.445   1.00 18.35 ?  109 LEU   B H    1 
ATOM   5576 H  HA   . LEU   B 1 109 ? 34.549 -24.478 3.898   1.00 17.24 ?  109 LEU   B HA   1 
ATOM   5577 H  HB2  . LEU   B 1 109 ? 34.188 -26.786 4.199   1.00 17.37 ?  109 LEU   B HB2  1 
ATOM   5578 H  HB3  . LEU   B 1 109 ? 32.869 -26.666 3.335   1.00 17.37 ?  109 LEU   B HB3  1 
ATOM   5579 H  HG   . LEU   B 1 109 ? 34.085 -26.326 1.427   1.00 17.26 ?  109 LEU   B HG   1 
ATOM   5580 H  HD11 . LEU   B 1 109 ? 36.484 -26.379 1.541   1.00 16.99 ?  109 LEU   B HD11 1 
ATOM   5581 H  HD12 . LEU   B 1 109 ? 35.837 -25.049 2.118   1.00 16.99 ?  109 LEU   B HD12 1 
ATOM   5582 H  HD13 . LEU   B 1 109 ? 36.343 -26.183 3.110   1.00 16.99 ?  109 LEU   B HD13 1 
ATOM   5583 H  HD21 . LEU   B 1 109 ? 35.265 -28.362 1.321   1.00 18.30 ?  109 LEU   B HD21 1 
ATOM   5584 H  HD22 . LEU   B 1 109 ? 35.073 -28.516 2.890   1.00 18.30 ?  109 LEU   B HD22 1 
ATOM   5585 H  HD23 . LEU   B 1 109 ? 33.808 -28.543 1.930   1.00 18.30 ?  109 LEU   B HD23 1 
ATOM   5586 N  N    . LYS   B 1 110 ? 31.559 -24.024 2.859   1.00 13.70 ?  110 LYS   B N    1 
ATOM   5587 C  CA   . LYS   B 1 110 ? 30.801 -23.261 1.871   1.00 13.56 ?  110 LYS   B CA   1 
ATOM   5588 C  C    . LYS   B 1 110 ? 31.142 -21.773 1.959   1.00 13.04 ?  110 LYS   B C    1 
ATOM   5589 O  O    . LYS   B 1 110 ? 31.397 -21.122 0.941   1.00 12.81 ?  110 LYS   B O    1 
ATOM   5590 C  CB   . LYS   B 1 110 ? 29.294 -23.507 2.021   1.00 14.33 ?  110 LYS   B CB   1 
ATOM   5591 C  CG   . LYS   B 1 110 ? 28.479 -22.872 0.899   1.00 14.70 ?  110 LYS   B CG   1 
ATOM   5592 C  CD   . LYS   B 1 110 ? 27.021 -23.317 0.907   1.00 15.16 ?  110 LYS   B CD   1 
ATOM   5593 C  CE   . LYS   B 1 110 ? 26.276 -22.777 -0.312  1.00 15.86 ?  110 LYS   B CE   1 
ATOM   5594 N  NZ   . LYS   B 1 110 ? 26.602 -23.508 -1.559  1.00 16.24 ?  110 LYS   B NZ   1 
ATOM   5595 H  H    . LYS   B 1 110 ? 31.088 -24.428 3.449   1.00 16.44 ?  110 LYS   B H    1 
ATOM   5596 H  HA   . LYS   B 1 110 ? 31.055 -23.566 0.983   1.00 16.27 ?  110 LYS   B HA   1 
ATOM   5597 H  HB2  . LYS   B 1 110 ? 29.129 -24.467 2.004   1.00 17.19 ?  110 LYS   B HB2  1 
ATOM   5598 H  HB3  . LYS   B 1 110 ? 28.995 -23.136 2.862   1.00 17.19 ?  110 LYS   B HB3  1 
ATOM   5599 H  HG2  . LYS   B 1 110 ? 28.488 -21.907 1.005   1.00 17.63 ?  110 LYS   B HG2  1 
ATOM   5600 H  HG3  . LYS   B 1 110 ? 28.858 -23.117 0.043   1.00 17.63 ?  110 LYS   B HG3  1 
ATOM   5601 H  HD2  . LYS   B 1 110 ? 26.978 -24.291 0.878   1.00 18.19 ?  110 LYS   B HD2  1 
ATOM   5602 H  HD3  . LYS   B 1 110 ? 26.579 -22.989 1.706   1.00 18.19 ?  110 LYS   B HD3  1 
ATOM   5603 H  HE2  . LYS   B 1 110 ? 25.319 -22.851 -0.164  1.00 19.03 ?  110 LYS   B HE2  1 
ATOM   5604 H  HE3  . LYS   B 1 110 ? 26.517 -21.844 -0.441  1.00 19.03 ?  110 LYS   B HE3  1 
ATOM   5605 H  HZ1  . LYS   B 1 110 ? 26.156 -23.164 -2.244  1.00 19.49 ?  110 LYS   B HZ1  1 
ATOM   5606 H  HZ2  . LYS   B 1 110 ? 27.477 -23.450 -1.723  1.00 19.49 ?  110 LYS   B HZ2  1 
ATOM   5607 H  HZ3  . LYS   B 1 110 ? 26.385 -24.368 -1.471  1.00 19.49 ?  110 LYS   B HZ3  1 
ATOM   5608 N  N    . SER   B 1 111 ? 31.158 -21.220 3.176   1.00 13.65 ?  111 SER   B N    1 
ATOM   5609 C  CA   . SER   B 1 111 ? 31.549 -19.822 3.351   1.00 13.64 ?  111 SER   B CA   1 
ATOM   5610 C  C    . SER   B 1 111 ? 32.933 -19.563 2.771   1.00 12.81 ?  111 SER   B C    1 
ATOM   5611 O  O    . SER   B 1 111 ? 33.163 -18.525 2.132   1.00 13.10 ?  111 SER   B O    1 
ATOM   5612 C  CB   . SER   B 1 111 ? 31.537 -19.458 4.833   1.00 14.77 ?  111 SER   B CB   1 
ATOM   5613 O  OG   . SER   B 1 111 ? 30.229 -19.463 5.361   1.00 16.64 ?  111 SER   B OG   1 
ATOM   5614 H  H    . SER   B 1 111 ? 30.961 -21.634 3.900   1.00 16.38 ?  111 SER   B H    1 
ATOM   5615 H  HA   . SER   B 1 111 ? 30.916 -19.254 2.889   1.00 16.37 ?  111 SER   B HA   1 
ATOM   5616 H  HB2  . SER   B 1 111 ? 32.073 -20.104 5.319   1.00 17.73 ?  111 SER   B HB2  1 
ATOM   5617 H  HB3  . SER   B 1 111 ? 31.904 -18.572 4.941   1.00 17.73 ?  111 SER   B HB3  1 
ATOM   5618 H  HG   . SER   B 1 111 ? 30.244 -19.270 6.183   1.00 19.97 ?  111 SER   B HG   1 
ATOM   5619 N  N    . ALA   B 1 112 ? 33.872 -20.484 2.999   1.00 12.85 ?  112 ALA   B N    1 
ATOM   5620 C  CA   . ALA   B 1 112 ? 35.217 -20.314 2.461   1.00 12.57 ?  112 ALA   B CA   1 
ATOM   5621 C  C    . ALA   B 1 112 ? 35.186 -20.216 0.940   1.00 12.21 ?  112 ALA   B C    1 
ATOM   5622 O  O    . ALA   B 1 112 ? 35.819 -19.334 0.350   1.00 12.55 ?  112 ALA   B O    1 
ATOM   5623 C  CB   . ALA   B 1 112 ? 36.115 -21.463 2.930   1.00 13.25 ?  112 ALA   B CB   1 
ATOM   5624 H  H    . ALA   B 1 112 ? 33.756 -21.206 3.463   1.00 15.41 ?  112 ALA   B H    1 
ATOM   5625 H  HA   . ALA   B 1 112 ? 35.588 -19.491 2.806   1.00 15.08 ?  112 ALA   B HA   1 
ATOM   5626 H  HB1  . ALA   B 1 112 ? 37.008 -21.332 2.569   1.00 15.90 ?  112 ALA   B HB1  1 
ATOM   5627 H  HB2  . ALA   B 1 112 ? 36.155 -21.459 3.903   1.00 15.90 ?  112 ALA   B HB2  1 
ATOM   5628 H  HB3  . ALA   B 1 112 ? 35.752 -22.304 2.619   1.00 15.90 ?  112 ALA   B HB3  1 
ATOM   5629 N  N    . TYR   B 1 113 ? 34.457 -21.119 0.283   1.00 12.28 ?  113 TYR   B N    1 
ATOM   5630 C  CA   . TYR   B 1 113 ? 34.383 -21.073 -1.172  1.00 12.15 ?  113 TYR   B CA   1 
ATOM   5631 C  C    . TYR   B 1 113 ? 33.675 -19.824 -1.688  1.00 11.86 ?  113 TYR   B C    1 
ATOM   5632 O  O    . TYR   B 1 113 ? 33.944 -19.393 -2.813  1.00 11.91 ?  113 TYR   B O    1 
ATOM   5633 C  CB   . TYR   B 1 113 ? 33.713 -22.335 -1.720  1.00 12.41 ?  113 TYR   B CB   1 
ATOM   5634 C  CG   . TYR   B 1 113 ? 34.672 -23.485 -1.979  1.00 12.62 ?  113 TYR   B CG   1 
ATOM   5635 C  CD1  . TYR   B 1 113 ? 35.671 -23.378 -2.941  1.00 12.92 ?  113 TYR   B CD1  1 
ATOM   5636 C  CD2  . TYR   B 1 113 ? 34.566 -24.681 -1.280  1.00 12.72 ?  113 TYR   B CD2  1 
ATOM   5637 C  CE1  . TYR   B 1 113 ? 36.551 -24.411 -3.187  1.00 12.98 ?  113 TYR   B CE1  1 
ATOM   5638 C  CE2  . TYR   B 1 113 ? 35.438 -25.732 -1.520  1.00 12.90 ?  113 TYR   B CE2  1 
ATOM   5639 C  CZ   . TYR   B 1 113 ? 36.426 -25.594 -2.481  1.00 13.02 ?  113 TYR   B CZ   1 
ATOM   5640 O  OH   . TYR   B 1 113 ? 37.309 -26.614 -2.754  1.00 13.81 ?  113 TYR   B OH   1 
ATOM   5641 H  H    . TYR   B 1 113 ? 33.999 -21.756 0.655   1.00 14.73 ?  113 TYR   B H    1 
ATOM   5642 H  HA   . TYR   B 1 113 ? 35.285 -21.057 -1.509  1.00 14.58 ?  113 TYR   B HA   1 
ATOM   5643 H  HB2  . TYR   B 1 113 ? 33.051 -22.649 -1.080  1.00 14.89 ?  113 TYR   B HB2  1 
ATOM   5644 H  HB3  . TYR   B 1 113 ? 33.278 -22.120 -2.558  1.00 14.89 ?  113 TYR   B HB3  1 
ATOM   5645 H  HD1  . TYR   B 1 113 ? 35.757 -22.583 -3.422  1.00 15.51 ?  113 TYR   B HD1  1 
ATOM   5646 H  HD2  . TYR   B 1 113 ? 33.897 -24.774 -0.640  1.00 15.27 ?  113 TYR   B HD2  1 
ATOM   5647 H  HE1  . TYR   B 1 113 ? 37.208 -24.318 -3.839  1.00 15.58 ?  113 TYR   B HE1  1 
ATOM   5648 H  HE2  . TYR   B 1 113 ? 35.346 -26.528 -1.047  1.00 15.48 ?  113 TYR   B HE2  1 
ATOM   5649 H  HH   . TYR   B 1 113 ? 37.127 -27.281 -2.274  1.00 16.58 ?  113 TYR   B HH   1 
ATOM   5650 N  N    . GLU   B 1 114 ? 32.753 -19.244 -0.910  1.00 12.07 ?  114 GLU   B N    1 
ATOM   5651 C  CA   . GLU   B 1 114 ? 32.072 -18.037 -1.366  1.00 12.24 ?  114 GLU   B CA   1 
ATOM   5652 C  C    . GLU   B 1 114 ? 33.055 -16.913 -1.662  1.00 11.65 ?  114 GLU   B C    1 
ATOM   5653 O  O    . GLU   B 1 114 ? 32.777 -16.057 -2.503  1.00 11.95 ?  114 GLU   B O    1 
ATOM   5654 C  CB   . GLU   B 1 114 ? 31.009 -17.605 -0.352  1.00 12.61 ?  114 GLU   B CB   1 
ATOM   5655 C  CG   . GLU   B 1 114 ? 29.785 -18.522 -0.427  1.00 12.84 ?  114 GLU   B CG   1 
ATOM   5656 C  CD   . GLU   B 1 114 ? 28.764 -18.336 0.681   1.00 13.02 ?  114 GLU   B CD   1 
ATOM   5657 O  OE1  . GLU   B 1 114 ? 29.052 -17.713 1.726   1.00 13.01 ?  114 GLU   B OE1  1 
ATOM   5658 O  OE2  . GLU   B 1 114 ? 27.644 -18.874 0.514   1.00 13.53 -1 114 GLU   B OE2  1 
ATOM   5659 H  H    . GLU   B 1 114 ? 32.502 -19.533 -0.136  1.00 14.48 ?  114 GLU   B H    1 
ATOM   5660 H  HA   . GLU   B 1 114 ? 31.617 -18.236 -2.192  1.00 14.69 ?  114 GLU   B HA   1 
ATOM   5661 H  HB2  . GLU   B 1 114 ? 31.374 -17.658 0.546   1.00 15.14 ?  114 GLU   B HB2  1 
ATOM   5662 H  HB3  . GLU   B 1 114 ? 30.723 -16.700 -0.548  1.00 15.14 ?  114 GLU   B HB3  1 
ATOM   5663 H  HG2  . GLU   B 1 114 ? 29.341 -18.362 -1.272  1.00 15.41 ?  114 GLU   B HG2  1 
ATOM   5664 H  HG3  . GLU   B 1 114 ? 30.095 -19.440 -0.390  1.00 15.41 ?  114 GLU   B HG3  1 
ATOM   5665 N  N    . ASN   B 1 115 ? 34.219 -16.909 -1.008  1.00 11.55 ?  115 ASN   B N    1 
ATOM   5666 C  CA   . ASN   B 1 115 ? 35.211 -15.881 -1.306  1.00 11.39 ?  115 ASN   B CA   1 
ATOM   5667 C  C    . ASN   B 1 115 ? 35.620 -15.903 -2.771  1.00 11.06 ?  115 ASN   B C    1 
ATOM   5668 O  O    . ASN   B 1 115 ? 36.000 -14.863 -3.328  1.00 11.85 ?  115 ASN   B O    1 
ATOM   5669 C  CB   . ASN   B 1 115 ? 36.447 -16.063 -0.423  1.00 12.02 ?  115 ASN   B CB   1 
ATOM   5670 C  CG   . ASN   B 1 115 ? 36.181 -15.791 1.037   1.00 12.55 ?  115 ASN   B CG   1 
ATOM   5671 O  OD1  . ASN   B 1 115 ? 36.191 -14.640 1.477   1.00 14.54 ?  115 ASN   B OD1  1 
ATOM   5672 N  ND2  . ASN   B 1 115 ? 36.013 -16.853 1.811   1.00 12.75 ?  115 ASN   B ND2  1 
ATOM   5673 H  H    . ASN   B 1 115 ? 34.453 -17.472 -0.393  1.00 13.86 ?  115 ASN   B H    1 
ATOM   5674 H  HA   . ASN   B 1 115 ? 34.834 -15.009 -1.110  1.00 13.67 ?  115 ASN   B HA   1 
ATOM   5675 H  HB2  . ASN   B 1 115 ? 36.765 -16.975 -0.505  1.00 14.43 ?  115 ASN   B HB2  1 
ATOM   5676 H  HB3  . ASN   B 1 115 ? 37.137 -15.445 -0.715  1.00 14.43 ?  115 ASN   B HB3  1 
ATOM   5677 H  HD21 . ASN   B 1 115 ? 35.867 -16.752 2.656   1.00 15.30 ?  115 ASN   B HD21 1 
ATOM   5678 H  HD22 . ASN   B 1 115 ? 36.032 -17.643 1.474   1.00 15.30 ?  115 ASN   B HD22 1 
ATOM   5679 N  N    . PHE   B 1 116 ? 35.600 -17.082 -3.404  1.00 11.11 ?  116 PHE   B N    1 
ATOM   5680 C  CA   . PHE   B 1 116 ? 36.030 -17.176 -4.794  1.00 11.56 ?  116 PHE   B CA   1 
ATOM   5681 C  C    . PHE   B 1 116 ? 35.127 -16.357 -5.709  1.00 11.22 ?  116 PHE   B C    1 
ATOM   5682 O  O    . PHE   B 1 116 ? 35.560 -15.932 -6.785  1.00 11.75 ?  116 PHE   B O    1 
ATOM   5683 C  CB   . PHE   B 1 116 ? 36.001 -18.623 -5.309  1.00 11.34 ?  116 PHE   B CB   1 
ATOM   5684 C  CG   . PHE   B 1 116 ? 37.070 -19.573 -4.758  1.00 11.09 ?  116 PHE   B CG   1 
ATOM   5685 C  CD1  . PHE   B 1 116 ? 37.717 -19.390 -3.552  1.00 12.15 ?  116 PHE   B CD1  1 
ATOM   5686 C  CD2  . PHE   B 1 116 ? 37.370 -20.712 -5.488  1.00 11.58 ?  116 PHE   B CD2  1 
ATOM   5687 C  CE1  . PHE   B 1 116 ? 38.652 -20.321 -3.097  1.00 12.16 ?  116 PHE   B CE1  1 
ATOM   5688 C  CE2  . PHE   B 1 116 ? 38.298 -21.649 -5.039  1.00 11.92 ?  116 PHE   B CE2  1 
ATOM   5689 C  CZ   . PHE   B 1 116 ? 38.931 -21.454 -3.846  1.00 12.05 ?  116 PHE   B CZ   1 
ATOM   5690 H  H    . PHE   B 1 116 ? 35.352 -17.834 -3.052  1.00 13.33 ?  116 PHE   B H    1 
ATOM   5691 H  HA   . PHE   B 1 116 ? 36.935 -16.845 -4.873  1.00 13.87 ?  116 PHE   B HA   1 
ATOM   5692 H  HB2  . PHE   B 1 116 ? 35.133 -19.007 -5.089  1.00 13.61 ?  116 PHE   B HB2  1 
ATOM   5693 H  HB3  . PHE   B 1 116 ? 36.101 -18.602 -6.274  1.00 13.61 ?  116 PHE   B HB3  1 
ATOM   5694 H  HD1  . PHE   B 1 116 ? 37.527 -18.636 -3.038  1.00 14.58 ?  116 PHE   B HD1  1 
ATOM   5695 H  HD2  . PHE   B 1 116 ? 36.933 -20.865 -6.293  1.00 13.90 ?  116 PHE   B HD2  1 
ATOM   5696 H  HE1  . PHE   B 1 116 ? 39.090 -20.183 -2.288  1.00 14.59 ?  116 PHE   B HE1  1 
ATOM   5697 H  HE2  . PHE   B 1 116 ? 38.486 -22.404 -5.549  1.00 14.30 ?  116 PHE   B HE2  1 
ATOM   5698 H  HZ   . PHE   B 1 116 ? 39.566 -22.066 -3.546  1.00 14.46 ?  116 PHE   B HZ   1 
ATOM   5699 N  N    . ASN   B 1 117 ? 33.859 -16.150 -5.323  1.00 11.56 ?  117 ASN   B N    1 
ATOM   5700 C  CA   . ASN   B 1 117 ? 32.916 -15.453 -6.199  1.00 11.71 ?  117 ASN   B CA   1 
ATOM   5701 C  C    . ASN   B 1 117 ? 33.228 -13.973 -6.352  1.00 12.23 ?  117 ASN   B C    1 
ATOM   5702 O  O    . ASN   B 1 117 ? 32.640 -13.319 -7.214  1.00 13.49 ?  117 ASN   B O    1 
ATOM   5703 C  CB   . ASN   B 1 117 ? 31.490 -15.670 -5.708  1.00 11.88 ?  117 ASN   B CB   1 
ATOM   5704 C  CG   . ASN   B 1 117 ? 31.032 -17.078 -5.959  1.00 12.32 ?  117 ASN   B CG   1 
ATOM   5705 O  OD1  . ASN   B 1 117 ? 31.387 -17.671 -6.981  1.00 13.30 ?  117 ASN   B OD1  1 
ATOM   5706 N  ND2  . ASN   B 1 117 ? 30.299 -17.653 -5.014  1.00 12.51 ?  117 ASN   B ND2  1 
ATOM   5707 H  H    . ASN   B 1 117 ? 33.532 -16.400 -4.565  1.00 13.87 ?  117 ASN   B H    1 
ATOM   5708 H  HA   . ASN   B 1 117 ? 32.984 -15.857 -7.077  1.00 14.05 ?  117 ASN   B HA   1 
ATOM   5709 H  HB2  . ASN   B 1 117 ? 31.451 -15.501 -4.750  1.00 14.25 ?  117 ASN   B HB2  1 
ATOM   5710 H  HB3  . ASN   B 1 117 ? 30.898 -15.062 -6.177  1.00 14.25 ?  117 ASN   B HB3  1 
ATOM   5711 H  HD21 . ASN   B 1 117 ? 30.012 -18.456 -5.119  1.00 15.01 ?  117 ASN   B HD21 1 
ATOM   5712 H  HD22 . ASN   B 1 117 ? 30.078 -17.207 -4.310  1.00 15.01 ?  117 ASN   B HD22 1 
ATOM   5713 N  N    . GLN   B 1 118 ? 34.161 -13.447 -5.575  1.00 11.75 ?  118 GLN   B N    1 
ATOM   5714 C  CA   . GLN   B 1 118 ? 34.586 -12.058 -5.713  1.00 12.56 ?  118 GLN   B CA   1 
ATOM   5715 C  C    . GLN   B 1 118 ? 35.657 -11.866 -6.781  1.00 12.85 ?  118 GLN   B C    1 
ATOM   5716 O  O    . GLN   B 1 118 ? 36.125 -10.737 -6.964  1.00 14.06 ?  118 GLN   B O    1 
ATOM   5717 C  CB   . GLN   B 1 118 ? 35.063 -11.526 -4.358  1.00 13.08 ?  118 GLN   B CB   1 
ATOM   5718 C  CG   . GLN   B 1 118 ? 33.982 -11.559 -3.287  1.00 13.22 ?  118 GLN   B CG   1 
ATOM   5719 C  CD   . GLN   B 1 118 ? 32.805 -10.658 -3.623  1.00 13.09 ?  118 GLN   B CD   1 
ATOM   5720 O  OE1  . GLN   B 1 118 ? 32.987 -9.515  -4.059  1.00 13.87 ?  118 GLN   B OE1  1 
ATOM   5721 N  NE2  . GLN   B 1 118 ? 31.592 -11.156 -3.419  1.00 13.38 ?  118 GLN   B NE2  1 
ATOM   5722 H  H    . GLN   B 1 118 ? 34.583 -13.874 -4.953  1.00 14.10 ?  118 GLN   B H    1 
ATOM   5723 H  HA   . GLN   B 1 118 ? 33.819 -11.531 -5.981  1.00 15.07 ?  118 GLN   B HA   1 
ATOM   5724 H  HB2  . GLN   B 1 118 ? 35.809 -12.062 -4.051  1.00 15.70 ?  118 GLN   B HB2  1 
ATOM   5725 H  HB3  . GLN   B 1 118 ? 35.349 -10.600 -4.467  1.00 15.70 ?  118 GLN   B HB3  1 
ATOM   5726 H  HG2  . GLN   B 1 118 ? 33.656 -12.464 -3.197  1.00 15.86 ?  118 GLN   B HG2  1 
ATOM   5727 H  HG3  . GLN   B 1 118 ? 34.365 -11.255 -2.446  1.00 15.86 ?  118 GLN   B HG3  1 
ATOM   5728 H  HE21 . GLN   B 1 118 ? 31.503 -11.954 -3.114  1.00 16.06 ?  118 GLN   B HE21 1 
ATOM   5729 H  HE22 . GLN   B 1 118 ? 30.904 -10.679 -3.597  1.00 16.06 ?  118 GLN   B HE22 1 
ATOM   5730 N  N    . HIS   B 1 119 ? 36.014 -12.926 -7.510  1.00 11.99 ?  119 HIS   B N    1 
ATOM   5731 C  CA   . HIS   B 1 119 ? 37.056 -12.879 -8.526  1.00 12.38 ?  119 HIS   B CA   1 
ATOM   5732 C  C    . HIS   B 1 119 ? 36.577 -13.618 -9.760  1.00 12.48 ?  119 HIS   B C    1 
ATOM   5733 O  O    . HIS   B 1 119 ? 36.078 -14.738 -9.654  1.00 13.13 ?  119 HIS   B O    1 
ATOM   5734 C  CB   . HIS   B 1 119 ? 38.339 -13.506 -7.978  1.00 12.86 ?  119 HIS   B CB   1 
ATOM   5735 C  CG   . HIS   B 1 119 ? 38.817 -12.807 -6.752  1.00 14.13 ?  119 HIS   B CG   1 
ATOM   5736 N  ND1  . HIS   B 1 119 ? 39.605 -11.676 -6.803  1.00 15.53 ?  119 HIS   B ND1  1 
ATOM   5737 C  CD2  . HIS   B 1 119 ? 38.524 -13.008 -5.447  1.00 15.19 ?  119 HIS   B CD2  1 
ATOM   5738 C  CE1  . HIS   B 1 119 ? 39.807 -11.237 -5.575  1.00 16.51 ?  119 HIS   B CE1  1 
ATOM   5739 N  NE2  . HIS   B 1 119 ? 39.157 -12.020 -4.735  1.00 16.62 ?  119 HIS   B NE2  1 
ATOM   5740 H  H    . HIS   B 1 119 ? 35.650 -13.704 -7.436  1.00 14.39 ?  119 HIS   B H    1 
ATOM   5741 H  HA   . HIS   B 1 119 ? 37.235 -11.953 -8.768  1.00 14.86 ?  119 HIS   B HA   1 
ATOM   5742 H  HB2  . HIS   B 1 119 ? 38.167 -14.431 -7.758  1.00 15.43 ?  119 HIS   B HB2  1 
ATOM   5743 H  HB3  . HIS   B 1 119 ? 39.032 -13.443 -8.656  1.00 15.43 ?  119 HIS   B HB3  1 
ATOM   5744 H  HD2  . HIS   B 1 119 ? 37.992 -13.689 -5.100  1.00 18.23 ?  119 HIS   B HD2  1 
ATOM   5745 H  HE1  . HIS   B 1 119 ? 40.336 -10.511 -5.337  1.00 19.82 ?  119 HIS   B HE1  1 
ATOM   5746 H  HE2  . HIS   B 1 119 ? 39.161 -11.949 -3.877  1.00 19.95 ?  119 HIS   B HE2  1 
ATOM   5747 N  N    . GLU   B 1 120 ? 36.732 -13.006 -10.932 1.00 13.12 ?  120 GLU   B N    1 
ATOM   5748 C  CA   . GLU   B 1 120 ? 36.138 -13.596 -12.128 1.00 14.58 ?  120 GLU   B CA   1 
ATOM   5749 C  C    . GLU   B 1 120 ? 36.820 -14.894 -12.543 1.00 13.40 ?  120 GLU   B C    1 
ATOM   5750 O  O    . GLU   B 1 120 ? 36.162 -15.769 -13.117 1.00 13.57 ?  120 GLU   B O    1 
ATOM   5751 C  CB   . GLU   B 1 120 ? 36.136 -12.589 -13.277 1.00 19.29 ?  120 GLU   B CB   1 
ATOM   5752 C  CG   . GLU   B 1 120 ? 35.202 -11.411 -13.044 1.00 26.08 ?  120 GLU   B CG   1 
ATOM   5753 C  CD   . GLU   B 1 120 ? 35.043 -10.529 -14.268 1.00 32.51 ?  120 GLU   B CD   1 
ATOM   5754 O  OE1  . GLU   B 1 120 ? 36.032 -10.356 -15.013 1.00 34.56 ?  120 GLU   B OE1  1 
ATOM   5755 O  OE2  . GLU   B 1 120 ? 33.927 -10.013 -14.486 1.00 35.12 -1 120 GLU   B OE2  1 
ATOM   5756 H  H    . GLU   B 1 120 ? 37.158 -12.269 -11.066 1.00 15.74 ?  120 GLU   B H    1 
ATOM   5757 H  HA   . GLU   B 1 120 ? 35.212 -13.810 -11.934 1.00 17.49 ?  120 GLU   B HA   1 
ATOM   5758 H  HB2  . GLU   B 1 120 ? 37.029 -12.240 -13.391 1.00 23.15 ?  120 GLU   B HB2  1 
ATOM   5759 H  HB3  . GLU   B 1 120 ? 35.846 -13.038 -14.087 1.00 23.15 ?  120 GLU   B HB3  1 
ATOM   5760 H  HG2  . GLU   B 1 120 ? 34.321 -11.745 -12.804 1.00 31.30 ?  120 GLU   B HG2  1 
ATOM   5761 H  HG3  . GLU   B 1 120 ? 35.555 -10.864 -12.326 1.00 31.30 ?  120 GLU   B HG3  1 
ATOM   5762 N  N    . VAL   B 1 121 ? 38.120 -15.033 -12.284 1.00 12.94 ?  121 VAL   B N    1 
ATOM   5763 C  CA   . VAL   B 1 121 ? 38.865 -16.243 -12.628 1.00 12.83 ?  121 VAL   B CA   1 
ATOM   5764 C  C    . VAL   B 1 121 ? 39.979 -16.441 -11.606 1.00 12.06 ?  121 VAL   B C    1 
ATOM   5765 O  O    . VAL   B 1 121 ? 40.653 -15.479 -11.213 1.00 12.72 ?  121 VAL   B O    1 
ATOM   5766 C  CB   . VAL   B 1 121 ? 39.391 -16.193 -14.081 1.00 14.11 ?  121 VAL   B CB   1 
ATOM   5767 C  CG1  . VAL   B 1 121 ? 40.264 -14.967 -14.315 1.00 15.35 ?  121 VAL   B CG1  1 
ATOM   5768 C  CG2  . VAL   B 1 121 ? 40.135 -17.476 -14.431 1.00 15.69 ?  121 VAL   B CG2  1 
ATOM   5769 H  H    . VAL   B 1 121 ? 38.598 -14.428 -11.906 1.00 15.53 ?  121 VAL   B H    1 
ATOM   5770 H  HA   . VAL   B 1 121 ? 38.260 -16.998 -12.564 1.00 15.39 ?  121 VAL   B HA   1 
ATOM   5771 H  HB   . VAL   B 1 121 ? 38.630 -16.127 -14.682 1.00 16.94 ?  121 VAL   B HB   1 
ATOM   5772 H  HG11 . VAL   B 1 121 ? 40.574 -14.968 -15.234 1.00 18.42 ?  121 VAL   B HG11 1 
ATOM   5773 H  HG12 . VAL   B 1 121 ? 39.739 -14.167 -14.146 1.00 18.42 ?  121 VAL   B HG12 1 
ATOM   5774 H  HG13 . VAL   B 1 121 ? 41.022 -14.997 -13.711 1.00 18.42 ?  121 VAL   B HG13 1 
ATOM   5775 H  HG21 . VAL   B 1 121 ? 40.341 -17.473 -15.381 1.00 18.83 ?  121 VAL   B HG21 1 
ATOM   5776 H  HG22 . VAL   B 1 121 ? 40.958 -17.517 -13.919 1.00 18.83 ?  121 VAL   B HG22 1 
ATOM   5777 H  HG23 . VAL   B 1 121 ? 39.574 -18.238 -14.220 1.00 18.83 ?  121 VAL   B HG23 1 
ATOM   5778 N  N    . LEU   B 1 122 ? 40.167 -17.696 -11.171 1.00 11.89 ?  122 LEU   B N    1 
ATOM   5779 C  CA   . LEU   B 1 122 ? 41.149 -18.041 -10.146 1.00 11.61 ?  122 LEU   B CA   1 
ATOM   5780 C  C    . LEU   B 1 122 ? 41.807 -19.372 -10.465 1.00 11.37 ?  122 LEU   B C    1 
ATOM   5781 O  O    . LEU   B 1 122 ? 41.154 -20.295 -10.964 1.00 12.41 ?  122 LEU   B O    1 
ATOM   5782 C  CB   . LEU   B 1 122 ? 40.497 -18.262 -8.768  1.00 13.29 ?  122 LEU   B CB   1 
ATOM   5783 C  CG   . LEU   B 1 122 ? 39.463 -17.244 -8.278  1.00 13.40 ?  122 LEU   B CG   1 
ATOM   5784 C  CD1  . LEU   B 1 122 ? 38.067 -17.597 -8.749  1.00 14.12 ?  122 LEU   B CD1  1 
ATOM   5785 C  CD2  . LEU   B 1 122 ? 39.492 -17.118 -6.762  1.00 13.00 ?  122 LEU   B CD2  1 
ATOM   5786 H  H    . LEU   B 1 122 ? 39.727 -18.375 -11.465 1.00 14.26 ?  122 LEU   B H    1 
ATOM   5787 H  HA   . LEU   B 1 122 ? 41.825 -17.347 -10.078 1.00 13.93 ?  122 LEU   B HA   1 
ATOM   5788 H  HB2  . LEU   B 1 122 ? 40.059 -19.121 -8.781  1.00 15.95 ?  122 LEU   B HB2  1 
ATOM   5789 H  HB3  . LEU   B 1 122 ? 41.206 -18.274 -8.106  1.00 15.95 ?  122 LEU   B HB3  1 
ATOM   5790 H  HG   . LEU   B 1 122 ? 39.682 -16.373 -8.645  1.00 16.08 ?  122 LEU   B HG   1 
ATOM   5791 H  HD11 . LEU   B 1 122 ? 37.438 -16.952 -8.385  1.00 16.95 ?  122 LEU   B HD11 1 
ATOM   5792 H  HD12 . LEU   B 1 122 ? 38.043 -17.566 -9.719  1.00 16.95 ?  122 LEU   B HD12 1 
ATOM   5793 H  HD13 . LEU   B 1 122 ? 37.844 -18.487 -8.440  1.00 16.95 ?  122 LEU   B HD13 1 
ATOM   5794 H  HD21 . LEU   B 1 122 ? 38.814 -16.482 -6.480  1.00 15.60 ?  122 LEU   B HD21 1 
ATOM   5795 H  HD22 . LEU   B 1 122 ? 39.316 -17.985 -6.367  1.00 15.60 ?  122 LEU   B HD22 1 
ATOM   5796 H  HD23 . LEU   B 1 122 ? 40.370 -16.803 -6.487  1.00 15.60 ?  122 LEU   B HD23 1 
ATOM   5797 N  N    . LEU   B 1 123 ? 43.094 -19.471 -10.113 1.00 11.32 ?  123 LEU   B N    1 
ATOM   5798 C  CA   . LEU   B 1 123 ? 43.806 -20.739 -9.986  1.00 11.27 ?  123 LEU   B CA   1 
ATOM   5799 C  C    . LEU   B 1 123 ? 43.775 -21.132 -8.514  1.00 10.91 ?  123 LEU   B C    1 
ATOM   5800 O  O    . LEU   B 1 123 ? 44.127 -20.308 -7.661  1.00 11.51 ?  123 LEU   B O    1 
ATOM   5801 C  CB   . LEU   B 1 123 ? 45.254 -20.558 -10.447 1.00 11.84 ?  123 LEU   B CB   1 
ATOM   5802 C  CG   . LEU   B 1 123 ? 46.201 -21.737 -10.194 1.00 12.01 ?  123 LEU   B CG   1 
ATOM   5803 C  CD1  . LEU   B 1 123 ? 45.778 -22.973 -10.988 1.00 12.86 ?  123 LEU   B CD1  1 
ATOM   5804 C  CD2  . LEU   B 1 123 ? 47.622 -21.329 -10.541 1.00 12.81 ?  123 LEU   B CD2  1 
ATOM   5805 H  H    . LEU   B 1 123 ? 43.586 -18.788 -9.928  1.00 13.58 ?  123 LEU   B H    1 
ATOM   5806 H  HA   . LEU   B 1 123 ? 43.372 -21.428 -10.514 1.00 13.52 ?  123 LEU   B HA   1 
ATOM   5807 H  HB2  . LEU   B 1 123 ? 45.244 -20.400 -11.406 1.00 14.21 ?  123 LEU   B HB2  1 
ATOM   5808 H  HB3  . LEU   B 1 123 ? 45.622 -19.787 -9.996  1.00 14.21 ?  123 LEU   B HB3  1 
ATOM   5809 H  HG   . LEU   B 1 123 ? 46.184 -21.967 -9.251  1.00 14.42 ?  123 LEU   B HG   1 
ATOM   5810 H  HD11 . LEU   B 1 123 ? 46.413 -23.684 -10.820 1.00 15.43 ?  123 LEU   B HD11 1 
ATOM   5811 H  HD12 . LEU   B 1 123 ? 44.892 -23.239 -10.702 1.00 15.43 ?  123 LEU   B HD12 1 
ATOM   5812 H  HD13 . LEU   B 1 123 ? 45.770 -22.748 -11.931 1.00 15.43 ?  123 LEU   B HD13 1 
ATOM   5813 H  HD21 . LEU   B 1 123 ? 48.216 -22.074 -10.379 1.00 15.37 ?  123 LEU   B HD21 1 
ATOM   5814 H  HD22 . LEU   B 1 123 ? 47.656 -21.071 -11.477 1.00 15.37 ?  123 LEU   B HD22 1 
ATOM   5815 H  HD23 . LEU   B 1 123 ? 47.878 -20.573 -9.984  1.00 15.37 ?  123 LEU   B HD23 1 
ATOM   5816 N  N    . ALA   B 1 124 ? 43.348 -22.362 -8.203  1.00 11.18 ?  124 ALA   B N    1 
ATOM   5817 C  CA   . ALA   B 1 124 ? 43.081 -22.673 -6.806  1.00 10.94 ?  124 ALA   B CA   1 
ATOM   5818 C  C    . ALA   B 1 124 ? 43.358 -24.132 -6.477  1.00 10.88 ?  124 ALA   B C    1 
ATOM   5819 O  O    . ALA   B 1 124 ? 43.231 -25.012 -7.340  1.00 11.45 ?  124 ALA   B O    1 
ATOM   5820 C  CB   . ALA   B 1 124 ? 41.626 -22.362 -6.443  1.00 11.72 ?  124 ALA   B CB   1 
ATOM   5821 H  H    . ALA   B 1 124 ? 43.193 -23.005 -8.764  1.00 13.41 ?  124 ALA   B H    1 
ATOM   5822 H  HA   . ALA   B 1 124 ? 43.660 -22.122 -6.259  1.00 13.12 ?  124 ALA   B HA   1 
ATOM   5823 H  HB1  . ALA   B 1 124 ? 41.476 -22.573 -5.510  1.00 14.06 ?  124 ALA   B HB1  1 
ATOM   5824 H  HB2  . ALA   B 1 124 ? 41.463 -21.414 -6.597  1.00 14.06 ?  124 ALA   B HB2  1 
ATOM   5825 H  HB3  . ALA   B 1 124 ? 41.038 -22.890 -7.004  1.00 14.06 ?  124 ALA   B HB3  1 
ATOM   5826 N  N    . PRO   B 1 125 ? 43.644 -24.423 -5.211  1.00 11.29 ?  125 PRO   B N    1 
ATOM   5827 C  CA   . PRO   B 1 125 ? 43.584 -25.789 -4.690  1.00 11.92 ?  125 PRO   B CA   1 
ATOM   5828 C  C    . PRO   B 1 125 ? 42.186 -26.065 -4.144  1.00 12.17 ?  125 PRO   B C    1 
ATOM   5829 O  O    . PRO   B 1 125 ? 41.388 -25.149 -3.934  1.00 12.50 ?  125 PRO   B O    1 
ATOM   5830 C  CB   . PRO   B 1 125 ? 44.570 -25.717 -3.519  1.00 12.75 ?  125 PRO   B CB   1 
ATOM   5831 C  CG   . PRO   B 1 125 ? 44.319 -24.329 -2.955  1.00 12.73 ?  125 PRO   B CG   1 
ATOM   5832 C  CD   . PRO   B 1 125 ? 43.988 -23.454 -4.152  1.00 11.74 ?  125 PRO   B CD   1 
ATOM   5833 H  HA   . PRO   B 1 125 ? 43.856 -26.457 -5.337  1.00 14.30 ?  125 PRO   B HA   1 
ATOM   5834 H  HB2  . PRO   B 1 125 ? 44.364 -26.399 -2.858  1.00 15.31 ?  125 PRO   B HB2  1 
ATOM   5835 H  HB3  . PRO   B 1 125 ? 45.479 -25.801 -3.838  1.00 15.31 ?  125 PRO   B HB3  1 
ATOM   5836 H  HG2  . PRO   B 1 125 ? 43.567 -24.351 -2.337  1.00 15.28 ?  125 PRO   B HG2  1 
ATOM   5837 H  HG3  . PRO   B 1 125 ? 45.115 -24.004 -2.503  1.00 15.28 ?  125 PRO   B HG3  1 
ATOM   5838 H  HD2  . PRO   B 1 125 ? 43.235 -22.876 -3.958  1.00 14.08 ?  125 PRO   B HD2  1 
ATOM   5839 H  HD3  . PRO   B 1 125 ? 44.772 -22.936 -4.416  1.00 14.08 ?  125 PRO   B HD3  1 
ATOM   5840 N  N    . LEU   B 1 126 ? 41.920 -27.344 -3.868  1.00 12.55 ?  126 LEU   B N    1 
ATOM   5841 C  CA   . LEU   B 1 126 ? 40.698 -27.715 -3.161  1.00 13.07 ?  126 LEU   B CA   1 
ATOM   5842 C  C    . LEU   B 1 126 ? 40.806 -27.313 -1.699  1.00 13.26 ?  126 LEU   B C    1 
ATOM   5843 O  O    . LEU   B 1 126 ? 41.696 -27.771 -0.978  1.00 14.87 ?  126 LEU   B O    1 
ATOM   5844 C  CB   . LEU   B 1 126 ? 40.440 -29.211 -3.276  1.00 14.17 ?  126 LEU   B CB   1 
ATOM   5845 C  CG   . LEU   B 1 126 ? 39.914 -29.688 -4.630  1.00 15.31 ?  126 LEU   B CG   1 
ATOM   5846 C  CD1  . LEU   B 1 126 ? 39.959 -31.204 -4.709  1.00 17.29 ?  126 LEU   B CD1  1 
ATOM   5847 C  CD2  . LEU   B 1 126 ? 38.495 -29.196 -4.880  1.00 15.52 ?  126 LEU   B CD2  1 
ATOM   5848 H  H    . LEU   B 1 126 ? 42.428 -28.012 -4.066  1.00 15.06 ?  126 LEU   B H    1 
ATOM   5849 H  HA   . LEU   B 1 126 ? 39.947 -27.244 -3.551  1.00 15.69 ?  126 LEU   B HA   1 
ATOM   5850 H  HB2  . LEU   B 1 126 ? 41.272 -29.679 -3.102  1.00 17.00 ?  126 LEU   B HB2  1 
ATOM   5851 H  HB3  . LEU   B 1 126 ? 39.784 -29.462 -2.605  1.00 17.00 ?  126 LEU   B HB3  1 
ATOM   5852 H  HG   . LEU   B 1 126 ? 40.488 -29.334 -5.331  1.00 18.37 ?  126 LEU   B HG   1 
ATOM   5853 H  HD11 . LEU   B 1 126 ? 39.622 -31.483 -5.576  1.00 20.75 ?  126 LEU   B HD11 1 
ATOM   5854 H  HD12 . LEU   B 1 126 ? 40.872 -31.503 -4.595  1.00 20.75 ?  126 LEU   B HD12 1 
ATOM   5855 H  HD13 . LEU   B 1 126 ? 39.398 -31.570 -4.005  1.00 20.75 ?  126 LEU   B HD13 1 
ATOM   5856 H  HD21 . LEU   B 1 126 ? 38.157 -29.606 -5.689  1.00 18.63 ?  126 LEU   B HD21 1 
ATOM   5857 H  HD22 . LEU   B 1 126 ? 37.940 -29.439 -4.125  1.00 18.63 ?  126 LEU   B HD22 1 
ATOM   5858 H  HD23 . LEU   B 1 126 ? 38.509 -28.229 -4.981  1.00 18.63 ?  126 LEU   B HD23 1 
ATOM   5859 N  N    . LEU   B 1 127 ? 39.878 -26.476 -1.251  1.00 13.11 ?  127 LEU   B N    1 
ATOM   5860 C  CA   . LEU   B 1 127 ? 39.920 -25.980 0.114   1.00 13.60 ?  127 LEU   B CA   1 
ATOM   5861 C  C    . LEU   B 1 127 ? 39.653 -27.101 1.113   1.00 13.34 ?  127 LEU   B C    1 
ATOM   5862 O  O    . LEU   B 1 127 ? 38.840 -28.009 0.883   1.00 13.79 ?  127 LEU   B O    1 
ATOM   5863 C  CB   . LEU   B 1 127 ? 38.890 -24.866 0.312   1.00 13.78 ?  127 LEU   B CB   1 
ATOM   5864 C  CG   . LEU   B 1 127 ? 39.075 -23.605 -0.534  1.00 14.38 ?  127 LEU   B CG   1 
ATOM   5865 C  CD1  . LEU   B 1 127 ? 37.956 -22.635 -0.220  1.00 14.54 ?  127 LEU   B CD1  1 
ATOM   5866 C  CD2  . LEU   B 1 127 ? 40.435 -22.958 -0.293  1.00 15.18 ?  127 LEU   B CD2  1 
ATOM   5867 H  H    . LEU   B 1 127 ? 39.213 -26.174 -1.715  1.00 15.74 ?  127 LEU   B H    1 
ATOM   5868 H  HA   . LEU   B 1 127 ? 40.800 -25.612 0.293   1.00 16.32 ?  127 LEU   B HA   1 
ATOM   5869 H  HB2  . LEU   B 1 127 ? 38.010 -25.222 0.108   1.00 16.54 ?  127 LEU   B HB2  1 
ATOM   5870 H  HB3  . LEU   B 1 127 ? 38.912 -24.588 1.243   1.00 16.54 ?  127 LEU   B HB3  1 
ATOM   5871 H  HG   . LEU   B 1 127 ? 39.000 -23.833 -1.472  1.00 17.26 ?  127 LEU   B HG   1 
ATOM   5872 H  HD11 . LEU   B 1 127 ? 38.075 -21.826 -0.751  1.00 17.45 ?  127 LEU   B HD11 1 
ATOM   5873 H  HD12 . LEU   B 1 127 ? 37.102 -23.042 -0.433  1.00 17.45 ?  127 LEU   B HD12 1 
ATOM   5874 H  HD13 . LEU   B 1 127 ? 37.986 -22.407 0.725   1.00 17.45 ?  127 LEU   B HD13 1 
ATOM   5875 H  HD21 . LEU   B 1 127 ? 40.471 -22.104 -0.753  1.00 18.22 ?  127 LEU   B HD21 1 
ATOM   5876 H  HD22 . LEU   B 1 127 ? 40.559 -22.823 0.661   1.00 18.22 ?  127 LEU   B HD22 1 
ATOM   5877 H  HD23 . LEU   B 1 127 ? 41.125 -23.547 -0.635  1.00 18.22 ?  127 LEU   B HD23 1 
ATOM   5878 N  N    . SER   B 1 128 ? 40.348 -27.019 2.238   1.00 13.24 ?  128 SER   B N    1 
ATOM   5879 C  CA   . SER   B 1 128 ? 40.234 -27.933 3.360   1.00 13.76 ?  128 SER   B CA   1 
ATOM   5880 C  C    . SER   B 1 128 ? 40.730 -29.338 3.037   1.00 14.59 ?  128 SER   B C    1 
ATOM   5881 O  O    . SER   B 1 128 ? 40.634 -30.220 3.890   1.00 15.80 ?  128 SER   B O    1 
ATOM   5882 C  CB   . SER   B 1 128 ? 38.831 -27.950 3.983   1.00 14.30 ?  128 SER   B CB   1 
ATOM   5883 O  OG   . SER   B 1 128 ? 38.503 -26.675 4.528   1.00 14.75 ?  128 SER   B OG   1 
ATOM   5884 H  H    . SER   B 1 128 ? 40.934 -26.403 2.375   1.00 15.89 ?  128 SER   B H    1 
ATOM   5885 H  HA   . SER   B 1 128 ? 40.820 -27.602 4.045   1.00 16.51 ?  128 SER   B HA   1 
ATOM   5886 H  HB2  . SER   B 1 128 ? 38.179 -28.189 3.303   1.00 17.16 ?  128 SER   B HB2  1 
ATOM   5887 H  HB3  . SER   B 1 128 ? 38.813 -28.617 4.697   1.00 17.16 ?  128 SER   B HB3  1 
ATOM   5888 H  HG   . SER   B 1 128 ? 39.065 -26.469 5.114   1.00 17.70 ?  128 SER   B HG   1 
ATOM   5889 N  N    . ALA   B 1 129 ? 41.310 -29.556 1.855   1.00 15.49 ?  129 ALA   B N    1 
ATOM   5890 C  CA   . ALA   B 1 129 ? 41.857 -30.854 1.497   1.00 16.56 ?  129 ALA   B CA   1 
ATOM   5891 C  C    . ALA   B 1 129 ? 43.245 -31.035 2.099   1.00 15.65 ?  129 ALA   B C    1 
ATOM   5892 O  O    . ALA   B 1 129 ? 43.805 -30.137 2.744   1.00 15.57 ?  129 ALA   B O    1 
ATOM   5893 C  CB   . ALA   B 1 129 ? 41.916 -31.013 -0.021  1.00 18.72 ?  129 ALA   B CB   1 
ATOM   5894 H  H    . ALA   B 1 129 ? 41.395 -28.961 1.234   1.00 18.58 ?  129 ALA   B H    1 
ATOM   5895 H  HA   . ALA   B 1 129 ? 41.278 -31.547 1.847   1.00 19.87 ?  129 ALA   B HA   1 
ATOM   5896 H  HB1  . ALA   B 1 129 ? 42.272 -31.892 -0.234  1.00 22.46 ?  129 ALA   B HB1  1 
ATOM   5897 H  HB2  . ALA   B 1 129 ? 41.022 -30.924 -0.385  1.00 22.46 ?  129 ALA   B HB2  1 
ATOM   5898 H  HB3  . ALA   B 1 129 ? 42.494 -30.326 -0.390  1.00 22.46 ?  129 ALA   B HB3  1 
ATOM   5899 N  N    . GLY   B 1 130 ? 43.806 -32.222 1.874   1.00 15.68 ?  130 GLY   B N    1 
ATOM   5900 C  CA   . GLY   B 1 130 ? 45.190 -32.459 2.234   1.00 16.51 ?  130 GLY   B CA   1 
ATOM   5901 C  C    . GLY   B 1 130 ? 45.395 -32.358 3.727   1.00 16.41 ?  130 GLY   B C    1 
ATOM   5902 O  O    . GLY   B 1 130 ? 44.691 -32.998 4.522   1.00 17.21 ?  130 GLY   B O    1 
ATOM   5903 H  H    . GLY   B 1 130 ? 43.406 -32.893 1.512   1.00 18.82 ?  130 GLY   B H    1 
ATOM   5904 H  HA2  . GLY   B 1 130 ? 45.452 -33.346 1.944   1.00 19.82 ?  130 GLY   B HA2  1 
ATOM   5905 H  HA3  . GLY   B 1 130 ? 45.755 -31.807 1.795   1.00 19.82 ?  130 GLY   B HA3  1 
ATOM   5906 N  N    . ILE   B 1 131 ? 46.370 -31.532 4.118   1.00 16.80 ?  131 ILE   B N    1 
ATOM   5907 C  CA   . ILE   B 1 131 ? 46.723 -31.394 5.520   1.00 17.56 ?  131 ILE   B CA   1 
ATOM   5908 C  C    . ILE   B 1 131 ? 45.601 -30.799 6.350   1.00 16.54 ?  131 ILE   B C    1 
ATOM   5909 O  O    . ILE   B 1 131 ? 45.660 -30.867 7.579   1.00 18.22 ?  131 ILE   B O    1 
ATOM   5910 C  CB   . ILE   B 1 131 ? 48.043 -30.609 5.716   1.00 19.42 ?  131 ILE   B CB   1 
ATOM   5911 C  CG1  . ILE   B 1 131 ? 47.871 -29.124 5.356   1.00 20.76 ?  131 ILE   B CG1  1 
ATOM   5912 C  CG2  . ILE   B 1 131 ? 49.166 -31.249 4.904   1.00 20.58 ?  131 ILE   B CG2  1 
ATOM   5913 C  CD1  . ILE   B 1 131 ? 49.100 -28.278 5.657   1.00 21.97 ?  131 ILE   B CD1  1 
ATOM   5914 H  H    . ILE   B 1 131 ? 46.843 -31.050 3.583   1.00 20.16 ?  131 ILE   B H    1 
ATOM   5915 H  HA   . ILE   B 1 131 ? 46.876 -32.283 5.870   1.00 21.07 ?  131 ILE   B HA   1 
ATOM   5916 H  HB   . ILE   B 1 131 ? 48.280 -30.663 6.655   1.00 23.30 ?  131 ILE   B HB   1 
ATOM   5917 H  HG12 . ILE   B 1 131 ? 47.682 -29.054 4.408   1.00 24.91 ?  131 ILE   B HG12 1 
ATOM   5918 H  HG13 . ILE   B 1 131 ? 47.130 -28.754 5.865   1.00 24.91 ?  131 ILE   B HG13 1 
ATOM   5919 H  HG21 . ILE   B 1 131 ? 50.005 -30.846 5.166   1.00 24.70 ?  131 ILE   B HG21 1 
ATOM   5920 H  HG22 . ILE   B 1 131 ? 49.175 -32.198 5.082   1.00 24.70 ?  131 ILE   B HG22 1 
ATOM   5921 H  HG23 . ILE   B 1 131 ? 48.996 -31.086 3.962   1.00 24.70 ?  131 ILE   B HG23 1 
ATOM   5922 H  HD11 . ILE   B 1 131 ? 48.881 -27.346 5.508   1.00 26.36 ?  131 ILE   B HD11 1 
ATOM   5923 H  HD12 . ILE   B 1 131 ? 49.354 -28.416 6.583   1.00 26.36 ?  131 ILE   B HD12 1 
ATOM   5924 H  HD13 . ILE   B 1 131 ? 49.820 -28.551 5.070   1.00 26.36 ?  131 ILE   B HD13 1 
ATOM   5925 N  N    . PHE   B 1 132 ? 44.578 -30.217 5.713   1.00 15.13 ?  132 PHE   B N    1 
ATOM   5926 C  CA   . PHE   B 1 132 ? 43.414 -29.715 6.436   1.00 15.68 ?  132 PHE   B CA   1 
ATOM   5927 C  C    . PHE   B 1 132 ? 42.391 -30.809 6.758   1.00 16.92 ?  132 PHE   B C    1 
ATOM   5928 O  O    . PHE   B 1 132 ? 41.476 -30.561 7.551   1.00 18.62 ?  132 PHE   B O    1 
ATOM   5929 C  CB   . PHE   B 1 132 ? 42.739 -28.583 5.650   1.00 14.95 ?  132 PHE   B CB   1 
ATOM   5930 C  CG   . PHE   B 1 132 ? 43.435 -27.238 5.761   1.00 14.98 ?  132 PHE   B CG   1 
ATOM   5931 C  CD1  . PHE   B 1 132 ? 44.722 -27.047 5.274   1.00 15.75 ?  132 PHE   B CD1  1 
ATOM   5932 C  CD2  . PHE   B 1 132 ? 42.770 -26.144 6.306   1.00 14.50 ?  132 PHE   B CD2  1 
ATOM   5933 C  CE1  . PHE   B 1 132 ? 45.336 -25.803 5.365   1.00 16.48 ?  132 PHE   B CE1  1 
ATOM   5934 C  CE2  . PHE   B 1 132 ? 43.377 -24.901 6.389   1.00 15.08 ?  132 PHE   B CE2  1 
ATOM   5935 C  CZ   . PHE   B 1 132 ? 44.658 -24.736 5.922   1.00 16.08 ?  132 PHE   B CZ   1 
ATOM   5936 H  H    . PHE   B 1 132 ? 44.536 -30.100 4.861   1.00 18.16 ?  132 PHE   B H    1 
ATOM   5937 H  HA   . PHE   B 1 132 ? 43.715 -29.341 7.277   1.00 18.81 ?  132 PHE   B HA   1 
ATOM   5938 H  HB2  . PHE   B 1 132 ? 42.730 -28.826 4.713   1.00 17.94 ?  132 PHE   B HB2  1 
ATOM   5939 H  HB3  . PHE   B 1 132 ? 41.834 -28.474 5.975   1.00 17.94 ?  132 PHE   B HB3  1 
ATOM   5940 H  HD1  . PHE   B 1 132 ? 45.184 -27.763 4.901   1.00 18.90 ?  132 PHE   B HD1  1 
ATOM   5941 H  HD2  . PHE   B 1 132 ? 41.906 -26.254 6.626   1.00 17.40 ?  132 PHE   B HD2  1 
ATOM   5942 H  HE1  . PHE   B 1 132 ? 46.203 -25.688 5.046   1.00 19.78 ?  132 PHE   B HE1  1 
ATOM   5943 H  HE2  . PHE   B 1 132 ? 42.923 -24.182 6.769   1.00 18.10 ?  132 PHE   B HE2  1 
ATOM   5944 H  HZ   . PHE   B 1 132 ? 45.069 -23.899 5.983   1.00 19.30 ?  132 PHE   B HZ   1 
ATOM   5945 N  N    . GLY   B 1 133 ? 42.502 -32.003 6.161   1.00 16.83 ?  133 GLY   B N    1 
ATOM   5946 C  CA   . GLY   B 1 133 ? 41.791 -33.171 6.650   1.00 17.87 ?  133 GLY   B CA   1 
ATOM   5947 C  C    . GLY   B 1 133 ? 40.396 -33.432 6.110   1.00 18.21 ?  133 GLY   B C    1 
ATOM   5948 O  O    . GLY   B 1 133 ? 39.813 -34.461 6.462   1.00 20.05 ?  133 GLY   B O    1 
ATOM   5949 H  H    . GLY   B 1 133 ? 42.994 -32.152 5.470   1.00 20.19 ?  133 GLY   B H    1 
ATOM   5950 H  HA2  . GLY   B 1 133 ? 42.327 -33.954 6.455   1.00 21.44 ?  133 GLY   B HA2  1 
ATOM   5951 H  HA3  . GLY   B 1 133 ? 41.719 -33.098 7.614   1.00 21.44 ?  133 GLY   B HA3  1 
ATOM   5952 N  N    . ALA   B 1 134 ? 39.829 -32.557 5.289   1.00 17.18 ?  134 ALA   B N    1 
ATOM   5953 C  CA   . ALA   B 1 134 ? 38.503 -32.836 4.756   1.00 17.19 ?  134 ALA   B CA   1 
ATOM   5954 C  C    . ALA   B 1 134 ? 38.584 -33.834 3.603   1.00 17.09 ?  134 ALA   B C    1 
ATOM   5955 O  O    . ALA   B 1 134 ? 39.636 -34.032 2.989   1.00 17.94 ?  134 ALA   B O    1 
ATOM   5956 C  CB   . ALA   B 1 134 ? 37.832 -31.553 4.270   1.00 17.68 ?  134 ALA   B CB   1 
ATOM   5957 H  H    . ALA   B 1 134 ? 40.177 -31.809 5.036   1.00 20.62 ?  134 ALA   B H    1 
ATOM   5958 H  HA   . ALA   B 1 134 ? 37.951 -33.218 5.461   1.00 20.63 ?  134 ALA   B HA   1 
ATOM   5959 H  HB1  . ALA   B 1 134 ? 36.947 -31.769 3.937   1.00 21.21 ?  134 ALA   B HB1  1 
ATOM   5960 H  HB2  . ALA   B 1 134 ? 37.764 -30.931 5.011   1.00 21.21 ?  134 ALA   B HB2  1 
ATOM   5961 H  HB3  . ALA   B 1 134 ? 38.369 -31.168 3.561   1.00 21.21 ?  134 ALA   B HB3  1 
ATOM   5962 N  N    . ASP   B 1 135 ? 37.450 -34.460 3.314   1.00 17.42 ?  135 ASP   B N    1 
ATOM   5963 C  CA   . ASP   B 1 135 ? 37.353 -35.355 2.171   1.00 18.32 ?  135 ASP   B CA   1 
ATOM   5964 C  C    . ASP   B 1 135 ? 37.457 -34.524 0.900   1.00 17.19 ?  135 ASP   B C    1 
ATOM   5965 O  O    . ASP   B 1 135 ? 36.603 -33.657 0.670   1.00 16.85 ?  135 ASP   B O    1 
ATOM   5966 C  CB   . ASP   B 1 135 ? 36.009 -36.078 2.221   1.00 20.17 ?  135 ASP   B CB   1 
ATOM   5967 C  CG   . ASP   B 1 135 ? 35.822 -37.069 1.087   1.00 22.19 ?  135 ASP   B CG   1 
ATOM   5968 O  OD1  . ASP   B 1 135 ? 36.696 -37.142 0.199   1.00 22.03 ?  135 ASP   B OD1  1 
ATOM   5969 O  OD2  . ASP   B 1 135 ? 34.797 -37.794 1.097   1.00 25.00 -1 135 ASP   B OD2  1 
ATOM   5970 H  H    . ASP   B 1 135 ? 36.725 -34.381 3.766   1.00 20.91 ?  135 ASP   B H    1 
ATOM   5971 H  HA   . ASP   B 1 135 ? 38.071 -36.009 2.208   1.00 21.99 ?  135 ASP   B HA   1 
ATOM   5972 H  HB2  . ASP   B 1 135 ? 35.946 -36.561 3.055   1.00 24.21 ?  135 ASP   B HB2  1 
ATOM   5973 H  HB3  . ASP   B 1 135 ? 35.303 -35.421 2.155   1.00 24.21 ?  135 ASP   B HB3  1 
ATOM   5974 N  N    . PRO   B 1 136 ? 38.472 -34.732 0.060   1.00 17.30 ?  136 PRO   B N    1 
ATOM   5975 C  CA   . PRO   B 1 136 ? 38.573 -33.911 -1.156  1.00 16.38 ?  136 PRO   B CA   1 
ATOM   5976 C  C    . PRO   B 1 136 ? 37.387 -34.069 -2.086  1.00 15.79 ?  136 PRO   B C    1 
ATOM   5977 O  O    . PRO   B 1 136 ? 37.068 -33.121 -2.812  1.00 14.96 ?  136 PRO   B O    1 
ATOM   5978 C  CB   . PRO   B 1 136 ? 39.889 -34.382 -1.793  1.00 17.43 ?  136 PRO   B CB   1 
ATOM   5979 C  CG   . PRO   B 1 136 ? 40.085 -35.776 -1.254  1.00 18.56 ?  136 PRO   B CG   1 
ATOM   5980 C  CD   . PRO   B 1 136 ? 39.553 -35.728 0.148   1.00 18.22 ?  136 PRO   B CD   1 
ATOM   5981 H  HA   . PRO   B 1 136 ? 38.659 -32.972 -0.923  1.00 19.66 ?  136 PRO   B HA   1 
ATOM   5982 H  HB2  . PRO   B 1 136 ? 39.803 -34.394 -2.760  1.00 20.92 ?  136 PRO   B HB2  1 
ATOM   5983 H  HB3  . PRO   B 1 136 ? 40.613 -33.799 -1.518  1.00 20.92 ?  136 PRO   B HB3  1 
ATOM   5984 H  HG2  . PRO   B 1 136 ? 39.580 -36.411 -1.787  1.00 22.28 ?  136 PRO   B HG2  1 
ATOM   5985 H  HG3  . PRO   B 1 136 ? 41.028 -36.000 -1.253  1.00 22.28 ?  136 PRO   B HG3  1 
ATOM   5986 H  HD2  . PRO   B 1 136 ? 39.194 -36.589 0.408   1.00 21.86 ?  136 PRO   B HD2  1 
ATOM   5987 H  HD3  . PRO   B 1 136 ? 40.239 -35.425 0.767   1.00 21.86 ?  136 PRO   B HD3  1 
ATOM   5988 N  N    . ILE   B 1 137 ? 36.728 -35.236 -2.090  1.00 16.19 ?  137 ILE   B N    1 
ATOM   5989 C  CA   . ILE   B 1 137 ? 35.512 -35.401 -2.883  1.00 16.64 ?  137 ILE   B CA   1 
ATOM   5990 C  C    . ILE   B 1 137 ? 34.438 -34.429 -2.411  1.00 16.28 ?  137 ILE   B C    1 
ATOM   5991 O  O    . ILE   B 1 137 ? 33.723 -33.818 -3.217  1.00 15.75 ?  137 ILE   B O    1 
ATOM   5992 C  CB   . ILE   B 1 137 ? 35.034 -36.865 -2.826  1.00 18.90 ?  137 ILE   B CB   1 
ATOM   5993 C  CG1  . ILE   B 1 137 ? 36.052 -37.780 -3.514  1.00 21.40 ?  137 ILE   B CG1  1 
ATOM   5994 C  CG2  . ILE   B 1 137 ? 33.647 -37.004 -3.456  1.00 19.32 ?  137 ILE   B CG2  1 
ATOM   5995 C  CD1  . ILE   B 1 137 ? 35.709 -39.254 -3.448  1.00 23.65 ?  137 ILE   B CD1  1 
ATOM   5996 H  H    . ILE   B 1 137 ? 36.966 -35.938 -1.653  1.00 19.43 ?  137 ILE   B H    1 
ATOM   5997 H  HA   . ILE   B 1 137 ? 35.710 -35.196 -3.811  1.00 19.96 ?  137 ILE   B HA   1 
ATOM   5998 H  HB   . ILE   B 1 137 ? 34.966 -37.128 -1.899  1.00 22.68 ?  137 ILE   B HB   1 
ATOM   5999 H  HG12 . ILE   B 1 137 ? 36.112 -37.536 -4.450  1.00 25.68 ?  137 ILE   B HG12 1 
ATOM   6000 H  HG13 . ILE   B 1 137 ? 36.913 -37.661 -3.087  1.00 25.68 ?  137 ILE   B HG13 1 
ATOM   6001 H  HG21 . ILE   B 1 137 ? 33.384 -37.937 -3.465  1.00 23.19 ?  137 ILE   B HG21 1 
ATOM   6002 H  HG22 . ILE   B 1 137 ? 33.002 -36.501 -2.936  1.00 23.19 ?  137 ILE   B HG22 1 
ATOM   6003 H  HG23 . ILE   B 1 137 ? 33.675 -36.664 -4.365  1.00 23.19 ?  137 ILE   B HG23 1 
ATOM   6004 H  HD11 . ILE   B 1 137 ? 36.390 -39.743 -3.929  1.00 28.39 ?  137 ILE   B HD11 1 
ATOM   6005 H  HD12 . ILE   B 1 137 ? 35.687 -39.536 -2.519  1.00 28.39 ?  137 ILE   B HD12 1 
ATOM   6006 H  HD13 . ILE   B 1 137 ? 34.847 -39.410 -3.864  1.00 28.39 ?  137 ILE   B HD13 1 
ATOM   6007 N  N    . HIS   B 1 138 ? 34.311 -34.268 -1.095  1.00 16.39 ?  138 HIS   B N    1 
ATOM   6008 C  CA   . HIS   B 1 138 ? 33.355 -33.308 -0.562  1.00 16.64 ?  138 HIS   B CA   1 
ATOM   6009 C  C    . HIS   B 1 138 ? 33.772 -31.880 -0.881  1.00 15.85 ?  138 HIS   B C    1 
ATOM   6010 O  O    . HIS   B 1 138 ? 32.925 -31.035 -1.184  1.00 16.26 ?  138 HIS   B O    1 
ATOM   6011 C  CB   . HIS   B 1 138 ? 33.230 -33.484 0.944   1.00 18.05 ?  138 HIS   B CB   1 
ATOM   6012 C  CG   . HIS   B 1 138 ? 32.295 -32.504 1.577   1.00 18.90 ?  138 HIS   B CG   1 
ATOM   6013 N  ND1  . HIS   B 1 138 ? 30.952 -32.450 1.269   1.00 20.18 ?  138 HIS   B ND1  1 
ATOM   6014 C  CD2  . HIS   B 1 138 ? 32.512 -31.522 2.484   1.00 19.47 ?  138 HIS   B CD2  1 
ATOM   6015 C  CE1  . HIS   B 1 138 ? 30.380 -31.488 1.969   1.00 20.36 ?  138 HIS   B CE1  1 
ATOM   6016 N  NE2  . HIS   B 1 138 ? 31.304 -30.913 2.718   1.00 19.78 ?  138 HIS   B NE2  1 
ATOM   6017 H  H    . HIS   B 1 138 ? 34.764 -34.697 -0.504  1.00 19.66 ?  138 HIS   B H    1 
ATOM   6018 H  HA   . HIS   B 1 138 ? 32.486 -33.471 -0.962  1.00 19.97 ?  138 HIS   B HA   1 
ATOM   6019 H  HB2  . HIS   B 1 138 ? 32.895 -34.375 1.131   1.00 21.66 ?  138 HIS   B HB2  1 
ATOM   6020 H  HB3  . HIS   B 1 138 ? 34.102 -33.366 1.349   1.00 21.66 ?  138 HIS   B HB3  1 
ATOM   6021 H  HD2  . HIS   B 1 138 ? 33.321 -31.308 2.884   1.00 23.36 ?  138 HIS   B HD2  1 
ATOM   6022 H  HE1  . HIS   B 1 138 ? 29.475 -31.263 1.946   1.00 24.43 ?  138 HIS   B HE1  1 
ATOM   6023 H  HE2  . HIS   B 1 138 ? 31.166 -30.258 3.260   1.00 23.74 ?  138 HIS   B HE2  1 
ATOM   6024 N  N    . SER   B 1 139 ? 35.066 -31.582 -0.804  1.00 15.35 ?  139 SER   B N    1 
ATOM   6025 C  CA   . SER   B 1 139 ? 35.506 -30.232 -1.127  1.00 14.54 ?  139 SER   B CA   1 
ATOM   6026 C  C    . SER   B 1 139 ? 35.166 -29.885 -2.568  1.00 14.00 ?  139 SER   B C    1 
ATOM   6027 O  O    . SER   B 1 139 ? 34.723 -28.768 -2.854  1.00 13.89 ?  139 SER   B O    1 
ATOM   6028 C  CB   . SER   B 1 139 ? 37.004 -30.104 -0.877  1.00 14.87 ?  139 SER   B CB   1 
ATOM   6029 O  OG   . SER   B 1 139 ? 37.405 -28.769 -1.123  1.00 15.09 ?  139 SER   B OG   1 
ATOM   6030 H  H    . SER   B 1 139 ? 35.688 -32.126 -0.575  1.00 18.42 ?  139 SER   B H    1 
ATOM   6031 H  HA   . SER   B 1 139 ? 35.047 -29.604 -0.551  1.00 17.45 ?  139 SER   B HA   1 
ATOM   6032 H  HB2  . SER   B 1 139 ? 37.198 -30.334 0.046   1.00 17.85 ?  139 SER   B HB2  1 
ATOM   6033 H  HB3  . SER   B 1 139 ? 37.484 -30.699 -1.477  1.00 17.85 ?  139 SER   B HB3  1 
ATOM   6034 H  HG   . SER   B 1 139 ? 38.234 -28.686 -0.986  1.00 18.11 ?  139 SER   B HG   1 
ATOM   6035 N  N    . LEU   B 1 140 ? 35.361 -30.832 -3.488  1.00 13.31 ?  140 LEU   B N    1 
ATOM   6036 C  CA   . LEU   B 1 140 ? 35.005 -30.590 -4.879  1.00 13.49 ?  140 LEU   B CA   1 
ATOM   6037 C  C    . LEU   B 1 140 ? 33.506 -30.360 -5.021  1.00 13.82 ?  140 LEU   B C    1 
ATOM   6038 O  O    . LEU   B 1 140 ? 33.075 -29.479 -5.768  1.00 13.94 ?  140 LEU   B O    1 
ATOM   6039 C  CB   . LEU   B 1 140 ? 35.471 -31.759 -5.748  1.00 13.42 ?  140 LEU   B CB   1 
ATOM   6040 C  CG   . LEU   B 1 140 ? 35.123 -31.647 -7.229  1.00 13.65 ?  140 LEU   B CG   1 
ATOM   6041 C  CD1  . LEU   B 1 140 ? 35.679 -30.372 -7.836  1.00 14.83 ?  140 LEU   B CD1  1 
ATOM   6042 C  CD2  . LEU   B 1 140 ? 35.613 -32.875 -7.978  1.00 14.66 ?  140 LEU   B CD2  1 
ATOM   6043 H  H    . LEU   B 1 140 ? 35.691 -31.613 -3.334  1.00 15.97 ?  140 LEU   B H    1 
ATOM   6044 H  HA   . LEU   B 1 140 ? 35.467 -29.791 -5.183  1.00 16.19 ?  140 LEU   B HA   1 
ATOM   6045 H  HB2  . LEU   B 1 140 ? 36.437 -31.831 -5.680  1.00 16.10 ?  140 LEU   B HB2  1 
ATOM   6046 H  HB3  . LEU   B 1 140 ? 35.061 -32.572 -5.416  1.00 16.10 ?  140 LEU   B HB3  1 
ATOM   6047 H  HG   . LEU   B 1 140 ? 34.161 -31.613 -7.318  1.00 16.38 ?  140 LEU   B HG   1 
ATOM   6048 H  HD11 . LEU   B 1 140 ? 35.550 -30.403 -8.796  1.00 17.79 ?  140 LEU   B HD11 1 
ATOM   6049 H  HD12 . LEU   B 1 140 ? 35.201 -29.612 -7.464  1.00 17.79 ?  140 LEU   B HD12 1 
ATOM   6050 H  HD13 . LEU   B 1 140 ? 36.621 -30.307 -7.628  1.00 17.79 ?  140 LEU   B HD13 1 
ATOM   6051 H  HD21 . LEU   B 1 140 ? 35.377 -32.779 -8.915  1.00 17.60 ?  140 LEU   B HD21 1 
ATOM   6052 H  HD22 . LEU   B 1 140 ? 36.571 -32.942 -7.880  1.00 17.60 ?  140 LEU   B HD22 1 
ATOM   6053 H  HD23 . LEU   B 1 140 ? 35.179 -33.657 -7.606  1.00 17.60 ?  140 LEU   B HD23 1 
ATOM   6054 N  N    . ARG   B 1 141 ? 32.701 -31.153 -4.309  1.00 14.20 ?  141 ARG   B N    1 
ATOM   6055 C  CA   . ARG   B 1 141 ? 31.251 -30.977 -4.293  1.00 15.07 ?  141 ARG   B CA   1 
ATOM   6056 C  C    . ARG   B 1 141 ? 30.869 -29.568 -3.863  1.00 14.44 ?  141 ARG   B C    1 
ATOM   6057 O  O    . ARG   B 1 141 ? 30.069 -28.891 -4.525  1.00 14.74 ?  141 ARG   B O    1 
ATOM   6058 C  CB   . ARG   B 1 141 ? 30.662 -32.014 -3.326  1.00 16.80 ?  141 ARG   B CB   1 
ATOM   6059 C  CG   . ARG   B 1 141 ? 29.201 -31.888 -2.978  1.00 18.67 ?  141 ARG   B CG   1 
ATOM   6060 C  CD   . ARG   B 1 141 ? 28.382 -32.515 -4.031  1.00 20.48 ?  141 ARG   B CD   1 
ATOM   6061 N  NE   . ARG   B 1 141 ? 28.140 -31.614 -5.146  1.00 21.05 ?  141 ARG   B NE   1 
ATOM   6062 C  CZ   . ARG   B 1 141 ? 28.150 -31.979 -6.420  1.00 20.65 ?  141 ARG   B CZ   1 
ATOM   6063 N  NH1  . ARG   B 1 141 ? 28.583 -33.173 -6.796  1.00 20.55 ?  141 ARG   B NH1  1 
ATOM   6064 N  NH2  . ARG   B 1 141 ? 27.716 -31.123 -7.341  1.00 21.56 ?  141 ARG   B NH2  1 
ATOM   6065 H  H    . ARG   B 1 141 ? 32.977 -31.802 -3.821  1.00 17.04 ?  141 ARG   B H    1 
ATOM   6066 H  HA   . ARG   B 1 141 ? 30.891 -31.140 -5.177  1.00 18.08 ?  141 ARG   B HA   1 
ATOM   6067 H  HB2  . ARG   B 1 141 ? 30.798 -32.897 -3.712  1.00 20.16 ?  141 ARG   B HB2  1 
ATOM   6068 H  HB3  . ARG   B 1 141 ? 31.156 -31.963 -2.495  1.00 20.16 ?  141 ARG   B HB3  1 
ATOM   6069 H  HG2  . ARG   B 1 141 ? 29.034 -32.342 -2.139  1.00 22.41 ?  141 ARG   B HG2  1 
ATOM   6070 H  HG3  . ARG   B 1 141 ? 28.952 -30.950 -2.904  1.00 22.41 ?  141 ARG   B HG3  1 
ATOM   6071 H  HD2  . ARG   B 1 141 ? 28.837 -33.310 -4.355  1.00 24.58 ?  141 ARG   B HD2  1 
ATOM   6072 H  HD3  . ARG   B 1 141 ? 27.531 -32.764 -3.651  1.00 24.58 ?  141 ARG   B HD3  1 
ATOM   6073 H  HE   . ARG   B 1 141 ? 27.977 -30.789 -4.965  1.00 25.26 ?  141 ARG   B HE   1 
ATOM   6074 H  HH11 . ARG   B 1 141 ? 28.855 -33.743 -6.213  1.00 24.66 ?  141 ARG   B HH11 1 
ATOM   6075 H  HH12 . ARG   B 1 141 ? 28.587 -33.381 -7.627  1.00 24.66 ?  141 ARG   B HH12 1 
ATOM   6076 H  HH21 . ARG   B 1 141 ? 27.441 -30.340 -7.109  1.00 25.88 ?  141 ARG   B HH21 1 
ATOM   6077 H  HH22 . ARG   B 1 141 ? 27.738 -31.338 -8.175  1.00 25.88 ?  141 ARG   B HH22 1 
ATOM   6078 N  N    . VAL   B 1 142 ? 31.413 -29.116 -2.736  1.00 14.09 ?  142 VAL   B N    1 
ATOM   6079 C  CA   . VAL   B 1 142 ? 31.071 -27.784 -2.254  1.00 14.04 ?  142 VAL   B CA   1 
ATOM   6080 C  C    . VAL   B 1 142 ? 31.545 -26.725 -3.240  1.00 14.11 ?  142 VAL   B C    1 
ATOM   6081 O  O    . VAL   B 1 142 ? 30.842 -25.738 -3.496  1.00 14.60 ?  142 VAL   B O    1 
ATOM   6082 C  CB   . VAL   B 1 142 ? 31.617 -27.551 -0.834  1.00 14.69 ?  142 VAL   B CB   1 
ATOM   6083 C  CG1  . VAL   B 1 142 ? 31.308 -26.131 -0.371  1.00 14.91 ?  142 VAL   B CG1  1 
ATOM   6084 C  CG2  . VAL   B 1 142 ? 31.037 -28.572 0.133   1.00 15.51 ?  142 VAL   B CG2  1 
ATOM   6085 H  H    . VAL   B 1 142 ? 31.971 -29.549 -2.244  1.00 16.91 ?  142 VAL   B H    1 
ATOM   6086 H  HA   . VAL   B 1 142 ? 30.109 -27.716 -2.205  1.00 16.84 ?  142 VAL   B HA   1 
ATOM   6087 H  HB   . VAL   B 1 142 ? 32.582 -27.661 -0.844  1.00 17.63 ?  142 VAL   B HB   1 
ATOM   6088 H  HG11 . VAL   B 1 142 ? 31.491 -26.065 0.579   1.00 17.90 ?  142 VAL   B HG11 1 
ATOM   6089 H  HG12 . VAL   B 1 142 ? 31.872 -25.508 -0.858  1.00 17.90 ?  142 VAL   B HG12 1 
ATOM   6090 H  HG13 . VAL   B 1 142 ? 30.375 -25.940 -0.543  1.00 17.90 ?  142 VAL   B HG13 1 
ATOM   6091 H  HG21 . VAL   B 1 142 ? 31.363 -28.386 1.025   1.00 18.61 ?  142 VAL   B HG21 1 
ATOM   6092 H  HG22 . VAL   B 1 142 ? 30.068 -28.511 0.114   1.00 18.61 ?  142 VAL   B HG22 1 
ATOM   6093 H  HG23 . VAL   B 1 142 ? 31.314 -29.463 -0.141  1.00 18.61 ?  142 VAL   B HG23 1 
ATOM   6094 N  N    . CYS   B 1 143 ? 32.731 -26.915 -3.818  1.00 13.84 ?  143 CYS   B N    1 
ATOM   6095 C  CA   . CYS   B 1 143 ? 33.228 -25.980 -4.822  1.00 13.82 ?  143 CYS   B CA   1 
ATOM   6096 C  C    . CYS   B 1 143 ? 32.229 -25.836 -5.965  1.00 13.69 ?  143 CYS   B C    1 
ATOM   6097 O  O    . CYS   B 1 143 ? 31.828 -24.725 -6.327  1.00 13.75 ?  143 CYS   B O    1 
ATOM   6098 C  CB   . CYS   B 1 143 ? 34.580 -26.474 -5.347  1.00 14.00 ?  143 CYS   B CB   1 
ATOM   6099 S  SG   . CYS   B 1 143 ? 35.338 -25.368 -6.565  1.00 14.22 ?  143 CYS   B SG   1 
ATOM   6100 H  H    . CYS   B 1 143 ? 33.269 -27.562 -3.643  1.00 16.60 ?  143 CYS   B H    1 
ATOM   6101 H  HA   . CYS   B 1 143 ? 33.363 -25.106 -4.422  1.00 16.59 ?  143 CYS   B HA   1 
ATOM   6102 H  HB2  . CYS   B 1 143 ? 35.199 -26.566 -4.602  1.00 16.80 ?  143 CYS   B HB2  1 
ATOM   6103 H  HB3  . CYS   B 1 143 ? 34.457 -27.337 -5.769  1.00 16.80 ?  143 CYS   B HB3  1 
ATOM   6104 H  HG   . CYS   B 1 143 ? 36.410 -25.809 -6.884  1.00 17.06 ?  143 CYS   B HG   1 
ATOM   6105 N  N    . VAL   B 1 144 ? 31.824 -26.957 -6.552  1.00 14.40 ?  144 VAL   B N    1 
ATOM   6106 C  CA   . VAL   B 1 144 ? 30.923 -26.905 -7.698  1.00 15.35 ?  144 VAL   B CA   1 
ATOM   6107 C  C    . VAL   B 1 144 ? 29.584 -26.284 -7.323  1.00 15.53 ?  144 VAL   B C    1 
ATOM   6108 O  O    . VAL   B 1 144 ? 28.966 -25.580 -8.132  1.00 16.63 ?  144 VAL   B O    1 
ATOM   6109 C  CB   . VAL   B 1 144 ? 30.760 -28.320 -8.266  1.00 17.59 ?  144 VAL   B CB   1 
ATOM   6110 C  CG1  . VAL   B 1 144 ? 29.495 -28.443 -9.103  1.00 19.60 ?  144 VAL   B CG1  1 
ATOM   6111 C  CG2  . VAL   B 1 144 ? 32.008 -28.732 -9.051  1.00 17.65 ?  144 VAL   B CG2  1 
ATOM   6112 H  H    . VAL   B 1 144 ? 32.057 -27.753 -6.317  1.00 17.28 ?  144 VAL   B H    1 
ATOM   6113 H  HA   . VAL   B 1 144 ? 31.314 -26.356 -8.388  1.00 18.42 ?  144 VAL   B HA   1 
ATOM   6114 H  HB   . VAL   B 1 144 ? 30.676 -28.943 -7.524  1.00 21.11 ?  144 VAL   B HB   1 
ATOM   6115 H  HG11 . VAL   B 1 144 ? 29.567 -29.231 -9.668  1.00 23.52 ?  144 VAL   B HG11 1 
ATOM   6116 H  HG12 . VAL   B 1 144 ? 28.733 -28.538 -8.511  1.00 23.52 ?  144 VAL   B HG12 1 
ATOM   6117 H  HG13 . VAL   B 1 144 ? 29.400 -27.653 -9.653  1.00 23.52 ?  144 VAL   B HG13 1 
ATOM   6118 H  HG21 . VAL   B 1 144 ? 31.884 -29.632 -9.394  1.00 21.18 ?  144 VAL   B HG21 1 
ATOM   6119 H  HG22 . VAL   B 1 144 ? 32.133 -28.114 -9.788  1.00 21.18 ?  144 VAL   B HG22 1 
ATOM   6120 H  HG23 . VAL   B 1 144 ? 32.775 -28.706 -8.461  1.00 21.18 ?  144 VAL   B HG23 1 
ATOM   6121 N  N    . ASP   B 1 145 ? 29.114 -26.532 -6.106  1.00 15.44 ?  145 ASP   B N    1 
ATOM   6122 C  CA   . ASP   B 1 145 ? 27.802 -26.067 -5.681  1.00 16.08 ?  145 ASP   B CA   1 
ATOM   6123 C  C    . ASP   B 1 145 ? 27.826 -24.647 -5.133  1.00 15.67 ?  145 ASP   B C    1 
ATOM   6124 O  O    . ASP   B 1 145 ? 26.765 -24.115 -4.786  1.00 17.10 ?  145 ASP   B O    1 
ATOM   6125 C  CB   . ASP   B 1 145 ? 27.216 -26.989 -4.605  1.00 17.62 ?  145 ASP   B CB   1 
ATOM   6126 C  CG   . ASP   B 1 145 ? 26.858 -28.367 -5.121  1.00 19.28 ?  145 ASP   B CG   1 
ATOM   6127 O  OD1  . ASP   B 1 145 ? 26.766 -28.558 -6.348  1.00 19.71 ?  145 ASP   B OD1  1 
ATOM   6128 O  OD2  . ASP   B 1 145 ? 26.673 -29.258 -4.270  1.00 21.46 -1 145 ASP   B OD2  1 
ATOM   6129 H  H    . ASP   B 1 145 ? 29.543 -26.969 -5.504  1.00 18.53 ?  145 ASP   B H    1 
ATOM   6130 H  HA   . ASP   B 1 145 ? 27.209 -26.069 -6.446  1.00 19.29 ?  145 ASP   B HA   1 
ATOM   6131 H  HB2  . ASP   B 1 145 ? 27.861 -27.108 -3.904  1.00 21.14 ?  145 ASP   B HB2  1 
ATOM   6132 H  HB3  . ASP   B 1 145 ? 26.405 -26.582 -4.257  1.00 21.14 ?  145 ASP   B HB3  1 
ATOM   6133 N  N    . THR   B 1 146 ? 29.001 -24.024 -5.031  1.00 13.82 ?  146 THR   B N    1 
ATOM   6134 C  CA   . THR   B 1 146 ? 29.130 -22.704 -4.420  1.00 13.56 ?  146 THR   B CA   1 
ATOM   6135 C  C    . THR   B 1 146 ? 29.765 -21.671 -5.332  1.00 13.32 ?  146 THR   B C    1 
ATOM   6136 O  O    . THR   B 1 146 ? 29.313 -20.511 -5.373  1.00 13.57 ?  146 THR   B O    1 
ATOM   6137 C  CB   . THR   B 1 146 ? 29.960 -22.809 -3.135  1.00 14.00 ?  146 THR   B CB   1 
ATOM   6138 O  OG1  . THR   B 1 146 ? 29.385 -23.799 -2.277  1.00 14.09 ?  146 THR   B OG1  1 
ATOM   6139 C  CG2  . THR   B 1 146 ? 30.028 -21.473 -2.412  1.00 14.05 ?  146 THR   B CG2  1 
ATOM   6140 H  H    . THR   B 1 146 ? 29.751 -24.351 -5.308  1.00 16.59 ?  146 THR   B H    1 
ATOM   6141 H  HA   . THR   B 1 146 ? 28.253 -22.380 -4.184  1.00 16.28 ?  146 THR   B HA   1 
ATOM   6142 H  HB   . THR   B 1 146 ? 30.865 -23.071 -3.356  1.00 16.80 ?  146 THR   B HB   1 
ATOM   6143 H  HG1  . THR   B 1 146 ? 29.413 -24.556 -2.658  1.00 16.91 ?  146 THR   B HG1  1 
ATOM   6144 H  HG21 . THR   B 1 146 ? 30.374 -21.599 -1.515  1.00 16.85 ?  146 THR   B HG21 1 
ATOM   6145 H  HG22 . THR   B 1 146 ? 30.613 -20.864 -2.890  1.00 16.85 ?  146 THR   B HG22 1 
ATOM   6146 H  HG23 . THR   B 1 146 ? 29.142 -21.081 -2.355  1.00 16.85 ?  146 THR   B HG23 1 
ATOM   6147 N  N    . VAL   B 1 147 ? 30.833 -22.045 -6.030  1.00 13.31 ?  147 VAL   B N    1 
ATOM   6148 C  CA   . VAL   B 1 147 ? 31.560 -21.104 -6.866  1.00 13.05 ?  147 VAL   B CA   1 
ATOM   6149 C  C    . VAL   B 1 147 ? 30.834 -20.979 -8.191  1.00 13.13 ?  147 VAL   B C    1 
ATOM   6150 O  O    . VAL   B 1 147 ? 30.468 -21.985 -8.817  1.00 14.08 ?  147 VAL   B O    1 
ATOM   6151 C  CB   . VAL   B 1 147 ? 33.011 -21.567 -7.066  1.00 13.09 ?  147 VAL   B CB   1 
ATOM   6152 C  CG1  . VAL   B 1 147 ? 33.772 -20.546 -7.887  1.00 13.08 ?  147 VAL   B CG1  1 
ATOM   6153 C  CG2  . VAL   B 1 147 ? 33.686 -21.779 -5.724  1.00 13.21 ?  147 VAL   B CG2  1 
ATOM   6154 H  H    . VAL   B 1 147 ? 31.155 -22.844 -6.047  1.00 15.98 ?  147 VAL   B H    1 
ATOM   6155 H  HA   . VAL   B 1 147 ? 31.575 -20.233 -6.439  1.00 15.66 ?  147 VAL   B HA   1 
ATOM   6156 H  HB   . VAL   B 1 147 ? 33.015 -22.412 -7.549  1.00 15.71 ?  147 VAL   B HB   1 
ATOM   6157 H  HG11 . VAL   B 1 147 ? 34.717 -20.767 -7.865  1.00 15.69 ?  147 VAL   B HG11 1 
ATOM   6158 H  HG12 . VAL   B 1 147 ? 33.450 -20.562 -8.799  1.00 15.69 ?  147 VAL   B HG12 1 
ATOM   6159 H  HG13 . VAL   B 1 147 ? 33.632 -19.666 -7.499  1.00 15.69 ?  147 VAL   B HG13 1 
ATOM   6160 H  HG21 . VAL   B 1 147 ? 34.625 -21.979 -5.870  1.00 15.85 ?  147 VAL   B HG21 1 
ATOM   6161 H  HG22 . VAL   B 1 147 ? 33.600 -20.968 -5.197  1.00 15.85 ?  147 VAL   B HG22 1 
ATOM   6162 H  HG23 . VAL   B 1 147 ? 33.259 -22.518 -5.264  1.00 15.85 ?  147 VAL   B HG23 1 
ATOM   6163 N  N    . ARG   B 1 148 ? 30.628 -19.733 -8.616  1.00 13.05 ?  148 ARG   B N    1 
ATOM   6164 C  CA   . ARG   B 1 148 ? 29.999 -19.418 -9.887  1.00 13.38 ?  148 ARG   B CA   1 
ATOM   6165 C  C    . ARG   B 1 148 ? 30.957 -18.752 -10.862 1.00 13.51 ?  148 ARG   B C    1 
ATOM   6166 O  O    . ARG   B 1 148 ? 30.677 -18.737 -12.062 1.00 15.19 ?  148 ARG   B O    1 
ATOM   6167 C  CB   . ARG   B 1 148 ? 28.768 -18.523 -9.663  1.00 13.69 ?  148 ARG   B CB   1 
ATOM   6168 C  CG   . ARG   B 1 148 ? 27.678 -19.224 -8.857  1.00 14.53 ?  148 ARG   B CG   1 
ATOM   6169 C  CD   . ARG   B 1 148 ? 26.485 -18.318 -8.569  1.00 15.13 ?  148 ARG   B CD   1 
ATOM   6170 N  NE   . ARG   B 1 148 ? 26.878 -17.123 -7.834  1.00 15.22 ?  148 ARG   B NE   1 
ATOM   6171 C  CZ   . ARG   B 1 148 ? 27.172 -17.093 -6.542  1.00 14.34 ?  148 ARG   B CZ   1 
ATOM   6172 N  NH1  . ARG   B 1 148 ? 27.089 -18.174 -5.783  1.00 14.52 ?  148 ARG   B NH1  1 
ATOM   6173 N  NH2  . ARG   B 1 148 ? 27.574 -15.948 -5.997  1.00 14.39 ?  148 ARG   B NH2  1 
ATOM   6174 H  H    . ARG   B 1 148 ? 30.860 -19.029 -8.168  1.00 15.67 ?  148 ARG   B H    1 
ATOM   6175 H  HA   . ARG   B 1 148 ? 29.693 -20.239 -10.291 1.00 16.06 ?  148 ARG   B HA   1 
ATOM   6176 H  HB2  . ARG   B 1 148 ? 29.034 -17.727 -9.176  1.00 16.43 ?  148 ARG   B HB2  1 
ATOM   6177 H  HB3  . ARG   B 1 148 ? 28.393 -18.277 -10.523 1.00 16.43 ?  148 ARG   B HB3  1 
ATOM   6178 H  HG2  . ARG   B 1 148 ? 27.356 -19.993 -9.359  1.00 17.44 ?  148 ARG   B HG2  1 
ATOM   6179 H  HG3  . ARG   B 1 148 ? 28.046 -19.517 -8.008  1.00 17.44 ?  148 ARG   B HG3  1 
ATOM   6180 H  HD2  . ARG   B 1 148 ? 26.088 -18.040 -9.408  1.00 18.16 ?  148 ARG   B HD2  1 
ATOM   6181 H  HD3  . ARG   B 1 148 ? 25.836 -18.804 -8.036  1.00 18.16 ?  148 ARG   B HD3  1 
ATOM   6182 H  HE   . ARG   B 1 148 ? 26.939 -16.389 -8.271  1.00 18.26 ?  148 ARG   B HE   1 
ATOM   6183 H  HH11 . ARG   B 1 148 ? 26.828 -18.925 -6.120  1.00 17.42 ?  148 ARG   B HH11 1 
ATOM   6184 H  HH12 . ARG   B 1 148 ? 27.279 -18.133 -4.943  1.00 17.42 ?  148 ARG   B HH12 1 
ATOM   6185 H  HH21 . ARG   B 1 148 ? 27.638 -15.243 -6.479  1.00 17.27 ?  148 ARG   B HH21 1 
ATOM   6186 H  HH22 . ARG   B 1 148 ? 27.768 -15.915 -5.158  1.00 17.27 ?  148 ARG   B HH22 1 
ATOM   6187 N  N    . THR   B 1 149 ? 32.062 -18.192 -10.375 1.00 13.19 ?  149 THR   B N    1 
ATOM   6188 C  CA   . THR   B 1 149 ? 33.107 -17.638 -11.223 1.00 13.11 ?  149 THR   B CA   1 
ATOM   6189 C  C    . THR   B 1 149 ? 33.999 -18.777 -11.723 1.00 12.88 ?  149 THR   B C    1 
ATOM   6190 O  O    . THR   B 1 149 ? 33.809 -19.946 -11.377 1.00 13.25 ?  149 THR   B O    1 
ATOM   6191 C  CB   . THR   B 1 149 ? 33.880 -16.584 -10.441 1.00 13.12 ?  149 THR   B CB   1 
ATOM   6192 O  OG1  . THR   B 1 149 ? 34.328 -17.179 -9.221  1.00 13.37 ?  149 THR   B OG1  1 
ATOM   6193 C  CG2  . THR   B 1 149 ? 32.987 -15.374 -10.149 1.00 13.96 ?  149 THR   B CG2  1 
ATOM   6194 H  H    . THR   B 1 149 ? 32.223 -18.112 -9.536  1.00 15.83 ?  149 THR   B H    1 
ATOM   6195 H  HA   . THR   B 1 149 ? 32.700 -17.206 -11.993 1.00 15.74 ?  149 THR   B HA   1 
ATOM   6196 H  HB   . THR   B 1 149 ? 34.644 -16.295 -10.961 1.00 15.74 ?  149 THR   B HB   1 
ATOM   6197 H  HG1  . THR   B 1 149 ? 34.756 -16.610 -8.766  1.00 16.05 ?  149 THR   B HG1  1 
ATOM   6198 H  HG21 . THR   B 1 149 ? 33.492 -14.700 -9.668  1.00 16.75 ?  149 THR   B HG21 1 
ATOM   6199 H  HG22 . THR   B 1 149 ? 32.667 -14.991 -10.983 1.00 16.75 ?  149 THR   B HG22 1 
ATOM   6200 H  HG23 . THR   B 1 149 ? 32.225 -15.642 -9.614  1.00 16.75 ?  149 THR   B HG23 1 
ATOM   6201 N  N    . ASN   B 1 150 ? 34.967 -18.457 -12.572 1.00 13.06 ?  150 ASN   B N    1 
ATOM   6202 C  CA   . ASN   B 1 150 ? 35.731 -19.486 -13.269 1.00 13.42 ?  150 ASN   B CA   1 
ATOM   6203 C  C    . ASN   B 1 150 ? 36.896 -19.932 -12.394 1.00 13.09 ?  150 ASN   B C    1 
ATOM   6204 O  O    . ASN   B 1 150 ? 37.822 -19.157 -12.135 1.00 13.57 ?  150 ASN   B O    1 
ATOM   6205 C  CB   . ASN   B 1 150 ? 36.203 -18.956 -14.616 1.00 15.20 ?  150 ASN   B CB   1 
ATOM   6206 C  CG   . ASN   B 1 150 ? 35.057 -18.721 -15.556 1.00 17.84 ?  150 ASN   B CG   1 
ATOM   6207 O  OD1  . ASN   B 1 150 ? 34.164 -19.553 -15.659 1.00 18.92 ?  150 ASN   B OD1  1 
ATOM   6208 N  ND2  . ASN   B 1 150 ? 35.048 -17.573 -16.218 1.00 19.24 ?  150 ASN   B ND2  1 
ATOM   6209 H  H    . ASN   B 1 150 ? 35.205 -17.651 -12.762 1.00 15.67 ?  150 ASN   B H    1 
ATOM   6210 H  HA   . ASN   B 1 150 ? 35.153 -20.253 -13.434 1.00 16.11 ?  150 ASN   B HA   1 
ATOM   6211 H  HB2  . ASN   B 1 150 ? 36.660 -18.111 -14.482 1.00 18.25 ?  150 ASN   B HB2  1 
ATOM   6212 H  HB3  . ASN   B 1 150 ? 36.797 -19.601 -15.024 1.00 18.25 ?  150 ASN   B HB3  1 
ATOM   6213 H  HD21 . ASN   B 1 150 ? 34.409 -17.394 -16.767 1.00 23.08 ?  150 ASN   B HD21 1 
ATOM   6214 H  HD22 . ASN   B 1 150 ? 35.690 -17.009 -16.110 1.00 23.08 ?  150 ASN   B HD22 1 
ATOM   6215 N  N    . VAL   B 1 151 ? 36.850 -21.177 -11.933 1.00 12.75 ?  151 VAL   B N    1 
ATOM   6216 C  CA   . VAL   B 1 151 ? 37.868 -21.704 -11.039 1.00 12.69 ?  151 VAL   B CA   1 
ATOM   6217 C  C    . VAL   B 1 151 ? 38.577 -22.874 -11.711 1.00 12.74 ?  151 VAL   B C    1 
ATOM   6218 O  O    . VAL   B 1 151 ? 37.940 -23.808 -12.219 1.00 13.73 ?  151 VAL   B O    1 
ATOM   6219 C  CB   . VAL   B 1 151 ? 37.304 -22.037 -9.642  1.00 14.15 ?  151 VAL   B CB   1 
ATOM   6220 C  CG1  . VAL   B 1 151 ? 36.164 -23.047 -9.719  1.00 15.02 ?  151 VAL   B CG1  1 
ATOM   6221 C  CG2  . VAL   B 1 151 ? 38.416 -22.496 -8.707  1.00 14.42 ?  151 VAL   B CG2  1 
ATOM   6222 H  H    . VAL   B 1 151 ? 36.228 -21.744 -12.131 1.00 15.30 ?  151 VAL   B H    1 
ATOM   6223 H  HA   . VAL   B 1 151 ? 38.536 -21.010 -10.910 1.00 15.22 ?  151 VAL   B HA   1 
ATOM   6224 H  HB   . VAL   B 1 151 ? 36.936 -21.218 -9.267  1.00 16.98 ?  151 VAL   B HB   1 
ATOM   6225 H  HG11 . VAL   B 1 151 ? 35.837 -23.224 -8.821  1.00 18.02 ?  151 VAL   B HG11 1 
ATOM   6226 H  HG12 . VAL   B 1 151 ? 35.450 -22.684 -10.264 1.00 18.02 ?  151 VAL   B HG12 1 
ATOM   6227 H  HG13 . VAL   B 1 151 ? 36.496 -23.871 -10.114 1.00 18.02 ?  151 VAL   B HG13 1 
ATOM   6228 H  HG21 . VAL   B 1 151 ? 38.054 -22.583 -7.811  1.00 17.31 ?  151 VAL   B HG21 1 
ATOM   6229 H  HG22 . VAL   B 1 151 ? 38.758 -23.345 -9.013  1.00 17.31 ?  151 VAL   B HG22 1 
ATOM   6230 H  HG23 . VAL   B 1 151 ? 39.125 -21.829 -8.709  1.00 17.31 ?  151 VAL   B HG23 1 
ATOM   6231 N  N    . TYR   B 1 152 ? 39.905 -22.786 -11.731 1.00 12.32 ?  152 TYR   B N    1 
ATOM   6232 C  CA   . TYR   B 1 152 ? 40.810 -23.768 -12.308 1.00 12.39 ?  152 TYR   B CA   1 
ATOM   6233 C  C    . TYR   B 1 152 ? 41.529 -24.435 -11.142 1.00 11.92 ?  152 TYR   B C    1 
ATOM   6234 O  O    . TYR   B 1 152 ? 42.368 -23.807 -10.489 1.00 12.25 ?  152 TYR   B O    1 
ATOM   6235 C  CB   . TYR   B 1 152 ? 41.782 -23.057 -13.253 1.00 13.19 ?  152 TYR   B CB   1 
ATOM   6236 C  CG   . TYR   B 1 152 ? 41.099 -22.593 -14.520 1.00 13.77 ?  152 TYR   B CG   1 
ATOM   6237 C  CD1  . TYR   B 1 152 ? 40.424 -21.374 -14.582 1.00 14.34 ?  152 TYR   B CD1  1 
ATOM   6238 C  CD2  . TYR   B 1 152 ? 41.105 -23.396 -15.647 1.00 14.88 ?  152 TYR   B CD2  1 
ATOM   6239 C  CE1  . TYR   B 1 152 ? 39.781 -20.978 -15.741 1.00 15.42 ?  152 TYR   B CE1  1 
ATOM   6240 C  CE2  . TYR   B 1 152 ? 40.469 -23.012 -16.805 1.00 15.97 ?  152 TYR   B CE2  1 
ATOM   6241 C  CZ   . TYR   B 1 152 ? 39.810 -21.802 -16.854 1.00 15.89 ?  152 TYR   B CZ   1 
ATOM   6242 O  OH   . TYR   B 1 152 ? 39.177 -21.435 -18.016 1.00 18.28 ?  152 TYR   B OH   1 
ATOM   6243 H  H    . TYR   B 1 152 ? 40.333 -22.124 -11.379 1.00 14.78 ?  152 TYR   B H    1 
ATOM   6244 H  HA   . TYR   B 1 152 ? 40.307 -24.439 -12.801 1.00 14.86 ?  152 TYR   B HA   1 
ATOM   6245 H  HB2  . TYR   B 1 152 ? 42.145 -22.280 -12.799 1.00 15.82 ?  152 TYR   B HB2  1 
ATOM   6246 H  HB3  . TYR   B 1 152 ? 42.494 -23.666 -13.495 1.00 15.82 ?  152 TYR   B HB3  1 
ATOM   6247 H  HD1  . TYR   B 1 152 ? 40.396 -20.825 -13.829 1.00 17.20 ?  152 TYR   B HD1  1 
ATOM   6248 H  HD2  . TYR   B 1 152 ? 41.548 -24.215 -15.618 1.00 17.85 ?  152 TYR   B HD2  1 
ATOM   6249 H  HE1  . TYR   B 1 152 ? 39.334 -20.165 -15.771 1.00 18.50 ?  152 TYR   B HE1  1 
ATOM   6250 H  HE2  . TYR   B 1 152 ? 40.492 -23.561 -17.553 1.00 19.16 ?  152 TYR   B HE2  1 
ATOM   6251 H  HH   . TYR   B 1 152 ? 38.815 -20.681 -17.915 1.00 21.94 ?  152 TYR   B HH   1 
ATOM   6252 N  N    . LEU   B 1 153 ? 41.168 -25.692 -10.867 1.00 12.09 ?  153 LEU   B N    1 
ATOM   6253 C  CA   . LEU   B 1 153 ? 41.679 -26.438 -9.726  1.00 11.55 ?  153 LEU   B CA   1 
ATOM   6254 C  C    . LEU   B 1 153 ? 42.912 -27.237 -10.123 1.00 12.09 ?  153 LEU   B C    1 
ATOM   6255 O  O    . LEU   B 1 153 ? 42.896 -27.971 -11.118 1.00 13.22 ?  153 LEU   B O    1 
ATOM   6256 C  CB   . LEU   B 1 153 ? 40.601 -27.394 -9.207  1.00 11.97 ?  153 LEU   B CB   1 
ATOM   6257 C  CG   . LEU   B 1 153 ? 39.335 -26.737 -8.651  1.00 13.17 ?  153 LEU   B CG   1 
ATOM   6258 C  CD1  . LEU   B 1 153 ? 38.232 -27.777 -8.503  1.00 13.89 ?  153 LEU   B CD1  1 
ATOM   6259 C  CD2  . LEU   B 1 153 ? 39.624 -26.073 -7.311  1.00 13.74 ?  153 LEU   B CD2  1 
ATOM   6260 H  H    . LEU   B 1 153 ? 40.596 -26.143 -11.336 1.00 14.50 ?  153 LEU   B H    1 
ATOM   6261 H  HA   . LEU   B 1 153 ? 41.907 -25.817 -9.015  1.00 13.86 ?  153 LEU   B HA   1 
ATOM   6262 H  HB2  . LEU   B 1 153 ? 40.329 -27.976 -9.930  1.00 14.36 ?  153 LEU   B HB2  1 
ATOM   6263 H  HB3  . LEU   B 1 153 ? 40.983 -27.926 -8.488  1.00 14.36 ?  153 LEU   B HB3  1 
ATOM   6264 H  HG   . LEU   B 1 153 ? 39.024 -26.053 -9.268  1.00 15.81 ?  153 LEU   B HG   1 
ATOM   6265 H  HD11 . LEU   B 1 153 ? 37.419 -27.338 -8.197  1.00 16.67 ?  153 LEU   B HD11 1 
ATOM   6266 H  HD12 . LEU   B 1 153 ? 38.074 -28.194 -9.363  1.00 16.67 ?  153 LEU   B HD12 1 
ATOM   6267 H  HD13 . LEU   B 1 153 ? 38.510 -28.441 -7.855  1.00 16.67 ?  153 LEU   B HD13 1 
ATOM   6268 H  HD21 . LEU   B 1 153 ? 38.805 -25.692 -6.956  1.00 16.49 ?  153 LEU   B HD21 1 
ATOM   6269 H  HD22 . LEU   B 1 153 ? 39.974 -26.737 -6.696  1.00 16.49 ?  153 LEU   B HD22 1 
ATOM   6270 H  HD23 . LEU   B 1 153 ? 40.283 -25.369 -7.443  1.00 16.49 ?  153 LEU   B HD23 1 
ATOM   6271 N  N    . ALA   B 1 154 ? 43.965 -27.122 -9.323  1.00 12.33 ?  154 ALA   B N    1 
ATOM   6272 C  CA   . ALA   B 1 154 ? 45.194 -27.886 -9.504  1.00 13.71 ?  154 ALA   B CA   1 
ATOM   6273 C  C    . ALA   B 1 154 ? 45.254 -28.960 -8.427  1.00 14.08 ?  154 ALA   B C    1 
ATOM   6274 O  O    . ALA   B 1 154 ? 45.171 -28.656 -7.230  1.00 15.21 ?  154 ALA   B O    1 
ATOM   6275 C  CB   . ALA   B 1 154 ? 46.411 -26.968 -9.428  1.00 14.35 ?  154 ALA   B CB   1 
ATOM   6276 H  H    . ALA   B 1 154 ? 43.989 -26.589 -8.644  1.00 14.79 ?  154 ALA   B H    1 
ATOM   6277 H  HA   . ALA   B 1 154 ? 45.186 -28.313 -10.371 1.00 16.46 ?  154 ALA   B HA   1 
ATOM   6278 H  HB1  . ALA   B 1 154 ? 47.215 -27.495 -9.550  1.00 17.22 ?  154 ALA   B HB1  1 
ATOM   6279 H  HB2  . ALA   B 1 154 ? 46.348 -26.295 -10.127 1.00 17.22 ?  154 ALA   B HB2  1 
ATOM   6280 H  HB3  . ALA   B 1 154 ? 46.431 -26.534 -8.558  1.00 17.22 ?  154 ALA   B HB3  1 
ATOM   6281 N  N    . VAL   B 1 155 ? 45.373 -30.211 -8.856  1.00 13.26 ?  155 VAL   B N    1 
ATOM   6282 C  CA   . VAL   B 1 155 ? 45.483 -31.355 -7.959  1.00 13.39 ?  155 VAL   B CA   1 
ATOM   6283 C  C    . VAL   B 1 155 ? 46.821 -32.027 -8.234  1.00 13.18 ?  155 VAL   B C    1 
ATOM   6284 O  O    . VAL   B 1 155 ? 47.055 -32.526 -9.342  1.00 15.02 ?  155 VAL   B O    1 
ATOM   6285 C  CB   . VAL   B 1 155 ? 44.322 -32.342 -8.152  1.00 14.99 ?  155 VAL   B CB   1 
ATOM   6286 C  CG1  . VAL   B 1 155 ? 44.505 -33.550 -7.247  1.00 14.79 ?  155 VAL   B CG1  1 
ATOM   6287 C  CG2  . VAL   B 1 155 ? 42.997 -31.646 -7.872  1.00 15.88 ?  155 VAL   B CG2  1 
ATOM   6288 H  H    . VAL   B 1 155 ? 45.399 -30.427 -9.688  1.00 15.91 ?  155 VAL   B H    1 
ATOM   6289 H  HA   . VAL   B 1 155 ? 45.475 -31.049 -7.038  1.00 16.06 ?  155 VAL   B HA   1 
ATOM   6290 H  HB   . VAL   B 1 155 ? 44.314 -32.647 -9.073  1.00 17.99 ?  155 VAL   B HB   1 
ATOM   6291 H  HG11 . VAL   B 1 155 ? 43.678 -34.052 -7.215  1.00 17.75 ?  155 VAL   B HG11 1 
ATOM   6292 H  HG12 . VAL   B 1 155 ? 45.216 -34.113 -7.603  1.00 17.75 ?  155 VAL   B HG12 1 
ATOM   6293 H  HG13 . VAL   B 1 155 ? 44.744 -33.248 -6.356  1.00 17.75 ?  155 VAL   B HG13 1 
ATOM   6294 H  HG21 . VAL   B 1 155 ? 42.281 -32.295 -7.952  1.00 19.06 ?  155 VAL   B HG21 1 
ATOM   6295 H  HG22 . VAL   B 1 155 ? 43.018 -31.287 -6.970  1.00 19.06 ?  155 VAL   B HG22 1 
ATOM   6296 H  HG23 . VAL   B 1 155 ? 42.873 -30.931 -8.512  1.00 19.06 ?  155 VAL   B HG23 1 
ATOM   6297 N  N    . PHE   B 1 156 ? 47.690 -32.059 -7.220  1.00 13.97 ?  156 PHE   B N    1 
ATOM   6298 C  CA   . PHE   B 1 156 ? 49.068 -32.513 -7.418  1.00 15.16 ?  156 PHE   B CA   1 
ATOM   6299 C  C    . PHE   B 1 156 ? 49.162 -34.013 -7.700  1.00 16.08 ?  156 PHE   B C    1 
ATOM   6300 O  O    . PHE   B 1 156 ? 49.892 -34.440 -8.605  1.00 17.91 ?  156 PHE   B O    1 
ATOM   6301 C  CB   . PHE   B 1 156 ? 49.894 -32.142 -6.187  1.00 15.27 ?  156 PHE   B CB   1 
ATOM   6302 C  CG   . PHE   B 1 156 ? 51.320 -32.602 -6.245  1.00 15.79 ?  156 PHE   B CG   1 
ATOM   6303 C  CD1  . PHE   B 1 156 ? 52.204 -32.056 -7.156  1.00 17.40 ?  156 PHE   B CD1  1 
ATOM   6304 C  CD2  . PHE   B 1 156 ? 51.781 -33.564 -5.370  1.00 16.47 ?  156 PHE   B CD2  1 
ATOM   6305 C  CE1  . PHE   B 1 156 ? 53.525 -32.467 -7.202  1.00 18.59 ?  156 PHE   B CE1  1 
ATOM   6306 C  CE2  . PHE   B 1 156 ? 53.101 -33.978 -5.412  1.00 17.51 ?  156 PHE   B CE2  1 
ATOM   6307 C  CZ   . PHE   B 1 156 ? 53.966 -33.432 -6.334  1.00 18.26 ?  156 PHE   B CZ   1 
ATOM   6308 H  H    . PHE   B 1 156 ? 47.504 -31.832 -6.411  1.00 16.76 ?  156 PHE   B H    1 
ATOM   6309 H  HA   . PHE   B 1 156 ? 49.441 -32.044 -8.179  1.00 18.19 ?  156 PHE   B HA   1 
ATOM   6310 H  HB2  . PHE   B 1 156 ? 49.899 -31.175 -6.099  1.00 18.32 ?  156 PHE   B HB2  1 
ATOM   6311 H  HB3  . PHE   B 1 156 ? 49.486 -32.541 -5.404  1.00 18.32 ?  156 PHE   B HB3  1 
ATOM   6312 H  HD1  . PHE   B 1 156 ? 51.911 -31.400 -7.748  1.00 20.88 ?  156 PHE   B HD1  1 
ATOM   6313 H  HD2  . PHE   B 1 156 ? 51.195 -33.939 -4.751  1.00 19.76 ?  156 PHE   B HD2  1 
ATOM   6314 H  HE1  . PHE   B 1 156 ? 54.111 -32.093 -7.824  1.00 22.30 ?  156 PHE   B HE1  1 
ATOM   6315 H  HE2  . PHE   B 1 156 ? 53.399 -34.638 -4.824  1.00 21.01 ?  156 PHE   B HE2  1 
ATOM   6316 H  HZ   . PHE   B 1 156 ? 54.854 -33.712 -6.364  1.00 21.92 ?  156 PHE   B HZ   1 
ATOM   6317 N  N    . ASP   B 1 157 ? 48.494 -34.831 -6.897  1.00 16.42 ?  157 ASP   B N    1 
ATOM   6318 C  CA   . ASP   B 1 157 ? 48.643 -36.279 -6.985  1.00 17.54 ?  157 ASP   B CA   1 
ATOM   6319 C  C    . ASP   B 1 157 ? 47.736 -36.833 -8.079  1.00 17.83 ?  157 ASP   B C    1 
ATOM   6320 O  O    . ASP   B 1 157 ? 46.509 -36.714 -7.987  1.00 17.30 ?  157 ASP   B O    1 
ATOM   6321 C  CB   . ASP   B 1 157 ? 48.273 -36.887 -5.637  1.00 19.35 ?  157 ASP   B CB   1 
ATOM   6322 C  CG   . ASP   B 1 157 ? 48.414 -38.396 -5.611  1.00 21.11 ?  157 ASP   B CG   1 
ATOM   6323 O  OD1  . ASP   B 1 157 ? 48.745 -39.008 -6.654  1.00 21.54 ?  157 ASP   B OD1  1 
ATOM   6324 O  OD2  . ASP   B 1 157 ? 48.215 -38.972 -4.525  1.00 22.94 -1 157 ASP   B OD2  1 
ATOM   6325 H  H    . ASP   B 1 157 ? 47.957 -34.571 -6.285  1.00 19.70 ?  157 ASP   B H    1 
ATOM   6326 H  HA   . ASP   B 1 157 ? 49.565 -36.510 -7.192  1.00 21.05 ?  157 ASP   B HA   1 
ATOM   6327 H  HB2  . ASP   B 1 157 ? 48.847 -36.507 -4.957  1.00 23.22 ?  157 ASP   B HB2  1 
ATOM   6328 H  HB3  . ASP   B 1 157 ? 47.345 -36.670 -5.444  1.00 23.22 ?  157 ASP   B HB3  1 
ATOM   6329 N  N    . LYS   B 1 158 ? 48.336 -37.458 -9.100  1.00 19.06 ?  158 LYS   B N    1 
ATOM   6330 C  CA   . LYS   B 1 158 ? 47.557 -38.061 -10.185 1.00 20.20 ?  158 LYS   B CA   1 
ATOM   6331 C  C    . LYS   B 1 158 ? 46.494 -39.028 -9.659  1.00 20.00 ?  158 LYS   B C    1 
ATOM   6332 O  O    . LYS   B 1 158 ? 45.390 -39.118 -10.212 1.00 20.03 ?  158 LYS   B O    1 
ATOM   6333 C  CB   . LYS   B 1 158 ? 48.501 -38.769 -11.167 1.00 21.93 ?  158 LYS   B CB   1 
ATOM   6334 C  CG   . LYS   B 1 158 ? 47.822 -39.673 -12.183 1.00 24.16 ?  158 LYS   B CG   1 
ATOM   6335 C  CD   . LYS   B 1 158 ? 46.956 -38.898 -13.153 1.00 26.41 ?  158 LYS   B CD   1 
ATOM   6336 C  CE   . LYS   B 1 158 ? 46.383 -39.822 -14.213 1.00 27.93 ?  158 LYS   B CE   1 
ATOM   6337 N  NZ   . LYS   B 1 158 ? 45.304 -39.166 -15.001 1.00 28.34 ?  158 LYS   B NZ   1 
ATOM   6338 H  H    . LYS   B 1 158 ? 49.192 -37.543 -9.192  1.00 22.88 ?  158 LYS   B H    1 
ATOM   6339 H  HA   . LYS   B 1 158 ? 47.106 -37.355 -10.677 1.00 24.24 ?  158 LYS   B HA   1 
ATOM   6340 H  HB2  . LYS   B 1 158 ? 48.996 -38.094 -11.667 1.00 26.32 ?  158 LYS   B HB2  1 
ATOM   6341 H  HB3  . LYS   B 1 158 ? 49.125 -39.312 -10.662 1.00 26.32 ?  158 LYS   B HB3  1 
ATOM   6342 H  HG2  . LYS   B 1 158 ? 48.506 -40.129 -12.698 1.00 29.00 ?  158 LYS   B HG2  1 
ATOM   6343 H  HG3  . LYS   B 1 158 ? 47.269 -40.328 -11.729 1.00 29.00 ?  158 LYS   B HG3  1 
ATOM   6344 H  HD2  . LYS   B 1 158 ? 46.220 -38.488 -12.674 1.00 31.70 ?  158 LYS   B HD2  1 
ATOM   6345 H  HD3  . LYS   B 1 158 ? 47.492 -38.222 -13.596 1.00 31.70 ?  158 LYS   B HD3  1 
ATOM   6346 H  HE2  . LYS   B 1 158 ? 47.087 -40.084 -14.825 1.00 33.52 ?  158 LYS   B HE2  1 
ATOM   6347 H  HE3  . LYS   B 1 158 ? 46.007 -40.608 -13.783 1.00 33.52 ?  158 LYS   B HE3  1 
ATOM   6348 H  HZ1  . LYS   B 1 158 ? 44.987 -39.730 -15.612 1.00 34.01 ?  158 LYS   B HZ1  1 
ATOM   6349 H  HZ2  . LYS   B 1 158 ? 44.640 -38.920 -14.462 1.00 34.01 ?  158 LYS   B HZ2  1 
ATOM   6350 H  HZ3  . LYS   B 1 158 ? 45.625 -38.445 -15.412 1.00 34.01 ?  158 LYS   B HZ3  1 
ATOM   6351 N  N    . ASN   B 1 159 ? 46.815 -39.780 -8.605  1.00 20.45 ?  159 ASN   B N    1 
ATOM   6352 C  CA   . ASN   B 1 159 ? 45.863 -40.762 -8.094  1.00 21.02 ?  159 ASN   B CA   1 
ATOM   6353 C  C    . ASN   B 1 159 ? 44.662 -40.091 -7.425  1.00 19.85 ?  159 ASN   B C    1 
ATOM   6354 O  O    . ASN   B 1 159 ? 43.531 -40.586 -7.529  1.00 19.90 ?  159 ASN   B O    1 
ATOM   6355 C  CB   . ASN   B 1 159 ? 46.572 -41.728 -7.152  1.00 23.17 ?  159 ASN   B CB   1 
ATOM   6356 C  CG   . ASN   B 1 159 ? 47.604 -42.575 -7.865  1.00 25.34 ?  159 ASN   B CG   1 
ATOM   6357 O  OD1  . ASN   B 1 159 ? 47.363 -43.075 -8.972  1.00 26.12 ?  159 ASN   B OD1  1 
ATOM   6358 N  ND2  . ASN   B 1 159 ? 48.762 -42.748 -7.235  1.00 26.04 ?  159 ASN   B ND2  1 
ATOM   6359 H  H    . ASN   B 1 159 ? 47.561 -39.739 -8.186  1.00 24.54 ?  159 ASN   B H    1 
ATOM   6360 H  HA   . ASN   B 1 159 ? 45.528 -41.277 -8.847  1.00 25.23 ?  159 ASN   B HA   1 
ATOM   6361 H  HB2  . ASN   B 1 159 ? 47.025 -41.224 -6.461  1.00 27.81 ?  159 ASN   B HB2  1 
ATOM   6362 H  HB3  . ASN   B 1 159 ? 45.921 -42.327 -6.767  1.00 27.81 ?  159 ASN   B HB3  1 
ATOM   6363 H  HD21 . ASN   B 1 159 ? 49.387 -43.220 -7.597  1.00 31.24 ?  159 ASN   B HD21 1 
ATOM   6364 H  HD22 . ASN   B 1 159 ? 48.887 -42.401 -6.458  1.00 31.24 ?  159 ASN   B HD22 1 
ATOM   6365 N  N    . LEU   B 1 160 ? 44.874 -38.960 -6.742  1.00 18.65 ?  160 LEU   B N    1 
ATOM   6366 C  CA   . LEU   B 1 160 ? 43.739 -38.223 -6.199  1.00 17.57 ?  160 LEU   B CA   1 
ATOM   6367 C  C    . LEU   B 1 160 ? 42.950 -37.561 -7.315  1.00 16.72 ?  160 LEU   B C    1 
ATOM   6368 O  O    . LEU   B 1 160 ? 41.713 -37.565 -7.299  1.00 16.42 ?  160 LEU   B O    1 
ATOM   6369 C  CB   . LEU   B 1 160 ? 44.205 -37.190 -5.172  1.00 17.34 ?  160 LEU   B CB   1 
ATOM   6370 C  CG   . LEU   B 1 160 ? 43.075 -36.296 -4.642  1.00 17.29 ?  160 LEU   B CG   1 
ATOM   6371 C  CD1  . LEU   B 1 160 ? 41.949 -37.119 -4.028  1.00 18.25 ?  160 LEU   B CD1  1 
ATOM   6372 C  CD2  . LEU   B 1 160 ? 43.614 -35.296 -3.635  1.00 17.15 ?  160 LEU   B CD2  1 
ATOM   6373 H  H    . LEU   B 1 160 ? 45.653 -38.606 -6.591  1.00 22.38 ?  160 LEU   B H    1 
ATOM   6374 H  HA   . LEU   B 1 160 ? 43.157 -38.852 -5.754  1.00 21.08 ?  160 LEU   B HA   1 
ATOM   6375 H  HB2  . LEU   B 1 160 ? 44.601 -37.663 -4.417  1.00 20.80 ?  160 LEU   B HB2  1 
ATOM   6376 H  HB3  . LEU   B 1 160 ? 44.877 -36.621 -5.583  1.00 20.80 ?  160 LEU   B HB3  1 
ATOM   6377 H  HG   . LEU   B 1 160 ? 42.705 -35.797 -5.381  1.00 20.75 ?  160 LEU   B HG   1 
ATOM   6378 H  HD11 . LEU   B 1 160 ? 41.315 -36.518 -3.610  1.00 21.90 ?  160 LEU   B HD11 1 
ATOM   6379 H  HD12 . LEU   B 1 160 ? 41.507 -37.630 -4.726  1.00 21.90 ?  160 LEU   B HD12 1 
ATOM   6380 H  HD13 . LEU   B 1 160 ? 42.319 -37.723 -3.363  1.00 21.90 ?  160 LEU   B HD13 1 
ATOM   6381 H  HD21 . LEU   B 1 160 ? 42.886 -34.729 -3.340  1.00 20.58 ?  160 LEU   B HD21 1 
ATOM   6382 H  HD22 . LEU   B 1 160 ? 43.988 -35.777 -2.880  1.00 20.58 ?  160 LEU   B HD22 1 
ATOM   6383 H  HD23 . LEU   B 1 160 ? 44.301 -34.762 -4.061  1.00 20.58 ?  160 LEU   B HD23 1 
ATOM   6384 N  N    . TYR   B 1 161 ? 43.653 -36.993 -8.299  1.00 16.93 ?  161 TYR   B N    1 
ATOM   6385 C  CA   . TYR   B 1 161 ? 42.985 -36.426 -9.463  1.00 16.68 ?  161 TYR   B CA   1 
ATOM   6386 C  C    . TYR   B 1 161 ? 42.044 -37.448 -10.090 1.00 16.80 ?  161 TYR   B C    1 
ATOM   6387 O  O    . TYR   B 1 161 ? 40.875 -37.153 -10.352 1.00 16.62 ?  161 TYR   B O    1 
ATOM   6388 C  CB   . TYR   B 1 161 ? 44.025 -35.937 -10.479 1.00 17.53 ?  161 TYR   B CB   1 
ATOM   6389 C  CG   . TYR   B 1 161 ? 43.452 -35.478 -11.800 1.00 18.31 ?  161 TYR   B CG   1 
ATOM   6390 C  CD1  . TYR   B 1 161 ? 43.060 -34.158 -11.981 1.00 18.20 ?  161 TYR   B CD1  1 
ATOM   6391 C  CD2  . TYR   B 1 161 ? 43.294 -36.360 -12.866 1.00 18.89 ?  161 TYR   B CD2  1 
ATOM   6392 C  CE1  . TYR   B 1 161 ? 42.538 -33.726 -13.173 1.00 19.14 ?  161 TYR   B CE1  1 
ATOM   6393 C  CE2  . TYR   B 1 161 ? 42.763 -35.936 -14.066 1.00 20.00 ?  161 TYR   B CE2  1 
ATOM   6394 C  CZ   . TYR   B 1 161 ? 42.389 -34.615 -14.214 1.00 20.00 ?  161 TYR   B CZ   1 
ATOM   6395 O  OH   . TYR   B 1 161 ? 41.857 -34.171 -15.402 1.00 21.77 ?  161 TYR   B OH   1 
ATOM   6396 H  H    . TYR   B 1 161 ? 44.509 -36.933 -8.322  1.00 20.32 ?  161 TYR   B H    1 
ATOM   6397 H  HA   . TYR   B 1 161 ? 42.453 -35.663 -9.187  1.00 20.01 ?  161 TYR   B HA   1 
ATOM   6398 H  HB2  . TYR   B 1 161 ? 44.501 -35.183 -10.095 1.00 21.04 ?  161 TYR   B HB2  1 
ATOM   6399 H  HB3  . TYR   B 1 161 ? 44.644 -36.655 -10.666 1.00 21.04 ?  161 TYR   B HB3  1 
ATOM   6400 H  HD1  . TYR   B 1 161 ? 43.158 -33.545 -11.287 1.00 21.83 ?  161 TYR   B HD1  1 
ATOM   6401 H  HD2  . TYR   B 1 161 ? 43.544 -37.250 -12.771 1.00 22.66 ?  161 TYR   B HD2  1 
ATOM   6402 H  HE1  . TYR   B 1 161 ? 42.282 -32.834 -13.276 1.00 22.97 ?  161 TYR   B HE1  1 
ATOM   6403 H  HE2  . TYR   B 1 161 ? 42.662 -36.535 -14.774 1.00 24.00 ?  161 TYR   B HE2  1 
ATOM   6404 H  HH   . TYR   B 1 161 ? 41.816 -34.806 -15.954 1.00 26.13 ?  161 TYR   B HH   1 
ATOM   6405 N  N    . ASP   B 1 162 ? 42.535 -38.670 -10.311 1.00 17.21 ?  162 ASP   B N    1 
ATOM   6406 C  CA   . ASP   B 1 162 ? 41.708 -39.702 -10.931 1.00 17.97 ?  162 ASP   B CA   1 
ATOM   6407 C  C    . ASP   B 1 162 ? 40.502 -40.044 -10.065 1.00 17.30 ?  162 ASP   B C    1 
ATOM   6408 O  O    . ASP   B 1 162 ? 39.399 -40.258 -10.581 1.00 17.65 ?  162 ASP   B O    1 
ATOM   6409 C  CB   . ASP   B 1 162 ? 42.540 -40.963 -11.182 1.00 19.27 ?  162 ASP   B CB   1 
ATOM   6410 C  CG   . ASP   B 1 162 ? 43.548 -40.800 -12.303 1.00 21.02 ?  162 ASP   B CG   1 
ATOM   6411 O  OD1  . ASP   B 1 162 ? 43.436 -39.850 -13.101 1.00 21.55 ?  162 ASP   B OD1  1 
ATOM   6412 O  OD2  . ASP   B 1 162 ? 44.450 -41.658 -12.399 1.00 22.70 -1 162 ASP   B OD2  1 
ATOM   6413 H  H    . ASP   B 1 162 ? 43.331 -38.917 -10.117 1.00 20.65 ?  162 ASP   B H    1 
ATOM   6414 H  HA   . ASP   B 1 162 ? 41.383 -39.381 -11.785 1.00 21.56 ?  162 ASP   B HA   1 
ATOM   6415 H  HB2  . ASP   B 1 162 ? 43.035 -41.184 -10.380 1.00 23.12 ?  162 ASP   B HB2  1 
ATOM   6416 H  HB3  . ASP   B 1 162 ? 41.948 -41.691 -11.423 1.00 23.12 ?  162 ASP   B HB3  1 
ATOM   6417 N  N    A LYS   B 1 163 ? 40.694 -40.117 -8.747  0.56 16.65 ?  163 LYS   B N    1 
ATOM   6418 N  N    B LYS   B 1 163 ? 40.692 -40.106 -8.746  0.44 17.07 ?  163 LYS   B N    1 
ATOM   6419 C  CA   A LYS   B 1 163 ? 39.565 -40.393 -7.865  0.56 17.09 ?  163 LYS   B CA   1 
ATOM   6420 C  CA   B LYS   B 1 163 ? 39.570 -40.391 -7.858  0.44 17.58 ?  163 LYS   B CA   1 
ATOM   6421 C  C    A LYS   B 1 163 ? 38.525 -39.282 -7.936  0.56 15.85 ?  163 LYS   B C    1 
ATOM   6422 C  C    B LYS   B 1 163 ? 38.527 -39.281 -7.910  0.44 16.13 ?  163 LYS   B C    1 
ATOM   6423 O  O    A LYS   B 1 163 ? 37.316 -39.550 -7.954  0.56 16.38 ?  163 LYS   B O    1 
ATOM   6424 O  O    B LYS   B 1 163 ? 37.318 -39.549 -7.888  0.44 16.52 ?  163 LYS   B O    1 
ATOM   6425 C  CB   A LYS   B 1 163 ? 40.044 -40.577 -6.426  0.56 19.59 ?  163 LYS   B CB   1 
ATOM   6426 C  CB   B LYS   B 1 163 ? 40.069 -40.584 -6.427  0.44 20.09 ?  163 LYS   B CB   1 
ATOM   6427 C  CG   A LYS   B 1 163 ? 38.967 -41.150 -5.521  0.56 23.51 ?  163 LYS   B CG   1 
ATOM   6428 C  CG   B LYS   B 1 163 ? 38.995 -41.086 -5.484  0.44 23.43 ?  163 LYS   B CG   1 
ATOM   6429 C  CD   A LYS   B 1 163 ? 39.362 -41.132 -4.057  0.56 27.07 ?  163 LYS   B CD   1 
ATOM   6430 C  CD   B LYS   B 1 163 ? 39.520 -41.306 -4.078  0.44 26.64 ?  163 LYS   B CD   1 
ATOM   6431 C  CE   A LYS   B 1 163 ? 38.289 -41.800 -3.208  0.56 29.48 ?  163 LYS   B CE   1 
ATOM   6432 C  CE   B LYS   B 1 163 ? 38.471 -42.004 -3.226  0.44 28.94 ?  163 LYS   B CE   1 
ATOM   6433 N  NZ   A LYS   B 1 163 ? 38.430 -41.494 -1.759  0.56 30.91 ?  163 LYS   B NZ   1 
ATOM   6434 N  NZ   B LYS   B 1 163 ? 38.632 -41.726 -1.773  0.44 30.11 ?  163 LYS   B NZ   1 
ATOM   6435 H  H    A LYS   B 1 163 ? 41.452 -40.011 -8.350  0.56 19.98 ?  163 LYS   B H    1 
ATOM   6436 H  H    B LYS   B 1 163 ? 41.449 -39.989 -8.350  0.44 20.49 ?  163 LYS   B H    1 
ATOM   6437 H  HA   A LYS   B 1 163 ? 39.145 -41.218 -8.150  0.56 20.51 ?  163 LYS   B HA   1 
ATOM   6438 H  HA   B LYS   B 1 163 ? 39.148 -41.215 -8.143  0.44 21.10 ?  163 LYS   B HA   1 
ATOM   6439 H  HB2  A LYS   B 1 163 ? 40.798 -41.190 -6.419  0.56 23.50 ?  163 LYS   B HB2  1 
ATOM   6440 H  HB2  B LYS   B 1 163 ? 40.790 -41.233 -6.430  0.44 24.11 ?  163 LYS   B HB2  1 
ATOM   6441 H  HB3  A LYS   B 1 163 ? 40.312 -39.718 -6.068  0.56 23.50 ?  163 LYS   B HB3  1 
ATOM   6442 H  HB3  B LYS   B 1 163 ? 40.390 -39.735 -6.089  0.44 24.11 ?  163 LYS   B HB3  1 
ATOM   6443 H  HG2  A LYS   B 1 163 ? 38.157 -40.626 -5.620  0.56 28.21 ?  163 LYS   B HG2  1 
ATOM   6444 H  HG2  B LYS   B 1 163 ? 38.280 -40.433 -5.439  0.44 28.11 ?  163 LYS   B HG2  1 
ATOM   6445 H  HG3  A LYS   B 1 163 ? 38.798 -42.072 -5.777  0.56 28.21 ?  163 LYS   B HG3  1 
ATOM   6446 H  HG3  B LYS   B 1 163 ? 38.653 -41.933 -5.815  0.44 28.11 ?  163 LYS   B HG3  1 
ATOM   6447 H  HD2  A LYS   B 1 163 ? 40.193 -41.621 -3.940  0.56 32.49 ?  163 LYS   B HD2  1 
ATOM   6448 H  HD2  B LYS   B 1 163 ? 40.312 -41.867 -4.113  0.44 31.97 ?  163 LYS   B HD2  1 
ATOM   6449 H  HD3  A LYS   B 1 163 ? 39.464 -40.215 -3.760  0.56 32.49 ?  163 LYS   B HD3  1 
ATOM   6450 H  HD3  B LYS   B 1 163 ? 39.728 -40.451 -3.672  0.44 31.97 ?  163 LYS   B HD3  1 
ATOM   6451 H  HE2  A LYS   B 1 163 ? 37.413 -41.504 -3.501  0.56 35.38 ?  163 LYS   B HE2  1 
ATOM   6452 H  HE2  B LYS   B 1 163 ? 37.591 -41.699 -3.498  0.44 34.73 ?  163 LYS   B HE2  1 
ATOM   6453 H  HE3  A LYS   B 1 163 ? 38.359 -42.760 -3.317  0.56 35.38 ?  163 LYS   B HE3  1 
ATOM   6454 H  HE3  B LYS   B 1 163 ? 38.544 -42.963 -3.359  0.44 34.73 ?  163 LYS   B HE3  1 
ATOM   6455 H  HZ1  A LYS   B 1 163 ? 37.784 -41.900 -1.300  0.56 37.09 ?  163 LYS   B HZ1  1 
ATOM   6456 H  HZ1  B LYS   B 1 163 ? 38.000 -42.150 -1.311  0.44 36.13 ?  163 LYS   B HZ1  1 
ATOM   6457 H  HZ2  A LYS   B 1 163 ? 39.219 -41.780 -1.465  0.56 37.09 ?  163 LYS   B HZ2  1 
ATOM   6458 H  HZ2  B LYS   B 1 163 ? 39.430 -42.003 -1.497  0.44 36.13 ?  163 LYS   B HZ2  1 
ATOM   6459 H  HZ3  A LYS   B 1 163 ? 38.371 -40.616 -1.627  0.56 37.09 ?  163 LYS   B HZ3  1 
ATOM   6460 H  HZ3  B LYS   B 1 163 ? 38.561 -40.851 -1.623  0.44 36.13 ?  163 LYS   B HZ3  1 
ATOM   6461 N  N    . LEU   B 1 164 ? 38.979 -38.026 -7.976  1.00 15.02 ?  164 LEU   B N    1 
ATOM   6462 C  CA   . LEU   B 1 164 ? 38.062 -36.890 -8.034  1.00 14.97 ?  164 LEU   B CA   1 
ATOM   6463 C  C    . LEU   B 1 164 ? 37.285 -36.874 -9.345  1.00 15.36 ?  164 LEU   B C    1 
ATOM   6464 O  O    . LEU   B 1 164 ? 36.062 -36.680 -9.351  1.00 16.27 ?  164 LEU   B O    1 
ATOM   6465 C  CB   . LEU   B 1 164 ? 38.858 -35.592 -7.871  1.00 14.33 ?  164 LEU   B CB   1 
ATOM   6466 C  CG   . LEU   B 1 164 ? 39.377 -35.310 -6.465  1.00 15.12 ?  164 LEU   B CG   1 
ATOM   6467 C  CD1  . LEU   B 1 164 ? 40.469 -34.253 -6.513  1.00 14.96 ?  164 LEU   B CD1  1 
ATOM   6468 C  CD2  . LEU   B 1 164 ? 38.249 -34.866 -5.551  1.00 16.88 ?  164 LEU   B CD2  1 
ATOM   6469 H  H    A LEU   B 1 164 ? 39.814 -37.807 -7.967  0.56 18.02 ?  164 LEU   B H    1 
ATOM   6470 H  H    B LEU   B 1 164 ? 39.814 -37.808 -7.988  0.44 18.02 ?  164 LEU   B H    1 
ATOM   6471 H  HA   . LEU   B 1 164 ? 37.429 -36.955 -7.310  1.00 17.97 ?  164 LEU   B HA   1 
ATOM   6472 H  HB2  . LEU   B 1 164 ? 39.628 -35.625 -8.461  1.00 17.20 ?  164 LEU   B HB2  1 
ATOM   6473 H  HB3  . LEU   B 1 164 ? 38.289 -34.850 -8.125  1.00 17.20 ?  164 LEU   B HB3  1 
ATOM   6474 H  HG   . LEU   B 1 164 ? 39.762 -36.117 -6.099  1.00 18.14 ?  164 LEU   B HG   1 
ATOM   6475 H  HD11 . LEU   B 1 164 ? 40.780 -34.075 -5.610  1.00 17.95 ?  164 LEU   B HD11 1 
ATOM   6476 H  HD12 . LEU   B 1 164 ? 41.206 -34.580 -7.055  1.00 17.95 ?  164 LEU   B HD12 1 
ATOM   6477 H  HD13 . LEU   B 1 164 ? 40.111 -33.439 -6.903  1.00 17.95 ?  164 LEU   B HD13 1 
ATOM   6478 H  HD21 . LEU   B 1 164 ? 38.613 -34.647 -4.679  1.00 20.26 ?  164 LEU   B HD21 1 
ATOM   6479 H  HD22 . LEU   B 1 164 ? 37.817 -34.085 -5.933  1.00 20.26 ?  164 LEU   B HD22 1 
ATOM   6480 H  HD23 . LEU   B 1 164 ? 37.607 -35.589 -5.468  1.00 20.26 ?  164 LEU   B HD23 1 
ATOM   6481 N  N    . VAL   B 1 165 ? 37.984 -37.050 -10.468 1.00 16.58 ?  165 VAL   B N    1 
ATOM   6482 C  CA   . VAL   B 1 165 ? 37.335 -36.994 -11.774 1.00 17.70 ?  165 VAL   B CA   1 
ATOM   6483 C  C    . VAL   B 1 165 ? 36.411 -38.191 -11.956 1.00 19.38 ?  165 VAL   B C    1 
ATOM   6484 O  O    . VAL   B 1 165 ? 35.249 -38.051 -12.357 1.00 20.43 ?  165 VAL   B O    1 
ATOM   6485 C  CB   . VAL   B 1 165 ? 38.388 -36.909 -12.895 1.00 18.78 ?  165 VAL   B CB   1 
ATOM   6486 C  CG1  . VAL   B 1 165 ? 37.734 -37.013 -14.256 1.00 20.43 ?  165 VAL   B CG1  1 
ATOM   6487 C  CG2  . VAL   B 1 165 ? 39.182 -35.615 -12.786 1.00 18.06 ?  165 VAL   B CG2  1 
ATOM   6488 H  H    . VAL   B 1 165 ? 38.834 -37.207 -10.499 1.00 19.90 ?  165 VAL   B H    1 
ATOM   6489 H  HA   . VAL   B 1 165 ? 36.798 -36.193 -11.819 1.00 21.24 ?  165 VAL   B HA   1 
ATOM   6490 H  HB   . VAL   B 1 165 ? 39.018 -37.642 -12.804 1.00 22.53 ?  165 VAL   B HB   1 
ATOM   6491 H  HG11 . VAL   B 1 165 ? 38.364 -36.726 -14.933 1.00 24.52 ?  165 VAL   B HG11 1 
ATOM   6492 H  HG12 . VAL   B 1 165 ? 37.487 -37.940 -14.412 1.00 24.52 ?  165 VAL   B HG12 1 
ATOM   6493 H  HG13 . VAL   B 1 165 ? 36.948 -36.452 -14.270 1.00 24.52 ?  165 VAL   B HG13 1 
ATOM   6494 H  HG21 . VAL   B 1 165 ? 39.823 -35.569 -13.516 1.00 21.67 ?  165 VAL   B HG21 1 
ATOM   6495 H  HG22 . VAL   B 1 165 ? 38.571 -34.862 -12.840 1.00 21.67 ?  165 VAL   B HG22 1 
ATOM   6496 H  HG23 . VAL   B 1 165 ? 39.652 -35.596 -11.937 1.00 21.67 ?  165 VAL   B HG23 1 
ATOM   6497 N  N    . SER   B 1 166 ? 36.918 -39.392 -11.653 1.00 20.35 ?  166 SER   B N    1 
ATOM   6498 C  CA   . SER   B 1 166 ? 36.160 -40.603 -11.930 1.00 21.97 ?  166 SER   B CA   1 
ATOM   6499 C  C    . SER   B 1 166 ? 34.900 -40.686 -11.082 1.00 22.28 ?  166 SER   B C    1 
ATOM   6500 O  O    . SER   B 1 166 ? 33.923 -41.296 -11.513 1.00 23.73 ?  166 SER   B O    1 
ATOM   6501 C  CB   . SER   B 1 166 ? 37.031 -41.853 -11.758 1.00 22.82 ?  166 SER   B CB   1 
ATOM   6502 O  OG   . SER   B 1 166 ? 37.389 -42.053 -10.403 1.00 22.56 ?  166 SER   B OG   1 
ATOM   6503 H  H    . SER   B 1 166 ? 37.697 -39.525 -11.295 1.00 24.42 ?  166 SER   B H    1 
ATOM   6504 H  HA   . SER   B 1 166 ? 35.886 -40.580 -12.857 1.00 26.36 ?  166 SER   B HA   1 
ATOM   6505 H  HB2  . SER   B 1 166 ? 36.533 -42.627 -12.068 1.00 27.39 ?  166 SER   B HB2  1 
ATOM   6506 H  HB3  . SER   B 1 166 ? 37.837 -41.753 -12.295 1.00 27.39 ?  166 SER   B HB3  1 
ATOM   6507 H  HG   . SER   B 1 166 ? 37.846 -41.405 -10.132 1.00 27.07 ?  166 SER   B HG   1 
ATOM   6508 N  N    . SER   B 1 167 ? 34.887 -40.086 -9.892  1.00 20.85 ?  167 SER   B N    1 
ATOM   6509 C  CA   . SER   B 1 167 ? 33.724 -40.135 -9.011  1.00 20.34 ?  167 SER   B CA   1 
ATOM   6510 C  C    . SER   B 1 167 ? 32.809 -38.915 -9.118  1.00 19.50 ?  167 SER   B C    1 
ATOM   6511 O  O    . SER   B 1 167 ? 31.728 -38.916 -8.517  1.00 19.67 ?  167 SER   B O    1 
ATOM   6512 C  CB   . SER   B 1 167 ? 34.160 -40.310 -7.551  1.00 20.40 ?  167 SER   B CB   1 
ATOM   6513 O  OG   . SER   B 1 167 ? 34.824 -39.147 -7.075  1.00 20.07 ?  167 SER   B OG   1 
ATOM   6514 H  H    . SER   B 1 167 ? 35.545 -39.647 -9.572  1.00 25.02 ?  167 SER   B H    1 
ATOM   6515 H  HA   . SER   B 1 167 ? 33.193 -40.916 -9.249  1.00 24.40 ?  167 SER   B HA   1 
ATOM   6516 H  HB2  . SER   B 1 167 ? 33.371 -40.479 -7.008  1.00 24.49 ?  167 SER   B HB2  1 
ATOM   6517 H  HB3  . SER   B 1 167 ? 34.762 -41.072 -7.495  1.00 24.49 ?  167 SER   B HB3  1 
ATOM   6518 H  HG   . SER   B 1 167 ? 35.501 -39.001 -7.545  1.00 24.08 ?  167 SER   B HG   1 
ATOM   6519 N  N    . PHE   B 1 168 ? 33.191 -37.884 -9.870  1.00 19.15 ?  168 PHE   B N    1 
ATOM   6520 C  CA   . PHE   B 1 168 ? 32.354 -36.686 -9.938  1.00 18.48 ?  168 PHE   B CA   1 
ATOM   6521 C  C    . PHE   B 1 168 ? 31.041 -36.952 -10.668 1.00 16.38 ?  168 PHE   B C    1 
ATOM   6522 O  O    . PHE   B 1 168 ? 30.000 -36.356 -10.330 1.00 17.09 ?  168 PHE   B O    1 
ATOM   6523 C  CB   . PHE   B 1 168 ? 33.115 -35.553 -10.620 1.00 19.21 ?  168 PHE   B CB   1 
ATOM   6524 C  CG   . PHE   B 1 168 ? 32.312 -34.304 -10.761 1.00 19.36 ?  168 PHE   B CG   1 
ATOM   6525 C  CD1  . PHE   B 1 168 ? 31.962 -33.566 -9.639  1.00 20.45 ?  168 PHE   B CD1  1 
ATOM   6526 C  CD2  . PHE   B 1 168 ? 31.891 -33.871 -12.001 1.00 18.95 ?  168 PHE   B CD2  1 
ATOM   6527 C  CE1  . PHE   B 1 168 ? 31.203 -32.416 -9.750  1.00 20.99 ?  168 PHE   B CE1  1 
ATOM   6528 C  CE2  . PHE   B 1 168 ? 31.142 -32.709 -12.125 1.00 19.88 ?  168 PHE   B CE2  1 
ATOM   6529 C  CZ   . PHE   B 1 168 ? 30.794 -31.982 -10.994 1.00 20.23 ?  168 PHE   B CZ   1 
ATOM   6530 H  H    . PHE   B 1 168 ? 33.912 -37.851 -10.335 1.00 22.98 ?  168 PHE   B H    1 
ATOM   6531 H  HA   . PHE   B 1 168 ? 32.136 -36.404 -9.038  1.00 22.17 ?  168 PHE   B HA   1 
ATOM   6532 H  HB2  . PHE   B 1 168 ? 33.899 -35.344 -10.093 1.00 23.05 ?  168 PHE   B HB2  1 
ATOM   6533 H  HB3  . PHE   B 1 168 ? 33.374 -35.838 -11.508 1.00 23.05 ?  168 PHE   B HB3  1 
ATOM   6534 H  HD1  . PHE   B 1 168 ? 32.230 -33.863 -8.799  1.00 24.54 ?  168 PHE   B HD1  1 
ATOM   6535 H  HD2  . PHE   B 1 168 ? 32.122 -34.351 -12.761 1.00 22.73 ?  168 PHE   B HD2  1 
ATOM   6536 H  HE1  . PHE   B 1 168 ? 30.973 -31.936 -8.988  1.00 25.19 ?  168 PHE   B HE1  1 
ATOM   6537 H  HE2  . PHE   B 1 168 ? 30.863 -32.421 -12.967 1.00 23.86 ?  168 PHE   B HE2  1 
ATOM   6538 H  HZ   . PHE   B 1 168 ? 30.285 -31.208 -11.077 1.00 24.28 ?  168 PHE   B HZ   1 
ATOM   6539 N  N    . LEU   B 1 169 ? 31.075 -37.824 -11.671 1.00 16.46 ?  169 LEU   B N    1 
ATOM   6540 C  CA   . LEU   B 1 169 ? 29.898 -38.132 -12.474 1.00 18.46 ?  169 LEU   B CA   1 
ATOM   6541 C  C    . LEU   B 1 169 ? 29.909 -39.566 -12.988 1.00 21.01 ?  169 LEU   B C    1 
ATOM   6542 O  O    . LEU   B 1 169 ? 28.996 -39.991 -13.701 1.00 23.39 ?  169 LEU   B O    1 
ATOM   6543 C  CB   . LEU   B 1 169 ? 29.813 -37.179 -13.663 1.00 20.52 ?  169 LEU   B CB   1 
ATOM   6544 C  CG   . LEU   B 1 169 ? 28.547 -36.327 -13.744 1.00 23.60 ?  169 LEU   B CG   1 
ATOM   6545 C  CD1  . LEU   B 1 169 ? 28.516 -35.574 -15.057 1.00 24.71 ?  169 LEU   B CD1  1 
ATOM   6546 C  CD2  . LEU   B 1 169 ? 27.296 -37.173 -13.581 1.00 23.24 ?  169 LEU   B CD2  1 
ATOM   6547 O  OXT  . LEU   B 1 169 ? 30.841 -40.314 -12.712 1.00 21.89 -1 169 LEU   B OXT  1 
ATOM   6548 H  H    . LEU   B 1 169 ? 31.781 -38.250 -11.919 1.00 19.75 ?  169 LEU   B H    1 
ATOM   6549 H  HA   . LEU   B 1 169 ? 29.111 -38.009 -11.925 1.00 22.16 ?  169 LEU   B HA   1 
ATOM   6550 H  HB2  . LEU   B 1 169 ? 30.568 -36.571 -13.625 1.00 24.62 ?  169 LEU   B HB2  1 
ATOM   6551 H  HB3  . LEU   B 1 169 ? 29.860 -37.700 -14.480 1.00 24.62 ?  169 LEU   B HB3  1 
ATOM   6552 H  HG   . LEU   B 1 169 ? 28.562 -35.672 -13.028 1.00 28.32 ?  169 LEU   B HG   1 
ATOM   6553 H  HD11 . LEU   B 1 169 ? 27.720 -35.022 -15.084 1.00 29.65 ?  169 LEU   B HD11 1 
ATOM   6554 H  HD12 . LEU   B 1 169 ? 29.308 -35.019 -15.120 1.00 29.65 ?  169 LEU   B HD12 1 
ATOM   6555 H  HD13 . LEU   B 1 169 ? 28.501 -36.215 -15.785 1.00 29.65 ?  169 LEU   B HD13 1 
ATOM   6556 H  HD21 . LEU   B 1 169 ? 26.543 -36.705 -13.969 1.00 27.89 ?  169 LEU   B HD21 1 
ATOM   6557 H  HD22 . LEU   B 1 169 ? 27.429 -38.022 -14.033 1.00 27.89 ?  169 LEU   B HD22 1 
ATOM   6558 H  HD23 . LEU   B 1 169 ? 27.142 -37.325 -12.636 1.00 27.89 ?  169 LEU   B HD23 1 
HETATM 6559 C  C1   T TFA   C 2 .   ? 12.134 -1.206  1.470   0.10 5.76  ?  201 TFA   A C1   1 
HETATM 6560 C  C2   T TFA   C 2 .   ? 12.722 -1.701  0.122   0.10 7.33  ?  201 TFA   A C2   1 
HETATM 6561 O  O    T TFA   C 2 .   ? 12.864 -1.450  2.442   0.10 4.10  ?  201 TFA   A O    1 
HETATM 6562 F  F1   T TFA   C 2 .   ? 12.758 -3.044  0.082   0.10 8.06  ?  201 TFA   A F1   1 
HETATM 6563 F  F2   T TFA   C 2 .   ? 11.999 -1.327  -0.945  0.10 7.54  ?  201 TFA   A F2   1 
HETATM 6564 F  F3   T TFA   C 2 .   ? 13.967 -1.265  -0.094  0.10 8.16  ?  201 TFA   A F3   1 
HETATM 6565 O  OXT  T TFA   C 2 .   ? 11.042 -0.638  1.397   0.10 6.19  ?  201 TFA   A OXT  1 
HETATM 6566 N  N2   B A1A9A D 3 .   ? 14.997 0.038   4.136   0.44 10.71 ?  202 A1A9A A N2   1 
HETATM 6567 C  C3   B A1A9A D 3 .   ? 12.035 1.283   0.995   0.44 12.84 ?  202 A1A9A A C3   1 
HETATM 6568 C  C6   B A1A9A D 3 .   ? 11.231 0.375   -1.539  0.44 12.84 ?  202 A1A9A A C6   1 
HETATM 6569 C  C9   B A1A9A D 3 .   ? 15.412 0.231   -0.218  0.44 11.36 ?  202 A1A9A A C9   1 
HETATM 6570 C  C12  B A1A9A D 3 .   ? 15.119 1.205   3.427   0.44 10.36 ?  202 A1A9A A C12  1 
HETATM 6571 C  C14  B A1A9A D 3 .   ? 15.367 2.262   5.583   0.44 10.75 ?  202 A1A9A A C14  1 
HETATM 6572 C  C17  B A1A9A D 3 .   ? 15.655 4.460   5.173   0.44 10.94 ?  202 A1A9A A C17  1 
HETATM 6573 C  C1   B A1A9A D 3 .   ? 13.530 -0.767  1.334   0.44 12.49 ?  202 A1A9A A C1   1 
HETATM 6574 C  C10  B A1A9A D 3 .   ? 15.232 1.755   -0.338  0.44 11.23 ?  202 A1A9A A C10  1 
HETATM 6575 C  C11  B A1A9A D 3 .   ? 15.245 2.276   1.124   0.44 10.73 ?  202 A1A9A A C11  1 
HETATM 6576 C  C13  B A1A9A D 3 .   ? 15.059 0.032   5.511   0.44 10.72 ?  202 A1A9A A C13  1 
HETATM 6577 C  C15  B A1A9A D 3 .   ? 15.324 2.427   4.159   0.44 10.57 ?  202 A1A9A A C15  1 
HETATM 6578 C  C16  B A1A9A D 3 .   ? 15.524 3.856   3.927   0.44 11.36 ?  202 A1A9A A C16  1 
HETATM 6579 C  C2   B A1A9A D 3 .   ? 12.539 0.068   0.514   0.44 12.04 ?  202 A1A9A A C2   1 
HETATM 6580 C  C4   B A1A9A D 3 .   ? 11.142 2.045   0.224   0.44 13.36 ?  202 A1A9A A C4   1 
HETATM 6581 C  C5   B A1A9A D 3 .   ? 10.734 1.586   -1.038  0.44 13.16 ?  202 A1A9A A C5   1 
HETATM 6582 C  C7   B A1A9A D 3 .   ? 12.132 -0.376  -0.763  0.44 11.92 ?  202 A1A9A A C7   1 
HETATM 6583 C  C8   B A1A9A D 3 .   ? 15.007 -0.142  1.271   0.44 10.97 ?  202 A1A9A A C8   1 
HETATM 6584 N  N1   B A1A9A D 3 .   ? 15.048 1.128   2.043   0.44 10.22 ?  202 A1A9A A N1   1 
HETATM 6585 N  N3   B A1A9A D 3 .   ? 15.242 1.101   6.281   0.44 10.94 ?  202 A1A9A A N3   1 
HETATM 6586 N  N4   B A1A9A D 3 .   ? 15.563 3.486   6.116   0.44 10.70 ?  202 A1A9A A N4   1 
HETATM 6587 O  O1   B A1A9A D 3 .   ? 13.568 -2.092  0.849   0.44 14.61 ?  202 A1A9A A O1   1 
HETATM 6588 H  H4   B A1A9A D 3 .   ? 12.336 1.655   1.985   0.44 15.41 ?  202 A1A9A A H4   1 
HETATM 6589 H  H7   B A1A9A D 3 .   ? 10.907 0.016   -2.556  0.44 15.41 ?  202 A1A9A A H7   1 
HETATM 6590 H  H10  B A1A9A D 3 .   ? 16.446 -0.105  -0.483  0.44 13.64 ?  202 A1A9A A H10  1 
HETATM 6591 H  H9   B A1A9A D 3 .   ? 14.784 -0.301  -0.982  0.44 13.64 ?  202 A1A9A A H9   1 
HETATM 6592 H  H17  B A1A9A D 3 .   ? 15.815 5.478   5.527   0.44 13.13 ?  202 A1A9A A H17  1 
HETATM 6593 H  H1   B A1A9A D 3 .   ? 13.259 -0.797  2.426   0.44 14.98 ?  202 A1A9A A H1   1 
HETATM 6594 H  H12  B A1A9A D 3 .   ? 14.285 2.026   -0.853  0.44 13.48 ?  202 A1A9A A H12  1 
HETATM 6595 H  H11  B A1A9A D 3 .   ? 16.019 2.243   -1.001  0.44 13.48 ?  202 A1A9A A H11  1 
HETATM 6596 H  H14  B A1A9A D 3 .   ? 14.493 3.068   1.263   0.44 12.88 ?  202 A1A9A A H14  1 
HETATM 6597 H  H13  B A1A9A D 3 .   ? 16.246 2.798   1.303   0.44 12.88 ?  202 A1A9A A H13  1 
HETATM 6598 H  H15  B A1A9A D 3 .   ? 14.929 -0.942  6.071   0.44 12.86 ?  202 A1A9A A H15  1 
HETATM 6599 H  H16  B A1A9A D 3 .   ? 15.560 4.410   3.011   0.44 13.63 ?  202 A1A9A A H16  1 
HETATM 6600 H  H5   B A1A9A D 3 .   ? 10.731 3.016   0.636   0.44 16.03 ?  202 A1A9A A H5   1 
HETATM 6601 H  H6   B A1A9A D 3 .   ? 10.013 2.186   -1.657  0.44 15.79 ?  202 A1A9A A H6   1 
HETATM 6602 H  H8   B A1A9A D 3 .   ? 12.524 -1.336  -1.168  0.44 14.30 ?  202 A1A9A A H8   1 
HETATM 6603 H  H2   B A1A9A D 3 .   ? 15.769 -0.870  1.657   0.44 13.16 ?  202 A1A9A A H2   1 
HETATM 6604 H  H18  B A1A9A D 3 .   ? 15.625 3.654   7.162   0.44 12.84 ?  202 A1A9A A H18  1 
HETATM 6605 H  H3   B A1A9A D 3 .   ? 12.781 -2.591  1.109   0.44 17.54 ?  202 A1A9A A H3   1 
HETATM 6606 CL CL   B CL    E 4 .   ? 18.628 2.179   -0.921  0.44 16.16 ?  203 CL    A CL   1 
HETATM 6607 O  O    . HOH   F 5 .   ? 17.051 -17.978 14.940  1.00 28.40 ?  301 HOH   A O    1 
HETATM 6608 O  O    . HOH   F 5 .   ? 14.714 -4.590  20.589  1.00 46.44 ?  302 HOH   A O    1 
HETATM 6609 O  O    . HOH   F 5 .   ? 0.807  -4.059  0.055   1.00 27.39 ?  303 HOH   A O    1 
HETATM 6610 O  O    A HOH   F 5 .   ? 12.224 0.294   14.858  0.56 27.11 ?  304 HOH   A O    1 
HETATM 6611 O  O    . HOH   F 5 .   ? -0.657 -8.159  2.139   1.00 38.89 ?  305 HOH   A O    1 
HETATM 6612 O  O    . HOH   F 5 .   ? 34.299 -1.853  12.482  1.00 38.64 ?  306 HOH   A O    1 
HETATM 6613 O  O    A HOH   F 5 .   ? 4.639  3.975   0.603   0.56 20.30 ?  307 HOH   A O    1 
HETATM 6614 O  O    B HOH   F 5 .   ? 5.007  3.469   0.396   0.44 15.13 ?  308 HOH   A O    1 
HETATM 6615 O  O    B HOH   F 5 .   ? 21.660 3.040   -0.012  0.44 17.66 ?  309 HOH   A O    1 
HETATM 6616 O  O    . HOH   F 5 .   ? 14.986 3.854   17.721  1.00 38.60 ?  310 HOH   A O    1 
HETATM 6617 O  O    A HOH   F 5 .   ? -0.540 -3.031  3.079   0.56 28.20 ?  311 HOH   A O    1 
HETATM 6618 O  O    . HOH   F 5 .   ? 15.004 -12.101 18.685  1.00 34.55 ?  312 HOH   A O    1 
HETATM 6619 O  O    B HOH   F 5 .   ? 6.786  1.913   7.229   0.44 30.13 ?  313 HOH   A O    1 
HETATM 6620 O  O    . HOH   F 5 .   ? 18.856 -21.949 6.997   1.00 33.66 ?  314 HOH   A O    1 
HETATM 6621 O  O    . HOH   F 5 .   ? 19.816 -12.384 -9.074  1.00 24.57 ?  315 HOH   A O    1 
HETATM 6622 O  O    . HOH   F 5 .   ? 42.435 10.542  5.199   1.00 20.53 ?  316 HOH   A O    1 
HETATM 6623 O  O    . HOH   F 5 .   ? 9.803  -21.282 5.664   1.00 20.21 ?  317 HOH   A O    1 
HETATM 6624 O  O    . HOH   F 5 .   ? 28.927 0.509   -9.655  1.00 21.59 ?  318 HOH   A O    1 
HETATM 6625 O  O    . HOH   F 5 .   ? 15.199 -8.041  -9.819  1.00 22.50 ?  319 HOH   A O    1 
HETATM 6626 O  O    . HOH   F 5 .   ? 13.503 -15.227 -7.528  1.00 25.77 ?  320 HOH   A O    1 
HETATM 6627 O  O    . HOH   F 5 .   ? 15.118 -21.465 14.244  1.00 19.61 ?  321 HOH   A O    1 
HETATM 6628 O  O    . HOH   F 5 .   ? 28.057 -6.294  19.643  1.00 40.04 ?  322 HOH   A O    1 
HETATM 6629 O  O    . HOH   F 5 .   ? 14.621 -13.929 16.680  1.00 22.33 ?  323 HOH   A O    1 
HETATM 6630 O  O    . HOH   F 5 .   ? 31.006 6.139   -12.295 1.00 29.49 ?  324 HOH   A O    1 
HETATM 6631 O  O    . HOH   F 5 .   ? 9.154  -10.128 19.324  1.00 38.23 ?  325 HOH   A O    1 
HETATM 6632 O  O    . HOH   F 5 .   ? 13.115 -1.495  -6.677  1.00 17.89 ?  326 HOH   A O    1 
HETATM 6633 O  O    . HOH   F 5 .   ? 26.399 -19.292 -1.799  1.00 14.69 ?  327 HOH   A O    1 
HETATM 6634 O  O    . HOH   F 5 .   ? 27.291 13.786  2.917   1.00 31.13 ?  328 HOH   A O    1 
HETATM 6635 O  O    A HOH   F 5 .   ? 14.019 -4.532  -11.744 0.56 22.55 ?  329 HOH   A O    1 
HETATM 6636 O  O    . HOH   F 5 .   ? 33.926 -1.064  -8.932  1.00 28.04 ?  330 HOH   A O    1 
HETATM 6637 O  O    . HOH   F 5 .   ? 7.894  -12.406 -0.935  1.00 19.60 ?  331 HOH   A O    1 
HETATM 6638 O  O    . HOH   F 5 .   ? 6.891  -8.003  11.825  1.00 17.10 ?  332 HOH   A O    1 
HETATM 6639 O  O    . HOH   F 5 .   ? 30.164 -13.283 -8.617  1.00 20.33 ?  333 HOH   A O    1 
HETATM 6640 O  O    . HOH   F 5 .   ? 22.230 5.402   18.891  1.00 40.66 ?  334 HOH   A O    1 
HETATM 6641 O  O    B HOH   F 5 .   ? 14.932 -2.701  3.423   0.44 13.39 ?  335 HOH   A O    1 
HETATM 6642 O  O    B HOH   F 5 .   ? 18.480 -1.962  0.549   0.44 19.93 ?  336 HOH   A O    1 
HETATM 6643 O  O    . HOH   F 5 .   ? 36.142 -5.097  -0.586  1.00 35.35 ?  337 HOH   A O    1 
HETATM 6644 O  O    . HOH   F 5 .   ? 30.941 -18.087 7.803   1.00 20.37 ?  338 HOH   A O    1 
HETATM 6645 O  O    . HOH   F 5 .   ? 13.961 -22.977 7.435   1.00 18.79 ?  339 HOH   A O    1 
HETATM 6646 O  O    . HOH   F 5 .   ? 44.317 7.149   6.385   1.00 27.07 ?  340 HOH   A O    1 
HETATM 6647 O  O    . HOH   F 5 .   ? 28.213 -0.100  -13.393 1.00 37.89 ?  341 HOH   A O    1 
HETATM 6648 O  O    . HOH   F 5 .   ? 8.850  -12.079 17.080  1.00 43.41 ?  342 HOH   A O    1 
HETATM 6649 O  O    . HOH   F 5 .   ? 39.692 -1.031  -5.181  1.00 21.63 ?  343 HOH   A O    1 
HETATM 6650 O  O    T HOH   F 5 .   ? 15.348 -0.375  2.379   0.10 6.01  ?  344 HOH   A O    1 
HETATM 6651 O  O    . HOH   F 5 .   ? 37.536 2.777   10.151  1.00 30.90 ?  345 HOH   A O    1 
HETATM 6652 O  O    A HOH   F 5 .   ? 11.008 -0.329  1.923   0.46 29.01 ?  346 HOH   A O    1 
HETATM 6653 O  O    A HOH   F 5 .   ? 14.213 0.618   6.792   0.56 22.12 ?  347 HOH   A O    1 
HETATM 6654 O  O    B HOH   F 5 .   ? 14.861 7.281   7.406   0.44 19.95 ?  348 HOH   A O    1 
HETATM 6655 O  O    . HOH   F 5 .   ? 38.267 10.097  7.192   1.00 34.16 ?  349 HOH   A O    1 
HETATM 6656 O  O    . HOH   F 5 .   ? 14.282 -21.138 -4.268  1.00 31.19 ?  350 HOH   A O    1 
HETATM 6657 O  O    . HOH   F 5 .   ? 31.709 8.171   14.860  1.00 25.71 ?  351 HOH   A O    1 
HETATM 6658 O  O    . HOH   F 5 .   ? 20.548 -19.715 -5.127  1.00 29.81 ?  352 HOH   A O    1 
HETATM 6659 O  O    A HOH   F 5 .   ? 14.572 -3.608  3.088   0.56 13.92 ?  353 HOH   A O    1 
HETATM 6660 O  O    . HOH   F 5 .   ? 38.528 4.980   6.960   1.00 16.17 ?  354 HOH   A O    1 
HETATM 6661 O  O    . HOH   F 5 .   ? 21.184 -2.294  -2.309  1.00 15.48 ?  355 HOH   A O    1 
HETATM 6662 O  O    . HOH   F 5 .   ? 16.932 -19.207 4.857   1.00 16.42 ?  356 HOH   A O    1 
HETATM 6663 O  O    . HOH   F 5 .   ? 37.359 11.928  4.953   1.00 33.87 ?  357 HOH   A O    1 
HETATM 6664 O  O    . HOH   F 5 .   ? 18.613 -19.378 13.543  1.00 44.42 ?  358 HOH   A O    1 
HETATM 6665 O  O    . HOH   F 5 .   ? 37.152 -2.837  9.675   1.00 41.32 ?  359 HOH   A O    1 
HETATM 6666 O  O    . HOH   F 5 .   ? 26.794 11.430  1.694   1.00 17.11 ?  360 HOH   A O    1 
HETATM 6667 O  O    . HOH   F 5 .   ? 22.207 -19.195 11.362  1.00 35.72 ?  361 HOH   A O    1 
HETATM 6668 O  O    . HOH   F 5 .   ? 31.747 -9.292  -6.686  1.00 21.68 ?  362 HOH   A O    1 
HETATM 6669 O  O    . HOH   F 5 .   ? 42.514 4.254   5.332   1.00 30.01 ?  363 HOH   A O    1 
HETATM 6670 O  O    B HOH   F 5 .   ? 8.599  4.247   0.941   0.44 16.99 ?  364 HOH   A O    1 
HETATM 6671 O  O    . HOH   F 5 .   ? 27.290 -6.080  -13.945 1.00 39.90 ?  365 HOH   A O    1 
HETATM 6672 O  O    . HOH   F 5 .   ? 23.961 -2.049  -2.079  1.00 10.75 ?  366 HOH   A O    1 
HETATM 6673 O  O    . HOH   F 5 .   ? 16.450 -22.001 0.914   1.00 28.68 ?  367 HOH   A O    1 
HETATM 6674 O  O    . HOH   F 5 .   ? 30.983 -13.918 -2.482  1.00 13.89 ?  368 HOH   A O    1 
HETATM 6675 O  O    . HOH   F 5 .   ? 43.928 8.398   -3.099  1.00 26.18 ?  369 HOH   A O    1 
HETATM 6676 O  O    A HOH   F 5 .   ? 17.437 -1.668  0.436   0.56 19.12 ?  370 HOH   A O    1 
HETATM 6677 O  O    . HOH   F 5 .   ? 5.483  2.984   4.796   1.00 36.93 ?  371 HOH   A O    1 
HETATM 6678 O  O    . HOH   F 5 .   ? 21.838 -21.876 8.437   1.00 27.99 ?  372 HOH   A O    1 
HETATM 6679 O  O    . HOH   F 5 .   ? 35.694 -12.655 6.850   1.00 16.60 ?  373 HOH   A O    1 
HETATM 6680 O  O    . HOH   F 5 .   ? 17.054 -17.774 -5.095  1.00 27.07 ?  374 HOH   A O    1 
HETATM 6681 O  O    . HOH   F 5 .   ? 18.431 5.008   -15.149 1.00 38.59 ?  375 HOH   A O    1 
HETATM 6682 O  O    . HOH   F 5 .   ? 18.577 9.479   9.043   1.00 21.17 ?  376 HOH   A O    1 
HETATM 6683 O  O    B HOH   F 5 .   ? 11.509 6.488   10.061  0.44 24.95 ?  377 HOH   A O    1 
HETATM 6684 O  O    . HOH   F 5 .   ? 33.597 -7.141  4.270   1.00 16.80 ?  378 HOH   A O    1 
HETATM 6685 O  O    . HOH   F 5 .   ? 30.768 3.087   8.251   1.00 12.10 ?  379 HOH   A O    1 
HETATM 6686 O  O    . HOH   F 5 .   ? 21.272 10.244  15.069  1.00 35.27 ?  380 HOH   A O    1 
HETATM 6687 O  O    . HOH   F 5 .   ? 31.659 -7.278  -9.861  1.00 21.14 ?  381 HOH   A O    1 
HETATM 6688 O  O    . HOH   F 5 .   ? 22.680 12.467  1.595   1.00 15.96 ?  382 HOH   A O    1 
HETATM 6689 O  O    . HOH   F 5 .   ? 7.964  -21.436 4.016   1.00 43.11 ?  383 HOH   A O    1 
HETATM 6690 O  O    B HOH   F 5 .   ? 10.995 1.929   12.267  0.44 20.27 ?  384 HOH   A O    1 
HETATM 6691 O  O    . HOH   F 5 .   ? 22.600 -11.965 21.765  1.00 43.92 ?  385 HOH   A O    1 
HETATM 6692 O  O    . HOH   F 5 .   ? 6.589  -3.096  12.683  1.00 25.85 ?  386 HOH   A O    1 
HETATM 6693 O  O    . HOH   F 5 .   ? 25.607 -0.728  -7.304  1.00 15.80 ?  387 HOH   A O    1 
HETATM 6694 O  O    . HOH   F 5 .   ? 10.313 -22.117 -1.141  1.00 44.64 ?  388 HOH   A O    1 
HETATM 6695 O  O    . HOH   F 5 .   ? 7.540  -6.373  -6.764  1.00 44.34 ?  389 HOH   A O    1 
HETATM 6696 O  O    . HOH   F 5 .   ? 24.183 -7.755  14.409  1.00 17.44 ?  390 HOH   A O    1 
HETATM 6697 O  O    B HOH   F 5 .   ? 11.707 0.508   14.608  0.44 27.90 ?  391 HOH   A O    1 
HETATM 6698 O  O    . HOH   F 5 .   ? 33.420 -16.967 8.037   1.00 19.23 ?  392 HOH   A O    1 
HETATM 6699 O  O    . HOH   F 5 .   ? 14.405 -24.643 11.549  1.00 40.63 ?  393 HOH   A O    1 
HETATM 6700 O  O    A HOH   F 5 .   ? 3.526  -9.410  9.709   0.56 25.53 ?  394 HOH   A O    1 
HETATM 6701 O  O    . HOH   F 5 .   ? 37.467 -2.002  5.755   1.00 26.30 ?  395 HOH   A O    1 
HETATM 6702 O  O    . HOH   F 5 .   ? 13.841 -4.891  17.312  1.00 26.53 ?  396 HOH   A O    1 
HETATM 6703 O  O    . HOH   F 5 .   ? 27.449 -10.644 14.054  1.00 18.13 ?  397 HOH   A O    1 
HETATM 6704 O  O    . HOH   F 5 .   ? 43.341 7.847   2.748   1.00 27.26 ?  398 HOH   A O    1 
HETATM 6705 O  O    A HOH   F 5 .   ? 15.738 -0.901  5.263   0.56 19.02 ?  399 HOH   A O    1 
HETATM 6706 O  O    . HOH   F 5 .   ? 24.337 3.637   -1.795  1.00 14.74 ?  400 HOH   A O    1 
HETATM 6707 O  O    . HOH   F 5 .   ? 32.721 -9.214  5.955   1.00 20.50 ?  401 HOH   A O    1 
HETATM 6708 O  O    . HOH   F 5 .   ? 18.843 -0.692  -1.725  1.00 14.87 ?  402 HOH   A O    1 
HETATM 6709 O  O    . HOH   F 5 .   ? 14.493 -0.522  -12.230 1.00 21.76 ?  403 HOH   A O    1 
HETATM 6710 O  O    . HOH   F 5 .   ? 30.002 -10.116 12.950  1.00 21.23 ?  404 HOH   A O    1 
HETATM 6711 O  O    . HOH   F 5 .   ? 24.606 -17.538 12.641  1.00 24.80 ?  405 HOH   A O    1 
HETATM 6712 O  O    . HOH   F 5 .   ? 18.614 -2.367  -16.445 1.00 44.82 ?  406 HOH   A O    1 
HETATM 6713 O  O    . HOH   F 5 .   ? 28.456 -10.601 -13.969 1.00 46.65 ?  407 HOH   A O    1 
HETATM 6714 O  O    . HOH   F 5 .   ? 23.455 11.386  4.090   1.00 13.00 ?  408 HOH   A O    1 
HETATM 6715 O  O    . HOH   F 5 .   ? 20.001 4.571   -7.593  1.00 20.37 ?  409 HOH   A O    1 
HETATM 6716 O  O    . HOH   F 5 .   ? 21.709 -13.731 -8.243  1.00 39.32 ?  410 HOH   A O    1 
HETATM 6717 O  O    A HOH   F 5 .   ? 24.533 2.083   -6.986  0.56 14.00 ?  411 HOH   A O    1 
HETATM 6718 O  O    . HOH   F 5 .   ? 27.358 2.288   18.733  1.00 28.22 ?  412 HOH   A O    1 
HETATM 6719 O  O    . HOH   F 5 .   ? 38.114 -1.383  -1.949  1.00 18.64 ?  413 HOH   A O    1 
HETATM 6720 O  O    . HOH   F 5 .   ? 6.343  -5.425  11.040  1.00 17.12 ?  414 HOH   A O    1 
HETATM 6721 O  O    . HOH   F 5 .   ? 15.463 11.771  7.933   1.00 41.91 ?  415 HOH   A O    1 
HETATM 6722 O  O    . HOH   F 5 .   ? 23.888 -15.645 -9.209  1.00 34.00 ?  416 HOH   A O    1 
HETATM 6723 O  O    . HOH   F 5 .   ? 30.726 1.811   16.672  1.00 20.05 ?  417 HOH   A O    1 
HETATM 6724 O  O    . HOH   F 5 .   ? 23.826 -20.236 -1.369  1.00 16.91 ?  418 HOH   A O    1 
HETATM 6725 O  O    A HOH   F 5 .   ? 21.294 3.198   -0.349  0.56 9.86  ?  419 HOH   A O    1 
HETATM 6726 O  O    . HOH   F 5 .   ? 15.813 2.119   24.760  1.00 47.54 ?  420 HOH   A O    1 
HETATM 6727 O  O    . HOH   F 5 .   ? 20.490 -19.992 2.717   1.00 18.64 ?  421 HOH   A O    1 
HETATM 6728 O  O    B HOH   F 5 .   ? 22.910 5.926   -1.555  0.44 23.39 ?  422 HOH   A O    1 
HETATM 6729 O  O    B HOH   F 5 .   ? 12.160 -2.388  -4.429  0.44 19.20 ?  423 HOH   A O    1 
HETATM 6730 O  O    . HOH   F 5 .   ? 30.261 -12.922 13.485  1.00 20.14 ?  424 HOH   A O    1 
HETATM 6731 O  O    . HOH   F 5 .   ? 26.867 4.192   -0.673  1.00 12.52 ?  425 HOH   A O    1 
HETATM 6732 O  O    . HOH   F 5 .   ? 44.821 -0.647  3.059   1.00 38.84 ?  426 HOH   A O    1 
HETATM 6733 O  O    B HOH   F 5 .   ? 20.319 4.743   -2.487  0.44 29.33 ?  427 HOH   A O    1 
HETATM 6734 O  O    . HOH   F 5 .   ? 40.827 -8.255  -6.684  1.00 37.31 ?  428 HOH   A O    1 
HETATM 6735 O  O    . HOH   F 5 .   ? 32.561 -4.243  -9.913  1.00 29.12 ?  429 HOH   A O    1 
HETATM 6736 O  O    . HOH   F 5 .   ? 27.870 0.845   -7.130  1.00 13.82 ?  430 HOH   A O    1 
HETATM 6737 O  O    . HOH   F 5 .   ? 16.153 16.661  8.597   1.00 35.17 ?  431 HOH   A O    1 
HETATM 6738 O  O    . HOH   F 5 .   ? 34.950 -5.218  -3.098  1.00 18.16 ?  432 HOH   A O    1 
HETATM 6739 O  O    . HOH   F 5 .   ? 41.544 1.594   4.975   1.00 37.56 ?  433 HOH   A O    1 
HETATM 6740 O  O    . HOH   F 5 .   ? 22.712 8.055   18.420  1.00 47.52 ?  434 HOH   A O    1 
HETATM 6741 O  O    . HOH   F 5 .   ? 36.690 -4.956  5.338   1.00 23.02 ?  435 HOH   A O    1 
HETATM 6742 O  O    A HOH   F 5 .   ? 10.970 1.596   12.742  0.56 19.22 ?  436 HOH   A O    1 
HETATM 6743 O  O    . HOH   F 5 .   ? 16.101 -14.119 20.260  1.00 49.55 ?  437 HOH   A O    1 
HETATM 6744 O  O    . HOH   F 5 .   ? 15.915 6.901   2.928   1.00 16.52 ?  438 HOH   A O    1 
HETATM 6745 O  O    . HOH   F 5 .   ? 23.946 3.954   -4.733  1.00 21.73 ?  439 HOH   A O    1 
HETATM 6746 O  O    . HOH   F 5 .   ? 32.429 -10.627 3.205   1.00 32.27 ?  440 HOH   A O    1 
HETATM 6747 O  O    . HOH   F 5 .   ? 10.277 -13.659 -1.681  1.00 17.56 ?  441 HOH   A O    1 
HETATM 6748 O  O    . HOH   F 5 .   ? 27.081 -3.159  19.330  1.00 36.32 ?  442 HOH   A O    1 
HETATM 6749 O  O    A HOH   F 5 .   ? 11.674 -10.726 -10.080 0.56 32.92 ?  443 HOH   A O    1 
HETATM 6750 O  O    . HOH   F 5 .   ? 11.684 -10.636 16.898  1.00 22.95 ?  444 HOH   A O    1 
HETATM 6751 O  O    . HOH   F 5 .   ? 9.459  -16.231 -1.989  1.00 30.15 ?  445 HOH   A O    1 
HETATM 6752 O  O    . HOH   F 5 .   ? 23.550 -8.050  17.075  1.00 22.32 ?  446 HOH   A O    1 
HETATM 6753 O  O    . HOH   F 5 .   ? 18.340 -15.908 16.362  1.00 39.88 ?  447 HOH   A O    1 
HETATM 6754 O  O    A HOH   F 5 .   ? 13.967 -0.292  3.453   0.46 43.93 ?  448 HOH   A O    1 
HETATM 6755 O  O    A HOH   F 5 .   ? 18.808 2.078   -0.754  0.56 18.29 ?  449 HOH   A O    1 
HETATM 6756 O  O    . HOH   F 5 .   ? 23.225 -20.910 1.285   1.00 18.36 ?  450 HOH   A O    1 
HETATM 6757 O  O    A HOH   F 5 .   ? 16.205 2.995   -1.446  0.56 16.11 ?  451 HOH   A O    1 
HETATM 6758 O  O    . HOH   F 5 .   ? 20.503 -17.800 24.756  1.00 47.75 ?  452 HOH   A O    1 
HETATM 6759 O  O    . HOH   F 5 .   ? 34.341 -8.081  -0.568  1.00 29.27 ?  453 HOH   A O    1 
HETATM 6760 O  O    . HOH   F 5 .   ? 19.469 -10.957 24.065  1.00 57.08 ?  454 HOH   A O    1 
HETATM 6761 O  O    . HOH   F 5 .   ? 21.203 -9.163  21.323  1.00 47.30 ?  455 HOH   A O    1 
HETATM 6762 O  O    . HOH   F 5 .   ? 21.405 -14.702 17.992  1.00 50.45 ?  456 HOH   A O    1 
HETATM 6763 O  O    . HOH   F 5 .   ? 23.167 7.581   -3.262  1.00 35.47 ?  457 HOH   A O    1 
HETATM 6764 O  O    . HOH   F 5 .   ? 30.581 14.767  2.766   1.00 19.42 ?  458 HOH   A O    1 
HETATM 6765 O  O    . HOH   F 5 .   ? 37.608 -8.762  -3.340  1.00 24.90 ?  459 HOH   A O    1 
HETATM 6766 O  O    . HOH   F 5 .   ? 31.242 -12.770 -0.013  1.00 19.81 ?  460 HOH   A O    1 
HETATM 6767 O  O    B HOH   F 5 .   ? 7.774  1.704   -2.957  0.44 19.16 ?  461 HOH   A O    1 
HETATM 6768 O  O    . HOH   F 5 .   ? 29.743 -16.031 10.638  1.00 39.24 ?  462 HOH   A O    1 
HETATM 6769 O  O    . HOH   F 5 .   ? 24.782 5.574   20.778  1.00 51.15 ?  463 HOH   A O    1 
HETATM 6770 O  O    . HOH   F 5 .   ? -1.637 -4.700  7.601   1.00 53.60 ?  464 HOH   A O    1 
HETATM 6771 O  O    . HOH   F 5 .   ? 27.794 7.054   -6.484  1.00 37.30 ?  465 HOH   A O    1 
HETATM 6772 O  O    . HOH   F 5 .   ? 32.343 -15.892 10.886  1.00 35.17 ?  466 HOH   A O    1 
HETATM 6773 O  O    . HOH   F 5 .   ? 25.368 8.232   -4.871  1.00 37.46 ?  467 HOH   A O    1 
HETATM 6774 O  O    . HOH   F 5 .   ? 19.802 -17.313 -5.067  1.00 24.26 ?  468 HOH   A O    1 
HETATM 6775 O  O    . HOH   F 5 .   ? 29.726 -1.937  -12.712 1.00 44.55 ?  469 HOH   A O    1 
HETATM 6776 O  O    . HOH   F 5 .   ? 23.087 -22.380 -3.296  1.00 34.99 ?  470 HOH   A O    1 
HETATM 6777 O  O    . HOH   F 5 .   ? 27.370 -11.258 16.602  1.00 38.74 ?  471 HOH   A O    1 
HETATM 6778 O  O    . HOH   F 5 .   ? 24.578 14.666  7.853   1.00 36.05 ?  472 HOH   A O    1 
HETATM 6779 O  O    . HOH   F 5 .   ? 21.760 5.148   -5.644  1.00 34.17 ?  473 HOH   A O    1 
HETATM 6780 O  O    . HOH   F 5 .   ? 10.987 -14.955 -6.147  1.00 34.88 ?  474 HOH   A O    1 
HETATM 6781 O  O    . HOH   F 5 .   ? 15.710 -21.483 3.682   1.00 25.64 ?  475 HOH   A O    1 
HETATM 6782 O  O    . HOH   F 5 .   ? 39.526 -7.008  -3.535  1.00 45.06 ?  476 HOH   A O    1 
HETATM 6783 O  O    . HOH   F 5 .   ? 18.796 10.977  11.271  1.00 34.30 ?  477 HOH   A O    1 
HETATM 6784 O  O    . HOH   F 5 .   ? 26.781 11.661  -1.383  1.00 32.91 ?  478 HOH   A O    1 
HETATM 6785 O  O    . HOH   F 5 .   ? 11.875 -13.407 16.346  1.00 48.20 ?  479 HOH   A O    1 
HETATM 6786 O  O    . HOH   F 5 .   ? 23.480 13.740  5.503   1.00 18.85 ?  480 HOH   A O    1 
HETATM 6787 O  O    . HOH   F 5 .   ? 17.997 -16.296 -8.861  1.00 42.41 ?  481 HOH   A O    1 
HETATM 6788 O  O    . HOH   F 5 .   ? 12.211 1.619   17.350  1.00 41.06 ?  482 HOH   A O    1 
HETATM 6789 O  O    . HOH   F 5 .   ? 15.714 -17.141 -6.996  1.00 31.45 ?  483 HOH   A O    1 
HETATM 6790 O  O    . HOH   F 5 .   ? 25.768 10.756  -3.803  1.00 28.35 ?  484 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 13.990 -10.353 -10.966 1.00 32.37 ?  485 HOH   A O    1 
HETATM 6792 O  O    . HOH   F 5 .   ? 28.905 8.999   17.536  1.00 38.15 ?  486 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 35.223 7.430   12.278  1.00 48.25 ?  487 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 16.819 -20.519 16.074  1.00 30.23 ?  488 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 17.365 -18.664 19.809  1.00 50.58 ?  489 HOH   A O    1 
HETATM 6796 O  O    . HOH   F 5 .   ? 23.068 11.794  -4.109  1.00 19.54 ?  490 HOH   A O    1 
HETATM 6797 O  O    . HOH   F 5 .   ? 40.839 -3.980  -0.391  1.00 37.68 ?  491 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 16.017 -6.731  -11.951 1.00 43.38 ?  492 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 30.886 0.723   19.184  1.00 41.87 ?  493 HOH   A O    1 
HETATM 6800 O  O    . HOH   F 5 .   ? 13.821 -25.153 8.914   1.00 31.58 ?  494 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 44.519 10.447  -1.555  1.00 32.20 ?  495 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 28.549 -7.899  -15.296 1.00 51.95 ?  496 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 23.273 -12.815 19.346  1.00 42.23 ?  497 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 16.159 -23.344 5.795   1.00 29.92 ?  498 HOH   A O    1 
HETATM 6805 O  O    . HOH   F 5 .   ? 41.668 9.345   -4.084  1.00 31.63 ?  499 HOH   A O    1 
HETATM 6806 O  O    . HOH   F 5 .   ? 39.090 2.432   7.507   1.00 34.57 ?  500 HOH   A O    1 
HETATM 6807 O  O    . HOH   F 5 .   ? 18.348 -23.171 1.864   1.00 39.47 ?  501 HOH   A O    1 
HETATM 6808 O  O    . HOH   F 5 .   ? 40.531 -0.232  -7.789  1.00 36.65 ?  502 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? 19.962 -22.309 4.161   1.00 28.21 ?  503 HOH   A O    1 
HETATM 6810 O  O    . HOH   F 5 .   ? 28.548 -4.663  -12.312 1.00 35.53 ?  504 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 31.452 -0.554  -10.556 1.00 30.52 ?  505 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 30.730 5.770   -14.742 1.00 34.14 ?  506 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 30.715 -5.829  -11.861 1.00 49.78 ?  507 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 37.307 -6.651  7.560   1.00 26.90 ?  508 HOH   A O    1 
HETATM 6815 O  O    B HOH   F 5 .   ? 14.670 7.920   4.918   0.44 21.03 ?  509 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 22.980 -23.692 1.623   1.00 31.81 ?  510 HOH   A O    1 
HETATM 6817 O  O    B HOH   F 5 .   ? 6.797  -1.267  -3.410  0.44 43.25 ?  511 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 39.468 0.040   6.562   1.00 29.94 ?  512 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 20.409 -16.095 -7.429  1.00 27.17 ?  513 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 38.034 13.866  6.788   1.00 50.90 ?  514 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? 29.011 14.431  0.875   1.00 48.79 ?  515 HOH   A O    1 
HETATM 6822 O  O    A HOH   F 5 .   ? 8.192  -3.018  -5.685  0.56 31.02 ?  516 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 21.926 -23.978 4.462   1.00 27.38 ?  517 HOH   A O    1 
HETATM 6824 O  O    . HOH   F 5 .   ? 36.384 -6.538  10.188  1.00 47.26 ?  518 HOH   A O    1 
HETATM 6825 O  O    B HOH   F 5 .   ? 9.391  -1.649  -4.471  0.44 21.50 ?  519 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? 17.242 -6.533  -14.226 1.00 38.73 ?  520 HOH   A O    1 
HETATM 6827 O  O    T HOH   F 5 .   ? 11.865 -2.096  -3.665  0.10 5.85  ?  521 HOH   A O    1 
HETATM 6828 O  O    B HOH   F 5 .   ? 9.555  0.959   -4.973  0.44 18.83 ?  522 HOH   A O    1 
HETATM 6829 O  O    A HOH   F 5 .   ? 14.797 8.696   4.886   0.56 43.39 ?  523 HOH   A O    1 
HETATM 6830 O  O    . HOH   F 5 .   ? 24.021 9.049   -7.200  1.00 40.50 ?  524 HOH   A O    1 
HETATM 6831 O  O    . HOH   F 5 .   ? 15.844 -12.204 27.435  1.00 43.10 ?  525 HOH   A O    1 
HETATM 6832 O  O    . HOH   F 5 .   ? 16.353 -21.114 18.742  1.00 44.19 ?  526 HOH   A O    1 
HETATM 6833 O  O    . HOH   F 5 .   ? 14.667 -22.740 19.804  1.00 41.18 ?  527 HOH   A O    1 
HETATM 6834 O  O    . HOH   G 5 .   ? 29.729 -22.383 5.406   1.00 21.51 ?  201 HOH   B O    1 
HETATM 6835 O  O    . HOH   G 5 .   ? 52.798 -13.451 -20.275 1.00 33.94 ?  202 HOH   B O    1 
HETATM 6836 O  O    . HOH   G 5 .   ? 41.799 -35.998 -17.165 1.00 30.52 ?  203 HOH   B O    1 
HETATM 6837 O  O    . HOH   G 5 .   ? 48.036 -6.869  15.565  1.00 45.41 ?  204 HOH   B O    1 
HETATM 6838 O  O    . HOH   G 5 .   ? 27.633 -29.169 -1.868  1.00 39.18 ?  205 HOH   B O    1 
HETATM 6839 O  O    . HOH   G 5 .   ? 59.059 -18.778 6.788   1.00 35.15 ?  206 HOH   B O    1 
HETATM 6840 O  O    . HOH   G 5 .   ? 41.277 -7.831  5.471   1.00 39.32 ?  207 HOH   B O    1 
HETATM 6841 O  O    . HOH   G 5 .   ? 57.625 -24.483 5.046   1.00 33.96 ?  208 HOH   B O    1 
HETATM 6842 O  O    . HOH   G 5 .   ? 50.247 -3.246  7.261   1.00 37.16 ?  209 HOH   B O    1 
HETATM 6843 O  O    . HOH   G 5 .   ? 27.798 -41.812 -15.137 1.00 35.29 ?  210 HOH   B O    1 
HETATM 6844 O  O    . HOH   G 5 .   ? 37.897 -39.438 -0.180  1.00 36.83 ?  211 HOH   B O    1 
HETATM 6845 O  O    . HOH   G 5 .   ? 47.288 -7.408  -3.900  1.00 40.01 ?  212 HOH   B O    1 
HETATM 6846 O  O    . HOH   G 5 .   ? 54.406 -9.340  -8.786  1.00 19.37 ?  213 HOH   B O    1 
HETATM 6847 O  O    . HOH   G 5 .   ? 30.185 -41.013 -8.079  1.00 16.80 ?  214 HOH   B O    1 
HETATM 6848 O  O    . HOH   G 5 .   ? 56.248 -19.670 7.429   1.00 34.06 ?  215 HOH   B O    1 
HETATM 6849 O  O    . HOH   G 5 .   ? 58.139 -12.876 8.448   1.00 33.81 ?  216 HOH   B O    1 
HETATM 6850 O  O    . HOH   G 5 .   ? 56.630 -30.706 -7.778  1.00 36.32 ?  217 HOH   B O    1 
HETATM 6851 O  O    . HOH   G 5 .   ? 49.428 -22.662 -19.691 1.00 47.88 ?  218 HOH   B O    1 
HETATM 6852 O  O    . HOH   G 5 .   ? 44.368 -7.159  2.073   1.00 33.34 ?  219 HOH   B O    1 
HETATM 6853 O  O    . HOH   G 5 .   ? 50.671 -6.085  0.192   1.00 26.25 ?  220 HOH   B O    1 
HETATM 6854 O  O    . HOH   G 5 .   ? 55.318 -16.472 -14.322 1.00 35.27 ?  221 HOH   B O    1 
HETATM 6855 O  O    . HOH   G 5 .   ? 37.086 -19.757 -18.110 1.00 36.74 ?  222 HOH   B O    1 
HETATM 6856 O  O    . HOH   G 5 .   ? 34.489 -36.359 -7.191  1.00 18.25 ?  223 HOH   B O    1 
HETATM 6857 O  O    . HOH   G 5 .   ? 57.176 -26.848 -7.639  1.00 43.86 ?  224 HOH   B O    1 
HETATM 6858 O  O    . HOH   G 5 .   ? 44.923 -43.513 -10.497 1.00 27.99 ?  225 HOH   B O    1 
HETATM 6859 O  O    . HOH   G 5 .   ? 35.935 -43.229 -8.457  1.00 32.58 ?  226 HOH   B O    1 
HETATM 6860 O  O    . HOH   G 5 .   ? 29.764 -26.266 3.915   1.00 30.74 ?  227 HOH   B O    1 
HETATM 6861 O  O    . HOH   G 5 .   ? 57.366 -16.259 -12.134 1.00 18.91 ?  228 HOH   B O    1 
HETATM 6862 O  O    . HOH   G 5 .   ? 48.048 -24.497 -17.649 1.00 30.00 ?  229 HOH   B O    1 
HETATM 6863 O  O    . HOH   G 5 .   ? 45.032 -34.930 6.833   1.00 43.10 ?  230 HOH   B O    1 
HETATM 6864 O  O    . HOH   G 5 .   ? 51.619 -6.457  4.423   1.00 20.46 ?  231 HOH   B O    1 
HETATM 6865 O  O    . HOH   G 5 .   ? 51.522 -13.901 11.023  1.00 27.56 ?  232 HOH   B O    1 
HETATM 6866 O  O    . HOH   G 5 .   ? 41.485 -39.157 -14.869 1.00 22.73 ?  233 HOH   B O    1 
HETATM 6867 O  O    . HOH   G 5 .   ? 30.757 -28.731 4.255   1.00 27.31 ?  234 HOH   B O    1 
HETATM 6868 O  O    . HOH   G 5 .   ? 50.635 -12.944 -0.478  1.00 12.52 ?  235 HOH   B O    1 
HETATM 6869 O  O    . HOH   G 5 .   ? 34.824 -24.611 13.832  1.00 34.30 ?  236 HOH   B O    1 
HETATM 6870 O  O    . HOH   G 5 .   ? 39.229 -10.897 6.141   1.00 29.64 ?  237 HOH   B O    1 
HETATM 6871 O  O    . HOH   G 5 .   ? 31.712 -17.891 -14.448 1.00 33.17 ?  238 HOH   B O    1 
HETATM 6872 O  O    . HOH   G 5 .   ? 40.571 -15.999 14.154  1.00 26.20 ?  239 HOH   B O    1 
HETATM 6873 O  O    . HOH   G 5 .   ? 44.413 -27.705 -0.658  1.00 23.02 ?  240 HOH   B O    1 
HETATM 6874 O  O    . HOH   G 5 .   ? 41.274 -9.607  13.100  1.00 22.84 ?  241 HOH   B O    1 
HETATM 6875 O  O    . HOH   G 5 .   ? 46.310 -1.527  13.245  1.00 30.23 ?  242 HOH   B O    1 
HETATM 6876 O  O    . HOH   G 5 .   ? 48.484 -36.439 -15.472 1.00 44.49 ?  243 HOH   B O    1 
HETATM 6877 O  O    . HOH   G 5 .   ? 28.330 -19.704 -13.108 1.00 25.18 ?  244 HOH   B O    1 
HETATM 6878 O  O    . HOH   G 5 .   ? 42.487 -25.339 2.645   1.00 15.88 ?  245 HOH   B O    1 
HETATM 6879 O  O    . HOH   G 5 .   ? 25.375 -25.965 -1.346  1.00 32.83 ?  246 HOH   B O    1 
HETATM 6880 O  O    . HOH   G 5 .   ? 34.999 -7.989  -2.953  1.00 19.34 ?  247 HOH   B O    1 
HETATM 6881 O  O    . HOH   G 5 .   ? 32.807 -43.808 -11.302 1.00 19.81 ?  248 HOH   B O    1 
HETATM 6882 O  O    . HOH   G 5 .   ? 42.546 -22.851 3.844   1.00 12.26 ?  249 HOH   B O    1 
HETATM 6883 O  O    . HOH   G 5 .   ? 43.184 -32.383 -17.028 1.00 23.58 ?  250 HOH   B O    1 
HETATM 6884 O  O    . HOH   G 5 .   ? 34.114 -18.492 11.379  1.00 23.81 ?  251 HOH   B O    1 
HETATM 6885 O  O    . HOH   G 5 .   ? 29.785 -34.262 -0.457  1.00 36.69 ?  252 HOH   B O    1 
HETATM 6886 O  O    . HOH   G 5 .   ? 57.526 -24.352 -3.786  1.00 22.06 ?  253 HOH   B O    1 
HETATM 6887 O  O    . HOH   G 5 .   ? 50.892 -39.936 -8.126  1.00 33.10 ?  254 HOH   B O    1 
HETATM 6888 O  O    . HOH   G 5 .   ? 43.021 -43.225 -8.192  1.00 29.84 ?  255 HOH   B O    1 
HETATM 6889 O  O    . HOH   G 5 .   ? 41.782 -23.466 9.321   1.00 17.88 ?  256 HOH   B O    1 
HETATM 6890 O  O    . HOH   G 5 .   ? 27.084 -31.827 -9.954  1.00 22.76 ?  257 HOH   B O    1 
HETATM 6891 O  O    . HOH   G 5 .   ? 39.397 -11.067 0.345   1.00 17.30 ?  258 HOH   B O    1 
HETATM 6892 O  O    . HOH   G 5 .   ? 38.382 -11.034 -2.249  1.00 19.12 ?  259 HOH   B O    1 
HETATM 6893 O  O    . HOH   G 5 .   ? 29.655 -25.228 -10.823 1.00 17.03 ?  260 HOH   B O    1 
HETATM 6894 O  O    . HOH   G 5 .   ? 40.236 -12.728 -11.501 1.00 15.55 ?  261 HOH   B O    1 
HETATM 6895 O  O    . HOH   G 5 .   ? 47.908 -22.729 5.842   1.00 17.53 ?  262 HOH   B O    1 
HETATM 6896 O  O    . HOH   G 5 .   ? 43.269 -15.780 -12.164 1.00 14.64 ?  263 HOH   B O    1 
HETATM 6897 O  O    . HOH   G 5 .   ? 30.776 -15.707 2.647   1.00 14.34 ?  264 HOH   B O    1 
HETATM 6898 O  O    . HOH   G 5 .   ? 58.086 -10.606 -4.089  1.00 21.55 ?  265 HOH   B O    1 
HETATM 6899 O  O    . HOH   G 5 .   ? 38.818 -11.961 12.407  1.00 35.24 ?  266 HOH   B O    1 
HETATM 6900 O  O    . HOH   G 5 .   ? 56.109 -23.485 -14.654 1.00 27.32 ?  267 HOH   B O    1 
HETATM 6901 O  O    . HOH   G 5 .   ? 49.255 -28.654 -6.853  1.00 15.73 ?  268 HOH   B O    1 
HETATM 6902 O  O    . HOH   G 5 .   ? 42.247 -9.861  9.404   1.00 22.20 ?  269 HOH   B O    1 
HETATM 6903 O  O    . HOH   G 5 .   ? 28.223 -34.349 -9.430  1.00 21.76 ?  270 HOH   B O    1 
HETATM 6904 O  O    . HOH   G 5 .   ? 49.653 -0.476  10.279  1.00 29.58 ?  271 HOH   B O    1 
HETATM 6905 O  O    . HOH   G 5 .   ? 57.410 -9.184  1.430   1.00 19.94 ?  272 HOH   B O    1 
HETATM 6906 O  O    . HOH   G 5 .   ? 42.291 -34.667 3.754   1.00 27.62 ?  273 HOH   B O    1 
HETATM 6907 O  O    . HOH   G 5 .   ? 30.577 -42.189 -10.601 1.00 30.15 ?  274 HOH   B O    1 
HETATM 6908 O  O    . HOH   G 5 .   ? 56.833 -8.629  8.494   1.00 19.25 ?  275 HOH   B O    1 
HETATM 6909 O  O    . HOH   G 5 .   ? 59.697 -15.263 8.155   1.00 33.63 ?  276 HOH   B O    1 
HETATM 6910 O  O    . HOH   G 5 .   ? 34.903 -33.369 -19.183 1.00 31.09 ?  277 HOH   B O    1 
HETATM 6911 O  O    . HOH   G 5 .   ? 28.425 -30.837 -14.698 1.00 31.30 ?  278 HOH   B O    1 
HETATM 6912 O  O    . HOH   G 5 .   ? 27.887 -22.878 -8.019  1.00 18.44 ?  279 HOH   B O    1 
HETATM 6913 O  O    . HOH   G 5 .   ? 49.863 -24.676 5.784   1.00 33.25 ?  280 HOH   B O    1 
HETATM 6914 O  O    . HOH   G 5 .   ? 27.559 -26.720 -15.625 1.00 32.40 ?  281 HOH   B O    1 
HETATM 6915 O  O    . HOH   G 5 .   ? 56.982 -12.129 12.411  1.00 40.12 ?  282 HOH   B O    1 
HETATM 6916 O  O    . HOH   G 5 .   ? 52.475 -10.381 13.007  1.00 22.63 ?  283 HOH   B O    1 
HETATM 6917 O  O    . HOH   G 5 .   ? 46.560 -31.223 -4.732  1.00 21.34 ?  284 HOH   B O    1 
HETATM 6918 O  O    . HOH   G 5 .   ? 48.322 -25.020 3.110   1.00 13.56 ?  285 HOH   B O    1 
HETATM 6919 O  O    . HOH   G 5 .   ? 33.456 -15.299 -13.954 1.00 22.03 ?  286 HOH   B O    1 
HETATM 6920 O  O    . HOH   G 5 .   ? 42.886 -20.315 -20.786 1.00 38.04 ?  287 HOH   B O    1 
HETATM 6921 O  O    . HOH   G 5 .   ? 34.361 -12.729 2.628   1.00 25.33 ?  288 HOH   B O    1 
HETATM 6922 O  O    . HOH   G 5 .   ? 36.703 -12.748 -1.495  1.00 26.64 ?  289 HOH   B O    1 
HETATM 6923 O  O    . HOH   G 5 .   ? 47.023 -33.946 -4.574  1.00 17.53 ?  290 HOH   B O    1 
HETATM 6924 O  O    . HOH   G 5 .   ? 46.786 -29.480 9.852   1.00 32.76 ?  291 HOH   B O    1 
HETATM 6925 O  O    . HOH   G 5 .   ? 37.425 -18.163 13.084  1.00 30.46 ?  292 HOH   B O    1 
HETATM 6926 O  O    . HOH   G 5 .   ? 51.201 -37.597 -9.497  1.00 27.43 ?  293 HOH   B O    1 
HETATM 6927 O  O    . HOH   G 5 .   ? 45.313 -33.371 -15.894 1.00 23.23 ?  294 HOH   B O    1 
HETATM 6928 O  O    . HOH   G 5 .   ? 42.237 -9.915  -14.886 1.00 42.77 ?  295 HOH   B O    1 
HETATM 6929 O  O    . HOH   G 5 .   ? 37.278 -35.645 7.212   1.00 34.78 ?  296 HOH   B O    1 
HETATM 6930 O  O    . HOH   G 5 .   ? 48.611 -20.015 5.952   1.00 14.78 ?  297 HOH   B O    1 
HETATM 6931 O  O    . HOH   G 5 .   ? 43.461 -15.376 18.250  1.00 32.21 ?  298 HOH   B O    1 
HETATM 6932 O  O    . HOH   G 5 .   ? 44.535 -27.420 2.026   1.00 15.54 ?  299 HOH   B O    1 
HETATM 6933 O  O    . HOH   G 5 .   ? 42.597 -12.331 -18.528 1.00 31.09 ?  300 HOH   B O    1 
HETATM 6934 O  O    . HOH   G 5 .   ? 57.604 -22.079 3.101   1.00 27.46 ?  301 HOH   B O    1 
HETATM 6935 O  O    . HOH   G 5 .   ? 52.545 -35.640 -8.520  1.00 30.11 ?  302 HOH   B O    1 
HETATM 6936 O  O    . HOH   G 5 .   ? 53.114 -16.082 -12.687 1.00 29.65 ?  303 HOH   B O    1 
HETATM 6937 O  O    . HOH   G 5 .   ? 43.951 -29.331 -4.662  1.00 24.59 ?  304 HOH   B O    1 
HETATM 6938 O  O    . HOH   G 5 .   ? 51.325 -32.905 -10.641 1.00 39.14 ?  305 HOH   B O    1 
HETATM 6939 O  O    . HOH   G 5 .   ? 41.084 -5.441  11.484  1.00 50.53 ?  306 HOH   B O    1 
HETATM 6940 O  O    . HOH   G 5 .   ? 53.418 -30.152 4.529   1.00 18.78 ?  307 HOH   B O    1 
HETATM 6941 O  O    . HOH   G 5 .   ? 40.164 -10.815 -9.555  1.00 17.40 ?  308 HOH   B O    1 
HETATM 6942 O  O    . HOH   G 5 .   ? 25.889 -21.458 -3.542  1.00 17.00 ?  309 HOH   B O    1 
HETATM 6943 O  O    . HOH   G 5 .   ? 62.607 -13.558 4.779   1.00 29.14 ?  310 HOH   B O    1 
HETATM 6944 O  O    . HOH   G 5 .   ? 45.835 -40.365 -3.492  1.00 30.38 ?  311 HOH   B O    1 
HETATM 6945 O  O    . HOH   G 5 .   ? 37.764 -10.243 -10.783 1.00 18.03 ?  312 HOH   B O    1 
HETATM 6946 O  O    . HOH   G 5 .   ? 41.643 -8.059  1.360   1.00 26.60 ?  313 HOH   B O    1 
HETATM 6947 O  O    . HOH   G 5 .   ? 53.580 -12.565 -22.191 1.00 36.18 ?  314 HOH   B O    1 
HETATM 6948 O  O    . HOH   G 5 .   ? 43.109 -21.390 10.683  1.00 16.70 ?  315 HOH   B O    1 
HETATM 6949 O  O    . HOH   G 5 .   ? 32.758 -34.567 -5.921  1.00 16.87 ?  316 HOH   B O    1 
HETATM 6950 O  O    . HOH   G 5 .   ? 34.903 -33.486 4.494   1.00 29.66 ?  317 HOH   B O    1 
HETATM 6951 O  O    . HOH   G 5 .   ? 26.258 -20.996 -6.229  1.00 17.70 ?  318 HOH   B O    1 
HETATM 6952 O  O    . HOH   G 5 .   ? 52.480 -29.190 -13.021 1.00 25.19 ?  319 HOH   B O    1 
HETATM 6953 O  O    . HOH   G 5 .   ? 59.901 -17.135 -10.436 1.00 34.44 ?  320 HOH   B O    1 
HETATM 6954 O  O    . HOH   G 5 .   ? 48.093 -32.600 -16.591 1.00 42.92 ?  321 HOH   B O    1 
HETATM 6955 O  O    . HOH   G 5 .   ? 37.165 -30.562 -21.022 1.00 30.98 ?  322 HOH   B O    1 
HETATM 6956 O  O    . HOH   G 5 .   ? 38.253 -12.751 7.897   1.00 19.42 ?  323 HOH   B O    1 
HETATM 6957 O  O    . HOH   G 5 .   ? 27.932 -14.784 -9.398  1.00 32.99 ?  324 HOH   B O    1 
HETATM 6958 O  O    . HOH   G 5 .   ? 44.516 -24.584 9.598   1.00 19.75 ?  325 HOH   B O    1 
HETATM 6959 O  O    . HOH   G 5 .   ? 36.645 -12.400 4.255   1.00 17.94 ?  326 HOH   B O    1 
HETATM 6960 O  O    . HOH   G 5 .   ? 62.789 -20.081 -0.717  1.00 38.20 ?  327 HOH   B O    1 
HETATM 6961 O  O    . HOH   G 5 .   ? 38.276 -9.349  -13.257 1.00 27.65 ?  328 HOH   B O    1 
HETATM 6962 O  O    . HOH   G 5 .   ? 41.158 -24.476 15.828  1.00 43.60 ?  329 HOH   B O    1 
HETATM 6963 O  O    . HOH   G 5 .   ? 51.673 -6.000  -7.897  1.00 52.33 ?  330 HOH   B O    1 
HETATM 6964 O  O    . HOH   G 5 .   ? 44.073 -1.716  7.651   1.00 46.45 ?  331 HOH   B O    1 
HETATM 6965 O  O    . HOH   G 5 .   ? 47.067 -24.456 8.185   1.00 26.62 ?  332 HOH   B O    1 
HETATM 6966 O  O    . HOH   G 5 .   ? 43.052 -34.628 0.129   1.00 20.02 ?  333 HOH   B O    1 
HETATM 6967 O  O    . HOH   G 5 .   ? 33.473 -31.191 11.074  1.00 33.82 ?  334 HOH   B O    1 
HETATM 6968 O  O    . HOH   G 5 .   ? 48.502 -11.927 -13.907 1.00 27.15 ?  335 HOH   B O    1 
HETATM 6969 O  O    . HOH   G 5 .   ? 47.394 -27.394 2.042   1.00 14.98 ?  336 HOH   B O    1 
HETATM 6970 O  O    . HOH   G 5 .   ? 42.834 -43.507 -14.333 1.00 40.83 ?  337 HOH   B O    1 
HETATM 6971 O  O    . HOH   G 5 .   ? 46.785 -19.848 12.269  1.00 29.64 ?  338 HOH   B O    1 
HETATM 6972 O  O    . HOH   G 5 .   ? 36.962 -15.109 -16.521 1.00 42.17 ?  339 HOH   B O    1 
HETATM 6973 O  O    . HOH   G 5 .   ? 45.646 -36.231 -16.057 1.00 34.60 ?  340 HOH   B O    1 
HETATM 6974 O  O    . HOH   G 5 .   ? 39.442 -23.590 -20.304 1.00 38.45 ?  341 HOH   B O    1 
HETATM 6975 O  O    . HOH   G 5 .   ? 28.855 -42.926 -12.381 1.00 41.63 ?  342 HOH   B O    1 
HETATM 6976 O  O    . HOH   G 5 .   ? 38.422 -12.223 -16.236 1.00 42.62 ?  343 HOH   B O    1 
HETATM 6977 O  O    . HOH   G 5 .   ? 32.924 -14.676 1.059   1.00 19.73 ?  344 HOH   B O    1 
HETATM 6978 O  O    . HOH   G 5 .   ? 37.019 -45.292 -9.688  1.00 37.80 ?  345 HOH   B O    1 
HETATM 6979 O  O    . HOH   G 5 .   ? 38.519 -22.362 15.030  1.00 41.46 ?  346 HOH   B O    1 
HETATM 6980 O  O    . HOH   G 5 .   ? 39.765 -44.290 -11.210 1.00 37.96 ?  347 HOH   B O    1 
HETATM 6981 O  O    . HOH   G 5 .   ? 40.375 -43.467 -9.076  1.00 27.46 ?  348 HOH   B O    1 
HETATM 6982 O  O    . HOH   G 5 .   ? 27.706 -26.559 -0.556  1.00 31.47 ?  349 HOH   B O    1 
HETATM 6983 O  O    . HOH   G 5 .   ? 33.674 -9.326  -8.855  1.00 33.30 ?  350 HOH   B O    1 
HETATM 6984 O  O    . HOH   G 5 .   ? 62.460 -20.097 -4.803  1.00 44.41 ?  351 HOH   B O    1 
HETATM 6985 O  O    . HOH   G 5 .   ? 44.146 -37.322 -17.695 1.00 34.11 ?  352 HOH   B O    1 
HETATM 6986 O  O    . HOH   G 5 .   ? 34.539 -10.297 7.556   1.00 23.91 ?  353 HOH   B O    1 
HETATM 6987 O  O    . HOH   G 5 .   ? 36.012 -8.568  -9.670  1.00 32.49 ?  354 HOH   B O    1 
HETATM 6988 O  O    . HOH   G 5 .   ? 55.583 -8.278  10.901  1.00 26.88 ?  355 HOH   B O    1 
HETATM 6989 O  O    . HOH   G 5 .   ? 23.096 -23.594 6.792   1.00 37.93 ?  356 HOH   B O    1 
HETATM 6990 O  O    . HOH   G 5 .   ? 56.471 -7.237  3.133   1.00 27.08 ?  357 HOH   B O    1 
HETATM 6991 O  O    . HOH   G 5 .   ? 43.122 -12.662 -21.188 1.00 42.78 ?  358 HOH   B O    1 
HETATM 6992 O  O    . HOH   G 5 .   ? 34.041 -7.736  11.429  1.00 39.56 ?  359 HOH   B O    1 
HETATM 6993 O  O    . HOH   G 5 .   ? 61.448 -19.839 1.645   1.00 36.18 ?  360 HOH   B O    1 
HETATM 6994 O  O    . HOH   G 5 .   ? 56.897 -21.505 -16.368 1.00 41.15 ?  361 HOH   B O    1 
HETATM 6995 O  O    . HOH   G 5 .   ? 40.194 -8.829  9.936   1.00 42.17 ?  362 HOH   B O    1 
HETATM 6996 O  O    . HOH   G 5 .   ? 27.062 -25.949 -11.424 1.00 33.33 ?  363 HOH   B O    1 
HETATM 6997 O  O    . HOH   G 5 .   ? 54.075 -5.690  3.096   1.00 33.62 ?  364 HOH   B O    1 
HETATM 6998 O  O    . HOH   G 5 .   ? 32.400 -23.596 14.089  1.00 40.07 ?  365 HOH   B O    1 
HETATM 6999 O  O    . HOH   G 5 .   ? 36.107 -8.669  9.030   1.00 36.56 ?  366 HOH   B O    1 
HETATM 7000 O  O    . HOH   G 5 .   ? 41.781 -10.087 -17.408 1.00 53.52 ?  367 HOH   B O    1 
HETATM 7001 O  O    . HOH   G 5 .   ? 48.293 -26.526 8.824   1.00 41.11 ?  368 HOH   B O    1 
HETATM 7002 O  O    . HOH   G 5 .   ? 40.003 -11.370 -13.947 1.00 30.77 ?  369 HOH   B O    1 
HETATM 7003 O  O    . HOH   G 5 .   ? 39.801 -6.982  7.839   1.00 42.55 ?  370 HOH   B O    1 
HETATM 7004 O  O    . HOH   G 5 .   ? 58.904 -10.385 9.252   1.00 36.59 ?  371 HOH   B O    1 
HETATM 7005 O  O    . HOH   G 5 .   ? 55.947 -7.768  -0.599  1.00 34.61 ?  372 HOH   B O    1 
HETATM 7006 O  O    . HOH   G 5 .   ? 51.976 -12.908 13.368  1.00 33.86 ?  373 HOH   B O    1 
HETATM 7007 O  O    . HOH   G 5 .   ? 37.994 -10.582 10.021  1.00 30.61 ?  374 HOH   B O    1 
HETATM 7008 O  O    . HOH   G 5 .   ? 62.926 -12.332 6.963   1.00 36.86 ?  375 HOH   B O    1 
HETATM 7009 O  O    . HOH   G 5 .   ? 44.122 -5.567  -3.503  1.00 43.78 ?  376 HOH   B O    1 
HETATM 7010 O  O    . HOH   G 5 .   ? 41.775 -6.712  -4.786  1.00 48.61 ?  377 HOH   B O    1 
HETATM 7011 O  O    . HOH   G 5 .   ? 42.627 -17.165 -23.159 1.00 44.38 ?  378 HOH   B O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 36.431 -22.753 13.287  1.00 26.37 ?  379 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 39.631 -14.064 15.671  1.00 51.66 ?  380 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 40.003 -7.585  3.224   1.00 34.73 ?  381 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 52.796 -29.857 7.189   1.00 24.75 ?  382 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 60.409 -22.245 2.851   1.00 48.97 ?  383 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 40.876 -9.849  15.811  1.00 43.81 ?  384 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 46.641 -5.374  2.956   1.00 42.17 ?  385 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 25.747 -18.823 -11.934 1.00 40.80 ?  386 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 35.218 -20.279 13.255  1.00 31.20 ?  387 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 23.850 -20.841 -7.662  1.00 29.61 ?  388 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 35.219 -33.741 7.273   1.00 40.16 ?  389 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 40.646 -6.609  -0.899  1.00 24.05 ?  390 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 44.032 -31.758 -3.776  1.00 35.36 ?  391 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 26.598 -27.986 -13.517 1.00 34.91 ?  392 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 27.788 -27.069 2.144   1.00 30.74 ?  393 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 34.269 -33.411 9.601   1.00 33.39 ?  394 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 24.602 -20.652 -10.550 1.00 39.27 ?  395 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 50.579 -30.742 8.721   1.00 28.23 ?  396 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 26.806 -30.654 -12.579 1.00 28.81 ?  397 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 45.645 -20.291 15.202  1.00 54.83 ?  398 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 57.536 -6.457  -2.329  1.00 33.59 ?  399 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 40.950 -11.765 -22.331 1.00 41.10 ?  400 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   . VAL   A 3   ? 0.6285 0.6393 0.7128 -0.0198 -0.0505 0.1032  3   VAL   A N   
2    C  CA  . VAL   A 3   ? 0.6257 0.6363 0.6926 -0.0224 -0.0485 0.1051  3   VAL   A CA  
3    C  C   . VAL   A 3   ? 0.6069 0.6228 0.6445 -0.0319 -0.0479 0.1166  3   VAL   A C   
4    O  O   . VAL   A 3   ? 0.6095 0.6251 0.6608 -0.0297 -0.0521 0.1204  3   VAL   A O   
5    C  CB  . VAL   A 3   ? 0.6380 0.6444 0.7071 -0.0177 -0.0470 0.0959  3   VAL   A CB  
6    C  CG1 . VAL   A 3   ? 0.6427 0.6471 0.7084 -0.0151 -0.0471 0.0927  3   VAL   A CG1 
7    C  CG2 . VAL   A 3   ? 0.6420 0.6481 0.7089 -0.0167 -0.0463 0.0930  3   VAL   A CG2 
16   N  N   . ASN   A 4   ? 0.5807 0.6035 0.5674 -0.0439 -0.0439 0.1239  4   ASN   A N   
17   C  CA  . ASN   A 4   ? 0.5518 0.5817 0.4837 -0.0576 -0.0399 0.1287  4   ASN   A CA  
18   C  C   . ASN   A 4   ? 0.5105 0.5575 0.4300 -0.0719 -0.0302 0.1018  4   ASN   A C   
19   O  O   . ASN   A 4   ? 0.5102 0.5576 0.4201 -0.0731 -0.0303 0.1053  4   ASN   A O   
20   C  CB  . ASN   A 4   ? 0.5604 0.5823 0.4455 -0.0582 -0.0447 0.1591  4   ASN   A CB  
21   C  CG  . ASN   A 4   ? 0.5651 0.5800 0.4080 -0.0601 -0.0484 0.1873  4   ASN   A CG  
22   O  OD1 . ASN   A 4   ? 0.5681 0.5781 0.3932 -0.0608 -0.0513 0.1970  4   ASN   A OD1 
23   N  ND2 . ASN   A 4   ? 0.5650 0.5787 0.3974 -0.0601 -0.0490 0.1987  4   ASN   A ND2 
30   N  N   . SER   A 5   ? 0.4665 0.5287 0.3847 -0.0868 -0.0220 0.0713  5   SER   A N   
31   C  CA  . SER   A 5   ? 0.4204 0.4985 0.3481 -0.0997 -0.0100 0.0376  5   SER   A CA  
32   C  C   . SER   A 5   ? 0.3740 0.4611 0.2998 -0.1029 0.0010  0.0181  5   SER   A C   
33   O  O   . SER   A 5   ? 0.3770 0.4669 0.2906 -0.0964 -0.0041 0.0038  5   SER   A O   
34   C  CB  . SER   A 5   ? 0.4260 0.5068 0.3785 -0.1056 -0.0085 0.0250  5   SER   A CB  
35   O  OG  . SER   A 5   ? 0.4303 0.5113 0.3956 -0.1099 -0.0058 0.0179  5   SER   A OG  
41   N  N   . PHE   A 6   ? 0.3225 0.4157 0.2501 -0.1105 0.0163  0.0202  6   PHE   A N   
42   C  CA  . PHE   A 6   ? 0.2766 0.3699 0.2144 -0.1095 0.0211  0.0273  6   PHE   A CA  
43   C  C   . PHE   A 6   ? 0.2725 0.3570 0.2320 -0.1063 0.0443  0.0211  6   PHE   A C   
44   O  O   . PHE   A 6   ? 0.2816 0.3599 0.2620 -0.1100 0.0499  0.0404  6   PHE   A O   
45   C  CB  . PHE   A 6   ? 0.2544 0.3364 0.1845 -0.0979 0.0080  0.0468  6   PHE   A CB  
46   C  CG  . PHE   A 6   ? 0.2372 0.3082 0.1807 -0.0845 0.0070  0.0503  6   PHE   A CG  
47   C  CD1 . PHE   A 6   ? 0.2272 0.2955 0.1837 -0.0719 0.0012  0.0502  6   PHE   A CD1 
48   C  CD2 . PHE   A 6   ? 0.2461 0.3004 0.2072 -0.0674 0.0104  0.0473  6   PHE   A CD2 
49   C  CE1 . PHE   A 6   ? 0.2275 0.2856 0.1940 -0.0674 0.0118  0.0511  6   PHE   A CE1 
50   C  CE2 . PHE   A 6   ? 0.2437 0.2937 0.2231 -0.0592 0.0060  0.0384  6   PHE   A CE2 
51   C  CZ  . PHE   A 6   ? 0.2332 0.2861 0.2033 -0.0640 0.0029  0.0385  6   PHE   A CZ  
61   N  N   A SER   A 7   ? 0.2664 0.3489 0.2316 -0.1018 0.0510  0.0151  7   SER   A N   
62   N  N   B SER   A 7   ? 0.2688 0.3458 0.2349 -0.0992 0.0527  0.0134  7   SER   A N   
63   C  CA  A SER   A 7   ? 0.2625 0.3397 0.2437 -0.0914 0.0529  0.0020  7   SER   A CA  
64   C  CA  B SER   A 7   ? 0.2673 0.3335 0.2460 -0.0877 0.0577  0.0019  7   SER   A CA  
65   C  C   A SER   A 7   ? 0.2437 0.3055 0.2069 -0.0834 0.0543  0.0074  7   SER   A C   
66   C  C   B SER   A 7   ? 0.2499 0.3092 0.2189 -0.0751 0.0629  0.0097  7   SER   A C   
67   O  O   A SER   A 7   ? 0.2536 0.3002 0.2093 -0.0880 0.0494  0.0141  7   SER   A O   
68   O  O   B SER   A 7   ? 0.2577 0.3046 0.2202 -0.0770 0.0585  0.0097  7   SER   A O   
69   C  CB  A SER   A 7   ? 0.2792 0.3601 0.2825 -0.0850 0.0552  -0.0025 7   SER   A CB  
70   C  CB  B SER   A 7   ? 0.2825 0.3412 0.2732 -0.0870 0.0603  -0.0056 7   SER   A CB  
71   O  OG  A SER   A 7   ? 0.2946 0.3725 0.3135 -0.0782 0.0536  -0.0064 7   SER   A OG  
72   O  OG  B SER   A 7   ? 0.2941 0.3459 0.2975 -0.0876 0.0606  -0.0110 7   SER   A OG  
83   N  N   A GLY   A 8   ? 0.2207 0.2781 0.1813 -0.0688 0.0472  -0.0044 8   GLY   A N   
84   N  N   B GLY   A 8   ? 0.2277 0.2894 0.2022 -0.0610 0.0616  0.0120  8   GLY   A N   
85   C  CA  A GLY   A 8   ? 0.2040 0.2520 0.1754 -0.0473 0.0471  -0.0048 8   GLY   A CA  
86   C  CA  B GLY   A 8   ? 0.2126 0.2671 0.1999 -0.0477 0.0480  0.0184  8   GLY   A CA  
87   C  C   A GLY   A 8   ? 0.1825 0.2290 0.1713 -0.0292 0.0408  -0.0028 8   GLY   A C   
88   C  C   B GLY   A 8   ? 0.1874 0.2461 0.1826 -0.0355 0.0428  0.0242  8   GLY   A C   
89   O  O   A GLY   A 8   ? 0.1848 0.2331 0.1797 -0.0153 0.0476  -0.0121 8   GLY   A O   
90   O  O   B GLY   A 8   ? 0.1875 0.2501 0.1874 -0.0243 0.0442  0.0169  8   GLY   A O   
97   N  N   A TYR   A 9   ? 0.1676 0.2071 0.1717 -0.0218 0.0326  0.0039  9   TYR   A N   
98   N  N   B TYR   A 9   ? 0.1704 0.2269 0.1799 -0.0301 0.0334  0.0319  9   TYR   A N   
99   C  CA  A TYR   A 9   ? 0.1562 0.1853 0.1613 -0.0198 0.0203  0.0094  9   TYR   A CA  
100  C  CA  B TYR   A 9   ? 0.1595 0.2073 0.1673 -0.0234 0.0239  0.0350  9   TYR   A CA  
101  C  C   A TYR   A 9   ? 0.1551 0.1750 0.1553 -0.0149 0.0207  0.0267  9   TYR   A C   
102  C  C   B TYR   A 9   ? 0.1582 0.1925 0.1638 -0.0148 0.0270  0.0389  9   TYR   A C   
103  O  O   A TYR   A 9   ? 0.1738 0.1875 0.1719 -0.0224 0.0074  0.0287  9   TYR   A O   
104  O  O   B TYR   A 9   ? 0.1679 0.2094 0.1887 -0.0248 0.0108  0.0409  9   TYR   A O   
105  C  CB  A TYR   A 9   ? 0.1546 0.1821 0.1648 -0.0204 0.0276  0.0024  9   TYR   A CB  
106  C  CB  B TYR   A 9   ? 0.1591 0.2077 0.1706 -0.0213 0.0155  0.0313  9   TYR   A CB  
107  C  CG  A TYR   A 9   ? 0.1563 0.1755 0.1741 -0.0080 0.0322  -0.0062 9   TYR   A CG  
108  C  CG  B TYR   A 9   ? 0.1586 0.2059 0.1721 -0.0180 0.0133  0.0220  9   TYR   A CG  
109  C  CD1 A TYR   A 9   ? 0.1585 0.1705 0.1720 -0.0128 0.0360  -0.0158 9   TYR   A CD1 
110  C  CD1 B TYR   A 9   ? 0.1639 0.2060 0.1772 -0.0194 0.0191  0.0185  9   TYR   A CD1 
111  C  CD2 A TYR   A 9   ? 0.1594 0.1701 0.1842 -0.0068 0.0281  -0.0018 9   TYR   A CD2 
112  C  CD2 B TYR   A 9   ? 0.1523 0.2034 0.1642 -0.0163 0.0114  0.0212  9   TYR   A CD2 
113  C  CE1 A TYR   A 9   ? 0.1644 0.1753 0.1899 -0.0130 0.0406  -0.0244 9   TYR   A CE1 
114  C  CE1 B TYR   A 9   ? 0.1616 0.1989 0.1742 -0.0213 0.0271  0.0161  9   TYR   A CE1 
115  C  CE2 A TYR   A 9   ? 0.1603 0.1758 0.1886 -0.0116 0.0320  -0.0084 9   TYR   A CE2 
116  C  CE2 B TYR   A 9   ? 0.1513 0.1996 0.1532 -0.0130 0.0199  0.0194  9   TYR   A CE2 
117  C  CZ  A TYR   A 9   ? 0.1604 0.1781 0.2001 -0.0198 0.0477  -0.0133 9   TYR   A CZ  
118  C  CZ  B TYR   A 9   ? 0.1514 0.1949 0.1679 -0.0179 0.0352  0.0136  9   TYR   A CZ  
119  O  OH  A TYR   A 9   ? 0.1712 0.1834 0.2255 -0.0271 0.0477  -0.0173 9   TYR   A OH  
120  O  OH  B TYR   A 9   ? 0.1504 0.1936 0.1890 -0.0232 0.0416  0.0114  9   TYR   A OH  
139  N  N   A LEU   A 10  ? 0.1491 0.1604 0.1644 -0.0085 0.0212  0.0194  10  LEU   A N   
140  N  N   B LEU   A 10  ? 0.1558 0.1726 0.1567 -0.0036 0.0317  0.0313  10  LEU   A N   
141  C  CA  A LEU   A 10  ? 0.1386 0.1552 0.1797 -0.0097 0.0229  0.0265  10  LEU   A CA  
142  C  CA  B LEU   A 10  ? 0.1485 0.1597 0.1636 -0.0066 0.0278  0.0310  10  LEU   A CA  
143  C  C   A LEU   A 10  ? 0.1378 0.1464 0.1929 -0.0069 0.0287  0.0264  10  LEU   A C   
144  C  C   B LEU   A 10  ? 0.1462 0.1465 0.1585 -0.0117 0.0253  0.0317  10  LEU   A C   
145  O  O   A LEU   A 10  ? 0.1447 0.1442 0.2089 -0.0060 0.0451  0.0247  10  LEU   A O   
146  O  O   B LEU   A 10  ? 0.1445 0.1358 0.1680 -0.0090 0.0369  0.0354  10  LEU   A O   
147  C  CB  A LEU   A 10  ? 0.1391 0.1662 0.2172 -0.0115 0.0182  0.0334  10  LEU   A CB  
148  C  CB  B LEU   A 10  ? 0.1463 0.1573 0.1919 -0.0050 0.0101  0.0378  10  LEU   A CB  
149  C  CG  A LEU   A 10  ? 0.1628 0.1780 0.2768 -0.0045 -0.0054 0.0452  10  LEU   A CG  
150  C  CG  B LEU   A 10  ? 0.1511 0.1666 0.2318 -0.0051 -0.0185 0.0415  10  LEU   A CG  
151  C  CD1 A LEU   A 10  ? 0.1777 0.1934 0.3001 -0.0088 -0.0075 0.0571  10  LEU   A CD1 
152  C  CD1 B LEU   A 10  ? 0.1621 0.1838 0.2664 -0.0161 -0.0104 0.0477  10  LEU   A CD1 
153  C  CD2 A LEU   A 10  ? 0.1754 0.1872 0.2961 0.0094  0.0104  0.0333  10  LEU   A CD2 
154  C  CD2 B LEU   A 10  ? 0.1612 0.1735 0.2463 0.0033  -0.0296 0.0418  10  LEU   A CD2 
177  N  N   A LYS   A 11  ? 0.1412 0.1442 0.1939 -0.0080 0.0213  0.0259  11  LYS   A N   
178  N  N   B LYS   A 11  ? 0.1526 0.1470 0.1567 -0.0172 0.0118  0.0358  11  LYS   A N   
179  C  CA  A LYS   A 11  ? 0.1475 0.1437 0.2069 -0.0184 0.0211  0.0207  11  LYS   A CA  
180  C  CA  B LYS   A 11  ? 0.1592 0.1437 0.1578 -0.0269 0.0027  0.0314  11  LYS   A CA  
181  C  C   A LYS   A 11  ? 0.1428 0.1534 0.2131 -0.0190 0.0280  0.0060  11  LYS   A C   
182  C  C   B LYS   A 11  ? 0.1452 0.1350 0.1678 -0.0293 -0.0009 0.0253  11  LYS   A C   
183  O  O   A LYS   A 11  ? 0.1483 0.1709 0.2517 -0.0431 0.0402  -0.0108 11  LYS   A O   
184  O  O   B LYS   A 11  ? 0.1417 0.1297 0.2006 -0.0254 -0.0030 0.0134  11  LYS   A O   
185  C  CB  A LYS   A 11  ? 0.1586 0.1434 0.2115 -0.0152 0.0155  0.0239  11  LYS   A CB  
186  C  CB  B LYS   A 11  ? 0.1756 0.1392 0.1462 -0.0301 -0.0044 0.0241  11  LYS   A CB  
187  C  CG  A LYS   A 11  ? 0.1713 0.1410 0.2214 -0.0135 0.0133  0.0248  11  LYS   A CG  
188  C  CG  B LYS   A 11  ? 0.1886 0.1402 0.1451 -0.0340 -0.0049 0.0343  11  LYS   A CG  
189  C  CD  A LYS   A 11  ? 0.1867 0.1462 0.2357 -0.0077 0.0112  0.0264  11  LYS   A CD  
190  C  CD  B LYS   A 11  ? 0.2024 0.1483 0.1479 -0.0288 -0.0010 0.0373  11  LYS   A CD  
191  C  CE  A LYS   A 11  ? 0.1966 0.1508 0.2365 -0.0030 0.0099  0.0281  11  LYS   A CE  
192  C  CE  B LYS   A 11  ? 0.2082 0.1534 0.1405 -0.0251 0.0001  0.0444  11  LYS   A CE  
193  N  NZ  A LYS   A 11  ? 0.1943 0.1522 0.2349 0.0058  0.0130  0.0194  11  LYS   A NZ  
194  N  NZ  B LYS   A 11  ? 0.2097 0.1617 0.1442 -0.0222 -0.0042 0.0408  11  LYS   A NZ  
221  N  N   A LEU   A 12  ? 0.1375 0.1448 0.1872 -0.0193 0.0288  0.0137  12  LEU   A N   
222  N  N   B LEU   A 12  ? 0.1406 0.1473 0.1619 -0.0240 -0.0044 0.0185  12  LEU   A N   
223  C  CA  A LEU   A 12  ? 0.1463 0.1538 0.1811 -0.0189 0.0116  0.0209  12  LEU   A CA  
224  C  CA  B LEU   A 12  ? 0.1385 0.1570 0.1628 -0.0210 0.0002  0.0246  12  LEU   A CA  
225  C  C   A LEU   A 12  ? 0.1525 0.1466 0.1810 -0.0252 0.0122  0.0213  12  LEU   A C   
226  C  C   B LEU   A 12  ? 0.1415 0.1619 0.1549 -0.0187 0.0090  0.0282  12  LEU   A C   
227  O  O   A LEU   A 12  ? 0.1555 0.1554 0.1700 -0.0230 0.0223  0.0044  12  LEU   A O   
228  O  O   B LEU   A 12  ? 0.1488 0.1668 0.1541 -0.0105 0.0122  0.0166  12  LEU   A O   
229  C  CB  A LEU   A 12  ? 0.1578 0.1573 0.1808 -0.0152 0.0022  0.0237  12  LEU   A CB  
230  C  CB  B LEU   A 12  ? 0.1461 0.1633 0.1842 -0.0178 0.0051  0.0343  12  LEU   A CB  
231  C  CG  A LEU   A 12  ? 0.1723 0.1702 0.1990 -0.0071 0.0079  0.0271  12  LEU   A CG  
232  C  CG  B LEU   A 12  ? 0.1480 0.1688 0.2046 -0.0152 0.0142  0.0424  12  LEU   A CG  
233  C  CD1 A LEU   A 12  ? 0.1822 0.1808 0.2109 -0.0011 0.0093  0.0426  12  LEU   A CD1 
234  C  CD1 B LEU   A 12  ? 0.1510 0.1809 0.2216 -0.0077 0.0214  0.0554  12  LEU   A CD1 
235  C  CD2 A LEU   A 12  ? 0.1747 0.1759 0.2106 -0.0068 0.0075  0.0212  12  LEU   A CD2 
236  C  CD2 B LEU   A 12  ? 0.1419 0.1715 0.2012 -0.0123 0.0226  0.0266  12  LEU   A CD2 
259  N  N   A THR   A 13  ? 0.1491 0.1371 0.2045 -0.0246 0.0048  0.0202  13  THR   A N   
260  N  N   B THR   A 13  ? 0.1378 0.1563 0.1628 -0.0205 -0.0000 0.0272  13  THR   A N   
261  C  CA  A THR   A 13  ? 0.1518 0.1446 0.2017 -0.0170 0.0188  0.0187  13  THR   A CA  
262  C  CA  B THR   A 13  ? 0.1371 0.1580 0.1680 -0.0277 0.0060  0.0287  13  THR   A CA  
263  C  C   A THR   A 13  ? 0.1525 0.1402 0.2008 -0.0139 0.0091  0.0279  13  THR   A C   
264  C  C   B THR   A 13  ? 0.1436 0.1586 0.1824 -0.0263 0.0063  0.0292  13  THR   A C   
265  O  O   A THR   A 13  ? 0.1554 0.1452 0.1954 -0.0007 0.0090  0.0240  13  THR   A O   
266  O  O   B THR   A 13  ? 0.1497 0.1618 0.1901 -0.0316 -0.0094 0.0238  13  THR   A O   
267  C  CB  A THR   A 13  ? 0.1618 0.1702 0.2251 -0.0179 0.0200  0.0159  13  THR   A CB  
268  C  CB  B THR   A 13  ? 0.1406 0.1745 0.1703 -0.0296 0.0073  0.0370  13  THR   A CB  
269  O  OG1 A THR   A 13  ? 0.1661 0.1757 0.2476 -0.0191 0.0090  0.0188  13  THR   A OG1 
270  O  OG1 B THR   A 13  ? 0.1351 0.1833 0.1728 -0.0353 0.0050  0.0566  13  THR   A OG1 
271  C  CG2 A THR   A 13  ? 0.1704 0.1814 0.2319 -0.0121 0.0243  0.0055  13  THR   A CG2 
272  C  CG2 B THR   A 13  ? 0.1484 0.1827 0.1737 -0.0190 0.0086  0.0202  13  THR   A CG2 
287  N  N   A ASP   A 14  ? 0.1555 0.1434 0.2242 -0.0162 0.0060  0.0332  14  ASP   A N   
288  N  N   B ASP   A 14  ? 0.1419 0.1553 0.1984 -0.0284 0.0080  0.0334  14  ASP   A N   
289  C  CA  A ASP   A 14  ? 0.1626 0.1558 0.2435 -0.0149 -0.0021 0.0454  14  ASP   A CA  
290  C  CA  B ASP   A 14  ? 0.1551 0.1610 0.2219 -0.0185 -0.0033 0.0514  14  ASP   A CA  
291  C  C   A ASP   A 14  ? 0.1559 0.1576 0.2127 -0.0129 0.0011  0.0306  14  ASP   A C   
292  C  C   B ASP   A 14  ? 0.1484 0.1607 0.2003 -0.0200 -0.0065 0.0508  14  ASP   A C   
293  O  O   A ASP   A 14  ? 0.1711 0.1601 0.2111 -0.0100 0.0098  0.0294  14  ASP   A O   
294  O  O   B ASP   A 14  ? 0.1536 0.1615 0.2032 -0.0254 -0.0046 0.0436  14  ASP   A O   
295  C  CB  A ASP   A 14  ? 0.1855 0.1839 0.3132 -0.0175 -0.0003 0.0661  14  ASP   A CB  
296  C  CB  B ASP   A 14  ? 0.1781 0.1758 0.2794 -0.0144 -0.0124 0.0578  14  ASP   A CB  
297  C  CG  A ASP   A 14  ? 0.2113 0.2205 0.3878 -0.0216 0.0020  0.0705  14  ASP   A CG  
298  C  CG  B ASP   A 14  ? 0.2013 0.2170 0.3360 -0.0060 -0.0132 0.0541  14  ASP   A CG  
299  O  OD1 A ASP   A 14  ? 0.2259 0.2203 0.4082 -0.0190 0.0006  0.0665  14  ASP   A OD1 
300  O  OD1 B ASP   A 14  ? 0.2135 0.2238 0.3523 0.0092  -0.0214 0.0644  14  ASP   A OD1 
301  O  OD2 A ASP   A 14  ? 0.2307 0.2537 0.4271 -0.0197 -0.0095 0.0650  14  ASP   A OD2 
302  O  OD2 B ASP   A 14  ? 0.2160 0.2472 0.3668 -0.0096 -0.0236 0.0442  14  ASP   A OD2 
311  N  N   A ASN   A 15  ? 0.1412 0.1478 0.1982 -0.0188 0.0039  0.0200  15  ASN   A N   
312  N  N   B ASN   A 15  ? 0.1458 0.1518 0.1868 -0.0151 -0.0024 0.0632  15  ASN   A N   
313  C  CA  A ASN   A 15  ? 0.1350 0.1500 0.2198 -0.0174 -0.0056 0.0118  15  ASN   A CA  
314  C  CA  B ASN   A 15  ? 0.1444 0.1487 0.1947 -0.0123 0.0010  0.0548  15  ASN   A CA  
315  C  C   A ASN   A 15  ? 0.1358 0.1470 0.2359 -0.0160 0.0026  0.0079  15  ASN   A C   
316  C  C   B ASN   A 15  ? 0.1432 0.1483 0.1961 -0.0164 0.0080  0.0470  15  ASN   A C   
317  O  O   A ASN   A 15  ? 0.1347 0.1406 0.2542 -0.0076 0.0050  0.0015  15  ASN   A O   
318  O  O   B ASN   A 15  ? 0.1430 0.1528 0.1957 -0.0155 0.0086  0.0291  15  ASN   A O   
319  C  CB  A ASN   A 15  ? 0.1271 0.1470 0.2266 -0.0127 0.0032  0.0067  15  ASN   A CB  
320  C  CB  B ASN   A 15  ? 0.1482 0.1509 0.2007 -0.0072 0.0019  0.0534  15  ASN   A CB  
321  C  CG  A ASN   A 15  ? 0.1304 0.1561 0.2372 -0.0105 0.0077  0.0000  15  ASN   A CG  
322  C  CG  B ASN   A 15  ? 0.1497 0.1599 0.2069 -0.0044 0.0134  0.0431  15  ASN   A CG  
323  O  OD1 A ASN   A 15  ? 0.1393 0.1569 0.2487 -0.0191 0.0176  -0.0067 15  ASN   A OD1 
324  O  OD1 B ASN   A 15  ? 0.1493 0.1567 0.2169 -0.0033 0.0320  0.0417  15  ASN   A OD1 
325  N  ND2 A ASN   A 15  ? 0.1351 0.1728 0.2372 -0.0167 0.0077  0.0052  15  ASN   A ND2 
326  N  ND2 B ASN   A 15  ? 0.1567 0.1743 0.2093 -0.0120 0.0115  0.0461  15  ASN   A ND2 
339  N  N   A VAL   A 16  ? 0.1360 0.1494 0.2338 -0.0183 -0.0020 0.0216  16  VAL   A N   
340  N  N   B VAL   A 16  ? 0.1465 0.1462 0.1999 -0.0233 0.0013  0.0606  16  VAL   A N   
341  C  CA  A VAL   A 16  ? 0.1297 0.1551 0.2237 -0.0220 0.0047  0.0240  16  VAL   A CA  
342  C  CA  B VAL   A 16  ? 0.1499 0.1555 0.1995 -0.0209 0.0019  0.0629  16  VAL   A CA  
343  C  C   A VAL   A 16  ? 0.1206 0.1533 0.2099 -0.0257 0.0002  0.0258  16  VAL   A C   
344  C  C   B VAL   A 16  ? 0.1487 0.1674 0.1958 -0.0201 -0.0080 0.0665  16  VAL   A C   
345  O  O   A VAL   A 16  ? 0.1153 0.1487 0.2207 -0.0291 0.0067  0.0187  16  VAL   A O   
346  O  O   B VAL   A 16  ? 0.1494 0.1730 0.1987 -0.0165 -0.0064 0.0633  16  VAL   A O   
347  C  CB  A VAL   A 16  ? 0.1475 0.1721 0.2237 -0.0051 0.0199  0.0315  16  VAL   A CB  
348  C  CB  B VAL   A 16  ? 0.1614 0.1642 0.1981 -0.0053 0.0168  0.0593  16  VAL   A CB  
349  C  CG1 A VAL   A 16  ? 0.1600 0.1826 0.2251 0.0022  0.0204  0.0339  16  VAL   A CG1 
350  C  CG1 B VAL   A 16  ? 0.1692 0.1686 0.1980 0.0038  0.0209  0.0592  16  VAL   A CG1 
351  C  CG2 A VAL   A 16  ? 0.1563 0.1809 0.2267 -0.0020 0.0320  0.0296  16  VAL   A CG2 
352  C  CG2 B VAL   A 16  ? 0.1681 0.1743 0.2117 -0.0042 0.0299  0.0513  16  VAL   A CG2 
371  N  N   A TYR   A 17  ? 0.1220 0.1482 0.2005 -0.0205 0.0052  0.0406  17  TYR   A N   
372  N  N   B TYR   A 17  ? 0.1486 0.1674 0.1980 -0.0189 -0.0082 0.0674  17  TYR   A N   
373  C  CA  A TYR   A 17  ? 0.1314 0.1545 0.1800 -0.0246 -0.0005 0.0419  17  TYR   A CA  
374  C  CA  B TYR   A 17  ? 0.1493 0.1693 0.1835 -0.0234 -0.0074 0.0614  17  TYR   A CA  
375  C  C   A TYR   A 17  ? 0.1284 0.1478 0.1749 -0.0224 0.0004  0.0302  17  TYR   A C   
376  C  C   B TYR   A 17  ? 0.1451 0.1662 0.1861 -0.0243 -0.0045 0.0522  17  TYR   A C   
377  O  O   A TYR   A 17  ? 0.1180 0.1332 0.1501 -0.0218 0.0020  0.0236  17  TYR   A O   
378  O  O   B TYR   A 17  ? 0.1406 0.1670 0.1764 -0.0351 -0.0134 0.0481  17  TYR   A O   
379  C  CB  A TYR   A 17  ? 0.1530 0.1571 0.1869 -0.0333 -0.0093 0.0453  17  TYR   A CB  
380  C  CB  B TYR   A 17  ? 0.1584 0.1738 0.1856 -0.0263 -0.0126 0.0570  17  TYR   A CB  
381  C  CG  A TYR   A 17  ? 0.1715 0.1682 0.1993 -0.0356 -0.0320 0.0441  17  TYR   A CG  
382  C  CG  B TYR   A 17  ? 0.1713 0.1856 0.1952 -0.0235 -0.0200 0.0452  17  TYR   A CG  
383  C  CD1 A TYR   A 17  ? 0.1801 0.1729 0.2138 -0.0302 -0.0362 0.0418  17  TYR   A CD1 
384  C  CD1 B TYR   A 17  ? 0.1821 0.1888 0.2098 -0.0109 -0.0263 0.0434  17  TYR   A CD1 
385  C  CD2 A TYR   A 17  ? 0.1770 0.1732 0.1959 -0.0421 -0.0376 0.0496  17  TYR   A CD2 
386  C  CD2 B TYR   A 17  ? 0.1789 0.1937 0.1969 -0.0205 -0.0213 0.0432  17  TYR   A CD2 
387  C  CE1 A TYR   A 17  ? 0.1787 0.1743 0.2192 -0.0359 -0.0397 0.0423  17  TYR   A CE1 
388  C  CE1 B TYR   A 17  ? 0.1915 0.1951 0.2199 -0.0094 -0.0213 0.0497  17  TYR   A CE1 
389  C  CE2 A TYR   A 17  ? 0.1804 0.1717 0.2103 -0.0403 -0.0391 0.0441  17  TYR   A CE2 
390  C  CE2 B TYR   A 17  ? 0.1876 0.1948 0.2064 -0.0124 -0.0233 0.0429  17  TYR   A CE2 
391  C  CZ  A TYR   A 17  ? 0.1807 0.1679 0.2101 -0.0430 -0.0394 0.0440  17  TYR   A CZ  
392  C  CZ  B TYR   A 17  ? 0.1925 0.1973 0.2199 -0.0070 -0.0266 0.0468  17  TYR   A CZ  
393  O  OH  A TYR   A 17  ? 0.1924 0.1661 0.2079 -0.0340 -0.0359 0.0387  17  TYR   A OH  
394  O  OH  B TYR   A 17  ? 0.1981 0.2050 0.2395 0.0029  -0.0310 0.0445  17  TYR   A OH  
413  N  N   . ILE   A 18  ? 0.1391 0.1602 0.1934 -0.0253 0.0064  0.0547  18  ILE   A N   
414  C  CA  . ILE   A 18  ? 0.1383 0.1589 0.1850 -0.0142 0.0155  0.0526  18  ILE   A CA  
415  C  C   . ILE   A 18  ? 0.1405 0.1684 0.1898 -0.0148 0.0231  0.0482  18  ILE   A C   
416  O  O   . ILE   A 18  ? 0.1412 0.1832 0.2069 -0.0193 0.0242  0.0533  18  ILE   A O   
417  C  CB  . ILE   A 18  ? 0.1443 0.1644 0.1912 -0.0034 0.0135  0.0515  18  ILE   A CB  
418  C  CG1 . ILE   A 18  ? 0.1565 0.1725 0.1857 0.0021  0.0097  0.0555  18  ILE   A CG1 
419  C  CG2 . ILE   A 18  ? 0.1497 0.1729 0.2143 -0.0097 0.0037  0.0531  18  ILE   A CG2 
420  C  CD1 . ILE   A 18  ? 0.1896 0.1912 0.2012 0.0107  -0.0010 0.0534  18  ILE   A CD1 
433  N  N   A LYS   A 19  ? 0.1473 0.1689 0.1951 -0.0059 0.0355  0.0435  19  LYS   A N   
434  N  N   B LYS   A 19  ? 0.1370 0.1665 0.1812 -0.0055 0.0332  0.0454  19  LYS   A N   
435  C  CA  A LYS   A 19  ? 0.1650 0.1802 0.1957 -0.0061 0.0341  0.0406  19  LYS   A CA  
436  C  CA  B LYS   A 19  ? 0.1423 0.1743 0.1708 -0.0042 0.0358  0.0442  19  LYS   A CA  
437  C  C   A LYS   A 19  ? 0.1605 0.1708 0.2020 -0.0064 0.0351  0.0416  19  LYS   A C   
438  C  C   B LYS   A 19  ? 0.1360 0.1682 0.1769 -0.0009 0.0312  0.0336  19  LYS   A C   
439  O  O   A LYS   A 19  ? 0.1487 0.1673 0.1899 -0.0081 0.0253  0.0461  19  LYS   A O   
440  O  O   B LYS   A 19  ? 0.1322 0.1644 0.1688 -0.0025 0.0224  0.0329  19  LYS   A O   
441  C  CB  A LYS   A 19  ? 0.1838 0.2034 0.2008 -0.0062 0.0308  0.0328  19  LYS   A CB  
442  C  CB  B LYS   A 19  ? 0.1543 0.1913 0.1658 0.0005  0.0364  0.0478  19  LYS   A CB  
443  C  CG  A LYS   A 19  ? 0.2044 0.2161 0.2025 -0.0044 0.0252  0.0298  19  LYS   A CG  
444  C  CG  B LYS   A 19  ? 0.1741 0.2089 0.1818 -0.0005 0.0371  0.0386  19  LYS   A CG  
445  C  CD  A LYS   A 19  ? 0.2196 0.2244 0.1983 -0.0004 0.0288  0.0286  19  LYS   A CD  
446  C  CD  B LYS   A 19  ? 0.1906 0.2244 0.1886 -0.0034 0.0348  0.0326  19  LYS   A CD  
447  C  CE  A LYS   A 19  ? 0.2254 0.2282 0.1993 -0.0026 0.0344  0.0268  19  LYS   A CE  
448  C  CE  B LYS   A 19  ? 0.1985 0.2352 0.1959 -0.0091 0.0328  0.0310  19  LYS   A CE  
449  N  NZ  A LYS   A 19  ? 0.2305 0.2271 0.1976 -0.0036 0.0372  0.0220  19  LYS   A NZ  
450  N  NZ  B LYS   A 19  ? 0.2037 0.2405 0.1953 -0.0075 0.0296  0.0245  19  LYS   A NZ  
477  N  N   A ASN   A 20  ? 0.1723 0.1716 0.2200 -0.0105 0.0426  0.0433  20  ASN   A N   
478  N  N   B ASN   A 20  ? 0.1383 0.1713 0.1875 -0.0017 0.0344  0.0329  20  ASN   A N   
479  C  CA  A ASN   A 20  ? 0.1870 0.1777 0.2232 -0.0031 0.0459  0.0376  20  ASN   A CA  
480  C  CA  B ASN   A 20  ? 0.1402 0.1803 0.1928 0.0076  0.0362  0.0285  20  ASN   A CA  
481  C  C   A ASN   A 20  ? 0.1932 0.1820 0.2108 -0.0063 0.0484  0.0349  20  ASN   A C   
482  C  C   B ASN   A 20  ? 0.1525 0.1877 0.2010 0.0050  0.0459  0.0213  20  ASN   A C   
483  O  O   A ASN   A 20  ? 0.2018 0.1789 0.1994 -0.0116 0.0416  0.0343  20  ASN   A O   
484  O  O   B ASN   A 20  ? 0.1613 0.1866 0.2168 0.0073  0.0439  0.0212  20  ASN   A O   
485  C  CB  A ASN   A 20  ? 0.2019 0.1823 0.2418 0.0032  0.0503  0.0384  20  ASN   A CB  
486  C  CB  B ASN   A 20  ? 0.1362 0.1846 0.1962 0.0139  0.0293  0.0308  20  ASN   A CB  
487  C  CG  A ASN   A 20  ? 0.2205 0.1890 0.2673 0.0121  0.0533  0.0343  20  ASN   A CG  
488  C  CG  B ASN   A 20  ? 0.1353 0.1851 0.1945 0.0214  0.0216  0.0296  20  ASN   A CG  
489  O  OD1 A ASN   A 20  ? 0.2404 0.2046 0.3036 0.0164  0.0549  0.0170  20  ASN   A OD1 
490  O  OD1 B ASN   A 20  ? 0.1375 0.1786 0.2012 0.0256  0.0237  0.0119  20  ASN   A OD1 
491  N  ND2 A ASN   A 20  ? 0.2239 0.1820 0.2724 0.0171  0.0461  0.0442  20  ASN   A ND2 
492  N  ND2 B ASN   A 20  ? 0.1427 0.1912 0.2086 0.0261  0.0101  0.0462  20  ASN   A ND2 
505  N  N   A ALA   A 21  ? 0.1949 0.1878 0.2112 -0.0045 0.0414  0.0271  21  ALA   A N   
506  N  N   B ALA   A 21  ? 0.1623 0.1919 0.2000 0.0017  0.0391  0.0078  21  ALA   A N   
507  C  CA  A ALA   A 21  ? 0.1949 0.1842 0.2125 -0.0061 0.0371  0.0349  21  ALA   A CA  
508  C  CA  B ALA   A 21  ? 0.1718 0.1891 0.2008 -0.0074 0.0336  0.0087  21  ALA   A CA  
509  C  C   A ALA   A 21  ? 0.1828 0.1791 0.2159 -0.0046 0.0332  0.0311  21  ALA   A C   
510  C  C   B ALA   A 21  ? 0.1638 0.1778 0.1852 -0.0094 0.0441  0.0136  21  ALA   A C   
511  O  O   A ALA   A 21  ? 0.1808 0.1858 0.2255 -0.0057 0.0297  0.0230  21  ALA   A O   
512  O  O   B ALA   A 21  ? 0.1583 0.1805 0.1912 -0.0099 0.0469  0.0115  21  ALA   A O   
513  C  CB  A ALA   A 21  ? 0.2083 0.1920 0.2128 -0.0089 0.0388  0.0422  21  ALA   A CB  
514  C  CB  B ALA   A 21  ? 0.1906 0.2007 0.2226 -0.0125 0.0203  0.0042  21  ALA   A CB  
525  N  N   A ASP   A 22  ? 0.1769 0.1730 0.2249 -0.0055 0.0343  0.0256  22  ASP   A N   
526  N  N   B ASP   A 22  ? 0.1655 0.1715 0.1880 -0.0102 0.0476  0.0119  22  ASP   A N   
527  C  CA  A ASP   A 22  ? 0.1754 0.1696 0.2142 -0.0034 0.0287  0.0328  22  ASP   A CA  
528  C  CA  B ASP   A 22  ? 0.1717 0.1695 0.1890 -0.0047 0.0439  0.0099  22  ASP   A CA  
529  C  C   A ASP   A 22  ? 0.1659 0.1713 0.1809 0.0012  0.0269  0.0351  22  ASP   A C   
530  C  C   B ASP   A 22  ? 0.1630 0.1639 0.1544 -0.0099 0.0367  0.0152  22  ASP   A C   
531  O  O   A ASP   A 22  ? 0.1720 0.1719 0.1882 -0.0009 0.0311  0.0369  22  ASP   A O   
532  O  O   B ASP   A 22  ? 0.1642 0.1687 0.1581 -0.0117 0.0363  0.0092  22  ASP   A O   
533  C  CB  A ASP   A 22  ? 0.1918 0.1703 0.2512 -0.0018 0.0203  0.0215  22  ASP   A CB  
534  C  CB  B ASP   A 22  ? 0.1935 0.1770 0.2191 0.0088  0.0624  -0.0004 22  ASP   A CB  
535  C  CG  A ASP   A 22  ? 0.2076 0.1744 0.2812 -0.0059 0.0031  0.0236  22  ASP   A CG  
536  C  CG  B ASP   A 22  ? 0.2092 0.1807 0.2396 0.0166  0.0824  -0.0033 22  ASP   A CG  
537  O  OD1 A ASP   A 22  ? 0.2003 0.1737 0.2949 -0.0244 -0.0101 0.0287  22  ASP   A OD1 
538  O  OD1 B ASP   A 22  ? 0.2085 0.1757 0.2132 0.0139  0.0811  0.0066  22  ASP   A OD1 
539  O  OD2 A ASP   A 22  ? 0.2284 0.1844 0.3029 0.0061  0.0089  0.0082  22  ASP   A OD2 
540  O  OD2 B ASP   A 22  ? 0.2262 0.1912 0.2759 0.0152  0.0905  -0.0016 22  ASP   A OD2 
549  N  N   A ILE   A 23  ? 0.1655 0.1736 0.1661 0.0015  0.0262  0.0324  23  ILE   A N   
550  N  N   B ILE   A 23  ? 0.1579 0.1609 0.1468 -0.0070 0.0231  0.0194  23  ILE   A N   
551  C  CA  A ILE   A 23  ? 0.1706 0.1717 0.1591 0.0005  0.0273  0.0234  23  ILE   A CA  
552  C  CA  B ILE   A 23  ? 0.1545 0.1633 0.1303 -0.0067 0.0130  0.0255  23  ILE   A CA  
553  C  C   A ILE   A 23  ? 0.1732 0.1678 0.1610 0.0028  0.0400  0.0210  23  ILE   A C   
554  C  C   B ILE   A 23  ? 0.1556 0.1708 0.1453 -0.0153 0.0161  0.0128  23  ILE   A C   
555  O  O   A ILE   A 23  ? 0.1794 0.1706 0.1626 0.0029  0.0342  0.0121  23  ILE   A O   
556  O  O   B ILE   A 23  ? 0.1588 0.1672 0.1500 -0.0110 0.0143  0.0097  23  ILE   A O   
557  C  CB  A ILE   A 23  ? 0.1724 0.1693 0.1458 0.0039  0.0242  0.0116  23  ILE   A CB  
558  C  CB  B ILE   A 23  ? 0.1511 0.1585 0.1210 -0.0012 0.0110  0.0287  23  ILE   A CB  
559  C  CG1 A ILE   A 23  ? 0.1731 0.1669 0.1514 0.0042  0.0212  0.0033  23  ILE   A CG1 
560  C  CG1 B ILE   A 23  ? 0.1556 0.1621 0.1290 -0.0006 0.0091  0.0219  23  ILE   A CG1 
561  C  CG2 A ILE   A 23  ? 0.1740 0.1753 0.1463 0.0047  0.0216  0.0216  23  ILE   A CG2 
562  C  CG2 B ILE   A 23  ? 0.1477 0.1530 0.1204 0.0065  0.0156  0.0272  23  ILE   A CG2 
563  C  CD1 A ILE   A 23  ? 0.1733 0.1705 0.1544 0.0006  0.0159  -0.0079 23  ILE   A CD1 
564  C  CD1 B ILE   A 23  ? 0.1584 0.1599 0.1476 0.0020  0.0078  0.0200  23  ILE   A CD1 
587  N  N   A VAL   A 24  ? 0.1817 0.1673 0.1630 0.0038  0.0392  0.0190  24  VAL   A N   
588  N  N   B VAL   A 24  ? 0.1628 0.1787 0.1666 -0.0241 0.0167  0.0056  24  VAL   A N   
589  C  CA  A VAL   A 24  ? 0.1979 0.1821 0.1770 -0.0057 0.0393  0.0129  24  VAL   A CA  
590  C  CA  B VAL   A 24  ? 0.1762 0.1864 0.1796 -0.0290 0.0198  0.0066  24  VAL   A CA  
591  C  C   A VAL   A 24  ? 0.2084 0.1946 0.1790 -0.0135 0.0373  0.0115  24  VAL   A C   
592  C  C   B VAL   A 24  ? 0.1815 0.2072 0.1790 -0.0336 0.0270  -0.0131 24  VAL   A C   
593  O  O   A VAL   A 24  ? 0.2210 0.1996 0.1793 -0.0142 0.0370  0.0106  24  VAL   A O   
594  O  O   B VAL   A 24  ? 0.1852 0.2117 0.1846 -0.0214 0.0233  -0.0143 24  VAL   A O   
595  C  CB  A VAL   A 24  ? 0.1993 0.1872 0.2012 -0.0025 0.0404  0.0167  24  VAL   A CB  
596  C  CB  B VAL   A 24  ? 0.1862 0.1848 0.2082 -0.0294 0.0159  0.0208  24  VAL   A CB  
597  C  CG1 A VAL   A 24  ? 0.2018 0.1907 0.2193 0.0043  0.0362  0.0045  24  VAL   A CG1 
598  C  CG1 B VAL   A 24  ? 0.2013 0.1908 0.2311 -0.0226 0.0023  0.0195  24  VAL   A CG1 
599  C  CG2 A VAL   A 24  ? 0.2099 0.1938 0.2045 0.0006  0.0514  0.0293  24  VAL   A CG2 
600  C  CG2 B VAL   A 24  ? 0.1937 0.1858 0.2154 -0.0271 0.0221  0.0304  24  VAL   A CG2 
619  N  N   A GLU   A 25  ? 0.2136 0.2098 0.1881 -0.0178 0.0412  0.0003  25  GLU   A N   
620  N  N   B GLU   A 25  ? 0.1880 0.2233 0.1778 -0.0395 0.0511  -0.0168 25  GLU   A N   
621  C  CA  A GLU   A 25  ? 0.2278 0.2310 0.1945 -0.0154 0.0439  -0.0010 25  GLU   A CA  
622  C  CA  B GLU   A 25  ? 0.2066 0.2429 0.1889 -0.0469 0.0640  -0.0214 25  GLU   A CA  
623  C  C   A GLU   A 25  ? 0.2092 0.2348 0.1698 -0.0206 0.0526  -0.0038 25  GLU   A C   
624  C  C   B GLU   A 25  ? 0.2014 0.2460 0.1502 -0.0479 0.0656  -0.0194 25  GLU   A C   
625  O  O   A GLU   A 25  ? 0.2096 0.2373 0.1915 -0.0119 0.0434  -0.0081 25  GLU   A O   
626  O  O   B GLU   A 25  ? 0.2065 0.2482 0.1499 -0.0437 0.0651  -0.0252 25  GLU   A O   
627  C  CB  A GLU   A 25  ? 0.2576 0.2542 0.2376 -0.0128 0.0399  0.0045  25  GLU   A CB  
628  C  CB  B GLU   A 25  ? 0.2303 0.2536 0.2200 -0.0534 0.0812  -0.0228 25  GLU   A CB  
629  C  CG  A GLU   A 25  ? 0.2864 0.2740 0.3041 -0.0168 0.0283  -0.0035 25  GLU   A CG  
630  C  CG  B GLU   A 25  ? 0.2584 0.2719 0.2729 -0.0506 0.0794  -0.0233 25  GLU   A CG  
631  C  CD  A GLU   A 25  ? 0.3063 0.2913 0.3645 -0.0207 0.0179  -0.0070 25  GLU   A CD  
632  C  CD  B GLU   A 25  ? 0.2785 0.2860 0.3272 -0.0540 0.0716  -0.0198 25  GLU   A CD  
633  O  OE1 A GLU   A 25  ? 0.3144 0.2982 0.3762 -0.0165 0.0069  -0.0121 25  GLU   A OE1 
634  O  OE1 B GLU   A 25  ? 0.2845 0.2897 0.3465 -0.0555 0.0670  -0.0185 25  GLU   A OE1 
635  O  OE2 A GLU   A 25  ? 0.3112 0.3002 0.3960 -0.0279 0.0127  -0.0136 25  GLU   A OE2 
636  O  OE2 B GLU   A 25  ? 0.2928 0.2915 0.3513 -0.0510 0.0712  -0.0175 25  GLU   A OE2 
649  N  N   A GLU   A 26  ? 0.2004 0.2382 0.1672 -0.0329 0.0500  -0.0013 26  GLU   A N   
650  N  N   B GLU   A 26  ? 0.1983 0.2442 0.1468 -0.0527 0.0560  -0.0271 26  GLU   A N   
651  C  CA  A GLU   A 26  ? 0.1998 0.2493 0.1521 -0.0456 0.0489  0.0045  26  GLU   A CA  
652  C  CA  B GLU   A 26  ? 0.2010 0.2449 0.1431 -0.0551 0.0518  -0.0215 26  GLU   A CA  
653  C  C   A GLU   A 26  ? 0.1995 0.2478 0.1450 -0.0409 0.0446  0.0084  26  GLU   A C   
654  C  C   B GLU   A 26  ? 0.1986 0.2366 0.1266 -0.0578 0.0438  -0.0170 26  GLU   A C   
655  O  O   A GLU   A 26  ? 0.2090 0.2484 0.1565 -0.0412 0.0416  0.0092  26  GLU   A O   
656  O  O   B GLU   A 26  ? 0.2040 0.2300 0.1323 -0.0564 0.0431  -0.0097 26  GLU   A O   
657  C  CB  A GLU   A 26  ? 0.2101 0.2598 0.1685 -0.0544 0.0457  0.0080  26  GLU   A CB  
658  C  CB  B GLU   A 26  ? 0.2154 0.2560 0.1651 -0.0589 0.0463  -0.0259 26  GLU   A CB  
659  C  CG  A GLU   A 26  ? 0.2328 0.2808 0.2229 -0.0566 0.0378  0.0023  26  GLU   A CG  
660  C  CG  B GLU   A 26  ? 0.2268 0.2634 0.1761 -0.0684 0.0565  -0.0247 26  GLU   A CG  
661  C  CD  A GLU   A 26  ? 0.2510 0.2979 0.2609 -0.0636 0.0391  0.0030  26  GLU   A CD  
662  C  CD  B GLU   A 26  ? 0.2375 0.2716 0.1754 -0.0825 0.0720  -0.0181 26  GLU   A CD  
663  O  OE1 A GLU   A 26  ? 0.2534 0.3167 0.2680 -0.0580 0.0486  0.0015  26  GLU   A OE1 
664  O  OE1 B GLU   A 26  ? 0.2383 0.2900 0.1799 -0.0814 0.0831  -0.0228 26  GLU   A OE1 
665  O  OE2 A GLU   A 26  ? 0.2739 0.3048 0.2786 -0.0627 0.0285  0.0042  26  GLU   A OE2 
666  O  OE2 B GLU   A 26  ? 0.2497 0.2710 0.1422 -0.0825 0.0837  -0.0124 26  GLU   A OE2 
679  N  N   A ALA   A 27  ? 0.1898 0.2453 0.1500 -0.0422 0.0429  0.0083  27  ALA   A N   
680  N  N   B ALA   A 27  ? 0.1903 0.2389 0.1307 -0.0611 0.0286  -0.0156 27  ALA   A N   
681  C  CA  A ALA   A 27  ? 0.1965 0.2599 0.1452 -0.0421 0.0377  0.0074  27  ALA   A CA  
682  C  CA  B ALA   A 27  ? 0.1964 0.2527 0.1331 -0.0581 0.0185  -0.0163 27  ALA   A CA  
683  C  C   A ALA   A 27  ? 0.2240 0.2800 0.1535 -0.0516 0.0415  -0.0073 27  ALA   A C   
684  C  C   B ALA   A 27  ? 0.2186 0.2711 0.1452 -0.0623 0.0194  -0.0238 27  ALA   A C   
685  O  O   A ALA   A 27  ? 0.2347 0.2773 0.1571 -0.0555 0.0316  -0.0022 27  ALA   A O   
686  O  O   B ALA   A 27  ? 0.2249 0.2694 0.1402 -0.0639 0.0069  -0.0194 27  ALA   A O   
687  C  CB  A ALA   A 27  ? 0.1828 0.2565 0.1463 -0.0388 0.0308  0.0056  27  ALA   A CB  
688  C  CB  B ALA   A 27  ? 0.1865 0.2482 0.1419 -0.0559 0.0118  -0.0124 27  ALA   A CB  
699  N  N   A LYS   A 28  ? 0.2524 0.3033 0.1716 -0.0528 0.0312  -0.0337 28  LYS   A N   
700  N  N   B LYS   A 28  ? 0.2431 0.2931 0.1626 -0.0620 0.0181  -0.0431 28  LYS   A N   
701  C  CA  A LYS   A 28  ? 0.2854 0.3323 0.2036 -0.0501 0.0256  -0.0555 28  LYS   A CA  
702  C  CA  B LYS   A 28  ? 0.2723 0.3224 0.1886 -0.0567 0.0207  -0.0558 28  LYS   A CA  
703  C  C   A LYS   A 28  ? 0.3022 0.3531 0.1918 -0.0573 0.0319  -0.0487 28  LYS   A C   
704  C  C   B LYS   A 28  ? 0.2938 0.3474 0.1833 -0.0613 0.0331  -0.0464 28  LYS   A C   
705  O  O   A LYS   A 28  ? 0.3145 0.3627 0.2292 -0.0553 0.0146  -0.0488 28  LYS   A O   
706  O  O   B LYS   A 28  ? 0.3028 0.3552 0.2127 -0.0603 0.0199  -0.0444 28  LYS   A O   
707  C  CB  A LYS   A 28  ? 0.3046 0.3461 0.2527 -0.0358 0.0159  -0.0726 28  LYS   A CB  
708  C  CB  B LYS   A 28  ? 0.2838 0.3323 0.2256 -0.0431 0.0119  -0.0691 28  LYS   A CB  
709  C  CG  A LYS   A 28  ? 0.3224 0.3573 0.3085 -0.0240 0.0094  -0.0809 28  LYS   A CG  
710  C  CG  B LYS   A 28  ? 0.2972 0.3420 0.2768 -0.0305 0.0065  -0.0751 28  LYS   A CG  
711  C  CD  A LYS   A 28  ? 0.3377 0.3717 0.3722 -0.0145 0.0004  -0.0814 28  LYS   A CD  
712  C  CD  B LYS   A 28  ? 0.3125 0.3556 0.3398 -0.0196 -0.0002 -0.0737 28  LYS   A CD  
713  C  CE  A LYS   A 28  ? 0.3516 0.3828 0.4166 -0.0080 -0.0071 -0.0855 28  LYS   A CE  
714  C  CE  B LYS   A 28  ? 0.3271 0.3660 0.3884 -0.0140 -0.0038 -0.0781 28  LYS   A CE  
715  N  NZ  A LYS   A 28  ? 0.3608 0.3886 0.4466 -0.0036 -0.0068 -0.0899 28  LYS   A NZ  
716  N  NZ  B LYS   A 28  ? 0.3351 0.3713 0.4142 -0.0108 -0.0049 -0.0835 28  LYS   A NZ  
743  N  N   . LYS   A 29  ? 0.3056 0.3643 0.1751 -0.0694 0.0582  -0.0341 29  LYS   A N   
744  C  CA  . LYS   A 29  ? 0.3340 0.3969 0.2075 -0.0819 0.0883  -0.0175 29  LYS   A CA  
745  C  C   . LYS   A 29  ? 0.3422 0.3963 0.1876 -0.0940 0.0779  -0.0088 29  LYS   A C   
746  O  O   . LYS   A 29  ? 0.3552 0.4101 0.1933 -0.0864 0.0707  -0.0103 29  LYS   A O   
747  C  CB  . LYS   A 29  ? 0.3528 0.4304 0.2798 -0.0745 0.1081  -0.0112 29  LYS   A CB  
748  C  CG  . LYS   A 29  ? 0.3783 0.4596 0.3662 -0.0627 0.1103  -0.0096 29  LYS   A CG  
749  C  CD  . LYS   A 29  ? 0.4030 0.4837 0.4521 -0.0517 0.1073  -0.0103 29  LYS   A CD  
750  C  CE  . LYS   A 29  ? 0.4177 0.5020 0.5066 -0.0443 0.1076  -0.0132 29  LYS   A CE  
751  N  NZ  . LYS   A 29  ? 0.4262 0.5111 0.5435 -0.0403 0.1062  -0.0145 29  LYS   A NZ  
766  N  N   . VAL   A 30  ? 0.3343 0.3808 0.1754 -0.1077 0.0724  0.0010  30  VAL   A N   
767  C  CA  . VAL   A 30  ? 0.3341 0.3649 0.1623 -0.1184 0.0486  0.0207  30  VAL   A CA  
768  C  C   . VAL   A 30  ? 0.3404 0.3527 0.1348 -0.1172 0.0308  0.0345  30  VAL   A C   
769  O  O   . VAL   A 30  ? 0.3505 0.3578 0.1414 -0.1151 0.0208  0.0382  30  VAL   A O   
770  C  CB  . VAL   A 30  ? 0.3307 0.3618 0.2055 -0.1252 0.0286  0.0216  30  VAL   A CB  
771  C  CG1 . VAL   A 30  ? 0.3379 0.3600 0.2265 -0.1247 0.0221  0.0332  30  VAL   A CG1 
772  C  CG2 . VAL   A 30  ? 0.3265 0.3647 0.2320 -0.1330 0.0250  0.0162  30  VAL   A CG2 
782  N  N   . LYS   A 31  ? 0.3340 0.3409 0.1257 -0.1202 0.0171  0.0286  31  LYS   A N   
783  C  CA  . LYS   A 31  ? 0.3453 0.3411 0.1485 -0.1070 -0.0088 0.0280  31  LYS   A CA  
784  C  C   . LYS   A 31  ? 0.3142 0.3132 0.1186 -0.0867 -0.0174 0.0578  31  LYS   A C   
785  O  O   . LYS   A 31  ? 0.3175 0.3247 0.1359 -0.0805 -0.0324 0.0685  31  LYS   A O   
786  C  CB  . LYS   A 31  ? 0.3994 0.3803 0.2731 -0.1032 -0.0282 0.0128  31  LYS   A CB  
787  C  CG  . LYS   A 31  ? 0.4569 0.4205 0.4273 -0.0932 -0.0435 0.0029  31  LYS   A CG  
788  C  CD  . LYS   A 31  ? 0.5000 0.4574 0.5403 -0.0827 -0.0550 -0.0058 31  LYS   A CD  
789  C  CE  . LYS   A 31  ? 0.5310 0.4879 0.6141 -0.0746 -0.0639 -0.0132 31  LYS   A CE  
790  N  NZ  . LYS   A 31  ? 0.5500 0.4972 0.6546 -0.0700 -0.0696 -0.0182 31  LYS   A NZ  
804  N  N   . PRO   A 32  ? 0.2758 0.2801 0.1039 -0.0818 -0.0099 0.0452  32  PRO   A N   
805  C  CA  . PRO   A 32  ? 0.2639 0.2609 0.1387 -0.0723 -0.0194 0.0580  32  PRO   A CA  
806  C  C   . PRO   A 32  ? 0.2605 0.2546 0.1476 -0.0608 -0.0238 0.0657  32  PRO   A C   
807  O  O   . PRO   A 32  ? 0.2574 0.2483 0.1650 -0.0581 -0.0361 0.0686  32  PRO   A O   
808  C  CB  . PRO   A 32  ? 0.2531 0.2620 0.1417 -0.0739 -0.0173 0.0474  32  PRO   A CB  
809  C  CG  . PRO   A 32  ? 0.2476 0.2641 0.1063 -0.0687 -0.0287 0.0334  32  PRO   A CG  
810  C  CD  . PRO   A 32  ? 0.2559 0.2688 0.0983 -0.0758 -0.0169 0.0443  32  PRO   A CD  
818  N  N   . THR   A 33  ? 0.2632 0.2543 0.1452 -0.0538 -0.0247 0.0620  33  THR   A N   
819  C  CA  . THR   A 33  ? 0.2594 0.2568 0.1585 -0.0444 -0.0354 0.0610  33  THR   A CA  
820  C  C   . THR   A 33  ? 0.2286 0.2352 0.1455 -0.0452 -0.0338 0.0510  33  THR   A C   
821  O  O   . THR   A 33  ? 0.2274 0.2360 0.1627 -0.0476 -0.0403 0.0561  33  THR   A O   
822  C  CB  . THR   A 33  ? 0.2848 0.2768 0.1691 -0.0370 -0.0424 0.0811  33  THR   A CB  
823  O  OG1 . THR   A 33  ? 0.3082 0.2894 0.2025 -0.0277 -0.0302 0.0873  33  THR   A OG1 
824  C  CG2 . THR   A 33  ? 0.2895 0.2855 0.1888 -0.0318 -0.0471 0.0796  33  THR   A CG2 
832  N  N   . VAL   A 34  ? 0.2020 0.2143 0.1310 -0.0442 -0.0266 0.0470  34  VAL   A N   
833  C  CA  . VAL   A 34  ? 0.1819 0.1962 0.1253 -0.0384 -0.0147 0.0440  34  VAL   A CA  
834  C  C   . VAL   A 34  ? 0.1741 0.1887 0.1202 -0.0334 -0.0080 0.0313  34  VAL   A C   
835  O  O   . VAL   A 34  ? 0.1719 0.1866 0.1429 -0.0404 -0.0095 0.0402  34  VAL   A O   
836  C  CB  . VAL   A 34  ? 0.1929 0.1928 0.1494 -0.0338 -0.0086 0.0327  34  VAL   A CB  
837  C  CG1 . VAL   A 34  ? 0.1994 0.1984 0.1451 -0.0295 0.0080  0.0166  34  VAL   A CG1 
838  C  CG2 . VAL   A 34  ? 0.2013 0.2028 0.1867 -0.0206 -0.0192 0.0310  34  VAL   A CG2 
848  N  N   . VAL   A 35  ? 0.1611 0.1761 0.1229 -0.0350 -0.0100 0.0276  35  VAL   A N   
849  C  CA  . VAL   A 35  ? 0.1549 0.1676 0.1195 -0.0276 -0.0035 0.0208  35  VAL   A CA  
850  C  C   . VAL   A 35  ? 0.1451 0.1520 0.1114 -0.0187 0.0013  0.0171  35  VAL   A C   
851  O  O   . VAL   A 35  ? 0.1357 0.1619 0.1414 -0.0218 0.0132  0.0113  35  VAL   A O   
852  C  CB  . VAL   A 35  ? 0.1594 0.1737 0.1290 -0.0214 0.0093  0.0095  35  VAL   A CB  
853  C  CG1 . VAL   A 35  ? 0.1665 0.1777 0.1472 -0.0156 0.0000  0.0118  35  VAL   A CG1 
854  C  CG2 . VAL   A 35  ? 0.1599 0.1758 0.1476 -0.0139 0.0141  0.0081  35  VAL   A CG2 
864  N  N   . VAL   A 36  ? 0.1325 0.1522 0.1105 -0.0219 0.0098  0.0203  36  VAL   A N   
865  C  CA  . VAL   A 36  ? 0.1324 0.1367 0.1169 -0.0159 0.0076  0.0104  36  VAL   A CA  
866  C  C   . VAL   A 36  ? 0.1258 0.1408 0.1236 -0.0165 0.0095  0.0103  36  VAL   A C   
867  O  O   . VAL   A 36  ? 0.1301 0.1413 0.1428 -0.0096 0.0168  0.0177  36  VAL   A O   
868  C  CB  . VAL   A 36  ? 0.1288 0.1328 0.1302 -0.0106 0.0028  0.0121  36  VAL   A CB  
869  C  CG1 . VAL   A 36  ? 0.1373 0.1336 0.1364 -0.0134 0.0059  0.0038  36  VAL   A CG1 
870  C  CG2 . VAL   A 36  ? 0.1404 0.1335 0.1554 -0.0130 -0.0016 0.0206  36  VAL   A CG2 
880  N  N   . ASN   A 37  ? 0.1217 0.1286 0.1277 -0.0042 0.0102  0.0149  37  ASN   A N   
881  C  CA  . ASN   A 37  ? 0.1270 0.1235 0.1141 -0.0012 0.0149  0.0116  37  ASN   A CA  
882  C  C   . ASN   A 37  ? 0.1246 0.1259 0.1215 -0.0018 0.0151  0.0179  37  ASN   A C   
883  O  O   . ASN   A 37  ? 0.1355 0.1377 0.1259 0.0063  0.0138  0.0036  37  ASN   A O   
884  C  CB  . ASN   A 37  ? 0.1255 0.1254 0.1285 -0.0039 0.0080  0.0098  37  ASN   A CB  
885  C  CG  . ASN   A 37  ? 0.1237 0.1219 0.1317 -0.0007 0.0037  0.0060  37  ASN   A CG  
886  O  OD1 . ASN   A 37  ? 0.1226 0.1252 0.1608 -0.0022 0.0095  0.0158  37  ASN   A OD1 
887  N  ND2 . ASN   A 37  ? 0.1249 0.1282 0.1471 -0.0017 0.0029  0.0248  37  ASN   A ND2 
894  N  N   A ALA   A 38  ? 0.1241 0.1279 0.1339 0.0023  0.0154  0.0083  38  ALA   A N   
895  N  N   B ALA   A 38  ? 0.1250 0.1292 0.1310 0.0020  0.0123  0.0115  38  ALA   A N   
896  C  CA  A ALA   A 38  ? 0.1319 0.1314 0.1289 -0.0016 0.0108  0.0011  38  ALA   A CA  
897  C  CA  B ALA   A 38  ? 0.1315 0.1336 0.1277 -0.0003 0.0063  0.0085  38  ALA   A CA  
898  C  C   A ALA   A 38  ? 0.1271 0.1318 0.1304 -0.0010 0.0032  -0.0032 38  ALA   A C   
899  C  C   B ALA   A 38  ? 0.1268 0.1324 0.1293 0.0008  0.0012  0.0026  38  ALA   A C   
900  O  O   A ALA   A 38  ? 0.1299 0.1295 0.1396 0.0022  0.0033  0.0043  38  ALA   A O   
901  O  O   B ALA   A 38  ? 0.1272 0.1319 0.1378 0.0038  -0.0008 0.0117  38  ALA   A O   
902  C  CB  A ALA   A 38  ? 0.1324 0.1550 0.1372 -0.0136 0.0023  -0.0084 38  ALA   A CB  
903  C  CB  B ALA   A 38  ? 0.1338 0.1544 0.1368 -0.0098 -0.0042 0.0023  38  ALA   A CB  
914  N  N   . ALA   A 39  ? 0.1270 0.1287 0.1334 0.0047  0.0064  0.0096  39  ALA   A N   
915  C  CA  . ALA   A 39  ? 0.1308 0.1305 0.1306 -0.0022 0.0133  0.0083  39  ALA   A CA  
916  C  C   . ALA   A 39  ? 0.1295 0.1268 0.1261 0.0014  0.0074  0.0088  39  ALA   A C   
917  O  O   . ALA   A 39  ? 0.1426 0.1331 0.1367 -0.0048 0.0115  0.0052  39  ALA   A O   
918  C  CB  . ALA   A 39  ? 0.1344 0.1535 0.1417 -0.0033 -0.0049 0.0058  39  ALA   A CB  
925  N  N   . ASN   A 40  ? 0.1365 0.1316 0.1318 -0.0036 0.0235  0.0043  40  ASN   A N   
926  C  CA  . ASN   A 40  ? 0.1446 0.1301 0.1380 -0.0031 0.0110  0.0105  40  ASN   A CA  
927  C  C   . ASN   A 40  ? 0.1447 0.1242 0.1232 -0.0004 0.0214  0.0149  40  ASN   A C   
928  O  O   . ASN   A 40  ? 0.1393 0.1277 0.1349 -0.0033 0.0180  0.0191  40  ASN   A O   
929  C  CB  . ASN   A 40  ? 0.1539 0.1346 0.1445 0.0004  0.0001  0.0076  40  ASN   A CB  
930  C  CG  . ASN   A 40  ? 0.1605 0.1355 0.1683 0.0023  -0.0025 0.0160  40  ASN   A CG  
931  O  OD1 . ASN   A 40  ? 0.1720 0.1367 0.1891 0.0015  0.0014  0.0120  40  ASN   A OD1 
932  N  ND2 . ASN   A 40  ? 0.1609 0.1446 0.1959 0.0031  0.0019  0.0018  40  ASN   A ND2 
939  N  N   . VAL   A 41  ? 0.1576 0.1272 0.1312 -0.0033 0.0285  0.0193  41  VAL   A N   
940  C  CA  . VAL   A 41  ? 0.1579 0.1306 0.1565 -0.0035 0.0317  0.0120  41  VAL   A CA  
941  C  C   . VAL   A 41  ? 0.1545 0.1285 0.1556 -0.0006 0.0305  0.0140  41  VAL   A C   
942  O  O   . VAL   A 41  ? 0.1544 0.1276 0.1785 0.0032  0.0308  0.0097  41  VAL   A O   
943  C  CB  . VAL   A 41  ? 0.1707 0.1427 0.1581 -0.0058 0.0470  0.0068  41  VAL   A CB  
944  C  CG1 . VAL   A 41  ? 0.1833 0.1449 0.1704 -0.0028 0.0432  0.0014  41  VAL   A CG1 
945  C  CG2 . VAL   A 41  ? 0.1954 0.1590 0.1479 -0.0134 0.0496  0.0027  41  VAL   A CG2 
955  N  N   A TYR   A 42  ? 0.1454 0.1235 0.1631 -0.0044 0.0296  0.0222  42  TYR   A N   
956  N  N   B TYR   A 42  ? 0.1454 0.1252 0.1592 -0.0060 0.0286  0.0220  42  TYR   A N   
957  C  CA  A TYR   A 42  ? 0.1437 0.1230 0.1692 -0.0007 0.0283  0.0201  42  TYR   A CA  
958  C  CA  B TYR   A 42  ? 0.1410 0.1259 0.1650 -0.0046 0.0276  0.0206  42  TYR   A CA  
959  C  C   A TYR   A 42  ? 0.1370 0.1275 0.1645 -0.0021 0.0218  0.0192  42  TYR   A C   
960  C  C   B TYR   A 42  ? 0.1353 0.1271 0.1612 -0.0038 0.0207  0.0186  42  TYR   A C   
961  O  O   A TYR   A 42  ? 0.1396 0.1316 0.1808 -0.0113 0.0208  0.0082  42  TYR   A O   
962  O  O   B TYR   A 42  ? 0.1369 0.1286 0.1745 -0.0105 0.0197  0.0095  42  TYR   A O   
963  C  CB  A TYR   A 42  ? 0.1548 0.1302 0.1677 -0.0014 0.0244  0.0326  42  TYR   A CB  
964  C  CB  B TYR   A 42  ? 0.1447 0.1366 0.1641 -0.0043 0.0352  0.0250  42  TYR   A CB  
965  C  CG  A TYR   A 42  ? 0.1636 0.1431 0.1664 0.0083  0.0111  0.0379  42  TYR   A CG  
966  C  CG  B TYR   A 42  ? 0.1482 0.1497 0.1629 -0.0047 0.0284  0.0244  42  TYR   A CG  
967  C  CD1 A TYR   A 42  ? 0.1619 0.1550 0.1638 0.0040  0.0150  0.0422  42  TYR   A CD1 
968  C  CD1 B TYR   A 42  ? 0.1525 0.1593 0.1647 -0.0069 0.0251  0.0155  42  TYR   A CD1 
969  C  CD2 A TYR   A 42  ? 0.1758 0.1629 0.1812 0.0166  0.0123  0.0245  42  TYR   A CD2 
970  C  CD2 B TYR   A 42  ? 0.1470 0.1623 0.1670 0.0021  0.0212  0.0158  42  TYR   A CD2 
971  C  CE1 A TYR   A 42  ? 0.1635 0.1669 0.1625 0.0062  0.0202  0.0390  42  TYR   A CE1 
972  C  CE1 B TYR   A 42  ? 0.1529 0.1645 0.1560 -0.0050 0.0264  0.0116  42  TYR   A CE1 
973  C  CE2 A TYR   A 42  ? 0.1789 0.1751 0.1786 0.0146  0.0114  0.0252  42  TYR   A CE2 
974  C  CE2 B TYR   A 42  ? 0.1491 0.1654 0.1696 -0.0057 0.0176  0.0136  42  TYR   A CE2 
975  C  CZ  A TYR   A 42  ? 0.1757 0.1797 0.1714 0.0060  0.0229  0.0300  42  TYR   A CZ  
976  C  CZ  B TYR   A 42  ? 0.1545 0.1675 0.1524 -0.0073 0.0231  0.0140  42  TYR   A CZ  
977  O  OH  A TYR   A 42  ? 0.1801 0.2034 0.1948 -0.0000 0.0209  0.0174  42  TYR   A OH  
978  O  OH  B TYR   A 42  ? 0.1614 0.1770 0.1731 -0.0043 0.0167  0.0095  42  TYR   A OH  
997  N  N   . LEU   A 43  ? 0.1330 0.1263 0.1536 -0.0040 0.0188  0.0099  43  LEU   A N   
998  C  CA  . LEU   A 43  ? 0.1276 0.1256 0.1444 -0.0060 0.0147  0.0062  43  LEU   A CA  
999  C  C   . LEU   A 43  ? 0.1298 0.1303 0.1474 -0.0022 0.0076  0.0059  43  LEU   A C   
1000 O  O   . LEU   A 43  ? 0.1477 0.1316 0.1634 0.0030  -0.0051 0.0001  43  LEU   A O   
1001 C  CB  . LEU   A 43  ? 0.1364 0.1221 0.1520 -0.0074 0.0101  0.0012  43  LEU   A CB  
1002 C  CG  . LEU   A 43  ? 0.1406 0.1262 0.1603 -0.0056 0.0053  0.0099  43  LEU   A CG  
1003 C  CD1 . LEU   A 43  ? 0.1507 0.1334 0.1765 -0.0068 -0.0051 0.0152  43  LEU   A CD1 
1004 C  CD2 . LEU   A 43  ? 0.1567 0.1296 0.1712 -0.0096 0.0109  0.0159  43  LEU   A CD2 
1017 N  N   A LYS   A 44  ? 0.1375 0.1270 0.1434 -0.0030 0.0099  0.0104  44  LYS   A N   
1018 N  N   B LYS   A 44  ? 0.1405 0.1356 0.1506 -0.0015 0.0104  0.0081  44  LYS   A N   
1019 C  CA  A LYS   A 44  ? 0.1440 0.1235 0.1416 -0.0040 0.0163  0.0140  44  LYS   A CA  
1020 C  CA  B LYS   A 44  ? 0.1489 0.1401 0.1601 0.0001  0.0148  0.0087  44  LYS   A CA  
1021 C  C   A LYS   A 44  ? 0.1356 0.1226 0.1313 0.0035  0.0032  0.0123  44  LYS   A C   
1022 C  C   B LYS   A 44  ? 0.1336 0.1341 0.1433 0.0041  0.0013  0.0135  44  LYS   A C   
1023 O  O   A LYS   A 44  ? 0.1478 0.1349 0.1495 -0.0000 0.0062  -0.0001 44  LYS   A O   
1024 O  O   B LYS   A 44  ? 0.1329 0.1433 0.1485 0.0010  -0.0017 0.0155  44  LYS   A O   
1025 C  CB  A LYS   A 44  ? 0.1641 0.1337 0.1558 -0.0057 0.0228  0.0294  44  LYS   A CB  
1026 C  CB  B LYS   A 44  ? 0.1770 0.1609 0.1999 0.0054  0.0266  0.0105  44  LYS   A CB  
1027 C  CG  A LYS   A 44  ? 0.1898 0.1535 0.1974 -0.0160 0.0336  0.0375  44  LYS   A CG  
1028 C  CG  B LYS   A 44  ? 0.2035 0.1916 0.2617 0.0058  0.0343  0.0165  44  LYS   A CG  
1029 C  CD  A LYS   A 44  ? 0.2299 0.1997 0.2833 -0.0193 0.0228  0.0265  44  LYS   A CD  
1030 C  CD  B LYS   A 44  ? 0.2313 0.2259 0.3349 -0.0002 0.0252  0.0122  44  LYS   A CD  
1031 C  CE  A LYS   A 44  ? 0.2468 0.2293 0.3309 -0.0212 0.0209  0.0262  44  LYS   A CE  
1032 C  CE  B LYS   A 44  ? 0.2420 0.2439 0.3819 -0.0039 0.0178  0.0105  44  LYS   A CE  
1033 N  NZ  A LYS   A 44  ? 0.2546 0.2479 0.3444 -0.0196 0.0195  0.0245  44  LYS   A NZ  
1034 N  NZ  B LYS   A 44  ? 0.2484 0.2517 0.4122 -0.0059 0.0166  0.0019  44  LYS   A NZ  
1061 N  N   . HIS   A 45  ? 0.1249 0.1233 0.1456 0.0025  0.0001  0.0154  45  HIS   A N   
1062 C  CA  . HIS   A 45  ? 0.1321 0.1261 0.1515 -0.0003 -0.0059 0.0130  45  HIS   A CA  
1063 C  C   . HIS   A 45  ? 0.1372 0.1378 0.1623 0.0016  0.0006  0.0099  45  HIS   A C   
1064 O  O   . HIS   A 45  ? 0.1627 0.1518 0.1956 0.0224  0.0018  -0.0013 45  HIS   A O   
1065 C  CB  . HIS   A 45  ? 0.1336 0.1269 0.1394 -0.0018 0.0040  0.0062  45  HIS   A CB  
1066 C  CG  . HIS   A 45  ? 0.1279 0.1265 0.1295 -0.0066 0.0059  0.0083  45  HIS   A CG  
1067 N  ND1 . HIS   A 45  ? 0.1212 0.1357 0.1448 -0.0042 0.0029  0.0151  45  HIS   A ND1 
1068 C  CD2 . HIS   A 45  ? 0.1287 0.1347 0.1429 -0.0117 -0.0017 0.0171  45  HIS   A CD2 
1069 C  CE1 . HIS   A 45  ? 0.1229 0.1422 0.1334 -0.0085 0.0009  0.0179  45  HIS   A CE1 
1070 N  NE2 . HIS   A 45  ? 0.1234 0.1457 0.1370 -0.0054 0.0012  0.0231  45  HIS   A NE2 
1079 N  N   A GLY   A 46  ? 0.1425 0.1486 0.1683 0.0054  -0.0052 0.0181  46  GLY   A N   
1080 N  N   B GLY   A 46  ? 0.1448 0.1411 0.1604 0.0045  -0.0050 0.0142  46  GLY   A N   
1081 C  CA  A GLY   A 46  ? 0.1436 0.1543 0.1864 0.0088  -0.0148 0.0289  46  GLY   A CA  
1082 C  CA  B GLY   A 46  ? 0.1490 0.1438 0.1660 0.0073  -0.0093 0.0195  46  GLY   A CA  
1083 C  C   A GLY   A 46  ? 0.1468 0.1509 0.1953 0.0146  -0.0179 0.0381  46  GLY   A C   
1084 C  C   B GLY   A 46  ? 0.1501 0.1413 0.1648 0.0090  -0.0102 0.0259  46  GLY   A C   
1085 O  O   A GLY   A 46  ? 0.1530 0.1506 0.2268 0.0214  -0.0234 0.0408  46  GLY   A O   
1086 O  O   B GLY   A 46  ? 0.1560 0.1463 0.1935 0.0040  -0.0159 0.0088  46  GLY   A O   
1093 N  N   A GLY   A 47  ? 0.1414 0.1487 0.1779 0.0121  -0.0123 0.0338  47  GLY   A N   
1094 N  N   B GLY   A 47  ? 0.1523 0.1413 0.1539 0.0112  -0.0017 0.0192  47  GLY   A N   
1095 C  CA  A GLY   A 47  ? 0.1439 0.1519 0.1745 0.0125  -0.0154 0.0274  47  GLY   A CA  
1096 C  CA  B GLY   A 47  ? 0.1481 0.1463 0.1593 0.0121  -0.0079 0.0145  47  GLY   A CA  
1097 C  C   A GLY   A 47  ? 0.1369 0.1517 0.1618 0.0110  -0.0214 0.0160  47  GLY   A C   
1098 C  C   B GLY   A 47  ? 0.1384 0.1415 0.1401 0.0129  -0.0033 0.0093  47  GLY   A C   
1099 O  O   A GLY   A 47  ? 0.1331 0.1457 0.1821 0.0111  -0.0224 0.0251  47  GLY   A O   
1100 O  O   B GLY   A 47  ? 0.1346 0.1309 0.1436 0.0091  -0.0035 0.0230  47  GLY   A O   
1107 N  N   A GLY   A 48  ? 0.1362 0.1550 0.1583 0.0157  -0.0115 0.0047  48  GLY   A N   
1108 N  N   B GLY   A 48  ? 0.1351 0.1465 0.1384 0.0156  0.0042  0.0133  48  GLY   A N   
1109 C  CA  A GLY   A 48  ? 0.1260 0.1492 0.1591 0.0040  -0.0110 -0.0029 48  GLY   A CA  
1110 C  CA  B GLY   A 48  ? 0.1268 0.1383 0.1284 0.0129  0.0123  0.0055  48  GLY   A CA  
1111 C  C   A GLY   A 48  ? 0.1273 0.1375 0.1473 0.0011  0.0021  0.0022  48  GLY   A C   
1112 C  C   B GLY   A 48  ? 0.1337 0.1360 0.1338 0.0086  0.0121  0.0066  48  GLY   A C   
1113 O  O   A GLY   A 48  ? 0.1470 0.1380 0.1449 0.0026  0.0006  0.0001  48  GLY   A O   
1114 O  O   B GLY   A 48  ? 0.1485 0.1400 0.1261 0.0082  0.0142  0.0037  48  GLY   A O   
1121 N  N   A VAL   A 49  ? 0.1240 0.1264 0.1647 -0.0039 -0.0083 0.0027  49  VAL   A N   
1122 N  N   B VAL   A 49  ? 0.1256 0.1318 0.1354 0.0075  0.0014  -0.0011 49  VAL   A N   
1123 C  CA  A VAL   A 49  ? 0.1365 0.1290 0.1610 -0.0051 0.0021  0.0077  49  VAL   A CA  
1124 C  CA  B VAL   A 49  ? 0.1226 0.1407 0.1299 0.0036  0.0061  0.0041  49  VAL   A CA  
1125 C  C   A VAL   A 49  ? 0.1368 0.1199 0.1370 -0.0032 0.0058  0.0173  49  VAL   A C   
1126 C  C   B VAL   A 49  ? 0.1216 0.1388 0.1214 0.0057  0.0084  -0.0082 49  VAL   A C   
1127 O  O   A VAL   A 49  ? 0.1439 0.1250 0.1397 -0.0147 0.0121  0.0027  49  VAL   A O   
1128 O  O   B VAL   A 49  ? 0.1252 0.1483 0.1240 0.0046  0.0127  -0.0032 49  VAL   A O   
1129 C  CB  A VAL   A 49  ? 0.1496 0.1273 0.1906 -0.0036 -0.0020 0.0022  49  VAL   A CB  
1130 C  CB  B VAL   A 49  ? 0.1146 0.1400 0.1448 0.0083  0.0094  0.0072  49  VAL   A CB  
1131 C  CG1 A VAL   A 49  ? 0.1519 0.1254 0.2032 0.0003  0.0014  -0.0065 49  VAL   A CG1 
1132 C  CG1 B VAL   A 49  ? 0.1009 0.1329 0.1388 0.0141  0.0063  0.0109  49  VAL   A CG1 
1133 C  CG2 A VAL   A 49  ? 0.1631 0.1308 0.2204 -0.0204 -0.0113 0.0061  49  VAL   A CG2 
1134 C  CG2 B VAL   A 49  ? 0.1232 0.1472 0.1621 0.0048  0.0086  0.0066  49  VAL   A CG2 
1153 N  N   A ALA   A 50  ? 0.1333 0.1158 0.1367 -0.0049 -0.0042 0.0171  50  ALA   A N   
1154 N  N   B ALA   A 50  ? 0.1241 0.1333 0.1194 0.0057  -0.0009 -0.0119 50  ALA   A N   
1155 C  CA  A ALA   A 50  ? 0.1258 0.1186 0.1379 -0.0104 0.0028  0.0186  50  ALA   A CA  
1156 C  CA  B ALA   A 50  ? 0.1228 0.1302 0.1249 0.0018  0.0010  -0.0077 50  ALA   A CA  
1157 C  C   A ALA   A 50  ? 0.1209 0.1180 0.1338 -0.0074 0.0000  0.0129  50  ALA   A C   
1158 C  C   B ALA   A 50  ? 0.1273 0.1289 0.1161 0.0009  0.0052  -0.0058 50  ALA   A C   
1159 O  O   A ALA   A 50  ? 0.1251 0.1247 0.1484 -0.0030 -0.0055 0.0048  50  ALA   A O   
1160 O  O   B ALA   A 50  ? 0.1301 0.1331 0.1193 -0.0013 0.0160  -0.0073 50  ALA   A O   
1161 C  CB  A ALA   A 50  ? 0.1258 0.1252 0.1242 -0.0148 0.0019  0.0100  50  ALA   A CB  
1162 C  CB  B ALA   A 50  ? 0.1243 0.1279 0.1240 0.0093  -0.0005 -0.0031 50  ALA   A CB  
1173 N  N   A GLY   A 51  ? 0.1256 0.1223 0.1440 0.0055  -0.0025 0.0108  51  GLY   A N   
1174 N  N   B GLY   A 51  ? 0.1332 0.1300 0.1356 0.0044  -0.0029 -0.0033 51  GLY   A N   
1175 C  CA  A GLY   A 51  ? 0.1379 0.1198 0.1472 0.0045  -0.0050 0.0132  51  GLY   A CA  
1176 C  CA  B GLY   A 51  ? 0.1420 0.1279 0.1406 0.0025  -0.0071 0.0007  51  GLY   A CA  
1177 C  C   A GLY   A 51  ? 0.1276 0.1235 0.1529 0.0020  0.0014  0.0006  51  GLY   A C   
1178 C  C   B GLY   A 51  ? 0.1328 0.1302 0.1496 0.0002  -0.0041 -0.0049 51  GLY   A C   
1179 O  O   A GLY   A 51  ? 0.1289 0.1345 0.1722 -0.0022 0.0026  -0.0082 51  GLY   A O   
1180 O  O   B GLY   A 51  ? 0.1321 0.1373 0.1628 -0.0018 -0.0134 -0.0099 51  GLY   A O   
1187 N  N   . ALA   A 52  ? 0.1288 0.1357 0.1468 -0.0021 0.0059  -0.0135 52  ALA   A N   
1188 C  CA  . ALA   A 52  ? 0.1289 0.1466 0.1598 -0.0024 0.0070  -0.0145 52  ALA   A CA  
1189 C  C   . ALA   A 52  ? 0.1271 0.1446 0.1410 -0.0140 0.0118  -0.0113 52  ALA   A C   
1190 O  O   . ALA   A 52  ? 0.1352 0.1582 0.1625 -0.0085 0.0108  -0.0220 52  ALA   A O   
1191 C  CB  . ALA   A 52  ? 0.1376 0.1768 0.1753 -0.0109 -0.0030 -0.0051 52  ALA   A CB  
1198 N  N   A LEU   A 53  ? 0.1291 0.1482 0.1408 -0.0106 0.0108  -0.0031 53  LEU   A N   
1199 N  N   B LEU   A 53  ? 0.1245 0.1480 0.1377 -0.0096 0.0089  -0.0090 53  LEU   A N   
1200 C  CA  A LEU   A 53  ? 0.1400 0.1478 0.1329 -0.0088 0.0130  0.0032  53  LEU   A CA  
1201 C  CA  B LEU   A 53  ? 0.1310 0.1475 0.1271 -0.0068 0.0084  -0.0071 53  LEU   A CA  
1202 C  C   A LEU   A 53  ? 0.1435 0.1491 0.1265 -0.0025 0.0099  0.0037  53  LEU   A C   
1203 C  C   B LEU   A 53  ? 0.1368 0.1479 0.1132 0.0019  0.0081  -0.0032 53  LEU   A C   
1204 O  O   A LEU   A 53  ? 0.1446 0.1563 0.1504 -0.0131 0.0091  0.0029  53  LEU   A O   
1205 O  O   B LEU   A 53  ? 0.1407 0.1522 0.1152 0.0005  0.0076  0.0006  53  LEU   A O   
1206 C  CB  A LEU   A 53  ? 0.1475 0.1460 0.1295 -0.0114 0.0142  0.0112  53  LEU   A CB  
1207 C  CB  B LEU   A 53  ? 0.1309 0.1464 0.1257 -0.0129 0.0040  -0.0053 53  LEU   A CB  
1208 C  CG  A LEU   A 53  ? 0.1426 0.1484 0.1397 -0.0097 0.0125  0.0122  53  LEU   A CG  
1209 C  CG  B LEU   A 53  ? 0.1282 0.1488 0.1295 -0.0118 -0.0019 -0.0057 53  LEU   A CG  
1210 C  CD1 A LEU   A 53  ? 0.1364 0.1527 0.1408 -0.0086 0.0091  0.0175  53  LEU   A CD1 
1211 C  CD1 B LEU   A 53  ? 0.1254 0.1542 0.1288 -0.0148 -0.0042 -0.0038 53  LEU   A CD1 
1212 C  CD2 A LEU   A 53  ? 0.1491 0.1650 0.1534 -0.0149 0.0125  0.0203  53  LEU   A CD2 
1213 C  CD2 B LEU   A 53  ? 0.1300 0.1508 0.1300 -0.0091 0.0026  -0.0110 53  LEU   A CD2 
1236 N  N   A ASN   A 54  ? 0.1337 0.1400 0.1222 -0.0050 0.0010  0.0062  54  ASN   A N   
1237 N  N   B ASN   A 54  ? 0.1299 0.1443 0.1170 0.0012  0.0039  -0.0034 54  ASN   A N   
1238 C  CA  A ASN   A 54  ? 0.1278 0.1373 0.1434 -0.0121 -0.0037 0.0018  54  ASN   A CA  
1239 C  CA  B ASN   A 54  ? 0.1260 0.1465 0.1321 -0.0027 0.0023  -0.0081 54  ASN   A CA  
1240 C  C   A ASN   A 54  ? 0.1320 0.1441 0.1485 -0.0104 0.0069  0.0021  54  ASN   A C   
1241 C  C   B ASN   A 54  ? 0.1309 0.1493 0.1407 -0.0075 0.0076  -0.0071 54  ASN   A C   
1242 O  O   A ASN   A 54  ? 0.1360 0.1478 0.1501 -0.0048 0.0040  -0.0092 54  ASN   A O   
1243 O  O   B ASN   A 54  ? 0.1338 0.1517 0.1416 -0.0082 0.0024  -0.0191 54  ASN   A O   
1244 C  CB  A ASN   A 54  ? 0.1241 0.1306 0.1529 -0.0142 -0.0122 -0.0001 54  ASN   A CB  
1245 C  CB  B ASN   A 54  ? 0.1238 0.1456 0.1344 0.0084  0.0009  -0.0078 54  ASN   A CB  
1246 C  CG  A ASN   A 54  ? 0.1251 0.1269 0.1542 -0.0119 -0.0072 0.0073  54  ASN   A CG  
1247 C  CG  B ASN   A 54  ? 0.1222 0.1451 0.1339 0.0165  0.0065  -0.0081 54  ASN   A CG  
1248 O  OD1 A ASN   A 54  ? 0.1264 0.1283 0.1561 -0.0183 -0.0063 0.0231  54  ASN   A OD1 
1249 O  OD1 B ASN   A 54  ? 0.1211 0.1496 0.1379 0.0160  0.0042  -0.0182 54  ASN   A OD1 
1250 N  ND2 A ASN   A 54  ? 0.1255 0.1311 0.1766 -0.0190 -0.0205 0.0075  54  ASN   A ND2 
1251 N  ND2 B ASN   A 54  ? 0.1309 0.1498 0.1546 0.0102  0.0000  0.0029  54  ASN   A ND2 
1264 N  N   . LYS   A 55  ? 0.1328 0.1459 0.1490 -0.0047 0.0033  -0.0115 55  LYS   A N   
1265 C  CA  . LYS   A 55  ? 0.1482 0.1511 0.1583 0.0016  0.0002  -0.0181 55  LYS   A CA  
1266 C  C   . LYS   A 55  ? 0.1443 0.1572 0.1593 0.0000  0.0108  -0.0270 55  LYS   A C   
1267 O  O   . LYS   A 55  ? 0.1523 0.1675 0.1651 -0.0006 0.0044  -0.0320 55  LYS   A O   
1268 C  CB  . LYS   A 55  ? 0.1483 0.1637 0.1824 0.0150  -0.0054 -0.0223 55  LYS   A CB  
1269 C  CG  . LYS   A 55  ? 0.1653 0.1962 0.1985 0.0271  -0.0142 -0.0280 55  LYS   A CG  
1270 C  CD  . LYS   A 55  ? 0.1779 0.2387 0.2126 0.0415  -0.0133 -0.0345 55  LYS   A CD  
1271 C  CE  . LYS   A 55  ? 0.1981 0.2777 0.2306 0.0530  -0.0234 -0.0445 55  LYS   A CE  
1272 N  NZ  . LYS   A 55  ? 0.2071 0.2893 0.2308 0.0666  -0.0339 -0.0421 55  LYS   A NZ  
1287 N  N   . ALA   A 56  ? 0.1471 0.1664 0.1659 -0.0088 0.0138  -0.0281 56  ALA   A N   
1288 C  CA  . ALA   A 56  ? 0.1548 0.1851 0.1602 -0.0158 0.0181  -0.0239 56  ALA   A CA  
1289 C  C   . ALA   A 56  ? 0.1581 0.2023 0.1417 -0.0150 0.0149  -0.0310 56  ALA   A C   
1290 O  O   . ALA   A 56  ? 0.1635 0.2319 0.1496 -0.0054 0.0254  -0.0223 56  ALA   A O   
1291 C  CB  . ALA   A 56  ? 0.1579 0.2041 0.1684 -0.0226 0.0152  -0.0091 56  ALA   A CB  
1297 N  N   . THR   A 57  ? 0.1464 0.1789 0.1370 -0.0169 0.0120  -0.0229 57  THR   A N   
1298 C  CA  . THR   A 57  ? 0.1498 0.1761 0.1337 -0.0144 0.0019  -0.0189 57  THR   A CA  
1299 C  C   . THR   A 57  ? 0.1512 0.1819 0.1412 -0.0090 0.0025  -0.0210 57  THR   A C   
1300 O  O   . THR   A 57  ? 0.1480 0.1833 0.1638 -0.0143 -0.0073 -0.0292 57  THR   A O   
1301 C  CB  . THR   A 57  ? 0.1476 0.1750 0.1409 -0.0138 0.0103  -0.0141 57  THR   A CB  
1302 O  OG1 . THR   A 57  ? 0.1345 0.1650 0.1439 -0.0109 0.0089  -0.0211 57  THR   A OG1 
1303 C  CG2 . THR   A 57  ? 0.1528 0.1742 0.1386 -0.0142 0.0051  -0.0056 57  THR   A CG2 
1311 N  N   . ASN   A 58  ? 0.1544 0.1757 0.1625 -0.0133 0.0062  -0.0362 58  ASN   A N   
1312 C  CA  . ASN   A 58  ? 0.1766 0.1681 0.1861 -0.0193 0.0123  -0.0431 58  ASN   A CA  
1313 C  C   . ASN   A 58  ? 0.1510 0.1547 0.1858 -0.0074 0.0028  -0.0308 58  ASN   A C   
1314 O  O   . ASN   A 58  ? 0.1516 0.1663 0.1937 -0.0182 0.0000  -0.0342 58  ASN   A O   
1315 C  CB  . ASN   A 58  ? 0.2312 0.1849 0.2322 -0.0259 0.0342  -0.0590 58  ASN   A CB  
1316 C  CG  . ASN   A 58  ? 0.2782 0.2099 0.3046 -0.0256 0.0373  -0.0498 58  ASN   A CG  
1317 O  OD1 . ASN   A 58  ? 0.3005 0.2011 0.3400 0.0078  0.0735  -0.0361 58  ASN   A OD1 
1318 N  ND2 . ASN   A 58  ? 0.2962 0.2332 0.3340 -0.0309 0.0252  -0.0519 58  ASN   A ND2 
1325 N  N   . ASN   A 59  ? 0.1297 0.1476 0.1736 -0.0089 -0.0063 -0.0181 59  ASN   A N   
1326 C  CA  . ASN   A 59  ? 0.1379 0.1392 0.1700 -0.0050 -0.0056 -0.0150 59  ASN   A CA  
1327 C  C   . ASN   A 59  ? 0.1366 0.1409 0.1589 -0.0031 -0.0053 -0.0103 59  ASN   A C   
1328 O  O   . ASN   A 59  ? 0.1349 0.1447 0.1573 -0.0080 0.0025  -0.0022 59  ASN   A O   
1329 C  CB  . ASN   A 59  ? 0.1451 0.1406 0.1708 -0.0038 -0.0196 -0.0187 59  ASN   A CB  
1330 C  CG  . ASN   A 59  ? 0.1472 0.1425 0.1678 -0.0037 -0.0249 -0.0026 59  ASN   A CG  
1331 O  OD1 . ASN   A 59  ? 0.1561 0.1470 0.1619 -0.0168 -0.0231 0.0035  59  ASN   A OD1 
1332 N  ND2 . ASN   A 59  ? 0.1516 0.1446 0.1856 -0.0108 -0.0113 0.0020  59  ASN   A ND2 
1339 N  N   . ALA   A 60  ? 0.1313 0.1476 0.1620 -0.0070 -0.0040 -0.0114 60  ALA   A N   
1340 C  CA  . ALA   A 60  ? 0.1334 0.1504 0.1589 -0.0054 -0.0119 -0.0053 60  ALA   A CA  
1341 C  C   . ALA   A 60  ? 0.1332 0.1440 0.1575 -0.0063 -0.0062 -0.0054 60  ALA   A C   
1342 O  O   . ALA   A 60  ? 0.1272 0.1445 0.1722 -0.0070 -0.0060 -0.0157 60  ALA   A O   
1343 C  CB  . ALA   A 60  ? 0.1464 0.1583 0.1647 -0.0066 -0.0156 -0.0177 60  ALA   A CB  
1349 N  N   . MET   A 61  ? 0.1263 0.1438 0.1482 -0.0057 0.0026  -0.0115 61  MET   A N   
1350 C  CA  . MET   A 61  ? 0.1330 0.1342 0.1436 -0.0059 0.0103  -0.0068 61  MET   A CA  
1351 C  C   . MET   A 61  ? 0.1281 0.1310 0.1467 -0.0068 0.0022  -0.0068 61  MET   A C   
1352 O  O   . MET   A 61  ? 0.1301 0.1342 0.1543 -0.0073 0.0102  -0.0012 61  MET   A O   
1353 C  CB  . MET   A 61  ? 0.1332 0.1411 0.1389 -0.0098 0.0062  -0.0090 61  MET   A CB  
1354 C  CG  . MET   A 61  ? 0.1318 0.1482 0.1569 -0.0076 0.0063  -0.0067 61  MET   A CG  
1355 S  SD  . MET   A 61  ? 0.1410 0.1457 0.1795 -0.0131 0.0051  -0.0182 61  MET   A SD  
1356 C  CE  . MET   A 61  ? 0.1614 0.1551 0.2021 -0.0163 0.0176  -0.0103 61  MET   A CE  
1366 N  N   . GLN   A 62  ? 0.1274 0.1280 0.1483 -0.0089 0.0056  -0.0035 62  GLN   A N   
1367 C  CA  . GLN   A 62  ? 0.1312 0.1244 0.1585 -0.0042 0.0039  -0.0016 62  GLN   A CA  
1368 C  C   . GLN   A 62  ? 0.1321 0.1176 0.1620 0.0005  0.0106  0.0018  62  GLN   A C   
1369 O  O   . GLN   A 62  ? 0.1348 0.1345 0.1583 -0.0015 0.0114  0.0010  62  GLN   A O   
1370 C  CB  . GLN   A 62  ? 0.1311 0.1253 0.1573 0.0002  0.0009  -0.0026 62  GLN   A CB  
1371 C  CG  . GLN   A 62  ? 0.1369 0.1265 0.1490 -0.0035 0.0012  0.0085  62  GLN   A CG  
1372 C  CD  . GLN   A 62  ? 0.1441 0.1329 0.1524 -0.0002 0.0077  0.0103  62  GLN   A CD  
1373 O  OE1 . GLN   A 62  ? 0.1423 0.1403 0.1690 -0.0022 0.0039  -0.0006 62  GLN   A OE1 
1374 N  NE2 . GLN   A 62  ? 0.1468 0.1344 0.1640 0.0006  0.0019  -0.0102 62  GLN   A NE2 
1383 N  N   . VAL   A 63  ? 0.1276 0.1314 0.1762 -0.0077 0.0144  -0.0181 63  VAL   A N   
1384 C  CA  . VAL   A 63  ? 0.1329 0.1386 0.1930 -0.0147 0.0044  -0.0136 63  VAL   A CA  
1385 C  C   . VAL   A 63  ? 0.1247 0.1424 0.1727 -0.0131 0.0018  -0.0125 63  VAL   A C   
1386 O  O   . VAL   A 63  ? 0.1261 0.1420 0.1880 -0.0159 0.0007  -0.0074 63  VAL   A O   
1387 C  CB  . VAL   A 63  ? 0.1432 0.1585 0.2141 -0.0141 0.0036  -0.0386 63  VAL   A CB  
1388 C  CG1 . VAL   A 63  ? 0.1633 0.1802 0.2484 -0.0126 -0.0071 -0.0564 63  VAL   A CG1 
1389 C  CG2 . VAL   A 63  ? 0.1560 0.1532 0.2332 -0.0182 0.0106  -0.0390 63  VAL   A CG2 
1399 N  N   . GLU   A 64  ? 0.1271 0.1470 0.1623 -0.0048 -0.0008 -0.0104 64  GLU   A N   
1400 C  CA  . GLU   A 64  ? 0.1276 0.1471 0.1648 -0.0078 -0.0038 0.0005  64  GLU   A CA  
1401 C  C   . GLU   A 64  ? 0.1210 0.1414 0.1600 -0.0082 0.0009  0.0047  64  GLU   A C   
1402 O  O   . GLU   A 64  ? 0.1250 0.1468 0.1688 -0.0015 0.0025  -0.0048 64  GLU   A O   
1403 C  CB  . GLU   A 64  ? 0.1367 0.1579 0.1635 -0.0111 0.0070  -0.0050 64  GLU   A CB  
1404 C  CG  . GLU   A 64  ? 0.1464 0.1598 0.1770 -0.0130 0.0109  -0.0054 64  GLU   A CG  
1405 C  CD  . GLU   A 64  ? 0.1564 0.1644 0.1777 -0.0215 0.0104  -0.0046 64  GLU   A CD  
1406 O  OE1 . GLU   A 64  ? 0.1537 0.1791 0.1978 -0.0269 0.0187  -0.0063 64  GLU   A OE1 
1407 O  OE2 . GLU   A 64  ? 0.1726 0.1659 0.1769 -0.0280 -0.0024 0.0078  64  GLU   A OE2 
1414 N  N   . SER   A 65  ? 0.1219 0.1382 0.1531 -0.0006 -0.0008 0.0015  65  SER   A N   
1415 C  CA  . SER   A 65  ? 0.1267 0.1284 0.1517 -0.0063 -0.0037 -0.0005 65  SER   A CA  
1416 C  C   . SER   A 65  ? 0.1262 0.1364 0.1546 -0.0054 -0.0024 -0.0008 65  SER   A C   
1417 O  O   . SER   A 65  ? 0.1345 0.1431 0.1766 0.0010  0.0155  -0.0060 65  SER   A O   
1418 C  CB  . SER   A 65  ? 0.1291 0.1281 0.1455 -0.0078 0.0085  0.0067  65  SER   A CB  
1419 O  OG  . SER   A 65  ? 0.1258 0.1468 0.1608 -0.0082 -0.0072 0.0109  65  SER   A OG  
1425 N  N   . ASP   A 66  ? 0.1283 0.1347 0.1595 -0.0050 0.0144  0.0033  66  ASP   A N   
1426 C  CA  . ASP   A 66  ? 0.1360 0.1478 0.1761 -0.0061 0.0106  0.0125  66  ASP   A CA  
1427 C  C   . ASP   A 66  ? 0.1336 0.1407 0.1805 -0.0102 0.0136  0.0102  66  ASP   A C   
1428 O  O   . ASP   A 66  ? 0.1385 0.1508 0.2026 -0.0040 0.0292  0.0184  66  ASP   A O   
1429 C  CB  . ASP   A 66  ? 0.1469 0.1532 0.2052 0.0018  0.0158  0.0286  66  ASP   A CB  
1430 C  CG  . ASP   A 66  ? 0.1701 0.1642 0.2297 -0.0043 0.0083  0.0446  66  ASP   A CG  
1431 O  OD1 . ASP   A 66  ? 0.1716 0.1967 0.2117 -0.0052 -0.0073 0.0431  66  ASP   A OD1 
1432 O  OD2 . ASP   A 66  ? 0.1862 0.1713 0.3211 0.0137  -0.0131 0.0293  66  ASP   A OD2 
1437 N  N   . ASP   A 67  ? 0.1344 0.1441 0.1826 -0.0043 0.0168  0.0131  67  ASP   A N   
1438 C  CA  . ASP   A 67  ? 0.1311 0.1565 0.1969 -0.0028 0.0079  0.0238  67  ASP   A CA  
1439 C  C   . ASP   A 67  ? 0.1325 0.1569 0.1946 0.0003  0.0122  0.0251  67  ASP   A C   
1440 O  O   . ASP   A 67  ? 0.1305 0.1656 0.2114 0.0014  0.0242  0.0279  67  ASP   A O   
1441 C  CB  . ASP   A 67  ? 0.1434 0.1651 0.2320 -0.0089 -0.0120 0.0264  67  ASP   A CB  
1442 C  CG  . ASP   A 67  ? 0.1399 0.1816 0.2652 -0.0093 -0.0331 0.0289  67  ASP   A CG  
1443 O  OD1 . ASP   A 67  ? 0.1447 0.1958 0.3386 -0.0143 -0.0366 0.0356  67  ASP   A OD1 
1444 O  OD2 . ASP   A 67  ? 0.1414 0.1842 0.2509 0.0005  -0.0130 0.0214  67  ASP   A OD2 
1449 N  N   . TYR   A 68  ? 0.1305 0.1450 0.1947 0.0024  0.0175  0.0290  68  TYR   A N   
1450 C  CA  . TYR   A 68  ? 0.1429 0.1426 0.1862 -0.0005 0.0172  0.0272  68  TYR   A CA  
1451 C  C   . TYR   A 68  ? 0.1371 0.1430 0.1868 -0.0017 0.0222  0.0173  68  TYR   A C   
1452 O  O   . TYR   A 68  ? 0.1421 0.1501 0.1986 0.0106  0.0315  0.0183  68  TYR   A O   
1453 C  CB  . TYR   A 68  ? 0.1500 0.1393 0.2006 0.0063  0.0380  0.0235  68  TYR   A CB  
1454 C  CG  . TYR   A 68  ? 0.1591 0.1541 0.2320 0.0031  0.0574  0.0287  68  TYR   A CG  
1455 C  CD1 . TYR   A 68  ? 0.1640 0.1639 0.2680 -0.0178 0.0481  -0.0062 68  TYR   A CD1 
1456 C  CD2 . TYR   A 68  ? 0.1797 0.1575 0.2707 0.0093  0.0653  0.0325  68  TYR   A CD2 
1457 C  CE1 . TYR   A 68  ? 0.1684 0.1700 0.3068 -0.0191 0.0526  -0.0134 68  TYR   A CE1 
1458 C  CE2 . TYR   A 68  ? 0.1729 0.1640 0.2909 0.0006  0.0790  0.0157  68  TYR   A CE2 
1459 C  CZ  . TYR   A 68  ? 0.1719 0.1670 0.3078 -0.0202 0.0573  -0.0118 68  TYR   A CZ  
1460 O  OH  . TYR   A 68  ? 0.1982 0.1677 0.3221 -0.0137 0.0265  -0.0288 68  TYR   A OH  
1470 N  N   . ILE   A 69  ? 0.1321 0.1365 0.1810 -0.0007 0.0086  0.0176  69  ILE   A N   
1471 C  CA  . ILE   A 69  ? 0.1399 0.1360 0.1719 0.0029  0.0104  0.0128  69  ILE   A CA  
1472 C  C   . ILE   A 69  ? 0.1396 0.1416 0.1680 0.0059  0.0203  0.0199  69  ILE   A C   
1473 O  O   . ILE   A 69  ? 0.1484 0.1507 0.1673 -0.0015 0.0272  0.0211  69  ILE   A O   
1474 C  CB  . ILE   A 69  ? 0.1482 0.1602 0.1755 0.0062  0.0135  0.0035  69  ILE   A CB  
1475 C  CG1 . ILE   A 69  ? 0.1448 0.1707 0.1857 0.0056  0.0149  -0.0107 69  ILE   A CG1 
1476 C  CG2 . ILE   A 69  ? 0.1687 0.1795 0.1877 0.0101  -0.0038 -0.0041 69  ILE   A CG2 
1477 C  CD1 . ILE   A 69  ? 0.1455 0.1815 0.1930 -0.0028 0.0163  -0.0152 69  ILE   A CD1 
1489 N  N   . ALA   A 70  ? 0.1448 0.1434 0.1815 -0.0058 0.0247  0.0208  70  ALA   A N   
1490 C  CA  . ALA   A 70  ? 0.1498 0.1545 0.2052 -0.0133 0.0345  0.0171  70  ALA   A CA  
1491 C  C   . ALA   A 70  ? 0.1479 0.1696 0.2041 -0.0101 0.0314  0.0184  70  ALA   A C   
1492 O  O   . ALA   A 70  ? 0.1608 0.2005 0.2221 0.0027  0.0465  0.0387  70  ALA   A O   
1493 C  CB  . ALA   A 70  ? 0.1549 0.1521 0.2300 -0.0186 0.0282  0.0146  70  ALA   A CB  
1499 N  N   . THR   A 71  ? 0.1429 0.1639 0.1877 -0.0063 0.0193  0.0220  71  THR   A N   
1500 C  CA  . THR   A 71  ? 0.1527 0.1851 0.2156 0.0109  0.0189  0.0236  71  THR   A CA  
1501 C  C   . THR   A 71  ? 0.1458 0.1769 0.2323 0.0132  0.0320  0.0223  71  THR   A C   
1502 O  O   . THR   A 71  ? 0.1465 0.1994 0.2734 0.0076  0.0397  -0.0031 71  THR   A O   
1503 C  CB  . THR   A 71  ? 0.1749 0.2045 0.2359 0.0130  -0.0093 0.0320  71  THR   A CB  
1504 O  OG1 . THR   A 71  ? 0.2014 0.2209 0.2377 0.0032  -0.0285 0.0186  71  THR   A OG1 
1505 C  CG2 . THR   A 71  ? 0.1884 0.2203 0.2683 0.0217  -0.0201 0.0439  71  THR   A CG2 
1513 N  N   . ASN   A 72  ? 0.1478 0.1590 0.2041 0.0097  0.0256  0.0232  72  ASN   A N   
1514 C  CA  . ASN   A 72  ? 0.1523 0.1602 0.2056 0.0136  0.0334  0.0173  72  ASN   A CA  
1515 C  C   . ASN   A 72  ? 0.1606 0.1554 0.1984 0.0042  0.0471  0.0102  72  ASN   A C   
1516 O  O   . ASN   A 72  ? 0.1759 0.1572 0.2384 0.0140  0.0351  -0.0001 72  ASN   A O   
1517 C  CB  . ASN   A 72  ? 0.1704 0.1630 0.2053 0.0106  0.0322  0.0219  72  ASN   A CB  
1518 C  CG  . ASN   A 72  ? 0.1944 0.1783 0.2158 0.0206  0.0297  0.0229  72  ASN   A CG  
1519 O  OD1 . ASN   A 72  ? 0.2083 0.2113 0.2338 0.0243  0.0392  0.0229  72  ASN   A OD1 
1520 N  ND2 . ASN   A 72  ? 0.2069 0.1779 0.2239 0.0477  0.0078  0.0135  72  ASN   A ND2 
1527 N  N   . GLY   A 73  ? 0.1637 0.1542 0.1889 0.0019  0.0400  0.0043  73  GLY   A N   
1528 C  CA  . GLY   A 73  ? 0.1698 0.1532 0.1792 -0.0004 0.0355  0.0088  73  GLY   A CA  
1529 C  C   . GLY   A 73  ? 0.1662 0.1444 0.1714 0.0012  0.0443  0.0224  73  GLY   A C   
1530 O  O   . GLY   A 73  ? 0.1643 0.1566 0.1813 0.0121  0.0364  0.0278  73  GLY   A O   
1534 N  N   . PRO   A 74  ? 0.1735 0.1530 0.1755 -0.0121 0.0454  0.0147  74  PRO   A N   
1535 C  CA  . PRO   A 74  ? 0.1645 0.1501 0.1867 -0.0003 0.0372  0.0151  74  PRO   A CA  
1536 C  C   . PRO   A 74  ? 0.1573 0.1378 0.1855 0.0026  0.0315  -0.0004 74  PRO   A C   
1537 O  O   . PRO   A 74  ? 0.1668 0.1396 0.2019 0.0080  0.0327  -0.0050 74  PRO   A O   
1538 C  CB  . PRO   A 74  ? 0.1818 0.1736 0.2048 0.0074  0.0452  0.0235  74  PRO   A CB  
1539 C  CG  . PRO   A 74  ? 0.2113 0.2082 0.2473 -0.0148 0.0334  0.0155  74  PRO   A CG  
1540 C  CD  . PRO   A 74  ? 0.1930 0.1869 0.1961 -0.0222 0.0366  0.0091  74  PRO   A CD  
1548 N  N   . LEU   A 75  ? 0.1546 0.1285 0.1756 0.0046  0.0195  -0.0014 75  LEU   A N   
1549 C  CA  . LEU   A 75  ? 0.1645 0.1270 0.1518 0.0023  0.0108  0.0012  75  LEU   A CA  
1550 C  C   . LEU   A 75  ? 0.1754 0.1380 0.1538 0.0068  0.0115  0.0075  75  LEU   A C   
1551 O  O   . LEU   A 75  ? 0.1995 0.1526 0.1580 0.0171  0.0077  0.0043  75  LEU   A O   
1552 C  CB  . LEU   A 75  ? 0.1677 0.1318 0.1564 -0.0064 0.0095  0.0137  75  LEU   A CB  
1553 C  CG  . LEU   A 75  ? 0.1797 0.1632 0.1628 -0.0341 0.0072  0.0126  75  LEU   A CG  
1554 C  CD1 . LEU   A 75  ? 0.1885 0.2124 0.1817 -0.0298 -0.0017 -0.0032 75  LEU   A CD1 
1555 C  CD2 . LEU   A 75  ? 0.2071 0.2048 0.2117 -0.0123 0.0101  0.0112  75  LEU   A CD2 
1567 N  N   . LYS   A 76  ? 0.1740 0.1362 0.1655 0.0009  0.0118  -0.0041 76  LYS   A N   
1568 C  CA  . LYS   A 76  ? 0.1693 0.1619 0.1784 -0.0094 0.0133  -0.0200 76  LYS   A CA  
1569 C  C   . LYS   A 76  ? 0.1646 0.1408 0.1418 -0.0009 0.0122  0.0035  76  LYS   A C   
1570 O  O   . LYS   A 76  ? 0.1690 0.1390 0.1389 0.0002  0.0185  0.0108  76  LYS   A O   
1571 C  CB  . LYS   A 76  ? 0.1697 0.1839 0.2306 0.0001  0.0115  -0.0447 76  LYS   A CB  
1572 C  CG  . LYS   A 76  ? 0.1806 0.1795 0.2894 0.0077  0.0103  -0.0434 76  LYS   A CG  
1573 C  CD  . LYS   A 76  ? 0.1880 0.1786 0.3416 0.0080  0.0028  -0.0523 76  LYS   A CD  
1574 C  CE  . LYS   A 76  ? 0.2065 0.2002 0.3999 -0.0009 0.0114  -0.0517 76  LYS   A CE  
1575 N  NZ  . LYS   A 76  ? 0.2093 0.1940 0.4373 -0.0181 0.0038  -0.0585 76  LYS   A NZ  
1589 N  N   . VAL   A 77  ? 0.1751 0.1475 0.1475 0.0036  0.0229  0.0075  77  VAL   A N   
1590 C  CA  . VAL   A 77  ? 0.1715 0.1535 0.1423 0.0090  0.0202  0.0035  77  VAL   A CA  
1591 C  C   . VAL   A 77  ? 0.1657 0.1481 0.1410 0.0080  0.0155  0.0005  77  VAL   A C   
1592 O  O   . VAL   A 77  ? 0.1714 0.1488 0.1512 0.0114  0.0310  -0.0133 77  VAL   A O   
1593 C  CB  . VAL   A 77  ? 0.1904 0.1753 0.1448 0.0025  0.0155  0.0202  77  VAL   A CB  
1594 C  CG1 . VAL   A 77  ? 0.1847 0.1948 0.1590 0.0101  0.0058  0.0093  77  VAL   A CG1 
1595 C  CG2 . VAL   A 77  ? 0.2181 0.1883 0.1663 -0.0020 0.0008  0.0233  77  VAL   A CG2 
1605 N  N   . GLY   A 78  ? 0.1594 0.1443 0.1346 0.0101  0.0219  0.0014  78  GLY   A N   
1606 C  CA  . GLY   A 78  ? 0.1609 0.1395 0.1462 0.0044  0.0193  0.0080  78  GLY   A CA  
1607 C  C   . GLY   A 78  ? 0.1479 0.1319 0.1472 0.0087  0.0180  0.0074  78  GLY   A C   
1608 O  O   . GLY   A 78  ? 0.1464 0.1384 0.1701 0.0049  0.0142  0.0212  78  GLY   A O   
1612 N  N   . GLY   A 79  ? 0.1538 0.1301 0.1485 0.0029  0.0135  0.0111  79  GLY   A N   
1613 C  CA  . GLY   A 79  ? 0.1492 0.1289 0.1648 0.0048  0.0158  0.0046  79  GLY   A CA  
1614 C  C   . GLY   A 79  ? 0.1358 0.1278 0.1561 -0.0037 0.0099  0.0088  79  GLY   A C   
1615 O  O   . GLY   A 79  ? 0.1386 0.1420 0.1674 0.0177  0.0132  0.0063  79  GLY   A O   
1619 N  N   . SER   A 80  ? 0.1332 0.1436 0.1698 0.0019  0.0126  -0.0032 80  SER   A N   
1620 C  CA  . SER   A 80  ? 0.1322 0.1344 0.1617 -0.0026 0.0089  0.0047  80  SER   A CA  
1621 C  C   . SER   A 80  ? 0.1276 0.1381 0.1609 -0.0040 0.0045  0.0084  80  SER   A C   
1622 O  O   . SER   A 80  ? 0.1294 0.1614 0.1866 0.0034  0.0097  -0.0025 80  SER   A O   
1623 C  CB  . SER   A 80  ? 0.1472 0.1372 0.1900 -0.0087 0.0071  0.0057  80  SER   A CB  
1624 O  OG  . SER   A 80  ? 0.1701 0.1381 0.2217 0.0050  -0.0029 0.0227  80  SER   A OG  
1630 N  N   . CYS   A 81  ? 0.1255 0.1345 0.1532 -0.0056 -0.0068 0.0153  81  CYS   A N   
1631 C  CA  . CYS   A 81  ? 0.1262 0.1456 0.1521 -0.0063 -0.0055 0.0274  81  CYS   A CA  
1632 C  C   . CYS   A 81  ? 0.1240 0.1410 0.1559 -0.0123 -0.0016 0.0286  81  CYS   A C   
1633 O  O   . CYS   A 81  ? 0.1242 0.1692 0.1730 -0.0012 0.0026  0.0310  81  CYS   A O   
1634 C  CB  . CYS   A 81  ? 0.1320 0.1520 0.1640 -0.0140 -0.0018 0.0244  81  CYS   A CB  
1635 S  SG  . CYS   A 81  ? 0.1480 0.1404 0.1585 -0.0155 0.0018  0.0116  81  CYS   A SG  
1641 N  N   . VAL   A 82  ? 0.1301 0.1453 0.1552 -0.0055 -0.0124 0.0202  82  VAL   A N   
1642 C  CA  . VAL   A 82  ? 0.1472 0.1539 0.1473 -0.0028 -0.0096 0.0302  82  VAL   A CA  
1643 C  C   . VAL   A 82  ? 0.1423 0.1583 0.1500 -0.0061 -0.0062 0.0247  82  VAL   A C   
1644 O  O   . VAL   A 82  ? 0.1346 0.1668 0.1836 -0.0037 -0.0034 0.0081  82  VAL   A O   
1645 C  CB  . VAL   A 82  ? 0.1728 0.1667 0.1617 -0.0013 0.0004  0.0331  82  VAL   A CB  
1646 C  CG1 . VAL   A 82  ? 0.1953 0.1820 0.1806 0.0055  0.0029  0.0221  82  VAL   A CG1 
1647 C  CG2 . VAL   A 82  ? 0.1777 0.1702 0.1907 -0.0077 -0.0062 0.0287  82  VAL   A CG2 
1657 N  N   . LEU   A 83  ? 0.1356 0.1545 0.1421 -0.0116 -0.0078 0.0077  83  LEU   A N   
1658 C  CA  . LEU   A 83  ? 0.1345 0.1569 0.1398 -0.0138 -0.0061 0.0094  83  LEU   A CA  
1659 C  C   . LEU   A 83  ? 0.1439 0.1628 0.1322 -0.0157 -0.0096 0.0149  83  LEU   A C   
1660 O  O   . LEU   A 83  ? 0.1482 0.1648 0.1491 -0.0207 -0.0041 0.0175  83  LEU   A O   
1661 C  CB  . LEU   A 83  ? 0.1436 0.1618 0.1467 -0.0125 -0.0082 0.0123  83  LEU   A CB  
1662 C  CG  . LEU   A 83  ? 0.1589 0.1686 0.1498 -0.0132 0.0047  0.0030  83  LEU   A CG  
1663 C  CD1 . LEU   A 83  ? 0.1752 0.1709 0.1628 -0.0219 0.0007  0.0235  83  LEU   A CD1 
1664 C  CD2 . LEU   A 83  ? 0.1618 0.1860 0.1627 -0.0104 0.0135  0.0085  83  LEU   A CD2 
1676 N  N   . SER   A 84  ? 0.1557 0.1675 0.1367 -0.0205 -0.0102 0.0197  84  SER   A N   
1677 C  CA  . SER   A 84  ? 0.1689 0.1756 0.1300 -0.0180 -0.0110 0.0167  84  SER   A CA  
1678 C  C   . SER   A 84  ? 0.1747 0.1727 0.1249 -0.0237 0.0029  0.0122  84  SER   A C   
1679 O  O   . SER   A 84  ? 0.1665 0.1836 0.1212 -0.0234 -0.0006 0.0064  84  SER   A O   
1680 C  CB  . SER   A 84  ? 0.1753 0.1949 0.1392 -0.0168 -0.0109 0.0036  84  SER   A CB  
1681 O  OG  . SER   A 84  ? 0.1779 0.2102 0.1577 -0.0189 -0.0116 -0.0078 84  SER   A OG  
1687 N  N   . GLY   A 85  ? 0.1857 0.1864 0.1365 -0.0251 0.0070  0.0078  85  GLY   A N   
1688 C  CA  . GLY   A 85  ? 0.1873 0.1942 0.1422 -0.0313 0.0082  -0.0013 85  GLY   A CA  
1689 C  C   . GLY   A 85  ? 0.1849 0.2012 0.1300 -0.0303 0.0041  0.0028  85  GLY   A C   
1690 O  O   . GLY   A 85  ? 0.1865 0.2074 0.1448 -0.0371 0.0186  -0.0141 85  GLY   A O   
1694 N  N   . HIS   A 86  ? 0.1828 0.1945 0.1245 -0.0287 -0.0046 0.0034  86  HIS   A N   
1695 C  CA  . HIS   A 86  ? 0.1963 0.2017 0.1271 -0.0300 0.0024  0.0033  86  HIS   A CA  
1696 C  C   . HIS   A 86  ? 0.2155 0.2170 0.1246 -0.0316 -0.0001 -0.0064 86  HIS   A C   
1697 O  O   . HIS   A 86  ? 0.2199 0.2407 0.1302 -0.0247 0.0080  0.0010  86  HIS   A O   
1698 C  CB  . HIS   A 86  ? 0.1960 0.1873 0.1346 -0.0229 0.0093  0.0028  86  HIS   A CB  
1699 C  CG  . HIS   A 86  ? 0.1865 0.1852 0.1406 -0.0112 0.0033  0.0069  86  HIS   A CG  
1700 N  ND1 . HIS   A 86  ? 0.1949 0.1828 0.1744 -0.0231 0.0009  0.0018  86  HIS   A ND1 
1701 C  CD2 . HIS   A 86  ? 0.1841 0.1764 0.1318 0.0007  0.0051  0.0105  86  HIS   A CD2 
1702 C  CE1 . HIS   A 86  ? 0.1920 0.1786 0.1660 -0.0181 0.0192  0.0065  86  HIS   A CE1 
1703 N  NE2 . HIS   A 86  ? 0.1858 0.1718 0.1494 -0.0031 0.0208  0.0184  86  HIS   A NE2 
1711 N  N   A ASN   A 87  ? 0.2291 0.2279 0.1330 -0.0300 0.0177  -0.0081 87  ASN   A N   
1712 N  N   B ASN   A 87  ? 0.2208 0.2219 0.1377 -0.0304 0.0167  -0.0174 87  ASN   A N   
1713 C  CA  A ASN   A 87  ? 0.2445 0.2368 0.1340 -0.0217 0.0442  -0.0054 87  ASN   A CA  
1714 C  CA  B ASN   A 87  ? 0.2282 0.2255 0.1483 -0.0229 0.0403  -0.0258 87  ASN   A CA  
1715 C  C   A ASN   A 87  ? 0.2423 0.2450 0.1461 -0.0248 0.0602  0.0075  87  ASN   A C   
1716 C  C   B ASN   A 87  ? 0.2195 0.2293 0.1559 -0.0205 0.0411  -0.0177 87  ASN   A C   
1717 O  O   A ASN   A 87  ? 0.2592 0.2553 0.1730 -0.0270 0.0825  0.0110  87  ASN   A O   
1718 O  O   B ASN   A 87  ? 0.2247 0.2290 0.1639 -0.0194 0.0433  -0.0106 87  ASN   A O   
1719 C  CB  A ASN   A 87  ? 0.2608 0.2449 0.1414 -0.0152 0.0415  -0.0042 87  ASN   A CB  
1720 C  CB  B ASN   A 87  ? 0.2457 0.2320 0.1601 -0.0212 0.0513  -0.0304 87  ASN   A CB  
1721 C  CG  A ASN   A 87  ? 0.2730 0.2558 0.1520 -0.0097 0.0383  0.0017  87  ASN   A CG  
1722 C  CG  B ASN   A 87  ? 0.2579 0.2413 0.1618 -0.0197 0.0675  -0.0273 87  ASN   A CG  
1723 O  OD1 A ASN   A 87  ? 0.2805 0.2565 0.1527 0.0031  0.0272  0.0121  87  ASN   A OD1 
1724 O  OD1 B ASN   A 87  ? 0.2671 0.2425 0.1639 -0.0119 0.0694  -0.0251 87  ASN   A OD1 
1725 N  ND2 A ASN   A 87  ? 0.2783 0.2713 0.1671 -0.0092 0.0341  0.0041  87  ASN   A ND2 
1726 N  ND2 B ASN   A 87  ? 0.2622 0.2544 0.1712 -0.0174 0.0708  -0.0222 87  ASN   A ND2 
1739 N  N   A LEU   A 88  ? 0.2219 0.2392 0.1490 -0.0300 0.0411  0.0153  88  LEU   A N   
1740 N  N   B LEU   A 88  ? 0.2062 0.2308 0.1583 -0.0251 0.0334  -0.0138 88  LEU   A N   
1741 C  CA  A LEU   A 88  ? 0.2060 0.2343 0.1698 -0.0375 0.0300  0.0253  88  LEU   A CA  
1742 C  CA  B LEU   A 88  ? 0.1965 0.2319 0.1698 -0.0303 0.0297  -0.0032 88  LEU   A CA  
1743 C  C   A LEU   A 88  ? 0.2011 0.2344 0.1665 -0.0357 0.0284  0.0263  88  LEU   A C   
1744 C  C   B LEU   A 88  ? 0.1957 0.2330 0.1627 -0.0333 0.0293  0.0087  88  LEU   A C   
1745 O  O   A LEU   A 88  ? 0.2044 0.2344 0.1870 -0.0353 0.0329  0.0432  88  LEU   A O   
1746 O  O   B LEU   A 88  ? 0.1978 0.2342 0.1829 -0.0354 0.0329  0.0155  88  LEU   A O   
1747 C  CB  A LEU   A 88  ? 0.2081 0.2345 0.1845 -0.0442 0.0081  0.0356  88  LEU   A CB  
1748 C  CB  B LEU   A 88  ? 0.1984 0.2342 0.1768 -0.0310 0.0182  -0.0073 88  LEU   A CB  
1749 C  CG  A LEU   A 88  ? 0.2215 0.2416 0.2142 -0.0450 -0.0008 0.0370  88  LEU   A CG  
1750 C  CG  B LEU   A 88  ? 0.2086 0.2407 0.1946 -0.0275 0.0157  -0.0123 88  LEU   A CG  
1751 C  CD1 A LEU   A 88  ? 0.2280 0.2452 0.2190 -0.0422 -0.0055 0.0321  88  LEU   A CD1 
1752 C  CD1 B LEU   A 88  ? 0.2116 0.2421 0.1909 -0.0248 0.0144  -0.0223 88  LEU   A CD1 
1753 C  CD2 A LEU   A 88  ? 0.2315 0.2500 0.2444 -0.0397 0.0027  0.0347  88  LEU   A CD2 
1754 C  CD2 B LEU   A 88  ? 0.2162 0.2474 0.2194 -0.0215 0.0195  -0.0106 88  LEU   A CD2 
1777 N  N   . ALA   A 89  ? 0.1940 0.2274 0.1512 -0.0332 0.0211  0.0067  89  ALA   A N   
1778 C  CA  . ALA   A 89  ? 0.2049 0.2234 0.1315 -0.0299 0.0082  0.0173  89  ALA   A CA  
1779 C  C   . ALA   A 89  ? 0.2124 0.2305 0.1291 -0.0298 -0.0079 0.0193  89  ALA   A C   
1780 O  O   . ALA   A 89  ? 0.2098 0.2245 0.1699 -0.0377 -0.0107 -0.0092 89  ALA   A O   
1781 C  CB  . ALA   A 89  ? 0.2044 0.2145 0.1232 -0.0331 0.0019  0.0230  89  ALA   A CB  
1788 N  N   . LYS   A 90  ? 0.2241 0.2459 0.1279 -0.0379 -0.0209 0.0197  90  LYS   A N   
1789 C  CA  . LYS   A 90  ? 0.2303 0.2589 0.1436 -0.0313 -0.0344 0.0231  90  LYS   A CA  
1790 C  C   . LYS   A 90  ? 0.2095 0.2354 0.1396 -0.0303 -0.0324 0.0111  90  LYS   A C   
1791 O  O   . LYS   A 90  ? 0.2094 0.2458 0.1773 -0.0349 -0.0351 -0.0000 90  LYS   A O   
1792 C  CB  . LYS   A 90  ? 0.2536 0.2908 0.1849 -0.0277 -0.0403 0.0463  90  LYS   A CB  
1793 C  CG  . LYS   A 90  ? 0.2867 0.3215 0.2871 -0.0266 -0.0407 0.0558  90  LYS   A CG  
1794 C  CD  . LYS   A 90  ? 0.3244 0.3485 0.3862 -0.0292 -0.0282 0.0588  90  LYS   A CD  
1795 C  CE  . LYS   A 90  ? 0.3592 0.3768 0.4637 -0.0304 -0.0174 0.0574  90  LYS   A CE  
1796 N  NZ  . LYS   A 90  ? 0.3721 0.3895 0.5162 -0.0299 -0.0116 0.0543  90  LYS   A NZ  
1810 N  N   . HIS   A 91  ? 0.1923 0.2120 0.1172 -0.0265 -0.0322 0.0215  91  HIS   A N   
1811 C  CA  . HIS   A 91  ? 0.1822 0.1927 0.1263 -0.0198 -0.0253 0.0196  91  HIS   A CA  
1812 C  C   . HIS   A 91  ? 0.1681 0.1809 0.1204 -0.0224 -0.0126 0.0203  91  HIS   A C   
1813 O  O   . HIS   A 91  ? 0.1597 0.1909 0.1353 -0.0283 -0.0048 0.0234  91  HIS   A O   
1814 C  CB  . HIS   A 91  ? 0.1948 0.2196 0.1824 -0.0022 -0.0360 0.0177  91  HIS   A CB  
1815 C  CG  . HIS   A 91  ? 0.2369 0.2669 0.2480 0.0113  -0.0590 0.0074  91  HIS   A CG  
1816 N  ND1 . HIS   A 91  ? 0.2480 0.2924 0.2889 0.0179  -0.0653 -0.0083 91  HIS   A ND1 
1817 C  CD2 . HIS   A 91  ? 0.2635 0.2873 0.2682 0.0172  -0.0753 0.0176  91  HIS   A CD2 
1818 C  CE1 . HIS   A 91  ? 0.2662 0.3036 0.2990 0.0188  -0.0679 0.0017  91  HIS   A CE1 
1819 N  NE2 . HIS   A 91  ? 0.2777 0.3047 0.2917 0.0226  -0.0749 0.0119  91  HIS   A NE2 
1827 N  N   . CYS   A 92  ? 0.1529 0.1721 0.1272 -0.0222 -0.0126 0.0220  92  CYS   A N   
1828 C  CA  . CYS   A 92  ? 0.1421 0.1634 0.1334 -0.0164 -0.0002 0.0168  92  CYS   A CA  
1829 C  C   . CYS   A 92  ? 0.1396 0.1568 0.1228 -0.0165 0.0028  0.0183  92  CYS   A C   
1830 O  O   . CYS   A 92  ? 0.1366 0.1612 0.1445 -0.0181 -0.0027 0.0115  92  CYS   A O   
1831 C  CB  . CYS   A 92  ? 0.1439 0.1628 0.1442 -0.0118 -0.0097 0.0075  92  CYS   A CB  
1832 S  SG  . CYS   A 92  ? 0.1471 0.1486 0.1278 -0.0148 -0.0013 0.0115  92  CYS   A SG  
1838 N  N   . LEU   A 93  ? 0.1365 0.1408 0.1300 -0.0151 0.0036  0.0168  93  LEU   A N   
1839 C  CA  . LEU   A 93  ? 0.1305 0.1321 0.1347 -0.0091 0.0005  0.0156  93  LEU   A CA  
1840 C  C   . LEU   A 93  ? 0.1256 0.1251 0.1365 -0.0019 0.0059  0.0143  93  LEU   A C   
1841 O  O   . LEU   A 93  ? 0.1216 0.1348 0.1460 -0.0056 0.0038  0.0147  93  LEU   A O   
1842 C  CB  . LEU   A 93  ? 0.1384 0.1392 0.1490 -0.0055 -0.0090 0.0237  93  LEU   A CB  
1843 C  CG  . LEU   A 93  ? 0.1438 0.1379 0.1565 -0.0034 0.0004  0.0212  93  LEU   A CG  
1844 C  CD1 . LEU   A 93  ? 0.1473 0.1447 0.1825 -0.0031 0.0122  0.0178  93  LEU   A CD1 
1845 C  CD2 . LEU   A 93  ? 0.1560 0.1363 0.1719 -0.0111 -0.0021 0.0145  93  LEU   A CD2 
1857 N  N   . HIS   A 94  ? 0.1200 0.1205 0.1359 -0.0071 0.0074  0.0224  94  HIS   A N   
1858 C  CA  . HIS   A 94  ? 0.1189 0.1245 0.1396 -0.0053 0.0026  0.0220  94  HIS   A CA  
1859 C  C   . HIS   A 94  ? 0.1176 0.1207 0.1439 -0.0056 -0.0015 0.0109  94  HIS   A C   
1860 O  O   . HIS   A 94  ? 0.1220 0.1433 0.1751 0.0005  0.0051  -0.0093 94  HIS   A O   
1861 C  CB  . HIS   A 94  ? 0.1185 0.1218 0.1420 -0.0043 -0.0017 0.0143  94  HIS   A CB  
1862 C  CG  . HIS   A 94  ? 0.1279 0.1215 0.1305 -0.0050 -0.0035 0.0156  94  HIS   A CG  
1863 N  ND1 . HIS   A 94  ? 0.1259 0.1253 0.1374 -0.0054 0.0021  0.0164  94  HIS   A ND1 
1864 C  CD2 . HIS   A 94  ? 0.1339 0.1360 0.1353 -0.0112 -0.0088 0.0081  94  HIS   A CD2 
1865 C  CE1 . HIS   A 94  ? 0.1293 0.1326 0.1349 -0.0111 -0.0078 0.0084  94  HIS   A CE1 
1866 N  NE2 . HIS   A 94  ? 0.1379 0.1340 0.1423 -0.0113 -0.0021 0.0017  94  HIS   A NE2 
1874 N  N   . VAL   A 95  ? 0.1151 0.1209 0.1289 -0.0031 0.0043  0.0104  95  VAL   A N   
1875 C  CA  . VAL   A 95  ? 0.1238 0.1195 0.1262 -0.0044 0.0077  0.0072  95  VAL   A CA  
1876 C  C   . VAL   A 95  ? 0.1234 0.1164 0.1150 -0.0075 0.0088  0.0105  95  VAL   A C   
1877 O  O   . VAL   A 95  ? 0.1281 0.1315 0.1330 0.0068  0.0103  0.0095  95  VAL   A O   
1878 C  CB  . VAL   A 95  ? 0.1288 0.1273 0.1504 -0.0049 0.0055  0.0110  95  VAL   A CB  
1879 C  CG1 . VAL   A 95  ? 0.1473 0.1247 0.1578 -0.0126 0.0109  -0.0045 95  VAL   A CG1 
1880 C  CG2 . VAL   A 95  ? 0.1275 0.1363 0.1470 -0.0151 0.0071  0.0190  95  VAL   A CG2 
1890 N  N   . VAL   A 96  ? 0.1266 0.1220 0.1202 -0.0020 0.0049  0.0119  96  VAL   A N   
1891 C  CA  . VAL   A 96  ? 0.1373 0.1219 0.1289 0.0032  0.0123  0.0151  96  VAL   A CA  
1892 C  C   . VAL   A 96  ? 0.1382 0.1288 0.1271 0.0002  0.0126  0.0107  96  VAL   A C   
1893 O  O   . VAL   A 96  ? 0.1493 0.1386 0.1536 -0.0031 0.0173  -0.0063 96  VAL   A O   
1894 C  CB  . VAL   A 96  ? 0.1355 0.1315 0.1349 0.0019  0.0184  0.0131  96  VAL   A CB  
1895 C  CG1 . VAL   A 96  ? 0.1444 0.1440 0.1275 -0.0034 0.0169  0.0145  96  VAL   A CG1 
1896 C  CG2 . VAL   A 96  ? 0.1380 0.1398 0.1404 -0.0113 0.0195  0.0126  96  VAL   A CG2 
1906 N  N   A GLY   A 97  ? 0.1372 0.1345 0.1382 -0.0035 0.0043  0.0056  97  GLY   A N   
1907 N  N   B GLY   A 97  ? 0.1421 0.1357 0.1274 -0.0024 0.0071  0.0094  97  GLY   A N   
1908 C  CA  A GLY   A 97  ? 0.1444 0.1477 0.1393 -0.0054 -0.0044 0.0112  97  GLY   A CA  
1909 C  CA  B GLY   A 97  ? 0.1518 0.1465 0.1209 -0.0033 0.0037  0.0177  97  GLY   A CA  
1910 C  C   A GLY   A 97  ? 0.1473 0.1603 0.1365 -0.0032 -0.0093 0.0056  97  GLY   A C   
1911 C  C   B GLY   A 97  ? 0.1582 0.1571 0.1138 -0.0012 0.0047  0.0156  97  GLY   A C   
1912 O  O   A GLY   A 97  ? 0.1578 0.1569 0.1608 -0.0059 -0.0115 0.0156  97  GLY   A O   
1913 O  O   B GLY   A 97  ? 0.1643 0.1566 0.1196 -0.0017 0.0134  0.0250  97  GLY   A O   
1920 N  N   A PRO   A 98  ? 0.1457 0.1679 0.1264 -0.0029 -0.0062 0.0081  98  PRO   A N   
1921 N  N   B PRO   A 98  ? 0.1641 0.1598 0.1150 -0.0038 0.0006  0.0175  98  PRO   A N   
1922 C  CA  A PRO   A 98  ? 0.1555 0.1874 0.1256 -0.0077 -0.0020 0.0105  98  PRO   A CA  
1923 C  CA  B PRO   A 98  ? 0.1752 0.1801 0.1193 -0.0077 -0.0016 0.0131  98  PRO   A CA  
1924 C  C   A PRO   A 98  ? 0.1578 0.1958 0.1286 -0.0081 -0.0090 0.0194  98  PRO   A C   
1925 C  C   B PRO   A 98  ? 0.1812 0.1887 0.1146 -0.0141 -0.0075 0.0290  98  PRO   A C   
1926 O  O   A PRO   A 98  ? 0.1507 0.1759 0.1426 -0.0041 -0.0097 0.0172  98  PRO   A O   
1927 O  O   B PRO   A 98  ? 0.1775 0.1800 0.1369 -0.0094 -0.0000 0.0185  98  PRO   A O   
1928 C  CB  A PRO   A 98  ? 0.1741 0.1982 0.1279 -0.0010 0.0009  -0.0023 98  PRO   A CB  
1929 C  CB  B PRO   A 98  ? 0.1887 0.1800 0.1176 0.0011  -0.0031 0.0059  98  PRO   A CB  
1930 C  CG  A PRO   A 98  ? 0.1698 0.1917 0.1364 0.0038  0.0040  -0.0122 98  PRO   A CG  
1931 C  CG  B PRO   A 98  ? 0.1850 0.1732 0.1190 0.0025  0.0003  0.0064  98  PRO   A CG  
1932 C  CD  A PRO   A 98  ? 0.1539 0.1746 0.1302 0.0020  0.0004  -0.0048 98  PRO   A CD  
1933 C  CD  B PRO   A 98  ? 0.1728 0.1607 0.1094 -0.0006 0.0045  0.0137  98  PRO   A CD  
1948 N  N   A ASN   A 99  ? 0.1625 0.2194 0.1339 -0.0090 -0.0004 0.0334  99  ASN   A N   
1949 N  N   B ASN   A 99  ? 0.1899 0.2066 0.1182 -0.0152 -0.0104 0.0473  99  ASN   A N   
1950 C  CA  A ASN   A 99  ? 0.1799 0.2345 0.1393 -0.0113 0.0002  0.0520  99  ASN   A CA  
1951 C  CA  B ASN   A 99  ? 0.2052 0.2236 0.1368 -0.0122 -0.0184 0.0575  99  ASN   A CA  
1952 C  C   A ASN   A 99  ? 0.1966 0.2632 0.1262 -0.0213 0.0064  0.0678  99  ASN   A C   
1953 C  C   B ASN   A 99  ? 0.2108 0.2358 0.1444 -0.0074 -0.0160 0.0428  99  ASN   A C   
1954 O  O   A ASN   A 99  ? 0.2012 0.2551 0.1218 -0.0100 0.0005  0.0583  99  ASN   A O   
1955 O  O   B ASN   A 99  ? 0.2154 0.2349 0.1594 0.0050  -0.0236 0.0473  99  ASN   A O   
1956 C  CB  A ASN   A 99  ? 0.1776 0.2191 0.1748 -0.0101 -0.0104 0.0469  99  ASN   A CB  
1957 C  CB  B ASN   A 99  ? 0.2112 0.2327 0.1835 -0.0124 -0.0284 0.0701  99  ASN   A CB  
1958 C  CG  A ASN   A 99  ? 0.1758 0.2057 0.2128 -0.0091 -0.0226 0.0287  99  ASN   A CG  
1959 C  CG  B ASN   A 99  ? 0.2170 0.2462 0.2302 -0.0126 -0.0353 0.0773  99  ASN   A CG  
1960 O  OD1 A ASN   A 99  ? 0.1839 0.2198 0.2077 -0.0016 -0.0199 0.0152  99  ASN   A OD1 
1961 O  OD1 B ASN   A 99  ? 0.2249 0.2543 0.2284 -0.0163 -0.0413 0.0959  99  ASN   A OD1 
1962 N  ND2 A ASN   A 99  ? 0.1772 0.1872 0.2396 -0.0103 -0.0270 0.0368  99  ASN   A ND2 
1963 N  ND2 B ASN   A 99  ? 0.2195 0.2509 0.2481 -0.0061 -0.0293 0.0740  99  ASN   A ND2 
1976 N  N   A VAL   A 100 ? 0.2130 0.2938 0.1407 -0.0318 -0.0201 0.0850  100 VAL   A N   
1977 N  N   B VAL   A 100 ? 0.2129 0.2356 0.1403 -0.0029 -0.0311 0.0190  100 VAL   A N   
1978 C  CA  A VAL   A 100 ? 0.2397 0.3248 0.1792 -0.0356 -0.0215 0.0892  100 VAL   A CA  
1979 C  CA  B VAL   A 100 ? 0.2217 0.2312 0.1612 -0.0003 -0.0405 0.0057  100 VAL   A CA  
1980 C  C   A VAL   A 100 ? 0.2453 0.3482 0.1902 -0.0365 -0.0171 0.1151  100 VAL   A C   
1981 C  C   B VAL   A 100 ? 0.2108 0.2242 0.1358 0.0021  -0.0357 0.0100  100 VAL   A C   
1982 O  O   A VAL   A 100 ? 0.2445 0.3618 0.2063 -0.0278 -0.0091 0.1150  100 VAL   A O   
1983 O  O   B VAL   A 100 ? 0.2175 0.2223 0.1349 0.0071  -0.0215 0.0153  100 VAL   A O   
1984 C  CB  A VAL   A 100 ? 0.2600 0.3257 0.2095 -0.0390 -0.0247 0.0766  100 VAL   A CB  
1985 C  CB  B VAL   A 100 ? 0.2435 0.2385 0.2016 -0.0077 -0.0496 -0.0039 100 VAL   A CB  
1986 C  CG1 A VAL   A 100 ? 0.2608 0.3283 0.2327 -0.0439 -0.0187 0.0744  100 VAL   A CG1 
1987 C  CG1 B VAL   A 100 ? 0.2480 0.2471 0.2236 -0.0087 -0.0433 -0.0062 100 VAL   A CG1 
1988 C  CG2 A VAL   A 100 ? 0.2705 0.3278 0.2263 -0.0400 -0.0271 0.0648  100 VAL   A CG2 
1989 C  CG2 B VAL   A 100 ? 0.2552 0.2383 0.2115 -0.0138 -0.0555 -0.0088 100 VAL   A CG2 
2008 N  N   A ASN   A 101 ? 0.2596 0.3589 0.2173 -0.0435 -0.0097 0.1279  101 ASN   A N   
2009 N  N   B ASN   A 101 ? 0.1982 0.2319 0.1462 0.0014  -0.0255 0.0165  101 ASN   A N   
2010 C  CA  A ASN   A 101 ? 0.2839 0.3672 0.2341 -0.0457 -0.0000 0.1393  101 ASN   A CA  
2011 C  CA  B ASN   A 101 ? 0.1997 0.2515 0.1510 0.0041  -0.0235 0.0329  101 ASN   A CA  
2012 C  C   A ASN   A 101 ? 0.3076 0.3882 0.2487 -0.0460 0.0203  0.1504  101 ASN   A C   
2013 C  C   B ASN   A 101 ? 0.2151 0.2778 0.1693 -0.0031 -0.0142 0.0481  101 ASN   A C   
2014 O  O   A ASN   A 101 ? 0.3205 0.3930 0.2738 -0.0441 0.0248  0.1447  101 ASN   A O   
2015 O  O   B ASN   A 101 ? 0.2206 0.2790 0.1944 -0.0056 -0.0054 0.0409  101 ASN   A O   
2016 C  CB  A ASN   A 101 ? 0.2823 0.3521 0.2432 -0.0484 -0.0041 0.1296  101 ASN   A CB  
2017 C  CB  B ASN   A 101 ? 0.1967 0.2557 0.1660 0.0043  -0.0198 0.0248  101 ASN   A CB  
2018 C  CG  A ASN   A 101 ? 0.2794 0.3393 0.2459 -0.0525 -0.0033 0.1056  101 ASN   A CG  
2019 C  CG  B ASN   A 101 ? 0.1886 0.2593 0.1777 0.0057  -0.0298 0.0176  101 ASN   A CG  
2020 O  OD1 A ASN   A 101 ? 0.2746 0.3370 0.2437 -0.0512 0.0038  0.0788  101 ASN   A OD1 
2021 O  OD1 B ASN   A 101 ? 0.1906 0.2677 0.1818 0.0097  -0.0389 0.0037  101 ASN   A OD1 
2022 N  ND2 A ASN   A 101 ? 0.2822 0.3310 0.2465 -0.0572 -0.0076 0.1096  101 ASN   A ND2 
2023 N  ND2 B ASN   A 101 ? 0.1775 0.2549 0.1798 0.0019  -0.0174 0.0224  101 ASN   A ND2 
2036 N  N   A LYS   A 102 ? 0.3114 0.4027 0.2617 -0.0513 0.0348  0.1466  102 LYS   A N   
2037 N  N   B LYS   A 102 ? 0.2236 0.3032 0.1855 -0.0118 -0.0105 0.0465  102 LYS   A N   
2038 C  CA  A LYS   A 102 ? 0.3190 0.4180 0.2671 -0.0545 0.0321  0.1292  102 LYS   A CA  
2039 C  CA  B LYS   A 102 ? 0.2450 0.3318 0.1984 -0.0153 -0.0078 0.0473  102 LYS   A CA  
2040 C  C   A LYS   A 102 ? 0.3223 0.4287 0.2561 -0.0473 0.0262  0.1293  102 LYS   A C   
2041 C  C   B LYS   A 102 ? 0.2595 0.3496 0.1914 -0.0092 0.0092  0.0536  102 LYS   A C   
2042 O  O   A LYS   A 102 ? 0.3235 0.4335 0.2532 -0.0446 0.0351  0.1336  102 LYS   A O   
2043 O  O   B LYS   A 102 ? 0.2558 0.3490 0.1886 -0.0033 0.0214  0.0579  102 LYS   A O   
2044 C  CB  A LYS   A 102 ? 0.3285 0.4251 0.2928 -0.0612 0.0257  0.1017  102 LYS   A CB  
2045 C  CB  B LYS   A 102 ? 0.2577 0.3417 0.2235 -0.0208 -0.0216 0.0334  102 LYS   A CB  
2046 C  CG  A LYS   A 102 ? 0.3383 0.4308 0.3170 -0.0652 0.0193  0.0722  102 LYS   A CG  
2047 C  CG  B LYS   A 102 ? 0.2732 0.3530 0.2461 -0.0259 -0.0353 0.0168  102 LYS   A CG  
2048 C  CD  A LYS   A 102 ? 0.3510 0.4386 0.3455 -0.0655 0.0124  0.0400  102 LYS   A CD  
2049 C  CD  B LYS   A 102 ? 0.2890 0.3643 0.2716 -0.0274 -0.0449 0.0010  102 LYS   A CD  
2050 C  CE  A LYS   A 102 ? 0.3622 0.4455 0.3705 -0.0644 0.0074  0.0166  102 LYS   A CE  
2051 C  CE  B LYS   A 102 ? 0.3004 0.3727 0.2875 -0.0260 -0.0485 -0.0087 102 LYS   A CE  
2052 N  NZ  A LYS   A 102 ? 0.3677 0.4491 0.3827 -0.0647 0.0066  0.0033  102 LYS   A NZ  
2053 N  NZ  B LYS   A 102 ? 0.3074 0.3781 0.2963 -0.0250 -0.0500 -0.0123 102 LYS   A NZ  
2080 N  N   A GLY   A 103 ? 0.3243 0.4370 0.2649 -0.0398 0.0077  0.1063  103 GLY   A N   
2081 N  N   B GLY   A 103 ? 0.2807 0.3701 0.2073 -0.0067 0.0086  0.0422  103 GLY   A N   
2082 C  CA  A GLY   A 103 ? 0.3215 0.4384 0.2493 -0.0344 0.0038  0.0943  103 GLY   A CA  
2083 C  CA  B GLY   A 103 ? 0.2972 0.3890 0.2290 -0.0014 0.0155  0.0358  103 GLY   A CA  
2084 C  C   A GLY   A 103 ? 0.3132 0.4404 0.2399 -0.0340 0.0107  0.0817  103 GLY   A C   
2085 C  C   B GLY   A 103 ? 0.3113 0.4063 0.2534 0.0010  0.0266  0.0332  103 GLY   A C   
2086 O  O   A GLY   A 103 ? 0.3183 0.4431 0.2429 -0.0330 0.0068  0.0793  103 GLY   A O   
2087 O  O   B GLY   A 103 ? 0.3183 0.4070 0.2653 0.0039  0.0351  0.0340  103 GLY   A O   
2094 N  N   A GLU   A 104 ? 0.2941 0.4381 0.2031 -0.0374 0.0198  0.0742  104 GLU   A N   
2095 N  N   B GLU   A 104 ? 0.3168 0.4252 0.2503 0.0007  0.0258  0.0275  104 GLU   A N   
2096 C  CA  A GLU   A 104 ? 0.2729 0.4334 0.1776 -0.0429 0.0189  0.0582  104 GLU   A CA  
2097 C  CA  B GLU   A 104 ? 0.3172 0.4401 0.2511 -0.0027 0.0233  0.0175  104 GLU   A CA  
2098 C  C   A GLU   A 104 ? 0.2770 0.4435 0.1748 -0.0412 0.0189  0.0312  104 GLU   A C   
2099 C  C   B GLU   A 104 ? 0.3193 0.4569 0.2467 -0.0069 0.0303  -0.0008 104 GLU   A C   
2100 O  O   A GLU   A 104 ? 0.2684 0.4442 0.1673 -0.0424 0.0141  0.0291  104 GLU   A O   
2101 O  O   B GLU   A 104 ? 0.3180 0.4644 0.2452 -0.0065 0.0340  0.0001  104 GLU   A O   
2102 C  CB  A GLU   A 104 ? 0.2455 0.4172 0.1595 -0.0497 0.0228  0.0792  104 GLU   A CB  
2103 C  CB  B GLU   A 104 ? 0.3141 0.4368 0.2510 -0.0034 0.0095  0.0319  104 GLU   A CB  
2104 C  CG  A GLU   A 104 ? 0.2238 0.4011 0.1710 -0.0526 0.0228  0.0912  104 GLU   A CG  
2105 C  CG  B GLU   A 104 ? 0.3134 0.4331 0.2554 -0.0022 -0.0054 0.0449  104 GLU   A CG  
2106 C  CD  A GLU   A 104 ? 0.2047 0.3839 0.1685 -0.0524 0.0251  0.1006  104 GLU   A CD  
2107 C  CD  B GLU   A 104 ? 0.3119 0.4295 0.2555 -0.0011 -0.0182 0.0578  104 GLU   A CD  
2108 O  OE1 A GLU   A 104 ? 0.1851 0.3651 0.1504 -0.0482 0.0145  0.0952  104 GLU   A OE1 
2109 O  OE1 B GLU   A 104 ? 0.3089 0.4261 0.2439 0.0006  -0.0286 0.0675  104 GLU   A OE1 
2110 O  OE2 A GLU   A 104 ? 0.2197 0.3822 0.1827 -0.0560 0.0235  0.1154  104 GLU   A OE2 
2111 O  OE2 B GLU   A 104 ? 0.3175 0.4293 0.2684 -0.0014 -0.0197 0.0581  104 GLU   A OE2 
2124 N  N   A ASP   A 105 ? 0.2900 0.4518 0.2055 -0.0387 0.0258  -0.0001 105 ASP   A N   
2125 N  N   B ASP   A 105 ? 0.3204 0.4633 0.2521 -0.0104 0.0302  -0.0229 105 ASP   A N   
2126 C  CA  A ASP   A 105 ? 0.2943 0.4562 0.2499 -0.0330 0.0360  -0.0343 105 ASP   A CA  
2127 C  CA  B ASP   A 105 ? 0.3240 0.4695 0.2814 -0.0153 0.0214  -0.0447 105 ASP   A CA  
2128 C  C   A ASP   A 105 ? 0.2646 0.4392 0.2045 -0.0431 0.0287  -0.0613 105 ASP   A C   
2129 C  C   B ASP   A 105 ? 0.3086 0.4576 0.2505 -0.0270 0.0154  -0.0587 105 ASP   A C   
2130 O  O   A ASP   A 105 ? 0.2437 0.4287 0.1467 -0.0397 0.0328  -0.0911 105 ASP   A O   
2131 O  O   B ASP   A 105 ? 0.3007 0.4576 0.2267 -0.0275 0.0105  -0.0726 105 ASP   A O   
2132 C  CB  A ASP   A 105 ? 0.3224 0.4767 0.3296 -0.0211 0.0463  -0.0427 105 ASP   A CB  
2133 C  CB  B ASP   A 105 ? 0.3396 0.4842 0.3376 -0.0094 0.0161  -0.0537 105 ASP   A CB  
2134 C  CG  A ASP   A 105 ? 0.3456 0.4936 0.3986 -0.0103 0.0505  -0.0524 105 ASP   A CG  
2135 C  CG  B ASP   A 105 ? 0.3541 0.4967 0.3853 -0.0049 0.0091  -0.0648 105 ASP   A CG  
2136 O  OD1 A ASP   A 105 ? 0.3537 0.5016 0.4228 -0.0091 0.0488  -0.0579 105 ASP   A OD1 
2137 O  OD1 B ASP   A 105 ? 0.3602 0.5025 0.3986 -0.0050 0.0062  -0.0721 105 ASP   A OD1 
2138 O  OD2 A ASP   A 105 ? 0.3538 0.4986 0.4255 -0.0074 0.0567  -0.0558 105 ASP   A OD2 
2139 O  OD2 B ASP   A 105 ? 0.3588 0.5004 0.4086 -0.0025 0.0064  -0.0679 105 ASP   A OD2 
2148 N  N   A ILE   A 106 ? 0.2530 0.4303 0.2253 -0.0575 0.0040  -0.0645 106 ILE   A N   
2149 N  N   B ILE   A 106 ? 0.3003 0.4434 0.2551 -0.0379 0.0099  -0.0578 106 ILE   A N   
2150 C  CA  A ILE   A 106 ? 0.2358 0.4148 0.2402 -0.0745 -0.0206 -0.0770 106 ILE   A CA  
2151 C  CA  B ILE   A 106 ? 0.2888 0.4244 0.2675 -0.0467 0.0063  -0.0614 106 ILE   A CA  
2152 C  C   A ILE   A 106 ? 0.2213 0.3894 0.2449 -0.0967 -0.0174 -0.1068 106 ILE   A C   
2153 C  C   B ILE   A 106 ? 0.2805 0.3984 0.2693 -0.0539 0.0119  -0.0830 106 ILE   A C   
2154 O  O   A ILE   A 106 ? 0.2029 0.3797 0.2407 -0.1035 -0.0067 -0.1115 106 ILE   A O   
2155 O  O   B ILE   A 106 ? 0.2753 0.3927 0.2614 -0.0530 0.0174  -0.0871 106 ILE   A O   
2156 C  CB  A ILE   A 106 ? 0.2391 0.4226 0.2726 -0.0607 -0.0411 -0.0460 106 ILE   A CB  
2157 C  CB  B ILE   A 106 ? 0.2887 0.4296 0.2948 -0.0435 -0.0011 -0.0391 106 ILE   A CB  
2158 C  CG1 A ILE   A 106 ? 0.2316 0.4225 0.2991 -0.0485 -0.0553 -0.0248 106 ILE   A CG1 
2159 C  CG1 B ILE   A 106 ? 0.2874 0.4288 0.3191 -0.0409 -0.0044 -0.0228 106 ILE   A CG1 
2160 C  CG2 A ILE   A 106 ? 0.2456 0.4253 0.2829 -0.0580 -0.0420 -0.0390 106 ILE   A CG2 
2161 C  CG2 B ILE   A 106 ? 0.2898 0.4321 0.3028 -0.0430 -0.0029 -0.0327 106 ILE   A CG2 
2162 C  CD1 A ILE   A 106 ? 0.2331 0.4206 0.3142 -0.0367 -0.0555 -0.0149 106 ILE   A CD1 
2163 C  CD1 B ILE   A 106 ? 0.2903 0.4275 0.3308 -0.0372 -0.0052 -0.0150 106 ILE   A CD1 
2186 N  N   A GLN   A 107 ? 0.2372 0.3747 0.2746 -0.0959 0.0004  -0.1210 107 GLN   A N   
2187 N  N   B GLN   A 107 ? 0.2826 0.3788 0.3039 -0.0570 0.0177  -0.0921 107 GLN   A N   
2188 C  CA  A GLN   A 107 ? 0.2617 0.3566 0.3482 -0.0813 0.0327  -0.1141 107 GLN   A CA  
2189 C  CA  B GLN   A 107 ? 0.2844 0.3549 0.3503 -0.0534 0.0328  -0.0925 107 GLN   A CA  
2190 C  C   A GLN   A 107 ? 0.2450 0.3134 0.3421 -0.0694 0.0562  -0.0958 107 GLN   A C   
2191 C  C   B GLN   A 107 ? 0.2555 0.3133 0.3379 -0.0564 0.0521  -0.0873 107 GLN   A C   
2192 O  O   A GLN   A 107 ? 0.2535 0.3065 0.3930 -0.0635 0.0711  -0.0933 107 GLN   A O   
2193 O  O   B GLN   A 107 ? 0.2621 0.3087 0.3777 -0.0525 0.0627  -0.0871 107 GLN   A O   
2194 C  CB  A GLN   A 107 ? 0.2977 0.3793 0.4357 -0.0784 0.0328  -0.1112 107 GLN   A CB  
2195 C  CB  B GLN   A 107 ? 0.3135 0.3708 0.4190 -0.0470 0.0195  -0.0846 107 GLN   A CB  
2196 C  CG  A GLN   A 107 ? 0.3321 0.3999 0.5238 -0.0721 0.0301  -0.1012 107 GLN   A CG  
2197 C  CG  B GLN   A 107 ? 0.3390 0.3842 0.4886 -0.0409 0.0060  -0.0723 107 GLN   A CG  
2198 C  CD  A GLN   A 107 ? 0.3596 0.4147 0.6000 -0.0653 0.0300  -0.0894 107 GLN   A CD  
2199 C  CD  B GLN   A 107 ? 0.3595 0.3931 0.5477 -0.0343 -0.0052 -0.0581 107 GLN   A CD  
2200 O  OE1 A GLN   A 107 ? 0.3699 0.4193 0.6290 -0.0626 0.0311  -0.0881 107 GLN   A OE1 
2201 O  OE1 B GLN   A 107 ? 0.3680 0.3961 0.5705 -0.0332 -0.0089 -0.0513 107 GLN   A OE1 
2202 N  NE2 A GLN   A 107 ? 0.3696 0.4207 0.6268 -0.0636 0.0271  -0.0856 107 GLN   A NE2 
2203 N  NE2 B GLN   A 107 ? 0.3652 0.3948 0.5660 -0.0315 -0.0084 -0.0553 107 GLN   A NE2 
2220 N  N   . LEU   A 108 ? 0.2203 0.2706 0.2852 -0.0607 0.0561  -0.0911 108 LEU   A N   
2221 C  CA  . LEU   A 108 ? 0.1930 0.2092 0.2430 -0.0219 0.0454  -0.0439 108 LEU   A CA  
2222 C  C   . LEU   A 108 ? 0.1673 0.1542 0.2248 -0.0067 0.0350  -0.0067 108 LEU   A C   
2223 O  O   . LEU   A 108 ? 0.1569 0.1538 0.2322 -0.0021 0.0363  0.0066  108 LEU   A O   
2224 C  CB  . LEU   A 108 ? 0.1946 0.2168 0.2167 -0.0241 0.0465  -0.0317 108 LEU   A CB  
2225 C  CG  . LEU   A 108 ? 0.2079 0.2429 0.2373 -0.0290 0.0525  -0.0351 108 LEU   A CG  
2226 C  CD1 . LEU   A 108 ? 0.2259 0.2490 0.2316 -0.0359 0.0572  -0.0284 108 LEU   A CD1 
2227 C  CD2 . LEU   A 108 ? 0.2134 0.2647 0.2862 -0.0193 0.0441  -0.0244 108 LEU   A CD2 
2240 N  N   . LEU   A 109 ? 0.1527 0.1525 0.2143 0.0013  0.0244  0.0098  109 LEU   A N   
2241 C  CA  . LEU   A 109 ? 0.1471 0.1415 0.1962 0.0027  0.0138  0.0093  109 LEU   A CA  
2242 C  C   . LEU   A 109 ? 0.1403 0.1395 0.1916 -0.0029 0.0104  0.0051  109 LEU   A C   
2243 O  O   . LEU   A 109 ? 0.1475 0.1305 0.2076 -0.0038 -0.0029 -0.0026 109 LEU   A O   
2244 C  CB  . LEU   A 109 ? 0.1559 0.1548 0.2053 0.0069  0.0077  0.0234  109 LEU   A CB  
2245 C  CG  . LEU   A 109 ? 0.1446 0.1570 0.2056 0.0065  0.0096  0.0318  109 LEU   A CG  
2246 C  CD1 . LEU   A 109 ? 0.1528 0.1477 0.2162 0.0034  0.0188  0.0054  109 LEU   A CD1 
2247 C  CD2 . LEU   A 109 ? 0.1483 0.1839 0.2229 0.0003  0.0090  0.0267  109 LEU   A CD2 
2259 N  N   . LYS   A 110 ? 0.1368 0.1374 0.1850 -0.0029 0.0019  0.0036  110 LYS   A N   
2260 C  CA  . LYS   A 110 ? 0.1388 0.1354 0.1897 -0.0030 -0.0084 0.0074  110 LYS   A CA  
2261 C  C   . LYS   A 110 ? 0.1439 0.1301 0.1760 -0.0027 0.0055  -0.0052 110 LYS   A C   
2262 O  O   . LYS   A 110 ? 0.1360 0.1297 0.1819 -0.0076 0.0076  -0.0072 110 LYS   A O   
2263 C  CB  . LYS   A 110 ? 0.1434 0.1417 0.2105 -0.0050 -0.0087 -0.0032 110 LYS   A CB  
2264 C  CG  . LYS   A 110 ? 0.1451 0.1381 0.2092 -0.0026 -0.0132 -0.0074 110 LYS   A CG  
2265 C  CD  . LYS   A 110 ? 0.1516 0.1452 0.2325 -0.0087 -0.0128 -0.0064 110 LYS   A CD  
2266 C  CE  . LYS   A 110 ? 0.1604 0.1463 0.2427 -0.0028 0.0055  -0.0159 110 LYS   A CE  
2267 N  NZ  . LYS   A 110 ? 0.1665 0.1487 0.2525 -0.0105 0.0184  -0.0124 110 LYS   A NZ  
2281 N  N   . SER   A 111 ? 0.1416 0.1325 0.1863 0.0005  0.0017  0.0047  111 SER   A N   
2282 C  CA  . SER   A 111 ? 0.1343 0.1376 0.1901 -0.0016 0.0114  0.0020  111 SER   A CA  
2283 C  C   . SER   A 111 ? 0.1332 0.1300 0.1832 -0.0066 0.0112  0.0004  111 SER   A C   
2284 O  O   . SER   A 111 ? 0.1411 0.1273 0.1916 -0.0052 0.0077  0.0026  111 SER   A O   
2285 C  CB  . SER   A 111 ? 0.1508 0.1556 0.2006 -0.0020 0.0203  -0.0070 111 SER   A CB  
2286 O  OG  . SER   A 111 ? 0.1975 0.1745 0.2050 0.0038  0.0214  -0.0180 111 SER   A OG  
2292 N  N   . ALA   A 112 ? 0.1380 0.1241 0.1889 -0.0003 0.0142  0.0019  112 ALA   A N   
2293 C  CA  . ALA   A 112 ? 0.1388 0.1203 0.1864 -0.0048 0.0151  -0.0003 112 ALA   A CA  
2294 C  C   . ALA   A 112 ? 0.1308 0.1187 0.1886 -0.0040 0.0104  -0.0020 112 ALA   A C   
2295 O  O   . ALA   A 112 ? 0.1325 0.1205 0.1920 -0.0106 0.0131  0.0035  112 ALA   A O   
2296 C  CB  . ALA   A 112 ? 0.1450 0.1214 0.1906 -0.0051 0.0102  0.0048  112 ALA   A CB  
2302 N  N   . TYR   A 113 ? 0.1250 0.1284 0.1869 -0.0037 0.0135  0.0039  113 TYR   A N   
2303 C  CA  . TYR   A 113 ? 0.1247 0.1286 0.1895 -0.0005 0.0170  0.0111  113 TYR   A CA  
2304 C  C   . TYR   A 113 ? 0.1224 0.1258 0.1750 -0.0074 0.0184  0.0071  113 TYR   A C   
2305 O  O   . TYR   A 113 ? 0.1263 0.1305 0.1883 -0.0064 0.0135  0.0042  113 TYR   A O   
2306 C  CB  . TYR   A 113 ? 0.1233 0.1392 0.1885 -0.0052 0.0009  0.0153  113 TYR   A CB  
2307 C  CG  . TYR   A 113 ? 0.1249 0.1380 0.1768 -0.0108 0.0103  0.0160  113 TYR   A CG  
2308 C  CD1 . TYR   A 113 ? 0.1315 0.1451 0.1710 -0.0024 0.0091  0.0244  113 TYR   A CD1 
2309 C  CD2 . TYR   A 113 ? 0.1322 0.1399 0.1775 -0.0097 0.0024  0.0197  113 TYR   A CD2 
2310 C  CE1 . TYR   A 113 ? 0.1334 0.1575 0.1676 -0.0068 0.0116  0.0289  113 TYR   A CE1 
2311 C  CE2 . TYR   A 113 ? 0.1330 0.1475 0.1752 -0.0101 -0.0006 0.0251  113 TYR   A CE2 
2312 C  CZ  . TYR   A 113 ? 0.1345 0.1503 0.1631 -0.0013 0.0103  0.0297  113 TYR   A CZ  
2313 O  OH  . TYR   A 113 ? 0.1333 0.1555 0.1833 0.0084  0.0124  0.0213  113 TYR   A OH  
2323 N  N   . GLU   A 114 ? 0.1257 0.1229 0.1815 -0.0067 0.0133  0.0133  114 GLU   A N   
2324 C  CA  . GLU   A 114 ? 0.1291 0.1190 0.1851 -0.0001 0.0080  0.0114  114 GLU   A CA  
2325 C  C   . GLU   A 114 ? 0.1241 0.1259 0.1897 0.0018  0.0147  0.0109  114 GLU   A C   
2326 O  O   . GLU   A 114 ? 0.1289 0.1291 0.1939 -0.0004 0.0055  0.0103  114 GLU   A O   
2327 C  CB  . GLU   A 114 ? 0.1340 0.1249 0.1903 -0.0029 0.0037  0.0145  114 GLU   A CB  
2328 C  CG  . GLU   A 114 ? 0.1409 0.1287 0.1952 0.0006  0.0029  0.0003  114 GLU   A CG  
2329 C  CD  . GLU   A 114 ? 0.1423 0.1285 0.2018 -0.0054 0.0045  0.0051  114 GLU   A CD  
2330 O  OE1 . GLU   A 114 ? 0.1461 0.1265 0.2073 -0.0072 0.0130  -0.0035 114 GLU   A OE1 
2331 O  OE2 . GLU   A 114 ? 0.1619 0.1332 0.2241 -0.0128 0.0085  -0.0087 114 GLU   A OE2 
2338 N  N   . ASN   A 115 ? 0.1298 0.1267 0.1754 -0.0058 0.0120  0.0054  115 ASN   A N   
2339 C  CA  . ASN   A 115 ? 0.1311 0.1300 0.1829 -0.0085 0.0162  0.0097  115 ASN   A CA  
2340 C  C   . ASN   A 115 ? 0.1314 0.1297 0.1789 -0.0097 0.0050  0.0099  115 ASN   A C   
2341 O  O   . ASN   A 115 ? 0.1309 0.1391 0.1847 -0.0103 0.0109  0.0187  115 ASN   A O   
2342 C  CB  . ASN   A 115 ? 0.1449 0.1354 0.1655 -0.0128 0.0156  0.0013  115 ASN   A CB  
2343 C  CG  . ASN   A 115 ? 0.1402 0.1560 0.1723 -0.0167 0.0234  0.0044  115 ASN   A CG  
2344 O  OD1 . ASN   A 115 ? 0.1405 0.2518 0.2016 -0.0160 0.0297  0.0160  115 ASN   A OD1 
2345 N  ND2 . ASN   A 115 ? 0.1381 0.1355 0.1762 -0.0105 0.0254  0.0094  115 ASN   A ND2 
2352 N  N   . PHE   A 116 ? 0.1265 0.1264 0.1874 -0.0017 0.0082  0.0204  116 PHE   A N   
2353 C  CA  . PHE   A 116 ? 0.1273 0.1386 0.1841 -0.0003 0.0138  0.0162  116 PHE   A CA  
2354 C  C   . PHE   A 116 ? 0.1234 0.1424 0.1844 -0.0086 0.0142  0.0210  116 PHE   A C   
2355 O  O   . PHE   A 116 ? 0.1321 0.1492 0.1868 -0.0023 0.0090  0.0303  116 PHE   A O   
2356 C  CB  . PHE   A 116 ? 0.1288 0.1324 0.1929 -0.0051 0.0149  0.0194  116 PHE   A CB  
2357 C  CG  . PHE   A 116 ? 0.1285 0.1299 0.1726 -0.0063 0.0085  0.0095  116 PHE   A CG  
2358 C  CD1 . PHE   A 116 ? 0.1365 0.1301 0.1676 -0.0051 0.0172  0.0098  116 PHE   A CD1 
2359 C  CD2 . PHE   A 116 ? 0.1344 0.1362 0.1850 -0.0050 0.0161  0.0195  116 PHE   A CD2 
2360 C  CE1 . PHE   A 116 ? 0.1389 0.1220 0.1790 -0.0143 0.0088  0.0093  116 PHE   A CE1 
2361 C  CE2 . PHE   A 116 ? 0.1380 0.1357 0.2013 -0.0051 0.0143  0.0123  116 PHE   A CE2 
2362 C  CZ  . PHE   A 116 ? 0.1366 0.1221 0.1846 -0.0050 0.0043  0.0131  116 PHE   A CZ  
2372 N  N   . ASN   A 117 ? 0.1262 0.1335 0.1974 -0.0067 0.0137  0.0239  117 ASN   A N   
2373 C  CA  . ASN   A 117 ? 0.1298 0.1359 0.2009 -0.0034 0.0120  0.0298  117 ASN   A CA  
2374 C  C   . ASN   A 117 ? 0.1336 0.1441 0.2106 -0.0031 0.0119  0.0265  117 ASN   A C   
2375 O  O   . ASN   A 117 ? 0.1438 0.1478 0.2344 -0.0046 -0.0079 0.0393  117 ASN   A O   
2376 C  CB  . ASN   A 117 ? 0.1333 0.1403 0.2042 -0.0045 0.0114  0.0289  117 ASN   A CB  
2377 C  CG  . ASN   A 117 ? 0.1332 0.1373 0.2028 -0.0033 0.0154  0.0359  117 ASN   A CG  
2378 O  OD1 . ASN   A 117 ? 0.1336 0.1596 0.2183 -0.0158 0.0113  0.0248  117 ASN   A OD1 
2379 N  ND2 . ASN   A 117 ? 0.1330 0.1373 0.2072 -0.0002 0.0051  0.0319  117 ASN   A ND2 
2386 N  N   . GLN   A 118 ? 0.1268 0.1472 0.2075 -0.0099 0.0012  0.0306  118 GLN   A N   
2387 C  CA  . GLN   A 118 ? 0.1373 0.1547 0.2090 -0.0079 -0.0048 0.0337  118 GLN   A CA  
2388 C  C   . GLN   A 118 ? 0.1393 0.1601 0.1975 -0.0114 -0.0032 0.0332  118 GLN   A C   
2389 O  O   . GLN   A 118 ? 0.1399 0.1951 0.2190 -0.0025 -0.0125 0.0102  118 GLN   A O   
2390 C  CB  . GLN   A 118 ? 0.1350 0.1568 0.2166 -0.0043 0.0039  0.0331  118 GLN   A CB  
2391 C  CG  . GLN   A 118 ? 0.1346 0.1583 0.2202 -0.0025 0.0098  0.0309  118 GLN   A CG  
2392 C  CD  . GLN   A 118 ? 0.1311 0.1596 0.2306 0.0014  0.0104  0.0229  118 GLN   A CD  
2393 O  OE1 . GLN   A 118 ? 0.1383 0.1728 0.2537 0.0109  0.0057  0.0161  118 GLN   A OE1 
2394 N  NE2 . GLN   A 118 ? 0.1431 0.1544 0.2290 0.0020  0.0105  0.0236  118 GLN   A NE2 
2403 N  N   . HIS   A 119 ? 0.1435 0.1643 0.1835 -0.0090 -0.0009 0.0324  119 HIS   A N   
2404 C  CA  . HIS   A 119 ? 0.1467 0.1740 0.1873 -0.0108 -0.0074 0.0379  119 HIS   A CA  
2405 C  C   . HIS   A 119 ? 0.1509 0.1846 0.1834 -0.0094 0.0038  0.0447  119 HIS   A C   
2406 O  O   . HIS   A 119 ? 0.1573 0.1855 0.1903 -0.0243 -0.0015 0.0492  119 HIS   A O   
2407 C  CB  . HIS   A 119 ? 0.1544 0.1709 0.2047 -0.0081 0.0140  0.0343  119 HIS   A CB  
2408 C  CG  . HIS   A 119 ? 0.1571 0.1742 0.2490 -0.0026 0.0140  0.0428  119 HIS   A CG  
2409 N  ND1 . HIS   A 119 ? 0.1724 0.1930 0.2953 -0.0125 0.0098  0.0312  119 HIS   A ND1 
2410 C  CD2 . HIS   A 119 ? 0.1604 0.1789 0.2637 0.0151  0.0334  0.0608  119 HIS   A CD2 
2411 C  CE1 . HIS   A 119 ? 0.1717 0.1872 0.3017 -0.0209 0.0273  0.0536  119 HIS   A CE1 
2412 N  NE2 . HIS   A 119 ? 0.1777 0.1856 0.2945 0.0037  0.0434  0.0650  119 HIS   A NE2 
2420 N  N   . GLU   A 120 ? 0.1575 0.2120 0.1975 -0.0083 -0.0050 0.0705  120 GLU   A N   
2421 C  CA  . GLU   A 120 ? 0.1880 0.2450 0.2310 0.0002  -0.0079 0.1098  120 GLU   A CA  
2422 C  C   . GLU   A 120 ? 0.1655 0.2267 0.2007 -0.0119 -0.0040 0.1034  120 GLU   A C   
2423 O  O   . GLU   A 120 ? 0.1671 0.2118 0.2122 -0.0208 -0.0046 0.0919  120 GLU   A O   
2424 C  CB  . GLU   A 120 ? 0.2656 0.3135 0.2949 0.0171  -0.0035 0.1519  120 GLU   A CB  
2425 C  CG  . GLU   A 120 ? 0.3691 0.3934 0.4103 0.0274  0.0029  0.1559  120 GLU   A CG  
2426 C  CD  . GLU   A 120 ? 0.4629 0.4675 0.5300 0.0323  0.0189  0.1380  120 GLU   A CD  
2427 O  OE1 . GLU   A 120 ? 0.4831 0.4831 0.5613 0.0334  0.0233  0.1300  120 GLU   A OE1 
2428 O  OE2 . GLU   A 120 ? 0.5103 0.5103 0.5792 0.0336  0.0258  0.1304  120 GLU   A OE2 
2435 N  N   . VAL   A 121 ? 0.1607 0.2254 0.1733 -0.0131 0.0023  0.0770  121 VAL   A N   
2436 C  CA  . VAL   A 121 ? 0.1682 0.2303 0.1642 -0.0214 0.0225  0.0693  121 VAL   A CA  
2437 C  C   . VAL   A 121 ? 0.1579 0.2120 0.1465 -0.0238 0.0103  0.0517  121 VAL   A C   
2438 O  O   . VAL   A 121 ? 0.1642 0.2080 0.1661 -0.0270 -0.0055 0.0519  121 VAL   A O   
2439 C  CB  . VAL   A 121 ? 0.2087 0.2648 0.1912 -0.0066 0.0329  0.0702  121 VAL   A CB  
2440 C  CG1 . VAL   A 121 ? 0.2113 0.2800 0.1916 0.0022  0.0361  0.0714  121 VAL   A CG1 
2441 C  CG2 . VAL   A 121 ? 0.2298 0.2768 0.2284 -0.0144 0.0260  0.0538  121 VAL   A CG2 
2451 N  N   . LEU   A 122 ? 0.1458 0.1872 0.1556 -0.0219 0.0024  0.0391  122 LEU   A N   
2452 C  CA  . LEU   A 122 ? 0.1548 0.1670 0.1507 -0.0204 0.0151  0.0392  122 LEU   A CA  
2453 C  C   . LEU   A 122 ? 0.1502 0.1659 0.1498 -0.0278 0.0009  0.0372  122 LEU   A C   
2454 O  O   . LEU   A 122 ? 0.1534 0.1749 0.1828 -0.0314 -0.0046 0.0377  122 LEU   A O   
2455 C  CB  . LEU   A 122 ? 0.1745 0.1721 0.1808 -0.0076 0.0054  0.0431  122 LEU   A CB  
2456 C  CG  . LEU   A 122 ? 0.1787 0.1772 0.1714 -0.0125 0.0113  0.0385  122 LEU   A CG  
2457 C  CD1 . LEU   A 122 ? 0.1989 0.1745 0.1816 -0.0205 0.0256  0.0394  122 LEU   A CD1 
2458 C  CD2 . LEU   A 122 ? 0.1753 0.1666 0.1694 -0.0072 0.0206  0.0352  122 LEU   A CD2 
2470 N  N   A LEU   A 123 ? 0.1432 0.1659 0.1515 -0.0221 0.0033  0.0307  123 LEU   A N   
2471 N  N   B LEU   A 123 ? 0.1469 0.1649 0.1412 -0.0263 -0.0011 0.0293  123 LEU   A N   
2472 C  CA  A LEU   A 123 ? 0.1458 0.1654 0.1329 -0.0145 0.0010  0.0301  123 LEU   A CA  
2473 C  CA  B LEU   A 123 ? 0.1506 0.1628 0.1263 -0.0224 -0.0031 0.0261  123 LEU   A CA  
2474 C  C   A LEU   A 123 ? 0.1387 0.1525 0.1311 -0.0161 0.0072  0.0279  123 LEU   A C   
2475 C  C   B LEU   A 123 ? 0.1429 0.1562 0.1090 -0.0202 0.0001  0.0237  123 LEU   A C   
2476 O  O   A LEU   A 123 ? 0.1309 0.1493 0.1359 -0.0148 0.0181  0.0120  123 LEU   A O   
2477 O  O   B LEU   A 123 ? 0.1381 0.1546 0.1193 -0.0199 0.0113  0.0155  123 LEU   A O   
2478 C  CB  A LEU   A 123 ? 0.1513 0.1805 0.1245 -0.0179 0.0208  0.0282  123 LEU   A CB  
2479 C  CB  B LEU   A 123 ? 0.1593 0.1694 0.1293 -0.0313 0.0024  0.0251  123 LEU   A CB  
2480 C  CG  A LEU   A 123 ? 0.1585 0.1936 0.1318 -0.0079 0.0186  0.0068  123 LEU   A CG  
2481 C  CG  B LEU   A 123 ? 0.1658 0.1731 0.1280 -0.0321 0.0045  0.0189  123 LEU   A CG  
2482 C  CD1 A LEU   A 123 ? 0.1597 0.1988 0.1482 -0.0042 0.0189  -0.0045 123 LEU   A CD1 
2483 C  CD1 B LEU   A 123 ? 0.1706 0.1734 0.1413 -0.0336 0.0077  0.0174  123 LEU   A CD1 
2484 C  CD2 A LEU   A 123 ? 0.1655 0.2014 0.1379 -0.0092 0.0095  0.0048  123 LEU   A CD2 
2485 C  CD2 B LEU   A 123 ? 0.1682 0.1772 0.1322 -0.0346 -0.0034 0.0147  123 LEU   A CD2 
2508 N  N   A ALA   A 124 ? 0.1389 0.1409 0.1325 -0.0178 0.0146  0.0358  124 ALA   A N   
2509 N  N   B ALA   A 124 ? 0.1464 0.1476 0.1102 -0.0149 -0.0016 0.0236  124 ALA   A N   
2510 C  CA  A ALA   A 124 ? 0.1322 0.1354 0.1396 -0.0073 0.0110  0.0292  124 ALA   A CA  
2511 C  CA  B ALA   A 124 ? 0.1470 0.1490 0.1203 -0.0161 -0.0028 0.0197  124 ALA   A CA  
2512 C  C   A ALA   A 124 ? 0.1202 0.1355 0.1416 -0.0075 0.0102  0.0172  124 ALA   A C   
2513 C  C   B ALA   A 124 ? 0.1481 0.1488 0.1118 -0.0113 0.0015  0.0196  124 ALA   A C   
2514 O  O   A ALA   A 124 ? 0.1145 0.1322 0.1591 -0.0174 0.0196  0.0233  124 ALA   A O   
2515 O  O   B ALA   A 124 ? 0.1559 0.1542 0.1292 -0.0103 0.0049  0.0273  124 ALA   A O   
2516 C  CB  A ALA   A 124 ? 0.1387 0.1370 0.1607 -0.0040 0.0122  0.0280  124 ALA   A CB  
2517 C  CB  B ALA   A 124 ? 0.1403 0.1496 0.1422 -0.0208 -0.0008 0.0145  124 ALA   A CB  
2528 N  N   A PRO   A 125 ? 0.1195 0.1366 0.1529 -0.0087 0.0077  0.0199  125 PRO   A N   
2529 N  N   B PRO   A 125 ? 0.1384 0.1404 0.1008 -0.0120 -0.0005 0.0321  125 PRO   A N   
2530 C  CA  A PRO   A 125 ? 0.1244 0.1352 0.1489 0.0005  0.0085  0.0156  125 PRO   A CA  
2531 C  CA  B PRO   A 125 ? 0.1407 0.1377 0.1138 -0.0153 0.0036  0.0200  125 PRO   A CA  
2532 C  C   A PRO   A 125 ? 0.1183 0.1321 0.1450 -0.0017 0.0101  0.0216  125 PRO   A C   
2533 C  C   B PRO   A 125 ? 0.1458 0.1472 0.1274 -0.0110 -0.0022 0.0074  125 PRO   A C   
2534 O  O   A PRO   A 125 ? 0.1173 0.1302 0.1472 0.0013  0.0190  0.0175  125 PRO   A O   
2535 O  O   B PRO   A 125 ? 0.1483 0.1505 0.1378 -0.0075 0.0037  0.0074  125 PRO   A O   
2536 C  CB  A PRO   A 125 ? 0.1390 0.1356 0.1504 -0.0076 0.0055  0.0100  125 PRO   A CB  
2537 C  CB  B PRO   A 125 ? 0.1374 0.1352 0.1115 -0.0209 0.0068  0.0247  125 PRO   A CB  
2538 C  CG  A PRO   A 125 ? 0.1404 0.1381 0.1519 -0.0098 0.0101  0.0158  125 PRO   A CG  
2539 C  CG  B PRO   A 125 ? 0.1326 0.1339 0.1078 -0.0154 0.0048  0.0281  125 PRO   A CG  
2540 C  CD  A PRO   A 125 ? 0.1265 0.1451 0.1550 -0.0130 0.0131  0.0232  125 PRO   A CD  
2541 C  CD  B PRO   A 125 ? 0.1315 0.1359 0.1090 -0.0101 0.0086  0.0355  125 PRO   A CD  
2556 N  N   A LEU   A 126 ? 0.1148 0.1399 0.1562 0.0018  0.0155  0.0225  126 LEU   A N   
2557 N  N   B LEU   A 126 ? 0.1567 0.1570 0.1424 -0.0058 -0.0072 0.0022  126 LEU   A N   
2558 C  CA  A LEU   A 126 ? 0.1192 0.1444 0.1485 -0.0038 0.0139  0.0202  126 LEU   A CA  
2559 C  CA  B LEU   A 126 ? 0.1611 0.1667 0.1566 -0.0041 -0.0031 0.0018  126 LEU   A CA  
2560 C  C   A LEU   A 126 ? 0.1333 0.1409 0.1469 -0.0005 0.0071  0.0217  126 LEU   A C   
2561 C  C   B LEU   A 126 ? 0.1638 0.1624 0.1462 0.0092  0.0028  -0.0005 126 LEU   A C   
2562 O  O   A LEU   A 126 ? 0.1435 0.1423 0.1716 0.0084  0.0186  0.0261  126 LEU   A O   
2563 O  O   B LEU   A 126 ? 0.1740 0.1662 0.1667 0.0019  -0.0056 0.0060  126 LEU   A O   
2564 C  CB  A LEU   A 126 ? 0.1240 0.1550 0.1499 -0.0036 0.0060  0.0174  126 LEU   A CB  
2565 C  CB  B LEU   A 126 ? 0.1718 0.1829 0.2010 -0.0150 -0.0147 0.0035  126 LEU   A CB  
2566 C  CG  A LEU   A 126 ? 0.1220 0.1721 0.1546 -0.0175 0.0166  0.0108  126 LEU   A CG  
2567 C  CG  B LEU   A 126 ? 0.1751 0.1975 0.2309 -0.0232 -0.0251 0.0137  126 LEU   A CG  
2568 C  CD1 A LEU   A 126 ? 0.1294 0.1892 0.1828 -0.0147 0.0043  0.0100  126 LEU   A CD1 
2569 C  CD1 B LEU   A 126 ? 0.1741 0.2008 0.2333 -0.0243 -0.0334 0.0142  126 LEU   A CD1 
2570 C  CD2 A LEU   A 126 ? 0.1348 0.1708 0.1500 -0.0240 0.0179  0.0261  126 LEU   A CD2 
2571 C  CD2 B LEU   A 126 ? 0.1758 0.2009 0.2402 -0.0267 -0.0242 0.0197  126 LEU   A CD2 
2594 N  N   A LEU   A 127 ? 0.1315 0.1447 0.1329 -0.0025 0.0074  0.0195  127 LEU   A N   
2595 N  N   B LEU   A 127 ? 0.1625 0.1656 0.1349 0.0225  0.0063  0.0033  127 LEU   A N   
2596 C  CA  A LEU   A 127 ? 0.1261 0.1417 0.1268 -0.0088 0.0012  0.0061  127 LEU   A CA  
2597 C  CA  B LEU   A 127 ? 0.1637 0.1708 0.1358 0.0268  0.0005  0.0159  127 LEU   A CA  
2598 C  C   A LEU   A 127 ? 0.1241 0.1298 0.1256 -0.0064 -0.0001 -0.0050 127 LEU   A C   
2599 C  C   B LEU   A 127 ? 0.1655 0.1630 0.1201 0.0178  0.0018  0.0184  127 LEU   A C   
2600 O  O   A LEU   A 127 ? 0.1298 0.1298 0.1265 -0.0157 -0.0004 -0.0010 127 LEU   A O   
2601 O  O   B LEU   A 127 ? 0.1754 0.1655 0.1325 0.0150  -0.0044 0.0120  127 LEU   A O   
2602 C  CB  A LEU   A 127 ? 0.1366 0.1588 0.1351 0.0013  0.0053  0.0084  127 LEU   A CB  
2603 C  CB  B LEU   A 127 ? 0.1645 0.1891 0.1500 0.0345  0.0022  0.0209  127 LEU   A CB  
2604 C  CG  A LEU   A 127 ? 0.1446 0.1655 0.1436 0.0068  -0.0041 0.0132  127 LEU   A CG  
2605 C  CG  B LEU   A 127 ? 0.1612 0.2065 0.1569 0.0385  -0.0079 0.0317  127 LEU   A CG  
2606 C  CD1 A LEU   A 127 ? 0.1512 0.1540 0.1582 0.0030  -0.0057 0.0096  127 LEU   A CD1 
2607 C  CD1 B LEU   A 127 ? 0.1627 0.2054 0.1687 0.0361  -0.0027 0.0469  127 LEU   A CD1 
2608 C  CD2 A LEU   A 127 ? 0.1492 0.1628 0.1469 0.0312  -0.0019 0.0045  127 LEU   A CD2 
2609 C  CD2 B LEU   A 127 ? 0.1673 0.2197 0.1536 0.0468  -0.0131 0.0304  127 LEU   A CD2 
2632 N  N   A SER   A 128 ? 0.1265 0.1331 0.1380 -0.0107 -0.0135 -0.0084 128 SER   A N   
2633 N  N   B SER   A 128 ? 0.1615 0.1586 0.1199 0.0114  0.0072  0.0251  128 SER   A N   
2634 C  CA  A SER   A 128 ? 0.1389 0.1372 0.1355 -0.0114 -0.0095 -0.0065 128 SER   A CA  
2635 C  CA  B SER   A 128 ? 0.1667 0.1569 0.1151 0.0069  0.0109  0.0261  128 SER   A CA  
2636 C  C   A SER   A 128 ? 0.1423 0.1367 0.1252 -0.0087 -0.0165 0.0028  128 SER   A C   
2637 C  C   B SER   A 128 ? 0.1717 0.1552 0.1192 0.0126  0.0184  0.0253  128 SER   A C   
2638 O  O   A SER   A 128 ? 0.1489 0.1434 0.1439 -0.0098 -0.0139 0.0099  128 SER   A O   
2639 O  O   B SER   A 128 ? 0.1838 0.1639 0.1391 0.0078  0.0176  0.0222  128 SER   A O   
2640 C  CB  A SER   A 128 ? 0.1384 0.1476 0.1382 -0.0102 -0.0062 -0.0007 128 SER   A CB  
2641 C  CB  B SER   A 128 ? 0.1622 0.1613 0.1157 0.0031  0.0005  0.0180  128 SER   A CB  
2642 O  OG  A SER   A 128 ? 0.1390 0.1537 0.1545 -0.0082 0.0065  0.0048  128 SER   A OG  
2643 O  OG  B SER   A 128 ? 0.1608 0.1593 0.1327 0.0059  0.0016  0.0107  128 SER   A OG  
2654 N  N   A ALA   A 129 ? 0.1394 0.1446 0.1401 -0.0069 -0.0207 0.0089  129 ALA   A N   
2655 N  N   B ALA   A 129 ? 0.1716 0.1582 0.1367 0.0163  0.0112  0.0279  129 ALA   A N   
2656 C  CA  A ALA   A 129 ? 0.1386 0.1515 0.1502 -0.0017 -0.0114 0.0086  129 ALA   A CA  
2657 C  CA  B ALA   A 129 ? 0.1734 0.1601 0.1429 0.0194  0.0055  0.0195  129 ALA   A CA  
2658 C  C   A ALA   A 129 ? 0.1533 0.1517 0.1342 0.0024  -0.0068 0.0036  129 ALA   A C   
2659 C  C   B ALA   A 129 ? 0.1894 0.1638 0.1409 0.0176  -0.0107 0.0146  129 ALA   A C   
2660 O  O   A ALA   A 129 ? 0.1658 0.1604 0.1448 -0.0075 -0.0061 0.0126  129 ALA   A O   
2661 O  O   B ALA   A 129 ? 0.1959 0.1678 0.1520 0.0035  -0.0159 0.0154  129 ALA   A O   
2662 C  CB  A ALA   A 129 ? 0.1410 0.1570 0.1663 -0.0025 -0.0065 0.0104  129 ALA   A CB  
2663 C  CB  B ALA   A 129 ? 0.1725 0.1628 0.1487 0.0144  0.0139  0.0092  129 ALA   A CB  
2674 N  N   A GLY   A 130 ? 0.1576 0.1511 0.1458 0.0075  0.0033  0.0062  130 GLY   A N   
2675 N  N   B GLY   A 130 ? 0.2037 0.1712 0.1489 0.0234  -0.0180 0.0199  130 GLY   A N   
2676 C  CA  A GLY   A 130 ? 0.1710 0.1484 0.1228 0.0066  0.0134  0.0088  130 GLY   A CA  
2677 C  CA  B GLY   A 130 ? 0.2221 0.1786 0.1502 0.0177  -0.0219 0.0179  130 GLY   A CA  
2678 C  C   A GLY   A 130 ? 0.1696 0.1384 0.1029 0.0097  0.0061  0.0015  130 GLY   A C   
2679 C  C   B GLY   A 130 ? 0.2298 0.1812 0.1559 0.0087  -0.0253 0.0127  130 GLY   A C   
2680 O  O   A GLY   A 130 ? 0.1666 0.1398 0.1189 0.0085  -0.0009 0.0026  130 GLY   A O   
2681 O  O   B GLY   A 130 ? 0.2298 0.1810 0.1559 0.0046  -0.0254 0.0167  130 GLY   A O   
2688 N  N   A ILE   A 131 ? 0.1799 0.1327 0.1023 0.0040  0.0004  -0.0034 131 ILE   A N   
2689 N  N   B ILE   A 131 ? 0.2382 0.1869 0.1809 -0.0002 -0.0208 0.0105  131 ILE   A N   
2690 C  CA  A ILE   A 131 ? 0.1855 0.1350 0.0707 -0.0053 -0.0114 -0.0048 131 ILE   A CA  
2691 C  CA  B ILE   A 131 ? 0.2472 0.1918 0.2186 -0.0064 -0.0173 0.0079  131 ILE   A CA  
2692 C  C   A ILE   A 131 ? 0.1714 0.1383 0.0756 -0.0030 -0.0029 0.0056  131 ILE   A C   
2693 C  C   B ILE   A 131 ? 0.2343 0.1904 0.2038 -0.0008 -0.0102 0.0225  131 ILE   A C   
2694 O  O   A ILE   A 131 ? 0.1721 0.1401 0.0946 0.0001  -0.0046 0.0037  131 ILE   A O   
2695 O  O   B ILE   A 131 ? 0.2362 0.1955 0.2098 0.0045  -0.0082 0.0324  131 ILE   A O   
2696 C  CB  A ILE   A 131 ? 0.2094 0.1539 0.0934 -0.0179 -0.0170 -0.0110 131 ILE   A CB  
2697 C  CB  B ILE   A 131 ? 0.2676 0.2029 0.2740 -0.0169 -0.0179 -0.0051 131 ILE   A CB  
2698 C  CG1 A ILE   A 131 ? 0.2137 0.1867 0.1006 -0.0286 -0.0203 -0.0139 131 ILE   A CG1 
2699 C  CG1 B ILE   A 131 ? 0.2778 0.2181 0.3163 -0.0233 -0.0194 -0.0012 131 ILE   A CG1 
2700 C  CG2 A ILE   A 131 ? 0.2260 0.1406 0.1206 -0.0102 -0.0052 -0.0247 131 ILE   A CG2 
2701 C  CG2 B ILE   A 131 ? 0.2740 0.1983 0.2788 -0.0162 -0.0142 -0.0114 131 ILE   A CG2 
2702 C  CD1 A ILE   A 131 ? 0.2186 0.2004 0.1384 -0.0301 -0.0194 -0.0208 131 ILE   A CD1 
2703 C  CD1 B ILE   A 131 ? 0.2834 0.2265 0.3399 -0.0282 -0.0216 0.0029  131 ILE   A CD1 
2726 N  N   A PHE   A 132 ? 0.1627 0.1324 0.0931 0.0002  -0.0019 0.0120  132 PHE   A N   
2727 N  N   B PHE   A 132 ? 0.2215 0.1818 0.1803 0.0014  -0.0105 0.0105  132 PHE   A N   
2728 C  CA  A PHE   A 132 ? 0.1589 0.1410 0.1026 -0.0065 0.0059  0.0088  132 PHE   A CA  
2729 C  CA  B PHE   A 132 ? 0.2123 0.1847 0.1753 0.0030  -0.0120 0.0064  132 PHE   A CA  
2730 C  C   A PHE   A 132 ? 0.1610 0.1619 0.0962 0.0018  0.0084  0.0084  132 PHE   A C   
2731 C  C   B PHE   A 132 ? 0.2104 0.1903 0.1793 0.0045  -0.0108 0.0057  132 PHE   A C   
2732 O  O   A PHE   A 132 ? 0.1645 0.1825 0.1130 0.0058  0.0065  -0.0012 132 PHE   A O   
2733 O  O   B PHE   A 132 ? 0.2173 0.1953 0.1955 0.0057  -0.0106 0.0103  132 PHE   A O   
2734 C  CB  A PHE   A 132 ? 0.1565 0.1289 0.1058 -0.0081 -0.0020 0.0201  132 PHE   A CB  
2735 C  CB  B PHE   A 132 ? 0.2049 0.1865 0.1612 0.0048  -0.0169 0.0097  132 PHE   A CB  
2736 C  CG  A PHE   A 132 ? 0.1567 0.1319 0.1134 -0.0027 -0.0126 0.0176  132 PHE   A CG  
2737 C  CG  B PHE   A 132 ? 0.2006 0.1885 0.1541 0.0065  -0.0145 0.0064  132 PHE   A CG  
2738 C  CD1 A PHE   A 132 ? 0.1611 0.1434 0.1378 0.0011  -0.0190 0.0053  132 PHE   A CD1 
2739 C  CD1 B PHE   A 132 ? 0.1974 0.1923 0.1603 0.0060  -0.0143 -0.0008 132 PHE   A CD1 
2740 C  CD2 A PHE   A 132 ? 0.1582 0.1432 0.1311 0.0030  -0.0145 0.0048  132 PHE   A CD2 
2741 C  CD2 B PHE   A 132 ? 0.1978 0.1934 0.1584 0.0069  -0.0118 0.0067  132 PHE   A CD2 
2742 C  CE1 A PHE   A 132 ? 0.1624 0.1456 0.1447 0.0030  -0.0227 0.0024  132 PHE   A CE1 
2743 C  CE1 B PHE   A 132 ? 0.1956 0.1920 0.1579 0.0026  -0.0098 -0.0006 132 PHE   A CE1 
2744 C  CE2 A PHE   A 132 ? 0.1556 0.1495 0.1456 0.0103  -0.0168 0.0023  132 PHE   A CE2 
2745 C  CE2 B PHE   A 132 ? 0.1942 0.1935 0.1549 0.0061  -0.0072 0.0076  132 PHE   A CE2 
2746 C  CZ  A PHE   A 132 ? 0.1571 0.1493 0.1501 -0.0004 -0.0208 -0.0002 132 PHE   A CZ  
2747 C  CZ  B PHE   A 132 ? 0.1924 0.1928 0.1536 -0.0008 -0.0045 0.0034  132 PHE   A CZ  
2766 N  N   A GLY   A 133 ? 0.1638 0.1652 0.0977 0.0008  -0.0037 0.0143  133 GLY   A N   
2767 N  N   B GLY   A 133 ? 0.2030 0.1898 0.1704 0.0055  -0.0140 0.0004  133 GLY   A N   
2768 C  CA  A GLY   A 133 ? 0.1684 0.1721 0.1103 0.0035  -0.0129 0.0011  133 GLY   A CA  
2769 C  CA  B GLY   A 133 ? 0.1961 0.1938 0.1643 0.0003  -0.0165 -0.0074 133 GLY   A CA  
2770 C  C   A GLY   A 133 ? 0.1706 0.1827 0.1271 0.0067  -0.0219 -0.0077 133 GLY   A C   
2771 C  C   B GLY   A 133 ? 0.1914 0.2002 0.1678 -0.0045 -0.0144 -0.0144 133 GLY   A C   
2772 O  O   A GLY   A 133 ? 0.1823 0.1924 0.1323 0.0190  -0.0326 -0.0346 133 GLY   A O   
2773 O  O   B GLY   A 133 ? 0.2002 0.2125 0.1862 0.0009  -0.0093 -0.0275 133 GLY   A O   
2780 N  N   A ALA   A 134 ? 0.1729 0.1756 0.1450 -0.0029 -0.0160 -0.0099 134 ALA   A N   
2781 N  N   B ALA   A 134 ? 0.1863 0.1929 0.1604 -0.0147 -0.0157 -0.0145 134 ALA   A N   
2782 C  CA  A ALA   A 134 ? 0.1747 0.1657 0.1718 0.0040  -0.0181 -0.0118 134 ALA   A CA  
2783 C  CA  B ALA   A 134 ? 0.1840 0.1954 0.1682 -0.0164 -0.0162 -0.0147 134 ALA   A CA  
2784 C  C   A ALA   A 134 ? 0.1773 0.1618 0.1775 0.0060  -0.0089 -0.0033 134 ALA   A C   
2785 C  C   B ALA   A 134 ? 0.1862 0.2053 0.1669 -0.0202 -0.0079 -0.0214 134 ALA   A C   
2786 O  O   A ALA   A 134 ? 0.1974 0.1657 0.1988 0.0032  0.0151  -0.0094 134 ALA   A O   
2787 O  O   B ALA   A 134 ? 0.2048 0.2129 0.1774 -0.0216 -0.0068 -0.0336 134 ALA   A O   
2788 C  CB  A ALA   A 134 ? 0.1791 0.1660 0.2008 0.0077  -0.0277 -0.0171 134 ALA   A CB  
2789 C  CB  B ALA   A 134 ? 0.1898 0.1915 0.1849 -0.0152 -0.0201 -0.0111 134 ALA   A CB  
2800 N  N   A ASP   A 135 ? 0.1751 0.1661 0.1813 -0.0094 -0.0214 0.0007  135 ASP   A N   
2801 N  N   B ASP   A 135 ? 0.1816 0.2059 0.1718 -0.0163 -0.0030 -0.0216 135 ASP   A N   
2802 C  CA  A ASP   A 135 ? 0.1718 0.1760 0.2007 -0.0154 -0.0276 0.0100  135 ASP   A CA  
2803 C  CA  B ASP   A 135 ? 0.1827 0.2111 0.1786 -0.0132 -0.0057 -0.0165 135 ASP   A CA  
2804 C  C   A ASP   A 135 ? 0.1586 0.1701 0.1957 -0.0072 -0.0171 0.0173  135 ASP   A C   
2805 C  C   B ASP   A 135 ? 0.1821 0.1981 0.1702 -0.0056 -0.0034 -0.0066 135 ASP   A C   
2806 O  O   A ASP   A 135 ? 0.1537 0.1604 0.2054 -0.0031 -0.0150 0.0233  135 ASP   A O   
2807 O  O   B ASP   A 135 ? 0.1839 0.1966 0.1820 -0.0024 -0.0063 0.0045  135 ASP   A O   
2808 C  CB  A ASP   A 135 ? 0.1906 0.2029 0.2389 -0.0263 -0.0447 0.0053  135 ASP   A CB  
2809 C  CB  B ASP   A 135 ? 0.1935 0.2309 0.2193 -0.0198 -0.0093 -0.0279 135 ASP   A CB  
2810 C  CG  A ASP   A 135 ? 0.2060 0.2337 0.2830 -0.0347 -0.0493 -0.0011 135 ASP   A CG  
2811 C  CG  B ASP   A 135 ? 0.2037 0.2454 0.2598 -0.0252 -0.0115 -0.0394 135 ASP   A CG  
2812 O  OD1 A ASP   A 135 ? 0.1958 0.2385 0.2856 -0.0300 -0.0546 0.0141  135 ASP   A OD1 
2813 O  OD1 B ASP   A 135 ? 0.2052 0.2522 0.2647 -0.0347 -0.0209 -0.0384 135 ASP   A OD1 
2814 O  OD2 A ASP   A 135 ? 0.2260 0.2592 0.3250 -0.0377 -0.0378 -0.0218 135 ASP   A OD2 
2815 O  OD2 B ASP   A 135 ? 0.2147 0.2512 0.2944 -0.0264 -0.0010 -0.0432 135 ASP   A OD2 
2824 N  N   A PRO   A 136 ? 0.1507 0.1667 0.1856 -0.0033 -0.0097 0.0182  136 PRO   A N   
2825 N  N   B PRO   A 136 ? 0.1791 0.1865 0.1642 -0.0011 -0.0047 -0.0071 136 PRO   A N   
2826 C  CA  A PRO   A 136 ? 0.1469 0.1682 0.1891 -0.0101 -0.0018 0.0024  136 PRO   A CA  
2827 C  CA  B PRO   A 136 ? 0.1706 0.1812 0.1686 -0.0052 -0.0080 -0.0098 136 PRO   A CA  
2828 C  C   A PRO   A 136 ? 0.1364 0.1680 0.1807 -0.0062 0.0045  0.0066  136 PRO   A C   
2829 C  C   B PRO   A 136 ? 0.1618 0.1760 0.1791 -0.0004 -0.0123 -0.0091 136 PRO   A C   
2830 O  O   A PRO   A 136 ? 0.1334 0.1611 0.1574 -0.0054 0.0175  0.0015  136 PRO   A O   
2831 O  O   B PRO   A 136 ? 0.1612 0.1818 0.1813 -0.0045 -0.0175 -0.0079 136 PRO   A O   
2832 C  CB  A PRO   A 136 ? 0.1636 0.1679 0.2022 -0.0046 -0.0088 0.0027  136 PRO   A CB  
2833 C  CB  B PRO   A 136 ? 0.1796 0.1787 0.1620 -0.0028 -0.0106 -0.0068 136 PRO   A CB  
2834 C  CG  A PRO   A 136 ? 0.1734 0.1744 0.2129 0.0083  -0.0127 0.0071  136 PRO   A CG  
2835 C  CG  B PRO   A 136 ? 0.1858 0.1797 0.1589 -0.0002 -0.0168 -0.0132 136 PRO   A CG  
2836 C  CD  A PRO   A 136 ? 0.1631 0.1699 0.2019 0.0054  -0.0128 0.0254  136 PRO   A CD  
2837 C  CD  B PRO   A 136 ? 0.1866 0.1816 0.1581 0.0030  -0.0057 -0.0088 136 PRO   A CD  
2852 N  N   A ILE   A 137 ? 0.1366 0.1725 0.1974 -0.0078 -0.0002 0.0082  137 ILE   A N   
2853 N  N   B ILE   A 137 ? 0.1560 0.1738 0.1901 -0.0014 -0.0181 -0.0062 137 ILE   A N   
2854 C  CA  A ILE   A 137 ? 0.1407 0.1786 0.1971 -0.0092 0.0010  0.0027  137 ILE   A CA  
2855 C  CA  B ILE   A 137 ? 0.1538 0.1798 0.2010 -0.0050 -0.0162 -0.0030 137 ILE   A CA  
2856 C  C   A ILE   A 137 ? 0.1403 0.1791 0.1931 -0.0135 0.0049  0.0054  137 ILE   A C   
2857 C  C   B ILE   A 137 ? 0.1566 0.1839 0.1975 -0.0022 -0.0198 0.0048  137 ILE   A C   
2858 O  O   A ILE   A 137 ? 0.1415 0.1779 0.2023 -0.0157 0.0054  0.0064  137 ILE   A O   
2859 O  O   B ILE   A 137 ? 0.1662 0.1791 0.2057 -0.0024 -0.0230 0.0011  137 ILE   A O   
2860 C  CB  A ILE   A 137 ? 0.1466 0.1864 0.2129 -0.0046 -0.0163 -0.0100 137 ILE   A CB  
2861 C  CB  B ILE   A 137 ? 0.1504 0.1862 0.2144 -0.0058 -0.0158 -0.0165 137 ILE   A CB  
2862 C  CG1 A ILE   A 137 ? 0.1572 0.1955 0.2451 -0.0012 -0.0347 -0.0105 137 ILE   A CG1 
2863 C  CG1 B ILE   A 137 ? 0.1544 0.1903 0.2314 -0.0075 -0.0125 -0.0222 137 ILE   A CG1 
2864 C  CG2 A ILE   A 137 ? 0.1507 0.1828 0.2246 -0.0068 -0.0198 -0.0181 137 ILE   A CG2 
2865 C  CG2 B ILE   A 137 ? 0.1556 0.1914 0.2225 -0.0056 -0.0112 -0.0252 137 ILE   A CG2 
2866 C  CD1 A ILE   A 137 ? 0.1706 0.2051 0.2699 0.0020  -0.0418 -0.0076 137 ILE   A CD1 
2867 C  CD1 B ILE   A 137 ? 0.1606 0.1927 0.2465 -0.0041 -0.0104 -0.0269 137 ILE   A CD1 
2890 N  N   A HIS   A 138 ? 0.1438 0.1934 0.1937 -0.0125 0.0108  0.0101  138 HIS   A N   
2891 N  N   B HIS   A 138 ? 0.1537 0.1949 0.1897 -0.0004 -0.0163 0.0085  138 HIS   A N   
2892 C  CA  A HIS   A 138 ? 0.1513 0.1932 0.1948 -0.0097 0.0112  0.0066  138 HIS   A CA  
2893 C  CA  B HIS   A 138 ? 0.1550 0.2031 0.1893 0.0003  -0.0072 0.0059  138 HIS   A CA  
2894 C  C   A HIS   A 138 ? 0.1456 0.1871 0.1962 -0.0056 0.0055  0.0173  138 HIS   A C   
2895 C  C   B HIS   A 138 ? 0.1448 0.1913 0.1885 -0.0028 -0.0065 0.0168  138 HIS   A C   
2896 O  O   A HIS   A 138 ? 0.1453 0.1852 0.1996 -0.0097 0.0034  0.0186  138 HIS   A O   
2897 O  O   B HIS   A 138 ? 0.1446 0.1868 0.1852 -0.0073 0.0000  0.0216  138 HIS   A O   
2898 C  CB  A HIS   A 138 ? 0.1540 0.1960 0.1934 -0.0081 0.0035  -0.0113 138 HIS   A CB  
2899 C  CB  B HIS   A 138 ? 0.1728 0.2207 0.1961 0.0007  -0.0142 -0.0004 138 HIS   A CB  
2900 C  CG  A HIS   A 138 ? 0.1669 0.1966 0.2098 -0.0090 -0.0017 -0.0282 138 HIS   A CG  
2901 C  CG  B HIS   A 138 ? 0.1888 0.2304 0.2077 0.0018  -0.0131 -0.0134 138 HIS   A CG  
2902 N  ND1 A HIS   A 138 ? 0.1846 0.2006 0.2370 -0.0135 -0.0003 -0.0375 138 HIS   A ND1 
2903 N  ND1 B HIS   A 138 ? 0.2015 0.2369 0.2266 -0.0019 -0.0081 -0.0176 138 HIS   A ND1 
2904 C  CD2 A HIS   A 138 ? 0.1679 0.1929 0.2115 -0.0020 0.0033  -0.0331 138 HIS   A CD2 
2905 C  CD2 B HIS   A 138 ? 0.1927 0.2354 0.2128 0.0048  -0.0094 -0.0154 138 HIS   A CD2 
2906 C  CE1 A HIS   A 138 ? 0.1877 0.1998 0.2360 -0.0048 -0.0024 -0.0459 138 HIS   A CE1 
2907 C  CE1 B HIS   A 138 ? 0.2048 0.2391 0.2349 0.0030  -0.0055 -0.0199 138 HIS   A CE1 
2908 N  NE2 A HIS   A 138 ? 0.1792 0.1937 0.2147 0.0020  0.0018  -0.0450 138 HIS   A NE2 
2909 N  NE2 B HIS   A 138 ? 0.1972 0.2382 0.2183 0.0076  -0.0013 -0.0184 138 HIS   A NE2 
2924 N  N   . SER   A 139 ? 0.1390 0.1796 0.1861 -0.0017 -0.0028 0.0274  139 SER   A N   
2925 C  CA  . SER   A 139 ? 0.1341 0.1786 0.1853 -0.0059 0.0003  0.0322  139 SER   A CA  
2926 C  C   . SER   A 139 ? 0.1292 0.1660 0.1834 -0.0118 0.0033  0.0213  139 SER   A C   
2927 O  O   . SER   A 139 ? 0.1249 0.1623 0.2006 -0.0115 0.0052  0.0284  139 SER   A O   
2928 C  CB  . SER   A 139 ? 0.1320 0.1795 0.1816 -0.0108 -0.0064 0.0255  139 SER   A CB  
2929 O  OG  . SER   A 139 ? 0.1425 0.1739 0.1955 -0.0188 -0.0076 0.0393  139 SER   A OG  
2936 N  N   . LEU   A 140 ? 0.1314 0.1689 0.1781 -0.0087 -0.0015 0.0318  140 LEU   A N   
2937 C  CA  . LEU   A 140 ? 0.1334 0.1612 0.1838 -0.0119 0.0028  0.0206  140 LEU   A CA  
2938 C  C   . LEU   A 140 ? 0.1238 0.1705 0.1908 -0.0136 0.0046  0.0242  140 LEU   A C   
2939 O  O   . LEU   A 140 ? 0.1302 0.1716 0.2168 -0.0057 0.0028  0.0282  140 LEU   A O   
2940 C  CB  . LEU   A 140 ? 0.1351 0.1706 0.1894 -0.0140 0.0033  0.0211  140 LEU   A CB  
2941 C  CG  . LEU   A 140 ? 0.1350 0.1827 0.1943 -0.0190 0.0059  0.0298  140 LEU   A CG  
2942 C  CD1 . LEU   A 140 ? 0.1389 0.1888 0.2118 -0.0115 0.0046  0.0290  140 LEU   A CD1 
2943 C  CD2 . LEU   A 140 ? 0.1410 0.2015 0.2066 -0.0172 0.0163  0.0373  140 LEU   A CD2 
2955 N  N   . ARG   A 141 ? 0.1341 0.1734 0.1941 -0.0096 0.0041  0.0176  141 ARG   A N   
2956 C  CA  . ARG   A 141 ? 0.1452 0.1860 0.2053 -0.0160 -0.0049 0.0120  141 ARG   A CA  
2957 C  C   . ARG   A 141 ? 0.1486 0.1710 0.2072 -0.0144 -0.0041 0.0110  141 ARG   A C   
2958 O  O   . ARG   A 141 ? 0.1457 0.1688 0.2295 -0.0158 0.0020  0.0061  141 ARG   A O   
2959 C  CB  . ARG   A 141 ? 0.1627 0.2123 0.2234 -0.0248 -0.0020 -0.0045 141 ARG   A CB  
2960 C  CG  . ARG   A 141 ? 0.1906 0.2397 0.2561 -0.0286 0.0073  -0.0156 141 ARG   A CG  
2961 C  CD  . ARG   A 141 ? 0.2115 0.2532 0.2816 -0.0354 0.0024  -0.0272 141 ARG   A CD  
2962 N  NE  . ARG   A 141 ? 0.2042 0.2697 0.3083 -0.0323 -0.0055 -0.0167 141 ARG   A NE  
2963 C  CZ  . ARG   A 141 ? 0.2034 0.2887 0.3158 -0.0404 -0.0006 -0.0012 141 ARG   A CZ  
2964 N  NH1 . ARG   A 141 ? 0.1952 0.2926 0.2983 -0.0493 0.0229  -0.0122 141 ARG   A NH1 
2965 N  NH2 . ARG   A 141 ? 0.2089 0.2994 0.3468 -0.0340 -0.0131 0.0125  141 ARG   A NH2 
2979 N  N   . VAL   A 142 ? 0.1408 0.1649 0.1965 -0.0135 0.0035  0.0072  142 VAL   A N   
2980 C  CA  . VAL   A 142 ? 0.1467 0.1573 0.2054 -0.0093 0.0110  0.0106  142 VAL   A CA  
2981 C  C   . VAL   A 142 ? 0.1272 0.1516 0.2111 -0.0125 0.0117  0.0102  142 VAL   A C   
2982 O  O   . VAL   A 142 ? 0.1320 0.1545 0.2108 -0.0036 0.0074  0.0110  142 VAL   A O   
2983 C  CB  . VAL   A 142 ? 0.1507 0.1655 0.1971 -0.0066 0.0128  0.0063  142 VAL   A CB  
2984 C  CG1 . VAL   A 142 ? 0.1447 0.1623 0.2018 -0.0135 0.0175  0.0040  142 VAL   A CG1 
2985 C  CG2 . VAL   A 142 ? 0.1623 0.1836 0.2046 0.0060  0.0117  0.0098  142 VAL   A CG2 
2995 N  N   . CYS   A 143 ? 0.1330 0.1507 0.1977 -0.0151 0.0116  0.0166  143 CYS   A N   
2996 C  CA  . CYS   A 143 ? 0.1275 0.1531 0.1969 -0.0143 0.0154  0.0209  143 CYS   A CA  
2997 C  C   . CYS   A 143 ? 0.1288 0.1586 0.2094 -0.0123 0.0087  0.0302  143 CYS   A C   
2998 O  O   . CYS   A 143 ? 0.1281 0.1534 0.2171 -0.0068 0.0070  0.0322  143 CYS   A O   
2999 C  CB  . CYS   A 143 ? 0.1369 0.1536 0.1998 -0.0067 0.0144  0.0271  143 CYS   A CB  
3000 S  SG  . CYS   A 143 ? 0.1568 0.1645 0.1825 0.0021  0.0127  0.0177  143 CYS   A SG  
3006 N  N   . VAL   A 144 ? 0.1311 0.1617 0.2306 -0.0136 0.0135  0.0391  144 VAL   A N   
3007 C  CA  . VAL   A 144 ? 0.1426 0.1673 0.2686 -0.0147 0.0189  0.0443  144 VAL   A CA  
3008 C  C   . VAL   A 144 ? 0.1412 0.1560 0.2678 -0.0211 -0.0062 0.0350  144 VAL   A C   
3009 O  O   . VAL   A 144 ? 0.1554 0.1597 0.2695 -0.0132 -0.0112 0.0375  144 VAL   A O   
3010 C  CB  . VAL   A 144 ? 0.1675 0.1954 0.3354 -0.0031 0.0318  0.0550  144 VAL   A CB  
3011 C  CG1 . VAL   A 144 ? 0.1879 0.2169 0.3707 -0.0140 0.0131  0.0613  144 VAL   A CG1 
3012 C  CG2 . VAL   A 144 ? 0.1439 0.2004 0.3383 0.0011  0.0403  0.0623  144 VAL   A CG2 
3022 N  N   . ASP   A 145 ? 0.1468 0.1523 0.2769 -0.0216 -0.0070 0.0226  145 ASP   A N   
3023 C  CA  . ASP   A 145 ? 0.1580 0.1545 0.2800 -0.0246 -0.0104 0.0089  145 ASP   A CA  
3024 C  C   . ASP   A 145 ? 0.1591 0.1465 0.2662 -0.0118 -0.0056 -0.0004 145 ASP   A C   
3025 O  O   . ASP   A 145 ? 0.1679 0.1577 0.3088 -0.0139 -0.0076 -0.0274 145 ASP   A O   
3026 C  CB  . ASP   A 145 ? 0.1755 0.1831 0.3088 -0.0304 -0.0211 0.0079  145 ASP   A CB  
3027 C  CG  . ASP   A 145 ? 0.1905 0.2192 0.3401 -0.0487 -0.0386 0.0198  145 ASP   A CG  
3028 O  OD1 . ASP   A 145 ? 0.1848 0.2370 0.3455 -0.0576 -0.0279 0.0267  145 ASP   A OD1 
3029 O  OD2 . ASP   A 145 ? 0.2067 0.2382 0.3561 -0.0490 -0.0567 0.0250  145 ASP   A OD2 
3034 N  N   . THR   A 146 ? 0.1416 0.1405 0.2223 -0.0130 0.0028  0.0021  146 THR   A N   
3035 C  CA  . THR   A 146 ? 0.1393 0.1398 0.2126 -0.0050 0.0056  0.0003  146 THR   A CA  
3036 C  C   . THR   A 146 ? 0.1331 0.1445 0.2149 -0.0056 0.0093  0.0133  146 THR   A C   
3037 O  O   . THR   A 146 ? 0.1460 0.1577 0.2237 0.0016  -0.0022 0.0160  146 THR   A O   
3038 C  CB  . THR   A 146 ? 0.1366 0.1462 0.2128 -0.0016 0.0043  0.0114  146 THR   A CB  
3039 O  OG1 . THR   A 146 ? 0.1368 0.1586 0.2164 0.0020  -0.0027 0.0012  146 THR   A OG1 
3040 C  CG2 . THR   A 146 ? 0.1385 0.1475 0.2242 -0.0070 0.0103  0.0136  146 THR   A CG2 
3048 N  N   . VAL   A 147 ? 0.1293 0.1446 0.2105 -0.0043 0.0081  0.0217  147 VAL   A N   
3049 C  CA  . VAL   A 147 ? 0.1353 0.1477 0.2163 -0.0116 0.0217  0.0259  147 VAL   A CA  
3050 C  C   . VAL   A 147 ? 0.1348 0.1451 0.2314 -0.0139 0.0125  0.0293  147 VAL   A C   
3051 O  O   . VAL   A 147 ? 0.1373 0.1547 0.2503 -0.0175 0.0054  0.0321  147 VAL   A O   
3052 C  CB  . VAL   A 147 ? 0.1437 0.1498 0.2086 -0.0153 0.0222  0.0294  147 VAL   A CB  
3053 C  CG1 . VAL   A 147 ? 0.1697 0.1498 0.2148 -0.0107 0.0232  0.0312  147 VAL   A CG1 
3054 C  CG2 . VAL   A 147 ? 0.1468 0.1507 0.2060 -0.0145 0.0164  0.0234  147 VAL   A CG2 
3064 N  N   . ARG   A 148 ? 0.1332 0.1442 0.2387 -0.0157 0.0145  0.0392  148 ARG   A N   
3065 C  CA  . ARG   A 148 ? 0.1441 0.1517 0.2286 -0.0148 0.0082  0.0513  148 ARG   A CA  
3066 C  C   . ARG   A 148 ? 0.1554 0.1540 0.2288 -0.0187 0.0039  0.0653  148 ARG   A C   
3067 O  O   . ARG   A 148 ? 0.1851 0.1682 0.2464 -0.0265 0.0123  0.0600  148 ARG   A O   
3068 C  CB  . ARG   A 148 ? 0.1486 0.1570 0.2377 -0.0108 0.0139  0.0419  148 ARG   A CB  
3069 C  CG  . ARG   A 148 ? 0.1665 0.1574 0.2723 -0.0107 0.0229  0.0376  148 ARG   A CG  
3070 C  CD  . ARG   A 148 ? 0.1820 0.1511 0.2843 -0.0031 0.0334  0.0497  148 ARG   A CD  
3071 N  NE  . ARG   A 148 ? 0.1753 0.1554 0.2810 0.0067  0.0439  0.0496  148 ARG   A NE  
3072 C  CZ  . ARG   A 148 ? 0.1729 0.1440 0.2696 0.0033  0.0462  0.0409  148 ARG   A CZ  
3073 N  NH1 . ARG   A 148 ? 0.1812 0.1477 0.2727 -0.0086 0.0383  0.0177  148 ARG   A NH1 
3074 N  NH2 . ARG   A 148 ? 0.1692 0.1605 0.2782 0.0127  0.0517  0.0455  148 ARG   A NH2 
3088 N  N   . THR   A 149 ? 0.1527 0.1631 0.2212 -0.0216 -0.0058 0.0519  149 THR   A N   
3089 C  CA  . THR   A 149 ? 0.1527 0.1688 0.2218 -0.0146 0.0008  0.0545  149 THR   A CA  
3090 C  C   . THR   A 149 ? 0.1488 0.1697 0.2090 -0.0201 0.0070  0.0602  149 THR   A C   
3091 O  O   . THR   A 149 ? 0.1444 0.1779 0.2198 -0.0215 -0.0007 0.0511  149 THR   A O   
3092 C  CB  . THR   A 149 ? 0.1544 0.1801 0.2182 -0.0120 0.0033  0.0494  149 THR   A CB  
3093 O  OG1 . THR   A 149 ? 0.1561 0.1675 0.2234 -0.0248 0.0031  0.0424  149 THR   A OG1 
3094 C  CG2 . THR   A 149 ? 0.1550 0.1934 0.2178 -0.0058 -0.0017 0.0418  149 THR   A CG2 
3102 N  N   . ASN   A 150 ? 0.1539 0.1736 0.2034 -0.0123 0.0042  0.0650  150 ASN   A N   
3103 C  CA  . ASN   A 150 ? 0.1654 0.1869 0.2060 -0.0167 0.0042  0.0551  150 ASN   A CA  
3104 C  C   . ASN   A 150 ? 0.1448 0.1768 0.1982 -0.0190 -0.0023 0.0495  150 ASN   A C   
3105 O  O   . ASN   A 150 ? 0.1554 0.1849 0.2237 -0.0190 -0.0157 0.0384  150 ASN   A O   
3106 C  CB  . ASN   A 150 ? 0.2092 0.2143 0.2370 -0.0244 0.0262  0.0689  150 ASN   A CB  
3107 C  CG  . ASN   A 150 ? 0.2647 0.2466 0.2979 -0.0203 0.0094  0.0788  150 ASN   A CG  
3108 O  OD1 . ASN   A 150 ? 0.2887 0.2536 0.3185 -0.0275 0.0157  0.0902  150 ASN   A OD1 
3109 N  ND2 . ASN   A 150 ? 0.2903 0.2686 0.3338 -0.0149 -0.0090 0.0776  150 ASN   A ND2 
3116 N  N   . VAL   A 151 ? 0.1452 0.1604 0.2007 -0.0194 -0.0066 0.0451  151 VAL   A N   
3117 C  CA  . VAL   A 151 ? 0.1485 0.1557 0.1936 -0.0200 -0.0017 0.0432  151 VAL   A CA  
3118 C  C   . VAL   A 151 ? 0.1408 0.1557 0.1989 -0.0304 0.0049  0.0431  151 VAL   A C   
3119 O  O   . VAL   A 151 ? 0.1508 0.1652 0.2262 -0.0259 0.0033  0.0340  151 VAL   A O   
3120 C  CB  . VAL   A 151 ? 0.1742 0.1743 0.1974 -0.0043 -0.0001 0.0416  151 VAL   A CB  
3121 C  CG1 . VAL   A 151 ? 0.1776 0.1951 0.2153 -0.0101 -0.0014 0.0437  151 VAL   A CG1 
3122 C  CG2 . VAL   A 151 ? 0.1851 0.1717 0.1987 0.0004  0.0169  0.0394  151 VAL   A CG2 
3132 N  N   . TYR   A 152 ? 0.1366 0.1618 0.1945 -0.0292 0.0043  0.0403  152 TYR   A N   
3133 C  CA  . TYR   A 152 ? 0.1423 0.1694 0.1711 -0.0243 0.0023  0.0431  152 TYR   A CA  
3134 C  C   . TYR   A 152 ? 0.1375 0.1590 0.1647 -0.0181 0.0137  0.0403  152 TYR   A C   
3135 O  O   . TYR   A 152 ? 0.1477 0.1576 0.1709 -0.0232 0.0165  0.0426  152 TYR   A O   
3136 C  CB  . TYR   A 152 ? 0.1580 0.1829 0.1699 -0.0184 0.0082  0.0501  152 TYR   A CB  
3137 C  CG  . TYR   A 152 ? 0.1627 0.2065 0.1681 -0.0251 0.0118  0.0537  152 TYR   A CG  
3138 C  CD1 . TYR   A 152 ? 0.1732 0.2273 0.1895 -0.0191 0.0158  0.0619  152 TYR   A CD1 
3139 C  CD2 . TYR   A 152 ? 0.1735 0.2116 0.1640 -0.0407 0.0050  0.0528  152 TYR   A CD2 
3140 C  CE1 . TYR   A 152 ? 0.2070 0.2419 0.1985 -0.0106 0.0063  0.0701  152 TYR   A CE1 
3141 C  CE2 . TYR   A 152 ? 0.2016 0.2296 0.1859 -0.0386 0.0073  0.0603  152 TYR   A CE2 
3142 C  CZ  . TYR   A 152 ? 0.2215 0.2373 0.1828 -0.0256 -0.0021 0.0842  152 TYR   A CZ  
3143 O  OH  . TYR   A 152 ? 0.2521 0.2560 0.2156 -0.0228 0.0045  0.0943  152 TYR   A OH  
3153 N  N   . LEU   A 153 ? 0.1325 0.1543 0.1743 -0.0204 0.0171  0.0436  153 LEU   A N   
3154 C  CA  . LEU   A 153 ? 0.1299 0.1506 0.1760 -0.0134 0.0220  0.0389  153 LEU   A CA  
3155 C  C   . LEU   A 153 ? 0.1364 0.1511 0.1730 -0.0082 0.0272  0.0356  153 LEU   A C   
3156 O  O   . LEU   A 153 ? 0.1371 0.1620 0.2008 -0.0119 0.0350  0.0403  153 LEU   A O   
3157 C  CB  . LEU   A 153 ? 0.1295 0.1514 0.1810 -0.0097 0.0115  0.0309  153 LEU   A CB  
3158 C  CG  . LEU   A 153 ? 0.1364 0.1579 0.1841 -0.0089 0.0140  0.0314  153 LEU   A CG  
3159 C  CD1 . LEU   A 153 ? 0.1473 0.1625 0.1864 -0.0138 0.0033  0.0247  153 LEU   A CD1 
3160 C  CD2 . LEU   A 153 ? 0.1466 0.1663 0.1983 -0.0081 0.0224  0.0195  153 LEU   A CD2 
3172 N  N   A ALA   A 154 ? 0.1374 0.1463 0.1715 -0.0043 0.0245  0.0299  154 ALA   A N   
3173 N  N   B ALA   A 154 ? 0.1393 0.1521 0.1677 -0.0043 0.0189  0.0372  154 ALA   A N   
3174 C  CA  A ALA   A 154 ? 0.1454 0.1464 0.1667 -0.0072 0.0317  0.0223  154 ALA   A CA  
3175 C  CA  B ALA   A 154 ? 0.1470 0.1565 0.1589 -0.0072 0.0177  0.0365  154 ALA   A CA  
3176 C  C   A ALA   A 154 ? 0.1477 0.1408 0.1749 -0.0008 0.0288  0.0148  154 ALA   A C   
3177 C  C   B ALA   A 154 ? 0.1437 0.1550 0.1500 -0.0084 0.0124  0.0337  154 ALA   A C   
3178 O  O   A ALA   A 154 ? 0.1509 0.1503 0.1846 -0.0060 0.0291  0.0141  154 ALA   A O   
3179 O  O   B ALA   A 154 ? 0.1452 0.1614 0.1434 -0.0132 0.0160  0.0344  154 ALA   A O   
3180 C  CB  A ALA   A 154 ? 0.1546 0.1516 0.1797 -0.0033 0.0262  0.0128  154 ALA   A CB  
3181 C  CB  B ALA   A 154 ? 0.1565 0.1601 0.1686 -0.0034 0.0085  0.0286  154 ALA   A CB  
3192 N  N   A VAL   A 155 ? 0.1484 0.1416 0.1694 0.0081  0.0315  0.0225  155 VAL   A N   
3193 N  N   B VAL   A 155 ? 0.1390 0.1513 0.1540 -0.0075 0.0135  0.0463  155 VAL   A N   
3194 C  CA  A VAL   A 155 ? 0.1628 0.1502 0.1863 0.0063  0.0265  0.0296  155 VAL   A CA  
3195 C  CA  B VAL   A 155 ? 0.1513 0.1551 0.1735 -0.0062 0.0089  0.0506  155 VAL   A CA  
3196 C  CA  T VAL   A 155 ? 0.1659 0.1734 0.1663 -0.0067 0.0014  0.0153  155 VAL   A CA  
3197 C  C   A VAL   A 155 ? 0.1673 0.1568 0.2045 0.0165  0.0285  0.0441  155 VAL   A C   
3198 C  C   B VAL   A 155 ? 0.1486 0.1585 0.1896 -0.0018 0.0192  0.0597  155 VAL   A C   
3199 C  C   T VAL   A 155 ? 0.1666 0.1731 0.1661 -0.0040 0.0010  0.0145  155 VAL   A C   
3200 O  O   A VAL   A 155 ? 0.1669 0.1590 0.2137 0.0296  0.0394  0.0388  155 VAL   A O   
3201 O  O   B VAL   A 155 ? 0.1516 0.1687 0.1972 0.0017  0.0365  0.0525  155 VAL   A O   
3202 O  O   T VAL   A 155 ? 0.1664 0.1737 0.1622 -0.0035 -0.0006 0.0103  155 VAL   A O   
3203 C  CB  A VAL   A 155 ? 0.1728 0.1557 0.1915 0.0063  0.0068  0.0250  155 VAL   A CB  
3204 C  CB  B VAL   A 155 ? 0.1649 0.1629 0.1844 0.0010  -0.0105 0.0402  155 VAL   A CB  
3205 C  CB  T VAL   A 155 ? 0.1658 0.1745 0.1692 -0.0066 -0.0015 0.0165  155 VAL   A CB  
3206 C  CG1 A VAL   A 155 ? 0.1817 0.1621 0.1968 0.0119  0.0009  0.0256  155 VAL   A CG1 
3207 C  CG1 B VAL   A 155 ? 0.1711 0.1682 0.1945 0.0026  -0.0176 0.0387  155 VAL   A CG1 
3208 C  CG1 T VAL   A 155 ? 0.1676 0.1766 0.1724 -0.0052 -0.0022 0.0178  155 VAL   A CG1 
3209 C  CG2 A VAL   A 155 ? 0.1856 0.1623 0.2035 0.0078  -0.0063 0.0227  155 VAL   A CG2 
3210 C  CG2 B VAL   A 155 ? 0.1779 0.1669 0.1995 0.0072  -0.0227 0.0334  155 VAL   A CG2 
3211 C  CG2 T VAL   A 155 ? 0.1668 0.1752 0.1720 -0.0064 -0.0034 0.0170  155 VAL   A CG2 
3237 N  N   A PHE   A 156 ? 0.1793 0.1631 0.2306 0.0154  0.0310  0.0609  156 PHE   A N   
3238 N  N   B PHE   A 156 ? 0.1520 0.1553 0.2154 -0.0021 0.0185  0.0576  156 PHE   A N   
3239 N  N   T PHE   A 156 ? 0.1699 0.1727 0.1725 -0.0015 0.0042  0.0170  156 PHE   A N   
3240 C  CA  A PHE   A 156 ? 0.2022 0.1744 0.2644 0.0153  0.0261  0.0691  156 PHE   A CA  
3241 C  CA  B PHE   A 156 ? 0.1688 0.1533 0.2416 -0.0009 0.0125  0.0540  156 PHE   A CA  
3242 C  CA  T PHE   A 156 ? 0.1759 0.1735 0.1797 0.0017  0.0040  0.0176  156 PHE   A CA  
3243 C  C   A PHE   A 156 ? 0.2048 0.1803 0.2628 0.0220  0.0390  0.0657  156 PHE   A C   
3244 C  C   B PHE   A 156 ? 0.1654 0.1633 0.2294 0.0080  0.0194  0.0385  156 PHE   A C   
3245 C  C   T PHE   A 156 ? 0.1806 0.1807 0.1842 0.0046  0.0084  0.0157  156 PHE   A C   
3246 O  O   A PHE   A 156 ? 0.2093 0.1837 0.2711 0.0215  0.0513  0.0541  156 PHE   A O   
3247 O  O   B PHE   A 156 ? 0.1731 0.1689 0.2368 0.0120  0.0246  0.0174  156 PHE   A O   
3248 O  O   T PHE   A 156 ? 0.1822 0.1818 0.1836 0.0051  0.0120  0.0110  156 PHE   A O   
3249 C  CB  A PHE   A 156 ? 0.2278 0.1930 0.3015 0.0181  0.0114  0.0695  156 PHE   A CB  
3250 C  CB  B PHE   A 156 ? 0.1748 0.1564 0.2696 -0.0011 0.0049  0.0642  156 PHE   A CB  
3251 C  CB  T PHE   A 156 ? 0.1765 0.1692 0.1819 0.0055  0.0006  0.0173  156 PHE   A CB  
3252 C  CG  A PHE   A 156 ? 0.2607 0.2174 0.3289 0.0306  -0.0027 0.0606  156 PHE   A CG  
3253 C  CG  B PHE   A 156 ? 0.1852 0.1593 0.2687 0.0014  -0.0009 0.0744  156 PHE   A CG  
3254 C  CG  T PHE   A 156 ? 0.1810 0.1688 0.1817 0.0110  -0.0031 0.0165  156 PHE   A CG  
3255 C  CD1 A PHE   A 156 ? 0.2747 0.2320 0.3361 0.0380  -0.0061 0.0560  156 PHE   A CD1 
3256 C  CD1 B PHE   A 156 ? 0.1863 0.1629 0.2736 -0.0056 -0.0110 0.0590  156 PHE   A CD1 
3257 C  CD1 T PHE   A 156 ? 0.1833 0.1718 0.1837 0.0146  -0.0082 0.0131  156 PHE   A CD1 
3258 C  CD2 A PHE   A 156 ? 0.2774 0.2325 0.3411 0.0403  -0.0106 0.0548  156 PHE   A CD2 
3259 C  CD2 B PHE   A 156 ? 0.2026 0.1679 0.2711 0.0078  -0.0093 0.0815  156 PHE   A CD2 
3260 C  CD2 T PHE   A 156 ? 0.1868 0.1697 0.1849 0.0147  -0.0055 0.0149  156 PHE   A CD2 
3261 C  CE1 A PHE   A 156 ? 0.2848 0.2406 0.3478 0.0417  -0.0047 0.0477  156 PHE   A CE1 
3262 C  CE1 B PHE   A 156 ? 0.1907 0.1677 0.2742 -0.0136 -0.0141 0.0581  156 PHE   A CE1 
3263 C  CE1 T PHE   A 156 ? 0.1869 0.1728 0.1871 0.0138  -0.0098 0.0106  156 PHE   A CE1 
3264 C  CE2 A PHE   A 156 ? 0.2883 0.2423 0.3474 0.0437  -0.0104 0.0449  156 PHE   A CE2 
3265 C  CE2 B PHE   A 156 ? 0.2071 0.1704 0.2716 0.0032  -0.0127 0.0767  156 PHE   A CE2 
3266 C  CE2 T PHE   A 156 ? 0.1901 0.1709 0.1863 0.0155  -0.0088 0.0125  156 PHE   A CE2 
3267 C  CZ  A PHE   A 156 ? 0.2902 0.2457 0.3500 0.0427  -0.0056 0.0422  156 PHE   A CZ  
3268 C  CZ  B PHE   A 156 ? 0.1976 0.1653 0.2770 -0.0147 -0.0128 0.0665  156 PHE   A CZ  
3269 C  CZ  T PHE   A 156 ? 0.1890 0.1716 0.1885 0.0135  -0.0101 0.0098  156 PHE   A CZ  
3297 N  N   A ASP   A 157 ? 0.2049 0.1861 0.2642 0.0243  0.0392  0.0764  157 ASP   A N   
3298 N  N   B ASP   A 157 ? 0.1491 0.1613 0.2131 0.0132  0.0200  0.0403  157 ASP   A N   
3299 N  N   T ASP   A 157 ? 0.1838 0.1880 0.1906 0.0063  0.0089  0.0204  157 ASP   A N   
3300 C  CA  A ASP   A 157 ? 0.2149 0.1996 0.2748 0.0213  0.0403  0.0789  157 ASP   A CA  
3301 C  CA  B ASP   A 157 ? 0.1505 0.1655 0.2093 0.0097  0.0101  0.0486  157 ASP   A CA  
3302 C  CA  T ASP   A 157 ? 0.1892 0.1955 0.1980 0.0084  0.0088  0.0230  157 ASP   A CA  
3303 C  C   A ASP   A 157 ? 0.2121 0.2036 0.2750 0.0225  0.0474  0.0858  157 ASP   A C   
3304 C  C   B ASP   A 157 ? 0.1562 0.1741 0.2051 0.0137  0.0149  0.0540  157 ASP   A C   
3305 C  C   T ASP   A 157 ? 0.1958 0.2018 0.2057 0.0087  0.0101  0.0235  157 ASP   A C   
3306 O  O   A ASP   A 157 ? 0.2049 0.1993 0.2748 0.0240  0.0417  0.0858  157 ASP   A O   
3307 O  O   B ASP   A 157 ? 0.1562 0.1710 0.2099 0.0117  0.0087  0.0448  157 ASP   A O   
3308 O  O   T ASP   A 157 ? 0.1945 0.2005 0.2051 0.0093  0.0088  0.0235  157 ASP   A O   
3309 C  CB  A ASP   A 157 ? 0.2314 0.2095 0.2997 0.0242  0.0309  0.0725  157 ASP   A CB  
3310 C  CB  B ASP   A 157 ? 0.1486 0.1600 0.2082 0.0058  0.0020  0.0570  157 ASP   A CB  
3311 C  CB  T ASP   A 157 ? 0.1889 0.1969 0.2016 0.0113  0.0072  0.0254  157 ASP   A CB  
3312 C  CG  A ASP   A 157 ? 0.2487 0.2215 0.3340 0.0257  0.0211  0.0657  157 ASP   A CG  
3313 C  CG  B ASP   A 157 ? 0.1457 0.1595 0.2186 0.0073  -0.0044 0.0665  157 ASP   A CG  
3314 C  CG  T ASP   A 157 ? 0.1886 0.1987 0.2074 0.0138  0.0056  0.0273  157 ASP   A CG  
3315 O  OD1 A ASP   A 157 ? 0.2619 0.2352 0.3618 0.0265  0.0179  0.0543  157 ASP   A OD1 
3316 O  OD1 B ASP   A 157 ? 0.1533 0.1546 0.2358 0.0027  -0.0107 0.0463  157 ASP   A OD1 
3317 O  OD1 T ASP   A 157 ? 0.1870 0.1976 0.2134 0.0149  -0.0006 0.0258  157 ASP   A OD1 
3318 O  OD2 A ASP   A 157 ? 0.2497 0.2184 0.3370 0.0257  0.0213  0.0683  157 ASP   A OD2 
3319 O  OD2 B ASP   A 157 ? 0.1502 0.1701 0.2246 0.0151  -0.0059 0.0835  157 ASP   A OD2 
3320 O  OD2 T ASP   A 157 ? 0.1889 0.2013 0.2060 0.0154  0.0126  0.0292  157 ASP   A OD2 
3333 N  N   A LYS   A 158 ? 0.2204 0.2203 0.2879 0.0190  0.0564  0.0810  158 LYS   A N   
3334 N  N   B LYS   A 158 ? 0.1616 0.1878 0.2024 0.0137  0.0280  0.0612  158 LYS   A N   
3335 N  N   T LYS   A 158 ? 0.2044 0.2107 0.2159 0.0078  0.0125  0.0229  158 LYS   A N   
3336 C  CA  A LYS   A 158 ? 0.2226 0.2402 0.3126 0.0193  0.0639  0.0743  158 LYS   A CA  
3337 C  CA  B LYS   A 158 ? 0.1666 0.2068 0.2190 0.0180  0.0342  0.0648  158 LYS   A CA  
3338 C  CA  T LYS   A 158 ? 0.2116 0.2204 0.2306 0.0075  0.0135  0.0220  158 LYS   A CA  
3339 C  C   A LYS   A 158 ? 0.2055 0.2445 0.3007 0.0159  0.0551  0.0806  158 LYS   A C   
3340 C  C   B LYS   A 158 ? 0.1638 0.1963 0.2206 0.0168  0.0208  0.0610  158 LYS   A C   
3341 C  C   T LYS   A 158 ? 0.2129 0.2241 0.2289 0.0083  0.0109  0.0229  158 LYS   A C   
3342 O  O   A LYS   A 158 ? 0.2007 0.2463 0.3011 0.0144  0.0590  0.0839  158 LYS   A O   
3343 O  O   B LYS   A 158 ? 0.1670 0.1935 0.2374 0.0065  0.0260  0.0451  158 LYS   A O   
3344 O  O   T LYS   A 158 ? 0.2126 0.2248 0.2284 0.0083  0.0111  0.0224  158 LYS   A O   
3345 C  CB  A LYS   A 158 ? 0.2418 0.2515 0.3418 0.0213  0.0850  0.0657  158 LYS   A CB  
3346 C  CB  B LYS   A 158 ? 0.1845 0.2331 0.2481 0.0206  0.0501  0.0572  158 LYS   A CB  
3347 C  CB  T LYS   A 158 ? 0.2180 0.2256 0.2469 0.0064  0.0192  0.0207  158 LYS   A CB  
3348 C  CG  A LYS   A 158 ? 0.2635 0.2661 0.3647 0.0272  0.0980  0.0582  158 LYS   A CG  
3349 C  CG  B LYS   A 158 ? 0.2031 0.2535 0.2774 0.0211  0.0570  0.0497  158 LYS   A CG  
3350 C  CG  T LYS   A 158 ? 0.2248 0.2307 0.2612 0.0068  0.0231  0.0203  158 LYS   A CG  
3351 C  CD  A LYS   A 158 ? 0.2824 0.2805 0.3866 0.0345  0.1111  0.0518  158 LYS   A CD  
3352 C  CD  B LYS   A 158 ? 0.2210 0.2726 0.3044 0.0197  0.0622  0.0383  158 LYS   A CD  
3353 C  CD  T LYS   A 158 ? 0.2315 0.2359 0.2772 0.0078  0.0264  0.0193  158 LYS   A CD  
3354 C  CE  A LYS   A 158 ? 0.2950 0.2887 0.3942 0.0360  0.1199  0.0542  158 LYS   A CE  
3355 C  CE  B LYS   A 158 ? 0.2333 0.2852 0.3191 0.0183  0.0616  0.0321  158 LYS   A CE  
3356 C  CE  T LYS   A 158 ? 0.2359 0.2393 0.2882 0.0084  0.0274  0.0187  158 LYS   A CE  
3357 N  NZ  A LYS   A 158 ? 0.3007 0.2915 0.4003 0.0329  0.1245  0.0586  158 LYS   A NZ  
3358 N  NZ  B LYS   A 158 ? 0.2385 0.2893 0.3237 0.0185  0.0695  0.0299  158 LYS   A NZ  
3359 N  NZ  T LYS   A 158 ? 0.2386 0.2405 0.2943 0.0082  0.0279  0.0188  158 LYS   A NZ  
3399 N  N   A ASN   A 159 ? 0.1955 0.2444 0.3004 0.0076  0.0363  0.0766  159 ASN   A N   
3400 N  N   B ASN   A 159 ? 0.1662 0.1998 0.2365 0.0184  0.0036  0.0600  159 ASN   A N   
3401 N  N   T ASN   A 159 ? 0.2147 0.2258 0.2313 0.0071  0.0075  0.0223  159 ASN   A N   
3402 C  CA  A ASN   A 159 ? 0.1901 0.2449 0.2910 -0.0026 0.0211  0.0760  159 ASN   A CA  
3403 C  CA  B ASN   A 159 ? 0.1780 0.2075 0.2575 0.0219  -0.0003 0.0574  159 ASN   A CA  
3404 C  CA  T ASN   A 159 ? 0.2168 0.2270 0.2318 0.0047  0.0051  0.0209  159 ASN   A CA  
3405 C  C   A ASN   A 159 ? 0.1780 0.2426 0.2710 -0.0086 0.0137  0.0640  159 ASN   A C   
3406 C  C   B ASN   A 159 ? 0.1716 0.2027 0.2442 0.0176  0.0081  0.0492  159 ASN   A C   
3407 C  C   T ASN   A 159 ? 0.2163 0.2279 0.2267 0.0022  0.0058  0.0185  159 ASN   A C   
3408 O  O   A ASN   A 159 ? 0.1731 0.2442 0.2638 -0.0062 0.0023  0.0508  159 ASN   A O   
3409 O  O   B ASN   A 159 ? 0.1560 0.1971 0.2374 0.0168  -0.0059 0.0305  159 ASN   A O   
3410 O  O   T ASN   A 159 ? 0.2172 0.2298 0.2244 0.0026  0.0065  0.0162  159 ASN   A O   
3411 C  CB  A ASN   A 159 ? 0.1996 0.2522 0.3178 -0.0043 0.0142  0.0863  159 ASN   A CB  
3412 C  CB  B ASN   A 159 ? 0.2004 0.2241 0.3001 0.0320  -0.0149 0.0622  159 ASN   A CB  
3413 C  CB  T ASN   A 159 ? 0.2193 0.2274 0.2412 0.0045  0.0014  0.0208  159 ASN   A CB  
3414 C  CG  A ASN   A 159 ? 0.2108 0.2617 0.3419 -0.0036 0.0143  0.0947  159 ASN   A CG  
3415 C  CG  B ASN   A 159 ? 0.2178 0.2404 0.3378 0.0414  -0.0164 0.0560  159 ASN   A CG  
3416 C  CG  T ASN   A 159 ? 0.2220 0.2281 0.2506 0.0045  -0.0006 0.0193  159 ASN   A CG  
3417 O  OD1 A ASN   A 159 ? 0.2211 0.2709 0.3646 -0.0010 0.0206  0.0978  159 ASN   A OD1 
3418 O  OD1 B ASN   A 159 ? 0.2227 0.2500 0.3583 0.0456  0.0002  0.0486  159 ASN   A OD1 
3419 O  OD1 T ASN   A 159 ? 0.2242 0.2301 0.2586 0.0055  0.0023  0.0195  159 ASN   A OD1 
3420 N  ND2 A ASN   A 159 ? 0.2119 0.2643 0.3462 -0.0021 0.0048  0.0959  159 ASN   A ND2 
3421 N  ND2 B ASN   A 159 ? 0.2226 0.2485 0.3507 0.0495  -0.0310 0.0553  159 ASN   A ND2 
3422 N  ND2 T ASN   A 159 ? 0.2224 0.2283 0.2524 0.0047  -0.0055 0.0182  159 ASN   A ND2 
3441 N  N   A LEU   A 160 ? 0.1691 0.2363 0.2565 -0.0097 0.0111  0.0649  160 LEU   A N   
3442 N  N   B LEU   A 160 ? 0.1736 0.1986 0.2331 0.0217  0.0158  0.0542  160 LEU   A N   
3443 N  N   T LEU   A 160 ? 0.2144 0.2260 0.2243 0.0005  0.0052  0.0187  160 LEU   A N   
3444 C  CA  A LEU   A 160 ? 0.1728 0.2359 0.2373 -0.0120 0.0183  0.0676  160 LEU   A CA  
3445 C  CA  B LEU   A 160 ? 0.1847 0.2003 0.2239 0.0179  0.0213  0.0599  160 LEU   A CA  
3446 C  CA  T LEU   A 160 ? 0.2148 0.2252 0.2218 -0.0020 0.0063  0.0194  160 LEU   A CA  
3447 C  C   A LEU   A 160 ? 0.1632 0.2296 0.2257 -0.0140 0.0204  0.0673  160 LEU   A C   
3448 C  C   B LEU   A 160 ? 0.1750 0.1895 0.2126 0.0124  0.0251  0.0607  160 LEU   A C   
3449 O  O   A LEU   A 160 ? 0.1623 0.2348 0.2300 -0.0127 0.0163  0.0704  160 LEU   A O   
3450 O  O   B LEU   A 160 ? 0.1744 0.1962 0.2222 0.0082  0.0177  0.0594  160 LEU   A O   
3451 C  CB  A LEU   A 160 ? 0.1772 0.2386 0.2344 -0.0112 0.0221  0.0732  160 LEU   A CB  
3452 C  CB  B LEU   A 160 ? 0.1987 0.2092 0.2298 0.0183  0.0252  0.0621  160 LEU   A CB  
3453 C  CB  T LEU   A 160 ? 0.2138 0.2240 0.2207 -0.0037 0.0080  0.0203  160 LEU   A CB  
3454 C  CG  A LEU   A 160 ? 0.1843 0.2435 0.2519 -0.0120 0.0189  0.0594  160 LEU   A CG  
3455 C  CG  B LEU   A 160 ? 0.2114 0.2174 0.2473 0.0158  0.0229  0.0487  160 LEU   A CG  
3456 C  CG  T LEU   A 160 ? 0.2136 0.2233 0.2221 -0.0057 0.0093  0.0191  160 LEU   A CG  
3457 C  CD1 A LEU   A 160 ? 0.1938 0.2499 0.2648 -0.0123 0.0189  0.0482  160 LEU   A CD1 
3458 C  CD1 B LEU   A 160 ? 0.2113 0.2226 0.2540 0.0112  0.0287  0.0375  160 LEU   A CD1 
3459 C  CD1 T LEU   A 160 ? 0.2145 0.2238 0.2241 -0.0061 0.0090  0.0171  160 LEU   A CD1 
3460 C  CD2 A LEU   A 160 ? 0.1821 0.2411 0.2563 -0.0116 0.0161  0.0576  160 LEU   A CD2 
3461 C  CD2 B LEU   A 160 ? 0.2189 0.2171 0.2572 0.0171  0.0199  0.0478  160 LEU   A CD2 
3462 C  CD2 T LEU   A 160 ? 0.2128 0.2223 0.2225 -0.0064 0.0111  0.0194  160 LEU   A CD2 
3495 N  N   A TYR   A 161 ? 0.1614 0.2167 0.2230 -0.0153 0.0201  0.0651  161 TYR   A N   
3496 N  N   B TYR   A 161 ? 0.1694 0.1744 0.2039 0.0095  0.0269  0.0540  161 TYR   A N   
3497 C  CA  A TYR   A 161 ? 0.1578 0.2141 0.2255 -0.0083 0.0207  0.0606  161 TYR   A CA  
3498 C  CA  B TYR   A 161 ? 0.1703 0.1734 0.1989 0.0073  0.0273  0.0425  161 TYR   A CA  
3499 C  C   A TYR   A 161 ? 0.1550 0.2196 0.2312 -0.0034 0.0162  0.0643  161 TYR   A C   
3500 C  C   B TYR   A 161 ? 0.1745 0.1739 0.1999 0.0027  0.0257  0.0351  161 TYR   A C   
3501 O  O   A TYR   A 161 ? 0.1545 0.2208 0.2215 -0.0031 0.0157  0.0626  161 TYR   A O   
3502 O  O   B TYR   A 161 ? 0.1706 0.1736 0.1940 0.0048  0.0243  0.0335  161 TYR   A O   
3503 C  CB  A TYR   A 161 ? 0.1598 0.2115 0.2240 -0.0086 0.0249  0.0506  161 TYR   A CB  
3504 C  CB  B TYR   A 161 ? 0.1667 0.1783 0.1927 0.0035  0.0287  0.0399  161 TYR   A CB  
3505 C  CG  A TYR   A 161 ? 0.1543 0.2025 0.2195 -0.0031 0.0108  0.0376  161 TYR   A CG  
3506 C  CG  B TYR   A 161 ? 0.1553 0.1761 0.1912 0.0050  0.0278  0.0377  161 TYR   A CG  
3507 C  CD1 A TYR   A 161 ? 0.1530 0.2003 0.2237 -0.0005 0.0104  0.0361  161 TYR   A CD1 
3508 C  CD1 B TYR   A 161 ? 0.1545 0.1802 0.2024 0.0075  0.0269  0.0382  161 TYR   A CD1 
3509 C  CD2 A TYR   A 161 ? 0.1501 0.1962 0.2220 0.0027  -0.0001 0.0304  161 TYR   A CD2 
3510 C  CD2 B TYR   A 161 ? 0.1473 0.1707 0.1901 0.0038  0.0275  0.0398  161 TYR   A CD2 
3511 C  CE1 A TYR   A 161 ? 0.1495 0.1911 0.2212 0.0056  -0.0023 0.0376  161 TYR   A CE1 
3512 C  CE1 B TYR   A 161 ? 0.1493 0.1801 0.2033 0.0138  0.0211  0.0414  161 TYR   A CE1 
3513 C  CE2 A TYR   A 161 ? 0.1514 0.1843 0.2141 0.0021  -0.0065 0.0381  161 TYR   A CE2 
3514 C  CE2 B TYR   A 161 ? 0.1446 0.1711 0.1900 0.0018  0.0287  0.0486  161 TYR   A CE2 
3515 C  CZ  A TYR   A 161 ? 0.1588 0.1826 0.2126 -0.0002 -0.0102 0.0437  161 TYR   A CZ  
3516 C  CZ  B TYR   A 161 ? 0.1547 0.1801 0.1943 0.0051  0.0232  0.0490  161 TYR   A CZ  
3517 O  OH  A TYR   A 161 ? 0.1779 0.1766 0.2197 0.0000  -0.0180 0.0519  161 TYR   A OH  
3518 O  OH  B TYR   A 161 ? 0.1696 0.1846 0.2087 0.0049  0.0168  0.0487  161 TYR   A OH  
3537 N  N   A ASP   A 162 ? 0.1523 0.2302 0.2491 0.0017  0.0202  0.0702  162 ASP   A N   
3538 N  N   B ASP   A 162 ? 0.1746 0.1736 0.2026 -0.0038 0.0321  0.0305  162 ASP   A N   
3539 C  CA  A ASP   A 162 ? 0.1524 0.2410 0.2639 0.0052  0.0259  0.0735  162 ASP   A CA  
3540 C  CA  B ASP   A 162 ? 0.1791 0.1763 0.2140 0.0038  0.0311  0.0302  162 ASP   A CA  
3541 C  C   A ASP   A 162 ? 0.1486 0.2513 0.2649 -0.0025 0.0191  0.0682  162 ASP   A C   
3542 C  C   B ASP   A 162 ? 0.1855 0.1717 0.2159 0.0019  0.0155  0.0291  162 ASP   A C   
3543 O  O   A ASP   A 162 ? 0.1462 0.2453 0.2770 -0.0088 0.0155  0.0649  162 ASP   A O   
3544 O  O   B ASP   A 162 ? 0.1865 0.1733 0.2218 0.0032  0.0101  0.0247  162 ASP   A O   
3545 C  CB  A ASP   A 162 ? 0.1630 0.2459 0.2881 0.0108  0.0329  0.0707  162 ASP   A CB  
3546 C  CB  B ASP   A 162 ? 0.1771 0.1824 0.2308 0.0117  0.0378  0.0338  162 ASP   A CB  
3547 C  CG  A ASP   A 162 ? 0.1801 0.2609 0.3167 0.0147  0.0336  0.0610  162 ASP   A CG  
3548 C  CG  B ASP   A 162 ? 0.1766 0.1808 0.2340 0.0185  0.0467  0.0467  162 ASP   A CG  
3549 O  OD1 A ASP   A 162 ? 0.1941 0.2692 0.3285 0.0136  0.0323  0.0617  162 ASP   A OD1 
3550 O  OD1 B ASP   A 162 ? 0.1787 0.1814 0.2401 0.0238  0.0474  0.0493  162 ASP   A OD1 
3551 O  OD2 A ASP   A 162 ? 0.1891 0.2675 0.3303 0.0207  0.0419  0.0503  162 ASP   A OD2 
3552 O  OD2 B ASP   A 162 ? 0.1826 0.1797 0.2347 0.0269  0.0402  0.0562  162 ASP   A OD2 
3561 N  N   A LYS   A 163 ? 0.1501 0.2693 0.2658 0.0048  0.0036  0.0570  163 LYS   A N   
3562 N  N   B LYS   A 163 ? 0.2005 0.1811 0.2192 0.0011  0.0119  0.0283  163 LYS   A N   
3563 C  CA  A LYS   A 163 ? 0.1669 0.2890 0.2741 0.0056  -0.0041 0.0426  163 LYS   A CA  
3564 C  CA  B LYS   A 163 ? 0.2172 0.1933 0.2267 0.0030  0.0059  0.0311  163 LYS   A CA  
3565 C  C   A LYS   A 163 ? 0.1537 0.2743 0.2539 -0.0061 0.0143  0.0346  163 LYS   A C   
3566 C  C   B LYS   A 163 ? 0.2085 0.1722 0.2092 0.0002  0.0095  0.0246  163 LYS   A C   
3567 O  O   A LYS   A 163 ? 0.1559 0.2793 0.2634 -0.0116 0.0159  0.0257  163 LYS   A O   
3568 O  O   B LYS   A 163 ? 0.2045 0.1650 0.2012 -0.0043 0.0121  0.0019  163 LYS   A O   
3569 C  CB  A LYS   A 163 ? 0.2071 0.3189 0.3189 0.0230  -0.0163 0.0381  163 LYS   A CB  
3570 C  CB  B LYS   A 163 ? 0.2500 0.2289 0.2657 0.0098  0.0008  0.0374  163 LYS   A CB  
3571 C  CG  A LYS   A 163 ? 0.2433 0.3426 0.3739 0.0275  -0.0156 0.0329  163 LYS   A CG  
3572 C  CG  B LYS   A 163 ? 0.2810 0.2660 0.3177 0.0161  -0.0004 0.0363  163 LYS   A CG  
3573 C  CD  A LYS   A 163 ? 0.2703 0.3604 0.4296 0.0312  -0.0128 0.0290  163 LYS   A CD  
3574 C  CD  B LYS   A 163 ? 0.3058 0.2974 0.3760 0.0217  -0.0047 0.0308  163 LYS   A CD  
3575 C  CE  A LYS   A 163 ? 0.2870 0.3701 0.4717 0.0350  -0.0065 0.0290  163 LYS   A CE  
3576 C  CE  B LYS   A 163 ? 0.3228 0.3194 0.4186 0.0248  -0.0061 0.0273  163 LYS   A CE  
3577 N  NZ  A LYS   A 163 ? 0.2925 0.3749 0.4951 0.0356  -0.0043 0.0327  163 LYS   A NZ  
3578 N  NZ  B LYS   A 163 ? 0.3302 0.3296 0.4431 0.0283  -0.0068 0.0256  163 LYS   A NZ  
3605 N  N   A LEU   A 164 ? 0.1332 0.2501 0.2242 -0.0090 0.0202  0.0362  164 LEU   A N   
3606 N  N   B LEU   A 164 ? 0.1972 0.1660 0.2105 0.0011  0.0096  0.0373  164 LEU   A N   
3607 C  CA  A LEU   A 164 ? 0.1372 0.2373 0.2140 -0.0174 0.0335  0.0375  164 LEU   A CA  
3608 C  CA  B LEU   A 164 ? 0.1975 0.1717 0.2079 0.0019  0.0149  0.0386  164 LEU   A CA  
3609 C  C   A LEU   A 164 ? 0.1468 0.2315 0.2168 -0.0185 0.0327  0.0283  164 LEU   A C   
3610 C  C   B LEU   A 164 ? 0.1991 0.1644 0.2091 0.0040  0.0110  0.0341  164 LEU   A C   
3611 O  O   A LEU   A 164 ? 0.1459 0.2292 0.2171 -0.0225 0.0497  0.0206  164 LEU   A O   
3612 O  O   B LEU   A 164 ? 0.2002 0.1580 0.2229 0.0024  0.0178  0.0288  164 LEU   A O   
3613 C  CB  A LEU   A 164 ? 0.1344 0.2314 0.2100 -0.0233 0.0340  0.0475  164 LEU   A CB  
3614 C  CB  B LEU   A 164 ? 0.1938 0.1858 0.2120 0.0019  0.0187  0.0332  164 LEU   A CB  
3615 C  CG  A LEU   A 164 ? 0.1406 0.2324 0.2171 -0.0203 0.0236  0.0477  164 LEU   A CG  
3616 C  CG  B LEU   A 164 ? 0.1954 0.2017 0.2154 -0.0004 0.0231  0.0368  164 LEU   A CG  
3617 C  CD1 A LEU   A 164 ? 0.1316 0.2296 0.2213 -0.0231 0.0137  0.0567  164 LEU   A CD1 
3618 C  CD1 B LEU   A 164 ? 0.1892 0.2047 0.2182 0.0011  0.0245  0.0451  164 LEU   A CD1 
3619 C  CD2 A LEU   A 164 ? 0.1533 0.2370 0.2207 -0.0204 0.0320  0.0416  164 LEU   A CD2 
3620 C  CD2 B LEU   A 164 ? 0.1985 0.2099 0.2174 -0.0085 0.0280  0.0334  164 LEU   A CD2 
3643 N  N   A VAL   A 165 ? 0.1427 0.2300 0.2095 -0.0233 0.0317  0.0335  165 VAL   A N   
3644 N  N   B VAL   A 165 ? 0.1941 0.1693 0.2018 -0.0013 0.0092  0.0425  165 VAL   A N   
3645 C  CA  A VAL   A 165 ? 0.1516 0.2352 0.2022 -0.0173 0.0393  0.0299  165 VAL   A CA  
3646 C  CA  B VAL   A 165 ? 0.1984 0.1756 0.1989 -0.0038 0.0056  0.0452  165 VAL   A CA  
3647 C  C   A VAL   A 165 ? 0.1462 0.2370 0.1993 -0.0119 0.0385  0.0321  165 VAL   A C   
3648 C  C   B VAL   A 165 ? 0.1837 0.1716 0.1989 -0.0060 0.0087  0.0412  165 VAL   A C   
3649 O  O   A VAL   A 165 ? 0.1466 0.2357 0.2067 -0.0157 0.0375  0.0259  165 VAL   A O   
3650 O  O   B VAL   A 165 ? 0.1827 0.1696 0.2075 -0.0112 0.0124  0.0432  165 VAL   A O   
3651 C  CB  A VAL   A 165 ? 0.1695 0.2363 0.2005 -0.0202 0.0414  0.0243  165 VAL   A CB  
3652 C  CB  B VAL   A 165 ? 0.2202 0.1898 0.1972 -0.0086 0.0085  0.0478  165 VAL   A CB  
3653 C  CG1 A VAL   A 165 ? 0.1754 0.2377 0.1950 -0.0217 0.0385  0.0120  165 VAL   A CG1 
3654 C  CG1 B VAL   A 165 ? 0.2276 0.1963 0.1957 -0.0099 0.0074  0.0402  165 VAL   A CG1 
3655 C  CG2 A VAL   A 165 ? 0.1747 0.2370 0.2014 -0.0189 0.0379  0.0293  165 VAL   A CG2 
3656 C  CG2 B VAL   A 165 ? 0.2267 0.1914 0.1950 -0.0087 0.0030  0.0540  165 VAL   A CG2 
3675 N  N   A SER   A 166 ? 0.1442 0.2436 0.2151 -0.0115 0.0233  0.0376  166 SER   A N   
3676 N  N   B SER   A 166 ? 0.1718 0.1768 0.2030 -0.0072 0.0050  0.0336  166 SER   A N   
3677 C  CA  A SER   A 166 ? 0.1522 0.2550 0.2349 -0.0149 0.0233  0.0400  166 SER   A CA  
3678 C  CA  B SER   A 166 ? 0.1751 0.1965 0.2112 -0.0040 0.0015  0.0248  166 SER   A CA  
3679 C  C   A SER   A 166 ? 0.1578 0.2686 0.2448 -0.0110 0.0088  0.0279  166 SER   A C   
3680 C  C   B SER   A 166 ? 0.1764 0.2031 0.2157 -0.0009 -0.0090 0.0230  166 SER   A C   
3681 O  O   A SER   A 166 ? 0.1730 0.2737 0.2723 -0.0140 0.0080  0.0234  166 SER   A O   
3682 O  O   B SER   A 166 ? 0.1778 0.2015 0.2243 0.0056  -0.0174 0.0169  166 SER   A O   
3683 C  CB  A SER   A 166 ? 0.1663 0.2560 0.2663 -0.0147 0.0189  0.0468  166 SER   A CB  
3684 C  CB  B SER   A 166 ? 0.1802 0.2149 0.2370 0.0012  -0.0087 0.0169  166 SER   A CB  
3685 O  OG  A SER   A 166 ? 0.1932 0.2615 0.2969 -0.0144 0.0204  0.0553  166 SER   A OG  
3686 O  OG  B SER   A 166 ? 0.1971 0.2316 0.2601 -0.0011 -0.0044 0.0180  166 SER   A OG  
3697 N  N   A SER   A 167 ? 0.1594 0.2751 0.2259 0.0024  0.0105  0.0235  167 SER   A N   
3698 N  N   B SER   A 167 ? 0.1849 0.2233 0.2055 0.0034  -0.0120 0.0336  167 SER   A N   
3699 C  CA  A SER   A 167 ? 0.1742 0.2813 0.2260 0.0135  0.0084  0.0150  167 SER   A CA  
3700 C  CA  B SER   A 167 ? 0.2042 0.2412 0.2141 0.0001  -0.0178 0.0380  167 SER   A CA  
3701 C  C   A SER   A 167 ? 0.1765 0.2804 0.2295 0.0178  0.0223  0.0188  167 SER   A C   
3702 C  C   B SER   A 167 ? 0.2148 0.2555 0.2257 0.0030  -0.0029 0.0421  167 SER   A C   
3703 O  O   A SER   A 167 ? 0.1916 0.2837 0.2348 0.0249  0.0199  0.0209  167 SER   A O   
3704 O  O   B SER   A 167 ? 0.2256 0.2619 0.2326 0.0054  -0.0029 0.0394  167 SER   A O   
3705 C  CB  A SER   A 167 ? 0.1866 0.2891 0.2178 0.0204  0.0202  0.0107  167 SER   A CB  
3706 C  CB  B SER   A 167 ? 0.2147 0.2456 0.2140 -0.0085 -0.0192 0.0411  167 SER   A CB  
3707 O  OG  A SER   A 167 ? 0.1909 0.2934 0.2222 0.0216  0.0363  0.0098  167 SER   A OG  
3708 O  OG  B SER   A 167 ? 0.2195 0.2451 0.2218 -0.0158 -0.0159 0.0374  167 SER   A OG  
3719 N  N   A PHE   A 168 ? 0.1647 0.2787 0.2406 0.0225  0.0224  0.0236  168 PHE   A N   
3720 N  N   B PHE   A 168 ? 0.2136 0.2623 0.2435 0.0069  0.0050  0.0546  168 PHE   A N   
3721 C  CA  A PHE   A 168 ? 0.1600 0.2834 0.2591 0.0159  0.0255  0.0280  168 PHE   A CA  
3722 C  CA  B PHE   A 168 ? 0.2134 0.2778 0.2690 0.0036  0.0150  0.0553  168 PHE   A CA  
3723 C  C   A PHE   A 168 ? 0.1743 0.3018 0.2979 0.0098  0.0626  0.0216  168 PHE   A C   
3724 C  C   B PHE   A 168 ? 0.2225 0.2935 0.3042 -0.0101 0.0342  0.0370  168 PHE   A C   
3725 O  O   A PHE   A 168 ? 0.1765 0.3040 0.3227 -0.0021 0.0699  0.0406  168 PHE   A O   
3726 O  O   B PHE   A 168 ? 0.2270 0.2933 0.3291 -0.0168 0.0422  0.0404  168 PHE   A O   
3727 C  CB  A PHE   A 168 ? 0.1565 0.2789 0.2513 0.0061  0.0003  0.0251  168 PHE   A CB  
3728 C  CB  B PHE   A 168 ? 0.2091 0.2811 0.2664 0.0115  0.0125  0.0664  168 PHE   A CB  
3729 C  CG  A PHE   A 168 ? 0.1492 0.2759 0.2419 -0.0060 -0.0180 0.0247  168 PHE   A CG  
3730 C  CG  B PHE   A 168 ? 0.2048 0.2858 0.2635 0.0138  0.0146  0.0780  168 PHE   A CG  
3731 C  CD1 A PHE   A 168 ? 0.1515 0.2776 0.2425 -0.0124 -0.0186 0.0302  168 PHE   A CD1 
3732 C  CD1 B PHE   A 168 ? 0.2065 0.2895 0.2630 0.0132  0.0211  0.0871  168 PHE   A CD1 
3733 C  CD2 A PHE   A 168 ? 0.1488 0.2726 0.2431 -0.0115 -0.0138 0.0242  168 PHE   A CD2 
3734 C  CD2 B PHE   A 168 ? 0.2023 0.2869 0.2669 0.0120  0.0220  0.0823  168 PHE   A CD2 
3735 C  CE1 A PHE   A 168 ? 0.1427 0.2742 0.2320 -0.0191 -0.0200 0.0343  168 PHE   A CE1 
3736 C  CE1 B PHE   A 168 ? 0.2029 0.2900 0.2627 0.0120  0.0264  0.0958  168 PHE   A CE1 
3737 C  CE2 A PHE   A 168 ? 0.1580 0.2678 0.2456 -0.0161 -0.0103 0.0326  168 PHE   A CE2 
3738 C  CE2 B PHE   A 168 ? 0.2060 0.2854 0.2691 0.0105  0.0274  0.0905  168 PHE   A CE2 
3739 C  CZ  A PHE   A 168 ? 0.1504 0.2688 0.2400 -0.0180 -0.0182 0.0342  168 PHE   A CZ  
3740 C  CZ  B PHE   A 168 ? 0.2025 0.2866 0.2666 0.0119  0.0269  0.0953  168 PHE   A CZ  
3759 N  N   A LEU   A 169 ? 0.2205 0.3213 0.3400 0.0008  0.0628  -0.0028 169 LEU   A N   
3760 N  N   B LEU   A 169 ? 0.2430 0.3090 0.3272 -0.0213 0.0337  0.0163  169 LEU   A N   
3761 C  CA  A LEU   A 169 ? 0.2856 0.3486 0.4025 0.0019  0.0303  -0.0184 169 LEU   A CA  
3762 C  CA  B LEU   A 169 ? 0.2752 0.3303 0.3661 -0.0229 0.0166  0.0011  169 LEU   A CA  
3763 C  C   A LEU   A 169 ? 0.3005 0.3563 0.4304 0.0048  0.0212  -0.0140 169 LEU   A C   
3764 C  C   B LEU   A 169 ? 0.2711 0.3331 0.3730 -0.0243 0.0095  0.0125  169 LEU   A C   
3765 O  O   A LEU   A 169 ? 0.3063 0.3597 0.4367 0.0107  0.0160  -0.0164 169 LEU   A O   
3766 O  O   B LEU   A 169 ? 0.2720 0.3356 0.3764 -0.0194 0.0055  0.0157  169 LEU   A O   
3767 C  CB  A LEU   A 169 ? 0.3260 0.3675 0.4205 -0.0009 0.0144  -0.0383 169 LEU   A CB  
3768 C  CB  B LEU   A 169 ? 0.3047 0.3475 0.3867 -0.0252 0.0097  -0.0238 169 LEU   A CB  
3769 C  CG  A LEU   A 169 ? 0.3593 0.3836 0.4350 -0.0051 0.0037  -0.0580 169 LEU   A CG  
3770 C  CG  B LEU   A 169 ? 0.3304 0.3627 0.4051 -0.0280 0.0048  -0.0452 169 LEU   A CG  
3771 C  CD1 A LEU   A 169 ? 0.3700 0.3877 0.4424 -0.0069 -0.0014 -0.0643 169 LEU   A CD1 
3772 C  CD1 B LEU   A 169 ? 0.3386 0.3665 0.4137 -0.0291 0.0020  -0.0525 169 LEU   A CD1 
3773 C  CD2 A LEU   A 169 ? 0.3707 0.3909 0.4354 -0.0070 0.0019  -0.0652 169 LEU   A CD2 
3774 C  CD2 B LEU   A 169 ? 0.3402 0.3705 0.4082 -0.0287 0.0052  -0.0512 169 LEU   A CD2 
3775 O  OXT A LEU   A 169 ? 0.2982 0.3598 0.4381 0.0019  0.0222  -0.0113 169 LEU   A OXT 
3776 O  OXT B LEU   A 169 ? 0.2607 0.3329 0.3638 -0.0304 0.0070  0.0169  169 LEU   A OXT 
3799 N  N   A SER   B 1   ? 0.3896 0.3630 0.3938 -0.0943 -0.0838 0.0442  1   SER   B N   
3800 N  N   B SER   B 1   ? 0.3573 0.3532 0.3684 -0.0888 -0.0735 0.0415  1   SER   B N   
3801 C  CA  A SER   B 1   ? 0.3849 0.3635 0.3990 -0.0975 -0.0827 0.0423  1   SER   B CA  
3802 C  CA  B SER   B 1   ? 0.3522 0.3545 0.3703 -0.0905 -0.0732 0.0395  1   SER   B CA  
3803 C  C   A SER   B 1   ? 0.3635 0.3613 0.3829 -0.0989 -0.0846 0.0571  1   SER   B C   
3804 C  C   B SER   B 1   ? 0.3329 0.3524 0.3444 -0.0885 -0.0814 0.0512  1   SER   B C   
3805 O  O   A SER   B 1   ? 0.3730 0.3640 0.3672 -0.0922 -0.0810 0.0566  1   SER   B O   
3806 O  O   B SER   B 1   ? 0.3352 0.3528 0.3183 -0.0864 -0.0877 0.0501  1   SER   B O   
3807 C  CB  A SER   B 1   ? 0.3965 0.3635 0.4084 -0.0965 -0.0805 0.0295  1   SER   B CB  
3808 C  CB  B SER   B 1   ? 0.3622 0.3554 0.3875 -0.0909 -0.0658 0.0281  1   SER   B CB  
3809 O  OG  A SER   B 1   ? 0.4083 0.3707 0.4406 -0.0930 -0.0784 0.0249  1   SER   B OG  
3810 O  OG  B SER   B 1   ? 0.3715 0.3621 0.4200 -0.0898 -0.0633 0.0230  1   SER   B OG  
3825 N  N   A MET   B 2   ? 0.3331 0.3530 0.3749 -0.1029 -0.0844 0.0860  2   MET   B N   
3826 N  N   B MET   B 2   ? 0.3138 0.3471 0.3378 -0.0841 -0.0785 0.0763  2   MET   B N   
3827 C  CA  A MET   B 2   ? 0.3080 0.3476 0.3812 -0.0913 -0.0820 0.1060  2   MET   B CA  
3828 C  CA  B MET   B 2   ? 0.2995 0.3430 0.3421 -0.0679 -0.0728 0.0945  2   MET   B CA  
3829 C  C   A MET   B 2   ? 0.2623 0.3182 0.3316 -0.0831 -0.0957 0.1330  2   MET   B C   
3830 C  C   B MET   B 2   ? 0.2728 0.3206 0.3085 -0.0547 -0.0725 0.1082  2   MET   B C   
3831 O  O   A MET   B 2   ? 0.2492 0.3227 0.3208 -0.0817 -0.1036 0.1424  2   MET   B O   
3832 O  O   B MET   B 2   ? 0.2730 0.3298 0.3170 -0.0487 -0.0700 0.1068  2   MET   B O   
3833 C  CB  A MET   B 2   ? 0.3365 0.3770 0.4560 -0.0727 -0.0621 0.0850  2   MET   B CB  
3834 C  CB  B MET   B 2   ? 0.3182 0.3651 0.3939 -0.0545 -0.0658 0.0908  2   MET   B CB  
3835 C  CG  A MET   B 2   ? 0.3621 0.4014 0.5231 -0.0537 -0.0429 0.0695  2   MET   B CG  
3836 C  CG  B MET   B 2   ? 0.3342 0.3846 0.4363 -0.0419 -0.0554 0.0936  2   MET   B CG  
3837 S  SD  A MET   B 2   ? 0.3850 0.4232 0.5876 -0.0371 -0.0313 0.0599  2   MET   B SD  
3838 S  SD  B MET   B 2   ? 0.3497 0.4042 0.4761 -0.0306 -0.0508 0.0976  2   MET   B SD  
3839 C  CE  A MET   B 2   ? 0.3889 0.4293 0.5938 -0.0349 -0.0255 0.0609  2   MET   B CE  
3840 C  CE  B MET   B 2   ? 0.3506 0.4074 0.4819 -0.0301 -0.0486 0.0944  2   MET   B CE  
3859 N  N   A VAL   B 3   ? 0.2329 0.2804 0.3056 -0.0825 -0.0931 0.1382  3   VAL   B N   
3860 N  N   B VAL   B 3   ? 0.2484 0.2870 0.2772 -0.0508 -0.0692 0.1130  3   VAL   B N   
3861 C  CA  A VAL   B 3   ? 0.2209 0.2488 0.2952 -0.0732 -0.0827 0.1232  3   VAL   B CA  
3862 C  CA  B VAL   B 3   ? 0.2331 0.2566 0.2624 -0.0427 -0.0595 0.0937  3   VAL   B CA  
3863 C  C   A VAL   B 3   ? 0.2012 0.2357 0.2582 -0.0616 -0.0736 0.1072  3   VAL   B C   
3864 C  C   B VAL   B 3   ? 0.2109 0.2421 0.2352 -0.0376 -0.0580 0.0884  3   VAL   B C   
3865 O  O   A VAL   B 3   ? 0.1920 0.2313 0.2658 -0.0649 -0.0702 0.1112  3   VAL   B O   
3866 O  O   B VAL   B 3   ? 0.2074 0.2438 0.2284 -0.0208 -0.0586 0.0839  3   VAL   B O   
3867 C  CB  A VAL   B 3   ? 0.2369 0.2425 0.3331 -0.0751 -0.0675 0.1101  3   VAL   B CB  
3868 C  CB  B VAL   B 3   ? 0.2441 0.2432 0.2776 -0.0432 -0.0451 0.0818  3   VAL   B CB  
3869 C  CG1 A VAL   B 3   ? 0.2424 0.2385 0.3484 -0.0797 -0.0632 0.1056  3   VAL   B CG1 
3870 C  CG1 B VAL   B 3   ? 0.2472 0.2374 0.2850 -0.0479 -0.0418 0.0757  3   VAL   B CG1 
3871 C  CG2 A VAL   B 3   ? 0.2422 0.2469 0.3500 -0.0711 -0.0554 0.1076  3   VAL   B CG2 
3872 C  CG2 B VAL   B 3   ? 0.2496 0.2437 0.2848 -0.0386 -0.0375 0.0820  3   VAL   B CG2 
3891 N  N   . ASN   B 4   ? 0.1968 0.2237 0.2299 -0.0507 -0.0640 0.0862  4   ASN   B N   
3892 C  CA  . ASN   B 4   ? 0.1970 0.2222 0.2089 -0.0569 -0.0499 0.0474  4   ASN   B CA  
3893 C  C   . ASN   B 4   ? 0.2074 0.2350 0.2019 -0.0628 -0.0284 0.0328  4   ASN   B C   
3894 O  O   . ASN   B 4   ? 0.2097 0.2459 0.2143 -0.0552 -0.0296 0.0121  4   ASN   B O   
3895 C  CB  . ASN   B 4   ? 0.1957 0.2167 0.2014 -0.0498 -0.0580 0.0380  4   ASN   B CB  
3896 C  CG  . ASN   B 4   ? 0.1960 0.2020 0.1899 -0.0456 -0.0577 0.0303  4   ASN   B CG  
3897 O  OD1 . ASN   B 4   ? 0.2012 0.1817 0.1914 -0.0418 -0.0549 0.0263  4   ASN   B OD1 
3898 N  ND2 . ASN   B 4   ? 0.2146 0.2079 0.1915 -0.0278 -0.0450 0.0211  4   ASN   B ND2 
3906 N  N   . SER   B 5   ? 0.2243 0.2537 0.2149 -0.0629 -0.0175 0.0334  5   SER   B N   
3907 C  CA  . SER   B 5   ? 0.2558 0.2895 0.2543 -0.0517 0.0054  0.0370  5   SER   B CA  
3908 C  C   . SER   B 5   ? 0.2742 0.2878 0.2769 -0.0675 0.0236  0.0381  5   SER   B C   
3909 O  O   . SER   B 5   ? 0.2915 0.2835 0.3288 -0.0628 0.0449  0.0328  5   SER   B O   
3910 C  CB  . SER   B 5   ? 0.2683 0.3168 0.2839 -0.0400 0.0145  0.0470  5   SER   B CB  
3911 O  OG  . SER   B 5   ? 0.2863 0.3385 0.3370 -0.0293 0.0190  0.0486  5   SER   B OG  
3917 N  N   . PHE   B 6   ? 0.2879 0.3017 0.2591 -0.0699 0.0320  0.0423  6   PHE   B N   
3918 C  CA  . PHE   B 6   ? 0.2946 0.3024 0.2319 -0.0849 0.0391  0.0260  6   PHE   B CA  
3919 C  C   . PHE   B 6   ? 0.3469 0.3319 0.2759 -0.0883 0.0608  -0.0078 6   PHE   B C   
3920 O  O   . PHE   B 6   ? 0.3577 0.3647 0.3035 -0.0790 0.0457  -0.0190 6   PHE   B O   
3921 C  CB  . PHE   B 6   ? 0.2628 0.2811 0.2021 -0.0767 0.0183  0.0234  6   PHE   B CB  
3922 C  CG  . PHE   B 6   ? 0.2270 0.2490 0.1844 -0.0775 -0.0016 0.0201  6   PHE   B CG  
3923 C  CD1 . PHE   B 6   ? 0.2266 0.2278 0.1768 -0.0685 -0.0185 0.0127  6   PHE   B CD1 
3924 C  CD2 . PHE   B 6   ? 0.2076 0.2479 0.1861 -0.0646 -0.0037 0.0391  6   PHE   B CD2 
3925 C  CE1 . PHE   B 6   ? 0.2223 0.2081 0.1822 -0.0575 -0.0218 0.0108  6   PHE   B CE1 
3926 C  CE2 . PHE   B 6   ? 0.2084 0.2359 0.2118 -0.0524 0.0021  0.0384  6   PHE   B CE2 
3927 C  CZ  . PHE   B 6   ? 0.2152 0.2166 0.2012 -0.0500 -0.0110 0.0138  6   PHE   B CZ  
3937 N  N   A SER   B 7   ? 0.3680 0.3169 0.2854 -0.1021 0.0763  -0.0286 7   SER   B N   
3938 N  N   B SER   B 7   ? 0.3656 0.3242 0.2925 -0.0957 0.0729  -0.0192 7   SER   B N   
3939 C  CA  A SER   B 7   ? 0.3885 0.3155 0.3161 -0.1025 0.0882  -0.0423 7   SER   B CA  
3940 C  CA  B SER   B 7   ? 0.3832 0.3257 0.3239 -0.0933 0.0814  -0.0266 7   SER   B CA  
3941 C  C   A SER   B 7   ? 0.3901 0.3027 0.3011 -0.1053 0.0986  -0.0482 7   SER   B C   
3942 C  C   B SER   B 7   ? 0.3854 0.3149 0.3113 -0.0955 0.0870  -0.0317 7   SER   B C   
3943 O  O   A SER   B 7   ? 0.3942 0.3024 0.3104 -0.1071 0.1002  -0.0424 7   SER   B O   
3944 O  O   B SER   B 7   ? 0.3885 0.3159 0.3169 -0.0967 0.0881  -0.0265 7   SER   B O   
3945 C  CB  A SER   B 7   ? 0.4020 0.3258 0.3602 -0.0979 0.0933  -0.0447 7   SER   B CB  
3946 C  CB  B SER   B 7   ? 0.3940 0.3361 0.3639 -0.0870 0.0848  -0.0269 7   SER   B CB  
3947 O  OG  A SER   B 7   ? 0.4106 0.3348 0.3929 -0.0957 0.0935  -0.0419 7   SER   B OG  
3948 O  OG  B SER   B 7   ? 0.4005 0.3444 0.3933 -0.0829 0.0841  -0.0237 7   SER   B OG  
3959 N  N   A GLY   B 8   ? 0.3879 0.2927 0.2957 -0.0996 0.1061  -0.0575 8   GLY   B N   
3960 N  N   B GLY   B 8   ? 0.3840 0.3036 0.3068 -0.0925 0.0913  -0.0413 8   GLY   B N   
3961 C  CA  A GLY   B 8   ? 0.3797 0.2794 0.2931 -0.0961 0.1076  -0.0621 8   GLY   B CA  
3962 C  CA  B GLY   B 8   ? 0.3775 0.2887 0.3017 -0.0910 0.0931  -0.0491 8   GLY   B CA  
3963 C  C   A GLY   B 8   ? 0.3685 0.2619 0.2875 -0.0930 0.1053  -0.0605 8   GLY   B C   
3964 C  C   B GLY   B 8   ? 0.3679 0.2695 0.2926 -0.0899 0.0926  -0.0537 8   GLY   B C   
3965 O  O   A GLY   B 8   ? 0.3719 0.2613 0.3070 -0.0913 0.1092  -0.0668 8   GLY   B O   
3966 O  O   B GLY   B 8   ? 0.3714 0.2744 0.3098 -0.0858 0.0921  -0.0566 8   GLY   B O   
3973 N  N   . TYR   B 9   ? 0.3597 0.2499 0.2720 -0.0849 0.0877  -0.0632 9   TYR   B N   
3974 C  CA  . TYR   B 9   ? 0.3414 0.2185 0.2374 -0.0680 0.0659  -0.0511 9   TYR   B CA  
3975 C  C   . TYR   B 9   ? 0.3384 0.2202 0.2271 -0.0628 0.0346  -0.0357 9   TYR   B C   
3976 O  O   . TYR   B 9   ? 0.3541 0.2399 0.2593 -0.0650 0.0308  -0.0220 9   TYR   B O   
3977 C  CB  . TYR   B 9   ? 0.3313 0.1905 0.2420 -0.0608 0.0641  -0.0418 9   TYR   B CB  
3978 C  CG  . TYR   B 9   ? 0.3205 0.1734 0.2466 -0.0652 0.0579  -0.0461 9   TYR   B CG  
3979 C  CD1 . TYR   B 9   ? 0.3226 0.1782 0.2694 -0.0764 0.0602  -0.0412 9   TYR   B CD1 
3980 C  CD2 . TYR   B 9   ? 0.3069 0.1708 0.2340 -0.0605 0.0515  -0.0466 9   TYR   B CD2 
3981 C  CE1 . TYR   B 9   ? 0.3196 0.1894 0.2744 -0.0816 0.0628  -0.0494 9   TYR   B CE1 
3982 C  CE2 . TYR   B 9   ? 0.3064 0.1724 0.2395 -0.0647 0.0542  -0.0470 9   TYR   B CE2 
3983 C  CZ  . TYR   B 9   ? 0.3119 0.1931 0.2665 -0.0750 0.0619  -0.0581 9   TYR   B CZ  
3984 O  OH  . TYR   B 9   ? 0.3054 0.2083 0.2786 -0.0867 0.0697  -0.0738 9   TYR   B OH  
3995 N  N   . LEU   B 10  ? 0.3173 0.1947 0.2069 -0.0597 0.0102  -0.0384 10  LEU   B N   
3996 C  CA  . LEU   B 10  ? 0.3094 0.1934 0.2059 -0.0652 -0.0202 -0.0387 10  LEU   B CA  
3997 C  C   . LEU   B 10  ? 0.2904 0.1921 0.2021 -0.0702 -0.0314 -0.0328 10  LEU   B C   
3998 O  O   . LEU   B 10  ? 0.2733 0.1926 0.2047 -0.0572 -0.0177 -0.0249 10  LEU   B O   
3999 C  CB  . LEU   B 10  ? 0.3203 0.1911 0.2265 -0.0649 -0.0440 -0.0175 10  LEU   B CB  
4000 C  CG  . LEU   B 10  ? 0.3349 0.1968 0.2638 -0.0603 -0.0662 -0.0084 10  LEU   B CG  
4001 C  CD1 . LEU   B 10  ? 0.3457 0.2152 0.2887 -0.0552 -0.0597 -0.0076 10  LEU   B CD1 
4002 C  CD2 . LEU   B 10  ? 0.3441 0.1974 0.2938 -0.0582 -0.0644 0.0168  10  LEU   B CD2 
4014 N  N   . LYS   B 11  ? 0.3040 0.2220 0.2124 -0.0633 -0.0452 -0.0250 11  LYS   B N   
4015 C  CA  . LYS   B 11  ? 0.3170 0.2525 0.2520 -0.0504 -0.0593 -0.0347 11  LYS   B CA  
4016 C  C   . LYS   B 11  ? 0.2964 0.2317 0.2522 -0.0694 -0.0512 -0.0465 11  LYS   B C   
4017 O  O   . LYS   B 11  ? 0.3105 0.2443 0.2746 -0.0815 -0.0405 -0.0709 11  LYS   B O   
4018 C  CB  . LYS   B 11  ? 0.3507 0.3036 0.3267 -0.0238 -0.0627 -0.0312 11  LYS   B CB  
4019 C  CG  . LYS   B 11  ? 0.3803 0.3379 0.3996 -0.0087 -0.0589 -0.0311 11  LYS   B CG  
4020 C  CD  . LYS   B 11  ? 0.4024 0.3616 0.4653 -0.0023 -0.0558 -0.0336 11  LYS   B CD  
4021 C  CE  . LYS   B 11  ? 0.4191 0.3772 0.5129 -0.0004 -0.0560 -0.0384 11  LYS   B CE  
4022 N  NZ  . LYS   B 11  ? 0.4283 0.3865 0.5375 -0.0006 -0.0599 -0.0400 11  LYS   B NZ  
4036 N  N   . LEU   B 12  ? 0.2609 0.2065 0.2435 -0.0653 -0.0552 -0.0377 12  LEU   B N   
4037 C  CA  . LEU   B 12  ? 0.2434 0.1864 0.2591 -0.0583 -0.0489 -0.0253 12  LEU   B CA  
4038 C  C   . LEU   B 12  ? 0.2300 0.1855 0.2627 -0.0589 -0.0624 -0.0200 12  LEU   B C   
4039 O  O   . LEU   B 12  ? 0.2262 0.1879 0.2806 -0.0663 -0.0709 -0.0105 12  LEU   B O   
4040 C  CB  . LEU   B 12  ? 0.2439 0.1685 0.2560 -0.0459 -0.0396 -0.0225 12  LEU   B CB  
4041 C  CG  . LEU   B 12  ? 0.2386 0.1637 0.2554 -0.0425 -0.0292 -0.0139 12  LEU   B CG  
4042 C  CD1 . LEU   B 12  ? 0.2465 0.1681 0.2476 -0.0289 -0.0215 0.0040  12  LEU   B CD1 
4043 C  CD2 . LEU   B 12  ? 0.2438 0.1664 0.2653 -0.0416 -0.0203 -0.0236 12  LEU   B CD2 
4055 N  N   . THR   B 13  ? 0.2232 0.1900 0.2728 -0.0555 -0.0591 -0.0303 13  THR   B N   
4056 C  CA  . THR   B 13  ? 0.2232 0.1984 0.2695 -0.0576 -0.0704 -0.0186 13  THR   B CA  
4057 C  C   . THR   B 13  ? 0.2586 0.2147 0.2858 -0.0663 -0.0841 -0.0196 13  THR   B C   
4058 O  O   . THR   B 13  ? 0.2733 0.2109 0.2996 -0.0646 -0.0492 -0.0183 13  THR   B O   
4059 C  CB  . THR   B 13  ? 0.2039 0.1953 0.2754 -0.0497 -0.0617 -0.0144 13  THR   B CB  
4060 O  OG1 . THR   B 13  ? 0.1896 0.1865 0.2813 -0.0419 -0.0535 -0.0215 13  THR   B OG1 
4061 C  CG2 . THR   B 13  ? 0.2115 0.2015 0.2817 -0.0455 -0.0452 -0.0020 13  THR   B CG2 
4069 N  N   A ASP   B 14  ? 0.2693 0.2288 0.2961 -0.0702 -0.1098 -0.0110 14  ASP   B N   
4070 N  N   B ASP   B 14  ? 0.2689 0.2284 0.2946 -0.0645 -0.0994 -0.0066 14  ASP   B N   
4071 C  CA  A ASP   B 14  ? 0.2787 0.2422 0.3274 -0.0697 -0.1086 0.0077  14  ASP   B CA  
4072 C  CA  B ASP   B 14  ? 0.2775 0.2411 0.3164 -0.0607 -0.0964 0.0111  14  ASP   B CA  
4073 C  C   A ASP   B 14  ? 0.2658 0.2229 0.2900 -0.0667 -0.0964 0.0093  14  ASP   B C   
4074 C  C   B ASP   B 14  ? 0.2618 0.2206 0.2867 -0.0596 -0.0916 0.0106  14  ASP   B C   
4075 O  O   A ASP   B 14  ? 0.2822 0.2332 0.2824 -0.0674 -0.0965 0.0171  14  ASP   B O   
4076 O  O   B ASP   B 14  ? 0.2715 0.2242 0.2822 -0.0571 -0.0948 0.0170  14  ASP   B O   
4077 C  CB  A ASP   B 14  ? 0.2965 0.2723 0.4027 -0.0728 -0.1167 0.0090  14  ASP   B CB  
4078 C  CB  B ASP   B 14  ? 0.2982 0.2716 0.3734 -0.0582 -0.0947 0.0172  14  ASP   B CB  
4079 C  CG  A ASP   B 14  ? 0.3191 0.2985 0.4752 -0.0708 -0.1115 0.0017  14  ASP   B CG  
4080 C  CG  B ASP   B 14  ? 0.3209 0.2988 0.4284 -0.0531 -0.0858 0.0156  14  ASP   B CG  
4081 O  OD1 A ASP   B 14  ? 0.3295 0.3035 0.4934 -0.0795 -0.1142 -0.0129 14  ASP   B OD1 
4082 O  OD1 B ASP   B 14  ? 0.3309 0.3086 0.4413 -0.0532 -0.0793 0.0125  14  ASP   B OD1 
4083 O  OD2 A ASP   B 14  ? 0.3235 0.3086 0.5082 -0.0673 -0.1036 0.0079  14  ASP   B OD2 
4084 O  OD2 B ASP   B 14  ? 0.3261 0.3068 0.4516 -0.0560 -0.0842 0.0147  14  ASP   B OD2 
4093 N  N   . ASN   B 15  ? 0.2313 0.1951 0.2682 -0.0576 -0.0884 0.0079  15  ASN   B N   
4094 C  CA  . ASN   B 15  ? 0.1903 0.1668 0.2442 -0.0385 -0.0668 0.0046  15  ASN   B CA  
4095 C  C   . ASN   B 15  ? 0.1748 0.1575 0.2310 -0.0223 -0.0506 0.0011  15  ASN   B C   
4096 O  O   . ASN   B 15  ? 0.1761 0.1565 0.2463 -0.0265 -0.0549 -0.0063 15  ASN   B O   
4097 C  CB  . ASN   B 15  ? 0.1852 0.1678 0.2550 -0.0213 -0.0635 0.0026  15  ASN   B CB  
4098 C  CG  . ASN   B 15  ? 0.1734 0.1642 0.2558 -0.0218 -0.0380 0.0120  15  ASN   B CG  
4099 O  OD1 . ASN   B 15  ? 0.1759 0.1913 0.2875 -0.0423 -0.0417 0.0214  15  ASN   B OD1 
4100 N  ND2 . ASN   B 15  ? 0.1728 0.1414 0.2511 -0.0127 -0.0172 -0.0058 15  ASN   B ND2 
4108 N  N   . VAL   B 16  ? 0.1806 0.1519 0.2265 -0.0291 -0.0555 -0.0029 16  VAL   B N   
4109 C  CA  . VAL   B 16  ? 0.1823 0.1546 0.2082 -0.0284 -0.0416 -0.0194 16  VAL   B CA  
4110 C  C   . VAL   B 16  ? 0.1780 0.1641 0.2143 -0.0366 -0.0449 -0.0180 16  VAL   B C   
4111 O  O   . VAL   B 16  ? 0.1818 0.1776 0.2399 -0.0386 -0.0375 -0.0299 16  VAL   B O   
4112 C  CB  . VAL   B 16  ? 0.1882 0.1511 0.2259 -0.0167 -0.0323 -0.0192 16  VAL   B CB  
4113 C  CG1 . VAL   B 16  ? 0.1927 0.1456 0.2120 -0.0009 -0.0266 -0.0076 16  VAL   B CG1 
4114 C  CG2 . VAL   B 16  ? 0.1851 0.1569 0.2463 -0.0148 -0.0303 -0.0194 16  VAL   B CG2 
4124 N  N   . TYR   B 17  ? 0.1865 0.1656 0.2083 -0.0337 -0.0436 -0.0249 17  TYR   B N   
4125 C  CA  . TYR   B 17  ? 0.1967 0.1783 0.1988 -0.0393 -0.0370 -0.0013 17  TYR   B CA  
4126 C  C   . TYR   B 17  ? 0.1862 0.1563 0.2003 -0.0386 -0.0290 -0.0058 17  TYR   B C   
4127 O  O   . TYR   B 17  ? 0.1790 0.1614 0.2092 -0.0297 -0.0388 -0.0254 17  TYR   B O   
4128 C  CB  . TYR   B 17  ? 0.2307 0.2205 0.2231 -0.0249 -0.0436 0.0322  17  TYR   B CB  
4129 C  CG  . TYR   B 17  ? 0.2594 0.2721 0.2728 -0.0216 -0.0601 0.0418  17  TYR   B CG  
4130 C  CD1 . TYR   B 17  ? 0.2741 0.2868 0.3006 -0.0194 -0.0659 0.0594  17  TYR   B CD1 
4131 C  CD2 . TYR   B 17  ? 0.2807 0.3003 0.3057 -0.0139 -0.0703 0.0442  17  TYR   B CD2 
4132 C  CE1 . TYR   B 17  ? 0.2918 0.3091 0.3219 -0.0134 -0.0754 0.0534  17  TYR   B CE1 
4133 C  CE2 . TYR   B 17  ? 0.2961 0.3179 0.3313 -0.0042 -0.0798 0.0501  17  TYR   B CE2 
4134 C  CZ  . TYR   B 17  ? 0.3049 0.3265 0.3415 -0.0044 -0.0840 0.0544  17  TYR   B CZ  
4135 O  OH  . TYR   B 17  ? 0.3204 0.3413 0.3626 0.0016  -0.0893 0.0569  17  TYR   B OH  
4145 N  N   . ILE   B 18  ? 0.1973 0.1516 0.2001 -0.0338 -0.0193 -0.0174 18  ILE   B N   
4146 C  CA  . ILE   B 18  ? 0.2034 0.1484 0.1874 -0.0340 -0.0186 -0.0200 18  ILE   B CA  
4147 C  C   . ILE   B 18  ? 0.2182 0.1553 0.1795 -0.0424 -0.0138 -0.0289 18  ILE   B C   
4148 O  O   . ILE   B 18  ? 0.2391 0.1693 0.1968 -0.0393 -0.0097 -0.0356 18  ILE   B O   
4149 C  CB  . ILE   B 18  ? 0.2070 0.1532 0.1988 -0.0417 -0.0145 -0.0195 18  ILE   B CB  
4150 C  CG1 . ILE   B 18  ? 0.2094 0.1576 0.2144 -0.0400 -0.0110 -0.0057 18  ILE   B CG1 
4151 C  CG2 . ILE   B 18  ? 0.2114 0.1598 0.2015 -0.0418 -0.0168 -0.0154 18  ILE   B CG2 
4152 C  CD1 . ILE   B 18  ? 0.2137 0.1859 0.2298 -0.0373 -0.0217 0.0115  18  ILE   B CD1 
4164 N  N   . LYS   B 19  ? 0.2168 0.1555 0.1960 -0.0243 0.0202  -0.0353 19  LYS   B N   
4165 C  CA  . LYS   B 19  ? 0.2222 0.1594 0.2114 -0.0286 0.0276  -0.0388 19  LYS   B CA  
4166 C  C   . LYS   B 19  ? 0.2040 0.1580 0.2314 -0.0253 0.0250  -0.0406 19  LYS   B C   
4167 O  O   . LYS   B 19  ? 0.1924 0.1598 0.2233 -0.0140 0.0148  -0.0368 19  LYS   B O   
4168 C  CB  . LYS   B 19  ? 0.2423 0.1788 0.2308 -0.0357 0.0381  -0.0290 19  LYS   B CB  
4169 C  CG  . LYS   B 19  ? 0.2668 0.2024 0.2477 -0.0427 0.0420  -0.0271 19  LYS   B CG  
4170 C  CD  . LYS   B 19  ? 0.2912 0.2298 0.2536 -0.0532 0.0458  -0.0225 19  LYS   B CD  
4171 C  CE  . LYS   B 19  ? 0.3186 0.2548 0.2739 -0.0520 0.0433  -0.0218 19  LYS   B CE  
4172 N  NZ  . LYS   B 19  ? 0.3345 0.2716 0.2819 -0.0534 0.0468  -0.0156 19  LYS   B NZ  
4186 N  N   . ASN   B 20  ? 0.2042 0.1739 0.2619 -0.0236 0.0288  -0.0554 20  ASN   B N   
4187 C  CA  . ASN   B 20  ? 0.1993 0.1886 0.2904 -0.0177 0.0300  -0.0684 20  ASN   B CA  
4188 C  C   . ASN   B 20  ? 0.1970 0.2027 0.2907 -0.0226 0.0423  -0.0755 20  ASN   B C   
4189 O  O   . ASN   B 20  ? 0.2100 0.2363 0.3063 -0.0370 0.0418  -0.0767 20  ASN   B O   
4190 C  CB  . ASN   B 20  ? 0.2230 0.1924 0.3227 0.0073  0.0193  -0.0701 20  ASN   B CB  
4191 C  CG  . ASN   B 20  ? 0.2466 0.1995 0.3473 0.0363  0.0222  -0.0813 20  ASN   B CG  
4192 O  OD1 . ASN   B 20  ? 0.2783 0.2257 0.3738 0.0494  0.0172  -0.0845 20  ASN   B OD1 
4193 N  ND2 . ASN   B 20  ? 0.2343 0.2020 0.3418 0.0368  0.0143  -0.0796 20  ASN   B ND2 
4200 N  N   . ALA   B 21  ? 0.1959 0.1859 0.2840 -0.0314 0.0438  -0.0551 21  ALA   B N   
4201 C  CA  . ALA   B 21  ? 0.2066 0.1912 0.2880 -0.0339 0.0350  -0.0433 21  ALA   B CA  
4202 C  C   . ALA   B 21  ? 0.2048 0.1687 0.2719 -0.0210 0.0295  -0.0298 21  ALA   B C   
4203 O  O   . ALA   B 21  ? 0.2056 0.1554 0.2798 -0.0253 0.0206  -0.0224 21  ALA   B O   
4204 C  CB  . ALA   B 21  ? 0.2282 0.2188 0.2914 -0.0432 0.0422  -0.0304 21  ALA   B CB  
4210 N  N   . ASP   B 22  ? 0.1963 0.1633 0.2682 -0.0163 0.0260  -0.0285 22  ASP   B N   
4211 C  CA  . ASP   B 22  ? 0.1907 0.1566 0.2549 -0.0094 0.0210  -0.0262 22  ASP   B CA  
4212 C  C   . ASP   B 22  ? 0.1854 0.1534 0.2104 -0.0159 0.0081  -0.0128 22  ASP   B C   
4213 O  O   . ASP   B 22  ? 0.1908 0.1595 0.2208 -0.0117 0.0058  -0.0028 22  ASP   B O   
4214 C  CB  . ASP   B 22  ? 0.1967 0.1672 0.2989 -0.0089 0.0112  -0.0069 22  ASP   B CB  
4215 C  CG  . ASP   B 22  ? 0.1978 0.1828 0.3453 -0.0046 -0.0079 -0.0049 22  ASP   B CG  
4216 O  OD1 . ASP   B 22  ? 0.2133 0.1721 0.3443 0.0000  -0.0266 -0.0078 22  ASP   B OD1 
4217 O  OD2 . ASP   B 22  ? 0.2073 0.2151 0.3942 0.0088  -0.0296 -0.0131 22  ASP   B OD2 
4222 N  N   . ILE   B 23  ? 0.1859 0.1468 0.1962 -0.0095 0.0008  0.0120  23  ILE   B N   
4223 C  CA  . ILE   B 23  ? 0.1738 0.1459 0.1808 -0.0091 -0.0078 0.0081  23  ILE   B CA  
4224 C  C   . ILE   B 23  ? 0.1659 0.1447 0.1818 -0.0072 -0.0161 -0.0012 23  ILE   B C   
4225 O  O   . ILE   B 23  ? 0.1614 0.1470 0.1784 -0.0090 -0.0108 0.0054  23  ILE   B O   
4226 C  CB  . ILE   B 23  ? 0.1739 0.1537 0.2016 -0.0159 -0.0031 0.0128  23  ILE   B CB  
4227 C  CG1 . ILE   B 23  ? 0.1735 0.1617 0.2186 -0.0150 0.0062  0.0228  23  ILE   B CG1 
4228 C  CG2 . ILE   B 23  ? 0.1834 0.1731 0.2161 -0.0163 -0.0036 0.0078  23  ILE   B CG2 
4229 C  CD1 . ILE   B 23  ? 0.1806 0.1764 0.2206 -0.0095 0.0092  0.0202  23  ILE   B CD1 
4241 N  N   . VAL   B 24  ? 0.1704 0.1453 0.1988 -0.0073 -0.0186 0.0016  24  VAL   B N   
4242 C  CA  . VAL   B 24  ? 0.1622 0.1521 0.2197 -0.0062 -0.0198 -0.0009 24  VAL   B CA  
4243 C  C   . VAL   B 24  ? 0.1619 0.1537 0.2330 -0.0114 -0.0184 0.0061  24  VAL   B C   
4244 O  O   . VAL   B 24  ? 0.1626 0.1579 0.2344 -0.0185 -0.0132 0.0105  24  VAL   B O   
4245 C  CB  . VAL   B 24  ? 0.1711 0.1688 0.2212 0.0009  -0.0250 0.0011  24  VAL   B CB  
4246 C  CG1 . VAL   B 24  ? 0.1700 0.1765 0.2432 -0.0096 -0.0284 0.0037  24  VAL   B CG1 
4247 C  CG2 . VAL   B 24  ? 0.1815 0.1982 0.2293 0.0035  -0.0303 -0.0041 24  VAL   B CG2 
4257 N  N   . GLU   B 25  ? 0.1790 0.1640 0.2373 -0.0122 -0.0049 0.0120  25  GLU   B N   
4258 C  CA  . GLU   B 25  ? 0.1937 0.1940 0.2547 -0.0016 0.0067  -0.0031 25  GLU   B CA  
4259 C  C   . GLU   B 25  ? 0.1887 0.1887 0.2140 -0.0081 0.0029  -0.0021 25  GLU   B C   
4260 O  O   . GLU   B 25  ? 0.1929 0.2014 0.2233 -0.0063 0.0106  0.0043  25  GLU   B O   
4261 C  CB  . GLU   B 25  ? 0.2385 0.2416 0.3296 0.0210  0.0127  -0.0026 25  GLU   B CB  
4262 C  CG  . GLU   B 25  ? 0.2867 0.2998 0.4374 0.0343  0.0122  -0.0041 25  GLU   B CG  
4263 C  CD  . GLU   B 25  ? 0.3263 0.3597 0.5270 0.0342  0.0109  -0.0044 25  GLU   B CD  
4264 O  OE1 . GLU   B 25  ? 0.3532 0.3842 0.5547 0.0388  0.0130  -0.0010 25  GLU   B OE1 
4265 O  OE2 . GLU   B 25  ? 0.3494 0.3791 0.5573 0.0349  0.0088  -0.0102 25  GLU   B OE2 
4272 N  N   . GLU   B 26  ? 0.1880 0.1803 0.1921 -0.0250 0.0005  0.0019  26  GLU   B N   
4273 C  CA  . GLU   B 26  ? 0.1845 0.1963 0.1949 -0.0357 -0.0089 0.0060  26  GLU   B CA  
4274 C  C   . GLU   B 26  ? 0.1688 0.1957 0.1830 -0.0236 0.0008  0.0167  26  GLU   B C   
4275 O  O   . GLU   B 26  ? 0.1900 0.2154 0.1818 -0.0254 -0.0053 0.0206  26  GLU   B O   
4276 C  CB  . GLU   B 26  ? 0.2189 0.2146 0.2067 -0.0411 -0.0119 0.0156  26  GLU   B CB  
4277 C  CG  . GLU   B 26  ? 0.2622 0.2470 0.2561 -0.0466 0.0059  -0.0099 26  GLU   B CG  
4278 C  CD  . GLU   B 26  ? 0.2898 0.2697 0.2699 -0.0683 0.0176  -0.0474 26  GLU   B CD  
4279 O  OE1 . GLU   B 26  ? 0.3107 0.2549 0.2804 -0.0755 0.0587  -0.0482 26  GLU   B OE1 
4280 O  OE2 . GLU   B 26  ? 0.2931 0.3086 0.3019 -0.0656 0.0146  -0.0339 26  GLU   B OE2 
4287 N  N   . ALA   B 27  ? 0.1552 0.1761 0.1832 -0.0227 0.0027  0.0213  27  ALA   B N   
4288 C  CA  . ALA   B 27  ? 0.1587 0.1716 0.1977 -0.0143 0.0003  0.0311  27  ALA   B CA  
4289 C  C   . ALA   B 27  ? 0.1656 0.1826 0.2230 -0.0140 0.0111  0.0425  27  ALA   B C   
4290 O  O   . ALA   B 27  ? 0.1734 0.1848 0.2367 -0.0003 0.0134  0.0451  27  ALA   B O   
4291 C  CB  . ALA   B 27  ? 0.1701 0.1570 0.2092 -0.0171 0.0020  0.0259  27  ALA   B CB  
4297 N  N   . LYS   B 28  ? 0.1598 0.2020 0.2538 -0.0181 0.0197  0.0542  28  LYS   B N   
4298 C  CA  . LYS   B 28  ? 0.1768 0.2372 0.2820 -0.0031 0.0511  0.0817  28  LYS   B CA  
4299 C  C   . LYS   B 28  ? 0.1971 0.2535 0.2711 -0.0020 0.0579  0.0771  28  LYS   B C   
4300 O  O   . LYS   B 28  ? 0.2214 0.2598 0.2807 -0.0074 0.0572  0.0785  28  LYS   B O   
4301 C  CB  . LYS   B 28  ? 0.2004 0.2754 0.3381 0.0135  0.0824  0.1024  28  LYS   B CB  
4302 C  CG  . LYS   B 28  ? 0.2427 0.3280 0.3831 0.0240  0.1024  0.1181  28  LYS   B CG  
4303 C  CD  . LYS   B 28  ? 0.3086 0.3927 0.4417 0.0315  0.1203  0.1223  28  LYS   B CD  
4304 C  CE  . LYS   B 28  ? 0.3606 0.4430 0.4915 0.0368  0.1244  0.1304  28  LYS   B CE  
4305 N  NZ  . LYS   B 28  ? 0.3869 0.4614 0.5126 0.0396  0.1240  0.1375  28  LYS   B NZ  
4319 N  N   . LYS   B 29  ? 0.2128 0.2759 0.2778 0.0137  0.0647  0.0659  29  LYS   B N   
4320 C  CA  . LYS   B 29  ? 0.2581 0.3103 0.3082 0.0136  0.0590  0.0674  29  LYS   B CA  
4321 C  C   . LYS   B 29  ? 0.2482 0.3128 0.2712 0.0171  0.0460  0.0787  29  LYS   B C   
4322 O  O   . LYS   B 29  ? 0.2634 0.3322 0.2764 0.0226  0.0454  0.0779  29  LYS   B O   
4323 C  CB  . LYS   B 29  ? 0.3176 0.3485 0.3919 0.0097  0.0540  0.0526  29  LYS   B CB  
4324 C  CG  . LYS   B 29  ? 0.3684 0.3822 0.4776 0.0026  0.0525  0.0468  29  LYS   B CG  
4325 C  CD  . LYS   B 29  ? 0.4127 0.4036 0.5437 -0.0065 0.0570  0.0426  29  LYS   B CD  
4326 C  CE  . LYS   B 29  ? 0.4452 0.4200 0.5876 -0.0123 0.0626  0.0384  29  LYS   B CE  
4327 N  NZ  . LYS   B 29  ? 0.4601 0.4258 0.6150 -0.0151 0.0646  0.0348  29  LYS   B NZ  
4341 N  N   . VAL   B 30  ? 0.2218 0.2948 0.2519 0.0086  0.0333  0.0808  30  VAL   B N   
4342 C  CA  . VAL   B 30  ? 0.2078 0.2860 0.2727 -0.0039 0.0045  0.0848  30  VAL   B CA  
4343 C  C   . VAL   B 30  ? 0.1905 0.2838 0.2641 -0.0047 0.0135  0.1060  30  VAL   B C   
4344 O  O   . VAL   B 30  ? 0.2069 0.3025 0.2708 0.0059  0.0158  0.1181  30  VAL   B O   
4345 C  CB  . VAL   B 30  ? 0.2133 0.2809 0.2987 -0.0155 -0.0220 0.0744  30  VAL   B CB  
4346 C  CG1 . VAL   B 30  ? 0.2177 0.2862 0.3007 -0.0143 -0.0207 0.0663  30  VAL   B CG1 
4347 C  CG2 . VAL   B 30  ? 0.2274 0.2820 0.3160 -0.0220 -0.0279 0.0621  30  VAL   B CG2 
4357 N  N   . LYS   B 31  ? 0.1805 0.2531 0.2977 -0.0239 0.0118  0.1072  31  LYS   B N   
4358 C  CA  . LYS   B 31  ? 0.1725 0.2504 0.3364 -0.0402 0.0024  0.1091  31  LYS   B CA  
4359 C  C   . LYS   B 31  ? 0.1610 0.2034 0.3014 -0.0357 -0.0235 0.0925  31  LYS   B C   
4360 O  O   . LYS   B 31  ? 0.1712 0.2165 0.3245 -0.0277 -0.0140 0.1103  31  LYS   B O   
4361 C  CB  . LYS   B 31  ? 0.2000 0.3041 0.3953 -0.0399 0.0258  0.1258  31  LYS   B CB  
4362 C  CG  . LYS   B 31  ? 0.2423 0.3596 0.4424 -0.0404 0.0382  0.1257  31  LYS   B CG  
4363 C  CD  . LYS   B 31  ? 0.2949 0.4188 0.4911 -0.0370 0.0335  0.1105  31  LYS   B CD  
4364 C  CE  . LYS   B 31  ? 0.3423 0.4558 0.5326 -0.0365 0.0280  0.0998  31  LYS   B CE  
4365 N  NZ  . LYS   B 31  ? 0.3590 0.4808 0.5477 -0.0325 0.0202  0.0943  31  LYS   B NZ  
4379 N  N   . PRO   B 32  ? 0.1716 0.1640 0.2278 -0.0317 -0.0439 0.0539  32  PRO   B N   
4380 C  CA  . PRO   B 32  ? 0.1844 0.1590 0.1929 -0.0322 -0.0401 0.0311  32  PRO   B CA  
4381 C  C   . PRO   B 32  ? 0.1976 0.1500 0.1875 -0.0328 -0.0598 0.0376  32  PRO   B C   
4382 O  O   . PRO   B 32  ? 0.2096 0.1523 0.2157 -0.0361 -0.0821 0.0256  32  PRO   B O   
4383 C  CB  . PRO   B 32  ? 0.1992 0.1541 0.1927 -0.0373 -0.0364 0.0175  32  PRO   B CB  
4384 C  CG  . PRO   B 32  ? 0.2130 0.1461 0.1952 -0.0290 -0.0531 0.0186  32  PRO   B CG  
4385 C  CD  . PRO   B 32  ? 0.1999 0.1540 0.2114 -0.0251 -0.0635 0.0276  32  PRO   B CD  
4393 N  N   . THR   B 33  ? 0.1958 0.1407 0.1793 -0.0326 -0.0515 0.0308  33  THR   B N   
4394 C  CA  . THR   B 33  ? 0.2005 0.1479 0.1692 -0.0362 -0.0498 0.0285  33  THR   B CA  
4395 C  C   . THR   B 33  ? 0.2039 0.1340 0.1792 -0.0320 -0.0515 0.0174  33  THR   B C   
4396 O  O   . THR   B 33  ? 0.2306 0.1374 0.1814 -0.0401 -0.0555 0.0201  33  THR   B O   
4397 C  CB  . THR   B 33  ? 0.2082 0.1616 0.1803 -0.0170 -0.0570 0.0267  33  THR   B CB  
4398 O  OG1 . THR   B 33  ? 0.1981 0.1639 0.1857 -0.0149 -0.0543 0.0355  33  THR   B OG1 
4399 C  CG2 . THR   B 33  ? 0.2283 0.1642 0.1994 -0.0121 -0.0505 0.0244  33  THR   B CG2 
4407 N  N   . VAL   B 34  ? 0.1937 0.1307 0.1620 -0.0289 -0.0446 0.0148  34  VAL   B N   
4408 C  CA  . VAL   B 34  ? 0.1773 0.1338 0.1516 -0.0224 -0.0369 0.0050  34  VAL   B CA  
4409 C  C   . VAL   B 34  ? 0.1623 0.1299 0.1426 -0.0267 -0.0227 0.0074  34  VAL   B C   
4410 O  O   . VAL   B 34  ? 0.1756 0.1301 0.1508 -0.0261 -0.0374 0.0044  34  VAL   B O   
4411 C  CB  . VAL   B 34  ? 0.1804 0.1455 0.1787 -0.0082 -0.0336 0.0021  34  VAL   B CB  
4412 C  CG1 . VAL   B 34  ? 0.1782 0.1595 0.1896 -0.0083 -0.0183 0.0016  34  VAL   B CG1 
4413 C  CG2 . VAL   B 34  ? 0.1881 0.1452 0.1967 -0.0100 -0.0294 0.0023  34  VAL   B CG2 
4423 N  N   . VAL   B 35  ? 0.1507 0.1279 0.1332 -0.0198 -0.0183 0.0099  35  VAL   B N   
4424 C  CA  . VAL   B 35  ? 0.1440 0.1262 0.1348 -0.0202 -0.0080 0.0063  35  VAL   B CA  
4425 C  C   . VAL   B 35  ? 0.1390 0.1211 0.1403 -0.0150 -0.0114 0.0068  35  VAL   B C   
4426 O  O   . VAL   B 35  ? 0.1442 0.1254 0.1464 -0.0211 -0.0056 -0.0036 35  VAL   B O   
4427 C  CB  . VAL   B 35  ? 0.1432 0.1474 0.1514 -0.0206 -0.0052 0.0027  35  VAL   B CB  
4428 C  CG1 . VAL   B 35  ? 0.1394 0.1564 0.1586 -0.0227 -0.0021 0.0105  35  VAL   B CG1 
4429 C  CG2 . VAL   B 35  ? 0.1481 0.1433 0.1605 -0.0107 0.0005  0.0011  35  VAL   B CG2 
4439 N  N   . VAL   B 36  ? 0.1387 0.1233 0.1396 -0.0170 -0.0130 0.0066  36  VAL   B N   
4440 C  CA  . VAL   B 36  ? 0.1336 0.1184 0.1363 -0.0141 -0.0077 0.0061  36  VAL   B CA  
4441 C  C   . VAL   B 36  ? 0.1324 0.1184 0.1341 -0.0150 -0.0084 0.0007  36  VAL   B C   
4442 O  O   . VAL   B 36  ? 0.1385 0.1296 0.1526 -0.0096 -0.0071 -0.0044 36  VAL   B O   
4443 C  CB  . VAL   B 36  ? 0.1342 0.1247 0.1391 -0.0136 -0.0097 0.0054  36  VAL   B CB  
4444 C  CG1 . VAL   B 36  ? 0.1337 0.1369 0.1609 -0.0179 -0.0120 0.0025  36  VAL   B CG1 
4445 C  CG2 . VAL   B 36  ? 0.1457 0.1300 0.1490 -0.0157 -0.0135 0.0030  36  VAL   B CG2 
4455 N  N   . ASN   B 37  ? 0.1312 0.1277 0.1329 -0.0034 -0.0115 0.0039  37  ASN   B N   
4456 C  CA  . ASN   B 37  ? 0.1320 0.1305 0.1422 0.0011  -0.0105 0.0047  37  ASN   B CA  
4457 C  C   . ASN   B 37  ? 0.1322 0.1313 0.1437 0.0031  -0.0097 -0.0022 37  ASN   B C   
4458 O  O   . ASN   B 37  ? 0.1429 0.1389 0.1437 -0.0009 -0.0061 0.0051  37  ASN   B O   
4459 C  CB  . ASN   B 37  ? 0.1364 0.1320 0.1357 -0.0030 -0.0168 0.0027  37  ASN   B CB  
4460 C  CG  . ASN   B 37  ? 0.1434 0.1323 0.1522 -0.0063 -0.0088 0.0043  37  ASN   B CG  
4461 O  OD1 . ASN   B 37  ? 0.1494 0.1372 0.1571 0.0042  -0.0222 0.0048  37  ASN   B OD1 
4462 N  ND2 . ASN   B 37  ? 0.1496 0.1322 0.1468 -0.0020 -0.0182 0.0069  37  ASN   B ND2 
4469 N  N   . ALA   B 38  ? 0.1428 0.1267 0.1421 0.0035  -0.0032 0.0044  38  ALA   B N   
4470 C  CA  . ALA   B 38  ? 0.1547 0.1322 0.1461 -0.0037 -0.0026 0.0121  38  ALA   B CA  
4471 C  C   . ALA   B 38  ? 0.1550 0.1289 0.1404 -0.0018 -0.0021 0.0158  38  ALA   B C   
4472 O  O   . ALA   B 38  ? 0.1631 0.1404 0.1599 0.0057  -0.0078 0.0111  38  ALA   B O   
4473 C  CB  . ALA   B 38  ? 0.1752 0.1395 0.1568 -0.0063 0.0092  0.0061  38  ALA   B CB  
4479 N  N   . ALA   B 39  ? 0.1528 0.1291 0.1381 0.0040  -0.0057 0.0089  39  ALA   B N   
4480 C  CA  . ALA   B 39  ? 0.1571 0.1382 0.1368 0.0041  -0.0105 0.0037  39  ALA   B CA  
4481 C  C   . ALA   B 39  ? 0.1622 0.1449 0.1264 0.0079  -0.0067 0.0011  39  ALA   B C   
4482 O  O   . ALA   B 39  ? 0.1639 0.1538 0.1540 -0.0018 -0.0033 0.0055  39  ALA   B O   
4483 C  CB  . ALA   B 39  ? 0.1559 0.1418 0.1601 -0.0079 -0.0061 -0.0044 39  ALA   B CB  
4489 N  N   . ASN   B 40  ? 0.1703 0.1669 0.1293 -0.0030 -0.0058 -0.0079 40  ASN   B N   
4490 C  CA  . ASN   B 40  ? 0.1783 0.1737 0.1431 -0.0032 -0.0112 -0.0068 40  ASN   B CA  
4491 C  C   . ASN   B 40  ? 0.1768 0.1701 0.1290 0.0054  -0.0131 -0.0033 40  ASN   B C   
4492 O  O   . ASN   B 40  ? 0.1711 0.1625 0.1433 0.0106  -0.0130 -0.0040 40  ASN   B O   
4493 C  CB  . ASN   B 40  ? 0.1885 0.1718 0.1608 0.0090  -0.0143 0.0022  40  ASN   B CB  
4494 C  CG  . ASN   B 40  ? 0.1909 0.1772 0.1963 0.0045  -0.0213 0.0132  40  ASN   B CG  
4495 O  OD1 . ASN   B 40  ? 0.1855 0.1767 0.2723 0.0038  -0.0338 0.0170  40  ASN   B OD1 
4496 N  ND2 . ASN   B 40  ? 0.1925 0.1780 0.1900 -0.0003 -0.0162 0.0134  40  ASN   B ND2 
4503 N  N   . VAL   B 41  ? 0.1877 0.1753 0.1348 0.0100  -0.0018 -0.0054 41  VAL   B N   
4504 C  CA  . VAL   B 41  ? 0.1928 0.1843 0.1323 0.0067  -0.0050 -0.0176 41  VAL   B CA  
4505 C  C   . VAL   B 41  ? 0.1927 0.1846 0.1356 0.0110  -0.0141 -0.0134 41  VAL   B C   
4506 O  O   . VAL   B 41  ? 0.1924 0.1798 0.1531 0.0111  -0.0150 -0.0137 41  VAL   B O   
4507 C  CB  . VAL   B 41  ? 0.2074 0.2032 0.1581 -0.0030 0.0107  -0.0284 41  VAL   B CB  
4508 C  CG1 . VAL   B 41  ? 0.2102 0.2081 0.1715 -0.0061 0.0170  -0.0210 41  VAL   B CG1 
4509 C  CG2 . VAL   B 41  ? 0.2179 0.2198 0.1746 -0.0146 0.0102  -0.0195 41  VAL   B CG2 
4519 N  N   . TYR   B 42  ? 0.1967 0.1876 0.1414 0.0090  -0.0234 0.0040  42  TYR   B N   
4520 C  CA  . TYR   B 42  ? 0.1979 0.1917 0.1534 0.0143  -0.0328 -0.0120 42  TYR   B CA  
4521 C  C   . TYR   B 42  ? 0.1831 0.1748 0.1599 0.0163  -0.0287 -0.0080 42  TYR   B C   
4522 O  O   . TYR   B 42  ? 0.1886 0.1844 0.1883 0.0096  -0.0334 -0.0187 42  TYR   B O   
4523 C  CB  . TYR   B 42  ? 0.2222 0.2207 0.1739 0.0124  -0.0326 0.0007  42  TYR   B CB  
4524 C  CG  . TYR   B 42  ? 0.2229 0.2413 0.1789 -0.0014 -0.0228 0.0124  42  TYR   B CG  
4525 C  CD1 . TYR   B 42  ? 0.2191 0.2410 0.1573 -0.0043 -0.0116 0.0124  42  TYR   B CD1 
4526 C  CD2 . TYR   B 42  ? 0.2385 0.2601 0.2175 0.0012  -0.0046 0.0212  42  TYR   B CD2 
4527 C  CE1 . TYR   B 42  ? 0.2337 0.2588 0.1725 0.0003  -0.0055 0.0171  42  TYR   B CE1 
4528 C  CE2 . TYR   B 42  ? 0.2459 0.2731 0.2153 0.0058  0.0139  0.0376  42  TYR   B CE2 
4529 C  CZ  . TYR   B 42  ? 0.2528 0.2822 0.2078 0.0183  0.0182  0.0271  42  TYR   B CZ  
4530 O  OH  . TYR   B 42  ? 0.2841 0.3096 0.2401 0.0392  0.0323  0.0366  42  TYR   B OH  
4540 N  N   . LEU   B 43  ? 0.1736 0.1588 0.1528 0.0073  -0.0174 -0.0129 43  LEU   B N   
4541 C  CA  . LEU   B 43  ? 0.1726 0.1599 0.1384 -0.0004 -0.0173 -0.0053 43  LEU   B CA  
4542 C  C   . LEU   B 43  ? 0.1807 0.1622 0.1383 0.0025  -0.0153 0.0032  43  LEU   B C   
4543 O  O   . LEU   B 43  ? 0.1726 0.1642 0.1742 0.0039  -0.0290 0.0043  43  LEU   B O   
4544 C  CB  . LEU   B 43  ? 0.1737 0.1511 0.1556 0.0016  -0.0266 -0.0058 43  LEU   B CB  
4545 C  CG  . LEU   B 43  ? 0.1730 0.1470 0.1709 0.0004  -0.0292 -0.0049 43  LEU   B CG  
4546 C  CD1 . LEU   B 43  ? 0.1826 0.1483 0.1925 0.0018  -0.0463 -0.0097 43  LEU   B CD1 
4547 C  CD2 . LEU   B 43  ? 0.1728 0.1527 0.1776 -0.0063 -0.0300 -0.0053 43  LEU   B CD2 
4559 N  N   . LYS   B 44  ? 0.1751 0.1601 0.1462 0.0047  -0.0141 0.0007  44  LYS   B N   
4560 C  CA  . LYS   B 44  ? 0.1880 0.1703 0.1487 0.0031  -0.0170 0.0101  44  LYS   B CA  
4561 C  C   . LYS   B 44  ? 0.1787 0.1654 0.1476 0.0056  -0.0166 0.0043  44  LYS   B C   
4562 O  O   . LYS   B 44  ? 0.1954 0.1652 0.1771 -0.0021 -0.0090 0.0040  44  LYS   B O   
4563 C  CB  . LYS   B 44  ? 0.2195 0.1915 0.1676 0.0078  -0.0278 0.0037  44  LYS   B CB  
4564 C  CG  . LYS   B 44  ? 0.2607 0.2195 0.2108 0.0067  -0.0581 0.0093  44  LYS   B CG  
4565 C  CD  . LYS   B 44  ? 0.2954 0.2398 0.2666 -0.0053 -0.0721 0.0114  44  LYS   B CD  
4566 C  CE  . LYS   B 44  ? 0.3266 0.2651 0.3205 -0.0094 -0.0765 0.0231  44  LYS   B CE  
4567 N  NZ  . LYS   B 44  ? 0.3379 0.2702 0.3441 -0.0084 -0.0869 0.0423  44  LYS   B NZ  
4581 N  N   . HIS   B 45  ? 0.1691 0.1620 0.1524 -0.0009 -0.0153 0.0113  45  HIS   B N   
4582 C  CA  . HIS   B 45  ? 0.1713 0.1568 0.1583 0.0054  -0.0132 -0.0021 45  HIS   B CA  
4583 C  C   . HIS   B 45  ? 0.1954 0.1708 0.1919 0.0130  -0.0255 -0.0019 45  HIS   B C   
4584 O  O   . HIS   B 45  ? 0.2064 0.2036 0.2288 0.0413  -0.0035 0.0023  45  HIS   B O   
4585 C  CB  . HIS   B 45  ? 0.1651 0.1602 0.1645 0.0018  -0.0119 -0.0053 45  HIS   B CB  
4586 C  CG  . HIS   B 45  ? 0.1636 0.1574 0.1635 -0.0073 -0.0141 0.0016  45  HIS   B CG  
4587 N  ND1 . HIS   B 45  ? 0.1679 0.1511 0.1601 -0.0052 -0.0166 -0.0051 45  HIS   B ND1 
4588 C  CD2 . HIS   B 45  ? 0.1713 0.1623 0.1701 -0.0105 -0.0224 0.0007  45  HIS   B CD2 
4589 C  CE1 . HIS   B 45  ? 0.1750 0.1461 0.1513 -0.0062 -0.0248 -0.0077 45  HIS   B CE1 
4590 N  NE2 . HIS   B 45  ? 0.1787 0.1525 0.1601 -0.0055 -0.0234 -0.0077 45  HIS   B NE2 
4598 N  N   A GLY   B 46  ? 0.2078 0.1730 0.2213 0.0113  -0.0398 0.0103  46  GLY   B N   
4599 N  N   B GLY   B 46  ? 0.2062 0.1773 0.2116 0.0113  -0.0376 0.0134  46  GLY   B N   
4600 C  CA  A GLY   B 46  ? 0.2174 0.1861 0.2604 0.0128  -0.0487 0.0129  46  GLY   B CA  
4601 C  CA  B GLY   B 46  ? 0.2151 0.1913 0.2398 0.0121  -0.0466 0.0221  46  GLY   B CA  
4602 C  C   A GLY   B 46  ? 0.2161 0.1993 0.2977 0.0255  -0.0471 0.0074  46  GLY   B C   
4603 C  C   B GLY   B 46  ? 0.2168 0.2062 0.2691 0.0211  -0.0462 0.0267  46  GLY   B C   
4604 O  O   A GLY   B 46  ? 0.2254 0.2084 0.3677 0.0300  -0.0333 -0.0186 46  GLY   B O   
4605 O  O   B GLY   B 46  ? 0.2274 0.2201 0.2949 0.0205  -0.0419 0.0374  46  GLY   B O   
4612 N  N   . GLY   B 47  ? 0.2113 0.2083 0.2720 0.0146  -0.0294 0.0102  47  GLY   B N   
4613 C  CA  . GLY   B 47  ? 0.2018 0.1824 0.2403 0.0053  -0.0235 0.0086  47  GLY   B CA  
4614 C  C   . GLY   B 47  ? 0.1788 0.1565 0.1996 0.0001  -0.0047 0.0166  47  GLY   B C   
4615 O  O   . GLY   B 47  ? 0.1901 0.1432 0.2026 0.0021  -0.0108 0.0147  47  GLY   B O   
4620 N  N   . GLY   B 48  ? 0.1601 0.1495 0.1994 0.0033  -0.0168 0.0180  48  GLY   B N   
4621 C  CA  . GLY   B 48  ? 0.1572 0.1446 0.1911 -0.0027 -0.0078 0.0117  48  GLY   B CA  
4622 C  C   . GLY   B 48  ? 0.1581 0.1409 0.1788 -0.0012 -0.0005 0.0116  48  GLY   B C   
4623 O  O   . GLY   B 48  ? 0.1513 0.1434 0.2061 0.0017  -0.0095 0.0101  48  GLY   B O   
4627 N  N   . VAL   B 49  ? 0.1593 0.1465 0.1670 0.0072  -0.0044 0.0128  49  VAL   B N   
4628 C  CA  . VAL   B 49  ? 0.1638 0.1557 0.1610 0.0099  -0.0146 -0.0100 49  VAL   B CA  
4629 C  C   . VAL   B 49  ? 0.1511 0.1499 0.1496 0.0102  -0.0142 -0.0014 49  VAL   B C   
4630 O  O   . VAL   B 49  ? 0.1558 0.1533 0.1670 0.0041  -0.0066 0.0052  49  VAL   B O   
4631 C  CB  . VAL   B 49  ? 0.1655 0.1731 0.1846 0.0006  -0.0262 0.0023  49  VAL   B CB  
4632 C  CG1 . VAL   B 49  ? 0.1703 0.1802 0.1768 0.0028  -0.0311 0.0068  49  VAL   B CG1 
4633 C  CG2 . VAL   B 49  ? 0.1799 0.1827 0.2069 -0.0083 -0.0424 -0.0049 49  VAL   B CG2 
4643 N  N   . ALA   B 50  ? 0.1445 0.1433 0.1591 0.0035  -0.0127 0.0051  50  ALA   B N   
4644 C  CA  . ALA   B 50  ? 0.1502 0.1366 0.1508 0.0058  -0.0113 0.0054  50  ALA   B CA  
4645 C  C   . ALA   B 50  ? 0.1571 0.1415 0.1518 0.0037  0.0002  0.0041  50  ALA   B C   
4646 O  O   . ALA   B 50  ? 0.1573 0.1411 0.1558 0.0015  -0.0069 0.0049  50  ALA   B O   
4647 C  CB  . ALA   B 50  ? 0.1539 0.1415 0.1630 -0.0017 -0.0122 0.0101  50  ALA   B CB  
4653 N  N   . GLY   B 51  ? 0.1514 0.1472 0.1658 0.0078  -0.0125 0.0113  51  GLY   B N   
4654 C  CA  . GLY   B 51  ? 0.1484 0.1585 0.1868 0.0155  -0.0188 0.0109  51  GLY   B CA  
4655 C  C   . GLY   B 51  ? 0.1511 0.1554 0.1793 0.0180  -0.0156 0.0152  51  GLY   B C   
4656 O  O   . GLY   B 51  ? 0.1540 0.1623 0.2000 0.0065  -0.0166 0.0016  51  GLY   B O   
4660 N  N   . ALA   B 52  ? 0.1501 0.1500 0.1753 0.0135  -0.0077 0.0164  52  ALA   B N   
4661 C  CA  . ALA   B 52  ? 0.1574 0.1554 0.1777 0.0135  -0.0014 0.0030  52  ALA   B CA  
4662 C  C   . ALA   B 52  ? 0.1474 0.1528 0.1664 0.0070  -0.0040 0.0037  52  ALA   B C   
4663 O  O   . ALA   B 52  ? 0.1440 0.1595 0.1931 0.0107  -0.0011 0.0023  52  ALA   B O   
4664 C  CB  . ALA   B 52  ? 0.1726 0.1648 0.1772 0.0036  0.0009  0.0018  52  ALA   B CB  
4670 N  N   . LEU   B 53  ? 0.1427 0.1462 0.1590 0.0167  0.0012  0.0038  53  LEU   B N   
4671 C  CA  . LEU   B 53  ? 0.1435 0.1571 0.1553 0.0112  -0.0092 0.0044  53  LEU   B CA  
4672 C  C   . LEU   B 53  ? 0.1496 0.1525 0.1499 0.0069  -0.0019 0.0122  53  LEU   B C   
4673 O  O   . LEU   B 53  ? 0.1528 0.1533 0.1642 -0.0033 -0.0026 0.0182  53  LEU   B O   
4674 C  CB  . LEU   B 53  ? 0.1441 0.1645 0.1710 0.0083  -0.0064 0.0135  53  LEU   B CB  
4675 C  CG  . LEU   B 53  ? 0.1429 0.1769 0.1739 0.0010  -0.0073 0.0206  53  LEU   B CG  
4676 C  CD1 . LEU   B 53  ? 0.1470 0.1979 0.2015 0.0071  -0.0115 0.0099  53  LEU   B CD1 
4677 C  CD2 . LEU   B 53  ? 0.1599 0.2020 0.2036 -0.0120 -0.0112 -0.0078 53  LEU   B CD2 
4689 N  N   . ASN   B 54  ? 0.1488 0.1434 0.1509 0.0055  -0.0079 0.0104  54  ASN   B N   
4690 C  CA  . ASN   B 54  ? 0.1514 0.1506 0.1617 0.0021  -0.0139 0.0018  54  ASN   B CA  
4691 C  C   . ASN   B 54  ? 0.1488 0.1573 0.1839 -0.0011 -0.0045 0.0042  54  ASN   B C   
4692 O  O   . ASN   B 54  ? 0.1484 0.1640 0.1923 -0.0056 -0.0017 0.0072  54  ASN   B O   
4693 C  CB  . ASN   B 54  ? 0.1581 0.1677 0.1655 0.0057  -0.0112 0.0046  54  ASN   B CB  
4694 C  CG  . ASN   B 54  ? 0.1551 0.1746 0.1692 0.0025  -0.0152 0.0043  54  ASN   B CG  
4695 O  OD1 . ASN   B 54  ? 0.1536 0.1705 0.1850 -0.0007 -0.0200 -0.0042 54  ASN   B OD1 
4696 N  ND2 . ASN   B 54  ? 0.1658 0.1967 0.1986 -0.0074 -0.0340 0.0155  54  ASN   B ND2 
4703 N  N   . LYS   B 55  ? 0.1466 0.1609 0.1976 0.0064  -0.0053 0.0078  55  LYS   B N   
4704 C  CA  . LYS   B 55  ? 0.1512 0.1774 0.2173 0.0134  -0.0133 0.0103  55  LYS   B CA  
4705 C  C   . LYS   B 55  ? 0.1450 0.1728 0.2101 0.0135  -0.0007 -0.0037 55  LYS   B C   
4706 O  O   . LYS   B 55  ? 0.1381 0.1871 0.2373 0.0106  -0.0010 -0.0033 55  LYS   B O   
4707 C  CB  . LYS   B 55  ? 0.1636 0.1966 0.2624 0.0277  0.0018  0.0308  55  LYS   B CB  
4708 C  CG  . LYS   B 55  ? 0.2016 0.2214 0.3532 0.0343  0.0240  0.0410  55  LYS   B CG  
4709 C  CD  . LYS   B 55  ? 0.2383 0.2456 0.4276 0.0454  0.0362  0.0562  55  LYS   B CD  
4710 C  CE  . LYS   B 55  ? 0.2635 0.2706 0.4973 0.0464  0.0447  0.0587  55  LYS   B CE  
4711 N  NZ  . LYS   B 55  ? 0.2661 0.2868 0.5337 0.0492  0.0280  0.0702  55  LYS   B NZ  
4725 N  N   . ALA   B 56  ? 0.1482 0.1746 0.1896 0.0035  -0.0010 -0.0026 56  ALA   B N   
4726 C  CA  . ALA   B 56  ? 0.1597 0.1966 0.1854 0.0055  0.0021  -0.0013 56  ALA   B CA  
4727 C  C   . ALA   B 56  ? 0.1615 0.1947 0.1788 0.0077  0.0113  0.0094  56  ALA   B C   
4728 O  O   . ALA   B 56  ? 0.1728 0.2031 0.1956 0.0084  0.0209  0.0101  56  ALA   B O   
4729 C  CB  . ALA   B 56  ? 0.1664 0.2134 0.1870 -0.0053 0.0034  0.0014  56  ALA   B CB  
4735 N  N   . THR   B 57  ? 0.1602 0.1820 0.1847 0.0029  0.0150  0.0113  57  THR   B N   
4736 C  CA  . THR   B 57  ? 0.1596 0.1806 0.1934 0.0012  0.0086  0.0126  57  THR   B CA  
4737 C  C   . THR   B 57  ? 0.1601 0.1932 0.2081 -0.0057 0.0084  0.0131  57  THR   B C   
4738 O  O   . THR   B 57  ? 0.1682 0.1934 0.2174 -0.0225 0.0127  0.0066  57  THR   B O   
4739 C  CB  . THR   B 57  ? 0.1649 0.1649 0.1793 0.0013  0.0065  0.0160  57  THR   B CB  
4740 O  OG1 . THR   B 57  ? 0.1624 0.1570 0.1928 -0.0037 0.0041  0.0089  57  THR   B OG1 
4741 C  CG2 . THR   B 57  ? 0.1639 0.1708 0.1770 -0.0007 0.0014  0.0104  57  THR   B CG2 
4749 N  N   . ASN   B 58  ? 0.1449 0.2139 0.2247 -0.0159 -0.0024 0.0036  58  ASN   B N   
4750 C  CA  . ASN   B 58  ? 0.1663 0.2555 0.2742 -0.0322 0.0121  0.0107  58  ASN   B CA  
4751 C  C   . ASN   B 58  ? 0.1505 0.2297 0.2412 -0.0195 -0.0180 0.0056  58  ASN   B C   
4752 O  O   . ASN   B 58  ? 0.1617 0.2376 0.2446 -0.0235 -0.0142 -0.0107 58  ASN   B O   
4753 C  CB  . ASN   B 58  ? 0.2748 0.3415 0.4147 -0.0503 0.0495  0.0261  58  ASN   B CB  
4754 C  CG  . ASN   B 58  ? 0.3968 0.4279 0.5624 -0.0538 0.0720  0.0416  58  ASN   B CG  
4755 O  OD1 . ASN   B 58  ? 0.4211 0.4461 0.6153 -0.0557 0.0789  0.0441  58  ASN   B OD1 
4756 N  ND2 . ASN   B 58  ? 0.4737 0.4737 0.6112 -0.0550 0.0835  0.0461  58  ASN   B ND2 
4763 N  N   . ASN   B 59  ? 0.1512 0.2096 0.2311 -0.0136 -0.0179 0.0153  59  ASN   B N   
4764 C  CA  . ASN   B 59  ? 0.1564 0.2090 0.2159 -0.0160 -0.0249 0.0239  59  ASN   B CA  
4765 C  C   . ASN   B 59  ? 0.1497 0.1989 0.2013 -0.0175 -0.0186 0.0162  59  ASN   B C   
4766 O  O   . ASN   B 59  ? 0.1521 0.2016 0.2082 -0.0184 -0.0184 0.0037  59  ASN   B O   
4767 C  CB  . ASN   B 59  ? 0.1645 0.2278 0.2225 -0.0136 -0.0330 0.0186  59  ASN   B CB  
4768 C  CG  . ASN   B 59  ? 0.1722 0.2484 0.2433 -0.0081 -0.0460 0.0078  59  ASN   B CG  
4769 O  OD1 . ASN   B 59  ? 0.1782 0.2555 0.2377 -0.0036 -0.0375 0.0231  59  ASN   B OD1 
4770 N  ND2 . ASN   B 59  ? 0.1784 0.2586 0.2559 -0.0098 -0.0508 0.0052  59  ASN   B ND2 
4777 N  N   . ALA   B 60  ? 0.1493 0.1915 0.1984 -0.0161 -0.0118 0.0118  60  ALA   B N   
4778 C  CA  . ALA   B 60  ? 0.1637 0.1781 0.2029 -0.0197 -0.0155 0.0142  60  ALA   B CA  
4779 C  C   . ALA   B 60  ? 0.1643 0.1647 0.1798 -0.0165 -0.0152 0.0036  60  ALA   B C   
4780 O  O   . ALA   B 60  ? 0.1670 0.1615 0.1896 -0.0208 -0.0080 -0.0075 60  ALA   B O   
4781 C  CB  . ALA   B 60  ? 0.1746 0.1764 0.2278 -0.0143 -0.0120 0.0120  60  ALA   B CB  
4787 N  N   . MET   B 61  ? 0.1555 0.1548 0.1726 -0.0144 -0.0093 0.0033  61  MET   B N   
4788 C  CA  . MET   B 61  ? 0.1505 0.1503 0.1681 -0.0082 -0.0160 0.0050  61  MET   B CA  
4789 C  C   . MET   B 61  ? 0.1598 0.1498 0.1668 -0.0112 -0.0197 0.0030  61  MET   B C   
4790 O  O   . MET   B 61  ? 0.1630 0.1481 0.1640 -0.0044 -0.0124 -0.0109 61  MET   B O   
4791 C  CB  . MET   B 61  ? 0.1494 0.1571 0.1701 -0.0045 -0.0203 0.0020  61  MET   B CB  
4792 C  CG  . MET   B 61  ? 0.1467 0.1556 0.1693 -0.0038 -0.0114 0.0040  61  MET   B CG  
4793 S  SD  . MET   B 61  ? 0.1483 0.1556 0.1793 -0.0040 -0.0111 -0.0094 61  MET   B SD  
4794 C  CE  . MET   B 61  ? 0.1560 0.1729 0.1930 0.0056  -0.0167 -0.0255 61  MET   B CE  
4804 N  N   . GLN   B 62  ? 0.1532 0.1582 0.1677 -0.0065 -0.0239 0.0103  62  GLN   B N   
4805 C  CA  . GLN   B 62  ? 0.1594 0.1572 0.1754 -0.0012 -0.0253 -0.0025 62  GLN   B CA  
4806 C  C   . GLN   B 62  ? 0.1559 0.1670 0.1764 -0.0074 -0.0330 0.0012  62  GLN   B C   
4807 O  O   . GLN   B 62  ? 0.1691 0.1695 0.1776 -0.0039 -0.0369 -0.0073 62  GLN   B O   
4808 C  CB  . GLN   B 62  ? 0.1589 0.1683 0.1811 -0.0014 -0.0210 0.0071  62  GLN   B CB  
4809 C  CG  . GLN   B 62  ? 0.1648 0.1712 0.1773 0.0010  -0.0278 0.0034  62  GLN   B CG  
4810 C  CD  . GLN   B 62  ? 0.1658 0.1654 0.1604 0.0028  -0.0311 0.0086  62  GLN   B CD  
4811 O  OE1 . GLN   B 62  ? 0.1642 0.1645 0.1829 -0.0012 -0.0284 -0.0037 62  GLN   B OE1 
4812 N  NE2 . GLN   B 62  ? 0.1654 0.1682 0.1747 -0.0003 -0.0245 -0.0056 62  GLN   B NE2 
4821 N  N   . VAL   B 63  ? 0.1597 0.1734 0.1956 -0.0127 -0.0268 -0.0057 63  VAL   B N   
4822 C  CA  . VAL   B 63  ? 0.1759 0.1721 0.2189 -0.0158 -0.0389 -0.0060 63  VAL   B CA  
4823 C  C   . VAL   B 63  ? 0.1741 0.1596 0.1981 -0.0227 -0.0423 -0.0110 63  VAL   B C   
4824 O  O   . VAL   B 63  ? 0.1891 0.1586 0.2100 -0.0203 -0.0546 -0.0114 63  VAL   B O   
4825 C  CB  . VAL   B 63  ? 0.1752 0.1870 0.2554 -0.0207 -0.0383 -0.0110 63  VAL   B CB  
4826 C  CG1 . VAL   B 63  ? 0.1841 0.1879 0.2672 -0.0329 -0.0288 -0.0160 63  VAL   B CG1 
4827 C  CG2 . VAL   B 63  ? 0.1643 0.1989 0.2651 -0.0163 -0.0403 -0.0056 63  VAL   B CG2 
4837 N  N   . GLU   B 64  ? 0.1697 0.1526 0.1911 -0.0160 -0.0311 -0.0088 64  GLU   B N   
4838 C  CA  . GLU   B 64  ? 0.1736 0.1478 0.1841 -0.0122 -0.0350 -0.0052 64  GLU   B CA  
4839 C  C   . GLU   B 64  ? 0.1673 0.1456 0.1759 -0.0058 -0.0314 -0.0138 64  GLU   B C   
4840 O  O   . GLU   B 64  ? 0.1761 0.1549 0.1824 -0.0092 -0.0333 -0.0167 64  GLU   B O   
4841 C  CB  . GLU   B 64  ? 0.1726 0.1546 0.1840 -0.0154 -0.0257 0.0012  64  GLU   B CB  
4842 C  CG  . GLU   B 64  ? 0.1796 0.1619 0.1747 -0.0230 -0.0302 -0.0102 64  GLU   B CG  
4843 C  CD  . GLU   B 64  ? 0.1824 0.1732 0.1872 -0.0292 -0.0309 -0.0049 64  GLU   B CD  
4844 O  OE1 . GLU   B 64  ? 0.1807 0.1874 0.2032 -0.0293 -0.0301 -0.0260 64  GLU   B OE1 
4845 O  OE2 . GLU   B 64  ? 0.1946 0.1798 0.1860 -0.0347 -0.0495 -0.0073 64  GLU   B OE2 
4852 N  N   . SER   B 65  ? 0.1653 0.1435 0.1689 -0.0072 -0.0234 -0.0136 65  SER   B N   
4853 C  CA  . SER   B 65  ? 0.1678 0.1456 0.1686 -0.0006 -0.0220 -0.0114 65  SER   B CA  
4854 C  C   . SER   B 65  ? 0.1705 0.1530 0.1685 -0.0033 -0.0310 -0.0171 65  SER   B C   
4855 O  O   . SER   B 65  ? 0.1732 0.1579 0.1693 -0.0027 -0.0277 -0.0221 65  SER   B O   
4856 C  CB  . SER   B 65  ? 0.1713 0.1496 0.1679 -0.0099 -0.0258 -0.0057 65  SER   B CB  
4857 O  OG  . SER   B 65  ? 0.1720 0.1469 0.1751 -0.0104 -0.0217 -0.0163 65  SER   B OG  
4863 N  N   . ASP   B 66  ? 0.1756 0.1576 0.1757 -0.0041 -0.0333 -0.0137 66  ASP   B N   
4864 C  CA  . ASP   B 66  ? 0.1814 0.1645 0.1608 -0.0023 -0.0337 -0.0115 66  ASP   B CA  
4865 C  C   . ASP   B 66  ? 0.1899 0.1672 0.1584 -0.0039 -0.0293 -0.0118 66  ASP   B C   
4866 O  O   . ASP   B 66  ? 0.1897 0.1768 0.1636 0.0038  -0.0292 -0.0156 66  ASP   B O   
4867 C  CB  . ASP   B 66  ? 0.1999 0.1781 0.1812 0.0046  -0.0473 -0.0108 66  ASP   B CB  
4868 C  CG  . ASP   B 66  ? 0.2328 0.1990 0.2095 0.0126  -0.0664 -0.0020 66  ASP   B CG  
4869 O  OD1 . ASP   B 66  ? 0.2561 0.1918 0.2222 0.0086  -0.0624 0.0046  66  ASP   B OD1 
4870 O  OD2 . ASP   B 66  ? 0.2505 0.2164 0.2653 0.0285  -0.0624 0.0008  66  ASP   B OD2 
4875 N  N   . ASP   B 67  ? 0.1864 0.1587 0.1528 -0.0091 -0.0330 -0.0151 67  ASP   B N   
4876 C  CA  . ASP   B 67  ? 0.2009 0.1534 0.1724 -0.0067 -0.0329 -0.0082 67  ASP   B CA  
4877 C  C   . ASP   B 67  ? 0.1948 0.1575 0.1843 0.0005  -0.0333 -0.0143 67  ASP   B C   
4878 O  O   . ASP   B 67  ? 0.1931 0.1685 0.1937 0.0014  -0.0250 -0.0211 67  ASP   B O   
4879 C  CB  . ASP   B 67  ? 0.2255 0.1632 0.1953 -0.0155 -0.0447 -0.0001 67  ASP   B CB  
4880 C  CG  . ASP   B 67  ? 0.2590 0.1701 0.2104 -0.0136 -0.0712 -0.0062 67  ASP   B CG  
4881 O  OD1 . ASP   B 67  ? 0.2837 0.1728 0.2146 -0.0112 -0.0704 -0.0082 67  ASP   B OD1 
4882 O  OD2 . ASP   B 67  ? 0.2717 0.1821 0.2270 -0.0004 -0.0822 -0.0103 67  ASP   B OD2 
4887 N  N   . TYR   B 68  ? 0.1876 0.1562 0.1810 -0.0018 -0.0454 -0.0260 68  TYR   B N   
4888 C  CA  . TYR   B 68  ? 0.1891 0.1746 0.1911 0.0079  -0.0420 -0.0337 68  TYR   B CA  
4889 C  C   . TYR   B 68  ? 0.1812 0.1717 0.1849 0.0038  -0.0374 -0.0396 68  TYR   B C   
4890 O  O   . TYR   B 68  ? 0.1860 0.1848 0.1967 0.0020  -0.0317 -0.0564 68  TYR   B O   
4891 C  CB  . TYR   B 68  ? 0.1915 0.1969 0.1987 0.0143  -0.0476 -0.0428 68  TYR   B CB  
4892 C  CG  . TYR   B 68  ? 0.1993 0.2182 0.2131 0.0133  -0.0398 -0.0620 68  TYR   B CG  
4893 C  CD1 . TYR   B 68  ? 0.2025 0.2192 0.2431 -0.0072 -0.0401 -0.0682 68  TYR   B CD1 
4894 C  CD2 . TYR   B 68  ? 0.2052 0.2409 0.2337 0.0220  -0.0518 -0.0613 68  TYR   B CD2 
4895 C  CE1 . TYR   B 68  ? 0.2075 0.2346 0.2715 -0.0028 -0.0365 -0.0679 68  TYR   B CE1 
4896 C  CE2 . TYR   B 68  ? 0.2083 0.2465 0.2499 0.0163  -0.0447 -0.0772 68  TYR   B CE2 
4897 C  CZ  . TYR   B 68  ? 0.2013 0.2435 0.2654 0.0031  -0.0463 -0.0832 68  TYR   B CZ  
4898 O  OH  . TYR   B 68  ? 0.1948 0.2647 0.2922 0.0011  -0.0448 -0.0655 68  TYR   B OH  
4908 N  N   . ILE   B 69  ? 0.1802 0.1637 0.1823 0.0033  -0.0342 -0.0355 69  ILE   B N   
4909 C  CA  . ILE   B 69  ? 0.1864 0.1712 0.1905 -0.0003 -0.0279 -0.0358 69  ILE   B CA  
4910 C  C   . ILE   B 69  ? 0.1858 0.1710 0.1922 0.0092  -0.0339 -0.0287 69  ILE   B C   
4911 O  O   . ILE   B 69  ? 0.1910 0.1807 0.1909 0.0092  -0.0251 -0.0312 69  ILE   B O   
4912 C  CB  . ILE   B 69  ? 0.1938 0.1731 0.2137 -0.0034 -0.0072 -0.0301 69  ILE   B CB  
4913 C  CG1 . ILE   B 69  ? 0.1943 0.1744 0.2260 -0.0119 -0.0002 -0.0282 69  ILE   B CG1 
4914 C  CG2 . ILE   B 69  ? 0.2110 0.1811 0.2226 -0.0009 -0.0095 -0.0208 69  ILE   B CG2 
4915 C  CD1 . ILE   B 69  ? 0.1913 0.1821 0.2332 -0.0188 0.0050  -0.0300 69  ILE   B CD1 
4927 N  N   . ALA   B 70  ? 0.1795 0.1707 0.1917 0.0096  -0.0393 -0.0279 70  ALA   B N   
4928 C  CA  . ALA   B 70  ? 0.1856 0.1708 0.1770 0.0051  -0.0444 -0.0243 70  ALA   B CA  
4929 C  C   . ALA   B 70  ? 0.1948 0.1696 0.1941 0.0004  -0.0494 -0.0362 70  ALA   B C   
4930 O  O   . ALA   B 70  ? 0.2027 0.1691 0.1967 0.0036  -0.0491 -0.0329 70  ALA   B O   
4931 C  CB  . ALA   B 70  ? 0.1897 0.1847 0.1740 -0.0024 -0.0418 -0.0183 70  ALA   B CB  
4937 N  N   . THR   B 71  ? 0.1990 0.1699 0.2011 0.0070  -0.0580 -0.0398 71  THR   B N   
4938 C  CA  . THR   B 71  ? 0.2126 0.1751 0.2170 0.0112  -0.0682 -0.0397 71  THR   B CA  
4939 C  C   . THR   B 71  ? 0.2087 0.1815 0.2376 0.0278  -0.0641 -0.0529 71  THR   B C   
4940 O  O   . THR   B 71  ? 0.2153 0.1895 0.2730 0.0369  -0.0570 -0.0608 71  THR   B O   
4941 C  CB  . THR   B 71  ? 0.2378 0.1970 0.2387 0.0006  -0.0774 -0.0142 71  THR   B CB  
4942 O  OG1 . THR   B 71  ? 0.2526 0.2223 0.2683 -0.0197 -0.0788 0.0112  71  THR   B OG1 
4943 C  CG2 . THR   B 71  ? 0.2555 0.1914 0.2533 0.0063  -0.0685 -0.0005 71  THR   B CG2 
4951 N  N   . ASN   B 72  ? 0.2010 0.1852 0.2337 0.0218  -0.0667 -0.0670 72  ASN   B N   
4952 C  CA  . ASN   B 72  ? 0.2025 0.2004 0.2300 0.0203  -0.0557 -0.0706 72  ASN   B CA  
4953 C  C   . ASN   B 72  ? 0.1982 0.2159 0.2346 0.0066  -0.0358 -0.0680 72  ASN   B C   
4954 O  O   . ASN   B 72  ? 0.1991 0.2307 0.2611 0.0119  -0.0168 -0.0695 72  ASN   B O   
4955 C  CB  . ASN   B 72  ? 0.2066 0.2123 0.2356 0.0174  -0.0659 -0.0614 72  ASN   B CB  
4956 C  CG  . ASN   B 72  ? 0.2221 0.2262 0.2490 0.0301  -0.0588 -0.0432 72  ASN   B CG  
4957 O  OD1 . ASN   B 72  ? 0.2403 0.2459 0.2572 0.0172  -0.0433 -0.0429 72  ASN   B OD1 
4958 N  ND2 . ASN   B 72  ? 0.2337 0.2346 0.2856 0.0456  -0.0562 -0.0132 72  ASN   B ND2 
4965 N  N   . GLY   B 73  ? 0.2042 0.2154 0.2159 0.0041  -0.0336 -0.0652 73  GLY   B N   
4966 C  CA  . GLY   B 73  ? 0.1977 0.2214 0.1995 0.0004  -0.0292 -0.0534 73  GLY   B CA  
4967 C  C   . GLY   B 73  ? 0.1917 0.2185 0.1656 0.0060  -0.0284 -0.0532 73  GLY   B C   
4968 O  O   . GLY   B 73  ? 0.1818 0.2018 0.1805 0.0054  -0.0218 -0.0432 73  GLY   B O   
4972 N  N   . PRO   B 74  ? 0.1913 0.2272 0.1590 0.0028  -0.0313 -0.0392 74  PRO   B N   
4973 C  CA  . PRO   B 74  ? 0.1864 0.2236 0.1419 0.0072  -0.0246 -0.0260 74  PRO   B CA  
4974 C  C   . PRO   B 74  ? 0.1757 0.2097 0.1503 0.0078  -0.0163 -0.0204 74  PRO   B C   
4975 O  O   . PRO   B 74  ? 0.1777 0.2075 0.1890 0.0110  -0.0108 -0.0284 74  PRO   B O   
4976 C  CB  . PRO   B 74  ? 0.2062 0.2404 0.1535 0.0020  -0.0159 -0.0183 74  PRO   B CB  
4977 C  CG  . PRO   B 74  ? 0.2177 0.2503 0.1759 0.0013  -0.0137 -0.0192 74  PRO   B CG  
4978 C  CD  . PRO   B 74  ? 0.2133 0.2430 0.1690 0.0034  -0.0157 -0.0306 74  PRO   B CD  
4986 N  N   . LEU   B 75  ? 0.1701 0.1962 0.1412 0.0078  -0.0182 -0.0159 75  LEU   B N   
4987 C  CA  . LEU   B 75  ? 0.1723 0.1969 0.1336 -0.0011 -0.0236 -0.0088 75  LEU   B CA  
4988 C  C   . LEU   B 75  ? 0.1739 0.2058 0.1353 0.0028  -0.0087 -0.0037 75  LEU   B C   
4989 O  O   . LEU   B 75  ? 0.1918 0.2167 0.1560 -0.0004 -0.0069 -0.0031 75  LEU   B O   
4990 C  CB  . LEU   B 75  ? 0.1879 0.2029 0.1304 -0.0119 -0.0245 0.0085  75  LEU   B CB  
4991 C  CG  . LEU   B 75  ? 0.2146 0.2140 0.1505 -0.0303 -0.0158 0.0059  75  LEU   B CG  
4992 C  CD1 . LEU   B 75  ? 0.2416 0.2249 0.1642 -0.0352 0.0049  -0.0024 75  LEU   B CD1 
4993 C  CD2 . LEU   B 75  ? 0.2435 0.2343 0.2109 -0.0237 -0.0020 0.0158  75  LEU   B CD2 
5005 N  N   . LYS   B 76  ? 0.1723 0.2236 0.1616 0.0018  -0.0045 0.0030  76  LYS   B N   
5006 C  CA  . LYS   B 76  ? 0.1912 0.2311 0.1970 -0.0080 0.0145  -0.0013 76  LYS   B CA  
5007 C  C   . LYS   B 76  ? 0.1765 0.2142 0.1653 -0.0003 0.0035  0.0159  76  LYS   B C   
5008 O  O   . LYS   B 76  ? 0.1765 0.2023 0.1678 -0.0032 -0.0051 0.0195  76  LYS   B O   
5009 C  CB  . LYS   B 76  ? 0.2080 0.2448 0.2670 -0.0142 0.0388  -0.0346 76  LYS   B CB  
5010 C  CG  . LYS   B 76  ? 0.2120 0.2662 0.3218 -0.0050 0.0335  -0.0474 76  LYS   B CG  
5011 C  CD  . LYS   B 76  ? 0.2090 0.2807 0.3675 0.0024  0.0173  -0.0658 76  LYS   B CD  
5012 C  CE  . LYS   B 76  ? 0.2152 0.3019 0.4275 0.0034  0.0010  -0.0782 76  LYS   B CE  
5013 N  NZ  . LYS   B 76  ? 0.2155 0.3097 0.4420 -0.0006 -0.0222 -0.0999 76  LYS   B NZ  
5027 N  N   . VAL   B 77  ? 0.1838 0.2217 0.1708 0.0074  0.0108  0.0226  77  VAL   B N   
5028 C  CA  . VAL   B 77  ? 0.1872 0.2086 0.1892 0.0169  0.0163  0.0408  77  VAL   B CA  
5029 C  C   . VAL   B 77  ? 0.1751 0.1934 0.1798 0.0178  0.0188  0.0369  77  VAL   B C   
5030 O  O   . VAL   B 77  ? 0.1781 0.1936 0.1816 0.0246  0.0283  0.0256  77  VAL   B O   
5031 C  CB  . VAL   B 77  ? 0.2022 0.2179 0.2184 0.0160  0.0214  0.0534  77  VAL   B CB  
5032 C  CG1 . VAL   B 77  ? 0.2090 0.2071 0.2424 0.0131  0.0277  0.0613  77  VAL   B CG1 
5033 C  CG2 . VAL   B 77  ? 0.2127 0.2371 0.2419 0.0072  0.0049  0.0581  77  VAL   B CG2 
5043 N  N   . GLY   B 78  ? 0.1723 0.1827 0.1730 0.0144  0.0157  0.0281  78  GLY   B N   
5044 C  CA  . GLY   B 78  ? 0.1665 0.1788 0.1596 0.0152  0.0177  0.0178  78  GLY   B CA  
5045 C  C   . GLY   B 78  ? 0.1610 0.1679 0.1618 0.0155  0.0147  0.0150  78  GLY   B C   
5046 O  O   . GLY   B 78  ? 0.1629 0.1662 0.1746 0.0192  0.0087  0.0192  78  GLY   B O   
5050 N  N   . GLY   B 79  ? 0.1532 0.1710 0.1658 0.0087  0.0095  0.0074  79  GLY   B N   
5051 C  CA  . GLY   B 79  ? 0.1545 0.1585 0.1739 0.0105  0.0029  0.0098  79  GLY   B CA  
5052 C  C   . GLY   B 79  ? 0.1498 0.1528 0.1591 0.0099  0.0016  0.0010  79  GLY   B C   
5053 O  O   . GLY   B 79  ? 0.1558 0.1487 0.1768 0.0099  0.0146  0.0129  79  GLY   B O   
5057 N  N   . SER   B 80  ? 0.1483 0.1489 0.1766 0.0098  0.0118  0.0057  80  SER   B N   
5058 C  CA  . SER   B 80  ? 0.1406 0.1442 0.1791 0.0067  0.0042  0.0108  80  SER   B CA  
5059 C  C   . SER   B 80  ? 0.1491 0.1424 0.1727 0.0141  -0.0097 0.0014  80  SER   B C   
5060 O  O   . SER   B 80  ? 0.1593 0.1476 0.1994 0.0122  -0.0057 -0.0014 80  SER   B O   
5061 C  CB  . SER   B 80  ? 0.1492 0.1498 0.1735 -0.0022 -0.0036 0.0044  80  SER   B CB  
5062 O  OG  . SER   B 80  ? 0.1559 0.1663 0.1846 -0.0006 -0.0088 0.0059  80  SER   B OG  
5068 N  N   . CYS   B 81  ? 0.1458 0.1298 0.1710 0.0042  -0.0126 -0.0015 81  CYS   B N   
5069 C  CA  . CYS   B 81  ? 0.1544 0.1266 0.1729 0.0056  -0.0145 0.0023  81  CYS   B CA  
5070 C  C   . CYS   B 81  ? 0.1514 0.1272 0.1556 -0.0026 -0.0154 -0.0056 81  CYS   B C   
5071 O  O   . CYS   B 81  ? 0.1715 0.1310 0.1638 0.0078  -0.0056 -0.0052 81  CYS   B O   
5072 C  CB  . CYS   B 81  ? 0.1694 0.1426 0.1699 -0.0009 -0.0179 -0.0015 81  CYS   B CB  
5073 S  SG  . CYS   B 81  ? 0.1678 0.1626 0.1650 -0.0054 -0.0261 -0.0116 81  CYS   B SG  
5079 N  N   . VAL   B 82  ? 0.1568 0.1261 0.1652 -0.0005 -0.0179 -0.0071 82  VAL   B N   
5080 C  CA  . VAL   B 82  ? 0.1613 0.1330 0.1621 -0.0085 -0.0134 0.0034  82  VAL   B CA  
5081 C  C   . VAL   B 82  ? 0.1679 0.1254 0.1704 -0.0029 -0.0124 0.0015  82  VAL   B C   
5082 O  O   . VAL   B 82  ? 0.1717 0.1247 0.1929 -0.0050 -0.0138 -0.0092 82  VAL   B O   
5083 C  CB  . VAL   B 82  ? 0.1696 0.1560 0.1706 -0.0055 -0.0160 0.0086  82  VAL   B CB  
5084 C  CG1 . VAL   B 82  ? 0.1893 0.1829 0.1761 -0.0049 -0.0135 0.0191  82  VAL   B CG1 
5085 C  CG2 . VAL   B 82  ? 0.1781 0.1619 0.1782 -0.0062 -0.0241 0.0151  82  VAL   B CG2 
5095 N  N   . LEU   B 83  ? 0.1524 0.1237 0.1680 -0.0120 -0.0216 -0.0076 83  LEU   B N   
5096 C  CA  . LEU   B 83  ? 0.1564 0.1270 0.1580 -0.0123 -0.0204 -0.0034 83  LEU   B CA  
5097 C  C   . LEU   B 83  ? 0.1539 0.1253 0.1594 -0.0190 -0.0216 0.0020  83  LEU   B C   
5098 O  O   . LEU   B 83  ? 0.1576 0.1418 0.1509 -0.0244 -0.0230 0.0070  83  LEU   B O   
5099 C  CB  . LEU   B 83  ? 0.1632 0.1380 0.1626 -0.0133 -0.0258 -0.0067 83  LEU   B CB  
5100 C  CG  . LEU   B 83  ? 0.1804 0.1621 0.1667 -0.0189 -0.0158 -0.0010 83  LEU   B CG  
5101 C  CD1 . LEU   B 83  ? 0.1914 0.1684 0.1767 -0.0170 -0.0256 -0.0024 83  LEU   B CD1 
5102 C  CD2 . LEU   B 83  ? 0.2051 0.1695 0.1793 -0.0114 -0.0183 -0.0167 83  LEU   B CD2 
5114 N  N   . SER   B 84  ? 0.1585 0.1426 0.1742 -0.0233 -0.0228 0.0063  84  SER   B N   
5115 C  CA  . SER   B 84  ? 0.1601 0.1585 0.1711 -0.0255 -0.0202 0.0191  84  SER   B CA  
5116 C  C   . SER   B 84  ? 0.1508 0.1744 0.1361 -0.0223 -0.0219 0.0260  84  SER   B C   
5117 O  O   . SER   B 84  ? 0.1533 0.1607 0.1405 -0.0205 -0.0176 0.0067  84  SER   B O   
5118 C  CB  . SER   B 84  ? 0.1823 0.1657 0.2169 -0.0289 0.0021  0.0115  84  SER   B CB  
5119 O  OG  . SER   B 84  ? 0.1836 0.1789 0.2602 -0.0335 0.0045  0.0211  84  SER   B OG  
5125 N  N   . GLY   B 85  ? 0.1544 0.1998 0.1428 -0.0279 -0.0233 0.0274  85  GLY   B N   
5126 C  CA  . GLY   B 85  ? 0.1537 0.2065 0.1639 -0.0368 -0.0175 -0.0017 85  GLY   B CA  
5127 C  C   . GLY   B 85  ? 0.1558 0.1892 0.1560 -0.0402 -0.0140 0.0048  85  GLY   B C   
5128 O  O   . GLY   B 85  ? 0.1613 0.1872 0.1596 -0.0526 0.0065  -0.0059 85  GLY   B O   
5132 N  N   . HIS   B 86  ? 0.1564 0.1728 0.1657 -0.0332 -0.0176 0.0218  86  HIS   B N   
5133 C  CA  . HIS   B 86  ? 0.1547 0.1713 0.1656 -0.0349 -0.0181 0.0254  86  HIS   B CA  
5134 C  C   . HIS   B 86  ? 0.1555 0.1833 0.1578 -0.0435 -0.0127 0.0344  86  HIS   B C   
5135 O  O   . HIS   B 86  ? 0.1692 0.1973 0.1690 -0.0350 0.0013  0.0287  86  HIS   B O   
5136 C  CB  . HIS   B 86  ? 0.1582 0.1744 0.1708 -0.0227 -0.0260 0.0163  86  HIS   B CB  
5137 C  CG  . HIS   B 86  ? 0.1654 0.1756 0.1633 -0.0145 -0.0297 0.0196  86  HIS   B CG  
5138 N  ND1 . HIS   B 86  ? 0.1776 0.1988 0.1824 -0.0234 -0.0310 0.0000  86  HIS   B ND1 
5139 C  CD2 . HIS   B 86  ? 0.1673 0.1772 0.1660 -0.0096 -0.0253 0.0171  86  HIS   B CD2 
5140 C  CE1 . HIS   B 86  ? 0.1829 0.1995 0.1733 -0.0162 -0.0233 -0.0197 86  HIS   B CE1 
5141 N  NE2 . HIS   B 86  ? 0.1746 0.1912 0.1599 -0.0009 -0.0168 0.0026  86  HIS   B NE2 
5149 N  N   . ASN   B 87  ? 0.1568 0.1894 0.1748 -0.0369 -0.0110 0.0244  87  ASN   B N   
5150 C  CA  . ASN   B 87  ? 0.1671 0.2088 0.1716 -0.0375 0.0114  0.0204  87  ASN   B CA  
5151 C  C   . ASN   B 87  ? 0.1792 0.1947 0.1550 -0.0303 0.0183  0.0147  87  ASN   B C   
5152 O  O   . ASN   B 87  ? 0.2032 0.2077 0.1847 -0.0247 0.0358  0.0154  87  ASN   B O   
5153 C  CB  . ASN   B 87  ? 0.1710 0.2443 0.1948 -0.0317 0.0128  0.0094  87  ASN   B CB  
5154 C  CG  . ASN   B 87  ? 0.1780 0.2653 0.2019 0.0009  0.0167  0.0274  87  ASN   B CG  
5155 O  OD1 . ASN   B 87  ? 0.1714 0.2476 0.1942 0.0004  0.0343  0.0456  87  ASN   B OD1 
5156 N  ND2 . ASN   B 87  ? 0.2106 0.2807 0.2408 0.0066  0.0205  0.0216  87  ASN   B ND2 
5163 N  N   . LEU   B 88  ? 0.1618 0.1770 0.1503 -0.0334 0.0146  0.0060  88  LEU   B N   
5164 C  CA  . LEU   B 88  ? 0.1754 0.1761 0.1573 -0.0329 0.0029  -0.0008 88  LEU   B CA  
5165 C  C   . LEU   B 88  ? 0.1730 0.1666 0.1531 -0.0371 -0.0057 -0.0011 88  LEU   B C   
5166 O  O   . LEU   B 88  ? 0.1960 0.1708 0.1849 -0.0225 -0.0290 -0.0069 88  LEU   B O   
5167 C  CB  . LEU   B 88  ? 0.1850 0.1835 0.1624 -0.0417 -0.0097 0.0187  88  LEU   B CB  
5168 C  CG  . LEU   B 88  ? 0.2237 0.2113 0.1881 -0.0339 -0.0309 0.0350  88  LEU   B CG  
5169 C  CD1 . LEU   B 88  ? 0.2369 0.2446 0.2007 -0.0423 -0.0239 0.0484  88  LEU   B CD1 
5170 C  CD2 . LEU   B 88  ? 0.2594 0.2348 0.2337 0.0069  -0.0542 0.0226  88  LEU   B CD2 
5182 N  N   . ALA   B 89  ? 0.1635 0.1588 0.1379 -0.0379 0.0103  0.0048  89  ALA   B N   
5183 C  CA  . ALA   B 89  ? 0.1617 0.1515 0.1357 -0.0376 0.0033  0.0112  89  ALA   B CA  
5184 C  C   . ALA   B 89  ? 0.1725 0.1558 0.1446 -0.0390 0.0107  0.0078  89  ALA   B C   
5185 O  O   . ALA   B 89  ? 0.1564 0.1641 0.1819 -0.0399 0.0094  -0.0217 89  ALA   B O   
5186 C  CB  . ALA   B 89  ? 0.1598 0.1539 0.1547 -0.0370 0.0004  0.0145  89  ALA   B CB  
5192 N  N   . LYS   B 90  ? 0.2069 0.1425 0.1533 -0.0407 -0.0093 0.0127  90  LYS   B N   
5193 C  CA  . LYS   B 90  ? 0.2207 0.1420 0.1471 -0.0426 -0.0100 0.0139  90  LYS   B CA  
5194 C  C   . LYS   B 90  ? 0.2056 0.1370 0.1553 -0.0448 -0.0113 0.0027  90  LYS   B C   
5195 O  O   . LYS   B 90  ? 0.2192 0.1578 0.1747 -0.0630 -0.0007 0.0023  90  LYS   B O   
5196 C  CB  . LYS   B 90  ? 0.2438 0.1547 0.1647 -0.0340 0.0055  0.0229  90  LYS   B CB  
5197 C  CG  . LYS   B 90  ? 0.2520 0.1646 0.1760 -0.0217 0.0330  0.0175  90  LYS   B CG  
5198 C  CD  . LYS   B 90  ? 0.2873 0.1928 0.2359 -0.0180 0.0595  -0.0111 90  LYS   B CD  
5199 C  CE  . LYS   B 90  ? 0.3045 0.2081 0.2954 -0.0271 0.0772  -0.0252 90  LYS   B CE  
5200 N  NZ  . LYS   B 90  ? 0.3190 0.2009 0.3031 -0.0361 0.0984  -0.0336 90  LYS   B NZ  
5214 N  N   . HIS   B 91  ? 0.1816 0.1252 0.1468 -0.0261 -0.0292 0.0049  91  HIS   B N   
5215 C  CA  . HIS   B 91  ? 0.1709 0.1330 0.1589 -0.0254 -0.0279 0.0038  91  HIS   B CA  
5216 C  C   . HIS   B 91  ? 0.1592 0.1336 0.1399 -0.0273 -0.0056 0.0010  91  HIS   B C   
5217 O  O   . HIS   B 91  ? 0.1677 0.1383 0.1391 -0.0243 -0.0207 0.0007  91  HIS   B O   
5218 C  CB  . HIS   B 91  ? 0.1831 0.1389 0.1978 -0.0123 -0.0173 0.0125  91  HIS   B CB  
5219 C  CG  . HIS   B 91  ? 0.2229 0.1528 0.2594 0.0008  0.0164  0.0251  91  HIS   B CG  
5220 N  ND1 . HIS   B 91  ? 0.2575 0.1589 0.3130 -0.0034 0.0254  0.0107  91  HIS   B ND1 
5221 C  CD2 . HIS   B 91  ? 0.2353 0.1849 0.3010 0.0185  0.0052  0.0604  91  HIS   B CD2 
5222 C  CE1 . HIS   B 91  ? 0.2598 0.1729 0.3276 0.0130  0.0252  0.0188  91  HIS   B CE1 
5223 N  NE2 . HIS   B 91  ? 0.2463 0.1907 0.3286 0.0296  0.0208  0.0600  91  HIS   B NE2 
5231 N  N   . CYS   B 92  ? 0.1503 0.1316 0.1346 -0.0248 -0.0187 -0.0014 92  CYS   B N   
5232 C  CA  . CYS   B 92  ? 0.1444 0.1264 0.1366 -0.0235 -0.0150 0.0046  92  CYS   B CA  
5233 C  C   . CYS   B 92  ? 0.1428 0.1214 0.1347 -0.0147 -0.0124 0.0069  92  CYS   B C   
5234 O  O   . CYS   B 92  ? 0.1478 0.1315 0.1580 -0.0188 -0.0092 -0.0052 92  CYS   B O   
5235 C  CB  . CYS   B 92  ? 0.1477 0.1413 0.1414 -0.0140 -0.0078 0.0046  92  CYS   B CB  
5236 S  SG  . CYS   B 92  ? 0.1479 0.1406 0.1425 -0.0122 -0.0142 0.0047  92  CYS   B SG  
5242 N  N   . LEU   B 93  ? 0.1363 0.1288 0.1368 -0.0135 -0.0083 -0.0023 93  LEU   B N   
5243 C  CA  . LEU   B 93  ? 0.1340 0.1304 0.1369 -0.0038 -0.0108 0.0047  93  LEU   B CA  
5244 C  C   . LEU   B 93  ? 0.1286 0.1288 0.1336 -0.0029 -0.0105 0.0042  93  LEU   B C   
5245 O  O   . LEU   B 93  ? 0.1424 0.1211 0.1565 -0.0066 -0.0121 -0.0008 93  LEU   B O   
5246 C  CB  . LEU   B 93  ? 0.1425 0.1338 0.1540 -0.0025 -0.0138 0.0050  93  LEU   B CB  
5247 C  CG  . LEU   B 93  ? 0.1375 0.1397 0.1650 -0.0047 -0.0097 0.0100  93  LEU   B CG  
5248 C  CD1 . LEU   B 93  ? 0.1383 0.1503 0.1649 0.0032  -0.0139 0.0042  93  LEU   B CD1 
5249 C  CD2 . LEU   B 93  ? 0.1385 0.1453 0.1781 -0.0057 -0.0124 0.0004  93  LEU   B CD2 
5261 N  N   . HIS   B 94  ? 0.1367 0.1255 0.1314 -0.0081 -0.0146 0.0038  94  HIS   B N   
5262 C  CA  . HIS   B 94  ? 0.1385 0.1244 0.1357 0.0012  -0.0056 0.0069  94  HIS   B CA  
5263 C  C   . HIS   B 94  ? 0.1386 0.1222 0.1515 -0.0007 -0.0072 0.0068  94  HIS   B C   
5264 O  O   . HIS   B 94  ? 0.1452 0.1325 0.1834 -0.0048 0.0076  -0.0037 94  HIS   B O   
5265 C  CB  . HIS   B 94  ? 0.1400 0.1306 0.1470 0.0015  -0.0134 -0.0045 94  HIS   B CB  
5266 C  CG  . HIS   B 94  ? 0.1405 0.1266 0.1498 -0.0057 -0.0196 0.0007  94  HIS   B CG  
5267 N  ND1 . HIS   B 94  ? 0.1454 0.1316 0.1494 -0.0080 -0.0224 0.0012  94  HIS   B ND1 
5268 C  CD2 . HIS   B 94  ? 0.1473 0.1291 0.1463 -0.0061 -0.0189 0.0013  94  HIS   B CD2 
5269 C  CE1 . HIS   B 94  ? 0.1466 0.1319 0.1552 -0.0147 -0.0185 0.0014  94  HIS   B CE1 
5270 N  NE2 . HIS   B 94  ? 0.1425 0.1354 0.1603 -0.0193 -0.0192 0.0021  94  HIS   B NE2 
5278 N  N   . VAL   B 95  ? 0.1330 0.1241 0.1541 0.0010  -0.0051 0.0016  95  VAL   B N   
5279 C  CA  . VAL   B 95  ? 0.1330 0.1338 0.1532 0.0006  0.0016  0.0143  95  VAL   B CA  
5280 C  C   . VAL   B 95  ? 0.1387 0.1342 0.1579 -0.0032 0.0060  0.0047  95  VAL   B C   
5281 O  O   . VAL   B 95  ? 0.1463 0.1320 0.1716 0.0047  -0.0007 0.0115  95  VAL   B O   
5282 C  CB  . VAL   B 95  ? 0.1349 0.1288 0.1580 -0.0036 -0.0119 0.0045  95  VAL   B CB  
5283 C  CG1 . VAL   B 95  ? 0.1455 0.1517 0.1860 -0.0088 -0.0044 0.0162  95  VAL   B CG1 
5284 C  CG2 . VAL   B 95  ? 0.1493 0.1290 0.1593 -0.0001 -0.0147 0.0039  95  VAL   B CG2 
5294 N  N   . VAL   B 96  ? 0.1430 0.1353 0.1637 0.0106  0.0029  0.0114  96  VAL   B N   
5295 C  CA  . VAL   B 96  ? 0.1542 0.1482 0.1511 0.0088  -0.0003 0.0119  96  VAL   B CA  
5296 C  C   . VAL   B 96  ? 0.1559 0.1528 0.1534 0.0063  0.0006  0.0178  96  VAL   B C   
5297 O  O   . VAL   B 96  ? 0.1594 0.1589 0.1853 0.0016  0.0182  0.0108  96  VAL   B O   
5298 C  CB  . VAL   B 96  ? 0.1641 0.1648 0.1579 0.0057  0.0037  0.0059  96  VAL   B CB  
5299 C  CG1 . VAL   B 96  ? 0.1710 0.1750 0.1650 0.0108  0.0067  0.0118  96  VAL   B CG1 
5300 C  CG2 . VAL   B 96  ? 0.1677 0.1700 0.1610 0.0040  0.0098  0.0019  96  VAL   B CG2 
5310 N  N   . GLY   B 97  ? 0.1609 0.1492 0.1511 0.0015  0.0005  0.0248  97  GLY   B N   
5311 C  CA  . GLY   B 97  ? 0.1753 0.1571 0.1597 -0.0028 0.0040  0.0202  97  GLY   B CA  
5312 C  C   . GLY   B 97  ? 0.1866 0.1634 0.1695 0.0079  0.0009  0.0132  97  GLY   B C   
5313 O  O   . GLY   B 97  ? 0.1988 0.1744 0.1622 0.0027  0.0017  0.0103  97  GLY   B O   
5317 N  N   . PRO   B 98  ? 0.1973 0.1683 0.1808 0.0034  0.0189  0.0252  98  PRO   B N   
5318 C  CA  . PRO   B 98  ? 0.2114 0.1843 0.1792 0.0142  0.0229  0.0196  98  PRO   B CA  
5319 C  C   . PRO   B 98  ? 0.2236 0.1853 0.1468 0.0233  0.0285  0.0352  98  PRO   B C   
5320 O  O   . PRO   B 98  ? 0.2182 0.1811 0.1719 0.0192  0.0263  0.0343  98  PRO   B O   
5321 C  CB  . PRO   B 98  ? 0.1984 0.1880 0.2009 0.0067  0.0314  0.0218  98  PRO   B CB  
5322 C  CG  . PRO   B 98  ? 0.1895 0.1803 0.1993 0.0052  0.0249  0.0397  98  PRO   B CG  
5323 C  CD  . PRO   B 98  ? 0.1813 0.1730 0.2005 0.0070  0.0208  0.0371  98  PRO   B CD  
5331 N  N   . ASN   B 99  ? 0.2291 0.2022 0.1660 0.0388  0.0283  0.0160  99  ASN   B N   
5332 C  CA  . ASN   B 99  ? 0.2519 0.2086 0.1783 0.0438  0.0196  0.0407  99  ASN   B CA  
5333 C  C   . ASN   B 99  ? 0.2858 0.2396 0.2119 0.0377  0.0321  0.0727  99  ASN   B C   
5334 O  O   . ASN   B 99  ? 0.2935 0.2444 0.2187 0.0386  0.0240  0.0705  99  ASN   B O   
5335 C  CB  . ASN   B 99  ? 0.2601 0.2070 0.1780 0.0423  0.0123  0.0339  99  ASN   B CB  
5336 C  CG  . ASN   B 99  ? 0.2647 0.2106 0.2002 0.0403  0.0025  0.0299  99  ASN   B CG  
5337 O  OD1 . ASN   B 99  ? 0.2665 0.2136 0.2151 0.0384  0.0015  0.0321  99  ASN   B OD1 
5338 N  ND2 . ASN   B 99  ? 0.2666 0.2099 0.2100 0.0445  -0.0147 0.0250  99  ASN   B ND2 
5345 N  N   A VAL   B 100 ? 0.3067 0.2522 0.2523 0.0289  0.0358  0.0898  100 VAL   B N   
5346 N  N   B VAL   B 100 ? 0.3078 0.2526 0.2514 0.0291  0.0325  0.0878  100 VAL   B N   
5347 C  CA  A VAL   B 100 ? 0.3388 0.2709 0.3001 0.0164  0.0399  0.1053  100 VAL   B CA  
5348 C  CA  B VAL   B 100 ? 0.3383 0.2698 0.2952 0.0178  0.0337  0.1014  100 VAL   B CA  
5349 C  C   A VAL   B 100 ? 0.3609 0.2755 0.2940 0.0223  0.0382  0.1200  100 VAL   B C   
5350 C  C   B VAL   B 100 ? 0.3603 0.2748 0.2916 0.0233  0.0331  0.1177  100 VAL   B C   
5351 O  O   A VAL   B 100 ? 0.3667 0.2832 0.2966 0.0212  0.0423  0.1130  100 VAL   B O   
5352 O  O   B VAL   B 100 ? 0.3651 0.2805 0.2918 0.0219  0.0358  0.1124  100 VAL   B O   
5353 C  CB  A VAL   B 100 ? 0.3495 0.2847 0.3521 0.0016  0.0429  0.1092  100 VAL   B CB  
5354 C  CB  B VAL   B 100 ? 0.3472 0.2813 0.3400 0.0039  0.0344  0.1022  100 VAL   B CB  
5355 C  CG1 A VAL   B 100 ? 0.3557 0.2902 0.3765 -0.0009 0.0430  0.1077  100 VAL   B CG1 
5356 C  CG1 B VAL   B 100 ? 0.3526 0.2857 0.3606 0.0016  0.0340  0.1007  100 VAL   B CG1 
5357 C  CG2 A VAL   B 100 ? 0.3510 0.2907 0.3690 -0.0055 0.0469  0.1135  100 VAL   B CG2 
5358 C  CG2 B VAL   B 100 ? 0.3483 0.2861 0.3554 -0.0026 0.0367  0.1044  100 VAL   B CG2 
5377 N  N   . ASN   B 101 ? 0.3772 0.2787 0.2937 0.0331  0.0268  0.1301  101 ASN   B N   
5378 C  CA  . ASN   B 101 ? 0.4166 0.2993 0.3079 0.0458  0.0091  0.1357  101 ASN   B CA  
5379 C  C   . ASN   B 101 ? 0.4555 0.3388 0.3086 0.0471  -0.0022 0.1501  101 ASN   B C   
5380 O  O   . ASN   B 101 ? 0.4640 0.3528 0.3405 0.0528  -0.0018 0.1273  101 ASN   B O   
5381 C  CB  . ASN   B 101 ? 0.4186 0.2828 0.3275 0.0455  0.0151  0.1154  101 ASN   B CB  
5382 C  CG  . ASN   B 101 ? 0.4200 0.2673 0.3368 0.0477  0.0170  0.1077  101 ASN   B CG  
5383 O  OD1 . ASN   B 101 ? 0.4248 0.2627 0.3613 0.0422  0.0264  0.0977  101 ASN   B OD1 
5384 N  ND2 . ASN   B 101 ? 0.4166 0.2622 0.3372 0.0502  0.0175  0.0985  101 ASN   B ND2 
5392 N  N   . LYS   B 102 ? 0.4822 0.3720 0.3248 0.0362  0.0008  0.1477  102 LYS   B N   
5393 C  CA  . LYS   B 102 ? 0.5082 0.4124 0.3488 0.0206  0.0126  0.1215  102 LYS   B CA  
5394 C  C   . LYS   B 102 ? 0.5032 0.4141 0.3330 0.0210  0.0214  0.1291  102 LYS   B C   
5395 O  O   . LYS   B 102 ? 0.5119 0.4207 0.3472 0.0205  0.0113  0.1214  102 LYS   B O   
5396 C  CB  . LYS   B 102 ? 0.5360 0.4478 0.4063 0.0066  0.0220  0.0746  102 LYS   B CB  
5397 C  CG  . LYS   B 102 ? 0.5598 0.4788 0.4688 -0.0048 0.0318  0.0304  102 LYS   B CG  
5398 C  CD  . LYS   B 102 ? 0.5794 0.5034 0.5325 -0.0127 0.0424  -0.0041 102 LYS   B CD  
5399 C  CE  . LYS   B 102 ? 0.5931 0.5200 0.5830 -0.0188 0.0486  -0.0293 102 LYS   B CE  
5400 N  NZ  . LYS   B 102 ? 0.6004 0.5294 0.6125 -0.0210 0.0511  -0.0446 102 LYS   B NZ  
5414 N  N   . GLY   B 103 ? 0.4863 0.4053 0.3281 0.0212  0.0372  0.1321  103 GLY   B N   
5415 C  CA  . GLY   B 103 ? 0.4668 0.3970 0.3378 0.0212  0.0536  0.1136  103 GLY   B CA  
5416 C  C   . GLY   B 103 ? 0.4426 0.3834 0.3341 0.0188  0.0671  0.0920  103 GLY   B C   
5417 O  O   . GLY   B 103 ? 0.4475 0.3931 0.3380 0.0186  0.0707  0.0934  103 GLY   B O   
5421 N  N   A GLU   B 104 ? 0.4269 0.3708 0.3254 0.0183  0.0751  0.0761  104 GLU   B N   
5422 N  N   B GLU   B 104 ? 0.4250 0.3688 0.3276 0.0150  0.0664  0.0766  104 GLU   B N   
5423 C  CA  A GLU   B 104 ? 0.4092 0.3578 0.3121 0.0211  0.0774  0.0554  104 GLU   B CA  
5424 C  CA  B GLU   B 104 ? 0.4056 0.3536 0.3150 0.0133  0.0618  0.0571  104 GLU   B CA  
5425 C  C   A GLU   B 104 ? 0.4113 0.3597 0.3237 0.0063  0.1078  0.0530  104 GLU   B C   
5426 C  C   B GLU   B 104 ? 0.4005 0.3502 0.3206 0.0043  0.0841  0.0533  104 GLU   B C   
5427 O  O   A GLU   B 104 ? 0.4130 0.3631 0.3338 0.0032  0.1103  0.0509  104 GLU   B O   
5428 O  O   B GLU   B 104 ? 0.4023 0.3521 0.3305 0.0024  0.0851  0.0488  104 GLU   B O   
5429 C  CB  A GLU   B 104 ? 0.3930 0.3408 0.2939 0.0380  0.0430  0.0307  104 GLU   B CB  
5430 C  CB  B GLU   B 104 ? 0.3941 0.3401 0.2997 0.0195  0.0313  0.0369  104 GLU   B CB  
5431 C  CG  A GLU   B 104 ? 0.3786 0.3263 0.2739 0.0557  0.0052  0.0030  104 GLU   B CG  
5432 C  CG  B GLU   B 104 ? 0.3849 0.3290 0.2839 0.0261  -0.0007 0.0142  104 GLU   B CG  
5433 C  CD  A GLU   B 104 ? 0.3658 0.3101 0.2481 0.0726  -0.0283 -0.0139 104 GLU   B CD  
5434 C  CD  B GLU   B 104 ? 0.3782 0.3170 0.2648 0.0307  -0.0274 -0.0003 104 GLU   B CD  
5435 O  OE1 A GLU   B 104 ? 0.3510 0.2922 0.2161 0.0882  -0.0248 -0.0185 104 GLU   B OE1 
5436 O  OE1 B GLU   B 104 ? 0.3714 0.3058 0.2463 0.0336  -0.0261 -0.0025 104 GLU   B OE1 
5437 O  OE2 A GLU   B 104 ? 0.3679 0.3151 0.2430 0.0708  -0.0554 -0.0243 104 GLU   B OE2 
5438 O  OE2 B GLU   B 104 ? 0.3789 0.3193 0.2587 0.0305  -0.0475 -0.0092 104 GLU   B OE2 
5451 N  N   A ASP   B 105 ? 0.4075 0.3577 0.3224 -0.0055 0.1346  0.0524  105 ASP   B N   
5452 N  N   B ASP   B 105 ? 0.3908 0.3446 0.3103 -0.0034 0.1047  0.0534  105 ASP   B N   
5453 C  CA  A ASP   B 105 ? 0.4066 0.3556 0.3418 -0.0161 0.1537  0.0395  105 ASP   B CA  
5454 C  CA  B ASP   B 105 ? 0.3834 0.3388 0.3170 -0.0106 0.1204  0.0436  105 ASP   B CA  
5455 C  C   A ASP   B 105 ? 0.3917 0.3306 0.3052 -0.0296 0.1644  0.0388  105 ASP   B C   
5456 C  C   B ASP   B 105 ? 0.3734 0.3235 0.2968 -0.0190 0.1236  0.0348  105 ASP   B C   
5457 O  O   A ASP   B 105 ? 0.3856 0.3243 0.2872 -0.0307 0.1735  0.0425  105 ASP   B O   
5458 O  O   B ASP   B 105 ? 0.3684 0.3184 0.2832 -0.0194 0.1282  0.0352  105 ASP   B O   
5459 C  CB  A ASP   B 105 ? 0.4191 0.3766 0.4078 -0.0112 0.1561  0.0204  105 ASP   B CB  
5460 C  CB  B ASP   B 105 ? 0.3848 0.3482 0.3507 -0.0079 0.1294  0.0385  105 ASP   B CB  
5461 C  CG  A ASP   B 105 ? 0.4287 0.3923 0.4705 -0.0103 0.1597  0.0061  105 ASP   B CG  
5462 C  CG  B ASP   B 105 ? 0.3844 0.3534 0.3821 -0.0097 0.1411  0.0389  105 ASP   B CG  
5463 O  OD1 A ASP   B 105 ? 0.4284 0.3963 0.4812 -0.0143 0.1683  0.0055  105 ASP   B OD1 
5464 O  OD1 B ASP   B 105 ? 0.3820 0.3565 0.3862 -0.0151 0.1475  0.0403  105 ASP   B OD1 
5465 O  OD2 A ASP   B 105 ? 0.4341 0.3989 0.5028 -0.0057 0.1532  -0.0038 105 ASP   B OD2 
5466 O  OD2 B ASP   B 105 ? 0.3814 0.3531 0.3872 -0.0092 0.1507  0.0425  105 ASP   B OD2 
5475 N  N   A ILE   B 106 ? 0.3828 0.3095 0.3040 -0.0384 0.1544  0.0365  106 ILE   B N   
5476 N  N   B ILE   B 106 ? 0.3679 0.3117 0.2963 -0.0232 0.1141  0.0269  106 ILE   B N   
5477 C  CA  A ILE   B 106 ? 0.3656 0.2856 0.3103 -0.0521 0.1537  0.0317  106 ILE   B CA  
5478 C  CA  B ILE   B 106 ? 0.3568 0.2998 0.3026 -0.0296 0.1112  0.0175  106 ILE   B CA  
5479 C  C   A ILE   B 106 ? 0.3352 0.2750 0.3044 -0.0490 0.1478  0.0136  106 ILE   B C   
5480 C  C   B ILE   B 106 ? 0.3344 0.2953 0.2981 -0.0256 0.1064  -0.0003 106 ILE   B C   
5481 O  O   A ILE   B 106 ? 0.3246 0.2507 0.2924 -0.0541 0.1483  0.0053  106 ILE   B O   
5482 O  O   B ILE   B 106 ? 0.3266 0.2810 0.2858 -0.0287 0.1027  -0.0105 106 ILE   B O   
5483 C  CB  A ILE   B 106 ? 0.3834 0.2793 0.3295 -0.0609 0.1489  0.0375  106 ILE   B CB  
5484 C  CB  B ILE   B 106 ? 0.3703 0.2981 0.3173 -0.0359 0.1106  0.0212  106 ILE   B CB  
5485 C  CG1 A ILE   B 106 ? 0.3919 0.2816 0.3339 -0.0541 0.1421  0.0302  106 ILE   B CG1 
5486 C  CG1 B ILE   B 106 ? 0.3769 0.3000 0.3230 -0.0314 0.1056  0.0161  106 ILE   B CG1 
5487 C  CG2 A ILE   B 106 ? 0.3900 0.2799 0.3430 -0.0683 0.1481  0.0441  106 ILE   B CG2 
5488 C  CG2 B ILE   B 106 ? 0.3754 0.3001 0.3290 -0.0411 0.1114  0.0247  106 ILE   B CG2 
5489 C  CD1 A ILE   B 106 ? 0.3958 0.2842 0.3286 -0.0484 0.1412  0.0298  106 ILE   B CD1 
5490 C  CD1 B ILE   B 106 ? 0.3800 0.3018 0.3226 -0.0272 0.1039  0.0154  106 ILE   B CD1 
5513 N  N   A GLN   B 107 ? 0.3197 0.2907 0.3205 -0.0401 0.1339  0.0118  107 GLN   B N   
5514 N  N   B GLN   B 107 ? 0.3222 0.3064 0.3145 -0.0197 0.1008  -0.0019 107 GLN   B N   
5515 C  CA  A GLN   B 107 ? 0.3054 0.3069 0.3446 -0.0291 0.1126  0.0105  107 GLN   B CA  
5516 C  CA  B GLN   B 107 ? 0.3104 0.3165 0.3370 -0.0133 0.0911  0.0004  107 GLN   B CA  
5517 C  C   A GLN   B 107 ? 0.2751 0.2886 0.3127 -0.0186 0.0902  -0.0001 107 GLN   B C   
5518 C  C   B GLN   B 107 ? 0.2798 0.2954 0.3063 -0.0089 0.0825  -0.0043 107 GLN   B C   
5519 O  O   A GLN   B 107 ? 0.2690 0.2905 0.3305 -0.0179 0.0683  -0.0130 107 GLN   B O   
5520 O  O   B GLN   B 107 ? 0.2769 0.2993 0.3181 -0.0077 0.0677  -0.0145 107 GLN   B O   
5521 C  CB  A GLN   B 107 ? 0.3335 0.3430 0.4225 -0.0238 0.0908  0.0137  107 GLN   B CB  
5522 C  CB  B GLN   B 107 ? 0.3364 0.3481 0.4063 -0.0092 0.0763  0.0039  107 GLN   B CB  
5523 C  CG  A GLN   B 107 ? 0.3617 0.3756 0.4996 -0.0162 0.0608  0.0143  107 GLN   B CG  
5524 C  CG  B GLN   B 107 ? 0.3613 0.3764 0.4746 -0.0035 0.0551  0.0056  107 GLN   B CG  
5525 C  CD  A GLN   B 107 ? 0.3820 0.4004 0.5614 -0.0133 0.0398  0.0154  107 GLN   B CD  
5526 C  CD  B GLN   B 107 ? 0.3798 0.3981 0.5298 -0.0011 0.0400  0.0071  107 GLN   B CD  
5527 O  OE1 A GLN   B 107 ? 0.3898 0.4099 0.5858 -0.0119 0.0356  0.0130  107 GLN   B OE1 
5528 O  OE1 B GLN   B 107 ? 0.3868 0.4057 0.5499 -0.0006 0.0374  0.0066  107 GLN   B OE1 
5529 N  NE2 A GLN   B 107 ? 0.3900 0.4086 0.5814 -0.0099 0.0314  0.0193  107 GLN   B NE2 
5530 N  NE2 B GLN   B 107 ? 0.3871 0.4059 0.5486 0.0018  0.0344  0.0096  107 GLN   B NE2 
5547 N  N   . LEU   B 108 ? 0.2521 0.2710 0.2779 0.0013  0.0831  -0.0019 108 LEU   B N   
5548 C  CA  . LEU   B 108 ? 0.2297 0.2405 0.2314 0.0159  0.0531  0.0123  108 LEU   B CA  
5549 C  C   . LEU   B 108 ? 0.1980 0.1985 0.2253 0.0157  0.0320  0.0259  108 LEU   B C   
5550 O  O   . LEU   B 108 ? 0.1995 0.1860 0.2163 0.0175  0.0195  0.0237  108 LEU   B O   
5551 C  CB  . LEU   B 108 ? 0.2427 0.2567 0.2151 0.0140  0.0521  0.0226  108 LEU   B CB  
5552 C  CG  . LEU   B 108 ? 0.2609 0.2865 0.2305 0.0194  0.0477  -0.0013 108 LEU   B CG  
5553 C  CD1 . LEU   B 108 ? 0.2680 0.3001 0.2185 0.0114  0.0538  0.0020  108 LEU   B CD1 
5554 C  CD2 . LEU   B 108 ? 0.2758 0.3001 0.2492 0.0313  0.0348  -0.0164 108 LEU   B CD2 
5567 N  N   . LEU   B 109 ? 0.1873 0.1762 0.2175 0.0108  0.0305  0.0198  109 LEU   B N   
5568 C  CA  . LEU   B 109 ? 0.1694 0.1500 0.2265 0.0086  0.0288  0.0283  109 LEU   B CA  
5569 C  C   . LEU   B 109 ? 0.1544 0.1359 0.2244 0.0016  0.0233  0.0204  109 LEU   B C   
5570 O  O   . LEU   B 109 ? 0.1518 0.1353 0.2220 0.0026  0.0218  0.0306  109 LEU   B O   
5571 C  CB  . LEU   B 109 ? 0.1723 0.1435 0.2342 0.0073  0.0203  0.0343  109 LEU   B CB  
5572 C  CG  . LEU   B 109 ? 0.1700 0.1448 0.2317 0.0049  0.0155  0.0271  109 LEU   B CG  
5573 C  CD1 . LEU   B 109 ? 0.1621 0.1589 0.2171 0.0144  0.0194  0.0306  109 LEU   B CD1 
5574 C  CD2 . LEU   B 109 ? 0.1815 0.1535 0.2443 0.0098  0.0135  0.0242  109 LEU   B CD2 
5586 N  N   . LYS   B 110 ? 0.1510 0.1403 0.2293 -0.0039 0.0288  0.0198  110 LYS   B N   
5587 C  CA  . LYS   B 110 ? 0.1500 0.1404 0.2249 -0.0006 0.0198  0.0169  110 LYS   B CA  
5588 C  C   . LYS   B 110 ? 0.1440 0.1431 0.2083 0.0003  0.0197  0.0097  110 LYS   B C   
5589 O  O   . LYS   B 110 ? 0.1407 0.1456 0.2004 -0.0056 0.0127  0.0085  110 LYS   B O   
5590 C  CB  . LYS   B 110 ? 0.1507 0.1421 0.2515 -0.0035 0.0249  0.0103  110 LYS   B CB  
5591 C  CG  . LYS   B 110 ? 0.1478 0.1403 0.2703 -0.0040 0.0058  0.0111  110 LYS   B CG  
5592 C  CD  . LYS   B 110 ? 0.1533 0.1437 0.2791 -0.0031 0.0122  0.0144  110 LYS   B CD  
5593 C  CE  . LYS   B 110 ? 0.1495 0.1572 0.2958 -0.0058 0.0095  0.0043  110 LYS   B CE  
5594 N  NZ  . LYS   B 110 ? 0.1520 0.1703 0.2949 -0.0025 0.0001  -0.0033 110 LYS   B NZ  
5608 N  N   . SER   B 111 ? 0.1506 0.1461 0.2219 -0.0046 0.0251  0.0135  111 SER   B N   
5609 C  CA  . SER   B 111 ? 0.1555 0.1478 0.2149 0.0033  0.0143  0.0142  111 SER   B CA  
5610 C  C   . SER   B 111 ? 0.1524 0.1367 0.1975 0.0039  0.0059  0.0094  111 SER   B C   
5611 O  O   . SER   B 111 ? 0.1460 0.1382 0.2135 -0.0018 0.0071  0.0142  111 SER   B O   
5612 C  CB  . SER   B 111 ? 0.1678 0.1709 0.2226 0.0020  0.0383  0.0250  111 SER   B CB  
5613 O  OG  . SER   B 111 ? 0.1860 0.2074 0.2390 0.0057  0.0351  0.0265  111 SER   B OG  
5619 N  N   . ALA   B 112 ? 0.1440 0.1403 0.2038 0.0059  0.0121  0.0154  112 ALA   B N   
5620 C  CA  . ALA   B 112 ? 0.1392 0.1465 0.1918 0.0012  0.0046  0.0026  112 ALA   B CA  
5621 C  C   . ALA   B 112 ? 0.1323 0.1408 0.1906 0.0001  0.0038  0.0015  112 ALA   B C   
5622 O  O   . ALA   B 112 ? 0.1329 0.1390 0.2049 -0.0046 0.0048  -0.0010 112 ALA   B O   
5623 C  CB  . ALA   B 112 ? 0.1428 0.1560 0.2046 0.0043  0.0144  0.0137  112 ALA   B CB  
5629 N  N   . TYR   B 113 ? 0.1303 0.1285 0.2076 -0.0015 0.0086  0.0059  113 TYR   B N   
5630 C  CA  . TYR   B 113 ? 0.1309 0.1242 0.2065 0.0002  0.0074  0.0001  113 TYR   B CA  
5631 C  C   . TYR   B 113 ? 0.1278 0.1213 0.2014 -0.0058 0.0020  0.0039  113 TYR   B C   
5632 O  O   . TYR   B 113 ? 0.1322 0.1244 0.1960 -0.0062 -0.0024 -0.0022 113 TYR   B O   
5633 C  CB  . TYR   B 113 ? 0.1379 0.1245 0.2091 -0.0029 0.0080  0.0041  113 TYR   B CB  
5634 C  CG  . TYR   B 113 ? 0.1386 0.1263 0.2147 -0.0041 0.0038  0.0099  113 TYR   B CG  
5635 C  CD1 . TYR   B 113 ? 0.1411 0.1276 0.2225 -0.0031 0.0054  0.0116  113 TYR   B CD1 
5636 C  CD2 . TYR   B 113 ? 0.1444 0.1274 0.2115 -0.0036 0.0055  0.0110  113 TYR   B CD2 
5637 C  CE1 . TYR   B 113 ? 0.1431 0.1332 0.2171 -0.0023 0.0108  0.0102  113 TYR   B CE1 
5638 C  CE2 . TYR   B 113 ? 0.1489 0.1215 0.2199 0.0029  0.0014  0.0100  113 TYR   B CE2 
5639 C  CZ  . TYR   B 113 ? 0.1381 0.1261 0.2307 0.0072  0.0049  0.0087  113 TYR   B CZ  
5640 O  OH  . TYR   B 113 ? 0.1455 0.1261 0.2533 0.0083  0.0118  0.0119  113 TYR   B OH  
5650 N  N   . GLU   B 114 ? 0.1285 0.1171 0.2128 -0.0025 0.0075  0.0096  114 GLU   B N   
5651 C  CA  . GLU   B 114 ? 0.1280 0.1197 0.2173 0.0005  0.0047  0.0073  114 GLU   B CA  
5652 C  C   . GLU   B 114 ? 0.1259 0.1218 0.1950 0.0007  0.0025  0.0064  114 GLU   B C   
5653 O  O   . GLU   B 114 ? 0.1290 0.1230 0.2021 -0.0008 0.0008  0.0065  114 GLU   B O   
5654 C  CB  . GLU   B 114 ? 0.1295 0.1274 0.2224 -0.0030 0.0058  0.0049  114 GLU   B CB  
5655 C  CG  . GLU   B 114 ? 0.1333 0.1282 0.2264 -0.0038 0.0063  0.0095  114 GLU   B CG  
5656 C  CD  . GLU   B 114 ? 0.1300 0.1373 0.2272 -0.0052 0.0020  0.0060  114 GLU   B CD  
5657 O  OE1 . GLU   B 114 ? 0.1311 0.1481 0.2151 -0.0105 0.0148  0.0086  114 GLU   B OE1 
5658 O  OE2 . GLU   B 114 ? 0.1295 0.1530 0.2314 -0.0160 0.0099  0.0077  114 GLU   B OE2 
5665 N  N   . ASN   B 115 ? 0.1303 0.1200 0.1887 -0.0046 -0.0016 0.0029  115 ASN   B N   
5666 C  CA  . ASN   B 115 ? 0.1326 0.1270 0.1731 -0.0104 -0.0016 0.0031  115 ASN   B CA  
5667 C  C   . ASN   B 115 ? 0.1267 0.1202 0.1734 -0.0131 -0.0076 -0.0028 115 ASN   B C   
5668 O  O   . ASN   B 115 ? 0.1390 0.1240 0.1874 -0.0104 0.0010  0.0045  115 ASN   B O   
5669 C  CB  . ASN   B 115 ? 0.1424 0.1374 0.1770 -0.0148 0.0024  0.0072  115 ASN   B CB  
5670 C  CG  . ASN   B 115 ? 0.1511 0.1402 0.1854 -0.0002 -0.0070 -0.0012 115 ASN   B CG  
5671 O  OD1 . ASN   B 115 ? 0.1893 0.1534 0.2099 -0.0029 0.0064  -0.0157 115 ASN   B OD1 
5672 N  ND2 . ASN   B 115 ? 0.1512 0.1512 0.1819 -0.0053 0.0006  -0.0019 115 ASN   B ND2 
5679 N  N   . PHE   B 116 ? 0.1263 0.1244 0.1713 -0.0083 -0.0067 0.0058  116 PHE   B N   
5680 C  CA  . PHE   B 116 ? 0.1338 0.1261 0.1793 -0.0048 -0.0050 0.0050  116 PHE   B CA  
5681 C  C   . PHE   B 116 ? 0.1364 0.1185 0.1715 -0.0096 -0.0095 0.0041  116 PHE   B C   
5682 O  O   . PHE   B 116 ? 0.1397 0.1243 0.1827 -0.0003 -0.0094 0.0034  116 PHE   B O   
5683 C  CB  . PHE   B 116 ? 0.1297 0.1246 0.1766 -0.0073 -0.0197 0.0080  116 PHE   B CB  
5684 C  CG  . PHE   B 116 ? 0.1280 0.1186 0.1748 -0.0058 -0.0065 0.0051  116 PHE   B CG  
5685 C  CD1 . PHE   B 116 ? 0.1385 0.1268 0.1963 -0.0034 -0.0082 0.0044  116 PHE   B CD1 
5686 C  CD2 . PHE   B 116 ? 0.1324 0.1299 0.1778 -0.0049 -0.0057 -0.0050 116 PHE   B CD2 
5687 C  CE1 . PHE   B 116 ? 0.1379 0.1304 0.1938 -0.0057 -0.0135 0.0085  116 PHE   B CE1 
5688 C  CE2 . PHE   B 116 ? 0.1356 0.1269 0.1902 -0.0025 -0.0014 -0.0014 116 PHE   B CE2 
5689 C  CZ  . PHE   B 116 ? 0.1289 0.1310 0.1981 -0.0070 -0.0148 0.0062  116 PHE   B CZ  
5699 N  N   . ASN   B 117 ? 0.1309 0.1223 0.1861 -0.0074 -0.0127 0.0050  117 ASN   B N   
5700 C  CA  . ASN   B 117 ? 0.1374 0.1212 0.1864 0.0001  -0.0151 0.0004  117 ASN   B CA  
5701 C  C   . ASN   B 117 ? 0.1423 0.1262 0.1960 0.0019  -0.0101 0.0009  117 ASN   B C   
5702 O  O   . ASN   B 117 ? 0.1525 0.1292 0.2308 -0.0033 -0.0301 0.0106  117 ASN   B O   
5703 C  CB  . ASN   B 117 ? 0.1395 0.1240 0.1877 0.0013  -0.0141 -0.0080 117 ASN   B CB  
5704 C  CG  . ASN   B 117 ? 0.1327 0.1268 0.2086 0.0020  -0.0100 -0.0051 117 ASN   B CG  
5705 O  OD1 . ASN   B 117 ? 0.1574 0.1243 0.2235 -0.0100 -0.0022 -0.0014 117 ASN   B OD1 
5706 N  ND2 . ASN   B 117 ? 0.1362 0.1307 0.2084 0.0006  -0.0062 -0.0003 117 ASN   B ND2 
5713 N  N   . GLN   B 118 ? 0.1431 0.1171 0.1861 -0.0079 -0.0171 -0.0016 118 GLN   B N   
5714 C  CA  . GLN   B 118 ? 0.1503 0.1250 0.2021 0.0015  -0.0103 -0.0022 118 GLN   B CA  
5715 C  C   . GLN   B 118 ? 0.1556 0.1208 0.2118 0.0030  -0.0151 -0.0027 118 GLN   B C   
5716 O  O   . GLN   B 118 ? 0.1715 0.1174 0.2452 -0.0064 -0.0042 0.0002  118 GLN   B O   
5717 C  CB  . GLN   B 118 ? 0.1557 0.1261 0.2153 0.0036  -0.0151 -0.0005 118 GLN   B CB  
5718 C  CG  . GLN   B 118 ? 0.1637 0.1259 0.2127 0.0079  -0.0103 -0.0069 118 GLN   B CG  
5719 C  CD  . GLN   B 118 ? 0.1614 0.1241 0.2117 0.0051  -0.0096 -0.0173 118 GLN   B CD  
5720 O  OE1 . GLN   B 118 ? 0.1696 0.1217 0.2358 0.0062  -0.0011 -0.0025 118 GLN   B OE1 
5721 N  NE2 . GLN   B 118 ? 0.1616 0.1275 0.2193 0.0048  -0.0101 -0.0042 118 GLN   B NE2 
5730 N  N   . HIS   B 119 ? 0.1500 0.1253 0.1804 -0.0017 -0.0145 0.0063  119 HIS   B N   
5731 C  CA  . HIS   B 119 ? 0.1568 0.1367 0.1771 0.0015  -0.0194 0.0031  119 HIS   B CA  
5732 C  C   . HIS   B 119 ? 0.1612 0.1384 0.1747 -0.0018 -0.0238 0.0060  119 HIS   B C   
5733 O  O   . HIS   B 119 ? 0.1669 0.1371 0.1950 -0.0227 -0.0210 0.0083  119 HIS   B O   
5734 C  CB  . HIS   B 119 ? 0.1630 0.1486 0.1768 0.0002  -0.0234 0.0035  119 HIS   B CB  
5735 C  CG  . HIS   B 119 ? 0.1689 0.1720 0.1959 0.0116  -0.0376 -0.0184 119 HIS   B CG  
5736 N  ND1 . HIS   B 119 ? 0.1773 0.1877 0.2250 0.0071  -0.0508 -0.0306 119 HIS   B ND1 
5737 C  CD2 . HIS   B 119 ? 0.1846 0.1910 0.2018 0.0377  -0.0458 -0.0196 119 HIS   B CD2 
5738 C  CE1 . HIS   B 119 ? 0.1954 0.2026 0.2294 0.0209  -0.0554 -0.0452 119 HIS   B CE1 
5739 N  NE2 . HIS   B 119 ? 0.1964 0.2126 0.2226 0.0336  -0.0481 -0.0407 119 HIS   B NE2 
5747 N  N   . GLU   B 120 ? 0.1784 0.1434 0.1766 -0.0096 -0.0347 0.0095  120 GLU   B N   
5748 C  CA  . GLU   B 120 ? 0.2026 0.1580 0.1932 -0.0074 -0.0506 0.0305  120 GLU   B CA  
5749 C  C   . GLU   B 120 ? 0.1851 0.1439 0.1802 -0.0168 -0.0416 0.0296  120 GLU   B C   
5750 O  O   . GLU   B 120 ? 0.1804 0.1523 0.1828 -0.0132 -0.0339 0.0154  120 GLU   B O   
5751 C  CB  . GLU   B 120 ? 0.2700 0.1925 0.2705 0.0173  -0.0805 0.0593  120 GLU   B CB  
5752 C  CG  . GLU   B 120 ? 0.3355 0.2768 0.3786 0.0349  -0.1032 0.0801  120 GLU   B CG  
5753 C  CD  . GLU   B 120 ? 0.3920 0.3561 0.4870 0.0390  -0.1080 0.0914  120 GLU   B CD  
5754 O  OE1 . GLU   B 120 ? 0.4115 0.3797 0.5221 0.0346  -0.1031 0.1000  120 GLU   B OE1 
5755 O  OE2 . GLU   B 120 ? 0.4113 0.3865 0.5365 0.0400  -0.1060 0.0870  120 GLU   B OE2 
5762 N  N   . VAL   B 121 ? 0.1780 0.1377 0.1761 -0.0196 -0.0289 0.0211  121 VAL   B N   
5763 C  CA  . VAL   B 121 ? 0.1781 0.1497 0.1596 -0.0138 -0.0260 0.0098  121 VAL   B CA  
5764 C  C   . VAL   B 121 ? 0.1633 0.1407 0.1543 -0.0209 -0.0208 0.0062  121 VAL   B C   
5765 O  O   . VAL   B 121 ? 0.1656 0.1393 0.1785 -0.0254 -0.0266 0.0032  121 VAL   B O   
5766 C  CB  . VAL   B 121 ? 0.1954 0.1802 0.1607 -0.0043 -0.0271 0.0155  121 VAL   B CB  
5767 C  CG1 . VAL   B 121 ? 0.2036 0.1970 0.1827 -0.0138 -0.0153 0.0058  121 VAL   B CG1 
5768 C  CG2 . VAL   B 121 ? 0.2195 0.2037 0.1731 0.0041  -0.0216 0.0100  121 VAL   B CG2 
5778 N  N   . LEU   B 122 ? 0.1594 0.1385 0.1537 -0.0166 -0.0270 0.0066  122 LEU   B N   
5779 C  CA  . LEU   B 122 ? 0.1520 0.1466 0.1424 -0.0198 -0.0221 0.0107  122 LEU   B CA  
5780 C  C   . LEU   B 122 ? 0.1514 0.1322 0.1483 -0.0251 -0.0215 0.0089  122 LEU   B C   
5781 O  O   . LEU   B 122 ? 0.1602 0.1307 0.1808 -0.0271 -0.0300 -0.0018 122 LEU   B O   
5782 C  CB  . LEU   B 122 ? 0.1751 0.1543 0.1756 -0.0044 -0.0220 0.0152  122 LEU   B CB  
5783 C  CG  . LEU   B 122 ? 0.1633 0.1602 0.1855 -0.0158 -0.0071 0.0120  122 LEU   B CG  
5784 C  CD1 . LEU   B 122 ? 0.1627 0.1809 0.1930 -0.0150 -0.0192 0.0013  122 LEU   B CD1 
5785 C  CD2 . LEU   B 122 ? 0.1630 0.1643 0.1665 -0.0088 -0.0037 0.0035  122 LEU   B CD2 
5797 N  N   . LEU   B 123 ? 0.1504 0.1231 0.1566 -0.0234 -0.0160 0.0077  123 LEU   B N   
5798 C  CA  . LEU   B 123 ? 0.1542 0.1242 0.1497 -0.0251 -0.0244 -0.0017 123 LEU   B CA  
5799 C  C   . LEU   B 123 ? 0.1481 0.1209 0.1455 -0.0203 -0.0185 -0.0032 123 LEU   B C   
5800 O  O   . LEU   B 123 ? 0.1590 0.1295 0.1490 -0.0274 -0.0233 0.0029  123 LEU   B O   
5801 C  CB  . LEU   B 123 ? 0.1578 0.1292 0.1630 -0.0191 -0.0172 -0.0052 123 LEU   B CB  
5802 C  CG  . LEU   B 123 ? 0.1537 0.1366 0.1662 -0.0125 -0.0061 0.0067  123 LEU   B CG  
5803 C  CD1 . LEU   B 123 ? 0.1623 0.1404 0.1859 -0.0102 0.0006  -0.0062 123 LEU   B CD1 
5804 C  CD2 . LEU   B 123 ? 0.1580 0.1513 0.1774 -0.0110 -0.0031 0.0217  123 LEU   B CD2 
5816 N  N   . ALA   B 124 ? 0.1442 0.1235 0.1570 -0.0184 -0.0073 -0.0008 124 ALA   B N   
5817 C  CA  . ALA   B 124 ? 0.1356 0.1258 0.1542 -0.0191 -0.0076 -0.0132 124 ALA   B CA  
5818 C  C   . ALA   B 124 ? 0.1311 0.1279 0.1546 -0.0197 -0.0100 -0.0058 124 ALA   B C   
5819 O  O   . ALA   B 124 ? 0.1439 0.1295 0.1616 -0.0123 -0.0150 0.0015  124 ALA   B O   
5820 C  CB  . ALA   B 124 ? 0.1457 0.1307 0.1689 -0.0067 -0.0023 -0.0068 124 ALA   B CB  
5826 N  N   . PRO   B 125 ? 0.1407 0.1289 0.1594 -0.0161 -0.0209 0.0084  125 PRO   B N   
5827 C  CA  . PRO   B 125 ? 0.1508 0.1281 0.1740 -0.0118 -0.0230 0.0169  125 PRO   B CA  
5828 C  C   . PRO   B 125 ? 0.1473 0.1228 0.1924 -0.0147 -0.0180 0.0042  125 PRO   B C   
5829 O  O   . PRO   B 125 ? 0.1482 0.1240 0.2026 -0.0099 -0.0090 0.0138  125 PRO   B O   
5830 C  CB  . PRO   B 125 ? 0.1494 0.1538 0.1815 -0.0192 -0.0192 0.0252  125 PRO   B CB  
5831 C  CG  . PRO   B 125 ? 0.1536 0.1586 0.1717 -0.0278 -0.0175 0.0160  125 PRO   B CG  
5832 C  CD  . PRO   B 125 ? 0.1486 0.1436 0.1538 -0.0255 -0.0145 0.0090  125 PRO   B CD  
5840 N  N   . LEU   B 126 ? 0.1489 0.1184 0.2095 -0.0137 0.0026  0.0102  126 LEU   B N   
5841 C  CA  . LEU   B 126 ? 0.1502 0.1336 0.2130 -0.0117 0.0196  0.0137  126 LEU   B CA  
5842 C  C   . LEU   B 126 ? 0.1482 0.1414 0.2142 -0.0016 0.0174  0.0229  126 LEU   B C   
5843 O  O   . LEU   B 126 ? 0.1688 0.1680 0.2283 0.0169  -0.0093 -0.0019 126 LEU   B O   
5844 C  CB  . LEU   B 126 ? 0.1696 0.1345 0.2342 -0.0148 0.0256  0.0107  126 LEU   B CB  
5845 C  CG  . LEU   B 126 ? 0.1869 0.1438 0.2509 -0.0229 0.0212  -0.0099 126 LEU   B CG  
5846 C  CD1 . LEU   B 126 ? 0.2040 0.1594 0.2937 -0.0251 0.0159  -0.0217 126 LEU   B CD1 
5847 C  CD2 . LEU   B 126 ? 0.1866 0.1507 0.2524 -0.0258 0.0112  -0.0092 126 LEU   B CD2 
5859 N  N   . LEU   B 127 ? 0.1444 0.1266 0.2273 -0.0001 0.0148  0.0160  127 LEU   B N   
5860 C  CA  . LEU   B 127 ? 0.1510 0.1396 0.2262 -0.0054 0.0238  0.0185  127 LEU   B CA  
5861 C  C   . LEU   B 127 ? 0.1450 0.1363 0.2257 -0.0054 0.0205  0.0229  127 LEU   B C   
5862 O  O   . LEU   B 127 ? 0.1500 0.1398 0.2341 -0.0130 0.0095  0.0190  127 LEU   B O   
5863 C  CB  . LEU   B 127 ? 0.1622 0.1338 0.2277 -0.0041 0.0151  0.0198  127 LEU   B CB  
5864 C  CG  . LEU   B 127 ? 0.1718 0.1372 0.2374 0.0028  0.0134  0.0197  127 LEU   B CG  
5865 C  CD1 . LEU   B 127 ? 0.1795 0.1349 0.2381 0.0062  0.0011  0.0111  127 LEU   B CD1 
5866 C  CD2 . LEU   B 127 ? 0.1740 0.1458 0.2571 -0.0115 0.0162  0.0316  127 LEU   B CD2 
5878 N  N   . SER   B 128 ? 0.1489 0.1335 0.2207 -0.0008 -0.0030 0.0179  128 SER   B N   
5879 C  CA  . SER   B 128 ? 0.1667 0.1405 0.2155 0.0025  -0.0132 0.0254  128 SER   B CA  
5880 C  C   . SER   B 128 ? 0.1767 0.1424 0.2354 0.0024  -0.0230 0.0215  128 SER   B C   
5881 O  O   . SER   B 128 ? 0.1882 0.1460 0.2662 0.0019  -0.0233 0.0316  128 SER   B O   
5882 C  CB  . SER   B 128 ? 0.1758 0.1470 0.2205 0.0071  -0.0059 0.0282  128 SER   B CB  
5883 O  OG  . SER   B 128 ? 0.1801 0.1618 0.2185 0.0086  0.0056  0.0338  128 SER   B OG  
5889 N  N   . ALA   B 129 ? 0.1848 0.1488 0.2549 0.0176  -0.0187 0.0108  129 ALA   B N   
5890 C  CA  . ALA   B 129 ? 0.2009 0.1582 0.2701 0.0245  -0.0113 0.0025  129 ALA   B CA  
5891 C  C   . ALA   B 129 ? 0.1868 0.1512 0.2566 0.0127  0.0031  0.0062  129 ALA   B C   
5892 O  O   . ALA   B 129 ? 0.1772 0.1563 0.2580 0.0170  -0.0026 0.0098  129 ALA   B O   
5893 C  CB  . ALA   B 129 ? 0.2237 0.1821 0.3054 0.0333  -0.0016 -0.0008 129 ALA   B CB  
5899 N  N   . GLY   B 130 ? 0.1847 0.1492 0.2620 0.0199  -0.0001 0.0047  130 GLY   B N   
5900 C  CA  . GLY   B 130 ? 0.1892 0.1607 0.2775 0.0137  0.0132  0.0026  130 GLY   B CA  
5901 C  C   . GLY   B 130 ? 0.1907 0.1661 0.2668 0.0139  0.0058  0.0101  130 GLY   B C   
5902 O  O   . GLY   B 130 ? 0.2090 0.1729 0.2722 0.0154  0.0033  0.0169  130 GLY   B O   
5906 N  N   . ILE   B 131 ? 0.1884 0.1813 0.2687 0.0269  0.0020  0.0055  131 ILE   B N   
5907 C  CA  . ILE   B 131 ? 0.2054 0.1913 0.2704 0.0275  -0.0175 0.0171  131 ILE   B CA  
5908 C  C   . ILE   B 131 ? 0.2175 0.1777 0.2331 0.0200  -0.0111 0.0213  131 ILE   B C   
5909 O  O   . ILE   B 131 ? 0.2463 0.1987 0.2471 0.0253  -0.0289 0.0231  131 ILE   B O   
5910 C  CB  . ILE   B 131 ? 0.2028 0.2258 0.3092 0.0276  -0.0320 0.0300  131 ILE   B CB  
5911 C  CG1 . ILE   B 131 ? 0.2066 0.2454 0.3368 0.0031  -0.0222 0.0314  131 ILE   B CG1 
5912 C  CG2 . ILE   B 131 ? 0.2066 0.2429 0.3324 0.0294  -0.0267 0.0257  131 ILE   B CG2 
5913 C  CD1 . ILE   B 131 ? 0.2155 0.2635 0.3556 -0.0131 -0.0219 0.0367  131 ILE   B CD1 
5925 N  N   . PHE   B 132 ? 0.1965 0.1606 0.2178 0.0126  0.0095  0.0217  132 PHE   B N   
5926 C  CA  . PHE   B 132 ? 0.2116 0.1627 0.2214 0.0076  0.0234  0.0146  132 PHE   B CA  
5927 C  C   . PHE   B 132 ? 0.2313 0.1773 0.2344 0.0090  0.0317  0.0194  132 PHE   B C   
5928 O  O   . PHE   B 132 ? 0.2509 0.2015 0.2550 -0.0005 0.0435  0.0201  132 PHE   B O   
5929 C  CB  . PHE   B 132 ? 0.2003 0.1635 0.2043 0.0081  0.0191  0.0164  132 PHE   B CB  
5930 C  CG  . PHE   B 132 ? 0.1984 0.1674 0.2034 0.0115  0.0153  0.0218  132 PHE   B CG  
5931 C  CD1 . PHE   B 132 ? 0.2035 0.1652 0.2297 0.0079  0.0154  0.0223  132 PHE   B CD1 
5932 C  CD2 . PHE   B 132 ? 0.1960 0.1711 0.1838 0.0154  0.0099  0.0222  132 PHE   B CD2 
5933 C  CE1 . PHE   B 132 ? 0.2067 0.1712 0.2483 0.0072  0.0129  0.0197  132 PHE   B CE1 
5934 C  CE2 . PHE   B 132 ? 0.2014 0.1720 0.1997 0.0169  0.0054  0.0156  132 PHE   B CE2 
5935 C  CZ  . PHE   B 132 ? 0.2042 0.1714 0.2355 0.0095  -0.0019 0.0258  132 PHE   B CZ  
5945 N  N   . GLY   B 133 ? 0.2309 0.1692 0.2393 0.0014  0.0210  0.0436  133 GLY   B N   
5946 C  CA  . GLY   B 133 ? 0.2412 0.1835 0.2542 -0.0160 0.0149  0.0462  133 GLY   B CA  
5947 C  C   . GLY   B 133 ? 0.2446 0.1927 0.2547 -0.0261 0.0242  0.0489  133 GLY   B C   
5948 O  O   . GLY   B 133 ? 0.2654 0.2067 0.2897 -0.0366 0.0274  0.0625  133 GLY   B O   
5952 N  N   . ALA   B 134 ? 0.2215 0.1918 0.2396 -0.0231 0.0250  0.0330  134 ALA   B N   
5953 C  CA  . ALA   B 134 ? 0.2143 0.1904 0.2485 -0.0185 0.0253  0.0183  134 ALA   B CA  
5954 C  C   . ALA   B 134 ? 0.2184 0.1782 0.2528 -0.0082 0.0236  0.0255  134 ALA   B C   
5955 O  O   . ALA   B 134 ? 0.2193 0.1995 0.2626 0.0010  0.0276  0.0207  134 ALA   B O   
5956 C  CB  . ALA   B 134 ? 0.2139 0.1920 0.2658 -0.0134 0.0201  0.0140  134 ALA   B CB  
5962 N  N   . ASP   B 135 ? 0.2328 0.1721 0.2571 -0.0160 0.0100  0.0327  135 ASP   B N   
5963 C  CA  . ASP   B 135 ? 0.2467 0.1673 0.2822 -0.0132 -0.0031 0.0376  135 ASP   B CA  
5964 C  C   . ASP   B 135 ? 0.2300 0.1562 0.2669 -0.0016 -0.0044 0.0340  135 ASP   B C   
5965 O  O   . ASP   B 135 ? 0.2200 0.1509 0.2693 -0.0032 -0.0012 0.0346  135 ASP   B O   
5966 C  CB  . ASP   B 135 ? 0.2757 0.1779 0.3128 -0.0346 -0.0086 0.0386  135 ASP   B CB  
5967 C  CG  . ASP   B 135 ? 0.3052 0.1763 0.3617 -0.0580 -0.0112 0.0341  135 ASP   B CG  
5968 O  OD1 . ASP   B 135 ? 0.3168 0.1645 0.3558 -0.0429 -0.0242 0.0296  135 ASP   B OD1 
5969 O  OD2 . ASP   B 135 ? 0.3262 0.2088 0.4149 -0.0720 -0.0083 0.0171  135 ASP   B OD2 
5974 N  N   . PRO   B 136 ? 0.2256 0.1574 0.2742 0.0159  -0.0154 0.0251  136 PRO   B N   
5975 C  CA  . PRO   B 136 ? 0.2056 0.1462 0.2706 0.0149  -0.0194 0.0113  136 PRO   B CA  
5976 C  C   . PRO   B 136 ? 0.1825 0.1365 0.2809 0.0143  -0.0094 0.0078  136 PRO   B C   
5977 O  O   . PRO   B 136 ? 0.1652 0.1372 0.2660 0.0097  0.0002  0.0090  136 PRO   B O   
5978 C  CB  . PRO   B 136 ? 0.2159 0.1698 0.2767 0.0249  -0.0278 -0.0011 136 PRO   B CB  
5979 C  CG  . PRO   B 136 ? 0.2357 0.1784 0.2913 0.0334  -0.0189 -0.0003 136 PRO   B CG  
5980 C  CD  . PRO   B 136 ? 0.2341 0.1729 0.2853 0.0373  -0.0094 0.0105  136 PRO   B CD  
5988 N  N   . ILE   B 137 ? 0.1897 0.1328 0.2926 0.0133  -0.0084 0.0072  137 ILE   B N   
5989 C  CA  . ILE   B 137 ? 0.1962 0.1311 0.3048 -0.0000 -0.0019 0.0045  137 ILE   B CA  
5990 C  C   . ILE   B 137 ? 0.1882 0.1336 0.2968 -0.0055 0.0104  0.0168  137 ILE   B C   
5991 O  O   . ILE   B 137 ? 0.1778 0.1353 0.2854 -0.0108 0.0091  0.0059  137 ILE   B O   
5992 C  CB  . ILE   B 137 ? 0.2205 0.1409 0.3567 -0.0030 -0.0021 0.0067  137 ILE   B CB  
5993 C  CG1 . ILE   B 137 ? 0.2500 0.1550 0.4080 0.0032  0.0082  -0.0022 137 ILE   B CG1 
5994 C  CG2 . ILE   B 137 ? 0.2187 0.1431 0.3725 -0.0242 -0.0018 0.0064  137 ILE   B CG2 
5995 C  CD1 . ILE   B 137 ? 0.2707 0.1797 0.4484 0.0195  0.0132  0.0063  137 ILE   B CD1 
6007 N  N   . HIS   B 138 ? 0.1958 0.1373 0.2895 -0.0047 0.0188  0.0200  138 HIS   B N   
6008 C  CA  . HIS   B 138 ? 0.2072 0.1448 0.2803 -0.0009 0.0257  0.0207  138 HIS   B CA  
6009 C  C   . HIS   B 138 ? 0.1918 0.1407 0.2696 -0.0049 0.0242  0.0212  138 HIS   B C   
6010 O  O   . HIS   B 138 ? 0.1788 0.1460 0.2931 0.0008  0.0281  0.0314  138 HIS   B O   
6011 C  CB  . HIS   B 138 ? 0.2318 0.1582 0.2957 -0.0076 0.0416  0.0135  138 HIS   B CB  
6012 C  CG  . HIS   B 138 ? 0.2488 0.1770 0.2923 -0.0132 0.0575  0.0327  138 HIS   B CG  
6013 N  ND1 . HIS   B 138 ? 0.2578 0.1982 0.3106 -0.0109 0.0704  0.0291  138 HIS   B ND1 
6014 C  CD2 . HIS   B 138 ? 0.2602 0.1896 0.2899 -0.0090 0.0653  0.0304  138 HIS   B CD2 
6015 C  CE1 . HIS   B 138 ? 0.2621 0.1998 0.3117 -0.0109 0.0799  0.0275  138 HIS   B CE1 
6016 N  NE2 . HIS   B 138 ? 0.2650 0.1895 0.2970 -0.0012 0.0789  0.0227  138 HIS   B NE2 
6024 N  N   . SER   B 139 ? 0.1877 0.1319 0.2637 0.0018  0.0194  0.0160  139 SER   B N   
6025 C  CA  . SER   B 139 ? 0.1816 0.1271 0.2438 -0.0022 0.0233  -0.0012 139 SER   B CA  
6026 C  C   . SER   B 139 ? 0.1592 0.1212 0.2517 -0.0039 0.0127  0.0046  139 SER   B C   
6027 O  O   . SER   B 139 ? 0.1525 0.1202 0.2549 -0.0001 -0.0006 0.0099  139 SER   B O   
6028 C  CB  . SER   B 139 ? 0.1870 0.1269 0.2513 0.0023  0.0063  0.0028  139 SER   B CB  
6029 O  OG  . SER   B 139 ? 0.1898 0.1273 0.2563 -0.0014 -0.0061 0.0139  139 SER   B OG  
6035 N  N   . LEU   B 140 ? 0.1580 0.1148 0.2329 -0.0068 0.0086  0.0052  140 LEU   B N   
6036 C  CA  . LEU   B 140 ? 0.1535 0.1226 0.2365 -0.0037 0.0066  0.0027  140 LEU   B CA  
6037 C  C   . LEU   B 140 ? 0.1509 0.1235 0.2507 -0.0051 -0.0088 0.0015  140 LEU   B C   
6038 O  O   . LEU   B 140 ? 0.1480 0.1306 0.2511 -0.0043 -0.0105 0.0068  140 LEU   B O   
6039 C  CB  . LEU   B 140 ? 0.1489 0.1229 0.2380 -0.0096 0.0072  -0.0102 140 LEU   B CB  
6040 C  CG  . LEU   B 140 ? 0.1610 0.1260 0.2315 -0.0109 -0.0065 0.0018  140 LEU   B CG  
6041 C  CD1 . LEU   B 140 ? 0.1712 0.1343 0.2579 -0.0109 0.0022  -0.0008 140 LEU   B CD1 
6042 C  CD2 . LEU   B 140 ? 0.1816 0.1392 0.2363 -0.0127 -0.0142 -0.0074 140 LEU   B CD2 
6054 N  N   . ARG   B 141 ? 0.1458 0.1222 0.2716 -0.0144 -0.0009 -0.0093 141 ARG   B N   
6055 C  CA  . ARG   B 141 ? 0.1461 0.1251 0.3014 -0.0146 0.0122  -0.0032 141 ARG   B CA  
6056 C  C   . ARG   B 141 ? 0.1407 0.1274 0.2807 -0.0120 0.0058  -0.0022 141 ARG   B C   
6057 O  O   . ARG   B 141 ? 0.1447 0.1288 0.2866 -0.0142 -0.0012 -0.0096 141 ARG   B O   
6058 C  CB  . ARG   B 141 ? 0.1634 0.1398 0.3352 -0.0164 0.0311  -0.0036 141 ARG   B CB  
6059 C  CG  . ARG   B 141 ? 0.1936 0.1623 0.3537 -0.0177 0.0370  -0.0033 141 ARG   B CG  
6060 C  CD  . ARG   B 141 ? 0.2390 0.1869 0.3523 -0.0141 0.0316  -0.0191 141 ARG   B CD  
6061 N  NE  . ARG   B 141 ? 0.2628 0.1901 0.3469 -0.0329 0.0388  -0.0275 141 ARG   B NE  
6062 C  CZ  . ARG   B 141 ? 0.2775 0.1749 0.3322 -0.0349 0.0460  -0.0328 141 ARG   B CZ  
6063 N  NH1 . ARG   B 141 ? 0.2878 0.1620 0.3311 -0.0394 0.0416  -0.0318 141 ARG   B NH1 
6064 N  NH2 . ARG   B 141 ? 0.2895 0.1858 0.3440 -0.0223 0.0335  -0.0265 141 ARG   B NH2 
6078 N  N   . VAL   B 142 ? 0.1460 0.1235 0.2659 -0.0062 0.0101  -0.0035 142 VAL   B N   
6079 C  CA  . VAL   B 142 ? 0.1437 0.1276 0.2620 -0.0087 0.0117  -0.0038 142 VAL   B CA  
6080 C  C   . VAL   B 142 ? 0.1430 0.1252 0.2679 -0.0038 0.0030  -0.0032 142 VAL   B C   
6081 O  O   . VAL   B 142 ? 0.1488 0.1244 0.2818 -0.0009 0.0040  -0.0007 142 VAL   B O   
6082 C  CB  . VAL   B 142 ? 0.1566 0.1348 0.2669 0.0011  0.0170  0.0059  142 VAL   B CB  
6083 C  CG1 . VAL   B 142 ? 0.1623 0.1343 0.2700 0.0074  0.0172  0.0022  142 VAL   B CG1 
6084 C  CG2 . VAL   B 142 ? 0.1695 0.1415 0.2783 0.0042  0.0076  0.0071  142 VAL   B CG2 
6094 N  N   . CYS   B 143 ? 0.1378 0.1274 0.2605 -0.0049 0.0027  0.0067  143 CYS   B N   
6095 C  CA  . CYS   B 143 ? 0.1363 0.1254 0.2634 -0.0048 -0.0038 0.0034  143 CYS   B CA  
6096 C  C   . CYS   B 143 ? 0.1321 0.1261 0.2621 -0.0060 -0.0014 0.0001  143 CYS   B C   
6097 O  O   . CYS   B 143 ? 0.1401 0.1288 0.2535 -0.0068 -0.0059 -0.0020 143 CYS   B O   
6098 C  CB  . CYS   B 143 ? 0.1445 0.1344 0.2531 -0.0066 -0.0026 0.0016  143 CYS   B CB  
6099 S  SG  . CYS   B 143 ? 0.1450 0.1478 0.2474 -0.0042 -0.0011 0.0053  143 CYS   B SG  
6105 N  N   . VAL   B 144 ? 0.1387 0.1289 0.2796 -0.0072 -0.0025 -0.0082 144 VAL   B N   
6106 C  CA  . VAL   B 144 ? 0.1442 0.1390 0.2999 -0.0105 -0.0134 -0.0167 144 VAL   B CA  
6107 C  C   . VAL   B 144 ? 0.1409 0.1421 0.3070 -0.0093 -0.0140 0.0011  144 VAL   B C   
6108 O  O   . VAL   B 144 ? 0.1519 0.1603 0.3196 0.0012  -0.0137 0.0207  144 VAL   B O   
6109 C  CB  . VAL   B 144 ? 0.1668 0.1568 0.3448 -0.0112 -0.0208 -0.0256 144 VAL   B CB  
6110 C  CG1 . VAL   B 144 ? 0.1879 0.1966 0.3604 -0.0006 -0.0275 -0.0177 144 VAL   B CG1 
6111 C  CG2 . VAL   B 144 ? 0.1780 0.1486 0.3440 -0.0032 -0.0310 -0.0369 144 VAL   B CG2 
6121 N  N   . ASP   B 145 ? 0.1433 0.1314 0.3121 -0.0069 -0.0079 -0.0183 145 ASP   B N   
6122 C  CA  . ASP   B 145 ? 0.1430 0.1413 0.3265 -0.0039 0.0031  -0.0062 145 ASP   B CA  
6123 C  C   . ASP   B 145 ? 0.1415 0.1412 0.3128 -0.0045 0.0022  -0.0052 145 ASP   B C   
6124 O  O   . ASP   B 145 ? 0.1428 0.1536 0.3533 -0.0091 0.0070  -0.0221 145 ASP   B O   
6125 C  CB  . ASP   B 145 ? 0.1481 0.1488 0.3725 -0.0130 0.0184  -0.0110 145 ASP   B CB  
6126 C  CG  . ASP   B 145 ? 0.1631 0.1484 0.4210 -0.0236 0.0215  -0.0101 145 ASP   B CG  
6127 O  OD1 . ASP   B 145 ? 0.1706 0.1505 0.4279 -0.0216 -0.0162 -0.0222 145 ASP   B OD1 
6128 O  OD2 . ASP   B 145 ? 0.1995 0.1534 0.4622 -0.0264 0.0512  -0.0025 145 ASP   B OD2 
6133 N  N   . THR   B 146 ? 0.1356 0.1248 0.2648 -0.0081 -0.0043 0.0045  146 THR   B N   
6134 C  CA  . THR   B 146 ? 0.1408 0.1252 0.2493 -0.0072 0.0020  -0.0002 146 THR   B CA  
6135 C  C   . THR   B 146 ? 0.1411 0.1265 0.2387 -0.0061 -0.0007 -0.0005 146 THR   B C   
6136 O  O   . THR   B 146 ? 0.1457 0.1240 0.2458 -0.0027 -0.0054 0.0015  146 THR   B O   
6137 C  CB  . THR   B 146 ? 0.1483 0.1258 0.2578 -0.0005 0.0105  -0.0004 146 THR   B CB  
6138 O  OG1 . THR   B 146 ? 0.1510 0.1216 0.2630 -0.0083 0.0165  0.0120  146 THR   B OG1 
6139 C  CG2 . THR   B 146 ? 0.1538 0.1331 0.2467 0.0009  0.0094  -0.0047 146 THR   B CG2 
6147 N  N   . VAL   B 147 ? 0.1434 0.1288 0.2337 -0.0061 0.0011  -0.0025 147 VAL   B N   
6148 C  CA  . VAL   B 147 ? 0.1436 0.1292 0.2231 -0.0117 -0.0094 0.0018  147 VAL   B CA  
6149 C  C   . VAL   B 147 ? 0.1394 0.1266 0.2327 -0.0147 -0.0110 -0.0062 147 VAL   B C   
6150 O  O   . VAL   B 147 ? 0.1522 0.1370 0.2459 -0.0191 -0.0303 -0.0129 147 VAL   B O   
6151 C  CB  . VAL   B 147 ? 0.1474 0.1405 0.2095 -0.0088 -0.0125 0.0010  147 VAL   B CB  
6152 C  CG1 . VAL   B 147 ? 0.1456 0.1536 0.1977 -0.0164 -0.0065 0.0060  147 VAL   B CG1 
6153 C  CG2 . VAL   B 147 ? 0.1463 0.1453 0.2104 -0.0109 -0.0010 0.0020  147 VAL   B CG2 
6163 N  N   . ARG   B 148 ? 0.1405 0.1279 0.2276 -0.0068 -0.0216 -0.0117 148 ARG   B N   
6164 C  CA  . ARG   B 148 ? 0.1447 0.1467 0.2170 -0.0050 -0.0286 -0.0115 148 ARG   B CA  
6165 C  C   . ARG   B 148 ? 0.1498 0.1511 0.2125 -0.0066 -0.0324 -0.0102 148 ARG   B C   
6166 O  O   . ARG   B 148 ? 0.1686 0.1796 0.2290 -0.0227 -0.0448 -0.0076 148 ARG   B O   
6167 C  CB  . ARG   B 148 ? 0.1477 0.1522 0.2204 -0.0030 -0.0358 -0.0200 148 ARG   B CB  
6168 C  CG  . ARG   B 148 ? 0.1495 0.1657 0.2368 -0.0058 -0.0318 -0.0336 148 ARG   B CG  
6169 C  CD  . ARG   B 148 ? 0.1537 0.1779 0.2434 0.0048  -0.0393 -0.0351 148 ARG   B CD  
6170 N  NE  . ARG   B 148 ? 0.1619 0.1790 0.2372 0.0219  -0.0349 -0.0295 148 ARG   B NE  
6171 C  CZ  . ARG   B 148 ? 0.1530 0.1663 0.2254 0.0116  -0.0270 -0.0256 148 ARG   B CZ  
6172 N  NH1 . ARG   B 148 ? 0.1505 0.1655 0.2356 -0.0035 -0.0073 -0.0151 148 ARG   B NH1 
6173 N  NH2 . ARG   B 148 ? 0.1761 0.1529 0.2179 0.0165  -0.0223 -0.0181 148 ARG   B NH2 
6187 N  N   . THR   B 149 ? 0.1488 0.1421 0.2102 -0.0070 -0.0267 -0.0046 149 THR   B N   
6188 C  CA  . THR   B 149 ? 0.1568 0.1463 0.1952 -0.0112 -0.0240 -0.0008 149 THR   B CA  
6189 C  C   . THR   B 149 ? 0.1570 0.1430 0.1892 -0.0127 -0.0308 -0.0056 149 THR   B C   
6190 O  O   . THR   B 149 ? 0.1605 0.1376 0.2053 -0.0172 -0.0209 0.0053  149 THR   B O   
6191 C  CB  . THR   B 149 ? 0.1607 0.1421 0.1954 -0.0141 -0.0316 -0.0016 149 THR   B CB  
6192 O  OG1 . THR   B 149 ? 0.1628 0.1491 0.1963 -0.0221 -0.0318 -0.0001 149 THR   B OG1 
6193 C  CG2 . THR   B 149 ? 0.1721 0.1448 0.2135 -0.0045 -0.0275 -0.0040 149 THR   B CG2 
6201 N  N   . ASN   B 150 ? 0.1654 0.1441 0.1868 -0.0164 -0.0349 -0.0071 150 ASN   B N   
6202 C  CA  . ASN   B 150 ? 0.1708 0.1554 0.1839 -0.0195 -0.0312 -0.0046 150 ASN   B CA  
6203 C  C   . ASN   B 150 ? 0.1574 0.1513 0.1887 -0.0177 -0.0284 -0.0032 150 ASN   B C   
6204 O  O   . ASN   B 150 ? 0.1666 0.1471 0.2017 -0.0249 -0.0366 -0.0058 150 ASN   B O   
6205 C  CB  . ASN   B 150 ? 0.1953 0.1901 0.1923 -0.0192 -0.0380 0.0075  150 ASN   B CB  
6206 C  CG  . ASN   B 150 ? 0.2225 0.2315 0.2238 -0.0184 -0.0436 0.0294  150 ASN   B CG  
6207 O  OD1 . ASN   B 150 ? 0.2302 0.2477 0.2410 -0.0259 -0.0633 0.0253  150 ASN   B OD1 
6208 N  ND2 . ASN   B 150 ? 0.2320 0.2462 0.2527 -0.0037 -0.0378 0.0611  150 ASN   B ND2 
6215 N  N   . VAL   B 151 ? 0.1511 0.1494 0.1841 -0.0175 -0.0316 -0.0036 151 VAL   B N   
6216 C  CA  . VAL   B 151 ? 0.1554 0.1439 0.1828 -0.0223 -0.0241 -0.0027 151 VAL   B CA  
6217 C  C   . VAL   B 151 ? 0.1572 0.1394 0.1874 -0.0299 -0.0322 -0.0033 151 VAL   B C   
6218 O  O   . VAL   B 151 ? 0.1697 0.1464 0.2058 -0.0288 -0.0299 -0.0059 151 VAL   B O   
6219 C  CB  . VAL   B 151 ? 0.1791 0.1624 0.1960 -0.0063 -0.0215 -0.0047 151 VAL   B CB  
6220 C  CG1 . VAL   B 151 ? 0.1906 0.1663 0.2136 -0.0161 -0.0174 -0.0107 151 VAL   B CG1 
6221 C  CG2 . VAL   B 151 ? 0.1950 0.1715 0.1814 0.0071  -0.0255 0.0027  151 VAL   B CG2 
6231 N  N   . TYR   B 152 ? 0.1559 0.1298 0.1824 -0.0232 -0.0301 -0.0049 152 TYR   B N   
6232 C  CA  . TYR   B 152 ? 0.1580 0.1444 0.1682 -0.0251 -0.0201 -0.0118 152 TYR   B CA  
6233 C  C   . TYR   B 152 ? 0.1551 0.1344 0.1635 -0.0193 -0.0181 -0.0097 152 TYR   B C   
6234 O  O   . TYR   B 152 ? 0.1574 0.1363 0.1719 -0.0219 -0.0205 -0.0031 152 TYR   B O   
6235 C  CB  . TYR   B 152 ? 0.1689 0.1593 0.1728 -0.0263 -0.0195 0.0045  152 TYR   B CB  
6236 C  CG  . TYR   B 152 ? 0.1826 0.1713 0.1693 -0.0333 -0.0214 0.0029  152 TYR   B CG  
6237 C  CD1 . TYR   B 152 ? 0.1953 0.1862 0.1632 -0.0276 -0.0307 0.0027  152 TYR   B CD1 
6238 C  CD2 . TYR   B 152 ? 0.2049 0.1862 0.1742 -0.0334 -0.0130 -0.0014 152 TYR   B CD2 
6239 C  CE1 . TYR   B 152 ? 0.2119 0.2014 0.1725 -0.0292 -0.0284 0.0106  152 TYR   B CE1 
6240 C  CE2 . TYR   B 152 ? 0.2157 0.2126 0.1785 -0.0333 -0.0204 -0.0064 152 TYR   B CE2 
6241 C  CZ  . TYR   B 152 ? 0.2183 0.2239 0.1616 -0.0339 -0.0468 0.0142  152 TYR   B CZ  
6242 O  OH  . TYR   B 152 ? 0.2411 0.2573 0.1962 -0.0222 -0.0440 0.0237  152 TYR   B OH  
6252 N  N   . LEU   B 153 ? 0.1539 0.1306 0.1748 -0.0246 -0.0166 -0.0018 153 LEU   B N   
6253 C  CA  . LEU   B 153 ? 0.1555 0.1261 0.1572 -0.0185 -0.0127 -0.0096 153 LEU   B CA  
6254 C  C   . LEU   B 153 ? 0.1613 0.1271 0.1709 -0.0210 -0.0054 -0.0153 153 LEU   B C   
6255 O  O   . LEU   B 153 ? 0.1690 0.1448 0.1885 -0.0145 -0.0144 -0.0303 153 LEU   B O   
6256 C  CB  . LEU   B 153 ? 0.1555 0.1281 0.1712 -0.0229 -0.0103 -0.0033 153 LEU   B CB  
6257 C  CG  . LEU   B 153 ? 0.1577 0.1422 0.2006 -0.0248 -0.0093 -0.0026 153 LEU   B CG  
6258 C  CD1 . LEU   B 153 ? 0.1606 0.1540 0.2133 -0.0231 -0.0069 0.0093  153 LEU   B CD1 
6259 C  CD2 . LEU   B 153 ? 0.1606 0.1539 0.2077 -0.0254 0.0014  0.0046  153 LEU   B CD2 
6271 N  N   . ALA   B 154 ? 0.1506 0.1307 0.1871 -0.0091 -0.0151 -0.0083 154 ALA   B N   
6272 C  CA  . ALA   B 154 ? 0.1633 0.1410 0.2167 0.0018  -0.0164 -0.0148 154 ALA   B CA  
6273 C  C   . ALA   B 154 ? 0.1733 0.1458 0.2157 0.0064  -0.0255 -0.0153 154 ALA   B C   
6274 O  O   . ALA   B 154 ? 0.2040 0.1463 0.2276 0.0045  -0.0117 -0.0081 154 ALA   B O   
6275 C  CB  . ALA   B 154 ? 0.1547 0.1546 0.2360 -0.0021 -0.0141 -0.0243 154 ALA   B CB  
6281 N  N   . VAL   B 155 ? 0.1441 0.1350 0.2248 -0.0023 -0.0005 -0.0083 155 VAL   B N   
6282 C  CA  . VAL   B 155 ? 0.1397 0.1345 0.2344 -0.0001 -0.0151 -0.0082 155 VAL   B CA  
6283 C  C   . VAL   B 155 ? 0.1455 0.1357 0.2194 -0.0033 -0.0184 -0.0180 155 VAL   B C   
6284 O  O   . VAL   B 155 ? 0.1696 0.1553 0.2459 0.0062  -0.0176 -0.0332 155 VAL   B O   
6285 C  CB  . VAL   B 155 ? 0.1473 0.1502 0.2721 -0.0059 -0.0222 0.0065  155 VAL   B CB  
6286 C  CG1 . VAL   B 155 ? 0.1520 0.1437 0.2663 -0.0146 -0.0144 -0.0043 155 VAL   B CG1 
6287 C  CG2 . VAL   B 155 ? 0.1420 0.1639 0.2975 -0.0059 -0.0122 0.0309  155 VAL   B CG2 
6297 N  N   . PHE   B 156 ? 0.1391 0.1457 0.2458 0.0006  -0.0128 -0.0096 156 PHE   B N   
6298 C  CA  . PHE   B 156 ? 0.1398 0.1521 0.2842 0.0036  -0.0137 -0.0131 156 PHE   B CA  
6299 C  C   . PHE   B 156 ? 0.1372 0.1620 0.3118 0.0060  -0.0126 -0.0286 156 PHE   B C   
6300 O  O   . PHE   B 156 ? 0.1640 0.1810 0.3356 0.0227  -0.0021 -0.0367 156 PHE   B O   
6301 C  CB  . PHE   B 156 ? 0.1498 0.1489 0.2813 0.0008  -0.0198 -0.0004 156 PHE   B CB  
6302 C  CG  . PHE   B 156 ? 0.1474 0.1623 0.2903 0.0004  -0.0158 0.0161  156 PHE   B CG  
6303 C  CD1 . PHE   B 156 ? 0.1503 0.1863 0.3245 0.0024  -0.0093 0.0462  156 PHE   B CD1 
6304 C  CD2 . PHE   B 156 ? 0.1516 0.1780 0.2961 0.0070  -0.0196 0.0202  156 PHE   B CD2 
6305 C  CE1 . PHE   B 156 ? 0.1568 0.2033 0.3461 0.0011  -0.0083 0.0440  156 PHE   B CE1 
6306 C  CE2 . PHE   B 156 ? 0.1559 0.1932 0.3161 0.0113  -0.0201 0.0183  156 PHE   B CE2 
6307 C  CZ  . PHE   B 156 ? 0.1520 0.2028 0.3392 0.0139  -0.0217 0.0307  156 PHE   B CZ  
6317 N  N   . ASP   B 157 ? 0.1402 0.1518 0.3317 0.0090  -0.0270 -0.0085 157 ASP   B N   
6318 C  CA  . ASP   B 157 ? 0.1450 0.1582 0.3631 0.0080  -0.0317 -0.0136 157 ASP   B CA  
6319 C  C   . ASP   B 157 ? 0.1530 0.1524 0.3718 0.0079  -0.0273 -0.0360 157 ASP   B C   
6320 O  O   . ASP   B 157 ? 0.1479 0.1531 0.3563 0.0050  -0.0250 -0.0345 157 ASP   B O   
6321 C  CB  . ASP   B 157 ? 0.1773 0.1803 0.3778 -0.0010 -0.0491 -0.0024 157 ASP   B CB  
6322 C  CG  . ASP   B 157 ? 0.2122 0.1902 0.3996 -0.0079 -0.0412 -0.0076 157 ASP   B CG  
6323 O  OD1 . ASP   B 157 ? 0.2240 0.1808 0.4137 0.0005  -0.0392 -0.0040 157 ASP   B OD1 
6324 O  OD2 . ASP   B 157 ? 0.2417 0.2103 0.4197 -0.0077 -0.0260 -0.0060 157 ASP   B OD2 
6329 N  N   . LYS   B 158 ? 0.1568 0.1791 0.3884 0.0071  -0.0137 -0.0679 158 LYS   B N   
6330 C  CA  . LYS   B 158 ? 0.1744 0.1928 0.4004 0.0044  -0.0008 -0.0896 158 LYS   B CA  
6331 C  C   . LYS   B 158 ? 0.1719 0.1781 0.4098 0.0048  -0.0063 -0.0840 158 LYS   B C   
6332 O  O   . LYS   B 158 ? 0.1743 0.1816 0.4051 -0.0081 -0.0019 -0.0887 158 LYS   B O   
6333 C  CB  . LYS   B 158 ? 0.1971 0.2356 0.4007 0.0034  0.0140  -0.1084 158 LYS   B CB  
6334 C  CG  . LYS   B 158 ? 0.2318 0.2776 0.4087 0.0009  0.0157  -0.1179 158 LYS   B CG  
6335 C  CD  . LYS   B 158 ? 0.2570 0.3236 0.4231 -0.0031 0.0194  -0.1111 158 LYS   B CD  
6336 C  CE  . LYS   B 158 ? 0.2742 0.3489 0.4382 -0.0011 0.0170  -0.1045 158 LYS   B CE  
6337 N  NZ  . LYS   B 158 ? 0.2743 0.3658 0.4366 -0.0053 0.0149  -0.1016 158 LYS   B NZ  
6351 N  N   . ASN   B 159 ? 0.1754 0.1684 0.4334 0.0062  -0.0163 -0.0662 159 ASN   B N   
6352 C  CA  . ASN   B 159 ? 0.1834 0.1625 0.4529 0.0141  -0.0359 -0.0484 159 ASN   B CA  
6353 C  C   . ASN   B 159 ? 0.1696 0.1534 0.4313 0.0116  -0.0414 -0.0368 159 ASN   B C   
6354 O  O   . ASN   B 159 ? 0.1703 0.1467 0.4391 -0.0016 -0.0487 -0.0250 159 ASN   B O   
6355 C  CB  . ASN   B 159 ? 0.2034 0.1787 0.4984 0.0194  -0.0403 -0.0388 159 ASN   B CB  
6356 C  CG  . ASN   B 159 ? 0.2301 0.2000 0.5326 0.0197  -0.0462 -0.0581 159 ASN   B CG  
6357 O  OD1 . ASN   B 159 ? 0.2458 0.2098 0.5369 0.0264  -0.0499 -0.0672 159 ASN   B OD1 
6358 N  ND2 . ASN   B 159 ? 0.2325 0.2087 0.5481 0.0258  -0.0461 -0.0586 159 ASN   B ND2 
6365 N  N   . LEU   B 160 ? 0.1620 0.1472 0.3995 0.0061  -0.0410 -0.0314 160 LEU   B N   
6366 C  CA  . LEU   B 160 ? 0.1583 0.1515 0.3577 0.0065  -0.0391 -0.0197 160 LEU   B CA  
6367 C  C   . LEU   B 160 ? 0.1528 0.1423 0.3401 -0.0001 -0.0316 -0.0305 160 LEU   B C   
6368 O  O   . LEU   B 160 ? 0.1454 0.1457 0.3327 -0.0039 -0.0329 -0.0221 160 LEU   B O   
6369 C  CB  . LEU   B 160 ? 0.1570 0.1620 0.3396 0.0027  -0.0356 -0.0091 160 LEU   B CB  
6370 C  CG  . LEU   B 160 ? 0.1586 0.1781 0.3201 0.0076  -0.0372 -0.0014 160 LEU   B CG  
6371 C  CD1 . LEU   B 160 ? 0.1745 0.1942 0.3245 -0.0033 -0.0216 0.0058  160 LEU   B CD1 
6372 C  CD2 . LEU   B 160 ? 0.1631 0.1810 0.3076 0.0132  -0.0372 -0.0103 160 LEU   B CD2 
6384 N  N   . TYR   B 161 ? 0.1451 0.1534 0.3449 -0.0039 -0.0064 -0.0404 161 TYR   B N   
6385 C  CA  . TYR   B 161 ? 0.1551 0.1476 0.3310 -0.0119 0.0053  -0.0440 161 TYR   B CA  
6386 C  C   . TYR   B 161 ? 0.1642 0.1502 0.3238 -0.0126 0.0117  -0.0369 161 TYR   B C   
6387 O  O   . TYR   B 161 ? 0.1711 0.1500 0.3106 -0.0181 -0.0027 -0.0329 161 TYR   B O   
6388 C  CB  . TYR   B 161 ? 0.1741 0.1591 0.3329 -0.0220 0.0282  -0.0468 161 TYR   B CB  
6389 C  CG  . TYR   B 161 ? 0.2023 0.1670 0.3262 -0.0261 0.0359  -0.0585 161 TYR   B CG  
6390 C  CD1 . TYR   B 161 ? 0.2070 0.1630 0.3214 -0.0394 0.0408  -0.0597 161 TYR   B CD1 
6391 C  CD2 . TYR   B 161 ? 0.2230 0.1744 0.3201 -0.0273 0.0296  -0.0614 161 TYR   B CD2 
6392 C  CE1 . TYR   B 161 ? 0.2283 0.1817 0.3171 -0.0423 0.0444  -0.0581 161 TYR   B CE1 
6393 C  CE2 . TYR   B 161 ? 0.2451 0.1932 0.3217 -0.0319 0.0324  -0.0653 161 TYR   B CE2 
6394 C  CZ  . TYR   B 161 ? 0.2450 0.1957 0.3194 -0.0455 0.0329  -0.0559 161 TYR   B CZ  
6395 O  OH  . TYR   B 161 ? 0.2718 0.2148 0.3405 -0.0451 0.0298  -0.0520 161 TYR   B OH  
6405 N  N   . ASP   B 162 ? 0.1703 0.1499 0.3338 -0.0105 0.0023  -0.0525 162 ASP   B N   
6406 C  CA  . ASP   B 162 ? 0.1818 0.1567 0.3443 -0.0071 -0.0030 -0.0519 162 ASP   B CA  
6407 C  C   . ASP   B 162 ? 0.1772 0.1442 0.3360 -0.0097 -0.0110 -0.0396 162 ASP   B C   
6408 O  O   . ASP   B 162 ? 0.1827 0.1506 0.3374 -0.0168 -0.0272 -0.0308 162 ASP   B O   
6409 C  CB  . ASP   B 162 ? 0.1993 0.1705 0.3623 -0.0011 -0.0105 -0.0747 162 ASP   B CB  
6410 C  CG  . ASP   B 162 ? 0.2086 0.1986 0.3914 0.0072  -0.0095 -0.0854 162 ASP   B CG  
6411 O  OD1 . ASP   B 162 ? 0.2103 0.2202 0.3882 -0.0003 0.0028  -0.0843 162 ASP   B OD1 
6412 O  OD2 . ASP   B 162 ? 0.2241 0.2213 0.4172 0.0236  -0.0042 -0.0815 162 ASP   B OD2 
6417 N  N   A LYS   B 163 ? 0.1762 0.1321 0.3244 -0.0080 -0.0271 -0.0317 163 LYS   B N   
6418 N  N   B LYS   B 163 ? 0.1789 0.1429 0.3269 -0.0103 -0.0236 -0.0290 163 LYS   B N   
6419 C  CA  A LYS   B 163 ? 0.1848 0.1412 0.3234 -0.0175 -0.0286 -0.0148 163 LYS   B CA  
6420 C  CA  B LYS   B 163 ? 0.1876 0.1555 0.3249 -0.0183 -0.0256 -0.0136 163 LYS   B CA  
6421 C  C   A LYS   B 163 ? 0.1565 0.1380 0.3080 -0.0142 -0.0255 -0.0046 163 LYS   B C   
6422 C  C   B LYS   B 163 ? 0.1596 0.1446 0.3085 -0.0152 -0.0254 -0.0039 163 LYS   B C   
6423 O  O   A LYS   B 163 ? 0.1515 0.1481 0.3228 -0.0144 -0.0280 -0.0062 163 LYS   B O   
6424 O  O   B LYS   B 163 ? 0.1556 0.1525 0.3196 -0.0155 -0.0294 -0.0016 163 LYS   B O   
6425 C  CB  A LYS   B 163 ? 0.2218 0.1720 0.3504 -0.0195 -0.0317 -0.0048 163 LYS   B CB  
6426 C  CB  B LYS   B 163 ? 0.2233 0.1904 0.3496 -0.0219 -0.0280 -0.0053 163 LYS   B CB  
6427 C  CG  A LYS   B 163 ? 0.2747 0.2316 0.3870 -0.0214 -0.0254 0.0014  163 LYS   B CG  
6428 C  CG  B LYS   B 163 ? 0.2691 0.2395 0.3815 -0.0246 -0.0247 -0.0005 163 LYS   B CG  
6429 C  CD  A LYS   B 163 ? 0.3252 0.2776 0.4258 -0.0298 -0.0208 -0.0048 163 LYS   B CD  
6430 C  CD  B LYS   B 163 ? 0.3128 0.2817 0.4179 -0.0315 -0.0222 -0.0036 163 LYS   B CD  
6431 C  CE  A LYS   B 163 ? 0.3564 0.3126 0.4511 -0.0338 -0.0141 -0.0048 163 LYS   B CE  
6432 C  CE  B LYS   B 163 ? 0.3406 0.3146 0.4444 -0.0360 -0.0173 -0.0042 163 LYS   B CE  
6433 N  NZ  A LYS   B 163 ? 0.3774 0.3299 0.4671 -0.0363 -0.0110 -0.0095 163 LYS   B NZ  
6434 N  NZ  B LYS   B 163 ? 0.3576 0.3262 0.4601 -0.0387 -0.0152 -0.0068 163 LYS   B NZ  
6461 N  N   . LEU   B 164 ? 0.1417 0.1339 0.2950 -0.0131 -0.0254 -0.0058 164 LEU   B N   
6462 C  CA  . LEU   B 164 ? 0.1495 0.1345 0.2850 -0.0111 -0.0268 -0.0032 164 LEU   B CA  
6463 C  C   . LEU   B 164 ? 0.1564 0.1386 0.2886 -0.0135 -0.0367 -0.0039 164 LEU   B C   
6464 O  O   . LEU   B 164 ? 0.1505 0.1599 0.3077 -0.0168 -0.0419 -0.0048 164 LEU   B O   
6465 C  CB  . LEU   B 164 ? 0.1484 0.1335 0.2625 -0.0142 -0.0158 -0.0007 164 LEU   B CB  
6466 C  CG  . LEU   B 164 ? 0.1549 0.1494 0.2701 -0.0127 -0.0114 0.0014  164 LEU   B CG  
6467 C  CD1 . LEU   B 164 ? 0.1588 0.1470 0.2626 -0.0136 -0.0287 -0.0061 164 LEU   B CD1 
6468 C  CD2 . LEU   B 164 ? 0.1681 0.1864 0.2870 -0.0149 0.0054  -0.0176 164 LEU   B CD2 
6481 N  N   . VAL   B 165 ? 0.1899 0.1433 0.2969 -0.0201 -0.0364 -0.0132 165 VAL   B N   
6482 C  CA  . VAL   B 165 ? 0.2218 0.1549 0.2958 -0.0238 -0.0540 -0.0053 165 VAL   B CA  
6483 C  C   . VAL   B 165 ? 0.2445 0.1641 0.3277 -0.0374 -0.0827 -0.0078 165 VAL   B C   
6484 O  O   . VAL   B 165 ? 0.2601 0.1797 0.3366 -0.0430 -0.0842 -0.0001 165 VAL   B O   
6485 C  CB  . VAL   B 165 ? 0.2436 0.1765 0.2933 -0.0119 -0.0248 -0.0181 165 VAL   B CB  
6486 C  CG1 . VAL   B 165 ? 0.2609 0.1908 0.3246 -0.0153 -0.0168 -0.0183 165 VAL   B CG1 
6487 C  CG2 . VAL   B 165 ? 0.2385 0.1759 0.2718 -0.0074 -0.0140 -0.0188 165 VAL   B CG2 
6497 N  N   . SER   B 166 ? 0.2493 0.1551 0.3687 -0.0340 -0.0948 -0.0250 166 SER   B N   
6498 C  CA  . SER   B 166 ? 0.2464 0.1619 0.4265 -0.0358 -0.0894 -0.0312 166 SER   B CA  
6499 C  C   . SER   B 166 ? 0.2324 0.1714 0.4428 -0.0386 -0.0902 -0.0080 166 SER   B C   
6500 O  O   . SER   B 166 ? 0.2394 0.1941 0.4681 -0.0516 -0.0982 -0.0247 166 SER   B O   
6501 C  CB  . SER   B 166 ? 0.2471 0.1696 0.4506 -0.0251 -0.0859 -0.0393 166 SER   B CB  
6502 O  OG  . SER   B 166 ? 0.2320 0.1629 0.4622 -0.0175 -0.0900 -0.0217 166 SER   B OG  
6508 N  N   . SER   B 167 ? 0.2107 0.1632 0.4184 -0.0428 -0.0881 0.0330  167 SER   B N   
6509 C  CA  . SER   B 167 ? 0.2000 0.1714 0.4013 -0.0366 -0.0634 0.0288  167 SER   B CA  
6510 C  C   . SER   B 167 ? 0.1954 0.1750 0.3703 -0.0492 -0.0583 0.0411  167 SER   B C   
6511 O  O   . SER   B 167 ? 0.1982 0.1850 0.3641 -0.0509 -0.0540 0.0348  167 SER   B O   
6512 C  CB  . SER   B 167 ? 0.1887 0.1793 0.4072 -0.0294 -0.0319 0.0172  167 SER   B CB  
6513 O  OG  . SER   B 167 ? 0.1794 0.1855 0.3976 -0.0150 -0.0141 0.0178  167 SER   B OG  
6519 N  N   . PHE   B 168 ? 0.1967 0.1751 0.3559 -0.0430 -0.0483 0.0513  168 PHE   B N   
6520 C  CA  . PHE   B 168 ? 0.2033 0.1733 0.3254 -0.0470 -0.0396 0.0340  168 PHE   B CA  
6521 C  C   . PHE   B 168 ? 0.1757 0.1653 0.2813 -0.0259 -0.0167 0.0139  168 PHE   B C   
6522 O  O   . PHE   B 168 ? 0.2034 0.1587 0.2872 -0.0054 -0.0184 -0.0022 168 PHE   B O   
6523 C  CB  . PHE   B 168 ? 0.2229 0.1756 0.3313 -0.0535 -0.0534 0.0434  168 PHE   B CB  
6524 C  CG  . PHE   B 168 ? 0.2481 0.1643 0.3234 -0.0547 -0.0580 0.0177  168 PHE   B CG  
6525 C  CD1 . PHE   B 168 ? 0.2789 0.1664 0.3319 -0.0504 -0.0558 0.0173  168 PHE   B CD1 
6526 C  CD2 . PHE   B 168 ? 0.2388 0.1572 0.3238 -0.0488 -0.0579 0.0233  168 PHE   B CD2 
6527 C  CE1 . PHE   B 168 ? 0.2912 0.1792 0.3271 -0.0364 -0.0505 0.0162  168 PHE   B CE1 
6528 C  CE2 . PHE   B 168 ? 0.2655 0.1637 0.3263 -0.0341 -0.0656 0.0177  168 PHE   B CE2 
6529 C  CZ  . PHE   B 168 ? 0.2790 0.1645 0.3251 -0.0237 -0.0628 0.0247  168 PHE   B CZ  
6539 N  N   . LEU   B 169 ? 0.1753 0.1787 0.2714 -0.0033 0.0038  -0.0000 169 LEU   B N   
6540 C  CA  . LEU   B 169 ? 0.1969 0.2095 0.2952 -0.0072 0.0069  -0.0303 169 LEU   B CA  
6541 C  C   . LEU   B 169 ? 0.2230 0.2324 0.3429 0.0085  0.0015  -0.0516 169 LEU   B C   
6542 O  O   . LEU   B 169 ? 0.2444 0.2566 0.3875 0.0087  -0.0004 -0.0688 169 LEU   B O   
6543 C  CB  . LEU   B 169 ? 0.2148 0.2528 0.3119 -0.0200 0.0064  -0.0104 169 LEU   B CB  
6544 C  CG  . LEU   B 169 ? 0.2521 0.2916 0.3529 -0.0121 0.0078  -0.0048 169 LEU   B CG  
6545 C  CD1 . LEU   B 169 ? 0.2677 0.3130 0.3581 -0.0117 0.0079  0.0141  169 LEU   B CD1 
6546 C  CD2 . LEU   B 169 ? 0.2391 0.2977 0.3463 0.0001  0.0269  -0.0259 169 LEU   B CD2 
6547 O  OXT . LEU   B 169 ? 0.2411 0.2444 0.3462 0.0320  0.0040  -0.0443 169 LEU   B OXT 
6559 C  C1  T TFA   C .   ? 0.0807 0.0936 0.0446 0.0062  0.0172  0.0107  201 TFA   A C1  
6560 C  C2  T TFA   C .   ? 0.0994 0.1108 0.0681 -0.0056 0.0212  -0.0026 201 TFA   A C2  
6561 O  O   T TFA   C .   ? 0.0580 0.0716 0.0261 0.0090  0.0125  0.0121  201 TFA   A O   
6562 F  F1  T TFA   C .   ? 0.1082 0.1170 0.0810 -0.0042 0.0193  -0.0152 201 TFA   A F1  
6563 F  F2  T TFA   C .   ? 0.1047 0.1146 0.0673 -0.0024 0.0240  0.0058  201 TFA   A F2  
6564 F  F3  T TFA   C .   ? 0.1040 0.1225 0.0838 -0.0164 0.0221  -0.0052 201 TFA   A F3  
6565 O  OXT T TFA   C .   ? 0.0840 0.0963 0.0548 0.0232  0.0148  0.0139  201 TFA   A OXT 
6566 N  N2  B A1A9A D .   ? 0.1213 0.1369 0.1489 -0.0063 -0.0020 0.0063  202 A1A9A A N2  
6567 C  C3  B A1A9A D .   ? 0.1442 0.1723 0.1714 0.0008  0.0163  0.0257  202 A1A9A A C3  
6568 C  C6  B A1A9A D .   ? 0.1558 0.1820 0.1499 -0.0111 -0.0005 0.0221  202 A1A9A A C6  
6569 C  C9  B A1A9A D .   ? 0.1324 0.1430 0.1565 -0.0033 -0.0016 0.0277  202 A1A9A A C9  
6570 C  C12 B A1A9A D .   ? 0.1227 0.1316 0.1393 -0.0033 -0.0009 0.0178  202 A1A9A A C12 
6571 C  C14 B A1A9A D .   ? 0.1233 0.1433 0.1418 0.0025  -0.0017 0.0049  202 A1A9A A C14 
6572 C  C17 B A1A9A D .   ? 0.1203 0.1406 0.1548 -0.0072 -0.0061 0.0127  202 A1A9A A C17 
6573 C  C1  B A1A9A D .   ? 0.1416 0.1508 0.1821 -0.0078 -0.0047 0.0221  202 A1A9A A C1  
6574 C  C10 B A1A9A D .   ? 0.1391 0.1378 0.1500 -0.0078 -0.0090 0.0356  202 A1A9A A C10 
6575 C  C11 B A1A9A D .   ? 0.1350 0.1183 0.1544 0.0021  0.0042  0.0355  202 A1A9A A C11 
6576 C  C13 B A1A9A D .   ? 0.1307 0.1437 0.1328 0.0017  0.0058  0.0023  202 A1A9A A C13 
6577 C  C15 B A1A9A D .   ? 0.1200 0.1380 0.1436 0.0045  0.0139  0.0054  202 A1A9A A C15 
6578 C  C16 B A1A9A D .   ? 0.1272 0.1450 0.1594 -0.0069 0.0097  0.0146  202 A1A9A A C16 
6579 C  C2  B A1A9A D .   ? 0.1379 0.1593 0.1604 -0.0100 0.0113  0.0224  202 A1A9A A C2  
6580 C  C4  B A1A9A D .   ? 0.1561 0.1799 0.1718 0.0005  0.0119  0.0359  202 A1A9A A C4  
6581 C  C5  B A1A9A D .   ? 0.1582 0.1817 0.1601 -0.0096 0.0038  0.0295  202 A1A9A A C5  
6582 C  C7  B A1A9A D .   ? 0.1477 0.1662 0.1387 -0.0134 0.0019  0.0260  202 A1A9A A C7  
6583 C  C8  B A1A9A D .   ? 0.1230 0.1355 0.1583 -0.0037 0.0059  0.0172  202 A1A9A A C8  
6584 N  N1  B A1A9A D .   ? 0.1221 0.1227 0.1436 -0.0061 -0.0037 0.0289  202 A1A9A A N1  
6585 N  N3  B A1A9A D .   ? 0.1319 0.1463 0.1375 -0.0017 0.0104  0.0044  202 A1A9A A N3  
6586 N  N4  B A1A9A D .   ? 0.1240 0.1407 0.1419 -0.0024 -0.0147 0.0188  202 A1A9A A N4  
6587 O  O1  B A1A9A D .   ? 0.1679 0.1612 0.2262 -0.0073 -0.0094 0.0298  202 A1A9A A O1  
6606 CL CL  B CL    E .   ? 0.1683 0.1650 0.2809 -0.0101 0.0180  -0.0313 203 CL    A CL  
6607 O  O   . HOH   F .   ? 0.3281 0.2675 0.4833 -0.0292 -0.1490 0.1203  301 HOH   A O   
6608 O  O   . HOH   F .   ? 0.4051 0.8358 0.5236 -0.1225 0.0416  0.1136  302 HOH   A O   
6609 O  O   . HOH   F .   ? 0.2667 0.3722 0.4017 0.0451  -0.0884 0.0317  303 HOH   A O   
6610 O  O   A HOH   F .   ? 0.3678 0.3104 0.3520 0.0372  0.0628  0.0061  304 HOH   A O   
6611 O  O   . HOH   F .   ? 0.4905 0.4015 0.5857 0.0450  -0.0611 0.0040  305 HOH   A O   
6612 O  O   . HOH   F .   ? 0.6825 0.4485 0.3373 0.1946  -0.0952 0.0785  306 HOH   A O   
6613 O  O   A HOH   F .   ? 0.2409 0.1649 0.3655 0.0338  -0.0012 0.0382  307 HOH   A O   
6614 O  O   B HOH   F .   ? 0.1854 0.1289 0.2605 0.0121  -0.0209 0.0338  308 HOH   A O   
6615 O  O   B HOH   F .   ? 0.2454 0.1968 0.2289 0.0789  -0.0634 0.0531  309 HOH   A O   
6616 O  O   . HOH   F .   ? 0.4341 0.5005 0.5319 0.1389  0.1073  -0.0904 310 HOH   A O   
6617 O  O   A HOH   F .   ? 0.2343 0.4174 0.4197 0.0477  0.0055  0.0514  311 HOH   A O   
6618 O  O   . HOH   F .   ? 0.4961 0.4177 0.3991 -0.0848 0.1059  0.0602  312 HOH   A O   
6619 O  O   B HOH   F .   ? 0.4881 0.2247 0.4321 -0.0182 0.0448  0.0172  313 HOH   A O   
6620 O  O   . HOH   F .   ? 0.4975 0.2105 0.5708 0.0464  0.0652  0.0151  314 HOH   A O   
6621 O  O   . HOH   F .   ? 0.2050 0.3556 0.3731 -0.0344 0.0454  -0.1174 315 HOH   A O   
6622 O  O   . HOH   F .   ? 0.2148 0.1940 0.3711 -0.0403 0.0110  -0.0211 316 HOH   A O   
6623 O  O   . HOH   F .   ? 0.2419 0.2479 0.2782 -0.0193 -0.0083 -0.0242 317 HOH   A O   
6624 O  O   . HOH   F .   ? 0.2777 0.3639 0.1788 -0.0314 0.0397  0.0586  318 HOH   A O   
6625 O  O   . HOH   F .   ? 0.2788 0.2982 0.2780 0.0152  -0.0360 -0.0716 319 HOH   A O   
6626 O  O   . HOH   F .   ? 0.3573 0.2923 0.3297 -0.0784 -0.0023 -0.0286 320 HOH   A O   
6627 O  O   . HOH   F .   ? 0.2207 0.2424 0.2818 -0.0299 -0.0487 0.1017  321 HOH   A O   
6628 O  O   . HOH   F .   ? 0.7137 0.4925 0.3150 -0.0047 -0.0860 0.0962  322 HOH   A O   
6629 O  O   . HOH   F .   ? 0.2983 0.3038 0.2465 -0.0836 0.0145  0.0437  323 HOH   A O   
6630 O  O   . HOH   F .   ? 0.5118 0.2664 0.3424 -0.1177 0.0911  0.0172  324 HOH   A O   
6631 O  O   . HOH   F .   ? 0.5282 0.4884 0.4361 -0.0275 0.1385  0.2222  325 HOH   A O   
6632 O  O   . HOH   F .   ? 0.2461 0.2024 0.2314 -0.0211 -0.0279 -0.0039 326 HOH   A O   
6633 O  O   . HOH   F .   ? 0.1598 0.1531 0.2454 -0.0218 0.0084  0.0003  327 HOH   A O   
6634 O  O   . HOH   F .   ? 0.5115 0.2057 0.4658 0.0316  -0.1070 0.0320  328 HOH   A O   
6635 O  O   A HOH   F .   ? 0.3375 0.2984 0.2208 -0.0738 -0.0352 0.0061  329 HOH   A O   
6636 O  O   . HOH   F .   ? 0.3237 0.4477 0.2940 0.0135  0.0385  0.0239  330 HOH   A O   
6637 O  O   . HOH   F .   ? 0.1651 0.3159 0.2636 0.0035  0.0409  0.0313  331 HOH   A O   
6638 O  O   . HOH   F .   ? 0.2049 0.2287 0.2159 -0.0221 0.0308  0.0415  332 HOH   A O   
6639 O  O   . HOH   F .   ? 0.1809 0.2827 0.3090 0.0246  -0.0131 -0.0118 333 HOH   A O   
6640 O  O   . HOH   F .   ? 0.6283 0.4174 0.4993 0.0671  0.2379  -0.0525 334 HOH   A O   
6641 O  O   B HOH   F .   ? 0.1841 0.1341 0.1905 -0.0213 -0.0107 0.0008  335 HOH   A O   
6642 O  O   B HOH   F .   ? 0.2640 0.2110 0.2822 0.0124  -0.0631 -0.0299 336 HOH   A O   
6643 O  O   . HOH   F .   ? 0.5297 0.3585 0.4551 -0.0005 0.1033  0.0098  337 HOH   A O   
6644 O  O   . HOH   F .   ? 0.2501 0.2352 0.2888 0.0263  0.0228  0.0403  338 HOH   A O   
6645 O  O   . HOH   F .   ? 0.2588 0.1941 0.2608 -0.0139 0.0028  0.0268  339 HOH   A O   
6646 O  O   . HOH   F .   ? 0.2437 0.4363 0.3485 0.0985  -0.0657 -0.0032 340 HOH   A O   
6647 O  O   . HOH   F .   ? 0.5460 0.5347 0.3587 -0.1113 0.2049  0.0914  341 HOH   A O   
6648 O  O   . HOH   F .   ? 0.6206 0.6043 0.4245 -0.1443 0.0327  0.2470  342 HOH   A O   
6649 O  O   . HOH   F .   ? 0.2023 0.2040 0.4154 0.0168  0.0968  -0.0146 343 HOH   A O   
6650 O  O   T HOH   F .   ? 0.0629 0.0584 0.1072 -0.0181 -0.0101 0.0279  344 HOH   A O   
6651 O  O   . HOH   F .   ? 0.2407 0.5322 0.4011 0.0329  -0.0653 0.1681  345 HOH   A O   
6652 O  O   A HOH   F .   ? 0.4706 0.2813 0.3502 0.0166  0.0762  0.0624  346 HOH   A O   
6653 O  O   A HOH   F .   ? 0.2332 0.3946 0.2124 0.1221  -0.0168 -0.0112 347 HOH   A O   
6654 O  O   B HOH   F .   ? 0.3048 0.2747 0.1787 -0.0883 -0.0116 0.0359  348 HOH   A O   
6655 O  O   . HOH   F .   ? 0.4931 0.3908 0.4138 -0.0324 -0.0151 -0.0272 349 HOH   A O   
6656 O  O   . HOH   F .   ? 0.3165 0.3433 0.5251 -0.0802 -0.1197 -0.0861 350 HOH   A O   
6657 O  O   . HOH   F .   ? 0.3697 0.3918 0.2153 -0.1211 -0.0148 -0.0706 351 HOH   A O   
6658 O  O   . HOH   F .   ? 0.3127 0.3628 0.4569 -0.0862 -0.1115 -0.0307 352 HOH   A O   
6659 O  O   A HOH   F .   ? 0.1388 0.2106 0.1797 0.0449  0.0345  0.0492  353 HOH   A O   
6660 O  O   . HOH   F .   ? 0.1574 0.2298 0.2270 -0.0013 -0.0131 0.0495  354 HOH   A O   
6661 O  O   . HOH   F .   ? 0.1550 0.1873 0.2459 0.0116  -0.0297 -0.0540 355 HOH   A O   
6662 O  O   . HOH   F .   ? 0.1687 0.1839 0.2714 -0.0237 0.0034  0.0461  356 HOH   A O   
6663 O  O   . HOH   F .   ? 0.4719 0.3094 0.5057 -0.1876 0.1437  -0.0215 357 HOH   A O   
6664 O  O   . HOH   F .   ? 0.6983 0.5176 0.4720 -0.1529 -0.1100 0.2630  358 HOH   A O   
6665 O  O   . HOH   F .   ? 0.3521 0.7400 0.4777 -0.0624 -0.1269 0.0531  359 HOH   A O   
6666 O  O   . HOH   F .   ? 0.2241 0.1795 0.2464 0.0265  -0.0296 0.0032  360 HOH   A O   
6667 O  O   . HOH   F .   ? 0.6568 0.3635 0.3367 -0.0531 -0.0290 0.1175  361 HOH   A O   
6668 O  O   . HOH   F .   ? 0.3729 0.2000 0.2509 0.1014  0.0447  0.0104  362 HOH   A O   
6669 O  O   . HOH   F .   ? 0.3802 0.4148 0.3453 0.1859  0.0704  0.0445  363 HOH   A O   
6670 O  O   B HOH   F .   ? 0.2246 0.2141 0.2066 0.0693  -0.0541 0.0004  364 HOH   A O   
6671 O  O   . HOH   F .   ? 0.4714 0.6375 0.4070 -0.0372 -0.0045 0.1845  365 HOH   A O   
6672 O  O   . HOH   F .   ? 0.1338 0.1358 0.1390 -0.0053 0.0078  0.0131  366 HOH   A O   
6673 O  O   . HOH   F .   ? 0.3258 0.2542 0.5098 -0.0581 -0.0600 0.0628  367 HOH   A O   
6674 O  O   . HOH   F .   ? 0.1560 0.1329 0.2387 -0.0040 0.0106  -0.0103 368 HOH   A O   
6675 O  O   . HOH   F .   ? 0.2724 0.4443 0.2780 0.0636  0.0777  0.1619  369 HOH   A O   
6676 O  O   A HOH   F .   ? 0.3559 0.1726 0.1981 0.0158  0.0527  -0.0013 370 HOH   A O   
6677 O  O   . HOH   F .   ? 0.5032 0.5513 0.3486 0.2891  -0.0168 -0.1072 371 HOH   A O   
6678 O  O   . HOH   F .   ? 0.3851 0.2397 0.4385 -0.1020 0.0455  0.0641  372 HOH   A O   
6679 O  O   . HOH   F .   ? 0.1620 0.1972 0.2714 0.0078  -0.0074 0.0074  373 HOH   A O   
6680 O  O   . HOH   F .   ? 0.2741 0.4203 0.3339 -0.0376 0.0905  -0.0053 374 HOH   A O   
6681 O  O   . HOH   F .   ? 0.4004 0.7440 0.3219 0.1525  -0.0124 0.1684  375 HOH   A O   
6682 O  O   . HOH   F .   ? 0.2053 0.2761 0.3231 0.0282  0.0624  -0.0576 376 HOH   A O   
6683 O  O   B HOH   F .   ? 0.3060 0.2650 0.3770 0.0211  0.1013  -0.0514 377 HOH   A O   
6684 O  O   . HOH   F .   ? 0.2029 0.1951 0.2402 -0.0407 0.0046  0.0359  378 HOH   A O   
6685 O  O   . HOH   F .   ? 0.1529 0.1611 0.1460 -0.0075 -0.0072 -0.0033 379 HOH   A O   
6686 O  O   . HOH   F .   ? 0.3191 0.6884 0.3324 0.0712  0.0910  -0.0810 380 HOH   A O   
6687 O  O   . HOH   F .   ? 0.3010 0.2910 0.2113 0.0261  0.0601  -0.0017 381 HOH   A O   
6688 O  O   . HOH   F .   ? 0.1895 0.1800 0.2371 0.0166  -0.0261 0.0248  382 HOH   A O   
6689 O  O   . HOH   F .   ? 0.7708 0.3445 0.5228 -0.0863 -0.1389 -0.0046 383 HOH   A O   
6690 O  O   B HOH   F .   ? 0.2970 0.3307 0.1424 -0.0539 0.0606  0.0334  384 HOH   A O   
6691 O  O   . HOH   F .   ? 0.5525 0.5040 0.6121 -0.0865 0.0124  0.1345  385 HOH   A O   
6692 O  O   . HOH   F .   ? 0.2920 0.3379 0.3522 -0.0565 0.1314  0.0084  386 HOH   A O   
6693 O  O   . HOH   F .   ? 0.1816 0.2312 0.1874 -0.0199 -0.0077 0.0626  387 HOH   A O   
6694 O  O   . HOH   F .   ? 0.4899 0.5918 0.6143 -0.0820 0.0788  0.0597  388 HOH   A O   
6695 O  O   . HOH   F .   ? 0.3356 0.8861 0.4631 -0.1125 -0.0898 0.0788  389 HOH   A O   
6696 O  O   . HOH   F .   ? 0.2633 0.2132 0.1860 -0.0639 0.0037  0.0383  390 HOH   A O   
6697 O  O   B HOH   F .   ? 0.3547 0.3409 0.3645 0.0068  0.0441  0.0451  391 HOH   A O   
6698 O  O   . HOH   F .   ? 0.1884 0.2788 0.2636 0.0372  0.0292  0.0833  392 HOH   A O   
6699 O  O   . HOH   F .   ? 0.5911 0.3805 0.5720 -0.0425 0.1597  -0.1267 393 HOH   A O   
6700 O  O   A HOH   F .   ? 0.2897 0.3404 0.3401 0.0572  0.1406  0.1595  394 HOH   A O   
6701 O  O   . HOH   F .   ? 0.2532 0.4044 0.3415 -0.0340 0.0974  -0.0749 395 HOH   A O   
6702 O  O   . HOH   F .   ? 0.3236 0.3840 0.3006 -0.1386 0.0674  0.0176  396 HOH   A O   
6703 O  O   . HOH   F .   ? 0.1985 0.2473 0.2430 -0.0356 -0.0524 0.0522  397 HOH   A O   
6704 O  O   . HOH   F .   ? 0.2181 0.4939 0.3238 -0.0329 0.0009  0.0779  398 HOH   A O   
6705 O  O   A HOH   F .   ? 0.2232 0.1804 0.3191 -0.0179 0.0280  0.0130  399 HOH   A O   
6706 O  O   . HOH   F .   ? 0.1846 0.2063 0.1693 -0.0046 0.0112  0.0142  400 HOH   A O   
6707 O  O   . HOH   F .   ? 0.1873 0.2029 0.3887 0.0291  0.0884  0.0986  401 HOH   A O   
6708 O  O   . HOH   F .   ? 0.1793 0.1814 0.2043 -0.0003 -0.0236 -0.0052 402 HOH   A O   
6709 O  O   . HOH   F .   ? 0.2406 0.3896 0.1966 0.0060  -0.0295 0.0006  403 HOH   A O   
6710 O  O   . HOH   F .   ? 0.1878 0.2658 0.3530 -0.0114 -0.0177 0.0111  404 HOH   A O   
6711 O  O   . HOH   F .   ? 0.3630 0.2603 0.3188 -0.0087 -0.0321 0.1004  405 HOH   A O   
6712 O  O   . HOH   F .   ? 0.7374 0.5280 0.4376 -0.0830 -0.0306 0.2203  406 HOH   A O   
6713 O  O   . HOH   F .   ? 0.6753 0.6464 0.4506 0.1637  -0.0776 -0.0038 407 HOH   A O   
6714 O  O   . HOH   F .   ? 0.1396 0.1490 0.2052 -0.0015 -0.0035 0.0046  408 HOH   A O   
6715 O  O   . HOH   F .   ? 0.2187 0.2248 0.3304 0.0029  -0.0185 0.0730  409 HOH   A O   
6716 O  O   . HOH   F .   ? 0.3534 0.5818 0.5587 -0.0212 0.0804  0.0709  410 HOH   A O   
6717 O  O   A HOH   F .   ? 0.1641 0.1629 0.2049 -0.0015 -0.0394 0.0231  411 HOH   A O   
6718 O  O   . HOH   F .   ? 0.4805 0.3903 0.2015 -0.0572 0.1047  0.0476  412 HOH   A O   
6719 O  O   . HOH   F .   ? 0.2437 0.2124 0.2520 -0.0540 -0.0032 0.0571  413 HOH   A O   
6720 O  O   . HOH   F .   ? 0.1756 0.2246 0.2503 -0.0221 0.0553  0.0508  414 HOH   A O   
6721 O  O   . HOH   F .   ? 0.3734 0.6511 0.5679 0.1073  -0.0495 0.1838  415 HOH   A O   
6722 O  O   . HOH   F .   ? 0.5346 0.2576 0.4995 0.0734  0.0032  -0.0082 416 HOH   A O   
6723 O  O   . HOH   F .   ? 0.2871 0.2824 0.1923 -0.0856 -0.0589 0.0220  417 HOH   A O   
6724 O  O   . HOH   F .   ? 0.1610 0.1751 0.3063 0.0005  -0.0059 0.0182  418 HOH   A O   
6725 O  O   A HOH   F .   ? 0.1123 0.1451 0.1170 0.0263  -0.0212 -0.0180 419 HOH   A O   
6726 O  O   . HOH   F .   ? 0.5627 0.7495 0.4941 0.0015  0.1341  0.0865  420 HOH   A O   
6727 O  O   . HOH   F .   ? 0.2279 0.1805 0.2997 -0.0048 -0.0294 0.0109  421 HOH   A O   
6728 O  O   B HOH   F .   ? 0.2913 0.3482 0.2491 0.1881  0.0104  -0.0122 422 HOH   A O   
6729 O  O   B HOH   F .   ? 0.2323 0.3032 0.1940 -0.0394 -0.0528 0.0618  423 HOH   A O   
6730 O  O   . HOH   F .   ? 0.2026 0.3012 0.2613 -0.0063 -0.0466 0.0474  424 HOH   A O   
6731 O  O   . HOH   F .   ? 0.1753 0.1394 0.1609 -0.0206 0.0159  0.0015  425 HOH   A O   
6732 O  O   . HOH   F .   ? 0.6257 0.3991 0.4509 0.1345  -0.1132 0.1353  426 HOH   A O   
6733 O  O   B HOH   F .   ? 0.4578 0.2822 0.3745 -0.1293 0.0530  -0.0383 427 HOH   A O   
6734 O  O   . HOH   F .   ? 0.3038 0.3644 0.7495 0.0012  0.1257  -0.0182 428 HOH   A O   
6735 O  O   . HOH   F .   ? 0.2879 0.6379 0.1808 -0.0686 0.0468  -0.0199 429 HOH   A O   
6736 O  O   . HOH   F .   ? 0.2014 0.1731 0.1507 -0.0018 0.0196  0.0177  430 HOH   A O   
6737 O  O   . HOH   F .   ? 0.4657 0.4704 0.4001 0.1359  -0.0925 -0.1421 431 HOH   A O   
6738 O  O   . HOH   F .   ? 0.3417 0.1330 0.2152 0.0070  -0.0464 0.0117  432 HOH   A O   
6739 O  O   . HOH   F .   ? 0.5148 0.6028 0.3095 -0.1078 -0.0074 0.1365  433 HOH   A O   
6740 O  O   . HOH   F .   ? 0.6227 0.7480 0.4350 0.0592  0.2878  -0.0797 434 HOH   A O   
6741 O  O   . HOH   F .   ? 0.2277 0.4119 0.2348 0.1369  -0.0176 -0.0011 435 HOH   A O   
6742 O  O   A HOH   F .   ? 0.2442 0.2921 0.1939 -0.0286 0.0702  0.0067  436 HOH   A O   
6743 O  O   . HOH   F .   ? 0.6134 0.6075 0.6618 -0.1453 -0.0930 -0.0390 437 HOH   A O   
6744 O  O   . HOH   F .   ? 0.1795 0.1839 0.2643 0.0198  -0.0309 0.0086  438 HOH   A O   
6745 O  O   . HOH   F .   ? 0.1989 0.2248 0.4019 0.0031  -0.0370 -0.0356 439 HOH   A O   
6746 O  O   . HOH   F .   ? 0.4277 0.2332 0.5651 -0.0856 -0.2224 0.1204  440 HOH   A O   
6747 O  O   . HOH   F .   ? 0.1650 0.2071 0.2950 -0.0052 0.0148  0.0206  441 HOH   A O   
6748 O  O   . HOH   F .   ? 0.4854 0.5057 0.3889 -0.0048 -0.1421 0.0055  442 HOH   A O   
6749 O  O   A HOH   F .   ? 0.3749 0.4604 0.4153 -0.0649 -0.0673 -0.0409 443 HOH   A O   
6750 O  O   . HOH   F .   ? 0.2944 0.3467 0.2308 -0.0124 -0.0375 0.0404  444 HOH   A O   
6751 O  O   . HOH   F .   ? 0.3140 0.2468 0.5847 -0.0474 0.1562  -0.0261 445 HOH   A O   
6752 O  O   . HOH   F .   ? 0.3651 0.2907 0.1924 -0.0810 0.0269  0.0644  446 HOH   A O   
6753 O  O   . HOH   F .   ? 0.5428 0.4742 0.4984 -0.0735 -0.1246 -0.1281 447 HOH   A O   
6754 O  O   A HOH   F .   ? 0.7332 0.5050 0.4310 0.2785  0.1681  0.1911  448 HOH   A O   
6755 O  O   A HOH   F .   ? 0.1558 0.3651 0.1738 0.0290  -0.0193 -0.1031 449 HOH   A O   
6756 O  O   . HOH   F .   ? 0.2485 0.1696 0.2793 0.0033  -0.0112 0.0196  450 HOH   A O   
6757 O  O   A HOH   F .   ? 0.2228 0.2130 0.1764 0.0164  0.0170  0.0131  451 HOH   A O   
6758 O  O   . HOH   F .   ? 0.5854 0.6364 0.5927 0.0721  -0.1233 0.0507  452 HOH   A O   
6759 O  O   . HOH   F .   ? 0.4184 0.3867 0.3072 0.2376  -0.0438 -0.0446 453 HOH   A O   
6760 O  O   . HOH   F .   ? 0.7562 0.8074 0.6050 0.1003  -0.0466 0.0150  454 HOH   A O   
6761 O  O   . HOH   F .   ? 0.5641 0.5664 0.6668 -0.1314 -0.0605 -0.1212 455 HOH   A O   
6762 O  O   . HOH   F .   ? 0.6435 0.5003 0.7733 0.1016  -0.1086 0.1641  456 HOH   A O   
6763 O  O   . HOH   F .   ? 0.3289 0.4291 0.5896 -0.0057 0.1146  -0.1767 457 HOH   A O   
6764 O  O   . HOH   F .   ? 0.2451 0.2116 0.2813 0.0087  0.0426  0.0217  458 HOH   A O   
6765 O  O   . HOH   F .   ? 0.1911 0.2498 0.5054 -0.0225 -0.0891 0.0798  459 HOH   A O   
6766 O  O   . HOH   F .   ? 0.2149 0.2735 0.2642 -0.0055 -0.0220 -0.0506 460 HOH   A O   
6767 O  O   B HOH   F .   ? 0.3443 0.2241 0.1597 0.0697  -0.0298 0.0053  461 HOH   A O   
6768 O  O   . HOH   F .   ? 0.6438 0.3298 0.5172 -0.0542 -0.0284 0.0641  462 HOH   A O   
6769 O  O   . HOH   F .   ? 0.6838 0.7878 0.4718 0.1310  -0.0657 -0.0718 463 HOH   A O   
6770 O  O   . HOH   F .   ? 1.0269 0.5076 0.5021 0.0041  0.3151  0.1167  464 HOH   A O   
6771 O  O   . HOH   F .   ? 0.4171 0.5300 0.4700 0.0528  0.0063  0.1187  465 HOH   A O   
6772 O  O   . HOH   F .   ? 0.4424 0.3832 0.5107 0.0076  -0.0003 0.0457  466 HOH   A O   
6773 O  O   . HOH   F .   ? 0.3974 0.5011 0.5248 0.1229  -0.1179 0.1760  467 HOH   A O   
6774 O  O   . HOH   F .   ? 0.2785 0.2551 0.3883 -0.0572 0.0434  -0.0685 468 HOH   A O   
6775 O  O   . HOH   F .   ? 0.6306 0.6094 0.4528 -0.1111 0.0992  0.1002  469 HOH   A O   
6776 O  O   . HOH   F .   ? 0.3210 0.4679 0.5404 -0.1354 0.0315  -0.1592 470 HOH   A O   
6777 O  O   . HOH   F .   ? 0.4479 0.6242 0.4000 -0.1253 -0.1180 0.2315  471 HOH   A O   
6778 O  O   . HOH   F .   ? 0.4203 0.4504 0.4992 0.0304  -0.0254 0.0885  472 HOH   A O   
6779 O  O   . HOH   F .   ? 0.3248 0.2684 0.7051 0.0779  -0.1969 -0.0644 473 HOH   A O   
6780 O  O   . HOH   F .   ? 0.3948 0.5480 0.3825 0.0449  -0.0508 -0.0856 474 HOH   A O   
6781 O  O   . HOH   F .   ? 0.2812 0.3260 0.3670 -0.1218 0.0547  -0.0391 475 HOH   A O   
6782 O  O   . HOH   F .   ? 0.6264 0.3451 0.7405 0.1006  0.0475  0.2013  476 HOH   A O   
6783 O  O   . HOH   F .   ? 0.2736 0.4886 0.5410 0.0868  0.0164  -0.1811 477 HOH   A O   
6784 O  O   . HOH   F .   ? 0.2860 0.4769 0.4874 -0.0332 -0.0270 0.0038  478 HOH   A O   
6785 O  O   . HOH   F .   ? 0.5621 0.6355 0.6338 -0.0455 0.0795  0.2675  479 HOH   A O   
6786 O  O   . HOH   F .   ? 0.2745 0.1779 0.2640 0.0258  -0.0741 -0.0239 480 HOH   A O   
6787 O  O   . HOH   F .   ? 0.4988 0.5635 0.5490 0.1276  0.0254  -0.1017 481 HOH   A O   
6788 O  O   . HOH   F .   ? 0.5622 0.5302 0.4678 0.0673  0.1585  0.1065  482 HOH   A O   
6789 O  O   . HOH   F .   ? 0.4104 0.4969 0.2877 0.0049  -0.0202 -0.0255 483 HOH   A O   
6790 O  O   . HOH   F .   ? 0.4554 0.2848 0.3371 0.0247  0.0715  -0.0028 484 HOH   A O   
6791 O  O   . HOH   F .   ? 0.5157 0.4125 0.3017 0.0189  -0.1033 -0.0708 485 HOH   A O   
6792 O  O   . HOH   F .   ? 0.4127 0.4582 0.5785 -0.1916 -0.0389 -0.0307 486 HOH   A O   
6793 O  O   . HOH   F .   ? 0.5714 0.6349 0.6270 -0.1553 -0.1340 -0.0499 487 HOH   A O   
6794 O  O   . HOH   F .   ? 0.4907 0.3190 0.3391 -0.1265 -0.1494 0.0787  488 HOH   A O   
6795 O  O   . HOH   F .   ? 0.6313 0.5677 0.7229 -0.0270 0.0247  -0.0935 489 HOH   A O   
6796 O  O   . HOH   F .   ? 0.2561 0.2294 0.2570 0.0277  -0.0321 -0.0122 490 HOH   A O   
6797 O  O   . HOH   F .   ? 0.6212 0.3915 0.4188 0.0273  -0.0019 -0.1198 491 HOH   A O   
6798 O  O   . HOH   F .   ? 0.6261 0.5560 0.4663 -0.1142 -0.0783 -0.0915 492 HOH   A O   
6799 O  O   . HOH   F .   ? 0.8911 0.3675 0.3322 -0.0201 -0.1361 0.0399  493 HOH   A O   
6800 O  O   . HOH   F .   ? 0.4228 0.3246 0.4525 -0.1275 -0.0470 0.1404  494 HOH   A O   
6801 O  O   . HOH   F .   ? 0.3233 0.3573 0.5430 0.0159  0.1953  0.0943  495 HOH   A O   
6802 O  O   . HOH   F .   ? 0.5942 0.6867 0.6930 0.1289  0.2160  -0.1192 496 HOH   A O   
6803 O  O   . HOH   F .   ? 0.5608 0.6609 0.3829 -0.0273 0.0812  0.1208  497 HOH   A O   
6804 O  O   . HOH   F .   ? 0.2919 0.3344 0.5105 -0.0093 0.0918  -0.0374 498 HOH   A O   
6805 O  O   . HOH   F .   ? 0.2822 0.5625 0.3571 0.1207  0.1014  0.2384  499 HOH   A O   
6806 O  O   . HOH   F .   ? 0.2539 0.2647 0.7949 -0.0116 -0.1187 0.0528  500 HOH   A O   
6807 O  O   . HOH   F .   ? 0.4672 0.4758 0.5566 -0.1070 -0.0708 0.0076  501 HOH   A O   
6808 O  O   . HOH   F .   ? 0.5545 0.3344 0.5037 -0.0450 0.2562  0.0353  502 HOH   A O   
6809 O  O   . HOH   F .   ? 0.3124 0.2272 0.5325 -0.0100 0.0262  0.1020  503 HOH   A O   
6810 O  O   . HOH   F .   ? 0.5634 0.3754 0.4112 0.0030  0.0876  -0.0375 504 HOH   A O   
6811 O  O   . HOH   F .   ? 0.4875 0.4101 0.2622 -0.1365 0.1539  -0.0718 505 HOH   A O   
6812 O  O   . HOH   F .   ? 0.6713 0.2621 0.3638 -0.0571 0.0766  0.0616  506 HOH   A O   
6813 O  O   . HOH   F .   ? 0.4766 0.8386 0.5761 -0.0817 -0.0989 0.2546  507 HOH   A O   
6814 O  O   . HOH   F .   ? 0.2930 0.4387 0.2904 0.0251  -0.0649 0.0219  508 HOH   A O   
6815 O  O   B HOH   F .   ? 0.2528 0.2660 0.2800 0.0555  0.1098  0.0627  509 HOH   A O   
6816 O  O   . HOH   F .   ? 0.4749 0.2557 0.4782 -0.1385 -0.0401 0.0499  510 HOH   A O   
6817 O  O   B HOH   F .   ? 0.4791 0.6471 0.5170 0.1266  0.0510  0.1754  511 HOH   A O   
6818 O  O   . HOH   F .   ? 0.2884 0.4352 0.4140 0.0819  0.0096  0.0230  512 HOH   A O   
6819 O  O   . HOH   F .   ? 0.3001 0.4142 0.3181 -0.0081 -0.0386 -0.0737 513 HOH   A O   
6820 O  O   . HOH   F .   ? 0.7543 0.4794 0.7003 0.1727  0.0515  0.1161  514 HOH   A O   
6821 O  O   . HOH   F .   ? 0.6249 0.7170 0.5120 0.1734  -0.0855 -0.0089 515 HOH   A O   
6822 O  O   A HOH   F .   ? 0.4442 0.3688 0.3655 0.0202  -0.1224 0.0530  516 HOH   A O   
6823 O  O   . HOH   F .   ? 0.3055 0.2748 0.4600 -0.0176 0.0175  0.0849  517 HOH   A O   
6824 O  O   . HOH   F .   ? 0.5972 0.7003 0.4979 0.3438  -0.0017 0.1531  518 HOH   A O   
6825 O  O   B HOH   F .   ? 0.2578 0.2364 0.3226 0.0176  -0.0706 0.1026  519 HOH   A O   
6826 O  O   . HOH   F .   ? 0.4789 0.5777 0.4151 -0.0313 -0.0655 -0.1329 520 HOH   A O   
6827 O  O   T HOH   F .   ? 0.0431 0.0997 0.0794 -0.0100 -0.0022 0.0500  521 HOH   A O   
6828 O  O   B HOH   F .   ? 0.2561 0.1877 0.2716 0.0194  -0.0682 0.0249  522 HOH   A O   
6829 O  O   A HOH   F .   ? 0.4851 0.7511 0.4123 0.2420  0.0824  -0.0256 523 HOH   A O   
6830 O  O   . HOH   F .   ? 0.3652 0.7240 0.4497 0.0663  0.0368  -0.1060 524 HOH   A O   
6831 O  O   . HOH   F .   ? 0.4216 0.6799 0.5361 -0.0372 -0.0510 -0.0484 525 HOH   A O   
6832 O  O   . HOH   F .   ? 0.5432 0.6008 0.5352 0.0595  0.0612  0.0441  526 HOH   A O   
6833 O  O   . HOH   F .   ? 0.4608 0.4884 0.6155 -0.0206 -0.1370 0.2911  527 HOH   A O   
6834 O  O   . HOH   G .   ? 0.2392 0.2490 0.3289 0.0135  0.0729  0.0388  201 HOH   B O   
6835 O  O   . HOH   G .   ? 0.3438 0.4236 0.5221 -0.0830 0.0662  -0.1295 202 HOH   B O   
6836 O  O   . HOH   G .   ? 0.4674 0.3080 0.3841 -0.0368 -0.0183 -0.1061 203 HOH   B O   
6837 O  O   . HOH   G .   ? 0.6211 0.6614 0.4428 0.0962  -0.0347 -0.1516 204 HOH   B O   
6838 O  O   . HOH   G .   ? 0.3203 0.4808 0.6873 -0.0756 0.0147  -0.0768 205 HOH   B O   
6839 O  O   . HOH   G .   ? 0.3079 0.6829 0.3449 0.0351  0.0121  0.2329  206 HOH   B O   
6840 O  O   . HOH   G .   ? 0.5029 0.5833 0.4079 0.2892  -0.1415 -0.0517 207 HOH   B O   
6841 O  O   . HOH   G .   ? 0.3282 0.5323 0.4300 0.2031  0.0491  0.0138  208 HOH   B O   
6842 O  O   . HOH   G .   ? 0.4589 0.5152 0.4378 0.2544  -0.0958 0.0066  209 HOH   B O   
6843 O  O   . HOH   G .   ? 0.2961 0.5151 0.5297 -0.0135 0.1629  -0.1953 210 HOH   B O   
6844 O  O   . HOH   G .   ? 0.7051 0.2797 0.4146 0.0732  0.0807  0.0022  211 HOH   B O   
6845 O  O   . HOH   G .   ? 0.4655 0.4138 0.6408 0.0046  -0.1275 0.2689  212 HOH   B O   
6846 O  O   . HOH   G .   ? 0.2011 0.2518 0.2831 0.0069  -0.0042 -0.0376 213 HOH   B O   
6847 O  O   . HOH   G .   ? 0.1688 0.1965 0.2730 -0.0146 -0.0018 0.0113  214 HOH   B O   
6848 O  O   . HOH   G .   ? 0.3010 0.2984 0.6948 0.0589  -0.1306 0.0590  215 HOH   B O   
6849 O  O   . HOH   G .   ? 0.5218 0.4065 0.3564 -0.0232 -0.1236 0.0869  216 HOH   B O   
6850 O  O   . HOH   G .   ? 0.3598 0.4962 0.5241 0.0861  -0.0070 0.1434  217 HOH   B O   
6851 O  O   . HOH   G .   ? 0.6247 0.5663 0.6283 0.0916  0.0031  -0.0123 218 HOH   B O   
6852 O  O   . HOH   G .   ? 0.3866 0.4638 0.4164 0.0321  0.0053  -0.1614 219 HOH   B O   
6853 O  O   . HOH   G .   ? 0.4839 0.2067 0.3068 -0.0136 -0.0957 0.0030  220 HOH   B O   
6854 O  O   . HOH   G .   ? 0.5870 0.3223 0.4306 -0.1487 0.0638  0.0550  221 HOH   B O   
6855 O  O   . HOH   G .   ? 0.4175 0.5805 0.3979 0.1797  -0.0187 -0.0185 222 HOH   B O   
6856 O  O   . HOH   G .   ? 0.1704 0.2128 0.3102 -0.0138 -0.0072 0.0014  223 HOH   B O   
6857 O  O   . HOH   G .   ? 0.5360 0.4741 0.6563 -0.0534 -0.1426 -0.1053 224 HOH   B O   
6858 O  O   . HOH   G .   ? 0.3877 0.2701 0.4055 0.0830  -0.0214 -0.0535 225 HOH   B O   
6859 O  O   . HOH   G .   ? 0.2654 0.3143 0.6584 -0.0041 0.0792  0.0477  226 HOH   B O   
6860 O  O   . HOH   G .   ? 0.3224 0.2147 0.6308 0.0284  0.2061  0.0949  227 HOH   B O   
6861 O  O   . HOH   G .   ? 0.2491 0.1902 0.2792 -0.0309 0.0987  -0.0061 228 HOH   B O   
6862 O  O   . HOH   G .   ? 0.4587 0.3226 0.3588 -0.1035 0.0293  -0.0839 229 HOH   B O   
6863 O  O   . HOH   G .   ? 0.6514 0.6384 0.3477 0.1340  -0.0092 0.1170  230 HOH   B O   
6864 O  O   . HOH   G .   ? 0.3830 0.1797 0.2148 0.0190  -0.0789 0.0031  231 HOH   B O   
6865 O  O   . HOH   G .   ? 0.3029 0.4206 0.3238 -0.1065 -0.0343 -0.0450 232 HOH   B O   
6866 O  O   . HOH   G .   ? 0.2314 0.2181 0.4140 -0.0376 -0.0052 -0.0610 233 HOH   B O   
6867 O  O   . HOH   G .   ? 0.3293 0.2317 0.4768 -0.0068 0.1562  0.0189  234 HOH   B O   
6868 O  O   . HOH   G .   ? 0.1506 0.1489 0.1761 -0.0152 -0.0112 -0.0021 235 HOH   B O   
6869 O  O   . HOH   G .   ? 0.6764 0.3748 0.2520 -0.0763 -0.0264 0.0253  236 HOH   B O   
6870 O  O   . HOH   G .   ? 0.3041 0.4736 0.3483 -0.1298 -0.0006 -0.0529 237 HOH   B O   
6871 O  O   . HOH   G .   ? 0.3053 0.5142 0.4408 -0.0344 -0.1103 0.1271  238 HOH   B O   
6872 O  O   . HOH   G .   ? 0.3906 0.3399 0.2650 0.0456  0.0771  0.0349  239 HOH   B O   
6873 O  O   . HOH   G .   ? 0.2144 0.4069 0.2534 -0.0447 -0.0218 0.0573  240 HOH   B O   
6874 O  O   . HOH   G .   ? 0.2866 0.2594 0.3217 0.0473  0.0160  -0.0914 241 HOH   B O   
6875 O  O   . HOH   G .   ? 0.3663 0.3422 0.4401 0.0483  -0.0772 -0.1861 242 HOH   B O   
6876 O  O   . HOH   G .   ? 0.6244 0.5024 0.5638 0.1494  0.0337  -0.1055 243 HOH   B O   
6877 O  O   . HOH   G .   ? 0.2411 0.4196 0.2959 -0.0449 -0.0624 -0.0452 244 HOH   B O   
6878 O  O   . HOH   G .   ? 0.1693 0.1516 0.2824 -0.0025 -0.0005 -0.0107 245 HOH   B O   
6879 O  O   . HOH   G .   ? 0.5431 0.3075 0.3968 -0.2228 -0.0544 0.0388  246 HOH   B O   
6880 O  O   . HOH   G .   ? 0.2190 0.1397 0.3761 0.0127  -0.0710 -0.0242 247 HOH   B O   
6881 O  O   . HOH   G .   ? 0.2110 0.2247 0.3169 -0.0444 0.0104  -0.0243 248 HOH   B O   
6882 O  O   . HOH   G .   ? 0.1543 0.1334 0.1781 0.0033  -0.0114 0.0074  249 HOH   B O   
6883 O  O   . HOH   G .   ? 0.3323 0.2436 0.3200 -0.0144 -0.0129 -0.0543 250 HOH   B O   
6884 O  O   . HOH   G .   ? 0.3382 0.3537 0.2126 0.0420  0.0732  0.0371  251 HOH   B O   
6885 O  O   . HOH   G .   ? 0.3883 0.4763 0.5296 -0.1656 -0.0312 0.0734  252 HOH   B O   
6886 O  O   . HOH   G .   ? 0.2899 0.2162 0.3321 0.0755  0.0872  0.0258  253 HOH   B O   
6887 O  O   . HOH   G .   ? 0.2185 0.4295 0.6098 0.0887  -0.0919 -0.1238 254 HOH   B O   
6888 O  O   . HOH   G .   ? 0.3177 0.1823 0.6336 -0.0258 -0.1436 -0.0162 255 HOH   B O   
6889 O  O   . HOH   G .   ? 0.2577 0.2238 0.1978 0.0006  -0.0205 0.0040  256 HOH   B O   
6890 O  O   . HOH   G .   ? 0.2345 0.1935 0.4366 0.0012  -0.0913 -0.0342 257 HOH   B O   
6891 O  O   . HOH   G .   ? 0.2342 0.2013 0.2219 -0.0329 -0.0555 0.0171  258 HOH   B O   
6892 O  O   . HOH   G .   ? 0.2462 0.2204 0.2598 0.0737  -0.0748 -0.0585 259 HOH   B O   
6893 O  O   . HOH   G .   ? 0.1664 0.1769 0.3037 -0.0203 -0.0228 0.0099  260 HOH   B O   
6894 O  O   . HOH   G .   ? 0.2160 0.1521 0.2226 -0.0262 -0.0375 0.0256  261 HOH   B O   
6895 O  O   . HOH   G .   ? 0.2440 0.2296 0.1924 0.0051  -0.0145 0.0015  262 HOH   B O   
6896 O  O   . HOH   G .   ? 0.1897 0.1877 0.1787 -0.0434 -0.0431 0.0063  263 HOH   B O   
6897 O  O   . HOH   G .   ? 0.1445 0.1751 0.2251 -0.0043 0.0040  0.0069  264 HOH   B O   
6898 O  O   . HOH   G .   ? 0.2370 0.3515 0.2304 -0.0719 0.0228  0.0436  265 HOH   B O   
6899 O  O   . HOH   G .   ? 0.2655 0.5102 0.5632 0.0420  0.0521  -0.0695 266 HOH   B O   
6900 O  O   . HOH   G .   ? 0.2531 0.4068 0.3780 0.0062  0.1041  0.0519  267 HOH   B O   
6901 O  O   . HOH   G .   ? 0.2043 0.1601 0.2333 -0.0287 -0.0158 0.0190  268 HOH   B O   
6902 O  O   . HOH   G .   ? 0.2623 0.3194 0.2619 -0.0467 -0.0869 0.0193  269 HOH   B O   
6903 O  O   . HOH   G .   ? 0.1839 0.1419 0.5011 -0.0099 -0.0323 -0.0173 270 HOH   B O   
6904 O  O   . HOH   G .   ? 0.4204 0.2822 0.4211 -0.0201 -0.1281 -0.0443 271 HOH   B O   
6905 O  O   . HOH   G .   ? 0.2672 0.2042 0.2864 -0.0623 0.0144  -0.0141 272 HOH   B O   
6906 O  O   . HOH   G .   ? 0.2853 0.2187 0.5454 0.0091  0.0704  0.0448  273 HOH   B O   
6907 O  O   . HOH   G .   ? 0.4746 0.4093 0.2618 0.0164  -0.0274 -0.0564 274 HOH   B O   
6908 O  O   . HOH   G .   ? 0.2412 0.2556 0.2346 -0.0379 -0.0680 -0.0259 275 HOH   B O   
6909 O  O   . HOH   G .   ? 0.2458 0.7774 0.2546 0.0815  -0.0389 -0.0404 276 HOH   B O   
6910 O  O   . HOH   G .   ? 0.3046 0.3475 0.5292 -0.0032 -0.0354 -0.1193 277 HOH   B O   
6911 O  O   . HOH   G .   ? 0.2175 0.4343 0.5374 -0.0502 -0.0395 -0.0992 278 HOH   B O   
6912 O  O   . HOH   G .   ? 0.1651 0.1604 0.3750 -0.0138 -0.0026 -0.0032 279 HOH   B O   
6913 O  O   . HOH   G .   ? 0.5999 0.3634 0.3000 0.2541  0.0834  0.0759  280 HOH   B O   
6914 O  O   . HOH   G .   ? 0.2667 0.4841 0.4804 -0.1027 -0.1257 0.0893  281 HOH   B O   
6915 O  O   . HOH   G .   ? 0.4396 0.5351 0.5496 0.0384  -0.1464 0.0261  282 HOH   B O   
6916 O  O   . HOH   G .   ? 0.3604 0.2974 0.2019 0.0357  -0.0746 -0.0350 283 HOH   B O   
6917 O  O   . HOH   G .   ? 0.2371 0.3447 0.2291 0.1096  -0.0197 -0.0269 284 HOH   B O   
6918 O  O   . HOH   G .   ? 0.1681 0.1617 0.1855 0.0015  -0.0024 0.0024  285 HOH   B O   
6919 O  O   . HOH   G .   ? 0.2587 0.2685 0.3100 0.0228  -0.0833 0.0154  286 HOH   B O   
6920 O  O   . HOH   G .   ? 0.4604 0.7344 0.2506 -0.0536 -0.0587 0.0146  287 HOH   B O   
6921 O  O   . HOH   G .   ? 0.2360 0.3670 0.3594 -0.0625 0.0649  -0.1380 288 HOH   B O   
6922 O  O   . HOH   G .   ? 0.3968 0.2322 0.3831 -0.1051 -0.2116 0.0942  289 HOH   B O   
6923 O  O   . HOH   G .   ? 0.1706 0.2021 0.2933 0.0198  -0.0123 0.0146  290 HOH   B O   
6924 O  O   . HOH   G .   ? 0.3375 0.4047 0.5025 0.1058  -0.0504 -0.0846 291 HOH   B O   
6925 O  O   . HOH   G .   ? 0.4262 0.4932 0.2381 0.0118  0.0546  0.0963  292 HOH   B O   
6926 O  O   . HOH   G .   ? 0.1774 0.3467 0.5182 0.0349  -0.0072 -0.1582 293 HOH   B O   
6927 O  O   . HOH   G .   ? 0.3358 0.2709 0.2761 -0.0258 0.0239  -0.1100 294 HOH   B O   
6928 O  O   . HOH   G .   ? 0.4484 0.7516 0.4252 0.1605  -0.1114 0.1816  295 HOH   B O   
6929 O  O   . HOH   G .   ? 0.5063 0.3035 0.5115 -0.0419 0.0040  0.1241  296 HOH   B O   
6930 O  O   . HOH   G .   ? 0.1673 0.2160 0.1783 -0.0179 -0.0225 0.0051  297 HOH   B O   
6931 O  O   . HOH   G .   ? 0.4600 0.5307 0.2332 0.1289  -0.0744 -0.0261 298 HOH   B O   
6932 O  O   . HOH   G .   ? 0.1793 0.1663 0.2447 0.0002  0.0026  0.0179  299 HOH   B O   
6933 O  O   . HOH   G .   ? 0.5313 0.3887 0.2613 0.1419  -0.1252 0.0233  300 HOH   B O   
6934 O  O   . HOH   G .   ? 0.2770 0.3061 0.4601 -0.0486 -0.1314 0.0852  301 HOH   B O   
6935 O  O   . HOH   G .   ? 0.2134 0.2655 0.6650 0.0434  -0.0597 -0.0793 302 HOH   B O   
6936 O  O   . HOH   G .   ? 0.5723 0.3056 0.2487 -0.2001 0.0916  -0.0083 303 HOH   B O   
6937 O  O   . HOH   G .   ? 0.3532 0.1983 0.3828 0.0772  0.1164  0.0566  304 HOH   B O   
6938 O  O   . HOH   G .   ? 0.3357 0.3756 0.7760 -0.0049 -0.1026 0.1879  305 HOH   B O   
6939 O  O   . HOH   G .   ? 0.3365 0.7958 0.7876 0.2304  -0.0434 -0.1038 306 HOH   B O   
6940 O  O   . HOH   G .   ? 0.2151 0.1623 0.3360 0.0269  -0.0970 0.0003  307 HOH   B O   
6941 O  O   . HOH   G .   ? 0.2197 0.1716 0.2696 -0.0253 -0.0310 -0.0092 308 HOH   B O   
6942 O  O   . HOH   G .   ? 0.1676 0.1589 0.3194 0.0125  -0.0091 -0.0043 309 HOH   B O   
6943 O  O   . HOH   G .   ? 0.2414 0.3269 0.5388 -0.0208 -0.0761 -0.0235 310 HOH   B O   
6944 O  O   . HOH   G .   ? 0.3247 0.2793 0.5501 -0.0389 -0.1031 0.1352  311 HOH   B O   
6945 O  O   . HOH   G .   ? 0.2410 0.1528 0.2912 -0.0103 -0.0223 0.0289  312 HOH   B O   
6946 O  O   . HOH   G .   ? 0.4505 0.2618 0.2985 0.1759  0.1264  0.0572  313 HOH   B O   
6947 O  O   . HOH   G .   ? 0.2290 0.6603 0.4853 -0.0963 -0.0366 0.0078  314 HOH   B O   
6948 O  O   . HOH   G .   ? 0.2343 0.2002 0.2001 -0.0063 0.0184  0.0140  315 HOH   B O   
6949 O  O   . HOH   G .   ? 0.1570 0.1966 0.2875 -0.0291 -0.0124 0.0029  316 HOH   B O   
6950 O  O   . HOH   G .   ? 0.2997 0.4421 0.3851 -0.1485 0.1014  -0.0902 317 HOH   B O   
6951 O  O   . HOH   G .   ? 0.1652 0.1723 0.3352 -0.0106 -0.0163 -0.0201 318 HOH   B O   
6952 O  O   . HOH   G .   ? 0.2748 0.2882 0.3942 -0.0450 0.0985  -0.1006 319 HOH   B O   
6953 O  O   . HOH   G .   ? 0.4469 0.3537 0.5082 0.0857  0.2024  0.1706  320 HOH   B O   
6954 O  O   . HOH   G .   ? 0.5963 0.4837 0.5507 0.1611  0.1317  -0.0114 321 HOH   B O   
6955 O  O   . HOH   G .   ? 0.4660 0.4621 0.2492 0.0697  -0.0465 -0.0564 322 HOH   B O   
6956 O  O   . HOH   G .   ? 0.1757 0.2968 0.2652 -0.0170 -0.0141 0.0750  323 HOH   B O   
6957 O  O   . HOH   G .   ? 0.7299 0.2066 0.3170 0.0235  -0.0910 0.0048  324 HOH   B O   
6958 O  O   . HOH   G .   ? 0.2908 0.2328 0.2268 0.0194  -0.0167 0.0221  325 HOH   B O   
6959 O  O   . HOH   G .   ? 0.1957 0.1957 0.2901 0.0315  0.0335  0.0179  326 HOH   B O   
6960 O  O   . HOH   G .   ? 0.4237 0.3983 0.6293 0.0570  -0.0199 0.1000  327 HOH   B O   
6961 O  O   . HOH   G .   ? 0.5090 0.2366 0.3050 0.0066  -0.0182 0.0728  328 HOH   B O   
6962 O  O   . HOH   G .   ? 0.5881 0.5535 0.5149 -0.1086 -0.0460 0.1492  329 HOH   B O   
6963 O  O   . HOH   G .   ? 0.6767 0.7467 0.5651 0.3555  -0.0403 -0.0974 330 HOH   B O   
6964 O  O   . HOH   G .   ? 0.5678 0.4839 0.7132 0.1185  -0.0705 0.1932  331 HOH   B O   
6965 O  O   . HOH   G .   ? 0.2768 0.2015 0.5330 -0.0111 -0.0093 0.0145  332 HOH   B O   
6966 O  O   . HOH   G .   ? 0.1761 0.2806 0.3038 0.0188  -0.0219 -0.0636 333 HOH   B O   
6967 O  O   . HOH   G .   ? 0.5607 0.3600 0.3642 -0.0258 0.1086  0.0976  334 HOH   B O   
6968 O  O   . HOH   G .   ? 0.2294 0.2419 0.5603 -0.0526 -0.0115 0.1481  335 HOH   B O   
6969 O  O   . HOH   G .   ? 0.1751 0.1523 0.2420 0.0078  -0.0228 0.0001  336 HOH   B O   
6970 O  O   . HOH   G .   ? 0.5195 0.4704 0.5616 -0.0365 -0.0441 -0.1207 337 HOH   B O   
6971 O  O   . HOH   G .   ? 0.4639 0.3263 0.3362 0.0486  -0.1079 -0.0674 338 HOH   B O   
6972 O  O   . HOH   G .   ? 0.4358 0.7726 0.3939 -0.0129 -0.0659 0.2232  339 HOH   B O   
6973 O  O   . HOH   G .   ? 0.5509 0.3513 0.4124 0.0288  0.0231  -0.1559 340 HOH   B O   
6974 O  O   . HOH   G .   ? 0.5118 0.5916 0.3576 0.0466  -0.1173 0.0042  341 HOH   B O   
6975 O  O   . HOH   G .   ? 0.2548 0.6291 0.6981 0.0612  -0.0311 -0.0571 342 HOH   B O   
6976 O  O   . HOH   G .   ? 0.7166 0.6061 0.2967 -0.0404 -0.0764 0.1113  343 HOH   B O   
6977 O  O   . HOH   G .   ? 0.2181 0.1985 0.3332 -0.0053 0.0456  -0.0122 344 HOH   B O   
6978 O  O   . HOH   G .   ? 0.3806 0.6633 0.3922 -0.1168 -0.1063 -0.1083 345 HOH   B O   
6979 O  O   . HOH   G .   ? 0.5261 0.5695 0.4795 -0.1176 0.0716  0.1246  346 HOH   B O   
6980 O  O   . HOH   G .   ? 0.3836 0.4814 0.5774 -0.0001 -0.0907 0.1221  347 HOH   B O   
6981 O  O   . HOH   G .   ? 0.2953 0.2334 0.5147 -0.0244 -0.1107 -0.0536 348 HOH   B O   
6982 O  O   . HOH   G .   ? 0.2241 0.3937 0.5781 0.0324  0.0389  0.0228  349 HOH   B O   
6983 O  O   . HOH   G .   ? 0.2510 0.5913 0.4228 0.1610  -0.0455 -0.1497 350 HOH   B O   
6984 O  O   . HOH   G .   ? 0.4573 0.6277 0.6023 0.0478  -0.0178 -0.0681 351 HOH   B O   
6985 O  O   . HOH   G .   ? 0.3384 0.4217 0.5361 -0.1245 0.0346  -0.0514 352 HOH   B O   
6986 O  O   . HOH   G .   ? 0.3077 0.2002 0.4004 0.0315  -0.1229 -0.0546 353 HOH   B O   
6987 O  O   . HOH   G .   ? 0.4791 0.3800 0.3756 0.0727  0.0973  -0.0552 354 HOH   B O   
6988 O  O   . HOH   G .   ? 0.4241 0.2358 0.3614 -0.1038 0.0759  -0.1073 355 HOH   B O   
6989 O  O   . HOH   G .   ? 0.4847 0.3449 0.6116 -0.1239 0.1148  0.0909  356 HOH   B O   
6990 O  O   . HOH   G .   ? 0.4044 0.2834 0.3412 -0.1085 -0.0164 -0.0455 357 HOH   B O   
6991 O  O   . HOH   G .   ? 0.5343 0.5575 0.5339 -0.0563 -0.0316 0.0496  358 HOH   B O   
6992 O  O   . HOH   G .   ? 0.4672 0.5422 0.4937 0.1836  -0.1318 0.1284  359 HOH   B O   
6993 O  O   . HOH   G .   ? 0.5202 0.3367 0.5176 0.0023  -0.1540 -0.0207 360 HOH   B O   
6994 O  O   . HOH   G .   ? 0.4694 0.4288 0.6653 -0.0577 0.0222  0.0890  361 HOH   B O   
6995 O  O   . HOH   G .   ? 0.5339 0.6871 0.3815 0.2038  -0.0317 0.0715  362 HOH   B O   
6996 O  O   . HOH   G .   ? 0.2394 0.3737 0.6534 -0.0803 -0.0540 -0.0929 363 HOH   B O   
6997 O  O   . HOH   G .   ? 0.4849 0.3460 0.4465 -0.1574 -0.0383 0.0188  364 HOH   B O   
6998 O  O   . HOH   G .   ? 0.6062 0.4726 0.4437 0.1046  0.0748  0.0740  365 HOH   B O   
6999 O  O   . HOH   G .   ? 0.4353 0.3679 0.5857 0.0719  -0.1190 0.0282  366 HOH   B O   
7000 O  O   . HOH   G .   ? 0.7557 0.7471 0.5306 0.2866  -0.1201 0.1037  367 HOH   B O   
7001 O  O   . HOH   G .   ? 0.5287 0.5420 0.4912 -0.1024 -0.0952 -0.1044 368 HOH   B O   
7002 O  O   . HOH   G .   ? 0.5542 0.2199 0.3948 0.0102  0.0163  0.0464  369 HOH   B O   
7003 O  O   . HOH   G .   ? 0.4506 0.6022 0.5640 0.2582  0.1423  0.1211  370 HOH   B O   
7004 O  O   . HOH   G .   ? 0.5044 0.5112 0.3747 0.1268  -0.1340 0.0738  371 HOH   B O   
7005 O  O   . HOH   G .   ? 0.6331 0.3938 0.2880 -0.0940 -0.1081 -0.0424 372 HOH   B O   
7006 O  O   . HOH   G .   ? 0.4526 0.3231 0.5109 0.0626  -0.1412 -0.0300 373 HOH   B O   
7007 O  O   . HOH   G .   ? 0.2550 0.5032 0.4047 0.0204  -0.0448 -0.0875 374 HOH   B O   
7008 O  O   . HOH   G .   ? 0.4377 0.4910 0.4720 -0.1058 -0.0314 0.0349  375 HOH   B O   
7009 O  O   . HOH   G .   ? 0.7287 0.4097 0.5250 -0.1115 -0.0328 -0.0019 376 HOH   B O   
7010 O  O   . HOH   G .   ? 0.5179 0.6600 0.6692 0.1802  0.0795  0.2714  377 HOH   B O   
7011 O  O   . HOH   G .   ? 0.5580 0.7170 0.4112 -0.1420 0.0568  -0.1435 378 HOH   B O   
7012 O  O   . HOH   G .   ? 0.3607 0.4240 0.2171 0.0111  0.0457  -0.0035 379 HOH   B O   
7013 O  O   . HOH   G .   ? 0.6921 0.6756 0.5949 -0.0413 0.1926  0.1736  380 HOH   B O   
7014 O  O   . HOH   G .   ? 0.3575 0.4335 0.5284 0.1141  0.0071  0.1162  381 HOH   B O   
7015 O  O   . HOH   G .   ? 0.3315 0.2679 0.3409 -0.0030 0.0075  0.0432  382 HOH   B O   
7016 O  O   . HOH   G .   ? 0.4470 0.8526 0.5610 0.0862  0.1924  0.1980  383 HOH   B O   
7017 O  O   . HOH   G .   ? 0.7133 0.5159 0.4354 0.1117  0.0067  0.0326  384 HOH   B O   
7018 O  O   . HOH   G .   ? 0.6552 0.4789 0.4681 0.1188  0.0869  -0.0808 385 HOH   B O   
7019 O  O   . HOH   G .   ? 0.5688 0.5123 0.4690 0.0024  -0.1132 0.0061  386 HOH   B O   
7020 O  O   . HOH   G .   ? 0.4466 0.3650 0.3737 0.0149  0.0263  -0.0223 387 HOH   B O   
7021 O  O   . HOH   G .   ? 0.2557 0.4658 0.4036 -0.0817 -0.1014 -0.0229 388 HOH   B O   
7022 O  O   . HOH   G .   ? 0.5192 0.4289 0.5777 -0.0829 -0.0187 -0.0451 389 HOH   B O   
7023 O  O   . HOH   G .   ? 0.3340 0.2287 0.3511 0.0520  -0.0256 -0.0131 390 HOH   B O   
7024 O  O   . HOH   G .   ? 0.4848 0.4005 0.4580 0.0164  0.0815  0.0644  391 HOH   B O   
7025 O  O   . HOH   G .   ? 0.2561 0.3878 0.6827 -0.1273 -0.0622 0.0541  392 HOH   B O   
7026 O  O   . HOH   G .   ? 0.3805 0.2244 0.5629 -0.0042 0.0705  0.0686  393 HOH   B O   
7027 O  O   . HOH   G .   ? 0.4350 0.4367 0.3970 -0.0376 0.0758  0.0614  394 HOH   B O   
7028 O  O   . HOH   G .   ? 0.4858 0.6166 0.3895 0.1408  0.0101  -0.0936 395 HOH   B O   
7029 O  O   . HOH   G .   ? 0.3144 0.3590 0.3993 0.0326  0.0002  -0.0407 396 HOH   B O   
7030 O  O   . HOH   G .   ? 0.2211 0.2694 0.6044 -0.0419 -0.1126 0.0364  397 HOH   B O   
7031 O  O   . HOH   G .   ? 0.6317 0.6975 0.7543 0.1480  -0.0481 0.2576  398 HOH   B O   
7032 O  O   . HOH   G .   ? 0.5489 0.4176 0.3099 -0.2025 -0.0482 0.1213  399 HOH   B O   
7033 O  O   . HOH   G .   ? 0.5649 0.5999 0.3967 0.2163  0.0157  -0.0288 400 HOH   B O   
# 
